{"protein": "MALVARSICVSYDEIAGICNNVSHRNFKKWVQWKNPFLFQDDARRNIRFNDRKLSCTKFIGASEKLQHSKSPKSGLISCGWEVNSSKVVSNAVIPKKWNLLKLKVVEVTAIVACTFFVMSSAQAVDALKTCTCLLKECRIELAKCIANPSCAANVACLQTCNNRPDETECQIKCGDLFANKVVDEFNECAVSRKKCVPQKSDVGEFPVPDPSVLVKSFNMADFNGKWFISSGLNPTFDAFDCQLHEFHLEDGKLVGNLSWRIKTPDGGFFTRTAVQKFAQDPSQPGMLYNHDNAYLHYQDDWYILSSKIENQPDDYVFVYYRGRNDAWDGYGGAFLYTRSATVPENIVPELNRAAQSVGKDFNKFIRTDNTCGPEPPLVERLEKTVEEGERTIIKEVEQLEGEIEGDLEKVGKTEMTLFQRLLEGFQELQKDEEYFLKELNKEERELLEDLKMEAGEVEKLFGRALPIRKLR", "text": "FUNCTION: Part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. Catalyzes the two-step mono de-epoxidation reaction. Stereospecific for all-trans xanthophylls. Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Binds to the thylakoid membrane at pH 5.2 and is released in the lumen at pH 7.2. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MSINRRSKNITEGVARAPNRSMYYAMGYQEADFKKPMIGVANGHSTITPCNSGLQKLADAAVEGIEAAGGNAQIFGTPTISDGMAMGTEGMKYSLVSREVIADCVETCVGGQWMDGVLVVGGCDKNMPGGMMGMLRANVPAIYVYGGTILPGKYKGQDLNIVSVFEAVGQFTAGNMSEEDFCQIERRAIPGSGSCGGMYTANTMSSAFEALGMSLPFASTMANVEDPIVAHTKEAARVLVEAVKADLKPRDIVTRKSIENAVAVIMATGGSTNAVLHFLAIAHAAGVEWTIDDFERVRRKVPVLCDLKPSGRYLAIDLHRAGGIPQVMKTLLAAGLIHGDCITITGRTVAENLADIPDAPRADQDVIRPITKPMYEQGHLAILKGNLSPEGAVAKITGLKNPSITGPARVFDDEQSALAAIMAKQIQAGDVMVLRYLGPMGGPGMPEMLAPTGALIGQGLGESVGLITDGRFSGGTWGMVVGHVAPEAAAGGTIALVQEGDSITIDAHTLVLNLNVSEAEIAKRRAAWKAPAPRYTRGVLAKFAKNASSASSGAVLDRFE", "text": "FUNCTION: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. SIMILARITY: Belongs to the IlvD/Edd family."}
{"protein": "MRSTSKAIPFSFHTSLIVQCLRPLRFTSAASPSSSSSSSSQWFGFLRNAITSSDLMLGKCTHARILTFEENPERFLINNLISMYSKCGSLTYARRVFDKMPDRDLVSWNSILAAYAQSSECVVENIQQAFLLFRILRQDVVYTSRMTLSPMLKLCLHSGYVWASESFHGYACKIGLDGDEFVAGALVNIYLKFGKVKEGKVLFEEMPYRDVVLWNLMLKAYLEMGFKEEAIDLSSAFHSSGLNPNEITLRLLARISGDDSDAGQVKSFANGNDASSVSEIIFRNKGLSEYLHSGQYSALLKCFADMVESDVECDQVTFILMLATAVKVDSLALGQQVHCMALKLGLDLMLTVSNSLINMYCKLRKFGFARTVFDNMSERDLISWNSVIAGIAQNGLEVEAVCLFMQLLRCGLKPDQYTMTSVLKAASSLPEGLSLSKQVHVHAIKINNVSDSFVSTALIDAYSRNRCMKEAEILFERHNFDLVAWNAMMAGYTQSHDGHKTLKLFALMHKQGERSDDFTLATVFKTCGFLFAINQGKQVHAYAIKSGYDLDLWVSSGILDMYVKCGDMSAAQFAFDSIPVPDDVAWTTMISGCIENGEEERAFHVFSQMRLMGVLPDEFTIATLAKASSCLTALEQGRQIHANALKLNCTNDPFVGTSLVDMYAKCGSIDDAYCLFKRIEMMNITAWNAMLVGLAQHGEGKETLQLFKQMKSLGIKPDKVTFIGVLSACSHSGLVSEAYKHMRSMHGDYGIKPEIEHYSCLADALGRAGLVKQAENLIESMSMEASASMYRTLLAACRVQGDTETGKRVATKLLELEPLDSSAYVLLSNMYAAASKWDEMKLARTMMKGHKVKKDPGFSWIEVKNKIHIFVVDDRSNRQTELIYRKVKDMIRDIKQEGYVPETDFTLVDVEEEEKERALYYHSEKLAVAFGLLSTPPSTPIRVIKNLRVCGDCHNAMKYIAKVYNREIVLRDANRFHRFKDGICSCGDYW", "text": "SIMILARITY: Belongs to the PPR family. PCMP-H subfamily."}
{"protein": "MKQLKPNSKYLLYGQALSFMGDYCVLPALLILSTYYHDYWVTSGVIVVRSIPMVFQPFLGVLVDRLDRIKIMLWTDIIRGIIFLGLTFLPKGEYPLIFLALLFITYGSGVFFNPARLAVMSSLESDIKSINTLFAKATTISIIVGAAAGGLFLLGGSVELAVAFNGVTYLVSAFFISRIKLQFVPIQSENIKEAFQSFKEGLKEIKTNSFVLNAMFTMITMALLWGVVYSYFPIVSRFLGDGEIGNFILTFCIGFGGFIGAALVSKWGFNNNRGLTYFTVLSIVSLALFLFTPIFAVSVIAAILFFIAMEYGEVLAKVKVQENAANQIQGRIFSVAEASIGLCISIGSMFINILSAPVIMGLIVVIVCGLFLHTKLVNKSFLERDNKTEQKGVF", "text": "FUNCTION: Part of the bacilysin biosynthesis operon. May be involved in self-resistance to bacilysin by permitting efflux of this antibiotic. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Drug:H(+) antiporter-3 (DHA3) (TC 2.A.1.21) family."}
{"protein": "MLKQESNDIGSGENNRARPCDTCRSNACTVYCHADSAYLCMSCDAQVHSANRVASRHKRVRVCESCERAPAAFLCEADDASLCTACDSEVHSANPLARRHQRVPILPISGNSFSSMTTTHHQSEKTMTDPEKRLVVDQEEGEEGDKDAKEVASWLFPNSDKNNNNQNNGLLFSDEYLNLVDYNSSMDYKFTGEYSQHQQNCSVPQTSYGGDRVVPLKLEESRGHQCHNQQNFQFNIKYGSSGTHYNDNGSINHNAYISSMETGVVPESTACVTTASHPRTPKGTVEQQPDPASQMITVTQLSPMDREARVLRYREKRKTRKFEKTIRYASRKAYAEIRPRVNGRFAKREIEAEEQGFNTMLMYNTGYGIVPSF", "text": "FUNCTION: Transcription factor that acts in the long day flowering pathway and may mediate between the circadian clock and the control of flowering. Plays a role in the regulation of flowering time by acting on 'SUPPRESSOR OF OVEREXPRESSION OF CO1', 'TERMINAL FLOWER 1' and 'FLOWERING LOCUS T'. Also regulates P5CS2 and ACS10 (involved in proline and ethylene biosynthesis, respectively). Regulates the expression of NAKR1 by binding to the 5'-TGTG(N2-3)ATG-3' motif (PubMed:27255839). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CONSTANS family."}
{"protein": "MLTLARQQQRQNIRWLLCLSVLMLLALLLSLCAGELWILPGDWFSPRGELFVWQIRLPRTLAVLLVGAALAISGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPNWALGLCAIAGALIITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSVDLRQLMYWMMGGFGGVDWRQSWLMLALIPVLLWICCQSRPMNILALGEISARQLGLPLWFWRNVLVAATGWMVGVSVALAGAIGFIGLVIPHILRLCGLTDHRVLLPGCALAGASALLLADIVARLALAAAELPIGVVTATLGAPVFIWLLLKAGR", "text": "FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily."}
{"protein": "MNLPPLTPATLIRRYKRFLADCALASGEIITVHCPNSGSMRSCAEPGQPILISQSGNPKRKLPWTWELYWSGASWVCINTQHPNAVVAEAIAAGDIPALQNYAQLRREVPYGSHERVDVLLSSEGRPPCYVEVKSCTLLEEDGVIRFPDAVSSRALRHLGALTEVVRGGGRAVMLFLIGREDGRGFAPADAIDPAYGKALRRARTDGVEILAYRTRLSPDKISLSVAEPLLF", "text": "SIMILARITY: Belongs to the SfsA family."}
{"protein": "MQPPPSLCGLALLALVLACGMAEVWGEEREMPSAPATPPLLGASEILTPSTKTSWPRDSNASLPRSSAPAEIPKEGRTAGAPRRTPPPCQRPTEIKDTFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVILAVPEAIGFNLVTIDYKGSYLRICLLNPTQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFGLCWLALHLSRILKLTLYDQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS", "text": "FUNCTION: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=internalized after activation by endothelins. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRB sub-subfamily."}
{"protein": "MAPAMEEIRQAQRAEGPAAVLAIGTSTPPNALYQADYPDYYFRITKSEHLTELKEKFKRMCDKSMIKKRYMYLTEEILKENPNICAFMAPSLDARQDIVVTEVPKLAKEAAVRAIKEWGHPKSRITHLIFCTTSGIDMPGADYQLTRLLGLRPSVNRFMLYQQGCFAGGTVLRLAKDLAENNAGARVLVVCSEITAVTFRGPSESHLDSLVGQALFGDGAAAIIVGSDPDSATERPLFQLVSASQTILPESEGAIDGHLREIGLTFHLLKDVPGLISKNIQKCLLDAFKPLGVHDWNSIFWIAHPGGPAILDQVEIKLGLKAEKLAASRNVLAEYGNMSSACVLFILDEMRRRSAEAGQATTGEGLEWGVLFGFGPGLTVETIVLRSVPIAGAE", "text": "FUNCTION: The primary product of this enzyme is 4,2',4',6'- tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family."}
{"protein": "MAASGKLSTWRLPPLPTIREIIKLLRVQAAKQLSQNFLLDLRLTDKIVRKAGNLTNAYVYEVGPGPGGITRSILNADVAELLVVEKDTRFVPGLQMLSDAAPGKLRIVHGDVLTFKVEKAFSESLKRPWEDDPPDVHIIGNLPFSVSTPLIIKWLENISCRDGPFVYGRTQMTLTFQKEVAERLAANTGSKQRSRLSVMAQYLCNVRHIFTIPGRAFVPKPEVDVGVVHFTPLIQPKIEQPFKLVEKVVQNVFQFRRKYCHRGLRMLFPEAQRLESTGRLLELADVDPTLRPCQPSISHFKSLCDVYRKMCDEDPQLFAYNFREELKQRKSKNEEKEEDDAEN", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. KsgA subfamily."}
{"protein": "MKILSVLLLALIICSIVGWSEAQFTDVSCTTSKECWSVCQRLHNTSIGKCMNKKCRCYS", "text": "FUNCTION: Potent selective inhibitor of high conductance (maxi-K), different medium and small conductance calcium-activated potassium channels (KCa1.1/KCNMA1 and others), as well as a voltage-dependent potassium channel (Kv1.3/KCNA3>Kv1.2/KCNA2>Kv1.6/KCNA3>>Shaker/Sh). It blocks channel activity by a simple bimolecular inhibition process. FUNCTION: Has a pH-specific antimicrobial activity against bacteria (B.subtilis, E.coli and S.aureus) and the fungus C.albicans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 01 subfamily."}
{"protein": "MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQUGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFAAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRYGPMEEPLVIEKDLPHYF", "text": "FUNCTION: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (By similarity). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (By similarity). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (By similarity). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (By similarity). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (By similarity). Required for normal sperm development and male fertility (By similarity). Essential for maturation and survival of photoreceptor cells (By similarity). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (By similarity). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (By similarity). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down- regulator of the cellular 15-lipoxygenase pathway (By similarity). FUNCTION: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (By similarity). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (PubMed:24439385). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (By similarity). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (By similarity). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (By similarity). Required for normal sperm development and male fertility (By similarity). Essential for maturation and survival of photoreceptor cells (By similarity). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (By similarity). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (PubMed:11115402). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down- regulator of the cellular 15-lipoxygenase pathway (By similarity). SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm. SIMILARITY: Belongs to the glutathione peroxidase family."}
{"protein": "MNSYLEYTSCGDVLAFSPKFCRSDHRNMNLQPYPRSGADHSFMPVGGVPGSVAHQAPHQSPALYAPCSLDVAYEPTPPSDYSFLHSSPDYDYYGSNHQIEETGGHIPYGSSLFPGNGSYILNGQLSYRTLGEETQMAQCKEPLEVYPGGNLQSISPSPGTYPKPASPASDSYVSTFDWMKVKRNPPKKSIPSEYGVTSPPCNVRTNFTTKQLTELEKEFHFNKYLTRARRIEIANSLQLNDTQVKIWFQNRRMKQKKREREGTLPNSPPSGPASNFCVKPPHLKSVNETATLSPSKDASP", "text": "FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Acts downstream of meis3 to pattern the hindbrain. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family. Labial subfamily."}
{"protein": "MSHSISPIGHVRSCFKEKFAIPRQPQLAPAATGVLELLPPFDTGDAVEGLEQVSHVWLIFLFHQALEDKPRLKVRPPRLGGNQSMGVFATRATHRPNGLGQSVVKLEKVEPGRLWLSGIDLLDGTPVIDIKPYVPYADIVPDAHNAIADAPPSSIAVHWSDEALRQAHEHGLRLCQPVRELVGNASPRTRARPTRSRRPSAAMACACGTSTCTGTTPPMARSACWTCNAPPTETSLSPQD", "text": "SIMILARITY: Belongs to the tRNA methyltransferase O family."}
{"protein": "MLFIFQLTLLAFIGLSLALVIGVPVLLASPEGWAQSKGLVFSGSALWMLLVFVVGALNSFVS", "text": "FUNCTION: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbZ family."}
{"protein": "MSWQAYVDDHLMCDIEGQHLTAAAIIGHDGSVWAQSATFPQFKPEEVAAIIKDFDEPGSLAPTGLHLGGTKYMVIQGEPGAVIRGKKGAGGITVKKTGQALIFGIYDEPLTPGQCNIIVERLGDYLLEQGQ", "text": "FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family."}
{"protein": "MLIKGINHICFSVSNLETSIAFYEKVLEGELLVKGRKLAYFRICGTWVALNEETDIPRKEIHQSYTHIAFSIEKEDFERLLQRLKENDVHILQGRKRDVRDCKSIYFTDPDGHKFECHTGTLEERLQYYKEAKPHMTFY", "text": "FUNCTION: Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the fosfomycin resistance protein family. FosB subfamily."}
{"protein": "MTYIDTLGQQAKVASRQIAKLSTAAKNDLLNQVAKALVAESDYIITENAKDMANASENGISKIMQDRLLLTEDRIAGIAEGVRQVADLQDPIGQVVRGYTNLDGLKIVQKRVPMGVIAMIFESRPNVSIDAFSLAFKTNNAIILRGGRDAINSNKALVTVARKALKNAGITADAVQFVEDTSHEVAEELMVATKYVDLLIPRGGARLIQTVKEKAKVPVIETGVGNCHIYVDKYANLDMATQIVINAKTQRPSVCNAAESLVVHADIVEEFLPNLEKAILKIQSVEFRADERALKLMEKAVPASPEDFATEFLDYIMSVKVVDSLDEAINWINTYTTSHSEAIVTQDISRAEQFQDDVDAAAVYVNASTRFTDGFVFGLGAEIGISTQKMHARGPMGLEALTSTKFYINGQGQIRE", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family."}
{"protein": "MLEIDNQTPLESDFLLLEKIANVLAPTQIIELVLVSDETMREINRDLRGCDYATDVLSFPLEAIPHTPLGSVVINAPLAQTNALKLGHSLENEIALLFIHGVLHLLGYDHEKDKGEQRQKESELIKAFNLPLSLIERAQD", "text": "FUNCTION: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endoribonuclease YbeY family."}
{"protein": "MSEQEALKCSSARNRGGTQRVEGKLRASVEKGDYYEAHQMYRTLFFRYISQAKHTDARELMYNGAQLFFSYNQLNSAADLSMLVLESLEKSEAKVEDEDLEHLAKLFSLMDPNSPERVAFVSRALKWSTGGSGKLGAPKLHQLLAVTLWKEQNYSESRYHFLHSSDGEGCAQMLVEYSAQRGFRSEVDMFVAQAVLQFLCLKNKNSASVVFSTYTQKHPSIEKDPPFVQPLLNFIWFLLLAVDGGKLTVFTVLCEQYQPSLKRDPMYNEYLDRIGQLFFGVPPKQSSSYGGLLGNLLNSLMGSGEDEEGEEAQEHGSPIELD", "text": "FUNCTION: As part of a cytosolic protein quality control complex, the bag6/bat3 complex, maintains misfolded and hydrophobic patches- containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The bag6/bat3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The bag6/bat3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GET4 family."}
{"protein": "MNIIAELEAEQAAKLLAGKTIPEFQPGDTVIVNVKVKEGERTRVQAYEGVCIARNGGGLNESFTVRKISYGEGVERVFAIYSPNIDSIKVVRRGKVRRAKLYYLRDRRGKSARIAEKMESPAAKATREAAKKEAKAAKKNAAPAE", "text": "FUNCTION: This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family."}
{"protein": "MSELNVIKKERTAVINPIVTCQPLGAMYAVSGIERGMPLVHGSQGCSTFVRYGFARHFREPADIAVTSLHEDAAVFGGRKNLISGLGNLAARFKPDVMGVVTTCSSEIIGDDVAGFIKTAKVEIAKKMGEEAANKIKIVQINTPSFVEHQFKGYDNAIKAIVDTLAEPKDEENGKLNIIPGIVNPGDIREIKHMLSLMGVEGILLTDTSDPFDSPLRPSKADKNPYYQKGGTPLADLQDCANSLGTISLANYANSAPASLEKKYNMPSKVSEAPIGIQNTDSFIRTVKKFTGNDVTDEILDERGIVIDAMADVASRYLFGRKVAIYGDPSITVGMARFVAELGMIPKVVCTGVKNEYFVNDLKKVAKESDEDIDALFGQDLRALDVYLKENPVDLMIGSSDGRLMAKDLGIPLYRVGYPVYDRVGYQRRPIIGYNGALNLVDGITNTILDKYYETQDWKLQQ", "text": "FUNCTION: This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family."}
{"protein": "MPVINLLLLTMSILIAMAFLMLTERKILGYTQLRKGPNIVGPCGLLQPFADALKLFTKEPLKPSTSTTILYIVSPALALTIALLLWTPLPMPNPLINLNLGLLFILATSSLTVYSILWSGWASNSNYALIGTLRAVAQTISYEITLALILLSVLLMSGSFNLSTLITTQEHSWLLLPSWPLALMWFISTLAETNRAPFDLTEGESELVSGFNTEYAAGPFALFFMAEYTNIILMNALTAMIFLGTTFNIHSPELHTTLFTIKTLLLTSLFLWIRSTYPRFRYDQLMHLLWKNFLPLTLALLMWHISMPITTSGIPPQT", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MKRLTGTNEKISNILYQEQLELSKENLDVEATVREIIEKVKEEGDEALRAYSEKFDHVVLSELHVSDQVVNEAFDKIDKDVLTALENAKANIESYHKQQLKGGFEDQPSQGVLRGQLIRPIERVGVYVPGGTAAYPSSVLMNVIPAKIAGVKEIIMITPPQEHFVPAILVAAKLAGVDKIYQVGGAQGIAALAYGTQTLPKVDKITGPGNIFVATAKKLVYGVVGIDMIAGPSEIGVIADSTANPVYVAADLLSQAEHDVHARAILVTNSAELADAVELEIEKQLQTLPRQAIARPSIENNGRIIIAQDVESMFELMNLVAPEHLEIAIDKAYDYLERVQNAGSIFLGHYTSEPIGDYYAGANHVLPTTATSRFSSALGVHDFVKRIQYTQYSKAAVNAAEKDITTLAYAEGLQAHARAIEVRNDKN", "text": "FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. SIMILARITY: Belongs to the histidinol dehydrogenase family."}
{"protein": "MGKEKQHVSIVVIGHVDSGKSTTTGHLIYKCGGIEKRAIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETEKYSFTIIDAPGHRDFIKNMITGTSQADLAILVIASPPGEFEAGISQNGQTREHALLAYTLGVKQMIVACNKMDDKNVNWSQDRYEEVSKEMDLYLKKVGYNPAKVPKVPTSGWTGENLFERTDKTHALGKWYKGPCLLEALDNCDPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGLIKPGMVVTFAPSGLSTEVKSVEMHHEALPQAGPGDNVGFNVKNVSVKDLKRGYVCGDSKNDPPKGCASFNAQVIILNHPGEIHAGYAPVLDCHTAHIACKFSELILKMDRRSGKKLEDTPKMIKSGDAAMVKMVASKPMCVEAFTQYPPLGRFAVRDMRQTVAVGVIKSVEKKEVEGKMTKSAAKK", "text": "FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily."}
{"protein": "MSELLSFALFLASVLIYAWKAGRNTWWFAATLTVLGLFVVLNITLFASDYFTGAGINDAVLYTLTNSLTGAGVSKYILPGIGIVLGLTAVFGALGWILRRRRHHPHHFGYSLLALLLALGSVDASPAFRQITELVKSQSRDGDPDFAAYYKEPSKTIPDPKLNLVYIYGESLERTYFDNEAFPDLTPELGALKNEGLDFSHTQQLPGTDYTIAGMVASQCGIPLFAPFEGNASASVSSFFPQNICLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLYGSEELKSVVADPHYRNDWGFYDDTVLDEAWKKFEELSRSGQRFSLFTLTVDTHHPDGFISRTCNRKKYDFDGKPNQSFSAVSCSQENIAAFINKIKASPWFKDTVIVVSSDHLAMNNTAWKYLNKQDRNNLFFVIRGDKPQQETLAVKRNTMDNGATVLDILGGDNYLGLGRSSLSGQSMSEIFLNIKEKTLAWKPDIIRLWKFPKEMKEFTIDQQKNMIAFSGSHFRLPLLLRVSDKRVEPLPESEYSAPLRFQLADFAPRDNFVWVDRCYKMAQLWAPELALSTDWCVSQGQLGGQQIVQHVDKTTWKSKTAFKDTVIDMARYKGNVDTLKIVDNDIRYKADSFIFNVAGAPEEVKQFSGISRPESWGRWSNAQLGDEVKIEYKHPLPKKFDLVITAKAYGNNASRPIPVRVGNEEQTLVLGNEVTTTTLHFDNPTDADTLVIVPPEPVSTNEGNILGHSPRKLGIGMVDIKVVEREG", "text": "FUNCTION: Transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OpgB family."}
{"protein": "MTSVVVIGTQWGDEGKGKITDFLSQDAEVIARYQGGDNAGHTIVIDGKKFKLHLIPSGVFFPEKISVIGNGVVVNPKSLVKELEYLHTEGVSTENLRISDRAHVILPYHIKLDQLQEAAKGDNKIGTTNKGIGPAYMDKAARVGIRIADLLDKEIFASRLKTNLAEKNRLFSKMYESEELSFDEIFEEYYAYGQQIKQYVTDTSVILNDALDAGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKINKVVGVCKAYTSRVGDGPFPTELFDEVGERIREVGHEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNCIDVLSGLDTVKICVAYDLDGERIDYYPASLEQLKRCKPIYEELPGWEEDITGCRSLDELPENARNYVRRIGELVGIRISTFSVGPGREQTNILESVWSNI", "text": "FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylosuccinate synthetase family."}
{"protein": "MTKLRVGLLFGGRSGEHEVSINSAKAIATALSASENATKYDILPVYIRKDGCWQAPDVAQQVLESAQPLSTPTDKSPQLWQFPPQVNQVDVWFPILHGPNGEDGTLQGLLTLMQVPYVGSGVLGSAVGMDKITMKTVFAKAGLPQVKYMTLSRGQIWSNPCIFPKLCDEIEETLNYPCFVKPANLGSSVGIAKVRSRSELEKALDQAASYDRRIIVEAGVIAREVECAVLGNDNPKASVVGEITFNSDFYDYETKYTDGRAQLLIPASVPDSIMTQIQEMSLAAFAAVDAAGLARVDFFYVEKTGEILINEINTLPGFTAFSMYPQLWAATGISFPQLVDRLIELALERHQR", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-alanine--D-alanine ligase family."}
{"protein": "MKITTAWLKDHLDTKLNENQIIDKLTDIGLEVEGVDSQSGELDQFVIAKILKAEKHPDADRLRVCDVDIGSGKSVKVVCGAPNAKEGLLTIYAPPGAVVPKSQMKLVVSKIRGVTSYGMLCSESELNLSNESDGITELLPEKYNKKVGENYFPKKNLNVIDISITPNRADCLGVRGIARDLAAAGAGRLINQKEKKLDKKNKQTISVKIENEKNQACISFGSCLIKGVKNTESPEWLKDKIIALGQKPISAIVDITNYIMFDLNRPLHAYDVDKIDKAIVVRNSKKGETFEALDNKEYKLEDEMCVISDASGVLGLGGIIGGTRTGTELDTKNVLIESAYFSPRSIRKSSKILNIDTDAKFRFERGIDPLSIDQGLERAANLIQEICGGEVSEFDIQKIEDVKKKSLKFDPSLFEKITGFNIDIKEMIKILDNLGFEIKENKGILDAVIPSWRPDISQEVDVVEELVRIKGYDQIKIIEPEKVRKKQTLNLKQKLFHFLQRSIASKGYFEAITWSFTDSKINQLFIENNKEIKIINPISSDLNVLRSSIFSNLIIHLNKNLGRGFKDLSFFEIGPTFLGSEPGEQQTVATGLRSGKLARQSWLEKERLIDVFDVKSDVIKSLVEAGYNKDKLYIDDEAPSYYHPGKSGRIFLNKGKEKVVAFFGDIHPGILKKLDIKVESLVGFEIFLDNLKQPKKSLKDQKTQYKYSDFQKSERDFAFVLDKNFKVQELIETISNVDKELIKSVKVFDVYEGANIPEGKKSIALNVIIQPLEKTLTEDDLNKINQLIISAVESKTGAKIRS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily."}
{"protein": "MSDRPAARPWGKCGSLCRREEIMVAFKGVWTQAFWKAVTAEFLAMLIFVLLSLGSTINWGGKENPLPVDMVLISLCFGLSIATMVQCFGHISGGHINPAVTVAMVCTRKISIAKSVFYIAAQCLGAIIGAGILYLVTPPSVVGGLGVTTVHGNLTAGHGLLVELIITFQLVFTIFASCDSKRTDVTGSIALAIGFSVAIGHLFAINYTGASMNPARSFGPAVIMGNWENHWIYWVGPIIGAVLAGGLYEYVFCPDVELKRRFKEAFSKAAQQTKGSYMEVEDNRSQVETEDLILKPGLVHVIDIDRGDEKKGKDPSGEIAQTQH", "text": "FUNCTION: Forms a water-specific channel. Plays an important role in brain water homeostasis and in glymphatic solute transport. Required for a normal rate of water exchange across the blood brain interface. Required for normal levels of cerebrospinal fluid influx into the brain cortex and parenchyma along paravascular spaces that surround penetrating arteries, and for normal drainage of interstitial fluid along paravenous drainage pathways. Thereby, it is required for normal clearance of solutes from the brain interstitial fluid, including soluble beta-amyloid peptides derived from APP. Plays a redundant role in urinary water homeostasis and urinary concentrating ability. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Endosome membrane Cell membrane, sarcolemma; Multi-pass membrane protein Cell projection Note=Activation of the vasopressin receptor AVPR1A triggers AQP4 phosphorylation at Ser-180 and promotes its internalization from the cell membrane (By similarity). Detected on brain astrocyte processes and astrocyte endfeet close to capillaries (By similarity). SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MSSLISFIFLFLFSSITASAQNTFYLYHNCSVTTTFSSNSTYSTNLKTLLSSLSSLNASSYSTGFQTATAGQAPDRVTGLFLCRVDVSSEVCRSCVTFAVNETLTRCPKDKEGVFYYEQCLLRYSNRNIVATLNTDGGMFMQSARNPLSVKQDQFRDLVLTPMNLAAVEAARSFKKWAVRKIDLNASQSLYGMVRCTPDLREQDCLDCLKIGINQVTYDKIGGRILLPSCASRYDNYAFYNESNVGTPQDSSPRPGKGGNSSVIIIAVVVPITVLFLLLVAVFSVRAKNKRTLNEKEPVAEDGNDITTAGSLQFDFKAIEAATNCFLPINKLGQGGFGEVYKGTLSSGLQVAVKRLSKTSGQGEKEFENEVVVVAKLQHRNLVKLLGYCLEGEEKILVYEFVPNKSLDHFLFDSTMKMKLDWTRRYKIIGGIARGILYLHQDSRLTIIHRDLKAGNILLDDDMNPKIADFGMARIFGMDQTEAMTRRVVGTYGYMSPEYAMYGQFSMKSDVYSFGVLVLEIISGMKNSSLYQMDESVGNLVTYTWRLWSNGSPSELVDPSFGDNYQTSEITRCIHIALLCVQEDAEDRPTMSSIVQMLTTSLIALAEPRPPGFFFRSKQEQAGPSIDSSTHCSVDEASITRVTPR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CRK subfamily."}
{"protein": "MGMESSPESPQPVRVVLQAVGGWIGRLGRIWIEGQVAELHRRGGMAYITLRDPVANVSARVTCSIRVLRAADPPPEQGARVVVYAKPDFYVPRGTFSFQALEIRHVGLGELLARLERLRQALAAEGLFAESRKRKLPFLPGVVGLICGRDSAAERDVLENARRRWPAVRFEVREVAVQGDRAVPEVMAALEELDAHPEVDVIIIARGGGSLEDLLPFSDEALVRAVAAARTPVVSAIGHEQDTPLLDYVADLRASTPTDAAKKVVPDVGEQWELIRQLRDRARRVLEGGIAREEAWLASMRSRPVLANPVQEVERKIEQVFDLRDRGRRALTAALDRAGDNLAHIRARLHALSPATTLARGYAIVRRADGTVVRSAAEVAPGEELRLRFAEDGLVAIAQNREEDEL", "text": "FUNCTION: Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the XseA family."}
{"protein": "MVTIRLARGGSKKRPFYHLTVTNSRNARDGRFVERVGFFNPIAAGAEVKLSVNQERVSYWLSQGAQPSERVAQLLKDAAKAAA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MTVRILAVCGNGQGSSMIMKMKVDQFLTQSNIDHTVNSCAVGEYKSELSGADIIIASTHMAGEITVTGNKYVVGVRNMLSPADFGPKLLKVIKEHFPQDVK", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MPTTLIFTSFFLALLGLSLQRKHLLSLLLTLESMALALYVSTALWALNNTSLPIMAAPLIILTFSACEAGMGLSLMIATARTHNTDQLKALNLLKC", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
{"protein": "MKRRYFGTDGIRGQSNVFPMTPDLAMRVGIAAGTIFRRGNHRHRVVIGKDTRLSGYMLENAMVAGFTAAGLDAFILGPIPTPAVAMLTRSLRCDIGVMISASHNPYEDNGIKLFGPDGYKLSDDLEAEIEDLLEKDLNAQLAKSDDIGRAKRVDGVHDRYIEHAKRTLPRDVTLQGLRIAIDCANGAAYKVAPAVLWELGAEVVTIGNEPNGTNINLNCGSTSPVALQKKVDEVRADIGIALDGDADRVIIVDENGSIVDGDQLMAVIAESWAESQQLRGNGIVATVMSNLGLERFLDDRGMALARTRVGDRYVVEHMRQHNYNVGGEQSGHIVLSDYGTTGDGLVAALQILAAVKRTGRTVSEVCRRFEPVPQLLRNVRISGGKPLEDIQVQKAIADAEAELAKNGRLVIRPSGTEPLIRVMAEGDDRAQIERIVNELIGTISNVRTAA", "text": "FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MSSSKSLDWADDEDYGTGLPSIQTFDNPDGTKTMIEFRIDDNGKKVKVTRVIRKTVITERVQHAVAERKKWKKFGKEAGKNSGVDARTTSVGENVQLRLQLGWTTTKEEEQDEAALAAAKVKAKGSSVVRCRACKGNHFTAQCPYKSIIGPVDEPPLDASPVSSRASGALGEKGRYIAPHLRAGSGRESGDSMFKRERDDSATLRVTNLSDDTREEELRDLFRRFGGIQRVYLAKDKETGRAKGFAFVSYYDRDCAIKARDRLDGYGWNNLILRCEFSKPRD", "text": "FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit G family."}
{"protein": "MPRAVNGTIHKNRRKKVLAKAKGFRGGRSKLFRTAKSAVMKAGQWAYRDRRKKKSEFRKLWITRINAAVRENGMSYSKFIHALKTHGINLDRKTLADLAYNHKEVFNAIVEKTKVAK", "text": "FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
{"protein": "MLKTTKKSLLVFMGGFFLIFGVDQAIKYAILEGFRYESLMVDIVLVFNKGVAFSLLSFLEGGLKYLQILLILGLFIFLIRQIELFKTHAIEFGMVFGAGVSNVLDRFVHGGVVDYVYYHYGFDFAIFNFADVMIDVGVGVLLLRQFFFKQKQNKIKA", "text": "FUNCTION: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A8 family."}
{"protein": "MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H2A family."}
{"protein": "MGSSSLSEDYRQCLERELRRGRAGVCGDPSLRAVLWQILVEDFDLHGALQDDALALLTDGLWGRADLAPALRGLARAFELLELAAVHLYLLPWRKEFTTIKTFSGGYVHVLKGVLSDDLLLKSFQKMGYVRRDSHRLMVTALPPACQLVQVALGCFALRLECEILGEVLAQLGTSVLPAEELLQARRASGDVASCVAWLQQRLAQDEEPPPLPPRGSPAAYRAPLDLYRDLQEDEGSEDASLYGEPSPGPDSPPAELAYRPPLWEQSAKLWGTGGRAWEPPAEELPQASSPPYGALEEGLEPEPSAFSFLSLRRELSRPGDLATPESSAAASPRRIRAEGVPASAYRSVSEPPGYQAHSCLSPGALPTLCCDTCRQLHAAHCAALPACRPGHSLRVLLGDAQRRLWLQRAQMDTLLYNSPGARP", "text": "SIMILARITY: Belongs to the SPATA2 family."}
{"protein": "MLPYPQIDPVALAIGPLKIHWYGLMYLIGIGGAWLLASRRLNRFDPTWSREKLSDLVFWLSMGVIVGGRLGYVLFYDLHAYLANPTLIFEVWKGGMSFHGGFIGVMLAALWFGKRNNKSFFELMDFVAPLVPIGLGAGRIGNFINAELWGKPTDVPWAMIFPPFSDPAQLPRHPSQLYQFALEGVALFVILWLFSRKPRPTMAVSGMFALFYGIFRFIVEFVRVPDAQLGYIAWGWLTMGQILCVPMILAGLGLIWWAYNRKPTAKPA", "text": "FUNCTION: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Lgt family."}
{"protein": "MNSMEFPLLDRTTPNSVISTTPNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAIIDAITKLRKKVSREIYEDRIASQQEDRCFTTNHKFRVGRSIHTGNYDQELLYQSPSTSEILSETLFKYKSSLSSHELVN", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MIYNFGAGPSVLPKEVLKKVQEELLDFEKSGMSVMEISHRSKSFQEVIDEAQSNLRDLMSIPQNYKILFLQGGASTQFSMIPMNLALGKKAYYAISGAFGKKAYDEAVKLSQTLDFEAISLGSTQSEHYNHLLKIDKSKVDEKMAAYLHITTNNTIEGTTIFPENLPEVNSVPLIADMSSNILAVDYDVSKFGLIYAGAQKNLGIAGLTIVIIREDLLNQKESLSSMMDYRILAQNGSMYNTPPTFAIYLAGLVFKWVKEQGGVKKLEAINRQKARMLYDLIDQSDFYQSPVLNEAERSICNVVFTSPSKELDALFVQKAEEKGFKSIKGHRSVGGMRASIYNAFPIEGVLELVKFMKEFEEENK", "text": "FUNCTION: Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily."}
{"protein": "MATLCLFDMDGTLTAPRQKITEEMDGFLQKLRQKTKIGVVGGSDFEKLQEQLGNDVVEKYDYVFPENGLVAYKDGKLLCKQNIQGHLGEDVIQDLINYCLSYIANIKLPKKRGTFIEFRNGMLNVSPIGRSCSQEERIEFYELDKKEHIRQKFVADLRKEFAGKGLTFSIGGQISIDVFPEGWDKRYCLRHLEHAGYKTIYFFGDKTMPGGNDHEIFTDPRTVGYTVTAPEDTRRICEGLFP", "text": "FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol- phosphate-mannose required for a number of critical mannosyl transfer reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic PMM family."}
{"protein": "MLTTMSASSNTNSLIEKEIDDEDMLSPIKSNNLVVRVNQDTDDNLQALFDSVLNPGDAKRPLQLPLRMRKLPNSFFTPPAPSHSRANSADSTYDAGSQSSINIGNKASIVQQPDGQSPIAAIPQLQIQPSPQHSRLAIHHSRARSSPASLQQNYNVRARSDAAAANNPNANPSSQQQPAGPTFPENSAQEFPSGAPASSAIDLDAMNTCMSQDIPMSMQTVHKKQRSYDVISPIQLNRQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPRIQYRQQQQILMAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWEQAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPDNLVSSLQIEDNLCSNLFNDAQAIVNPPSSHKPDDLEWYKIN", "text": "FUNCTION: Transcriptional coactivator which is the critical downstream regulatory target in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:16096061, PubMed:18313299, PubMed:22615583, PubMed:27462444). The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein (PubMed:16096061, PubMed:19900439). The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam (PubMed:16096061, PubMed:18313299). Regulates the expression of G1/S-specific CycE and diap1, thereby promoting cell proliferation and inhibiting apoptosis (PubMed:18313299). Required for transcriptional activity of sd in wing imaginal disks (PubMed:18313299). Induces expression of expression of vestigial (vg) in wing and haltere disks and the expression of transcription factor E2f (E2f) (PubMed:18313299). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic (PubMed:18313299, PubMed:18256197, PubMed:19900439). sd promotes its nuclear localization (PubMed:18313299). 14-3-3epsilon, 14-3-3zeta and wts inhibit its nuclear localization (PubMed:18256197, PubMed:19900439). SIMILARITY: Belongs to the YAP1 family."}
{"protein": "MHTLVLVRHGQSVWNLENRFTGWTDVGLTPQGREEAAQAANLLRDGGYDFDACLTSVLSRAVMTLDILLTGLDRLWLPVTKSWRLNERHYGGLQGLNKAEMAAQYGEEQVFVWRRSYDTPPPALDPADERFPGRDRRYATLTDAELPRCESLKDTVARVMPFWHDVMAPAIASGTRLLVAAHGNSLRALVKYLDAIGDDAISECNIPTGVPLIYKLDASLKPLEHFYLGDAEAVARKAAAVAAQGKAKG", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
{"protein": "MAVPRNRHSNARKNIRRSHDAKKARHAAVCNNCKQAFIPHTVCTSCGFYNGKAVMTVEKK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
{"protein": "MMDKKKLHIAAGVICDKHNNVFIAQRPLKSHMGGFWEFPGGKLEDNETPEQALLRELQEEIGIDVTQCTLLDTVAHDFPDRHITLSFFLVTEWKNELTEKKGSCRVGHLLCL", "text": "FUNCTION: Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA. It prevents replicational errors by removing an oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MNIKTDGWSKKAHIVVAVSTGIDSMSLLYSLLNDYQHTYRKLTCVHVNHGLREQSYEEEAFLREYCHQHHIDIYIKRLDLSDIVADGNSIQQEARQRRYEWFGDIIAQLRADVLLTAHHLDDQFETIIYRLFTGRSTRNSLGMTYESYFNQYKVYRPMLNLKKTEILAYQYANQIPYYEDMSNQDRKYVRNDIRQRIIPAINENPHLNAHQLLKLKDWHDIELQSLKEQAETFINNEVSKSKYLTYSFSRTAFNELNVNIKSVVMDLLFEKLDCHLAMPQHAYDEWFEQIRNDKSQFNIHVTDEWIIQIAYDKLIIMAKSEMDQYILDRICIRKPGTYEFNDYQIDIHPDLPQQLYPLTVRVRQNGDVYKLNGQKGHKKVSRLFIDKKVTLAERQRIPLIINQENAVLAIGDLYVKENFKEFILISNNGDEL", "text": "FUNCTION: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family."}
{"protein": "MSYTFDWLSKDVVKKLQGRDLRPVKCLSDATKFCLFNILQETSSRLALKTEYIPVGFTLLHLLEPNIPVPEPEVSAPIPLKHTISQKLKADLDVETIAGGEAGFVKSCGYDIEVQSKSIPNPKLESLQNRKLLDQLPTFMKTCWKDGKNLYVVTEAYEVTKDTVLEGTSNSKFAIKGIINQLVKVGGSGQWQTEKTDSIPIQKGSVLAYKKQQLVIEDNTCVILTSANTKKKMTFPMRFVGMSGHLRYQDLVIETGSWINDIDPIGTIKEPTHLDFMCLQNEVSEQTRLLAELSKDVQEVVFSSFLHMLCDRDVLYDLMKMLELNQLGHMDGPGGKILDELRKDSSLSWINLKDLILYLLQALMVLSDTQLCLLALSVEMRLLPHQVELVKSILQPNFKYPWNIPFTLQPQLLAPLQGEGLAITYELLEECGLKMELNNPRSTWDLEAKMPLSALYGSLSFLQQLSEA", "text": "FUNCTION: [Gasdermin-C]: This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-C, N-terminal) binds to membranes and forms pores, triggering cell death. FUNCTION: [Gasdermin-C, N-terminal]: Pore-forming protein that causes membrane permeabilization and pyroptosis (By similarity). Released upon cleavage and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (By similarity). The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown (By similarity). SUBCELLULAR LOCATION: [Gasdermin-C]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Gasdermin-C, N-terminal]: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the gasdermin family."}
{"protein": "MAQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEDVLLKDH", "text": "FUNCTION: This protein is an aporepressor. When complexed with L- tryptophan it binds the operator region of the trp operon (5'- ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TrpR family."}
{"protein": "MTYSLLPHIHSPQDLHALSLDKLPVLCDEIRNKIIESLSLTGGHLASNLGGVELTVALHYVFSSPDDQFIFDVGHQSYVHKLLTGRNTEAFSNIRHDNGLSGFTTPQESNHDIFFSGHAGNALSLALGLAKGSSNSSSHILPILGDAAFSCGLTLEALNNIPADLSKFIIVLNDNQMSISENVGNIPQGISHWMYPQKISKLSQKIHSWIQNLPSFLHKKKTLSHKVDIALKSLSHPLFEQFGLHYVGPIDGHNVKKLVQALQMIKDQPQPILFHVCTVKGNGLAEAERDPIRYHGVKAHFQNTSLKKTSGNVELQTPISFPQHAGNILCRLGKKYPQLQVVTPAMSLGSCLEDFRKQFPDRFTDVGIAEGHAVTFSAGIARSGTPVCCSIYSTFLHRAMDNVFHDVCMQELPVIFAIDRAGLAFHDGRSHHGIYDLGFLCSMPNMVICQPRNALVLERLFFSSLLWKSPCAIRYPNIPANEKASNSFFPFSPILPGEAEILCQGDDLLLIALGHMCNTALTVKEHLLDYGISTTVVDPIFIKPLDRKLLQSLLTHHSKVIILEEHSIHGGLGSEFLLFLNQHNIKADVLSLGVPDMFIPHGNPETILNLIGLTSDHITQRILSHFKFFTPIPIERFFKA", "text": "FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP). SIMILARITY: Belongs to the transketolase family. DXPS subfamily."}
{"protein": "MISSIYIFKILLSYLGVEYEINQLSEINQEFTNKLESYNQFIKHTQKDEDYLLGQSAVISRYISNNHNFSGKSLQESARVDDIVESVLEIIEEYVLPIINSNIINEEITKLLCTHFNDFENQLSKSTFSAGDSTTLADLYLFILYDITLRYLENHGHLAHHFNEKYPHLERLKLHFLSNKSVSEFINSNNINSQSSQLII", "text": "SIMILARITY: Belongs to the GST superfamily."}
{"protein": "QFSPNLSFSAFFPIITFTTATMGFQKIKVANPIVEMDGDEMTRIIWKYIKDKLIFPFVELDIKYFDLGLPYRDETNDKVTVESAEATLKYNVAIKCATITPDEARVKEFGLKSMWRSPNGTIRNILNGTVFREPIICKNIPRLIPGWTKPICIGRHAFGDQYRATDSVIKGPGKLKLVFVPEGQGETTDLEVYNFTGEGGVALAMYNTDESIRSFAEASMAVALEKKWPLYLSTKNTILKKYDGRFKDIFQEVYEAGWKSKYEAAGIWYEHRLIDDMVAYALKSEGGYVWACKNYDGDVQSDFLAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHFRVHQKGGETSTNSIASIFAWTRGLAHRAKLDDNATLLDFTEKLEAACIGVVESGKMTKDLALILHGSKLSREHYLNTEEFIDAVAAELKTKISA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family."}
{"protein": "METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ", "text": "FUNCTION: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. SUBCELLULAR LOCATION: Cytoplasm, cytosol Preautophagosomal structure Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation. SIMILARITY: Belongs to the ATG13 family. Metazoan subfamily."}
{"protein": "MTFKVAIIGRPNVGKSTLFNRLVGRKLALVDDTPGVTRDRRVHAAKLYDLHFDVIDTAGFEDAGASTLPGRMRAQTEIAIHEADLIFFTIDAKSGLLPDDRTFAEIVRKSGKPVVLVANKAEAKGAQGGMLEAWELGLGEPIPVSAEHGQGMPDLRDAVIAALGEARAFGEEEEGEDDEIAATEVLIGEDIADPDAEDAHTYDNTKPMRIAVVGRPNAGKSTLINALIGEERLLTGPEAGITRDSISVDWDWHGRRLKLFDTAGMRRKARIHEKLEVMSVQDGLRAIRFAEIVIIVLDATIPFEKQDLQIADLIIREGRAPVIAFNKWDLIDHPQELLAELREKTERLLPQVRGIQAVPVSAETGRGLDKLMDAVLRTHKVWNSRVSTGKLNRWLEAILAHHPPPAVAGRRLKVKYVTQAKTRPPGFVVQCSRPDAMPQSYVRYLSNSLREAFDMPGVPIRIALRTSDNPFAGRAKKRG", "text": "FUNCTION: GTPase that plays an essential role in the late steps of ribosome biogenesis. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family."}
{"protein": "MDLVQKQKSLQDYTKSLFLEGILDSQFLQLQQLQDESNPDFVSQVVTLFFQDSDRILNDLSLSLDQQVVDFKKVDPHVHQLKGSSSSIGAQRVKNACVVFRSFCEQQNVEACHRCLQQVKQEYYLVKNRLETLFKLEQQIVASGGMIPAVELGF", "text": "FUNCTION: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction through the multistep His-to-Asp phosphorelay. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus."}
{"protein": "MESPSARTLGNSLGDDSGNGNENGNGSGNGNTTMMPHGIYHERQTRHLCGLHALNNLFQGPDMFSKSELDDYCTTLTPRNWLNPHRSWIGWGNYDVNVIMYALQQRNCEAVWFDRRRDPHCLNLSVIFGFILNVPAQMSLGYYIPLPFHMRHWLALRRLNGSYYNLDSKLREPKCLGTEQQFLEFLATQLQMDHELFLVLDEETDCKDKSQQRWLLPQFRD", "text": "FUNCTION: May act as a deubiquitinating enzyme."}
{"protein": "MQLDIKICGLKTEDAIAAALDGGASHVGFIFFPKSPRNVDIETAARLRHLASGRAQAVAVTVDADDEMLDRIVEGMRPDVLQLHGHERPVRVEALKKRYHLPVMKAVSVREASDLEVLPAYRGVADRFLLDAKPPAGAELPGGNGIPFDWSLLASLDGKVDYMLSGGLSAVNIGEALSIARPRGIDISSGVERAPGEKDPDLIRAFFSAVRAARGKRE", "text": "SIMILARITY: Belongs to the TrpF family."}
{"protein": "MLISQRPTLSEDVLTDNRSQFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFTTVPGVKEDVTEIILNLKSLVVSSEEDEPVTMYLRKQGPGEVTAGDIVPPAGVTVHNPGMHIATLNDKGKLEVELVVERGRGYVPAVQNRASGAEIGRIPVDSIYSPVLKVTYKVDATRVEQRTDFDKLILDVETKNSISPRDALASAGKTLVELFGLARELNVEAEGIEIGPSPAEADHIASFALPIDDLDLTVRSYNCLKREGVHTVGELVARTESDLLDIRNFGQKSIDEVKIKLHQLGLSLKDSPPSFDPSEVAGYDVATGTWSTEGAYDEQDYAETEQL", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the RNA polymerase alpha chain family."}
{"protein": "MGQKIHPLGFRLGVTQNHHSTWFAPLNNYSELLKEDERIRNCIQQYVRKYVRSSSRSAEIARVQIQKKTDLVEVQIHTASPSLLVQTRVPNRSTNTQEIGIEYLRRNIQNTLNPGNRKLNMTLSQVAKPYGEAIILAEYIALQLESRVAFRKTMKQAIKLANKSGNARGIKIQIAGRLNGAEIARVEWAREGRVPLHTLRAQIDYCHYPAQTIYGVLGIKVWVFQNKSLISNNQQM", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
{"protein": "MAVTLDRAVEASEIVDALKPFGVTQVDVAAVIQVSDRAVRGWRTGDIRPERYDRLAQLRDLVLLLSDSLTPRGVGQWLHAKNRLLDGQRPVDLLAKDRYEDVRSAAESFIDGAYV", "text": "FUNCTION: Probable antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the activity of cognate toxin Rv3189 by blocking access to the toxin active site. SIMILARITY: Belongs to the MbcA/ParS/Xre antitoxin family."}
{"protein": "MHLYRSHTCGALSRGDVGQTVRLSGWVHRKRDHGGVLFVDLRDHYGMTQIVADADSPALPILEALRVESVVTIDGEVKARSEGTVNANLSTGEIEVFARVATVLSAAEELPMPVAGEQEYPEDIRLRYRFLDLRRETLHANIVKRTKVISDMRRRMEGAGFTEYSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVIGGVFEAFADGRKVTPIGSFPRIPYAEAMLKYGSDKPDLRNPIIISDVSEEFAQSGFGLFEKIVGTGGVVRLIPAPNTADKSRKFFDEMNDWARAEGHAGLGYVTRKQGEFGGPIAKNHGADKMAALFDRLGLGPDDGCFFAAGKAEQAAKLAGAARTRVADQLGLIDKDRFELCWIVDFPFYEWDEENKKVEFSHNPFSMPQGGLDALNTQDPLTINAFQYDLVCNGFEIASGSIRNQSPETMVKAFEIVGLSKADVEERFGGLYRAFQYGAPPHGGMAAGVDRIVMLICGAQNLREITLFPMNQRAEDLLMGAPSPAALKQLRELNIRVVEQTKG", "text": "FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily."}
{"protein": "MQKYTSEARQLLALAIPVILAQVAQTAMGFVDTVMAGGYSATDMAAVAIGTSIWLPAILFGHGLLLALTPVIAQLNGSGRRERIAHQVRQGFWLAGFVSVLVMIVLWNAGYIIRSMHNIDPALADKAVGYLRALLWGAPGYLFFQVARNQCEGLAKTKPGMVMGFLGLLVNIPVNYIFIYGHFGMPELGGIGCGVATAAVYWVMFIAMLSYIKHARSMRDIRNEKGFGKPDSVAMKRLIQLGLPIALALFFEVTLFAVVALLVSPLGIVDVAGHQIALNFSSLMFVLPMSLAAAVTIRVGYRLGQGSTLDAQTAARTGLGVGICMAVVTAIFTVTLRKHIALLYNDNPEVVALAAQLMLLAAVYQISDSIQVIGSGILRGYKDTRSIFFITFTAYWVLGLPSGYILALTDLVVDRMGPAGFWMGFIIGLTSAAVLMMLRMRYLQRQPSAIILQRAAR", "text": "FUNCTION: Multidrug efflux pump that functions probably as a Na(+)/drug antiporter. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family. MdtK subfamily."}
{"protein": "MIISEANRKEICKYLFKEGVCFAKKDFNLAKHPLIDVPNLQVIKLMQSFKSKEYVRETFAWMHYYWFLTNEGIEFLRTYLNLPSDVVPATLKKSAKPGGRPFGGPPGDRSRGPRHEGGDRPRFGDRDGYRAGPRAGGEFGGEKGGAPADYQPSFQGSGRGFGRGAGGYSAAAPSGSGLP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family."}
{"protein": "MGKKSEKKVVEETMEVDEQPAVEPEAVPEEEPEVEDEDLNVPKKKKMEILDPKSFEQDPSNLTLILYEEDHTIGNSIKHILSRMDEVEFCGYNVPHPLEDKILFRVQTKDGINALEVLVKAFESVEQVFSTIRGKFEAAYEKSIA", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family."}
{"protein": "MVRATGSVASRSRRKRVLKQAKGFWGDRKGHFRQSRSSVMRAMAFNYMHRKDRKGDFRSLWITRLSVASRIHGLSYSRLINGLKQAGIHLNRKMLSEMAIHDPQGFAVVATQAKLALEAAVQG", "text": "FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity). SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
{"protein": "MGSWKSGQSYLAAGLLQNQVAVVTGGATGIGKAISRELLHLGCNVVIASRKLDRLTAAVDELRASQPPSSSTQVTAIQCNIRKEEEVNNLVKSTLAKYGKINFLVNNAGGQFMAPAEDITAKGWQAVIETNLTGTFYMCKAVYNSWMKDHGGSIVNIIVLLNNGFPTAAHSGAARAGVYNLTKTMALTWASSGVRINCVAPGTIYSQTAVDNYGELGQTMFEMAFENIPAKRVGLPEEISPLVCFLLSPAASFITGQLINVDGGQALYTRNFTIPDHDNWPVGAGDSSFIKKVKESLKKQARL", "text": "FUNCTION: Participates in chain elongation of fatty acids. Catalyzes the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1 to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA reductase activity. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MDKNTITGLVLIGILLVGFSFLSRPSEEQIAAQKRYYDSIAVVQQQEEALRAKTEAALANEKEETAADSASLFFSATKGKEAFTTIQNNLVEITLDNKGGRVYSALLKNYMGQDKKPVVLFNGSDASMNFNFYNKKGALQTKDFYFEAVNKTDSSVTMRLAADSASYIDFIYTLKPDNYLMSFVIKATGMDGKLAASTNYVDISWSQRARQIEKGYTYENRLADLTYKYTGDDVDNLSASKDDEKSVSERLDWIAFKNQFFSSVFIAEQDFEKTTVKSKMEKQGSGYIKDYSAEMSTFFDPTGKQPTDMYFYFGPNHYKTLTALDKGREEKWELNNLVYLGWPLIRWINKWITINVFDWLSGWGLSMGIVLLLLTIMVKIVVFPATWKTYMSSAKMRVLKPKIDEINKKYPKQEDAMKKQQEVMGLYSQYGVSPMGGCLPMLLQFPILMALFMFVPSAIELRQQSFLWADDLSTYDAFITFPFHIPFLGNHLSLFCLLMTVTNILNTKYTMQQQDTGAQPQMAAMKWMMYLMPIMFLFVLNDYPSGLNYYYFISTLISVVTMIILRRTTDENKLLTELEAKKKDPKQMKKTGFAARLEAMQKQQEQLAKERANKQNKK", "text": "FUNCTION: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily."}
{"protein": "MTTIAIVDYGVGNLRSVAQALRAAAPEADVRVVDAPEGIRSADRVVLPGQGAMPDCMSALGASGLQEAVIEAAASKPMFGVCVGEQMLFESSSEARPGTDKTPCLGLMPGEVIRFELDGMTQPDGSRYKVPQMGWNRVKQSRPHPLWDGIPDESWFYFVHSYFVRAQDPAHIAGETEYGVVFTSAVARDNIFATQFHPEKSAAMGLQLYRNFVHWNP", "text": "FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAKANIGKLLLTGVVGGAIALGGSAIYQSTTNQSANNSRSNTTSTKVSNVSVNVNTDVTSAIKKVSNSVVSVMNYQKDNSQSSDFSSIFGGNSGSSSSTDGLQLSSEGSGVIYKKSGGDAYVVTNYHVIAGNSSLDVLLSGGQKVKASVVGYDEYTDLAVLKISSEHVKDVATFADSSKLTIGEPAIAVGSPLGSQFANTATEGILSATSRQVTLTQENGQTTNINAIQTDAAINPGNSGGALINIEGQVIGITQSKITTTEDGSTSVEGLGFAIPSNDVVNIINKLEADGKISRPALGIRMVDLSQLSTNDSSQLKLPSSVTGGVVVYSVQSGLPAASAGLKAGDVITKVGDTAVTSSTDLQSALYSHNINDTVKVTYYRDGKSNTADVKLSKSTSDLETSSPSSSN", "text": "FUNCTION: Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S1C family."}
{"protein": "MKAEGGDHSMINLSVQQVLSLWAHGTVLRNLTEMWYWIFLWALFSSLFVHGAAGVLMFVMLQRHRQGRVISVIAVSIGFLASVTGAMITSAAVAGIYRVAGKNMAPLEALVWGVGQTVLTLIISFSRILATL", "text": "FUNCTION: Negatively regulates the canonical Wnt signaling in breast cancer cells. Exerts an inhibitory effect on breast cancer growth by inhibiting CTNNB1 stabilization and nucleus translocation, which reduces the activity of Wnt targets (PubMed:29367600). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM170 family."}
{"protein": "MTLNLAEYDVLVFDIEGTVCPISFVKDVLFPYALEALPKVLDQEWDSPEFAKYRDAFPEEYRNSRPDFEAHVRDLVKRDVKIAYLKSLQGYLWLQGYKSGDIVAPLFPDVDPFFNQAVKDGKKIIIYSSGSVPAQKLLFSHTNSEKSDMTPLIADYFDTTNAGPKTEVDSYRKIISSHPEHKDLGRWLFLSDNIHEVSAAVEAGIRSVPVIRDGNAPLPPDNSLTKLAISEFKHSEDA", "text": "FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3- diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK- MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family."}
{"protein": "MKNDLILRAAKGEEVERPPVWIMRQAGRYLPEYHKLRAKQSFFEMCQTPETACELTLQPVTRFKGLLDAAIIFSDILVIPQALGMQVVMLEQKGPHFPKPLVVPEDIDLLEKTPNISAKLGYVMDAISLTREKLDGQVPLMGFSGAPWTIMAYMIEGGGSKTFAKAKSWLFRYPEASHKLLKIITDATVSYLIQQVYAGAQLLQIFDSWAGELSPEDFTEYAYPYLVRICQEVKQHLKKKKRDEVPMIVFAKGAWYAIDQLCDSGYDVIGLDWTVSPKEAVRIRGNRRVTFQGNLDPNILYGTREIIEARTKEMIQDFGGGKQGYIINLGHGITPGVNPDDVRFFLEKCHQYGSA", "text": "FUNCTION: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family."}
{"protein": "MWSKRDEQKTYPPIRLNPFVFWSSAISISIFGMLFVLFPETSQHGLTWIQQQVNQLFGWYYMLVIILSLGFVAWLAFSQVGNIPLGKAQDKPEFGYLVWTSMLFSAGIGIALLYYGVAEPVDHFLRPPEGQGGTVEAAQNAMMYSFLHWGIHGWVLYALVGVTLGYFAFRRDLPLALRSALYPIFGERIHGLVGHMVDGFGILATIISLVTNLGIGALVMISGISYLFPDLPNTSSTLVVTVIMMMLVATLTTVIGIEKGLAWLSRINLRLLYLLLLFVFLTGPTNHLLNGLVQNTGDYLSHFVQKSFDLYLYDKNATGWLASWTIFYWAWWIAWAPFVGMFIARISKGRTIREVVLGVCLIPLGFTLAWISIFGNTAIDLILNHGQQIIGSLVIQDPALSLFKLLEYLPFHPYVAGIVVVICFVLFLTPVGSGTLMIANLSSQGGSSDSDSPIWLRVFWSIAITIVSIGLLLAGSFSAMQSAVVLCGLPFSVILLLYMFGLAKALKQETQQPVVESHTTETSGSD", "text": "FUNCTION: Sodium-independent high-affinity choline uptake system. Uptake is not proton coupled. May play a role in metabolic adaptation to choline-containing environments. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family."}
{"protein": "MLDLCITGGRVVLPSGVEETDVGIQAGKIARIGPINKKEARCIMNANGQYVFPGAVDTHVHFSEPGRTEWEGFFTGSRSLAAGGTTTYVEMPLNALPATTNRANLQRKLEAAKGQNYVDYSFYGGLVPTNLHELADLSASGVVAFKCFLSPCGSDIPGDFRNVDLNGLRAGMRLLAEKGQLLCVHAEDPSMISQLEAKLLSPVGADAYVASRPVEAEVKAVCDTLAAARETGCRIHFVHISSAAAIEAIERAKEEGVDVTVESCPHYFLLSAEELAELGPLAKCQPPLRPKQEQAKLWACLLDGQIDWLASDHSPCTPDLKDGDFLTAWGGISGCQNNIDIMFDAAVKRRGMPPEQLARLIATNPAKRMNLREKGEIAIGKDADFAFVDDRQSYTLTKEQLYYKNKHSPYVGRTIGCKVRRVLLRGQTIYTEEKGIIGKPSGELLHIH", "text": "FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family."}
{"protein": "MRKPIIAGNWKMNKTLAEAVSFVEEVKGQIPAASAVDAVVCSPALFLERLVAKAEGTDLQVGAQNMHFEKNGAFTGEISPVALSDLKVGYVVLGHSERREMFAETDESVNKKTLAAFEHGLTPIVCCGETLEERESGKTFDLVAGQVTKALAGLTEEQVKVTVIAYEPIWAIGTGKSSSSADANEVCAHIRKVVAEAVSPEAAEAVRIQYGGSVKPENIKEYMAQSDIDGALVGGASLEPASFLGLLGAVK", "text": "FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family."}
{"protein": "MKFEKGKVRILPKPSPTPTNPQTPLPLLPAQTKPVNSKRKSAASTPGNESKKSRKSNSTASTPNSATPTSVGTPPQKTSKPTGHRPVTSCTFCRQHKIKCNASDNYPNPCERCKKMGLKCEIDPEFRPRKGSQIQSLKSDVDELKAKIEMLTKNESLLTQALNQHNLNHASQQQQSSGSQSQQQHPPNPQRALSYTSANSSPQVAFSNASPIPSVTSIQQNAPLTHENSDNSPYALNTPENIEELQPISEFILGDVTLPLNRANELHDKFMTTHLPFLPIIISRSATELYHKSQLLFWAVILTASLSEPEPKLYMSLASLIKQLAIETCWIKTPRSTHVIQALIILSIWPLPNEKVLDDCSYRFVGLAKNLSLQLGLHRGGEFIQEFSRNQVSLGPDAERWRTRSWLAVFFCEQFWSSLLGLPPSINTTDYLLENARVDKSLPKNFRCLISLSIFQCKLVNIMGISVTRPDGLLEPSNRAGSLSLLDRELERLRFKLQFEEGGPIEVYYLYIKLMICCFAFLPGTPIEDQVKYVSFAYLSATRIVTIVSKMVNDISLIELPIYIRQAVTYSVFMLFKLHLSRYLIDKYVDSARQSIVTVHRLFRNTLSSWKDLQNDISRTAKVLENLNMVLYNYPEIFLNDSENEDSSIITRMRSHLTASLFYDLVWCVHEARRRSVLDKGKRQAQPNKKILPLPFYNQITKDDFKTITTTSPNGTTITTLVPTDQAMNQAKSKSFDSSKPLEINGIPLPMLEATGSTREVLDSLPSQSLPSQAPTLQQYPMQQDQQQQEPSQQQQQKHSQQSQQYQQQQQSNQQQPHLQHQRQFQQSPPPQFSMISSTPPLQQPPFILANSPLPQTYLPKIDEMNMSPEVKQENSVAPFASQITNFFDQQTSGWFNNDNQDDDFLGWFDVNMMQEK", "text": "FUNCTION: Transcription factor which plays an essential role in virulence by activating the transcription of iron uptake genes such as FRE7 in iron-poor environments such as the host bloodstream and internal organs. Promotes commensalism in a mouse model of gastrointestinal infection. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Interaction with SFU1 promotes cytoplasmic localization whereas interaction with SSN3 and subsequent phosphorylation promotes nuclear localization. Nuclear localization is associated with virulence."}
{"protein": "MNTNDIRTVKGEKSLQGTIKVPGDKSISHRSLIIGSIAEGETNIEGFLYSEDPLSTADCLRKLGVHIPEIKKDQPFTIRGLGIDGFREPKEILNCGNSGTTMRLLMGLLAGQTDRNFILTGDKSLNERPMGRVSKPLSLMGGKIYGRENGTKAPISITGNKLKGCVIGTPVASAQVKSAILLAGLNASGTTSVIEPASSRDHTERMLKAFGADIKIRGELGRNIVIKSGNNLTGQNILIPGDISSAAFWMIAASIVPESEILVKNVGLNPTRTGILHVMDEMGCDYKIIEKSTIAGEPIGSIKVKYVSNLKPFKVQGDILPKLIDEIPILTVAACFCNGVSEIKDAKELRVKETDRLKVMARQLKKFGANITEKEDGLIITGESKFHSAEVDSETDHRVSMSLAIASLLAKGSTRIARAGASNVSYPTFWDDLEKLIN", "text": "FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family."}
{"protein": "MANAGLQLLGFILAFLGWIGAIVSTALPQWRIYSYAGDNIVTAQAMYEGLWMSCVSQSTGQIQCKVFDSLLNLSSTLQATRALMVVGILLGVIAIFVATVGMKCMKCLEDDEVQKMRMAVIGGAIFLLAGLAILVATAWYGNRIVQEFYDPMTPVNARYEFGQALFTGWAAASLCLLGGALLCCSCPRKTTSYPTPRPYPKPAPSSGKDYV", "text": "FUNCTION: (Microbial infection) Acts as a co-receptor for hepatitis C virus (HCV) in hepatocytes (PubMed:17325668, PubMed:20375010, PubMed:24038151). Associates with CD81 and the CLDN1-CD81 receptor complex is essential for HCV entry into host cell (PubMed:20375010). Acts as a receptor for dengue virus (PubMed:24074594). FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions (PubMed:23407391). SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein Basolateral cell membrane Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. SIMILARITY: Belongs to the claudin family."}
{"protein": "MASNSTPKYNSNSLENSLRRSPGDGMNHEQNDEIPCLPGEALITDKDVIYMCPFYGPVKGRIHVTNYKLYFKGEEMEPLISFSVPLGVIARIEKMGGASSRGENSYGLDITCKDMRNLRFALKQEVHSRKQIFEDLTKYAFPLSHGLLLFAFQNEEKFPENGWAVYDAMTEFRRQGLPNGQWRITFINKNYELCDTYPPLLVVPYSASEEDLKKVAAFRSRNRIPVLSWLHPENQSAIMRCSQPLVGMSGKRNKDDERYLDIIRDTNGQTSKLTIYDARPNVNAVANKATGGGYESEDAYPNAELVFLDIHNIHVMRESLKKLKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVASGKSSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIVGFEVLVQKEWISFGHKFSSRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEHFLITVLDHLYSCRFGTFLYNCENIRDKEKVREKTQSLWSLISSEKSKYTNPFYTKELNRVLYPVASMRHLELWVNYYIRWNPRIRQQQPNPVEQRYMELLALRDDYVRRLEELQITNSPKMNSSTTSPSSPSQIMPQVHTPF", "text": "FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Cell projection, filopodium Cell projection, ruffle Late endosome Cytoplasm, myofibril, sarcomere. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily."}
{"protein": "MQRMIEISSPFFLNPDELSTPADWAAVFGNANPLALEIGCGIGDFIARTAADNPGTNYIAIDFYNKGCDKTCRRLERLAIPNVRVVRDEARKFIVERIPKGSLCAVHINCPDPWPKMRHRKRRLVNREFAAFIREYLAPGGDFYFATDFDDYGIDVAEFMPGVEGYANMLAPDRYRHELEGYHLSKYMMKFMAEGKRIYFVHYRKTAEGAA", "text": "FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family."}
{"protein": "MTDHYDVVVVGGGHAGCEAASAAARAGAKTALVTLRFDTIGVMSCNPAIGGLGKGHLVREIDAMDGLMGRVADAAGIQFRLLNRRKGPAVRGPRTQADRKLYRLAMQEAIRQQNDLDVVEGEVLDFEINEGRITAVLLAGGRRLACGAVVLTTGTFLRGLIHIGEKKIVAGRMNEQASLGLSATMDRAGFKLGRLKTGTPPRLDGKTIDWASLESQAADEDPVPFSLMSDRITTPQIECGITRTTSATHELIRANLGRSAMYSGSIEGVGPRYCPSIEDKIVKFGDRDGHQIFLEPEGLDDDTVYPNGISTSLPQDVQLEILKTIPGLERATMLQPGYAIEYDHVDPRELHQTLETKRIAGLFLAGQINGTTGYEEAAGQGLLAGLNAARRAAGGEQIVLSRTEAYIGVMVDDLTSRGISEPYRMFTSRAEFRLSLRADNADERLTPLAAKLGIASVQRMQRYGDVMQRLDAARELARSVAMTPNEAARQGLEINRDGVRRSGYELLAYPDVDVAWLARVEPKFAAIDAKTAERLETEAKYSVYLDRQKSDVAQIRHEESRLIPETVDFAGVPGLSNELKQKMQARRPRSIADAQRMEGMTPAALAIIVAHVRHYENAQRDVA", "text": "FUNCTION: NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmG family."}
{"protein": "MAIEKKFVNDGYVKASMDEYFAEQLNRAGYGGMELNRTPMGTQIIIYSEKPGMVIGKAGKVIRKLTRDVATKYNLENPQIDAQEVKKPELNAQMMASRLAASIERGWYFRKAGHNTIRAVMNAGALGCEVVISGKLTGARSRVEKFVDGYIKHSGHPVEEVVDEGFAVAIKKLGTLGCKVRIIQPGVVLPDSYKVRESVEIEEPAEKPAEKQVEKPAVAPKKEAAKAKAPAPAAAPEPAPTEEPEVAEPEEAEEAQVEASEDFEEAELIYVEGSEEVRRQVNGVWQHKHESYDYWHPMARVHKEAKE", "text": "FUNCTION: Binds the lower part of the 30S subunit head. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
{"protein": "MLGKGIKKSWGWLGLTVLLLGSPCGWAAEFSASFKGTDIQEFINTVSKNLNKTVIIDPTVRGTISVRSYDMMNEGQYYQFFLSVLDVYGFSVVPMDNGVLKVIRSKDAKSSSIPLANNEQPGIGDELVTRVVPLNNVAARDLAPLLRQLNDNAGAGTVVHYEPSNVLLMTGRAAVIKRLVDIVNTVDKTGDREMVTVPLTYASAEDVAKLVNDLNKSDEKNALPSTMLANVVADGRTNSVVVSGEENARQRAVEMIRQLDRKQVVQGGTKVIYLKYAKALDLIEVLAGNGTSGNRNSSSSNASRPSSPRSGSSSNSNSSSGSSGSSSGSSSSSSSSSSMGFGSAFGSTSSSGGRTITIQGKEVTVRAHDQTNSLIITAPPDIMRDLEQVINQLDIRRPQVLVEAIIAEIQDADGLNLGIQWANKRAGMTQFTNTGIPISTAVIGTDQFRSNGTLTTAYASALSSFNGVTAGFYRGNWSMLLTALSSDSKNDVLATPSIVTLDNMEATFNVGQEVPVLTGSQTTSADNIFNTVERKTVGIKLRVKPQINEGDSVLLQIEQEVSSVADSNSSTNSSLGVTFNTRTVNNAVMVTNGETVVVGGLLDKTSVESNDKVPLLGDIPWLGSLFRSKSQEVRKRNLMLFLRPTIIRDPGQFQEASINKYRSFNNEQQQQRGEGNGVLDNNTLRLSGGNTYTFRQVQSSISDFYKPEGR", "text": "FUNCTION: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for the translocation of the multiple pectic enzymes (Probable). This subunit forms the outer membrane channel (By similarity). SUBCELLULAR LOCATION: Cell outer membrane Note=Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane. SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily."}
{"protein": "MPIQVVSADFDKTATRPEEWPRGATPEIAFVGRSNVGKSSMLNALARRKGLARVSSTPGRTRALQFFDLSYRPTPAARPRAIRFCDLPGYGYAKVSRAERDRWTAMIEDYLRDRDVLRAVVLIVDARHAPSESDEDAAAFLVSAGRRLVVAATKTDKLPKARRVLALQQVERALGLARGDAVPFSAVEGTGTDALWARLAALAAEEARTAEADPPA", "text": "FUNCTION: Necessary for normal cell division and for the maintenance of normal septation. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family."}
{"protein": "MPTVISASMAPRTGASQVPRTMPQAAQGKGTEAGVGNPGGKYSAIISRNFPIIGVKEKTFEQLHKKCLEKKVLYLDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIGGANRTDICQGDLGDCWFLAAIACLTLNKRLLFRVIPHDQSFTENYAGIFHFQFWRYGDWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFFEIKDAPRDMYKIMKKAIERGSLMGCSIDDGTNMTYGTSPSGLKMGDLIARMVRNMDESRLRDSDLIPEGCSDDRPTRTIVPVQFETRMACGLVKGHAYSVTGLEEALFKGEKVKLVRLRNPWGQVEWNGSWSDSWKDWSFVDKDEKARLQHQVTEDGEFWMSYDDFIYHFTKLEICNLTADALESDKLQTWTVSVNEGRWVRGCSAGGCRNFPDTFWTNPQYRLKLLEEDDDPDDSEVICSFLVALMQKNRRKDRKLGANLFTIGFAIYEVPKEMHGNKQHLQKDFFLYNASKARSRTYINMREVSERFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEVENTISVDRPVRKKKTKPIIFVSDRANSNKELGVDQESEEGQDKTSPDKQEKSPKPEPSNTDQESEEQQQFRNIFRQIAGDDMEICADELKNVLNRVVNKHKDLKTEGFTLESCRSMIALMDTDGSGRLNLQEFHHLWKKIKSWQKIFKHYDTDQSGTINSYEMRNAVNDAGFHLNNQLYDIITMRYADKYMNIDFDSFICCFVRLEGMFRAFNAFDKDGDGIIKLNVLEWLQLTMYA", "text": "FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1. Mediates, with UTP25, the proteasome- independent degradation of p53/TP53. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the peptidase C2 family."}
{"protein": "MVSFRGLTTLTLLFTKLVNCNPVSTKNRDSIQFIYKEKDSIYSAINNQAINEKIHGVNLGGWLVLEPYITPSLFETFRTNPYNDDGIPVDEYHFCEKLGYEKAKERLYSHWSTFYKEEDFAKIASQGFNLVRIPIGYWAFTTLSHDPYVTAEQEYFLDRAIDWARKYGLKVWIDLHGAAGSQNGFDNSGLRDSYKFLEDENLSATMKALTYILSKYSTDVYLDTVIGIELLNEPLGPVIDMERLKNLLLKPAYDYLRNKINSNQIIVIHDAFQPYHYWDGFLNDEKNEYGVIIDHHHYQVFSQVELTRKMNERIKIACQWGKDAVSEKHWSVAGEFSAALTDCTKWLNGVGLGARYDGSWTKDNEKSHYINTCANNENIALWPEERKQNTRKFIEAQLDAFEMTGGWIMWCYKTENSIEWDVEKLIQLNIFPQPINDRKYPNQCH", "text": "FUNCTION: Probably involved in the processes of spore formation and contributes to ascospore thermoresistance by participating in the morphogenesis of ascospore walls. The enzyme may do this by modifying glucan linkages in the developing ascospore wall, thus strengthening it or lending it plasticity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MNNNKRSKLSTVPSSRPIRVGFVGLTSGKSWVAKTHFLAIQQLSSQFQIVALYNPTLKSSLQTIEQLQLKHATGFDSLESFAQYKDIDMIVVSVKVPEHYEVVKNILEHSSQNLNLRYLYVEWALAASVQQAEELYSISQQRANLQTIICLQGRKSPYIVRAKELISEGCIGDINSIEISGNGGWYGYERPMRSPEYLYDIESGVNLISNSFGHTIDVLQYITGSYFQKINAMISNNIPTQFLLDENGKRTKETISKTCPDHLLFQGILENGKVPVSCSFKGGTPVKKLTKNLVIDIHGTKGDLKIEGDAGFVEISNLVLYFYGIKNGNGSSNGTDNNGAAAIKDKEKVTKSPSPSTGTSEEEQTMEVFHLRNYNSVVGNILRIYESIADYHFLGKPESKSSRGPDDLFASTKFDKQGFRFEGFPTFKDAIILHRLIDAVFRSDKEEKTLDVSKIMI", "text": "FUNCTION: This protein is a negative regulator for the gene expression of the lactose/galactose metabolic genes. It seems to block activation by the transcriptional activator LAC9 in the absence of an inducing sugar. SIMILARITY: To yeast GAL80."}
{"protein": "MADEQFPAAATALEEYQSIEEQMASPEVVSNPDKLRKLGRRHAELGAIVDAYKAWLQVKDDLAAAQEMAGEDADFAEEAKRLEDELPGVEEKLRTALIPRDPDDARDTIMEIKAGTGGEEAALFAGDLLRMYTRYAEKRGWSVNVQSENTTELGGVKDVQIAIRAKGTPAPEDGVWASMKYEGGVHRVQRIPVTESQGRIQTSAAGVIVFPEADEDDDEIEIDPKDLKIDIFMSSGPGGQSVNTTYSAVRMTHLPTGITVNMQDEKSQIQNRAAALRVLKSRLLAMKHEQEAAEAADMRHSQVRSLDRSERIRTYNFPENRIVDHRTNYKAYNLDAVLDGDLQAVIDSDIQADEADRLANQK", "text": "FUNCTION: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
{"protein": "MNQKLKVAIIGSGNIGTDLMIKVLRNAKYLEMGAMVGIDAASDGLARAQRMGVTTTYAGVEGLIKLPEFADIDFVFDATSASAHVQNEALLRQAKPGIRLIDLTPAAIGPYCVPVVNLEEHLGKLNVNMVTCGGQATIPMVAAVSRVAKVHYAEIVASISSKSAGPGTRANIDEFTETTSKAIEVIGGAAKGKAIIIMNPAEPPLIMRDTVYVLSAAADQAAVAASVAEMVQAVQAYVPGYRLKQQVQFDVIPESAPLNIPGLGRFSGLKTSVFLEVEGAAHYLPAYAGNLDIMTSAALATAERMAQSMLNA", "text": "FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Can also act on propanal and butanal to form propanoyl-CoA and butanoyl-CoA, respectively. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. NADP(+) can replace NAD(+) but the rate of reaction is much slower. SIMILARITY: Belongs to the acetaldehyde dehydrogenase family."}
{"protein": "MVTIVLNKYKLLNKIGIGQQKLEDLLFNLKSEIKPVDESNIEIEINADRLDLLSSDGIARAIKGLLEKELGEAKYDITDTEYKLIVDNVRTRPYALAAVIYNAKIDLQELIQFQEKLHSTIGRKRKKVAIGIHDLKKIDSKRIEYREVPLSYKFIPLYEKEELTISEVLEKTEQGKLYGNISISNGVSPAIVQEDGEVLSIPPIINSDKTKLDESTKDLFIDVTGTSFEAVAQTLDIIVSNLAEAGGTIGRVKVIKTDNSFQQSSPLLIHKIQNVREEYANKILGIKISEEEICKHITRMRMNCNVENGIIRVTVPQYRVDIINEIDIVEDIAMSIGYNNLEPSKYISTNYGSYDYLTLLERKMRELSIGAGFVEVFNFVLIKNEKILDSKYVKILNPISEEYNAVRNSLIPILLDFLSKNQHAKFPIRIFETGDVVIYDSSTDTGFRNDKRAAYAIMDNKVSYEDVQAPIHYILKTLGIEVNYKEENNDIFIEGRSASIVYENEKIGVIGEINPDVLIRFGIEYPTVIAELYITEIAKKLNKR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily."}
{"protein": "MADAGIRRVVPSDLYPLVLGFLRDNQLSEVANKFAKATGATQQDANASSLLDIYSFWLKSAKVPERKLQANGPVAKKAKKKASSSDSEDSSEEEEEVQGPPAKKAAVPAKRVGLPPGKAAAKASESSSSEESSDDDDEEDQKKQPVQKGVKPQAKAAKAPPKKAKSSDSDSDSSSEDEPPKNQKPKITPVTVKAQTKAPPKPARAAPKIANGKAASSSSSSSSSSSSDDSEEEKAAATPKKTVPKKQVVAKAPVKAATTPTRKSSSSEDSSSDEEEEQKKPMKNKPGPYSSVPPPSAPPPKKSLGTQPPKKAVEKQQPVESSEDSSDESDSSSEEEKKPPTKAVVSKATTKPPPAKKAAESSSDSSDSDSSEDDEAPSKPAGTTKNSSNKPAVTTKSPAVKPAAAPKQPVGGGQKLLTRKADSSSSEEESSSSEEEKTKKMVATTKPKATAKAALSLPAKQAPQGSRDSSSDSDSSSSEEEEEKTSKSAVKKKPQKVAGGAAPSKPASAKKGKAESSNSSSSDDSSEEEEEKLKGKGSPRPQAPKANGTSALTAQNGKAAKNSEEEEEEKKKAAVVVSKSGSLKKRKQNEAAKEAETPQAKKIKLQTPNTFPKRKKGEKRASSPFRRVREEEIEVDSRVADNSFDAKRGAAGDWGERANQVLKFTKGKSFRHEKTKKKRGSYRGGSISVQVNSIKFDSE", "text": "FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (PubMed:10567578, PubMed:26399832). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus (PubMed:9016786). It has intrinsic GTPase and ATPase activities (PubMed:9016786). SUBCELLULAR LOCATION: Nucleus, nucleolus Cytoplasm Note=Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase. SIMILARITY: Belongs to the NOLC1 family."}
{"protein": "MVNYPHKLSSQKRQPSLSQPKNFANRGMSFEKMINATNDYYLSQGLAVIHKKPTPIQIVRVDYPQRSRAKIVEAYFRQASTTDYSGVYNGYYIDFEAKETKQKRAIPMKNFHPHQIQHMEQILAQQGICFVLLHFSSQQETYLLPAYDLIRFYHQDKGQKSMPLGYIREYGYEIKAGAFPQIPYLNVIKEHLLGGKTR", "text": "FUNCTION: Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecU family."}
{"protein": "LKCHKLVPPFWKTCPEGKNLCYKMYMVSTLTVPVKRGCIDVCPKNSALVKYVCCNTNKCN", "text": "FUNCTION: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily."}
{"protein": "MATQVKKELVAELVEKIKKAQSVVFVDYQGIKVNEETLLRKQMRENGAEYLVAKNRLFKIALKESGVEDSFDEILEGSTAFAFGYNDPVAPAKAVFDLAKAKAKAKLDVFKIKGGYLTGKKVSVKEVEELAKLPSREQLLSMLLNSMLGPIRKLAYATVAIADKKEGSAE", "text": "FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. SIMILARITY: Belongs to the universal ribosomal protein uL10 family."}
{"protein": "MTNIRKTHPLLKIVNSSFVDLPAPSSLSSWWNFGSLLGVCLAVQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWVLRYLHANGASMFFICLYLHVGRGLYYGSYTYSETWNVGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFAFHFLLPFVVAALVMVDLLFLHETGSNNPTGIPSDSDMIPFHPYYTIKDILGFLVMLTALSTLVLFSPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILAIVPMLHVSKQRSMMFRPLSQCLFWLLVAVLFTLTWIGGQPVEHPYIIIGQMASVLYFLIILVLMPLTSIVENRLLSW", "text": "FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family."}
{"protein": "MARNTLSSRFRRVDIDEFDENKFVDEQEEAAAAAGEPGPDPSEVDGLLRQGDMLRAFHAALRNSPVNTKNQAVKERAQGVVLKVLTNFKSSEIEQAVQSLDRNGIDLLMKYIYKGFEKPTENSSAVLLQWHEKALAVGGLGSIIRVLTARKTV", "text": "FUNCTION: May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection. SIMILARITY: Belongs to the ARPC5 family."}
{"protein": "MDSFSLLAALFFISAATWFISSRRRRNLPPGPFPYPIVGNMLQLGAQPHETFAKLSKKYGPLMSVHLGSLYTVIVSSPEMAKEIMLKYGTVFSGRTVAQAVHACDHDKISMGFLPIGAEWRDMRKICKEQMFSHQSMEDSQGLRKQKLQQLLDHAHRCSEQGRAIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLALIEGYLNDRIQSRKANPDAPKKDDFLETLVDILNSNDNKLKTDHLLHLMLDLFVGGSETSTTEIEWIMEELVAHPDKMAKVKAELKSVMGDEKVVDESLMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGTQVLINAWAMGRDSTIWNNPDAFQPERFLDNKIDFKGQDYELIPFGSGRRVCPGMPLANRMLHTVTATLVHNFDWKLERPDAPLAEHQGVLFGFAVRRAVPLRIVPYKA", "text": "FUNCTION: Monooxygenase that oxidizes ferruginol to produce sugiol (PubMed:26682704). Oxidizes ferruginol at C-12 to produce 11- hydroxyferruginol (PubMed:26682704). Can oxidize 11-hydroxyferruginol to 11-hydroxysugiol (PubMed:26682704). These products are intermediates in tanshinone biosynthesis (PubMed:26682704). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MNTCIQLLILCLVTVINSENSTDHSTENTIENETEDVTKTELLKTIENETENVIETELPETVETEIQTEALNLPQSPEQRYCRSKGQYCSRTYFHRCCGNLVCQLHGFFNGTCVDCLAERKFCIWSSECCSGRCRLFRCRKNTHVKVIHY", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the UPF0506 family."}
{"protein": "MRYLHKIELELNRLTSRYPFFKKIAFDAEIIKLVDDLNVDENVKCAIVAIDTSMRMQDFINEDNKDSFVLSTDVLSALFYKYLSQPFYQHDFLVLTDCVSRINELKSIRATITDEIALHNINKQIHYMFIQPYMNNEKVVSYE", "text": "FUNCTION: Catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. Large subunit Hexs-B catalyzes the condensation reaction and the final product chain length is cooperatively regulated by both the Hexs-A and Hexs-B subunits using the whole size of the hydrophobic cleft as a ruler."}
{"protein": "MATYVVGDLHGCFDELQLLLKQVNYNPAQDELWLTGDLVARGAKSLECLRFVKDPKNNAKTILGNHDLHLLATLLGIKKVKPNDQVDAIFAAEDRADLQNWLRNQPLLIQHPKYGFLLTHAGISPEWNLTETIACAREAEAVLQSGHYADYIAQMYENTPDHWSAEWQGIERWRYIINVFTRMRFCYADKRLDFACKLPVEDAPNELKPWFKLDNPLFHQQDIIFGHWASLMGKADKPNIYALDTGCAWGNHLTMIRWEDKQIFTQERLK", "text": "FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. SIMILARITY: Belongs to the Ap4A hydrolase family."}
{"protein": "MMSFLHIVFSILVLVAFILGNFANGFIALTNFIAWVKRQKISSADQIIAALAVSRVGLLWVILLHWYSTVLNPTSSSLKVTIFVSNAWAVTNHFSIWLATSLSIFYLRKIVNFSRLIFHHLKRKAKSVVLVIVLGALFFLVCHLVMENTYINVWTKEYEGNVTWKIKLRNAMYLSNLTVATLANLIPFTLTLISVLLLIYSLCKHLKKMQLHGKGSQDPSTKIHIKALQTVTSFLILLAIYFLCLIISFWXSETQLKELVLMLCQAVGIIYPSFHSFILIWGNKTLRQTFLSVLWQVTCWSKGQNQSTP", "text": "FUNCTION: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor T2R family."}
{"protein": "MYKFRIQGSDKPLSGEVTISGAKNAALPILFAALLAEEPVEVANVPKLRDVDTTIELLQRLGAKVSRNGSVHIDASEVNNFCAPYDLVKTMRASIWALGPLVARFGKGQVSLPGGCAIGARPVDLHIHGLEQLGATIKLEDGYVKAEVDGRLKGAHIVMDKVSVGATITVMCAATLAEGTTILENAAREPEIVDTAHFLNAIGAKVSGMGTDTITIEGVERLGGGYHEVVADRIETGTFLVAAAVSGGKVVCKNTKASLLESVLAKLEEAGAKVESGEDWISLDMTGRELKAVNIRTAPHPAFPTDMQAQFTLLNMMAKGPGIITETIFENRFMHIPELQRMGAHAEIEGNTAICGDTDGLSGAQVMATDLRASASLVIAGCIAKGETIVDRIYHIDRGYDKIEDKLTALGANIERVRSSEL", "text": "FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily."}
{"protein": "MLCLCLYVPLIGEAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPVENIPEIILYWKHSTIFDVGENLTVPDEFTVEERQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMCIVGGFTQMIREGGARSLWRGNGINVLKIAPESAIKFMAYEQIKRLIGSDQETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSGMLDCARKILAREGMAAFYKGYVPNMLGIIPYAGIDLAVYETLKNAWLQRYAVNSADPGVFVLLACGTMSSTCGQLASYPLALVRTRMQAQASMEGAPEVTMSSLFKQILRTEGAFGLYRGLAPNFMKVIPAVSISYVVYENLKITLGVQSR", "text": "FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MVQLNQNFINSIAKDMPDHLSMDEFISYCAKPLRPSIRVNTLKITTADFITMMNAKGWQFEPVPWCEDGFWVKVDDSVQLGNTVEHIQGLFYIQEASSMLPPKALFPEPIEDATSLTLLDMASAPGSKTTQLAAMMNNQGLLVANEYSSSRVKVLHANVQRMGASNLALTHFDARVFGKYLFESFDAILLDAPCGGEGTVRKDPDALKHWDESEIEAIASVQRDLIESAFLALKPGGSLVYSTCTLNRRENQDVCLHLKATYGDAVQFESLAGLFPGAEKASTSEGFLHVWPQIFDSEGFFIAKLTKIAAVPRNSEEPRKQKNFPFTPIDKKSRQALCDYFDTSFGIKLDGQGILMQRDDEFWLFPTNVDPLIGKIRFQRIGLKLADALKKGFKPRHEAVMALADRLRGIPLDEAQAIQYLMGRDIALTSKEKPQGERLVSYQGAHLGLVKHLGNKLKNSLPRDLVRDKICSSSAMAVDQQATGED", "text": "FUNCTION: Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family."}
{"protein": "MTKKNLAVCSFCGRSEKDVEKLIAGPSVYICDYCIKLCSGILDKTPAPATQEIATSSTSSPTSLRVLTPKEIKRHIDSYVIGQERAKKTISVAVYNHYKRIRALMQDKQVSYGKSNVLLLGPTGSGKTLIAKTLAKILDVPFTIADATTLTEAGYVGEDVENIVLRLLQAADYDVARAERGIIYIDEIDKIGRTTANVSITRDVSGEGVQQALLKIIEGTVANIPPKGGRKHPNQEYIRVNTENILFIVGGAFVNLDKIIAKRLGRTTIGFSEETDLAVTNRDHLLAKVETEDLIAFGMIPEFIGRFNCVVNCEELTLDELVEILTEPANAIVKQYTELFEEENVKLIFEKEALYAIAQKAKQAKTGARALGMILENLLRDLMFEIPSDPTVEAIRIEEDTITQNKPPVIIQKSPEAIA", "text": "FUNCTION: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. SIMILARITY: Belongs to the ClpX chaperone family."}
{"protein": "MSRFRILSVGRGMPKHEKGLFDDYAGRMKRYGGLELVEIAEGQRTGKESPATRSKAIADEGERILEKMDKRLWMALDRGGKLLDSETLAAQLLRWQEAGDRDVGLIIGGPDGLHERVLQGVAFKLAFGPMTFPHMLVRVMLAEQLYRAMTLQHGVPYHR", "text": "FUNCTION: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase RlmH family."}
{"protein": "MNNKEIGKLGEDFTIDFLNKRGFIILERNYKVPLGEVDIIAQKGDLLIFIEVKTRRNLDFGIPAEAVDRTKQTRIKKIAELYISTKKPKFKKIRFDIMSIILSKSGKILDWEYLINAF", "text": "SIMILARITY: Belongs to the UPF0102 family."}
{"protein": "MMASLFSVFDPTSSFLSNWLSMLIPLLFMVMSFWLIPSRPQFLAKSVLMGLNREMSLLMGPASFGANILVIALFLFILFNNFIGLFPYIFTATSHLAVTLSLAVPLWISFILYTWIKETTNALAHLVPLGTPAPLMPFMVLMEIISNMIRPITLSVRLAANMIAGHLLLTLLGAQGTLENLYVTSIVVFSQIILLMLEFSVAIIQSYVFMTLMTLYASE", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family."}
{"protein": "MAPKPGAEWSTALSHLVLGVVSLHAAVSTAEASRGAAAGFLLQVLAATTTLAPGLSTHEDCLAGAWVATVIGLPLLAFDFHWVNGDRSSANLLLGGGMVLAVAGGHLGPEGRSVAGQAMLLVVAVTILIVAVFTANTYGMWGGAMLGVAGLLSRLEEDRLLLLPKEDVCRWALAVGSWAYCRALHTQRLQWE", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MESIIEDVRVRKILDSRGNPTVEVDVITWNGFGRAAAPSGASTGSREVAAFPSGGVDEIITEVEDIISSELIGMDAVDLQDIDLVLKEIDGTENLSSLGGNTVVAVSMATAKAAASSYNMPLYRFLGGNLATSIPYPLGNMINGGAHAGKNAPDIQEFLVVPVGAEDITEAVFANAAVHKRIRELIQKKDPSFAGGKGDEGGWVPSLSNGDALEIQATACEEVTDELGVEVRPSLDLAASEFWDPEIEKYVYRQENVQKDTGEQIEFVKEIIETYDMYYVEDPLHEGDLEGFAELTSLVGDRCMICGDDIFVTNREILREGIEMGAANAIIIKPNQIGTLTDTYLTVKLALENRYTPVVSHRSGETTDDTIAHLAVAFGAPLIKTGAIGGERIAKLNELIRIQEEIPYSRMADLPF", "text": "FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. SUBCELLULAR LOCATION: Cytoplasm Secreted Cell surface Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. SIMILARITY: Belongs to the enolase family."}
{"protein": "MIWHVQNENFILDSTRIFMKAFHLLLFHGSFIFPECILIFGLILLLMIDSTSDQKDRPWFYFISSTSLVMSITALLFRWKEEPIISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKRDVRSNEATTKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALISTTVGIGFKLSPAPFHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFARIVSFGLRTGTDNIRDYAGLYTKDPFLALSSALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVSIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIEWSMTVCVIASTIPGISMNPILAIAQDTLF", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."}
{"protein": "MAQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAHTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDSLNVQKAYDVSATDVISSTYSDGTQALTAPTATDIKAALGNPTVTGDTLTAAVSFKDGKYYATVSGYTDAGDTAKNGKYEVTVDSATGAVSFGATPTKSTVTGDTAVTKVQVNAPVAADAATKKALQDGGVSSADASAATLVKMSYTDKNGKTIEGGYALKAGDKYYAADYDEATGAIKAKTTSYTAADGTTKTAANQLGGVDGKTEVVTIDGKTYNASKAAGHDFKAQPELAEAAAKTTENPLQKIDAALAQVDALRSDLGAVQNRFNSAITNLGNTVNNLSEARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR", "text": "FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the bacterial flagellin family."}
{"protein": "MAAQGEPQVQFKVVLVGDGGTGKTTFMKRHLTGEFEKEYVATLGVEVHTLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPSWHKDLVRVCENIPIVLCGNKVDVKDMKVKAKPILFHRKKNLQYYDISARSNYNFEKPFFWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEEDDL", "text": "FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport (By similarity). Required for the import of protein into the nucleus and also for RNA export (By similarity). Involved in chromatin condensation and control of cell cycle (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. Ran family."}
{"protein": "MRPNNRAVNEPRPIKITRHYTKHAEGSVLVEFGDTKVICTATVEDSVPRFLKGQGQGWVTAEYGMLPRSTHSRMLREAAKGKQGGRTMEIQRLIARSLRAMVDLTALGERSITLDCDVIQADGGTRTASITGACVALTDAINALVENGTLKTSPLKGLVAAVSVGIVNGEAVCDLEYVEDSAAETDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLNLAKQGCNMIFDAQRRALAADC", "text": "FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. SIMILARITY: Belongs to the RNase PH family."}
{"protein": "MEYQYPLDYDWSNEEMVTMVKFYEAIEKAYEKGIIREELMGLYRRFKEIVPSKAEEKKIDKEFQEVSGYSIYRAIQRAKEIEEQKLVKM", "text": "SIMILARITY: Belongs to the UPF0223 family."}
{"protein": "MARDEVRRILPADIKREVLIKDEKAETNPKWGFPPEKRPMEMHMQFGIINLDKPPGPTSHEVVAWVKKLFNLNKAGHGGTLDPKVSGVLPVALERATRVVQALLPAGKEYVALMHLHGEVPEDKIYAVMKEFEGEIIQRPPLRSAVKRRLRTRKVYYIEILEIDGKDVLFRVGVEAGTYIRSLIHHIGLALGVGAHMAELRRTRSGPFKEDETLVTLHDLVDYYHFWKEDGIEEYFRKAIQPMEKAVEHLPKVWIRDSAVAAVTHGADLAVPGIVKVHKGIKKGDLVAVMTLKDELVALGKATMTSGEMLQKSKGIAVDVDKVFMPRDWYPKLW", "text": "FUNCTION: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 2 subfamily."}
{"protein": "MSLSDKDKAAVKGLWAKISPKADDIGAEALGRMLTVYPQTKTYFAHWADLSPGSGPVKKHGKVIMGAVGDAVSKIDDLVGGLAALSELHAFKLRVDPANFKILAHNVIVVIGMLYPGDFPPEVHMSVDKFFQNLALALSEKYR", "text": "FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
{"protein": "MVELTEFQKRRQENIKRNNDLLKKLHLGGAASRIKREAGVDDTHRTVVKKKKSPSVSRGRSASPKVAPVATRRSMRLRGEKVDNVGIPNVSDTQLMKMSLDGTSGSSVNDKELVDEIKDTPVIGDVKLSDLIKDEKEENLIEKFKSFANKNFSSGDFFEEIRKRQMENKAPELQKLQDDFDLQLYDVFQPNEIKLVYERITATYFHPSLDKKLIVAGDTSGNIGLWNVRDEPLSENGEDQMVEPDITKVKFFTKNVGKIDCFTSDTSKLLTASYDGSLRSIDLNSLQSNDILTLRNEYDDPLGISDFQFSYENPNVLLMTTLSGEFVNIDLREKIGEQISSNLRRLSDKKIGSFSINPNRPYEIATGSLDRTLKIWDIRKLVKKPEWSQYEDYDSCEIVSVYDSRLSVSAVSYSPTDNTLVCNGYDDTIRLFDVGSDNLPDDLQPKLTLKHNCQSGRWTSILKARFKQDQDVFAIANMKRAIDIYDSQGQQLAHLPTATVPAVISWHPLRNWIAGGNSSGKIFLFTDETVKKEEEE", "text": "FUNCTION: DNA-binding protein that binds to both single- and double- stranded DNA. Binds preferentially to UV-damaged DNA. May be involved in DNA-metabolic processes. SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family."}
{"protein": "MLNTLIVGASGYAGAELVSYVNRHPHMTITALTVSAQSNDAGKLISDLHPQLKGIVDLPLQPMSDVRDFSADVDVVFLATAHEVSHDLAPQFLQAGCVVFDLSGAFRVNDRAFYEKYYGFTHQYPELLEQAVYGLAEWNVDKLNTANLIAVPGCYPTAAQLSLKPLIDGGLLDLTQWPVINATSGVSGAGRKAAISNSFCEVSLQPYGVFTHRHQPEIAVHLGAEVIFTPHLGNFPRGILETITCRLKAGVTHAQVADVLQKAYGDKPLVRLYDKGVPALKNVVGLPFCDIGFAVQGEHLIVVATEDNLLKGAAAQAVQCANIRFGFAETQSLI", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1 subfamily."}
{"protein": "MFLINLLLLIVPVLLAVAFLTLIERKILGYMQFRKGPNIVGPHGLLQPIADAVKLFIKEPLRPLTSSIYMFILAPILALSLALTIWVPLPMPLPLIDLNLGLLFILSVSGLSVYSILWSGWASNSKYALTGALRAVAQTISYEVTLAIILLSIMLINGSFTLTTLNLTQEFMWLVVPTWPLMLMWFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFAMFFLAEYANIIIMNALTVILFFGTYHLIFLPELSTTNFMVKTMLLTSLFLWVRASYPRFRYDQLMHLLWKNFLPITLVTCLWYIMFPTMLSGTPPQM", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MTNFEKIIAQNKLKTNAVLATYCVIFAFIGLLVDVIRINANDLGTALFKLMTFQIFPTITIIMFLVAFVIIVVCIQNFSSIMLSGDEYKLIDKSKVLSSKENQIHRLLLELLEEAKLHFEPKLYIIKAPYMNAFASGWNESNSLIALTSALIERLDRDELKAVIAHELSHIRHNDIRLTMCVGILSNIMLLVANFSVYFFMGNRKNSGANLARMILLVLQIILPFLTLLLQMYLSRTREYMADSGAAFLMHDNKPMIRALQKISNDYANNDYKGVDQNSTRSAAYLFSAEMFSTHPSIKNRIQSLSRRVI", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family."}
{"protein": "MGVSKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVALWLGIGATLPIEKSLTLGLF", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family. PetD subfamily."}
{"protein": "MLIAQRPTLVEDPISEFRSRFVIEPLEPGFGYTLGNSLRRTLLSSIPGASVTSIRIDGVLHEFSTVPGVKEDVTDLILNLKELVVSSDNDEPTVMYLRKQGPGEVTAADIAPPAGVEVHSPELRLATLNDKGKLEIELTVERGRGYVSAAQNKQAGQEIGRIPIDSIYSPVLKVTYKVEATRVEQRTDFDRLIVDVETKPSISPRDAMASAGKTLVGLFGLAQELNAEAEGVDIGPSAADAALAADLALPIEEMDLTVRSYNCLKREGIHTIGELVSRSEADLLDIRNFGQKSIDEVKTKLGAMGLQLKDSPPGFDPRQAVDTYGTDSYNPAFSDPSDDGAEFVETEQY", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the RNA polymerase alpha chain family."}
{"protein": "MASTLITNIGELVTNDPEAADDGRGLLGIVEQAALVIDGSTVAWVGRAADAPDADQLVDAGGRAVLPGFVDSHSHLVFAGDRAAEFAARMAGTPYAAGGIRTTVAATRAATDEQLTSHVARLVEEMRRQGTTTVEIKSGYGLTVHDEARSLAVARQFTEETTFLGAHVVPDGDPGEYVDLVTGPMLDAAREHARWIDVFCERGAFDADQARAILDAGAAAGLRGRLHANQLTYGEGVRLAAELGLVAVDHCTYLADEDVAALRDSGTIATLLPGVEFSTRQPYPDARRLLDAGVRVALASDCNPGSCFTSSIPLCIALAVREMGMTPAEAVHAATYRGAQALDRDGQHGIGALVPGRRADLAVLDAPSHVHLAYRPGVPLVRQTWVAGRPL", "text": "FUNCTION: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. HutI family."}
{"protein": "MLLLGSFGGGAIRYRGGVLDALGLNFLAFGHAQGISNTVLWVGQLLLIGAWVHLGRRLFKKKVADDTADAADLGLVKRTLYAMVVPLIFAAPMMSRDVYSYLMQGAMLRDGFDPYTEGAAVNPGPMLLEVSHDWRNTTTPYGPLHLWIGDMITTVVGDNVTLGVVAYKILSIIGLAVTGWSIVRIAQHFGANPAIALWIGVANPVMIIHMIGGMHNESLMVGLVSVGLLLALKKRFVAGVALIAVAVSLKATAAIALPFVVWIGMHHFAGFLATKKGKDSPTLKQQVPAFFATGAAGVAVTGVVVSAITWASGASWGWISEISGNSKVINPLAFPSLVASVITMVAEVFVDDFDYNAVVNVVRSISMLIMLGGLVVCWWLFRQNERRAVTGTAAAYAVAFVFNSVTLPWYYASLISLLGTFKPPMWLIRFAAGASVFIALMFTGSGNHQLYNIVTVIIAAIIAWLATVVIFDDTDPATTATEKPSPHTVS", "text": "FUNCTION: Involved in the latter stages of the biosynthesis of the alpha-(1->6) mannan core of lipomannan (LM). Catalyzes the addition of alpha-(1->6)-mannose residue. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MptA/B family."}
{"protein": "MAEKESTSPHLIVPILLLVGWIVGCIIVIYIVFF", "text": "FUNCTION: Enhances the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by displacing ATP2A1/SERCA1 inhibitors, thereby acting as a key regulator of skeletal muscle activity (PubMed:26816378, PubMed:30299255). Does not directly stimulate SERCA pump activity (PubMed:26816378). Enhances sarcoplasmic reticulum Ca(2+) uptake and myocyte contractility by displacing the SERCA inhibitory peptides sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (PubMed:26816378, PubMed:30299255). SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Single-pass membrane protein."}
{"protein": "MSSVLNPSSPHSWDLCCSSSSNRSYHRPTHPIVGLLVGQLSVVLLIGAFIKFFIFGEAPPSPSRSQTHRTSQHKRSYSIHGARDLSPRTLKEKPSSNVLRPVPSSSTNTRSILRKTYYSANPTNFPSKHGRHRPHHSTHQPESLDWFNVLIAQTIAQYRQTAYILKDSPTASILESLATTLNNPEKKPSFIDEITVTDISLGEEFPIFSNCRVIAIDDPNSDGGRLQALMDVDLSDDNLSLAIETNLVLNYPKPYSAILPVALSVSVVRFSGTLCISFVPGTTESSTNLTPTSSNIDTNLRSNELRGKTAPQESSTTDEGSQGGATSTTGIPKTSLAFSFLPDYRLDLSVRSLIGSRSRLQDVPKVAQLVEARVHAWFEERVVEPRVQVVALPGIWPRMGRTGVRGQEEQPDVSSSDAAGVSGAKVSMLGSRDTGAEMLHAAREVDAEGLRYRRNPPPGDKGSSSKYAQQNQSSRERGRADDPFRIPGSLPDAVPIT", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta- barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MMM1 family."}
{"protein": "MADEEIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEAIFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "text": "FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
{"protein": "MSEKQNSRDHKRRLLAAKFELRRKLYKAFCKDPDLPSDMRDKHRYKLSKLPRNSSFARVRNRCISTGRPRSVSEFFRIYRIVFRGLASRGSLMGIKKSSW", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS14 family."}
{"protein": "MKRKLISPLFLIAALFSSTGQADSLKGYWHYDEFLAEFPEQRPISELFAQTVRDKPSALTVAQEQPVIISVVYPGQQISDYWVRNIKAFEKRMDALGIRYQINQVFTRPNLDTRQQSVSLMEALKNKSDYLIFTLDTTRHRKFIEHVLHSSETKLILQNITTPVKDWQGKQPMMYIGFDHEYGAQLLAQYYQAHAPKKPYSVLYFSEGYISEARGDTFIQDMNAVHHFPLASSYYTKATEQSGYEATLNIVKNNPEIGFIYACATDVALGAAQALKELNRQDILVNGWGGGSAELEALAKGELDVTVMRMNDDTGVAMAEAIKWDLEGKSVPLVYSGDFEVVTKQDSAARIAELKARAFRYSDR", "text": "FUNCTION: Binds to the signaling molecule autoinducer 2 (AI-2), a furanosyl borate diester, (3a-methyl-5,6-dihydrofuro- [2,3d][1,3,2]dioxaborole-2,2,6,6a-tetraol). This complex then interacts with the LuxQ sensor protein (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family."}
{"protein": "MGAPKQKWTSEEEDALRAGVRKHGAGKWRTIQKDPEFSPVLSSRSNIDLKDKWRNLSFSASGLGSSKLRVPKITGPSSSPSSSSQPLLLPAANKFTEATLPADAEKKPQDGKTLPKYGAMIMEALLELNEPNGSDIAAIFGFIEQRYAVQPTFRRFLASKLRRLADSNKIEKIDKSYRLPDSLATRTPAPMNASAPKQKDPSKPSKVSKAIGLFSASSPALEAAMAAAVKVADAEAKAHDAHDQTMEAERIFKMAEDTESLLIIAAEIYDRCSRGEITTLVPVAQREI", "text": "FUNCTION: Binds preferentially double-stranded telomeric repeats, but may also bind to the single telomeric strand. SUBCELLULAR LOCATION: Nucleus Chromosome Nucleus, nucleolus Chromosome, telomere Note=Localized to the nucleolus during interphase. SIMILARITY: Belongs to the histone H1/H5 family. SMH subfamily."}
{"protein": "MMVHAHPDDESIVTGATLAKYAAEGAGVTLVTCTLGEEGEVIPDDLAHLTSDREGTLGEHRIGELDKACLALGVRDHRFLGGPGRYRDSGMMGAPTNEHPRAFWGADVEEAATLLAQVIREVRPHVLVSYDEHGGYGHPDHIQAHRVARRAFLRAGERAMPGTPWQVRKLYAIAQPVSRIEESIARLREESGSFTPPARVSDIARGTPETAVTTRVDATDHWAAKALAMRAHATQITVEGERFALSNDIAQEIDAVEYFTLLVGPTPRIQHGEYETDLFAGL", "text": "FUNCTION: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2- deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway. SIMILARITY: Belongs to the MshB deacetylase family."}
{"protein": "MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKTSMPDEGERSCPVCRISYQHKNIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDRKVICWLCERSQEHRGHHTFLTEEVAQEYQVKLQAALQMLRQKQQEAEELEADIREEKASWKTQIQYDKTNILADFEQLRHILDWVESNELQNLEKEEKDVLKRLMRSEIEMVQQTQSVRELISDLEHRLQGSVMELLQGVDGVIKRMKNVTLKKPETFPKNRRRVFRAADLKVMLEVLRELRDVRRYWVDVTVAPNNISYAVISEDMRQVSSPEPQIIFEAQGTISQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDAMYNIEQNENYQPKYGYWVIGLEEGVKCNAFQDGSIHTPSAPFIVPLSVNICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCTVPMTLCSPSS", "text": "FUNCTION: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1- UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK- responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly localizes in cytoplasmic bodies. Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27. In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1. SIMILARITY: Belongs to the TRIM/RBCC family."}
{"protein": "MKLTPREQEKLLIVVAADLARRRKERGLKLNYPEAVALITYELLEGARDGRTVAELMQYGATILTRDDVMEGVADMIDEIQVEATFPDGTKLVTVHQPIRS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease gamma subunit family."}
{"protein": "MMENYKHTTVLLDEAVNGLNIRPDGIYIDGTFGRGGHSRLILSQLGEEGRLLAIDRDPQAIAVAKTIDDPRFSIIHGPFSALGEYVAERDLIGKIDGILLDLGVSSPQLDDAERGFSFMRDGPLDMRMDPTRGQSAAEWLQTAEEADIAWVLKTYGEERFAKRIARAIVERNREQPMTRTKELAEVVAVATPVKDKFKHPATRTFQAVRIWVNSELEEIEQALKSSLNVLAPGGRLSIISFHSLEDRIVKRFMRENSRGPQVPAGLPMTEEQLKKLGGRQLRALGKLMPGEEEVAENPRARSSVLRIAERTNA", "text": "FUNCTION: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family."}
{"protein": "MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAARFVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLGRRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMKIYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFALSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLILLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVLLMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERIKYD", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN- acyl-PI during GPI precursor assembly. FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN- acyl-PI during GPI precursor assembly (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGM family."}
{"protein": "MGDLKSGFEEVDGVRLGYLIIKGKQMFALSQVFTDLLKNIPRTTVHKRMDHLKVKKHHCDLEELRKLKAINSIAFHAAKCTLISREDVEALYTSCKTERVLKTKRRRVGRALATKAPPPERAAAASPRPGFWKDKHQLWRGLSGAARPLPISAQSQRPGAAAARPAAHLPQIFSKYPGSHYPEIVRSPCKPPLNYETAPLQGNYVAFPSDPAYFRSLLCSKHPAAAAAAAAAAAAAAAAAAAAAYYQVSAAGPQPKAAAGAGGPGSLSYRCKRKRGGAKDCLLAPHAGARRLLLLPRSYKAKAAAAAAAAAAAAAAAAGATCLERFHLVNGFCPPPHHHHHHHHHHHHHHHRAQPPQQSHHPPHHHRPQPHLGSFPESCSSDSESSSYSDHAANDSDFGSSLSSSSNSVSSEEEEEEGEEEEEEEEEEGGSGASDSSEVSSEEEDSSTESDSSSGSSQVSVQSIRFRRTSFCKPPSVQAQANFLYHLASAAAATKPAAFEDAGRLPDLKSSVKAESPAEWNLQSWAPKASPVYCPASLGSCFAEIRNDRVSEITFPHSEISNAVKRTDLTINCLAEGASSPSPKTNNAFPQQRILREARKCLQTTPTTHCADNNTIAARFLNNDSSGAEANSEKYSKILHCPEFATDLPSSQTDPEVNAAGAAATKAENPCTDTGDKTLPFLHNIKIKVEDSSANEEYEPHLFTNKLKCECNDTKGEFYSVTESKEEDALLTTAKEGFACPEKETPSLNPLAQSQGLSCTLGSPKPEDGEYKFGARVRKNYRTLVLGKRPVLQTPPVKPNLKSARSPRPTGKTETNEGTLDDFTVINRRKKVASNVASAVKRPFHFMANFPCPPSLIIGRDGDLWPAYSLNTTKDSQTPHKAHPIWKWQLGGSAIPLPPSHKFRKFNS", "text": "SIMILARITY: Belongs to the DACH/dachshund family."}
{"protein": "MTKILGSDPVKRGMAQMQKGGVIMDVVNAEQARIAEAAGAVAVMALERVPSDIRAAGGVARMANTTIVREVMEAVSIPVMAKARIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLLKSDYTVPFVCGCRDLGEALRRIGEGASMLRTKGEPGTGNVVEAVRHLRKVNAQLRKVINMSHDELMTEAKYLGAPFELLLQIKTLGKLPVVNFAAGGIATPADAALMMELGADGVFVGSGIFKSENPEKFAKAIVQATTHYQDYDLIARLSADLGEPMRGVEISELAVQDRMQERGW", "text": "FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. SIMILARITY: Belongs to the PdxS/SNZ family."}
{"protein": "MLRATKVCIYPTPEQAEHLNAQFGAVRFVYSKSLHIKKHAYQRHGVSLTPRKDIKPLLAVAKKFRKFRKFRKYAWLKEYDSIALQQAVINLDVAFSNCFNPKLKARFPMFKRKHGKLLG", "text": "FUNCTION: Expressed but non-essential protein, involved in the virulence of Salmonellas."}
{"protein": "MGYLFEETLSSNPKTPIVVDDDNELGLMAVRLANAAAFPMVLKASLELGVFDTLYAEASRTDSFLSPSEIASKLPTTPRNPGAPVLLDRMLRLLASYSMVKCEKVSVGKGERVYRAEPICRFFLKNNIQDIGSLASQVIVNFDSVFLNTWAQLKDVVLEGGDAFGRAHGGMKLFDYMGTDERFSKLFNQTGFTIAVVKKALEVYQGFKGVNVLVDVGGGVGNTLGVVTSKYPNIKGINFDLTCALAQAPSYPGVEHVAGDMFVDVPTGDAMILKRILHDWTDEDCVKILKNCWKSLPENGKVVVIELVTPDEAENGDINANIAFDMDMLMFTQCSGGKERSRAEFEALAAASCFTHCKFVCQAYHCWIIEFCK", "text": "FUNCTION: Involved in indole glucosinolate biosynthesis. Catalyzes methoxylation reactions of the glucosinolate indole ring. Converts the hydroxy intermediates 4-hydroxy-indol-3-yl-methylglucosinolate (4OH- I3M) and 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) to 4- methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3- yl-methylglucosinolate (1MO-I3M), respectively. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MAQVHYYGTGRRKNAIARVFLSPGSGTVQVNDKELGAYLGRKTLEMIVRQPLEVTGTAGRFNVRATVSGGGISGQAGAIKLGIARALVQADPNLRPVLKKAGFLTRDPRMKERKKYGLKKARRAPQFSKR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MASLDRVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYREGTPEEKAFYIELWDVGGSVGSASSVKSTRAVFYNSVNGIILVHDLTNKKSSQNLYRWSLEALSKDSSPTGIIVSNGDYDREQFAENAVPLLLIGTKFDQIPENKRNDVLTRTAFLSEDFNAEEINLDCTNPRYLAAGSSNAVKLSRFFDKVIEKRYFTRDPSQMQSFTDRRRFNFKSLHSD", "text": "FUNCTION: Required for KRAS signaling regulation and modulation of cell proliferation (PubMed:31406347). Regulator of KRAS prenylation, and probably prenylation of other small GTPases (By similarity). Required for lymphocyte development and function (By similarity). Not required for myeloid cell development (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MEKVQQTIRAPRGTELQTKGWVQEAALRMLMNNLDPEVAEKPEELVVYGGIGRAARNWESYQAIVDSLKTLESDETLLVQSGKPVAIFKSHEDAPRVLLANSNLVPKWANWDHFRELEKKGLMMYGQMTAGSWIYIGTQGILQGTYETFGEAARQHFGGSLKGTLTLTAGLGGMGGAQPLAVTMNGGVVIAIDVDKRSIDRRIEKRYCDMYTESLEEALAVANEYKEKKEPISIGLLGNAAEILPELVKRNITPDLVTDQTSAHDPLNGYIPVGYTLEEAAKLREEDPERYVQLSKESMTKHVEAMLAMQEKGAITFDYGNNIRQVAFDEGLKNAFDFPGFVPAFIRPLFCEGKGPFRWVALSGDPEDIYKTDEVILREFADNEHLCNWIRMARQQVEFQGLPSRICWLGYGERAKFGRIINEMVANGELSAPIVIGRDHLDCGSVASPNRETEAMKDGSDAVADWPILNALINSVNGASWVSVHHGGGVGMGYSLHAGMVIVADGTEAAAKRIERVLTSDPGMGVVRHVDAGYDLAVETAKEKGVNIPMMK", "text": "FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5- propionate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urocanase family."}
{"protein": "MLNFFAAAPRGYEYALSLELAELGASEIKESVAGVYFSAPLELGYRITLWSRLASRIIFVIYKGPCESPEQLYNAAYGIDWQMQFSNRSTFSIDFHGLGGFIKNTQFGALKIKDAIVDRFRDDDFSRPNVERVDADFRIDAHFRRGEITIGFNFSGPALHKRGYRSTTGEAPLKENLAANMLVRSGWQAAQVDLLDPFCGSGTILIEAAMMACDIAPGIHRERFGFDHWLPHNKKVWEELLNEARARASIGKTRCEIKFYGSDIDSRLVALAKRNAENAGVLELIDFNVCNALDVKAPAGSGYLISNPPYGERLGNVTSLLQLYYQLGDKFKADFGGWSIAILNSDVELLSALKLKADKQMKMNNGALECAFNLYTVHALNTRRVDPANIKIEGDVSDIAVPFANRIKKNFKQLEKWAKKEGIDSYRLYDADIPEYNVAIDKYLDYVVIQEYSAPSEIPEAVTKRRLTDVLISLPSAIGIDPNHIILKTRERKKGTNQYEKLAASKLELITTEYGAKFKLNLKEYLDTGLFLDHRLTRKLVGEKSKGRSVCNLFSYTGSASVHAALGGATSVTTVDMSNTYIDWAKENFALNGLNSDKYQFVQANCLQWMKRTHDRFDLIFIDPPTFSNSKRMEDSFDVQRDHLAMLTDVFKLLNPGGEIIFSNNKRKFKMEIAELEALGMSVKNIDNQTLPLDYKRNPHIHNTWLITHAG", "text": "FUNCTION: Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RlmKL family."}
{"protein": "MSLLTEVETPTRNGWECKCSGSSDPLVIAASIIGILHLILWILDRLFFKFIYRRLKYGLKGGPSTEGVPESMREEYRQEQQNAVDVDDGHFVNIELE", "text": "FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. SUBCELLULAR LOCATION: Virion membrane Host apical cell membrane; Single-pass type III membrane protein Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). SIMILARITY: Belongs to the influenza viruses matrix protein M2 family."}
{"protein": "MADEFFHAGKENCSEQARRSQVSGPRSQFQRSFIQRVTLLGKLPTRFVLHRERKQKVAAILGVDQEAMKSLPEGDLDHCLLSKVDLRRQQISQTMEEVQKIIHLLTTEISRQDSRFEAVPVSDTHNESIKVLAPSLFHVTVPLKGLAGYKGVQRQRWRYYNVQGAKLTCPLRDPEGLQQWLETEMFMKTLWQWHKADVNIEGDIVPAKVLQVFRTLVENAVRTCHLSGKVTVLEKRTTVWVAMETSTGQVELELAPTVEIPTTWPEKAQWPRCLKRWPSPERVECIKSFGFNLVAQSAYHWQLSFSQAEQVLFEQLDEDGGCRRQCFQVLRQLKEDVWCPGRRPVITTHHLQTVLFWTCEKYPHLKDWQVFHQALLRLVRKLHRCVSQHFLKHYFVPKSNLLQSANPSELDAVAQKVAFFLKNPQVELP", "text": "SIMILARITY: Belongs to the mab-21 family."}
{"protein": "MARRSKGRQIDGIVLLDKDTGMSSNYALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGVRTDTSDSDGEVVQTRDINFTQAQLETALEHFRGDTMQVPSMFSALKHQGQPLYKYAREGIEVPREARPITVFELNFIKLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTQVADYPYDKMVSLADLEALVTQAQQQELAVGELLDPLLLPMDTAVANFPEINLPESMLYYVMQGQAVQASGLKIDVLVRITIGEQRKFVGIGIMNDDGLLAPKRLIVIPAEESPE", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1 subfamily."}
{"protein": "MVKVLAVLYDGGKHGEEVPELLGTIQNELGLRKWLEDQGHTLVTTCDKDGENSTFDKELEDAEIIITTPFHPGYLTAERLARAKKLKLAVTAGIGSDHVDLNAANKTNGGITVAEVTGSNVVSVAEHVLMTILVLVRNFVPAHEQIQEGRWDVAEAAKNEFDLEGKVVGTVGVGRIGERVLRRLKPFDCKELLYYDYQPLSAEKEAEIGCRRVADLEEMLAQCDVVTINCPLHEKTQGLFNKELISKMKKGSWLVNTARGAIVVKEDVAEALKSGHLRGYGGDVWFPQPAPQDHPLRYAKNPFGGGNAMVPHMSGTSLDAQKRYAAGTKAIIESYLSGKHDYRPEDLIVYGGDYATKSYGERERAKAAAAAAKSA", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily."}
{"protein": "MIRVLVIDDSLFIRTVVQDMLSDDPDIQIVGVASDGLEALDKIRELKPDLITLDIEMPRLDGLSMLERKKEIDRFPKTLVLSSLTSEGAEMTKRAIALGADDFMLKPRGIKNIREIGGELKHKIKNICTIAYITAKPVLKDSNARNVVLIGSSAGGPPMLDTIVSKLPSDLNAAVIITQHMPKGGFTAALAARLNRISPLQIRETENGDVLKNGTVLVSRAGFHTIISSVLDKGGSQSGKIILTDSPPVHNVKPAVDKTFISAAQVFGNHCVTAILSGMGNDGGEGTEAIKKAGGVTIVCREEDCLVYGMARSALSRNCVDHVLSLQAIPEKIVETIRAMNG", "text": "FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CheB family."}
{"protein": "MKFFAVFALCVASVSAANLDAIAKPGFPAGRIINGHEADKGEAPFIVSLKAGKGHFCGGSIIAENWVLTAGHCLIFDEFEIVAGLHSRNDESDVQIRKVTGKHQQIVHEKYGGGVGPNDIGLIYVDKPFNLNALTRDGTAAVAKVNLPTGKYESTGKGKLYGWGLDNSGFSPNILNTLDVDIIGYEECKNALNSDDPLDPVNICSYTAGAIDGACNGDSGGPMVRITPDGTELVGIVSWGYQPCASTTMPSVYTWTSAFDKWIEDSIKNYAQLL", "text": "FUNCTION: Protein with lectin and protease activity involved in the establishment of trypanosome infections in tsetse flies. Binds D- glucosamine and agglutinates bloodstream-form trypanosomes and rabbit red blood cells. Capable of inducing transformation of bloodstream-form trypanosomes into procyclic (midgut) forms in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MARVENMTERYAVFGNPIGHSKSPKIHTMFAKETGQSLSYEAILAPIDAFEASFKEFAANEGYGANVTVPFKEQAFSLCDELSEQAQLAGAVNTLSVLADGKIRGDNTDGLGLVADLKRNLGDLCGLQVLLIGAGGAARGSVLPLLHSGIAKLTIVNRTQAKAEALVEIFTSYGDVTSLPITHVGQSYDVIINSTSSSLSGEVPNISPDTIAPHTVCYDMMYGKQSTAFNLWAKSLGAGQTIDGLGMLVGQAAASFSIWRKVTPSVEPVLAQLRSELIG", "text": "FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). SIMILARITY: Belongs to the shikimate dehydrogenase family."}
{"protein": "MGLEDEQKMLTESGDPEEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSHTEEDCTEELFDFLHARDHCVAHKLFNNLK", "text": "FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the UQCRH/QCR6 family."}
{"protein": "MTTPAYLLANFGGPRHAKDLQEFLISLLTDRDVTGTFLPRVLHRHLFTFIAKKRVPKVLPQYQSLQNWSPIYFDTETLAKTLSEILRAPVIPFHRYLPSTHEKTLLALRTLHTRHVIGIPLFPHFTYSVTGSIVRFFMKHVPEIPISWIPQFGSDSKFVSLITCHIRDFLQKLGILEKECCFLFSVHGLPVRYISQGDPYSKQCYESFSAITTNFKQSENFLCFQSKFGPGKWLSPSTAQLCQNIDTDKPNVIVVPFGFISDHLETLYEIERDYLPLLRSRGYRALRIPAIYSSPLWVSTLVDIVKENSTVVAEELIKSGKKHTGIR", "text": "FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferrochelatase family."}
{"protein": "MDESKRKALENALKAIEKEFGKGAVMRLGEMPKQQVDVIPTGSLALDLALGIGGIPRGRIVEIYGPESGGKTTLALTIIAQAQRRGGVAAFVDAEHALDPLYAQRLGVQVEDLLVSQPDTGEQALEIVELLARSGAVDVIVVDSVAALVPRAEIEGEMGDQHVGLQARLMSQALRKLTAVLAKSNTAAIFINQVREKVGVTYGNPETTPGGRALKFYASVRLDVRKSGQPIKVGNEAVGVKVRVKVVKNKLAPPFREAELEIYFGRGLDPVADLVNVAVAAGVIEKAGSWFSYGELRLGQGKEKAAEALRERPELLEEIRAKVLERSDQVVLAAGEDEGE", "text": "FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecA family."}
{"protein": "MAIVKVTDSDFDSKIESGVKLVDFWATWCGPCKMIAPVLEELAGDYDGKADILKLDVDENPSTAAKYEVMSIPTLIVFKDGEPVDKVVGFQPKENLAEVLDKHL", "text": "FUNCTION: Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). SIMILARITY: Belongs to the thioredoxin family."}
{"protein": "MNGTEGPNFYVPMSNKTGVVRSPFDYPQYYLAEPWQYSALAAYMFLLILLGLPINFMTLFVTIQHKKLRTPLNYILLNLVFANHFMVLCGFTVTMYTSMHGYFIFGPTGCYIEGFFATLGGEVALWSLVVLAVERYIVVCKPMANFRFGENHAIMGVAFTWIMALSCAAPPLFGWSRYIPEGMQCSCGVDYYTLKPEVNNESFVIYMFIVHFTIPLIVIFFCYGRLLCTVKEAAAQQQESLTTQKAEKEVTRMVVIMVVFFLICWVPYAYVAFYIFTHQGSNFGPVFMTVPAFFAKSSAIYNPVIYIVLNKQFRNCLITTLCCGKNPFGDEDGSSAATSKTEASSVSSSQVSPA", "text": "FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G- proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cell projection, cilium, photoreceptor outer segment Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MAVRGINKVILVGRLGKDPEVRYIPNGGAVANLQVATSESWRDKQTGEIREQTEWHRVVLFGKLAEVAGEYLRKGAQVYIEGQLRTRSWEDNGITRYVTEILVKTTGTMQMLGRAAGTQTQPEEAQQFSGQPQPESQPEPKKGGAKTKGRERKAAQPEPRQPSEPAYDFDDDIPF", "text": "FUNCTION: May contribute to the conjugative processing of DNA. It has a functional relationship with Psi (plasmid-mediated sos inhibition) proteins."}
{"protein": "MSRSLNLAVIPGDGIGQEVVAEGLKVLSAVLPQDVKLETKEFDFGARRYHATGETLTDADLDALKAHDAILLGAIGDPSVPSGVLERGFLLKLRFAFDHHVNLRPSKLLPGVATPLAGQPEIDFVVVREGTEGPYTGNGGTIRKGTEHEVATEVSVNTAYGVERVVRDAFARAQARPRKKLTLVHKNNVLTFAGHLWTNIFNKVAAEYPEVTTDYLHVDAATIFLVTDPARFDVIVTDNLFGDIITDLAAAVSGGIGVAASGNINPSGDFPSMFEPVHGSAPDIAGQGKADPTATVLSVALLLRHLGYEDEAARIEDAVSADLGERGDLPARSTSEIGDTLAARVAG", "text": "FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily."}
{"protein": "MMKPSNISISAVKLPQDLDDFKMLVQEYLQEFGMDLTFQNVDDELANPMRKYGPPHGIMLVARDEHGTALGCVAVHPFGGPGCCEMKRLYVRPESRGLKLGVLLVKEIIQYSEKLGYSSMVLDTLDTLLPAVRLYKSFGFKTTEPYYHNPIPNVVYMRLEMSK", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the acetyltransferase family."}
{"protein": "MDARQMKIKAAEAALEHVESGMRLGIGTGSTAEEFVRLLAEKVASGFQISGVPTSERTARLCLELGVPLKSLDELPELDLTIDGADEVDGKLRLIKGGGGALLREKIVASASTRMIVIADESKVVDVLGAFKLPIEINPFGQVATRLAIEKTASRLGLAGEIVVRSSGDGVFMTDGGHLILDASFGRIPDADALAVELNAIPGVVEHGLFIDVASMAIIAGPEGARTLTAS", "text": "FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. SIMILARITY: Belongs to the ribose 5-phosphate isomerase family."}
{"protein": "MLQNEVENFANLLEQATVYLAPYQEKIIVVKYGGNAMINEDRKKLVMQDILLLNQLGVKVVLVHGGGPEISQGVKLLGKEPQFINGLRVTDQDTINVVLQMLAGKVNKSLVALLKGKGVGLCGIDANMLQCEKLQAEVDYGFVGEIVKVNTQLLELALSANLIPVISTVGVDDQGVAYNINADTVASEIAMALGAAKLVSMTDIAGLLRDRFDESTLIPEVEVSEVQGLIDQGIIAGGMIPKIACCTDFINAGGIEANIIDGRVPHAILVSLFGGKNGTLFYKK", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB subfamily."}
{"protein": "MIQSTEFFWWKFELVFPPDVEESFLWFLNMAGIKSYAIERSPDNLQDQTLMVWLPSHEWLKKDREEFENSLLALNKAFREDVLNTKWEKIIDEDWSSSWKKFWKADPVGSKILILPSWLELPDIYSNRIVIKLDPGSAFGTGSHPTTRLCLEDLERNPPLGKKVVDIGCGSGVLGIAAIKLGAKEVRAIDIDSLAVRATSENIVLNNLSQKQLSVSLGSIENLANQLNPLSADLLICNTLSPVIKELAPYFFKLTHSYSRLCLSGLLVAQVEDITNFLSILGWELIDSYSSDNWALIRLCRNHP", "text": "FUNCTION: Methylates ribosomal protein L11. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family."}
{"protein": "MPAGRAVSGRLENDMTTHAMTDAARAGAVTRRGVPRHLADFSLAERRRWVAELGEPSFRAVQISAHYFGRLTENPDEMTDLPASSRRELVGVLLPPLLRPVRELACDNGLTRKILWRLSDGAYVESVLMRYPPRHSRHAALGAEADADGGSRHGRVTLCVSSQAGCGMGCPFCATGQAGLVRNLSAAEIVAQVAVAARTVARGEMAGGPGRLSNVVFMGMGEPLANYRSVVDAVRRITEPPPEGLGISQRSVTVSTVGLVPAIERLATEGLAVTLAVSLHAPDDELRNVLVPINRRWPVRDVLGAAARYAEVTKRRVSVEYALIRDVNDQPWRADALAAQVKEFLGRLGHVNLIPLNPTPGSPWTASTPRAQAEFVRRLAAAGVTVTVRDTRGREVNGACGQLAATVEFRGRTVQETPAPSMAALDDAVR", "text": "FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family."}
{"protein": "MATIYACRGFHRVPVKLSPSSTLQEVILSSYKQLGFSDWHNLELLHGDKKVDTSLLLRLSGIINGAKLIVKESATNQSGKSSSSISPQSKKIKVALQLPGAARIIDEASSETSIKQLLERHSLLTKVSHVLINGRNFKSEEFDNPLLLYGIREGSILIRLFPIKAQQSIVSEQAPVSQTFNGDVKEKKNADLMDIESENKKDDIVESFPKYPVDAHKLLEPLPTPIPSLPSTPSSYQNLPSQSLTGESLPTVSNQEKDEGVIEKVAVNNTPSVSSKSPFPKKKSFSSMLAQVKKEKAENNGSDGYDLQPTKSQLELYQSILRKRANQVSSTSLTKSSSPKPLPSSAIVKFDFGNGKSIVHEFSKDDNIETLRAFVASHLSPEESTSFQLTFSNYEALPTTGLIVEHIGRAVVRVHTISDPVYAQR", "text": "FUNCTION: Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. SUBCELLULAR LOCATION: Cytoplasm. Nucleus."}
{"protein": "MSRYRGPRLRVVRRLGELPGLSRKTPRRAYPPGQHGQARKKRSEYAAQLEEKQKLRFNYGLSERQLLRYVRKARRAGGSTGQTLLQLLEMRLDNTIFRLGMAPTIPAARQLVNHGHVLVNGRVVSIASYQCRPGDVIQSRDRDASRKLIETHMQFPGLANIPTHLDFDKNTLTGKVNGVIEREWIALEINELLVVEYYSRKG", "text": "FUNCTION: With S5 and S12 plays an important role in translational accuracy. FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
{"protein": "MDTLLRTHNRLELLYPLHELAKRHFLSPSPNPQNPNFKFFSRKPYQKKCRNGYIGVSSNQLLDLVPEIKKEHLEFDLPLYDPSKALTLDLAVVGGGPLARSCSTSLGGGLSVVSIDPNPKLIWPNNYGVWVDEFEDMDLLDCLDATWSGAIVYVDDRSTKNLSRPYARVNRKNLKSKMMKKCVSNGVRFHQATVVKAMHEEEKSYLICSDGVTIDARVVLDATGFSRCLVQYDKPYNPGYQVAYGILAEVEEHPFDVDKMVFMDWRDSHLNGKAELNERNAKIPTFLYAMPFSSNRIFLEETSLVARPGLKMEDIQERMVARLNHLGIRIKSIEEDERCVIPMGGPLPVIPQRVVGIGGTAGMVHPSTGYMVARTLAAAPIVANSIVQYLVSDSGLSGNDLSADVWKDLWPIERRRQREFFCFGMDILLKLDLEGTRRFFDAFFDLEPRYWHGFLSSRLFLPELVPFGLSLFSHASNTCKLEIMAKGTLPLVNMINNLVQDRD", "text": "FUNCTION: Catalyzes the double cyclization reaction which converts lycopene to beta-carotene and neurosporene to beta-zeacarotene. SUBCELLULAR LOCATION: Plastid, chloroplast Plastid, chromoplast Plastid, chromoplast membrane Plastid, chloroplast membrane Note=Exists as an inactive soluble form and an active membrane-bound form. SIMILARITY: Belongs to the lycopene cyclase family."}
{"protein": "MVMFSQDHVQIVYGSTRICKSLAPANKRKTHRTIVVAPRRGFLRIPPDGQDVNHVKIVPTTSSSLAPPRDDERRPTPPLRPPLTVYPYGTSLIRRSARDAKLRSKLIVFHITRPALGQHPQNPGISGPAAMDHSEFLTSFRREVDRQTVLTAESAPATAEVCLGDALPGGVMGGGGLPAGVGSASAAVAAAAAAVAGVPVAANPVMPATATVTTPPMIDLTSHHRPLTLFTPASAAAAPAVATNGGNATYILPADCRYAPLFASKYKYVFEEVSRLMRLHDSTAVQLQISASCGNAFQALKSALLKLHNVTVLAGQQLITQTMPHTPQAVATFKFFHQDPNRVLDCIRPVVPRSTSYHETGVYQMWVSGATKKDLFDAVTLCASIVEKQPDVFNINVSLLTYPSIAAPHLPLYNEFTSFRLPTS", "text": "FUNCTION: Plays a role in the inhibition of host DNA replication in the infected cell. Targets the mini-chromosome maintenance (MCM) complex and blocks the accumulation of MCM proteins and their loading onto host chromatin. SUBCELLULAR LOCATION: [Isoform UL117.5]: Host nucleus. SUBCELLULAR LOCATION: [Isoform UL117]: Host nucleus Note=The major fraction localizes to nuclear compartments. SIMILARITY: Belongs to the herpesviridae U84 family."}
{"protein": "MSTKEKLISHVMKEEPVGSRNKVTVVGVGMVGMASAISILLKDLCDELAMVDVMEDKLKGEVMDLQHGSLFLKTHKIVGDKDYSVTANSKLVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPNCILMVVSNPVDILTYVAWKLSGFPRHRVLGSGTNLDSARFRHLIGEKLNLHPSSCHAWIIGEHGDSSVPVWSGLNVAGVSLQGLNPQMGTEGDSENWKAIHKEVVDGAYEVIKLKGYTSWAIGMSVADLVESILKNLHKVHPVSTLVQGMHGVKDEVFLSVPCVLGNSGLTDVVHMTLKAEEEKQVQNSAETLWGVQKELTL", "text": "FUNCTION: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family."}
{"protein": "MILFPAIDLKNGQCVRLEQGDMDRATVFNLDPAAQAKSFAAQGFEYLHVVDLDGAFAGKPMNAQAVESMLQVVKMPVQLGGGIRDLATIEAWLGKGVSRVIIGTAAVRDPALVKDAAKKFPGRVAVGLDARDGKVAVQGWAESSEVTALEIAQRFEDAGVAAIIFTDIARDGLLKGLNLDATIELAATISTPVIASGGFGSIDDVKALILPRAAKLAGAIVGRALYDGRLDPTEALALMRRAAAA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MSQDVLADKPLLSRSMVAVLCAQFFSAFGDNALLFATLALIKQQLYPDWSQPILQMAFVATYIVLAPFVGQIADGFAKGRVMMVANGLKLAGALVICFGLNPFLGYSLVGVGAAAYSPAKYGILGEITSGEQLVKANGMMEASTIAAILLGSVAGGILADWHLMAALGVCALVYAIAVIANLFIPRLAAARSGASWRPRAMTGSFFTACRLLWQDSETRFSLAGTSLFWGAGVTLRFLLVLWVPVALGIADNATPTLLNAMVAIGIVVGAGAAARFVTLKTVKRCLPAGVLIGVMVTIFSLQNSMPMAYLLLIIIGILGGFFVVPLNALLQERGKHSVGAGNAIAVQNLGENTAMLFMLGLYSLVVKLGAPVVAVGVGFGVVFALAIALLWGWQWRQQRQKTRQPE", "text": "FUNCTION: Catalyzes the facilitated diffusion of 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) into the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. LplT (TC 2.A.1.42) family."}
{"protein": "MKYDHLLVRYGELTLKGSNRKKFVNQLRNNVNKSLKGLDGFVVKGKRDRMYIELEDHADINEITNRLSKIFGIKSISPVLKVEKSIEAMSAETIKFAQQFEENSTFKIDVKRADKNFPMDTYELQRELGGTVLKQIENVSVNVKRPDHEIRVEVRLDAIYMYEEVVPGSGGLPVGTGGKTLLMLSGGIDSPVAGMEVMRRGVTIEAIHFHSPPFTSDQAKEKVIELTRILAERVGPIKLHIVPFTELQKQVNKVVHPRYTMTSTRRMMMRVADKLVHQIGAYAIVNGENLGQVASQTLHSMYAINNVTSTPVLRPLLTYDKEEIIIKSKEIGTFETSIQPFEDCCTIFTPKNPVTEPNFDKVVQYESVFDFEEMINRAVENIETLEITSDYKTIKEQQTNQLINDFL", "text": "FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ThiI family."}
{"protein": "MNTLPEQYANTALPTLHGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVISRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLGKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG", "text": "FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. SIMILARITY: Belongs to the GlnD family."}
{"protein": "MTKVTLKGNPVQLEGKIPSPGDKAPDFKAIKQDLSEFSLKDYAGKVKILVAVPSLDTSVCALETKAFNEKAAGISGVTTLVISGDLPFAMGRFCSTEGINSPNLVTGSQYRDFSFSKAYGTHIADGPLKGLSARAVFVLDKSDTVRYVEIVPEITTEPNYTAAIAAANAAL", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. SIMILARITY: Belongs to the peroxiredoxin family. Tpx subfamily."}
{"protein": "MGRARRFQWPLLLLWAAAAGPGTGQEVQTENVTVAEGGVAEITCRLHQYDGSIVVIQNPARQTLFFNGTRALKDERFQLEEFSPRRVRIRLSDARLEDEGGYFCQLYTEDTHHQIATLTVLVAPENPVVEVREQAVEGGEVELSCLVPRSRPAAVLRWYRDRKELKGVSSGQENGKVWSVASTVRFRVDRKDDGGIVICEAQNQALPSGHSKQTQYVLDVQYSPTARIHASQAVVREGDTLVLTCAVTGNPRPNQIRWNRGNESLPERAEAVGETLTLPGLVSADNGTYTCEAANKHGHARALYVLVVYDPGAVVEAQTSVPYAIVGGILALLVFLIICVLVGMVWCSVRQKGSYLTHEASGLDEQGEAREAFLNGGDGHKRKEEFFI", "text": "FUNCTION: Involved in the cell-cell adhesion. Has calcium- and magnesium-independent cell-cell adhesion activity. May have tumor- suppressor activity. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the nectin family."}
{"protein": "SPPVCGNELLEEGEECDCGSPANCQDRCCNAATCKLTPGSQCSYGECCDQCKFKKARTVCRIARGDWNDDYCTGKSSDCPWNH", "text": "FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits aggregation induced by ADP, thrombin, platelet-activating factor and collagen (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily."}
{"protein": "MSSSDARSRIRDRGYSEVPRDTSCPDGTIRTFQSLHSSELAVSADPLPPPPLPLQPPFGPSFYSSDTEEPAVAPDLKPVRRFVPDSWKNFFRGKKKDPEWDNPVSDIRYISDGVECSPPASPARANHHPYKDPSRGSQGTFNSQHEADAMFAHDPYASLDRRTQTARTYSEKVEEYNLRYAYMKSWAGLLRILGVVELLLGAGVFACVTAYIHKDNEWYNLFGYTQPYGMGGLGSLGNTYGGYYYSGPKTPFVLVVAGLAWITTIIILVLGMSMYYRTILLDSNWWPLTEFGVNVALFILYMAAAIVYVNDTNRGGLCYYPLFNTPMNAMFCRVEGGQIAAMIFLFVTMIVYLVSALVCLKLWRHEAARRHREFLEQQEINDPSLSSKRKMCEAAISDRQRDQEVNVKDLRTTTKMTPELLSGHIPPGHIPKPIVMPDYVAKYPVIQTDDDRERYKAVFQDQFSEYKELSAEVQAILRKFDELDTVMSRLPHHSENRQEHERISRIHEEFRKKKNDPSFLEKKERCDYLKNKLSHIKQRIQEYDKVMNWDTQGYP", "text": "FUNCTION: Plays a role in the formation of tricellular tight junctions and of epithelial barriers (PubMed:16365161, PubMed:21245199). Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti (PubMed:26677943). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell junction, tight junction Note=Found at tricellular contacts. SIMILARITY: Belongs to the ELL/occludin family."}
{"protein": "MDTTMEADLGATGHRPRTELDDEDSYPQGGWDTVFLVALLLLGLPANGLMAWLAGSQARHGAGTRLALLLLSLALSDFLFLAAAAFQILEIRHGGHWPLGTAACRFYYFLWGVSYSSGLFLLAALSLDRCLLALCPHWYPGHRPVRLPLWVCAGVWVLATLFSVPWLVFPEAAVWWYDLVICLDFWDSEELSLRMLEVLGGFLPFLLLLVCHVLTQATACRTCHRQQQPAACRGFARVARTILSAYVVLRLPYQLAQLLYLAFLWDVYSGYLLWEALVYSDYLILLNSCLSPFLCLMASADLRTLLRSVLSSFAAALCEERPGSFTPTEPQTQLDSEGPTLPEPMAEAQSQMDPVAQPQVNPTLQPRSDPTAQPQLNPTAQPQSDPTAQPQLNLMAQPQSDSVAQPQADTNVQTPAPAASSVPSPCDEASPTPSSHPTPGALEDPATPPASEGESPSSTPPEAAPGAGPT", "text": "FUNCTION: Orphan receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MKVFILALLALAATTAIAQLETTCSQGFGQSQQQQQPGQRQLLEQMKPCVAFLQQKCGPLRMPFLQTQVEQLSSCQIVQYQCCQQLAQIPERTRCHAIHIVVEAIIQQQSQQQWQEPQQQAQHKSMRMLLENLSLMCNIYVPVQCQQQQQLGQQQQQQLQEQLTPCTTFLQQQCSPVTVPFPQIPVDQPTSCQNVQHQCCRQLSQIPEQFRCQAIHNVAEAIRQQQPQQQWQGMYQPQQPAQLESIRMSLQALRSMCSIYIPVQCPAPTTYNIPLVATYTGGAC", "text": "FUNCTION: Seed storage protein. Might be integrated via inter-chain disulfide bonds within the glutenin polymer (By similarity). SIMILARITY: Belongs to the prolamin family."}
{"protein": "MSDVRVIIQRDSEREERVVTTGTTAAELFAGERSIIAARVSGDLKDLAYEVKDGETVEAVEISSEDGLDILRHSTAHVMAQAVQELFPEAKLGIGPPVKDGFYYDFDVEKPFHPDDLKAIEKKMQEIQKRGQRFSRRVVTDEAAREELADEPYKLELIGLKGSASSDDGADVEVGAGELTIYDNLDAKTGELCWKDLCRGPHLPTTRNIPAFKLMRNAAAYWRGSEKNPMLQRIYGTAWPTKDELKAHLEFLAEAEKRDHRKLGSELDLFSIPEQIGSGLAVFHPKGGIIRRVMEDYSRRRHEEEGYEFVYTPHATKGKLFETSGHLDWYADGMYPPMQLDEGVDYYLKPMNCPMHNLIFDARGRSYRELPLRLFEFGTVYRYEKSGVVHGLTRARGFTQDDAHIYCTREQMSEELDKTLTFVLNLLRDYGLNDFYLELSTKDPEKFVGSDEAWEEATETLRQVAEKQNLELVADPGGAAFYGPKISVQARDAIGRTWQMSTIQLDFNLPERFSLEYTAADGAKTRPVMIHRALFGSIERFFAVLLEHYAGAMPPWLAPVQAVGIPVGDAHVQYLEEFAAEARRKGLRVDVDASSDRMQKKIRTQQKQKVPFMIIVGDEDMHGGTVSFRYRDGSQENGIPRDQALAKLVDVVERRIQV", "text": "FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MRLLFLAVLRPHTGNAVTAQRVRAHLEAAGHVCILKDAFDFESPSEIANLILAENCEAALALHLYRGGRLLQGHRIPFGVIFGGTDVNEDANQAEKNTVMGRVLEEARFAVAFTESMKEMAQVQWPHAKGKIYVQSQGIATTPNAAFNWNTFLQRSEINQSADNLHIFLLICGLRQVKDPLYLVDAFSEWHQEEPNVYLVILGPEVDPVFTREVKANVKRAAGVRLIGEMPQEDLHAVVKNCFAVVNSSVSEGMSAAILEAMDLEVPVLARNIPGNAAMVKHEVTGLLFSNPQEFVHLAKRLVSDPALEKEIVVNGKEYVRMYHSWQVERDTYQQLIRKLEGSTED", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MATELLCLHRPISLTHKLFRNPLPKVIQATPLTLKLRCSVSTENVSFSETETETRRSANYEPNSWDYDYLLSSDTDESIEVHKDKAKKLEAEVRREINNEKAEFLTLLELIDNVQRLGLGYRFESDIRRALDRFVSSGGFDGVTKTSLHGTALSFRLLRQHGFEVSQEAFSGFKDQNGNFLENLKEDIKAILSLYEASFLALEGENILDEAKVFAISHLKELSEEKIGKELAEQVSHALELPLHRRTQRLEAVWSIEAYRKKEDANQVLLELAILDYNMIQSVYQRDLRETSRWWRRVGLATKLHFARDRLIESFYWAVGVAFEPQYSDCRNSVAKMFSFVTIIDDIYDVYGTLDELELFTDAVERWDVNAINDLPDYMKLCFLALYNTINEIAYDNLKDKGENILPYLTKAWADLCNAFLQEAKWLYNKSTPTFDDYFGNAWKSSSGPLQLIFAYFAVVQNIKKEEIENLQKYHDIISRPSHIFRLCNDLASASAEIARGETANSVSCYMRTKGISEELATESVMNLIDETWKKMNKEKLGGSLFAKPFVETAINLARQSHCTYHNGDAHTSPDELTRKRVLSVITEPILPFER", "text": "FUNCTION: Lyase that catalyzes the formation of isoprene from dimethylallyl diphosphate. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
{"protein": "MHEEFPTETPAVVTCGLPYANGDLHVGHLRTYVSGDAYARALESLGQSVAFVSGSDMHGTPIAVNAAEEGVDPESFAVEYHEQYEETFPQFNIEFDNYGHTHDETNTEMTRSFVRSWIDDDHVVEKEIEVAWDAEADQPLPDRFVEGTCPYCGEKARGDECDEGCQRHLEPGEIEAPVSTITGNPAEYRTRPHKFLRLSDFQEYLRGFIDRLEGTENAQNQPREWIEGELQDLCITRDMDWGIDYPADGDESGEDLVLYVWVDAPIEYVSSTKQYSEQVGRDEYDWEAVWKNQVDGVPPEGGEIVHIIGHDIIQHHTVFWPAMLRGAGFNEPRAVMACGFVNLDGDAFSTSRNRAVWADDYIESGLHPDLYRYHIITGSEFTADVDFSWDGLQERTNSELVGTLGNFLYRSLLFAERNYGGTPDAAVSDEVRNEIEAAMADFRTAVNDYRVRGLGRAPVELATFGNEYIQRHEPWKLTDDDPEKARQVIRDCVQIAKAIAVLAEPVLPGKAAALWDQLGEDGSVHDAELGAALESPPEAFDEPDELFEKLEDDRIEELNRQLEERIEAADAGDEEGEDEDEEPPAADLEPVADERISFGDFQDLDIRVAEVLEAEPIEGADDLAKLAVDIGVETRQIVAGIKQLHDLDSLSGTRIVVVANLEKAELFGVESNGMLLAAGEQADLLTTLEDAEPGTKVQ", "text": "FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily."}
{"protein": "MAQIPPSLQDLVNRFNQAQAQLQNVLLRKQQYEAELKEVEKAISEIERLPQDAKIFKNVGNFLVPQSRDVALQELRDRKELLELHVKTLTRQESMLREQLDKLREEINKELAKLKGGATEAAKGGG", "text": "FUNCTION: Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin subunit beta family."}
{"protein": "MSLQWWRDTCREADPQMRRRAAERQDRLTKPRGSLGRLEQVAIDLAALQGRERPSLERLWVTVFAGDHGVVAEGVSAYPQAVTGEMLRNFVRGGAAISVLARELGAGLEVVDLGTAVPLEALPGVRHLRLAAGTANFVEAPAMGAEQCLLALEAGRESVRRAEQAGSQLFIGGEMGIGNTTAAAAMACALLDAPVSALVGPGTGLDASGVAHKTAVIERALALHGAHRADPFETLRRLGGLEIAALAGAYLACAQKGMVALVDGYICSVAALCAVRLNPACRDWLLFAHSGAEPGHRHVLEALAAQPLLDLGLRLGEGSGAALAVPLLRQACALHAGMATFAEAAVSDRPA", "text": "FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). SIMILARITY: Belongs to the CobT family."}
{"protein": "MSAQNLAPPLNTLDFDKKPEETRVVVAMSGGVDSSVVAGLLKQQGYDVLGITLQLYDHGAAVHRAGSCCAGQDIDDARHVCETLGIPHYVLDYEKRFRETVINPFAESYVAGETPIPCVSCNQTVKFADLLATAKELGADALATGHYIRSRPNPSSEHPGRRALFRPADADRDQSYFLFATTQEQIDYLRFPLGGLPKAETRRLAEEMGLVVAKKADSQDICFVPQGKYSDIITKLKPNAALAGEIVHLDGRVLGSHEGILHFTIGQRRGIGIATGEPLYVVYLDARSRRVIVGPKEALETHRVYLRDVNWLGDETLAEAASGEGFACYAKVRSTRAPAPAVLHVDATGTYVDLTIGEAGIAPGQACALYSAPGDDARVFGGGFIERSEREPSAEASLKALLASPVAA", "text": "FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmA/TRMU family."}
{"protein": "MAAASSVSSPPLCLAGRVAIVTGSSRGIGRAIAIHLAELGARVVVNYSTSPVEAEKVATAITTNCSKDAEVAGKSPRVIVVKADISEPSQVKSLFDEAERVFESPVHILVNSAAIADPNHSTISDMSVELFDRIISVNTRGAFICAREAANRLKRGGGGRIILLSTSLVQTLNTNYGSYTASKAAVEAMAKILAKELKGTEITVNCVSPGPVATEMFYTGLSNEIVEKVKSQNLFGRIGETKDIAPVVGFLASDAGEWINGQVIMANGGCLL", "text": "FUNCTION: Aldehyde reductase that catalyzes the reduction of the aldehyde carbonyl groups on saturated and alpha,beta-unsaturated aldehydes with more than 5 carbons (PubMed:21169366). No activity on alpha,beta-unsaturated ketones (PubMed:21169366). Can use propionaldehyde, butyraldehyde, methylglyoxal, (e)-2-pentenal, (E)-2- hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, but not propenal (acrolein), crotonaldehyde, 2-butanone, 3-buten-2-one or 1- penten-3-one (PubMed:21169366). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MVKPLPRLRLQGFNNLTKALSFNIYDVCYARTEEERQRYIEYIDEQYDADRLTQILTDVAEIIGANILNIARQDYDPQGASVTILISEEPVIDKKQAGKELISDAVVAHMDKSHITVHTYPETHPQEGIATFRADIDVATCGVISPLKALNYLIESLESDIVIMDYRVRGFTRDVKGRKHYIDHKINSIQQFLAKNVKSRYEMFDVNVYQENIFHTKMHLKDFDLDQYLFEERAKNLSFKERMKIETLLKREIEELFHGRNLSE", "text": "FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily."}
{"protein": "MDMHPWLPNIKYIEEMLKSIGVNSIDDLFIDVPEEIKLKKELDLDYKKPLSEYEIILKLQELQNKNKRLKMPPFLGGGLCPHYVPEVVKFIIKRSEFYTAYTPYQPEISQGLLQALFEYQSLIAELFEMEVVNASLYDWGSALAEAIMMANRINKKKTVLVPKLMNPYHKEVVKTWTYGKGIKLVEIPPNERGTIDVSKLESMINEDDVSAIYIQQPNFYGIFEDEIEYIVDIAKKKKIITIMGVSPLALGLIKPPGEYEIDITVGDGQELGLSLNFGGPLLGILATRWDGQLVRQMPGRIVGLTKDSEGKRGFTLILQTREQFARREKATSNITTNEALMAIAAAVYLSLLGRNGIKELAKEIYIRSHYAKKRLEELGVNTVYNGDFFEEFAVDFRTDYDIIHSRLLEKNIHGGLKLGKTQALFCVTEVHTKSMIDELIESIREVFSG", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily."}
{"protein": "MTPSIDALRDFRASTCNLVGTPTVTNDLSENIILTSLDDLHNWARLSSLWPLLYGTACCFIEFAALIGSRFDFDRFGLVPRSSPRQADLIIVAGTVTMKMAPALVRLYEQMPEPKYVIAMGACTITGGMFSSDSTTAVRGVDKLIPVDLYLPGCPPRPEAIFDAVIKLRKKVGNEALRERGKLLPTHRYFTVAHKMKQVKPIITGTYLRAKTQQNALQAGVALPVDFKAEALPTKVILSNSLSLDN", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MQIKREAVCGTLQSNDCLVRIVPSEKLELDLKSSVLNEFGAQIKKTVQEVLDEFEVKNAKLFIEDKGALDCTIKARVETALRRANEK", "text": "FUNCTION: Covalent carrier of the coenzyme of citrate lyase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CitD family."}
{"protein": "MKKEFLHFLAFLITFVFCVKTQQVVKILRSRTMIDFGLEFQKAQIEMHNNPEDRVRFVDAVNLCLPASDTFFQNPDRENKFSENYSIKLIDTTPHVSEIVLQTFVKEILSLSNINTEDTLGKETLGKETYRLSNLLKKSKFGMESHHRIQNNSEGPNTFENGLGISTPKHGIAHFADAIQRFLDHKGNSSSNTRAAGARVEAIREALNDRDAINKSEEARKAREEVFIPSEPSKPSIASKRSSASKSTKS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI", "text": "FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C- terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3). SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit family."}
{"protein": "MIRYTVAGHSRRCVVGASKRVGAIKCITVAATKRFISNKPNEVFTKLTNDNDPKRDAFFKYTWGSWLKNDKQEKEKRFTKFSIEGLNRILNDIYIQSNEMAKAPDGKILPPVFNKNLTVSLVNNVVPKNIGKINPNEKVQVTTLSSIHEGKHHRIYKVDTNLNKAFILRIPYPLENENTLSYRIRSEVATMDFADLKLGIKVPKIFCYGVNSLNPVRQPFVLQEFIEGELLMKDWDPLIEDGSSNQKKYDNVIKQVSDFQSKLVSLKLNAFGSIYFNNDLKDGNEKEFVKEDIYDGETNPDLQNRWKIGPSVERCLWRHKSHLDFHKQMKPFLGPWSKKSPMDIIKNTGLLEAENAKTRIAMKEAGSSAELMYPRTLKEQITTYENLAKIAPDLFNVKTKAIPNMQELLSPRLFHPDLDPMNIIVNKEAQEAYLLDFEGACTKPFILQNSPQFIAYDGPKIYDLKEDITDFDKLSEAEKVQYQFMYKRTRNQHQWEKKLNDNNPKLITAVAPPVKLLRSPYIAAVERKTEEEYLLIDESLLQLKEVWDIFAQNDLVNQKKFPLNYSKEDIERHVEDLQKLHEKLISTPFAATQGWIPQDMFDQLLNSGSIVKQENGDYTVKQPEATK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM9 family."}
{"protein": "MSDENRLVAAVRTEFGKGAARRARRDGQVPAVLYGHGEDPRHLNVPSREFAAILRAHGTNAVLTLDIDGKEQVALTKSVVVHPIRNYIEHADLLVIKKGEKVTVDVPVVVTGEAASGTLVAQDAATVSLEADALHIPEQIEVSVEGLEVGTQILANQLELPKGATLQADEELLIVNVVAAPTAADLEEETGEAEGETAAAPAEEGAES", "text": "FUNCTION: This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily."}
{"protein": "MPVESEHFETLQLHAGQEPDAATSSRAVPIYATTSYVFRDCDHGGRLFGLQEPGYIYSRMMNPTADVFEKRIAALEHGAAAIATSSGTSALFMALTTLAKAGDNIVSTSYLYGGTYNLFKVTLPRLGITTKFVNGDDPNDLAAQIDENTKAVYVESIGNPMYNVPDFERIAEVAHAAGVPLMVDNTFGGGGYLVRPIDHGADIVTHSATKWIGGHGTTIGGVIVDSGKFDWKKNSKRFPEFNEPHPGYHGMVFTETFGNLAYAFACRTQTLRDVGGNANPFGVFLLLQGLETLSLRMERHVQNAFALAKYLEKHPKVNWVSYPGLESHVSHKLAKKYLKNGYGAVLSFGAKGGPDQSRKVVNALKLASQLANVGDAKTLVIAPAYTTHLQLTDEEQISAGVTKDLIRVAVGIEHIDDIIADFAQALEVA", "text": "FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway (PubMed:11754480, PubMed:6526818). Can also use O-succinyl-L-homoserine and L-homoserine as substrates (PubMed:6526818). Has also cysteine synthase (O- acetylserine sulfhydrylase) activity in vitro, but in S.pombe, it seems only to be involved in the alternative pathway of methionine biosynthesis under cysteine deficiency conditions (PubMed:11754480). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
{"protein": "MLTLKLFVYTVVIFFVSLFVFGFLSNDPGRNPGRKE", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbI family."}
{"protein": "MVEDSQETTHFGFQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMGREKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF", "text": "FUNCTION: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- methyl-6-methoxy-1,4-benzoquinol (DMQH2). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family."}
{"protein": "MAKKEVVKIAKLQFIAGQAKPGPSLAGVGINMPEFTRQFNEQTRDRGNEPVPVEITAYKDKSFDFRLFTAPASFKILQAIKAKSGSANSKTNIIGTLTLAQLEEIAKYKLPDLNTDDYKVAMHTIAGTAKNMGVLVEGWDDVKKAKEEAKAAKLAQLKAEAKEAALKEAEKELVDSKGKEVEVKLVGEEEQSESENN", "text": "FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. SIMILARITY: Belongs to the universal ribosomal protein uL11 family."}
{"protein": "MSEVEKTYCGFIAIVGRPNVGKSTLLNELLGQKISITSRKPQTTRHRIMGIHTEGPYQAIYVDTPGLHIEEKRAINRLMNRAASSSLGDVELVIFVVEGTHWTADDEMVVNKLRSLQCPVLLAINKVDNVTDKTKLLPHMQFLSQQMNFLDVVPISAEKGMNVDTIASIVRKHMPEAEHHFPEDYITDRSQRFMASEIIREKLMRFLGEELPYSVTVEIEQFVPNERGGYNIHGLILVEREGQKKMVIGNKGSKIKVIGTEARQDMERMFEAKVHLELWVKVKSGWADDERALRSLGYTDDLK", "text": "FUNCTION: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family."}
{"protein": "MSHQTVALASKAKSPKPKRGKLDKEKMTALEKHVSFFDRNKDGTVYPWETYQGFRALGTGRLLAAFVAIFINMGLSKKTRPGKGFSPLFPIDVKNSHLCMHGSDTDVYDDDGRFVESKFEEIFNKHARTHKDALTAEEIQKMLKTNRDPFDITGWLSDYGEWKILHTLAQDKNGLLSEKSVRAIYDGSLFHQLEKKRSSSSSRGKKQKLP", "text": "FUNCTION: Probable calcium-binding peroxygenase. May be involved in pollination. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the caleosin family."}
{"protein": "MRRFVLIFVLLILPFQFSWAAAARYCQHEKATATWHLGHHEHRHQQPEGKTDAEKKPFVDTDCGVCHLVSLPFVYGQTQDVLIANRVEVTDTQHSSEFSSLNARAPDRPQWQRLA", "text": "FUNCTION: Component of the czc cation-efflux system that confers resistance to cobalt, zinc and cadmium. May have a regulatory function. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MQVELIIKNLNVYNSYFKKFIKGDILINKGKFLHIGKGYEDRLWSENVIDGEGKYIIPGLIDIHMHIESSMTIPREFSKAAIKHGVTTVVADPHEIANVFGIRGIEEFIKFKGNLDIFYGIPSSVPSTSSSLETTGEKITHNEVKRLLEYDNIICLGEVMNFKDLIEDDDSNINKIINISKEKNIPLEGHCPKIQGVDLSLYIYRGVNGDHTQQSVGSLQEKIQNGMFIEMQHKSMTLENIKFLIENNLYEHFALVTDDVMADKLVKGHLDEILKEAVKLGMSIENAIYASTYTPARRMNLLDRGTIAPGKLADFILLDSIEDFNIYEVYKNGEMVFNRDKGLKEEFFEDKSKLDYRFYNSIELNNITKESLEVKVPNKYKNKVNCRTMKVLKNTTFTEEGEVTLNVYNNILQWEKSSCALIAVFERYGKNNNISFGLVEGEIIKEGAIATTWAHDHHNLMVMGRNISDMTIAANEVINSRGGYVVSKNNEVIAKLELPIGGIISDEPIEIIGEKLGEVRSAMRDLGYNHMNEIMSFSTLSLPVSPALKITDKGLIDVKKGSIVSLFK", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family."}
{"protein": "MAALRLLLGIDYGTKQIGVAVGQAITGQARELCTLKAQNGVPDWDKVQALINEWKPDAIVVGLPLNMDGTPSEMSARAEKFSRKLNGRFGVTVYTHDERLTTFEAKGERMARGGQKGSYRDNPVDAIAAALLLQGWLDEHPELLNV", "text": "FUNCTION: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YqgF nuclease family."}
{"protein": "MYPAHLLVLLAVCVSLLGAASIPPQPLNLVQFSYLIQCANHGSRATWHYTDYGCYCGKGGSGTPVDELDRCCKIHDDCYGEAEKKGCYPKMSAYDYYCGENGPYCRNIKKECQRFVCDCDVEAAKCFARAPYNDANWNIDTKKRCQ", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits collagen- induced platelet aggregation. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
{"protein": "MILENFKRESLIPLPVTFISTTSKDGIRNIAPYSCVMPVLRPFDLICVASAKMRDTVVNIKDTGEFVINMPGVEMVDKVIPTASHVPFDVNEFELADLKERPSKKVKAPGIEGCYAWMECKLHNIYEDEYEGFPYLLILGKVVHLEVNDDIYNPEDGSWDIEKANPLMMVESDRGMHFCTVSDINKFEPYGAMFPDGKDPLAWMYEKRETRE", "text": "SIMILARITY: Belongs to the flavoredoxin family."}
{"protein": "MTELSALVERVEKLRGTMVLCVGDAMLDRFVYGSVERISPEAPIPVLCIERETAMLGGAGNVVRNLVAVGAEPAFVSVVGDDTAGREVTRLVGEHGEIDPCIVVEPGRQTTIKTRFFASHQQLLRADRESRSPVGEAIRAQLLTRIERLLPKAGVMVLSDYGKGVLAEPIAIELIRRAKAAGKQVIVDPKGTDYTIYAGATVVTPNRKELHEATGQAVDSDEQVVAAARQLIDSCGFEAVLVTRSQDGMTLVRADGQIDHLPAEAREVFDVSGAGDTVVATLAAALASGATLPEAAHLANVAAGIVVGKVGTAVAYGDELVVALHREDLTLGEAKIVPVTAAAEVVDRWRRKGQKVGFTNGCFDLLHPGHVSILAQAKGACDKLVVGLNSDASVQRLKGPTRPVQSEASRATVLSSLATVDLVVIFGEDTPLEVIGTLKPDVLVKGADYTIDKVVGADLVQSWGGKVVLAELVNGQSTTNTIKKMNGN", "text": "FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7- phosphate at the C-1 position to selectively form D-glycero-beta-D- manno-heptose-1,7-bisphosphate. FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D- manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose. SIMILARITY: In the N-terminal section; belongs to the carbohydrate kinase PfkB family. SIMILARITY: In the C-terminal section; belongs to the cytidylyltransferase family."}
{"protein": "MNTMSHKFVLALDEGTTSARAILFDSDLNIVNIGQYEFPQHYPQPGYVEHDPEEIWEAQMLAVKKAISKIDAKQIVAIGITNQRETTVLWDAKSGKPVYNAIVWQDRRTSPITDWLKANYFKMIKDKTGLVPDPYFSASKIKWILDNVPNVREKAERGEIKFGTLDTYLIWRLTNGKAHVTDYSNASRTMLFNINKLECDREILELLKIPESILPEVKPSSEIYGYSEALGNLIPISGDAGDQQAALFGQVAFNVGEIKATYGTGSFILMNIGNNPIRSENLLTTIAWGLEKNKATYALEGSIFITGAAVQWFRDGLRAIDVSDEIEPLASNVEDNGGVYFVPAFVGLGAPYWDPYARGLIIGITRGTTKAHIARAILESMAYQTRDVIEVMQKESGISINSLKVDGGAAKDNLLMQFQADILGIKVIRPKVMETTSMGVAMLAGLGVGLWNSLEELRSIWKVDKEFIPSMSEEKRRALYSGWKEAVKRAMGWAKVVGGQV", "text": "FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. SIMILARITY: Belongs to the FGGY kinase family."}
{"protein": "MAKKKIAISCGDIQGVGLELILKSHKEVNAFCEPLYLIDGELLERANQLLHNAYETKTLNALAIHSPLPLLNSSTIGKISAQSGAYSFESFKKACELADSEEVDGICTLPINKLAWQQAQIPFVGHTDFLKQRYKEHQIIMMLGCSKLFVGLFSDHVPLSAVSQLIQVEALVKFLLAFQKSTQAKIVQVCGFNPHAGEEGLFGKEDEKILKAIQKSNQTLGFECFLGPLPADSAFAPNKRKITPFYVSMSHDVGLAPLKALYFDESINVSLNAPILRVSTDHGTAFDIAYQNKANNKSYLNAIKYLA", "text": "FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PdxA family."}
{"protein": "MALVFVYGTLKRGQPNHRVLRDGAHGSAAFRARGRTLEPYPLVIAGEHNIPWLLHLPGSGRLVEGEVYAVDERMLRFLDDFESCPALYQRTVLRVQLLEDRAPGAEEPPAPTAVQCFVYSRATFPPEWAQLPHHDSYDSEGPHGLRYNPRENR", "text": "FUNCTION: Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl- alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine. SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family."}
{"protein": "MKVGIIGAMEQEVTLLRDRIENRQTFQRAGCEIYTGQINGVEVALLKSGIGKVSAALGTTLLLEHSKPDVVINTGSAGGLASTLNVGDIVISDEVRYHDADVTAFGYEPGQMAGCPAAFPADEKFIALAQDAIDDLQLNAVRGLVVSGDAFINGAEPLARIRTTFPKAIAVEMEATAIAHVCHQFGTPFVVVRAISDVADKASHLSFDEFLSVAAQQSTRMVEAILAKLAAR", "text": "FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation. SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN subfamily."}
{"protein": "MDKETIKAHKISDEEYAQILEILGREPNLLELGVISAMWSEHCSYKSSKKYLNGFPTKAPWVIQGPGENAGVIDIGQGMAAVFKVESHNHPSFIEPFAGAATGVGGILRDVFTMGARVVAGLNSLKFGDIHDEKCGKHQKYLVKGVVNGISHYGNCMGVPTIGGECAFDECFNGNILVNAFALGVCKSEDIFYAKAEGVGNPVIYVGSKTGRDGLGGAVMASDSFNEESKSLRPTVQIGDPFSEKLLMEACLELFKTDYIVGIQDMGAAGLTSSSFEMAGRSGSGMKLYLDKTPMRESGMTPYELMLSESQERMLICAKKGYEDKVIEIFKKWDLDAVVMGEVTNTGKMELFWHDELVGLIPIEPLSEKAPILSRPTSEPKYLSEIKNYKFELKSSVQELFIQMLQNENINNKAFIYDQFDSSVQTNTIKADGRLGASVIRIKENGASVAMAIECNSRLNYVNSKIGAALAVASAGRKVACTGAKPLAISDCLNYGNPQNPEVMWQFAQGCEGIKEACKELNTPVVSGNVSLYNETEGVSIYPSPTIVSVGVLEDANKTLKASFEKENLSVYLLGESLGEFSGSMVMKIQDKKVSGSLKELDYKAELALWDLLYKANQNSLLECANSVGIGGIAMTLAKMFAISSVGANLTSDFDDEKMIFDESASRAIIGLSKENEEAFLNLAKEFGVKAYKLGVSTSQKHFKLDSIELSKAELDKLYFESFKEQIQ", "text": "FUNCTION: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FGAMS family."}
{"protein": "MEKILYLDPFSGIAGDMFLGLLVDLGVDPEELKKRLSKLGVEFELRIRKVNKKGITATKVDVVFPGKEHHEDHIDHEHHGRHLSEIMKILERLEDPAREKATEMFETLAEAESKVHGLPKEKVHFHEVGAMDAVIEIAGAVVGLELLGVERVFCGAVNTGSGFVMTEHGRYPVPAPATAELLKGIPIYMDQKVRAELVTPTGAVILKELVDEFGTPILRIEKVGYGAGTVDLEIPNVLRGYLGFLEGKSERDILIETNVDDMNPQLFGYLMEKLFETGAKDVFYTPIYMKKNRPAVKVSVLCSEEKRDQILKVLFKESTSIGARVFHLEKVEAPRKVISVETEYGKIPVKVAYFDSEVVNVSPEYEACKKIAQEKEVPLKEIYNAVYRKISEVQGNV", "text": "FUNCTION: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent enzymes. SIMILARITY: Belongs to the LarC family."}
{"protein": "MEKFTKIQGIAAPMPLVNIDTDMIIPKVFLKSIQRTGFGKNLFDEMRYNRDGTEIPDFVLNKPQYRDAEILVAGDNFGCGSSREHAPWAIADFGIKCIISTSFADIFFNNSFKNGILPIVLPQEQVDILMKDAEKGANARMTVDLEAQEITTSDGEVIPFEVDAFKKHCLLNGLDDIGLTMEKAAAIDTFEAQAAQARPWV", "text": "FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily."}
{"protein": "MPWVEPKPRPGPEQKPKLTKPDSATGPQWYQESQESESEGKQPPPGPLAPPKSPEPSGPLASEQDAPLPEGDDAPPRPSMLDDAPRLPLELDDAPLPEEETPEPTAICRHRHRCHTDCLEGLLSRTFQWLGWQVGAHPWIFLLAPLMLTAALGTGFLYLPKDEEEDLEEHYTPVGSPAKAERRFVQGHFTTNDSYRFSASRRSTEANFVSLLVVSYSDSLLDPATFAEVSKLDGAVQDLRVAREKGSQIQYQQVCARYRALCVPPNPILYAWQVNKTLNLSSISFPAYNHGRHPLYLTGFFGGYILGGSLGMGQLLLRAKAMRLLYYLKTEDPEYDVQSKQWLTHLLDQFTNIKNILALKKIEVVHFTSLSRQLEFEATSVTVIPVFHLAYILIILFAVTSCFRFDCIRNKMCVAAFGVISAFLAVVSGFGLLLHIGVPFVIIVANSPFLILGVGVDDMFIMISAWHKTNLADDIRERMSNVYSKAAVSITITTITNILALYTGIMSSFRSVQCFCIYTGMTLLFCYFYNITCFGAFMALDGKREVVCLCWLKKADPKWPSFKKFCCFPFGSVPDEHGTDIHPISLFFRDYFGPFLTRSESKYFVVFIYVLYIISSIYGCFHVQEGLDLRNLASDDSYITPYFNVEENYFSDYGPRVMVIVTKKVDYWDKDVRQKLENCTKIFEKNVYVDKNLTEFWLDAYVQYLKGNSQDPNEKNTFMNNIPDFLSNFPNFQHDINISSSNEIISSRGFIQTTDVSSSAKKKILLFQLRRIAEDCQIPLMVYNQAFIYFDQYAAILEDTVRNVLVASAAMFIVSLLLIPYPLCSLWVTFAIGSVIVGVTGFMAFWKVNLDSISMINLVICIGFSFDFSVHISYAFVSSSQPSVNQKSVEALYLLGYPVLQSAISTIIGVCVLAAAKAYIFRTFFKIMFLVMIFGAAHGLIFIPVFLTFFGRFI", "text": "FUNCTION: May play a role in sperm development or sperm function (PubMed:17904097). However, does not appear to have an essential role in spermatogenesis or male fertility (PubMed:21439084). SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localizes to the midpiece of the sperm tail. SIMILARITY: Belongs to the patched family."}
{"protein": "MPINKYKAAVVTSEPVWENLEGGVVKTIEFINEAGKAGCKLIAFPEVWIPGYPYWMWKVNYLQSLPMLKAYRENSIAMDSSEMRRIRAAARDNQIYVSIGVSEIDHATLYLTQVLISPLGDVINHRRKIKPTHVEKLVYGDGSGDSFEPVTQTEIGRLGQLNCWENMNPFLKSLAVARGEQIHVAAWPVYPDLSKQVHPDPATNYADPASDLVTPAYAIETGTWVLAPFQRISVEGLKRHTPPGVEPETDATPYNGHARIFRPDGSLYAKPAVDFDGLMYVDIDLNESHLTKALADFAGHYMRPDLIRLLVDTRRKELVTEVGGGDNGGIQSYSTMARLGLDRPLEEEDYRQGTDAGETEKASSNGHA", "text": "FUNCTION: Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family."}
{"protein": "MYGDHRQIWERIVEVIKSELTPTSYNTWLVHIKPLAIIDDVLFLSTPNTFTKNIINGRYINIIYDAASKATNKLYEIKILSEDEEEYREIKESIEKENLTESTTLSTLNPKYTFDTFVVGNSNKLAHAACLAVAQAPAKAYNPLFIYGGVGLGKTHLMHAIGHFINKHQSGYKIMYVTSETFTNELVNSIKDDKNEEFRNKYRNIDVLLIDDIQFIAKKERTQEEFFHTFNTLYEANKQIVISSDRPPKEIPTLEERLRSRFEWGLIADIQPPDYETRIAILKKKAQTENLNIPDEVLAYVAEKIQSNIRELEGALIRIVAFSNLTKANIDLELAKHALKEIVSNKTREITVKLIQEEVCKYYNIKLEDFRSRKRTKNIAYPRQIAMYLARELTDLSLPKIGEEFGKDHTTVIHAYEKISNEIKQDELLSRQIEELKKRIKGY", "text": "FUNCTION: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaA family."}
{"protein": "MTSDFKVIIVGGSVAGLSLAHCLEKIGVSFVVLEKGNQIAPQLGASIGILPNGGRILDQLGIFHSIEDEIEPLESAMMRYPDGFSFKSQYPQALHTSFGYPVAFLERQRFLQILYDKLKSKDCVFTNKRVVSIASGQDKVTAKTSDGAKYLADIVIGADGVHSIVRSEIWRHLKENSQISVLEAPNASIKHDYSCIYGISLNVPQIILGIQLNCLDDGVSIHLFTGKQSKLFWFVIIKTPQASFAKVEIDNTHTARCICEGLRTKKVSDTLCFEDVWSRCTIFKMTPLEEGVFKHWNYGRLACIGDAIRKMAPNNGQGANMAIEDACSLANILQKKISHGSIRDQDINSMFQEFSMAQRARTESVCAQSEFLVRMHANQGIGRRLLGRYLIPFLYDAPAGLSGFSISGATRIEFIDLPTRSLRGAWGKSWRGSWEFILQSLVYLRPKFRIVYALYLVAAAAFILYCLSSLFP", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts (PubMed:16765617). The geranylgeranyl diphosphate (GGPP) synthase ltmG is proposed to catalyze the first step in lolitrem biosynthesis (PubMed:16765617, PubMed:15991026). LtmG catalyzes a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (PubMed:16765617, PubMed:15991026). GGPP then condenses with indole-3-glycerol phosphate to form 3-geranylgeranylindole, an acyclic intermediate, to be incorporated into paxilline (PubMed:16765617). Either ltmG or ltmC could be responsible for this step, as both are putative prenyl transferases (PubMed:16765617). The FAD-dependent monooxygenase ltmM then catalyzes the epoxidation of the two terminal alkenes of the geranylgeranyl moiety, which is subsequently cyclized by ltmC, to paspaline (PubMed:16765617, PubMed:15991026). The cytochrome P450 monooxygenases ltmQ and ltmP can sequentially oxidize paspaline to terpendole E and terpendole F (PubMed:22750140). Alternatively, ltmP converts paspaline to an intermediate which is oxidized by ltmQ to terpendole F (PubMed:22750140). LtmF, ltmK, ltmE and ltmJ appear to be unique to the epichloe endophytes (PubMed:16765617, PubMed:15991026). The prenyltransferase ltmF is involved in the 27-hydroxyl-O-prenylation (PubMed:22750140). The cytochrome P450 monooxygenase ltmK is required for the oxidative acetal ring formation (PubMed:22750140). The multi- functional prenyltransferase ltmE is required for C20- and C21- prenylations of the indole ring of paspalanes and acts together with the cytochrome P450 monooxygenase ltmJ to yield lolitremanes by multiple oxidations and ring closures (PubMed:22750140). The stereoisomer pairs of lolitriol and lolitrem N or lolitrem B and lolitrem F may be attributed to variations in the way in which ring closure can occur under the action of ltmJ (PubMed:22750140). While the major product of this pathway is lolitrem B, the prenyl transferases and cytochrome P450 monooxygenases identified in this pathway have a remarkable versatility in their regio- and stereo-specificities to generate a diverse range of metabolites that are products of a metabolic grid rather than a linear pathway (PubMed:22750140). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
{"protein": "MNALIGQLLNAPVALLKGATIALSFFSLYLFGLVIYRLIFHPLAQYPGPLLGRITNLYAAYHAWKGDIHEDIWRCHQKHGNCIRYAPDRLAFDTAKAVSDIYGYGGNVRKSQVYDTLVHRTANTLTMRDKKQHAQRRRIMSHGFSDAAIRSFEPRVQELIQTLCDLLIVKDASADSEWSAPQDMAPWFDYLTFDIMSSLIFSASYDTLRQEKYRSVIRAIEESNVRVSVLLQAPIVTLFRSDKKLFSQSILGRNHFTRFIGSTVKERVQKSKLLADRDIFSYFQSSKAAANGDSMNMNELSGEAATLIVAGSDTTATTLAATMFYLSQSADIYHRVAQEVRQCFNSEDEIHAGSQLNACRLLRACIDEALRMSPPAGSALWREVEAGGITVNGRFVPEGYDVGVGIYAVHHNPTVYPQPFRFDPDRWLVDDTHDVRSAFMPFSLGTRSCIGKGLAQMEALLTLANIIWRYDFRAVPGGAVQPEYKLKDHVTGAKTGPVLQYRRIVRDKIMIG", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety (PubMed:28365998). The first step of the pathway is provided by the HR- PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate (PubMed:28365998). The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec- 4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl (PubMed:28365998). 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4- enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid (PubMed:28365998). The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2- aminodec-4-enoic acid which is activated and incorporated by the adenylation domain (PubMed:28365998). The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (PubMed:28365998) (Probable). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring (PubMed:28365998). The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur (PubMed:28365998). This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate (PubMed:28365998). Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A (PubMed:28365998). Subsequent oxidation yields the maleimide scaffold oxaleimide I (PubMed:28365998). Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H (PubMed:28365998). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "METTAIIRGVHISAQKTRLVADLIRGKSVAQALNILTFSPKKAAVILKKAVESAIANAEHNDGADIDELKVTTIFVDKAQSMKRFSARAKGRGNRIEKQTCHITVKVGA", "text": "FUNCTION: This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). FUNCTION: The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL22 family."}
{"protein": "MIVILNNGGQYVHRIHRSLRYLKIPSKIIPNSTPLAEIEENKEIKGIILSGGPDIEKASNCLDIALNSKLPILGICLGHQIIAKAYGGEIGRAESEEYAHSKIFVKEENDLFKNVPKEFTAWASHKDEVVGAPLNFEILAYSNICEVEAMKHKEKPIYGVQFHPEVSHTENGAEILKNFCKVCGLLGE", "text": "FUNCTION: Catalyzes the synthesis of GMP from XMP."}
{"protein": "MQIFVKTLTGTTIALEVEPSDTIENVKAKIQDKEGIPPDQQRLIFADKQLEEGRTLSDYNIQKESTLHLVLRLRGGVMEPTLVALAKKYNWEKKVCRRCYARLPVRATNCRKKACGHCSNLRMKKKLR", "text": "FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored- polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). FUNCTION: [Large ribosomal subunit protein eL40]: Component of the 60S subunit of the ribosome. SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm Nucleus. SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family. SIMILARITY: In the N-terminal section; belongs to the ubiquitin family."}
{"protein": "MLKIMLAVFLGGGTGSVLRWWLGLRLNPVHHAIPVGTLTANLAGAFIIGAGLAWFNRMTHLDPMWKLLVTTGLCGGLTTFSTFSAEVVFLLQEGRIGWAGLNVALNLFGSFMMTALAFWLFSSLSVR", "text": "FUNCTION: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family."}
{"protein": "MNYLSNITTSQRPWLLLALAALGLELSALYFQYVLGLAPCIMCVYQRLAILAIFSAGAIGAIGHQNIVARILAYVLWGVGAIWGLIIALEHVEMQKNSGSLFFSCEFIPNFPTWAPLHEWIPFLFEATGDCGEISWRFFNYSMPQWMVVVYALFSIVFSIVLINRLVCAKKP", "text": "FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family."}
{"protein": "MKPLTNGDLFKSPTLIKISALVFVTVAFFYLGKHWSDDGYQQLVFFSSSTSGSSIPEVSVSPNSNRVFNLSAIIPTNHTQIEIPATIRQQPPSVVADTEKVKVEANPPPPPPPSPSPPPPPGPVKSFGIVDANGVMSDDFEVGEVESDTVEDWGNQTEIVEAKSDGDSKARVRIKKFGMCPESMREYIPCLDNTDVIKKLKSTERGERFERHCPEKGKGLNCLVPPPKGYRQPIPWPKSRDEVWFSNVPHTRLVEDKGGQNWISRDKNKFKFPGGGTQFIHGADQYLDQMSKMVSDITFGKHIRVAMDVGCGVASFGAYLLSRDVMTMSVAPKDVHENQIQFALERGVPAMAAAFATRRLLYPSQAFDLIHCSRCRINWTRDDGILLLEINRMLRAGGYFAWAAQPVYKHEPALEEQWTEMLNLTISLCWKLVKKEGYVAIWQKPFNNDCYLSREAGTKPPLCDESDDPDNVWYTNLKPCISRIPEKGYGGNVPLWPARLHTPPDRLQTIKFDSYIARKELFKAESKYWNEIIGGYVRALKWKKMKLRNVLDMRAGFGGFAAALNDHKLDCWVLSVVPVSGPNTLPVIYDRGLLGVMHDWCEPFDTYPRTYDFLHASGLFSIERKRCEMSTILLEMDRILRPGGRAYIRDSIDVMDEIQEITKAMGWHTSLRDTSEGPHASYRILTCEKRLLRA", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the methyltransferase superfamily."}
{"protein": "MKKNFRVKREKDFKAIFKEGTSFANRKFVVYQLENQKNHFRVGLSVSKKLGNAVTRNQIKRRIRHIIQNAKGSLVEDVDFVVIARKGVETLGYAEMEKNLLHVLKLSKIYREGNGSEKETKVD", "text": "FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. SIMILARITY: Belongs to the RnpA family."}
{"protein": "MEIKELIAKATANMEKAVEYLDEQLSHVRAGKASPKLLDGIMVMYYGNATPLTQVASINTPDAKTIVVTPWERSLIKDIEKAIMDSPLGITPENNGELIRLGLPPLTEERRRQLVKQIKGDAEDAKVSVRNARRDAIDAIKKSVKTDGTPEDVAKDAEAEMQKVHDRYIKKIDELFAEKEKEIMTV", "text": "FUNCTION: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RRF family."}
{"protein": "MNASLRTDDVMRYQDARFQTLAAKLLPTQYLVVDDTTALTTTLGSCVAACLRDPVLKIGGMNHFLLPEGNAGDGAPARYGSYAMELLINDMLKRGAHRKRIEAKVFGGANVLKGFTSNPVGTRNAEFVRQYLQAEHIPIIAEDLCGIHPRKIWFFADTGRVVVQRLPHAHEAEVAATESAVRARLSKAPVTGGVELFE", "text": "FUNCTION: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis. SIMILARITY: Belongs to the CheD family."}
{"protein": "MAEQHSTPEQAAAGKSHGGLGGSYKVIVYEMENFQGKRCELTAECPNLTESLLEKVGSIQVESGPWLAFERRAFRGEQYVLEKGDYPRWDAWSNSHHSDSLLSLRPLHIDGPDHKLHLFENPAFGGRKMEIVDDDVPSLWAHGFQDRVASVRAINGTWVGYEFPGYRGRQYVFERGEYRHWNEWDANQPQLQSVRRIRDQKWHKRGVFLSS", "text": "FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SIMILARITY: Belongs to the beta/gamma-crystallin family."}
{"protein": "MLRWTVHLEGGPRRVNHAAVAVGHRVYSFGGYCSGEDYETLRQIDVHIFNAVSLRWTKLPPVRPAARGQAPVVPYMRYGHSTVLIDDTVFLWGGRNDTEGACNVLYAFDVNTHKWSTPRVSGTVPGARDGHSACVLGKTMYIFGGYEQLADCFSNDIHKLDTSTMTWTLICTKGNPARWRDFHSATMLGSHMYVFGGRADRFGPFHSNNEIYCNRIRVFDTRTEAWLDCPPTPVLPEGRRSHSAFGYNGELYIFGGYNARLNRHFHDLWKFNPVSFTWKKIEPKGKGPCPRRRQCCCIVGDKIVLFGGTSPSPEEGLGDEFDLIDHSDLHILDFSPSLKTLCKLAVIQYNLDQSCLPHDIRWELNAMTTNSNISRPIVSSHG", "text": "FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(KLHDC3) complex specifically recognizes proteins with a glycine (Gly) at the C-terminus, leading to their ubiquitination and degradation: recognizes the C-terminal -Arg-(Xaa)n-Arg-Gly, -Arg- (Xaa)n-Lys-Gly, and -Arg-(Xaa)n-Gln-Gly degrons. The CRL2(KLHDC3) complex mediates ubiquitination and degradation of truncated SELENOV and SEPHS2 selenoproteins produced by failed UGA/Sec decoding, which end with a glycine. May be involved in meiotic recombination process. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MATFKDACFHYRKITKLNRELLRIGANSVWIPVSSNKIKGWCIECCQLTELTFCHGCSLAHVCQWCIQNKRCFLDNEPHLLKLRTFESPITKEKLQCIIDLYNLLFPINPGIINRFKKIVNQRKCRNEFEQSWYNQLLFPITLNAAVFKFHSREVYVFGLYEGSSSCINLPYRIVNCIDLYDRLLLDQINFERMSSLPASLQSVYANKYFKLSRLPSMKLKQIYYSDFSKQNLINKCKIKSRIVLRNLTEFTWDSQISLHYDVINNREKILTALSTSSLKRFETHDLNLGRIKADIFELGHHCKPNFISSNHWQPASNVSQCRWCNVKYVFRNMDWKMESMYNELLSFIQACYKSNVNVGNCSSIENAYPLVKDMIWHSITKYIDQTIEKLFNVMNPVEVDGQQVISFHWQIDVALYIHIKMILKTETLPFALTLYQFGSIIKGIVNQWYDVTELDYLPLCTEQTDKLVKLEEEGKISEEYELLISDSEDDDQ", "text": "FUNCTION: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complexes, to modulate their activities. SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton. SIMILARITY: Belongs to the rotavirus NSP1 family."}
{"protein": "MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITAPIDVHLMVKPVDRIVPDFAAAGASIITFHPEASEHVDRTLQLIKENGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRIDESGFDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRSELAKVSHE", "text": "FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family."}
{"protein": "MRHDNDSWDITTSVGSTALFVAASRALEARKPDPLAVDPYAEVFCRAAGGDWAGLFDAGADPKPDHVLFSEFGEQFVNFQGARTRYFDAYFAAASDAGVRQVVLLAAGLDSRAYRLPWPDGTVVYELDQPRVLEFKREVLAERGEQPVAQRREVAVDLRDDWCAALTAAGFDPARPSAWLAEGLLMYLPATAQEALFSGIDALSAPRSWAAVEESVPMPAEVFAYKREEERAAGEEGTFFTLVYNERHAPAERWFGERGWAAEPTSLADYLTRVGRPAPVDDPEFGAMISAIRLVTATKG", "text": "FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. SIMILARITY: Belongs to the UPF0677 family."}
{"protein": "MSAQSSSTANIFVVLRQLRSLCYSNRPVTTSLSYTASHRTQSTTSTNAIKTQWHSSASYSTAPPSKPEKRPVEDIDLSQPMKSKPKKPQPAWAVQKNALKAKFKEGWKPRKKVSPDTMESIRKLHSMDSVKYSTKNLAEEFKISPEAIRRILKSKWRATEAEEIDRRDRWEKRKIRIQEQMMELGLRHSDPVSEARPGLQEELSRGTSVWNATEKTAGGYLPQKSNREFFPKKRFGAEERSAQDGDPWDVSGRDDLIDTKRDSFGDNWPQNSHMRRGAQSRTQTEDYHRQGYRGKPNW", "text": "FUNCTION: Required for respiratory activity and maintenance and expression of the mitochondrial genome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRG9 family."}
{"protein": "MRLLFAIALLGAVFAEDAWKAANVDRTIDATSQIVKVSTLYSFENVGNGPQSKVLIALSKEESATLSFISAGIDGSKGKLKISEKPAEKDLAVYEVDLRTPVAKGAKVTIRINLRITQVLEPLPSKIQQSDSQFVVLHTSAYVPSLYETVTQKTTIRTTQGGKLLSATTVSPSKQETERVIYGPYVNIPAFETKPVKVHYENNSPFVIATIVERFIEVSHWGNIAVEEYIELVHKGAELDGPFSRIDYQMDRRGRRQPALQQFTTVLPAQAKDIYYRDEIGNISTSAVRIRADSVDVEIRPRFPLFGGWKTSYVIGYNLPSEEYLYSKGNQYALKTKLFDHVFNDIVVEKLRTKVLLPEHVKRVKVATPYAVDRRPEELKPTYLDTTGRLVLVLEKENIVPDHSQFFTVTYEFEFVDMLREPLLASAFFFSLFFVIIVYSRFDFTISSDPAKDAEERSQIILGNLAKSVDSKQSAYEDLIEASQQYKSTKNDADLQEAKKTFIAARNQENSTLTDKIATLKTDSGASAAEKASELLKYDKTVFDAVDNYLKAVEKSTTKTAGTEEQQFLNKVKDARNRADSVLASI", "text": "FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Cytoplasmic granule. SIMILARITY: Belongs to the OST1 family."}
{"protein": "MAELSTRYNLPTNITEKSINLDLNSTARWVKEPSVGGWTVKWGNFIFHIPNTGMTLLHHLKSNFVVPEWQQTRSLFSHLFKNPKSTIMEPFLALRILLGVALKDQELQQSLIPGFRSIVHMLSEWLLLEVTSAIHISPNLLGIYLTSDMFKILMAGVKNFFNKLFTLHVVNDHGKPSSIEIKLTGQQIIITRVNMGFLVEVRRIDIEPCCGETVLSESVVFGLVAEAVLREHSQIERGQPLNLTQYMNSKIAI", "text": "FUNCTION: May act as a minor matrix protein that plays a role in assembly of viral nucleocapsid and virion budding. Unlike Ebola VP24, mVP24 has no measurable impact of host dendritic cell function. SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein; Cytoplasmic side Host endomembrane system; Peripheral membrane protein Note=In virion, localizes on the intravirional side of the membrane. In the host cell, it is found associated with virus-induced membrane proliferation foci and to the plasma membrane where budding takes place (By similarity). SIMILARITY: Belongs to the filoviridae membrane-associated protein VP24 family."}
{"protein": "MKAYLDLMRHVLDNGTDKSDRTGTGTRSVFGYQMRFDLGKGFPLLTTKKLHLRSIIHELLWFLKGDTNIKYLKDNNVSIWDEWADENGDLGPVYGYQWRNWPAPDGRHIDQIANVLEQIKKNPDSRRLIVSAWNPALVDEMALPPCHALFQFYVADGKLSCQLYQRSADIFLGVPFNIASYALLTMMMAQVCGLEAGEFVHTFGDAHLYRNHFEQAALQLEREPRALPVMKINPEVKDLFSFKFEDFELEGYDPHPHIKAAVSV", "text": "FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily."}
{"protein": "MNEKSIRVLEYGKMIDRLEERCLSAMAKEKARELRPIQSFGEITQLQSETSEAQSILIQRGNIPLGGIHDIKQYLRKTEIGSYLDPKELLLVKDTLRTARNLKSFFKEGDDQTKHPIVSGLIQGLQSFRAIEDRIEICIVSDTEISDHASSTLKNIRRQISSKNDAVRNKLNGIINSSTTQKYLQDAIITMRQDRYVVPVKQEHRGNVPGLIHDQSSSGATLFVEPMAVVQLNNELRELKIKEHIEIERILMEIAEMIAQYATEMRNNQIILTAIDFVFAKGKLSLEMKGVEPLLNVEGNVHIKNGRHPLLNADEVVPTNLWIGETFQTLVITGPNTGGKTVTLKTLGLLSMMAQSGLHVPADYGTRLAIFDQIFADIGDEQSIEQSLSTFSSHMTNIVNIVEEVTSNSLVLFDELGAGTDPTEGAALGMAILNHLREMNVTTVATTHYSELKQYALTNEGVENASVEFDVATLSPTYRLLIGVPGKSNAFEISKKLGLPDGLVQRAKRFLSQDTIHFEDLLQNIEKNRRESEIERQEAKRIRLEAEKFAEGYEDRKQRLEAQRDQILRDAKKEAYRLVKEAKMDSEHIIKGLREMKFELEAKEMNKKMEDAKNQLTGKMNDLSDHHQQILNKKNKKPPKNLKPGDAVRILSLNQVGHVLNEVDPKGEVQVQAGIMKVNMHISNLERVSPEKDIQQSGTGKIMKSKTGDTKSEVDVRGKNLEEAMLEIDKYLDDSYIVGLTQVTIIHGVGTGVLKAGIKQMLKKNKHVRTHREGVYGEGGMGVTIVELK", "text": "FUNCTION: Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2 subfamily."}
{"protein": "MSLLQFSGLFVVWLLCTLFIATLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSVLVFRFDVGVAPPEILLQALLSAGCFYAVYYVTYKTRLRKRVADVPRRPLFTMNRVETNLTWMILMGIALVSVGIFFMHNGFLLFRLNSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISLWMLAAAGVLGIVGMFWLALKRYGMNVSGDEAFYTFLYLTRDTFSPWENLALLLQNYDNIDFQGLAPIVRDFYVFIPSWLWPGRPSMVLNSANYFTWEVLNNHSGLAISPTLIGSLVVMGGALFIPLGAIVVGLIIKWFDWLYELGNRETNRYKAAILHSFCFGAIFNMIVLAREGLDSFVSRVVFFIVVFGACLMIAKLLYWLFESAGLIHKRTKSSLRTQVEG", "text": "FUNCTION: Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WzyE family."}
{"protein": "MSHQEGSTGGLPDLVTESLFSSPEEQSGVAAVTAASSDIEMAATEPSTGDGGDTRDGGFLNDASTENQNTDSESSSEDVELESMGEGLFGYPLVGEETEREEEEEEMEEEGEEEEQPRMCPRCGGTNHDQCLLDEDQALEEWISSETSALPRSRWQVLTALRQRQLGSSARFVYEACGARTFVQRFRLQYLLGSHAGSVSTIHFNQRGTRLASSGDDLRVIVWDWVRQKPVLNFESGHDINVIQAKFFPNCGDSTLAMCGHDGQVRVAELINASYCENTKRVAKHRGPAHELALEPDSPYKFLTSGEDAVVFTIDLRQDRPASKVVVTRENDKKVGLYTISMNPANIYQFAVGGHDQFVRIYDQRRIDKKENNGVLKKFTPHHLVYCDFPTNITCVVYSHDGTELLASYNDEDIYLFNSSLSDGAQYVKRYKGHRNNDTIKCVNFYGPRSEFVVSGSDCGHVFFWEKSSSQIIQFMEGDRGDIVNCLEPHPYLPVLATSGLDQHVRIWTPTAKTATELTGLKDVIKKNKQERDEDNLNYTDSFDNRMLRFFVRHLLQRAHQPGWRDHGAEFPDEEELDESSSTSDTSEEEGQDRVQCIPS", "text": "SIMILARITY: Belongs to the WD repeat DCAF8 family."}
{"protein": "MSGWMSYFTGRKDTRESARDAIVGLRQQLLMLEKKEEFLQKKIEEEMKKAKANATGNKRLAMAALRQKKAHENELDRIAGTRLTLETQVNAIESANLNAETMVAMKKGADALKGIHSNLTAEGVDATMDKIREQMDLTNDISDAISNPVGMGIVLDEDDLKEELEALEQEQLDDRLAGADRVPSHLPASPVGQTTGRAAVEEDEDDEEAQLRKLQAELAM", "text": "FUNCTION: Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Also required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNF7 family."}
{"protein": "MDASDRSMAVKRMEMVQSLRQKGLVNERVLDAMQRIERHRFVDRESSVSAYEDSAYPIGYGQTISQPYTVAYMTTLLLERCPPPGKVLEIGTGSGYQAAILDALGYRVYSVERIPELHDRVVGLFRSLGLAISCRVGDGSLGWEEEAPFDGIMVTAAAPRCPEHLLEQLGDNGCLVIPVGEHNMQQMTVYRRVGERFEKELFHHFAFVPLIGREGWN", "text": "FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. L- isoaspartyl/D-aspartyl protein methyltransferase family."}
{"protein": "GLFLDTLKGLAGKLLQGLKCIKAGCKP", "text": "FUNCTION: Antibacterial activity against Gram-positive bacterium S.aureus (MIC=40 uM) and Gram-negative bacterium E.coli (MIC=2 uM). Has activity against C.albicans (MIC=46 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ranatuerin subfamily."}
{"protein": "MSVIDQNAIAVGPRISEADVGDYLALLKPRVMSLVIFTALIGLLIAPGHFHPVLAITSLLCIAVGAGASGALNMALEGDIDSLMSRTANRPIPRGRVTRQEALAFGITLSFFSVLTLGILVNWYAGALLAFTIFFYVVIYTLWLKRWTAQNIVIGGAAGALPPVVAWVAATGSIAPEPLLLFLIIFFWTPPHFWALALFRSDDYARAGVPMLPVVAGPDATRLQILLYTILLVAIAAAPWPLGYFDAVYGVVSLALGAGMLWFAIEVFRKRERSQSLRANRKLFAFSILYLFALFATLGLEAVARMIAPLIW", "text": "FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily."}
{"protein": "MPSPLNHHLSCFVLSVILLGSHVSTSKIPIAPQSVCEGLIEPSVLSIDKPLENIKANRGDSLVLRCAFYASPQPTIVWYHRGKRVDSHPAAHFETLLSATNLGQSVVESALRIDCLDERTAGEYFCEATSPCTQPVVTSSTVTINKAPKSITGTCKSIRQPLESPPIVSDFTLSRIELPGGVAQLACRVRGVPTPKTKWFKIEEDESLSTIDGQPNYMHLSNGDLLIVGDEETISESFRCVASNPLGSVHQDASVIYMMA", "text": "FUNCTION: Together with zig-8, required postembryonically to maintain the position of ASI and ASH head neuron cell bodies and ventral nerve cord axons of PVQ, PVP and HSN neurons by preventing their displacement that could occur during body growth and movement. May act by reducing L1CAM-like protein sax-7 (long isoform) adhesion. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKISQFGSLAFAPIVLLQLFIVQAQLLTDSNAQDLNTALGQKVQYTFLDTGNSNDQLLHLPSTTSSSIITGSLAAANFTGSSSSSSIPKVTSSVITSINYQSSNSTVVTQFTPLPSSSRNETKSSQTTNTISSSTSTGGVGSVKPCLYFVLMLETIAYLFS", "text": "SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Lipid-anchor, GPI-anchor."}
{"protein": "MPAPTGTDHPDITVTDSLGEHDVARARLMVDGAAAADGISPLSEQAVAAIDAAAGSGVRHVISAAGYANISPGRGDEPAMIEAVVDPQLRRRGHGRALLTTAFGEAERAGDARVWAHGDLPGAQALAASMGLVRRRELLQLRRGLGTGAPALPELIVDDSVRLRTYAGSADDAEILRVNNAAFDWHPEQGGWGAEQIAERVGAAWFDPEGLFLAFDAANPERLLGFHWTKQHDTELGEVYIVGVDPAAQGRGLGRLLTLAGLHHLAATGRSEVNLYVEGDNTAALHTYERLGFGRYAIDVAYGRPEGD", "text": "FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol. SIMILARITY: Belongs to the acetyltransferase family. MshD subfamily."}
{"protein": "MPHSVTLRGPSPWGFRLVGGRDFSAPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCHDHLTLSVSRPEGRSWPSAPDDSKAQAHRIHIDPEIQDGSPTTSRRPSGTGTGPEDGRPSLGSPYGQPPRFPVPHNGSSEATLPAQMSTLHVSPPPSADPARGLPRSRDCRVDLGSEVYRMLREPAEPVAAEPKQSGSFRYLQGMLEAGEGGDWPGPGGPRNLKPTASKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCESHAKARVKPPEGYDVVAVYPNAKVELV", "text": "FUNCTION: [Isoform 2]: Involved in reorganization of the actin cytoskeleton and in regulation of cell migration. In response to oxidative stress, binds to NQO1, which stabilizes it and protects it from ubiquitin-independent degradation by the core 20S proteasome. Stabilized protein is able to heterodimerize with isoform 1 changing the subcellular location of it from cytoskeleton and nuclei to cytosol, leading to loss of isoforms 1 ability to induce formation of actin stress fibers. Counteracts the effects produced by isoform 1 on organization of actin cytoskeleton and cell motility to fine-tune actin cytoskeleton rearrangement and to attenuate cell migration. FUNCTION: [Isoform 1]: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle (PubMed:19307596). Involved in reorganization of the actin cytoskeleton (PubMed:21636573). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1- containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton Nucleus Cytoplasm Cytoplasm, perinuclear region Cell projection, lamellipodium Cell projection, dendritic spine Early endosome membrane; Peripheral membrane protein; Cytoplasmic side Recycling endosome membrane; Peripheral membrane protein; Cytoplasmic side Synapse, synaptosome Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin (PubMed:10826496). Colocalizes with TRIP6 at cell-cell contacts and lamellipodia (PubMed:10826496). In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol (PubMed:21636573). Colocalizes with SRC at the perinuclear region, but not at focal adhesions (PubMed:19307596). SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Note=Stains more diffusely in the cytoplasm with thin fibers forming a dense mesh-like pattern."}
{"protein": "EDPGTMGPGNPAPSPDSDTPSDSSKGSDSNPALLLVGNAAPPVHKKDSVVWPAWVYCTRYSDRPSSGPRTRKLKKKKSEKEDKRPRTAFTAEQLQRLKAEFQANRYITEQRRQTLAQELSLNESQIKIWFQNKRAKIKKASGMKNGLALHLMAQGLYNHSTTTVQEKEESE", "text": "FUNCTION: Required for proper formation of the apical ectodermal ridge and correct dorsal-ventral patterning in the limb. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the engrailed homeobox family."}
{"protein": "MAALKGRRRTCEPGESMETESQETGSKGQAQVYLPGRGPPLREGEELVMDEEAYVLYHRAQTGAPCLSFDIVRDHLGDNRTELPLTLYLCAGTQAESSQSNRLMMLRMHNLHGTKPPPPEGSDDEEEEDDEEDEEERKPQLELAMVPHYGGINRVRVSWLGEEPVAGVWSEKGQVEVFALRRLLQVVDDPQALATFLRDEQTRMKPIFAFSGHMGEGFALDWSPRVPGRLLTGDCQKNIHLWTPTDGGSWHVDQRPFVGHTRSVEDLQWSPTEDTVFASCSADASIRIWDIRAAPSKACMLTTATAHDGDVNVINWSHREPFLLSGGDDGALKVWDLRQFKSGSPVATFKQHVAPVTSVEWHPQDSGVFAASGADNQITQWDLAVERDPEAGDAETDPGLADLPQQLLFVHQGETDLKELHWHPQCPGVLVSTALSGFTVFRTISV", "text": "FUNCTION: Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus Chromosome Note=Present in the nucleus throughout interphase and is detached from chromatin at the onset of mitosis and rebinds at telophase when the pre-replication complexes (pre-RC) is formed."}
{"protein": "MDPEETSVYLDYYYATSPNPDIRETHSHVPYTSVFLPVFYTAVFLTGVLGNLVLMGALHFKPGSRRLIDIFIINLAASDFIFLVTLPLWVDKEASLGLWRTGSFLCKGSSYMISVNMHCSVFLLTCMSVDRYLAIVCPVVSRKFRRTDCAYVVCASIWFISCLLGLPTLLSRELTLIDDKPYCAEKKATPLKLIWSLVALIFTFFVPLLNIVTCYCCIARKLCAHYQQSGRHNKKLKKSIKIILIVVAAFLVSWLPFNTFKLLAIVSGLQERYFPSAMLQLGMEVSGPLAFANSCVNPFIYYIFDSYIRRAIVHCLCPCLKNYDFGSSTETSDSHLTKALSTFIHAEDFTRRRKRSVSL", "text": "FUNCTION: Probable chemokine receptor. SIV-1 coreceptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MDPAERAQAARARVPRIDPYGFERPEDFDYAAYEEFFSTYLVILTKRAIKWSKLLKGSGGVRKSVTDLNRTFPDNVMFRKTADPCLQKTLYNVLLAYGLHNQDVGYCQGMNFIAGYLILITKNEEESFWLLDALVGRILPDYYSPAMLGLKTDQEVLAELVRMKLPAVAALMDGHGVLWTLLVSRWFICLFVDILPVETVLRIWDCLFNEGSKIIFRVALTLIKQHQEFILEASSVPDICDKFKQITKGDFVTECHTFMQKIFSEPGSLSMATITRLRESCRAALQAQS", "text": "FUNCTION: May act as a GTPase-activating protein for Rab family protein(s)."}
{"protein": "MLTLSDFDFPLPPELIAQSALPDRSASRLLVVERTAPEDTSEAVRLVDRAFSDILEYLNPDDLLVFNDTRVIKARFFGHKPSGGRIEVLVERVVDTHTVLAQVRASKTPVEGSLLHLADDAFAVTVGPRVDQFFTLRFPEPALDLIERYGRLPLPPYITHDPDAYDETRYQTVYARNPGAVAAPTAGLHFDDALFARLDAAGIRRAFLTLHVGAGTFQPVRTENLSEHKMHSEWYAISPELADAVRETRARGGRVIAVGTTSLRALESAAAEDGTLEAGSGDTDIFITPGYAFRIVDALITNFHLPKSTLLMLVSALAGVEAIRDAYRHAVDARYRFFSYGDAMLLTRRDRRA", "text": "FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the QueA family."}
{"protein": "MSQEIRAIVRIGDTDLDGNKQVAYSLTKIRGIGIATAYAICRKLGIDPHAILGALSEEQINKLDWAVRNLHELAPAWFLNRRKDPETGKDLHLIGAELVLAAKRDVDLMKKLKSWKGVRHSLGLKVRGQRTVTTGRLGPVAGVTKKKAAAGGK", "text": "FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. SIMILARITY: Belongs to the universal ribosomal protein uS13 family."}
{"protein": "MTIALGKYTKDEKDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFALIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL", "text": "FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family."}
{"protein": "MGRVRTKTVKRAARQIVEKYYGKLGLDFQYNKKVAEEVALIPSKRMRNKVAGFITHLMRRIQKGPVRGISLKLQEEERERRMDYIPEKSELEVPVIQVDQDTADMLNFLKISLPNLKVMSFNAHEHRERH", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS17 family."}
{"protein": "MAKDFLLEIGTEEIPAKFAPGVLNQLREQAQKHCQELRLDYQDLKVYTTPRRFAVLIQGLAEKQTDFTAEVKGPAVKAAYDAEGNPTKAAQGFARGQGVEPKDLFVQELNGVSYVYARKFELGQPTLQLLPKLCTDLITGLHFPKPMRWADLEFRFARPIRWIVALFGSEVIPFEFVGLASGKASRGHRTLGGPVTLDSPADYEKQMLQAFVMVDPEQRRQSVWEQIHALAAKVGGDVEKDDDLLDEVTHIIEYPTALLGEVAPNYMHLPEPVITTPMKEHQRYFPVRDKEGKLLPYFITVRNGDDHALAKVKAGNEKVLKARLEDAAFYYREDQKTPLAELVEKLDKVTYHEKLGSVRQRVERIRTLARGIAARLGMESKKQDLVERTALLAKADLVTLMVYDFPELQGIMGADYARMVGEKPEVCTGILEHYQPRFAGDELPQSYTGQIVSVADKLDAIVGAFGIGIQPTGSQDPYALRRQAQGVVGIILEAGWDISLEQLIAASYVNFAEQGISLLPLADLQSALQDFFQQRLRFVLQEQGARYDTLDAVLAQGSNQITRAARKAQVLAAKRETTEFVPYSQAYIRCLNLSKKAQTQPLDPKNLIDPTEIALAAALVQRQEAFAALIEKGDYAEAYALASELIPMIEALFNAVMIMVEDEILKQARLALLGECVAILGCLGDLSLLA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MLSIARVSLLRNARMVPVHAMQMRPVVVRRSLHNGSLLLQKKNEKNEAPKSILDDDMLARAGVEVEGNEAGSKDKSGRAGEAGESAEQDDSTGDKGSGKKKRSRKSSTDIKRERYANWFYILSLLGLASGALSMARDWDSDESEELKKEIPNGYTPALMYKRMKRRWESIFTFFQEPPFPDLLPPPPPPPYQRPLTLVLSLEDLLVHSEWTQQSGWRTAKRPGVDYFLGYLSQYYEIVLFSSNYMMYAEKIAEKLDPIHAFITYNLFKEHCLYKDGVHIKDLSKLNRDLGKVLIIDTDENSFKLQPENAIYLEPWDGKADDRLLRLIPFLEYLATQQVSDVRPILKSFPDNKNIPEAFEKRVQVLKEKFERDERVKNDKNLFLKLLGIGLIGTKPKFPLDLIREEGEKNYVRFMKLVEEEKEKIKLQQQAMGQQTFTLKDYVEGNIPTPEEQLKLQMEKQQEIEAQFEEQKKLKAQQGSK", "text": "FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to direct preproteins in transit and direct them to the channel protein TIM23, and possibly facilitates transfer of the translocating proteins from the TOM complex to the TIM23 complex (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM50 family."}
{"protein": "MTQRTLGGTNRKQKRTSGFRARMRKSNGRKVIQARRKKGRHRLSV", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
{"protein": "MDLRAFIRLVPDFPKPGILFRDITPLLRDPAGFRAAIEQLAAGTATMGSLDYVVGIESRGFILGAALAQHLGLGFVPVRKPGKLPPPVLSQSYSLEYGQDQLQLHAHALRPGDRVVIVDDVIATGGTAAATAQLVAQSGAEVGGFAFLIELAFLSGRKLLPPEIPTHVVMVDESN", "text": "FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MVALLGAGAISLVFTLFLTPLFIKLFHRLQWGQFIRDDGPQSHHTKRGTATMGGIVIILASVIGYFAGHLLTWDGIRFDPVTPSGLLVVFMMVGLGFVGFLDDYLKTRKQQSLGLGGWQKIAGQVIVATVFAVLAITLRDPVSGLTPASTAISLFRDLPLDFMALGAVIGTGLFIVWICLIVASASNGVNVADGLDGLAAGASIFSIGSYVIIGFWQFNQSCDSVSSYQNEYRCYEVASPLDLAIIAASIVGALIGFLWWNTSPAQIFMGDTGSLGLGGALAALAILSRTELLLVFIGGLFVIVAGSVVLQRAYFKITKGKRIFLMSPLHHHFELKGWAEVTVVVRFWIIAGLLVAAGVGTFYLEWITQ", "text": "FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily."}
{"protein": "MDTIAARALTVMRACATLQEARIVLEANVMEILGIAINRYNGLTLRGVTMRPTSLAQRNEMFFMCLDMMLSAAGINVGPISPDYTQHMATIGVLATPEIPFTTEAANEIARVTGETSTWGPARQPYGFFLETEETFQPGRWFMRAAQAATAVVCGPDMIQVSLNAGARGDVQQIFQGRNDPMMIYLVWRRIENFAMAQGNSQQTQAGVTVSVGGVDMRAGRIIAWDGQAALHVRNPTQQNAMVQIQVVFYISMDKTLNQYPALTAEIFNVYSFRDHTWHGLRTAIRNRTTLPNMLPPIFPPNDRDSILTLLLLSTLADVYTVLRPEFAMHGVNPMPWPLTAAIARAAYV", "text": "FUNCTION: The VP7 protein is one of the five proteins (with VP1, VP3, VP4, and VP6) which form the inner capsid of the virus. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the orbivirus VP7 family."}
{"protein": "MVKVSLDNVKLLVDVDKEPFFKPSSTTVGDILTKDALEFIVLLHRTFNNKRKQLLENRQVVQKKLDSGSYHLDFLPETANIRNDPTWQGPILAPGLINRSTEITGPPLRNMLINALNAPVNTYMTDFEDSASPTWNNMVYGQVNLYDAIRNQIDFDTPRKSYKLNGNVANLPTIIVRPRGWHMVEKHLYVDDEPISASIFDFGLYFYHNAKELIKLGKGPYFYLPKMEHHLEAKLWNDVFCVAQDYIGIPRGTIRATVLIETLPAAFQMEEIIYQLRQHSSGLNCGRWDYIFSTIKRLRNDPNHILPNRNQVTMTSPFMDAYVKRLINTCHRRGVHAMGGMAAQIPIKDDPAANEKAMTKVRNDKIRELTNGHDGSWVAHPALAPICNEVFINMGTPNQIYFIPENVVTAANLLETKIPNGEITTEGIVQNLDIGLQYMEAWLRGSGCVPINNLMEDAATAEVSRCQLYQWVKHGVTLKDTGEKVTPELTEKILKEQVERLSKASPLGDKNKFALAAKYFLPEIRGEKFSEFLTTLLYDEIVSTKATPTDLSKL", "text": "FUNCTION: Malate synthase which takes part in the glyoxylate cycle (PubMed:1454530). MLS1 activity is essential for cells to grow on oleic acid as a sole carbon source (PubMed:11846793). Two steps of the glyoxylate cycle take place in the cytosol, the splitting of isocitrate into succinate and glyoxylate, and the dehydrogenation of malate to oxaloacetate (PubMed:1454530). However, the formation of malate from glyoxylate and acetyl-CoA undertaken MLS1, occurs in the peroxisomes when cells are grown on oleic acid (Probable). The source of acetyl-CoA being either peroxisomal when breaking down fatty acids, or cytosolic when extra-cellular two-carbon substrates are used, therefore, although not strictly essential, the peroxisomal localization of MLS1 appears to be advantageous for cells growing on oleic acid, in that acetyl-CoA production and utilization are thereby intimately compartmentalized together to increase efficiency (Probable). SUBCELLULAR LOCATION: Peroxisome matrix Note=Imported in peroxisome via recognition by the peroxisomal targeting signal receptor PEX9 in an oleate-dependent manner. SIMILARITY: Belongs to the malate synthase family."}
{"protein": "MYDKQDKQAVAIIGSGNIGTDLMIKVLRDAKHLEMGAMVGIDPASDGLARAKRLGVATTAHGIEGLVTMPNFGAIRIAFDATSAGAHHRHAAVLREHGVTVIDLTPAAIGPFVVPVVNLFAHLDAPNLNMVTCGGQATIPIVHAVSRVAPVRYAEIVASIASRSAGPGTRANIDEFTETTSKAIETVGGAARGKAIIVLNPAEPPLMMRDTVYCLTEEEADTDEIESSIRAMVSAVASYVPGYRLKQAVQFDRYTAANPLALHANERRAGLKVSVFLEVEGAAHYLPSYAGNLDIMTSAALAAAEQIAASRVAA", "text": "SIMILARITY: Belongs to the acetaldehyde dehydrogenase family."}
{"protein": "MSATALGMIIFAYLCGSISSAILVCRIARLPDPRENGSGNPGATNVLRIGGRVAAAAVLVFDILKGMLPVWLAYKLDVPPLYLGLTAIAACLGHIYPVFFHFRGGKGVATAFGAIAPIGWDLTGLMTGTWLLTVLLSGYSSLGAIISALIAPFYVWWFKPQFTFPVAMLSCLILMRHHDNIQRLWRGQEGKIWGVFRKKKNDAAEQEEKKEE", "text": "FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PlsY family."}
{"protein": "MITVTNARKNYGNFAALDDVTIEIPSGELTALLGPSGSGKSTLLRSIAGLEALDDGVVVIAGKDVTRVAPQKRDIGFVFQHYAAFKHMTVRDNVAFGLKIRKRPKAEITKRVDELLGIVGLDGFQHRYPAQLSGGQRQRMALARALAVDPQVLLLDEPFGALDAKVRADLRTWLRRLHEEVHVTTVLVTHDQEEALDVADRIAVMNKGRIEQVGTPEDVYDRPANEFVMSFLGDVARLNGHLVRPHDIRVGRDPSMALAAHEGTAESAGVTRATVERVVHLGFEVRVELRNAATGDLFSAQVTRGDAEALRLTDGETVYARATRIPELPTQ", "text": "FUNCTION: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family."}
{"protein": "MKHVGPVEPAAGGPEVPPVAALGAAPESAAALFGPRLATAQRYAEVLGTAGVERGLLGPREVDRIWDRHILNSAAVAGLLGRGDRIIDIGSGAGLPGIPLAIARPDLEVVLLEPLLRRSEFLTEVVDELGLAVEVVRGRAEERPVRNRFGDRDAAVSRAVAALDKLTKWSMPLLRHDGRMLAIKGERAAEEVDRYRRVMTASGAADVRVVTCGANYLRPPATVVSARRAKPPHPKSARTGKAGTR", "text": "FUNCTION: Specifically methylates the N7 position of guanine in position 518 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family."}
{"protein": "MAKTIAYDEEARRGLERGLNSLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKEQIAATAGISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDAERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIQSGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLETADVSLLGKARKVVVTKDETTIVEGAGDAEAIQGRVAQIRAEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALLQSAPSLEELSLTGDEATGANIVRVALSAPLKQIALNGGLEPGVVAEKVSNLPAGHGLNAATGEYEDLLAAGVADPVKVTRSALQNAASIAALFLTTEAVVADKPEKAAAPAGDPTGGMGGMDF", "text": "FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Secreted, capsule Cell surface Secreted, cell wall. SIMILARITY: Belongs to the chaperonin (HSP60) family."}
{"protein": "MTGEITILYGSETGNAEEYAKYLKQRLRSYNLKPINLASLDDYPLKRLVTHTSYLIIICSTTGQGEIPRNGKKFMKFILKKKLPSDLFQHLQLTTFGVGDSSYVKYNYAIKKIHTRLMQLGCQLLSPRCEADEISPEGVDGYYIEWEAELIAALLNKFPSASKISSEAVPMPEYRISVSKSDTTIDPKEVIDNPIVSRLGKDGLKLGTVLENNRLTSSNHFQDVRDFKFSSNGLNYLPGDTVSLFPCNFDEDVDALLQSQPQWLKIADKPLNLKNFPHLEGGFADILTLRTLFKYHLDIMSIPRRSFFALLWHFVDPSTEDGEREQEKLKEFGSLDEPEELYDYANRPRRSILETLLEFENNLTIPVSYILDLFPLIRPRMFSIASCPSSKEVELVVAIVEYKTIIRKIRRGVCTRWLKNLKPGDQFLFSIQRSSFKYKDDNSPIIMVAPGTGIAPMKSLIDEVIQNNSKQELYLFFGCRFKEKDNLIESFWHGNENQNLHLVSAYSRDSNSKYRYVQDALFAHSELIGKLLIEQNAKVFVCGSSGKMPREVKITFVEIVKKFTGMDEGDAQKYIIGLEDNGRYKEDAW", "text": "FUNCTION: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. Positively controls H(2)O(2)-induced cell death. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Note=Relocalizes to mitochondria after H(2)O(2) exposure. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family. SIMILARITY: In the N-terminal section; belongs to the flavodoxin family."}
{"protein": "MSDSAYNPGQDGAKMGFADAMSYGDYLHLDALLDQQHCKSDAHDEMLFIIQHQTSELWMKLALHELQAAREALQQGQTAEMFKMLARVSRIFEQLNSAWDVLRTMTPADYTRFREALGPSSGFQSYQYRLIEYVLGNRNPNMLRPHEHVPEVHALLSAELARPSFYDEVNRYLFQTLDGHTENLPAPRLDAPHALDETIQERWLKVYGDIDTYWTLYELAEKLVDLEDYFRRWRFNHVTTVERVIGFKRGTGGTSGVQYLRRMLSVELFPELWTLRGDL", "text": "FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family."}
{"protein": "MSKKQGKPEYVTAISNRKARFEYEILDTIEAGIELLGSEVKSVRLGKASLSESYAMIHHGQVWLENMQITPYEHNTLDTLEPKRSRRLLLHKAEIMRLQSKISEKGLTLIPLKAYFNKRGVLKIELGLARGKKLYDKRETIKNRDAKRQLQQLRKQY", "text": "FUNCTION: Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans- translation. SUBCELLULAR LOCATION: Cytoplasm Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. SIMILARITY: Belongs to the SmpB family."}
{"protein": "MACGLVASNLNLKPGECLKVRGELAPDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNSKDDGTWGTEQRETAFPFQPGSITEVCITFDQADLTIKLPDGHEFKFPNRLNMEAINYMAADGDFKIKCVAFE", "text": "FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Cytoplasm Secreted Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion."}
{"protein": "MDRQKEFVLRTLEERDIRFVRLWFTDVLGFLKSVAIAPAELEGAFEEGIGFDGSSIEGFARVSESDTVAHPDPSTFQVLPWATSSGHHHSARMFCDITMPDGSPSWADPRHVLRRQLTKAGELGFSCYVHPEIEFFLLKPGPEDGSVPVPVDNAGYFDQAVHDSALNFRRHAIDALEFMGISVEFSHHEGAPGQQEIDLRFADALSMADNVMTFRYVIKEVALEEGARASFMPKPFGQHPGSAMHTHMSLFEGDVNAFHSADDPLQLSEVGKSFIAGILEHACEISAVTNQWVNSYKRLVQGGEAPTAASWGAANRSALVRVPMYTPHKTSSRRVEVRSPDSACNPYLTFAVLLAAGLRGVEKGYVLGPQAEDNVWDLTPEERRAMGYRELPSSLDSALRAMEASELVAEALGEHVFDFFLRNKRTEWANYRSHVTPYELRTYLSL", "text": "FUNCTION: Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback- inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
{"protein": "MALLVEKTTSGREYKVKDMSQADFGRLEIELAEVEMPGLMASRSEFGPSQPFKGAKITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDTTLLIHEGVKAEEIYEKSGQFPDPDSTDNAEFKIVLSIIKEGLKTDPKRYHKMKDRVVGVSEETTTGVKRLYQMQANGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVVAGYGDVGKGCAAALKQAGARVIVTEIDPICALQATMEGLQVLTLEDVVSEADIFVTTTGNKDIIMLDHMKKMKNNAIVCNIGHFDNEIDMLGLETHPGVKRITIKPQTDRWVFPETNTGIIILAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNEKSSGKYEKKVYVLPKHLDEKVAALHLEKLGAKLTKLSKDQADYISVPVEGPYKPFHYRY", "text": "FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. SIMILARITY: Belongs to the adenosylhomocysteinase family."}
{"protein": "MKYEKLEPAAIDETVAGLVGWTLAADRLSISKSYKFRNFVEAFGFMTEAALTAEKLNHHPEWFNVYSRVDVKLTTHDANGLTDHDVKLAKAMEKAAARRAD", "text": "SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family."}
{"protein": "MGSENSALKSYTLREPPFTLPSGLAVYPAVLQDGKFASVFVYKRENEDKVNKAAKHLKTLRHPCLLRFLSCTVEADGIHLVTERVQPLEVALETLSSAEVCAGIYDILLALIFLHDRGHLTHNNVCLSSVFVSEDGHWKLGGMETVCKVSQATPEFLRSIQSIRDPASIPPEEMSPEFTTLPECHGHARDAFSFGTLVESLLTILNEQVSADVLSSFQQTLHSTLLNPIPKCRPALCTLLSHDFFRNDFLEVVNFLKSLTLKSEEEKTEFFKFLLDRVSCLSEELIASRLVPLLLNQLVFAEPVAVKSFLPYLLGPKKDHAQGETPCLLSPALFQSRVIPVLLQLFEVHEEHVRMVLLSHIEAYVEHFTQEQLKKVILPQVLLGLRDTSDSIVAITLHSLAVLVSLLGPEVVVGGERTKIFKRTAPSFTKNTDLSLEDSPMCVVCSHHSQISPILENPFSSIFPKCFFSGSTPINSKKHIQRDYYNTLLQTGDPFSQPIKFPINGLSDVKNTSEDSENFPSSSKKSEEWPDWSEPEEPENQTVNIQIWPREPCDDVKSQCTTLDVEESSWDDCEPSSLDTKVNPGGGITATKPVTSGEQKPIPALLSLTEESMPWKSSLPQKISLVQRGDDADQIEPPKVSSQERPLKVPSELGLGEEFTIQVKKKPVKDPEMDWFADMIPEIKPSAAFLILPELRTEMVPKKDDVSPVMQFSSKFAAAEITEGEAEGWEEEGELNWEDNNW", "text": "FUNCTION: May play a role in regulating cell adhesion/migration complexes in migrating cells. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus Cell projection, lamellipodium Note=Colocalized with EZR/VIL2, actin and CD44 in lamellipodia. SIMILARITY: Belongs to the protein kinase superfamily."}
{"protein": "MTCPICGSKTAPSYRPFCSKRCADLDLAKWLNGSYAIPASSEDEEEPLDQEAETPVAPRH", "text": "FUNCTION: Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C- terminal domain of GyrB, which probably disrupts DNA binding by the gyrase. SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family."}
{"protein": "RGSNLTIHPLRNTNDIDY", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MNLLIVAIGGGIGAIARYLVGQWMMKRFPDPPFPIAMLVVNLLGSFGLGAFFGLYYHELFAASYDDIGYLFGGIGFFGAFTTYSTFSVEAVLLIREREWKKLFSYVLLSIVGSIAAFLLGFYGTSSW", "text": "FUNCTION: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family."}
{"protein": "MKGEAGHMLHNEKSKQEGHIWGSMRRTAFILGSGLLSFVAFWNSVTWHLQRFWGASGYFWQAQWERLLTTFEGKEWILFFIGAIQVPCLFFWSFNGLLLVVDTTGKPNFISRYRIQVGKNEPVDPVKLRQSIRTVLFNQCMISFPMVVFLYPFLKWWRDPCRRELPTFHWFLLELAIFTLIEEVLFYYSHRLLHHPTFYKKIHKKHHEWTAPIGVISLYAHPIEHAVSNMLPVIVGPLVMGSHLSSITMWFSLALIITTISHCGYHLPFLPSPEFHDYHHLKFNQCYGVLGVLDHLHGTDTMFKQTKAYERHVLLLGFTPLSESIPDSPKRME", "text": "FUNCTION: Promotes megakaryocyte differentiation by enhancing ERK phosphorylation and up-regulating RUNX1 expression. SUBCELLULAR LOCATION: Cytoplasm Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "VAGRSVVKIAEGYL", "text": "SUBCELLULAR LOCATION: Secreted, cell wall."}
{"protein": "MPVKIPDDLPAAEILESENIFVMSETRAANQDIRPMKVLILNLMPNKIETETQLLRLLGNTPLQVDVDLLRIHDKESKHTSIDHMNNFYRDFEAVRQKNYDGLIITGAPLGQIEFEEVSYWDHIREIIDWSQQHVTSVLFLCWAAHAALFHLYGLNRNLLEQKRSGVFVHRRTTQHFPLLRGFDDEFLAPHSRFAEMSLEQLKAHPELQVLTESDTAGAYMVLSRNNRNLFVMGHPEYQKSTLKDEYHRDLEQGLNPDVPQNYFRDDNPEKEPVARWHGHGSLLVSNWLNYYVYQLTPYNLDDMSGITPWENKQ", "text": "FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MetA family."}
{"protein": "MAQLSLLVLSLFLTLISLPPPGASISSCNGPCRDLNDCDGQLICIEGKCNDDPEVGTHICRGTTPSPQPGGCKPSGTLTCRGKSHPTYDCSPPVTSSTPAKLTNNDFSEGGDGGGPSECDESYHSNNERIVALSTGWYNGGSRCGKMIRITASNGKSVSAKVVDKCDSRHGCDKEHAGQPPCRNNIVDGSNAVWSALGLDKNVGVVDITWSMA", "text": "FUNCTION: Kissper is an anion-selective pore-forming peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kiwellin family."}
{"protein": "MASINLNIIMAFIMALMGVLIYRSHLMSTLLCLEGMMLSLFILVTLLISQSHMLTTSMMPLILLVFSACEAGVGLALLVTISTTYGNDHVQNLNLLQC", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
{"protein": "PYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKITETLLKSAKEVETKDQIAATAGISAGDQTIGDLIAEAMDKVGNEGVITVEESNTFGL", "text": "FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the chaperonin (HSP60) family."}
{"protein": "MKNTYTSGELEQFFSSDLSSTDGAVQVAIDLEEARQNQQIELIASENIVSKAVMEAQGTVLTNKYAEGYPGRRYYGGCEHVDLVETLAIDRAKLIFKADFVNVQPHSGAQANGAVMLALVKPGDTILGMSLDAGGHLTHGAKPAQSGKWFNAIHYGVRKDDMRIDYDQVLALAIEHQPKMIIAGGSAIPRQIDFAKFREIADQVGAILMVDMAHIAGLVAAGAHQNPLPFADVVTTTTHKTLRGPRGGLILTNNPDVAKKINSAVFPGLQGGPLMHVIAAKAVALGEVLEPSFGAYIKQVLSNARVLASTLQQRGCDIVTDGTDTHLMLVDLRPKGLKGNTTEESLERAGITCNKNGIPFDSEKPMVTSGIRLGTPAGTSRGFGNDEFELIGQWIGDVLDGLVANPEDNSVAEQKVLQQVQQLCLRFPLYS", "text": "FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family."}
{"protein": "MTKVTPTSLADLIRRPIVTEKATLLLENNQYVFEVDPRATKPQIKAAIEELFEVKVTGISTSNMPIKKKRIGKFIGHKAQYKRATVTLAPEFTINLFPEV", "text": "FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
{"protein": "MSDIPFWQTKTLEDMTDAEWESLCDGCGQCCLHKLMDEDTDEIYFTNVACRQLNIKTCQCRNYERRFEYEPDCIKLTRENLPTFEWLPVTCAYRLLAEGKPLPKWHPLIVGSKAAMHAERISVRHIAVKESEVVDWQDHILNKPDWAQ", "text": "SIMILARITY: Belongs to the UPF0260 family."}
{"protein": "MQQTCKRKIWMQISVALVTSLWMISAQAELLIKVTEGRVDAVPIAVVPFDGAKNAEEDVSAIVQADLHRSGQFKPLPPQDMLSRPRNEQEMIYRDFKVLGTEYVITGSMKRQETGGYEVGYALFDVARQKKLMSETYRPPASQLRDVAHAISDRIYEQLTGIPGAFSTKILYVTHNRHDANPYQLQYADADGHRVTTILRSNEPIMSPTWSPDGRKIAYVSFEDQGRPGIYIHNLATTEREKVSSFSGINGAPDWSPDGQHLALTLSRDGNPEIYMLNLSTKVLTRLTNNYGIDTEPRWLPDGEHLVFTSSRSGGPQIYKLNINDKSVRRVSFQGGYNARSDVTPDGRYLVYVHRRNGNYNVGVQDLQRGTFNIVTRTDMDESPSVAPNGSMVIYGTQHGGAGVLEAVSIDGRVKVELPSKEGEVREPAWSPFL", "text": "FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the TolB family."}
{"protein": "MAKVLVLYYSSYGHVETMAQHVAEGAKSVPGVEVTLKRVPETIPVDQAKAIGVKVDQAAPVATVDELANYDAIIFGTPTRFGNMAGQMRTFLDQTGGLWMKGALVGKIGSVFASTGTQHGGQETTITSFHTTLLHHGMVIVGVPYACSGLVDMKEITGGTPYGATTLAGADGSRQPSANELDIARYQGKHVAQLAAKLAA", "text": "SIMILARITY: Belongs to the WrbA family."}
{"protein": "MVKVYAPASSANMSVGFDVLGAAVTPVDGALLGDVVTVEAAETFSLNNLGRFADKLPSEPRENIVYQCWERFCQELGKQIPVAMTLEKNMPIGSGLGSSACSVVAALMAMNEHCGKLLNDTRLLALMGELEGRISGSIHYDNVAPCFLGGMQLMIEENDIISQQVPGFDEWLWVLAYPGIKVSTAEARAILPAQYRRQDCIAHGRHLAGFIHACYSRQPELAAKLMKDVIAEPYRERLLPGFRQARQAVAEIGAVASGISGSGPTLFALCDKPDTAQRVADWLGKNYLQNQEGFVHICRLDTAGARVLEN", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase subfamily."}
{"protein": "MIASVGDSRYYPKSVANGEKSDQRERLVSAIPVEDDSSFELKLRPQWLREFIGQPKVKENLAVAIEAARSRGEALDHVLLYGPPGLGKTTLANIIANEMQAQFQQTSGPTLQIKGDLTAILTNVRDKQVLFIDEVHRLQPALEELLYSAVEDYKLDIIIGQGPSARTHTIDVAPFTLVAATTRAGLLSAPLRSRFGIVLRLEFYTTEDLKIILKRSAEILNVEIDEGGAAEIATRCRGTPRIANRLLRRVRDYAQVRGAGKIDRETAQKALEMLEVDQHGFDEVDRRLMLTIIEKYQGGPVGLNTLAASLAEETDAIEEIYEPFLIQLGFLDRTPRGRVATHLAYEYFKMKPPKKQDSLF", "text": "FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuvB family."}
{"protein": "MAILVRLFFALFVVSVYFFRVRLRLSHIPGPFLASLTNINRRQWVTTGRAHTIHTELHRQYGKVVRAGPNTVFVSDPAAIPAIYRFNEPYQKSEFYDALMPYVRGKSIPDVFATRDEHIHRTMKQPIAAIYSMSNLVSFEPYVKSTIEYFFSRLDSLFVETGKVCNFGLWLHLFASDVMGEITFSRRLGFLETGGDMENVMANNWKFFVQAAPATQMPWLDYFWKRNPLLPGSVKPNKVIEFGVARIQERLHLSEKHPDHVNSRDFLSRFIAAKEKNSQIGPDAIMTWANSNIQAGSDTTAILLSALFYHLLKNPTSLAALCTEIDAAAKRGCLSSILTWKETRDLPYLDACVKEAARLHPPISLPLERVIPESGTVIGGFKIPGGTRVAMNPWAVHRDRDVFGADADTWRPERWLEGEEKAKTLYNSLLTFGGGHRSCLGKNISYLEIYKLVPSILLRYEIGLAEPEKEWHLENRWFVMPSRFYVRLKARNGVTKL", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3- methylorsellinate into nidulol (PubMed:24244835). CicB converts 3- methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine (PubMed:24244835). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MKFVNIYEIQRFDGQPTRHGIAPKKIFRSKYIPTGLVPRLKYWRDVPSRAEMSKRIGKYFEDEFKFYPNEEKLNEAVNIVQEKWISHYGTSLNVTSVSESFRTLPKSTSAGLPFKSGCTKYEARNKMMRFARSQWDRVSKELQLQVLPCRLGARCQLRKRGENKPRLIWAYPGYLSIIENQYLTAIKKVPPPNFIGWSTNWLDGGKSLNRLLFGDKWTWQSIAQIDFSSFDATVRTELIFHAFKILRSLFDLTRTENIMLDQLRHYFINTPILFYDKIIVKNRGIPSGSAFTQIIGTIVNMIACQYASLRSRDYNLRIPFSCWLGDDSFLNFETALCRQEFEYDYLEKFKELGLNVSIDKTHYTTRFIDDFEVRFKGVRPYVKFLGKQIDILLDLTFHNDLDKLDAQMALPEKEDLSAYETGVRLIGLVWAYGAHYDIYLRILKVYLSLKLKPEFHVQQLLSYSEKPERTKRYQENFFSSMKYQLNLDLDIYDLLAFPKFWDVSNRYFGSKYERLDFRSHKIYG", "text": "FUNCTION: RNA-dependent RNA polymerase which replicates the viral genome."}
{"protein": "MISVTELRNGTKVEMDGGLWECLEYSHLKMGRGGAKVVTKFRNMETGSIVDRTFNSGEKLQDIYVEGKKMQYLYRDGDDYVFMDMETFDQVHLPPALVGDTAKFMKENTEVEVAMYGDKALSITLPNQVILKIVQTDPGVRGDTVSGGTKPATLETGAVVQVPLFVEQGTDVKVDTRTGQYLSRA", "text": "FUNCTION: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the elongation factor P family."}
{"protein": "MRLHYLLFVFLILFLVPAPGDAFLPKTLRKFFCRIRGGRCAVLNCLGKEEQIGRCSNSGRKCCRKKK", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MPKASDIKKGSAIEHNGKVYFVKEITKLTPSGRAGATLFRMRMYDVATGSKADESFKTDEIITLADFSRRSATFSYVDGNEYVFMDSEDYTPYTFNKEAIEEELLFISEDTQGIQILIVDGVPVAIELPSAVDLEIVDTAPSIKGASASARTKPATMTTGLTVQVPEYIANGEKVKINTTEHKFMSRA", "text": "SIMILARITY: Belongs to the elongation factor P family."}
{"protein": "MIKSSVGGNEGKSKFFDQEKRLERTWNNSNWGKQGIISPVDGDMKIIDIELEKKMTKLEHENKLMKNALYELSRMENNDYAAWVIKVLFGEVAHGAK", "text": "FUNCTION: Protein that assembles into highly ordered structures and provides a specific site for viral DNA replication. Probably anchors the viral DNA replisome to the host membrane. SUBCELLULAR LOCATION: Host membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phi29likevirus DNA replication protein 1 family."}
{"protein": "MLKIGINGFGRIGRLVARIAMANPQVTLVGINDLVPASNLAYLFKYDSTHGSYGGTVVAKEEGIVIDDQFIPCFSQRNPAQLPWGDLGADYVVESTGLFTTYATAENHLKAGAKRVIISAPSKDPEKIPTFVVGVNHLNYNADTDKIVSNASCTTNCLAPIAKILDDNFGIVEGLMTTVHAMTATQPTVDGPSKKDFRGGRGAAQNIIPSSTGAAKAAALVLPQLKGKLTGMAFRVPTPNVSVVDLTFKTEKATSYEEICAAMKTAAEGELKGILGYTADDVVSMDFRTDPRSSIFDAGAGIGLNSNFFKVVSWYDNEWGYSCRVIDLMLTMASKDGLV", "text": "FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MAIYGIGTDIAQVSRVAAVLERTGGRFAEKVLGPDELRVFHARRARSEARGIAFLATRFSAKEAFSKAIGLGMHWPMTWRALQTLNHPSGEPYVVASGELADWLAARGITARVTVSDERDYAVSFVVAETDAAPAPAAAPVSRTSS", "text": "FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family."}
{"protein": "MTKKLHIKTWGCQMNEYDSSKMADLLDATHGYQLTEVAEEADVLLLNTCSIREKAQEKVFHQLGRWKLLKEKNPDLIIGVGGCVASQEGDHIRQRAHYVDIIFGPQTLHRLPEMINAVRGNRSPVVDISFPEIEKFDRLPEPRADGPTAFVSIMEGCNKYCTYCVVPYTRGEEVSRPCDDILFEIAQLAAQGVREVNLLGQNVNAWRGENYDGTTGSFADLLRLVAAIDGIDRIRFTTSHPIEFTDDIIEVYRDTPELVSFLHLPVQSGSDRVLNLMGRTHTALEYKAIIRKLREARPDIQISSDFIVGFPGETTDDFEKTMKLIADVNFDMSYSFIFSARPGTPAADMVDDVPEEDKKQRLYILQERINQQAMAWSRRMLGTVQRILVEGTSRKSLMELSGRTENNRVVNFEGTPDMVGKFVDVEIVDVYTNSLRGKIVRTEAEMGLRIAESPESVIARTRKENDLGVGIYQP", "text": "FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily."}
{"protein": "MKHWRLVSYDIREPKRLRRVAKIMEGFGERIQYSVFRIYSTDKELEKLRWKLAKVTEEEDNIFYLTLCTKCASGAHTQEKKSAWPEAPKTLKIL", "text": "FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2 protein family."}
{"protein": "SQCCYQICSPC", "text": "FUNCTION: Probable toxin that inhibits ion channels. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTRPVVTRFAPSPTGFLHIGGGRTALFNWLYARKHGGTMLLRIEDTDRQRSTQEAIDAILDGLKWLGIDWDGATVYQFARAARHREVAEQLLAAGKAYRCYATAEELTAMRDKARAEGRAKLYDGSWRDRDPSEAPAGVKPTIRLKAPLTGETVIEDQVQGRVAWQNENLDDLVLLRGDGTPTYMLAVVVDDHDMGVTHVIRGDDHLINAARQKQIYDAMEWELPVMAHIPLIHGPDGSKLSKRHGALGVDAYRAMGYLPAALRNYLVRLGWSHGDQEIFTTQEMIDAFDLPAIGRSAARFDFAKLESLNGHYIRQSDDHSLVTLLEDLLKYIPQGPAIAAKFDDSIRAKLTQAMPGLKERAKTLIELLDNAGFIFADRPLALDPKAQAVLTPETRQLIGRLRAALEDVSPWTAATTEAAMRAFAEQAGLKLGAVAQPLRVALTGRTTSPGIFDVLAVLGRDECLSRLADQSA", "text": "FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily."}
{"protein": "MGPRARPALLLLMLLQTAVLQGRLLRSHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDHESRRVEPRTPWVSSRISSQMWLQLSQSLKGWDHMFTVDFWTIMENHNHSKESHTLQVILGCEMQEDNSTEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQNRAYLERDCPAQLQQLLELGRGVLDQQVPPLVKVTHHVTSSVTTLRCRALNYYPQNITMKWLKDKQPMDAKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQVEHPGLDQPLIVIWEPSPSGTLVIGVISGIAVFVVILFIGILFIILRKRQGSRGAMGHYVLAERE", "text": "FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class I family."}
{"protein": "MMSYEPAEPVPVEEQPILEKLIGIRQRLAVLKRDRTRFIEKNEVFHLKDELVEQMNLLDSRRSTNSTRTIVDSQLEDCLHLLSLFYLAIGRNNDLPAFFVQLGTVRRLLEYNLEGACYTQNDLKPLKERLERIRAAIVEGSKKEDASPVVVKYLNNKLAVCDRNYSEAQHNISKISPELIGIQTRLVSIHRQIDGFAVRPTSDPGFIDRTMEQLKEIEEMKDSNGMFCDADHVPLQGQELCNGILEECFSFLEDAKTKEGLSDEMKSSPKLQQIYHRLDELLNKLKHLTLTHRWTLRETDLYVYRASLAEIDSMRIDGQFLDEQGNAPAGQRILLYLLRRCYAYIYQLLSSSEPVSEELMAVHNQLRTVKRCLLEVQRSGGICSERDLYPYQMKLASLENLRVNGKFLASDHSVPEGQELVNSLLTQCHQLIEELRDEKHQHDIEEREGSENTDGNL", "text": "FUNCTION: Involved in bleomycin tolerance with links to DNA repair and/or proteasome function. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CUB1 family."}
{"protein": "MTTPAPLTGLLPLNPEQLARLQAATTDLTPEQLAWVSGYFWGVLNPRSGAVAVTPAPEGKMPGVTLISASQTGNARRVAEALRDDLLAANLNVTLVNAGDYKFKQIASEKLLVIVTSTQGEGEPPEEAVALHKFLFSKKALKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDVLKSRAPVAAPSQSVATGAVNDIHTSPYTKDAPLTATLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVDGKTLPLAEALEWHFELTVNTANIVENYATLTRSESLLPLVGDKAQLQHYAATTPIVDMVRFSPAQLDAQALIGLLRPLTPRLYSIASAQAEVESEVHITVGVVRYDIEGRARAGGASSFLAGRVEEEGEVRVFIEHNDNFRLPANPQTPVIMIGPGTGIAPFRAFMQQRAADGAEGKNWLFFGNPHFTEDFLYQVEWQRYVKEGVLNRIDLAWSRDQKEKIYVQDKLREQGAELWRWINDGAHIYVCGDARCMAVDVEKALLEVIAEFGAMDIESADEYLSELRVERRYQRDVY", "text": "FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. SIMILARITY: In the N-terminal section; belongs to the flavodoxin family. SIMILARITY: Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family."}
{"protein": "MGLGLLLPLLLLWTRGTQGSELDPKGQHVCVASSPSAELQCCAGWRQKDQECTIPICEGPDACQKDEVCVKPGLCRCKPGFFGAHCSSRCPGQYWGPDCRESCPCHPHGQCEPATGACQCQADRWGARCEFPCACGPHGRCDPATGVCHCEPGWWSSTCRRPCQCNTAAARCEQATGACVCKPGWWGRRCSFRCNCHGSPCEQDSGRCACRPGWWGPECQQQCECVRGRCSAASGECTCPPGFRGARCELPCPAGSHGVQCAHSCGRCKHNEPCSPDTGSCESCEPGWNGTQCQQPCLPGTFGESCEQQCPHCRHGEACEPDTGHCQRCDPGWLGPRCEDPCPTGTFGEDCGSTCPTCVQGSCDTVTGDCVCSAGYWGPSCNASCPAGFHGNNCSVPCECPEGLCHPVSGSCQPGSGSRDTALIAGSLVPLLLLFLGLACCACCCWAPRSDLKDRPARDGATVSRMKLQVWGTLTSLGSTLPCRSLSSHKLPWVTVSHHDPEVPFNHSFIEPPSAGWATDDSFSSDPESGEADEVPAYCVPPQEGMVPVAQAGSSEASLAAGAFPPPEDASTPFAIPRTSSLARAKRPSVSFAEGTKFAPQSRRSSGELSSPLRKPKRLSRGAQSGPEGREAEESTGPEEAEAPESFPAAASPGDSATGHRRPPLGGRTVAEHVEAIEGSVQESSGPVTTIYMLAGKPRGSEGPVRSVFRHFGSFQKGQAEAKVKRAIPKPPRQALNRKKGSPGLASGSVGQSPNSAPKAGLPGATGPMAVRPEEAVRGLGAGTESSRRAQEPVSGCGSPEQDPQKQAEEERQEEPEYENVVPISRPPEP", "text": "FUNCTION: Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein. Plays a role in the regulation of neurite-like outgrowth (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MKTSLLADPLFFTTPQLARFRFAFKLTFAVVLSLFLGFHLQLGTPNTAVMTAAIVAGGPAFVAGGEPFSGAIRHRGMLRIVGTFIGCIGALAIIISTIRAPIVMMLLCCIWAGLCNWISSLVKIENSYIFGLAGYTTLIIILATQGTPMLTPQFAVERCSEIVLGIACVIFADLLFAPRSIKQDVDRSLRELMVGQYRLLQLSMSGADEGTIDTTWHALVRKTTALDGMRSNLMMESSRWQNSNRRLTSLHTQSLTMITQACETYLTLQDVPTHVKSSLKQVLDPPVESFGDVHHHVKALRHLIAADSRDVPPTLVSWVGAATRYLLLVKGVQTNGRISKIEADVLNHDVEIKVPSAETHHAMINGLRTGVATALGCLFWLSTGWSSGGICMMMIAVVTSLAMRLPNPKMVGMDFLYGTIYSLPLGALMFMFILPSTQQSILLLCLSLGAMTFFLGVEVQKRRLGSLGALISTINVLLLNNPMTFNISLFLDNAIGQIIGCFVALMVILLIRDNTKSHTGRTLLNRFVYGAVSALTTDTTRRKENHLPALYQQLFLLLNRFPDDMAKYRLALWMIIMHQRLRTLDIPQNAALSAFHRQIRATAEQVILARRDTTRSRYFTQLLEELERYQQILTEQQLPPNVTVPVGRLTGILRDYQHALSD", "text": "FUNCTION: Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic acid exporter ArAE (TC 2.A.85) family."}
{"protein": "MAIFSVYVVNKAGGLIYQLDSYAPRAEAEKTFSYPLDLLLKLHDERVLVAFGQRDGIRVGHAVLAINGMDVNGRYTADGKEVLEYLGNPANYPVSIRFGRPRLTSNEKLMLASMFHSLFAIGSQLSPEQGSSGIEMLETDTFKLHCYQTLTGIKFVVLADPRQAGIDSLLRKIYEIYSDFALKNPFYSLEMPIRCELFDQNLKLALEVAEKAGTFGPGS", "text": "FUNCTION: Core component of the TRAPP complexes which has a function of guanine nucleotide exchange factor activity for Rab1 GTPase. Plays a role in vesicular transport from endoplasmic reticulum to Golgi and autophagy (By similarity). May play a role in dendrite postsynaptic membrane trafficking (By similarity). FUNCTION: Core component of the TRAPP complexes which has a function of guanine nucleotide exchange factor activity for Rab1 GTPase (Probable). Plays a role in vesicular transport from endoplasmic reticulum to Golgi and autophagy (PubMed:31794024). May play a role in dendrite postsynaptic membrane trafficking (By similarity). SUBCELLULAR LOCATION: Postsynaptic cell membrane Golgi apparatus membrane Endoplasmic reticulum Vesicle Note=Associated with postsynaptic membranes and in intracellular cisterns and vesicles (Golgi). SIMILARITY: Belongs to the TRAPP small subunits family. TRAPPC4 subfamily."}
{"protein": "MVSKAARRRRAAPRQQQRQQSNRASNQPRRRRARRTRRQQRMAATNNMLKMSAPGLDFLKCAFASPDFSTDPGKGIPDKFQGLVLPKKHCLTQSITFTPGKQTMLLVAPIPGIACLKAEANVGASFSGVPLASVEFPGFDQLFGTSATDTAANVTAFRYASMAAGVYPTSNLMQFAGSIQVYKIPLKQVLNSYSQTVATVPPTNLAQNTIAIDGLEALDALPNNNYSGSFIEGCYSQSVCNEPEFEFHPIMEGYASVPPANVTNAQASMFTNLTFSGARYTGLGDMDAIAILVTTPTGAVNTAVLKVWACVEYRPNPNSTLYEFARESPANDEYALAAYRKIARDIPIAVACKDNATFWERVRSILKSGLNFASTIPGPVGVAATGIKGIIETIGSLWV", "text": "FUNCTION: [Capsid protein alpha]: Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, 240 calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid protein alpha generating capsid protein beta and the membrane-active peptide gamma. FUNCTION: [Membrane-lytic peptide gamma]: Membrane-permeabilizing peptide produced by virus maturation, thereby creating the infectious virion. After endocytosis into the host cell, peptide gamma is probably exposed in endosomes, where it permeabilizes the endosomal membrane, facilitating translocation of viral capsid or RNA into the cytoplasm. Involved in specific recognition and packaging of viral RNA during assembly. SUBCELLULAR LOCATION: [Membrane-lytic peptide gamma]: Virion Note=located inside the capsid. SUBCELLULAR LOCATION: [Capsid protein beta]: Virion. SIMILARITY: Belongs to the peptidase A6 family."}
{"protein": "MSLNSSLGHRKELSNLTEGASDQGGSGVTEFVAIVIITVFVCLGNLVIVITLYRKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLISSASMLTLGIIAVDRYYAVLYPMAYPMKITGNRAVMVLAYIWLHSLIGCLPPLFGWSSVEFDEFKWMCVAAWHREPGYTAFWQIWCALLPFLVMLVCYGFIFRVARVKARKVHCGAVVTVEVGVQRTGRKNSSTSTSSSGSRKSAFQGVVYSANQCKALVTILVVIGAFMVTWGPYMVVITSEALWGKNCVSPTLETWATWLSFTSAICHPLIYGLWNKTVRKELLGMCFGDRYYREPFVQRQRTSRLFSISNRITDLGLSPHLTALMAGEQPLGNSSSTGDTGFSCSQDSGTDVMLLEDYTSDDNPLHGTCPPKRRSSVTFEDEVEQIKEAAKNPILHVKADVHKSLDSYATSLAKAIEAEAKINLFGEEALPGVLLTARTVPGIGFGSRRGSRTLAGQRLQLQSIEEGDVLATEQR", "text": "FUNCTION: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Mainly localizes to primary cilium in a TULP3 and IFT-A complex-dependent manner. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes and is apparently not degraded (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "WIMGHMVNAIAQIDEFVNLGANSIETDVSFDSSANPEYTYHGVPCDCGRTCTKWEHFNEFLKGLRKATTPGDSKYHEKLVLVVFDLKTGSLYDNQASDAGKKLAKSLLQNYWNNGNNGGRAYIVLSIPNLAHYKLITGFKEALTSEGHPELMDKVGYDFSGNDDIGDVANAYKKAGVTGHVWQSDGITNCLLRGLDRVRKAVANRDSSNGYINKVYYWTVDKRQSTRDALDAGVDGIMTNYPDVIADVLNESAYKAKFRIASYDDNPWETFKN", "text": "FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod phospholipase D family. Class II subfamily."}
{"protein": "MNKSIAPATSVVAGNVKFGNALPLSVIAGPCQLESRAHALEVASALKEIATRLGIGLVYKTSFDKANRTSAASARGLGLDAALPIFAEIRDHLGLPVLTDVHENEQCARAAEAVDILQIPAFLCRQTDLLLAAAATGRIVNVKKGQFLAPWDMGNVVSKITHAGNSKVLVTERGVSFGYNTLVSDMRALPIMAKTTGAPVIFDATHSVQQPGGKGTSSGGEREYVPVLARAAVAVGVAGVFIETHPDPDHAPSDGPNMVPLREFEALIKTLMEFDALAKKRSTVGAV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsA family."}
{"protein": "MANTPSQQDQFANKAQAWSARFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLLDLEDVHLNIEKRLVELVGDAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQEDKEGLFDTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRGCDLADLSLAELQAYHPSIEADIHQVLTLEGSVAARKHTGGTAPERVREEAQRVIQETA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "LAAVSVDCSEYPKPTCTMEYRPLCGSDNKTYGNKCNFCNAVVESNGTLTLSHFGKC", "text": "SUBCELLULAR LOCATION: Secreted."}
{"protein": "MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL", "text": "FUNCTION: Glutathione S-transferase that catalyzes the conjugation of glutathione to exogenous and endogenous compounds (PubMed:14709161, PubMed:14742434). Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB) (PubMed:14709161). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the GST superfamily. Kappa family."}
{"protein": "MSQKWGLVHIYASYNNTILHVTDLTGAETIAKVSGGMIVRNQRDESSPYAAMQAAFKIADLMRDKGIDQVHVKVRATGGQKSKNPGPGAQAAIRALSRAGIRIGRIEDATPIPHDGTTPKRKNR", "text": "FUNCTION: Located on the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "MQVRMLGRVDLRETVEAMQAFTAQRTGDTPDVLWVCEHAPHFTQGLAGHADHLLAPGDIPVVATNRGGQVTFHGPGQVVAYPLVDLRRAGYYVKEYVHRVEEAAIRTLAHFGVTGHRVAGAPGIYVRLDDPRSHALLPQRPRKADPLEPAAAVPDFTGLGKIAALGIKVSRHCTYHGVALNVDMDLEPFSRINPCGYAGLPTVDLSTIGVHTTWDEAASVLASQLAIRLAP", "text": "FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LipB family."}
{"protein": "MHSRSCLPPLLLLLLVLLGSGVQGCPSGCQCNQPQTVFCTARQGTTVPRDVPPDTVGLYIFENGITTLDVGCFAGLPGLQLLDLSQNQITSLPGGIFQPLVNLSNLDLTANKLHEISNETFRGLRRLERLYLGKNRIRHIQPGAFDALDRLLELKLPDNELRVLPPLHLPRLLLLDLSHNSIPALEAGILDTANVEALRLAGLGLRQLDEGLFGRLLNLHDLDVSDNQLEHMPSVIQGLRGLTRLRLAGNTRIAQIRPEDLAGLTALQELDVSNLSLQALPSDLSSLFPRLRLLAAARNPFNCLCPLSWFGPWVRENHVVLASPEETRCHFPPKNAGRLLLDLDYADFGCPVTTTTATVPTIRSTIREPTLSTSSQAPTWPSLTEPTTQASTVLSTAPPTMRPAPQPQDCPASICLNGGSCRLGARHHWECLCPEGFIGLYCESPVEQGMKPSSIPDTPRPPPLLPLSIEPVSPTSLRVKLQRYLQGNTVQLRSLRLTYRNLSGPDKRLVTLRLPASLAEYTVTQLRPNATYSICVTPLGAGRTPEGEEACGEANTSQAVRSNHAPVTQAREGNLPLLIAPALAAVLLAVLAAAGAAYCVRRARATSTAQDKGQVGPGTGPLELEGVKAPLEPGSKATEGGGEALSGGPECEVPLMGYPGPSLQGVLPAKHYI", "text": "FUNCTION: May act as an inhibitor of TGF-beta signaling. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS", "text": "FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily."}
{"protein": "MTFTEQLSAAWQRNDSLLCVGLDPDPAKLPLSMTGTGGAIFSFCREIVDATADLVCAFKPQIAYFHSQRAEDQLEQLVEYIHDAHPGVPVILDAKRGDIGSTAEHYAIEAFERYKADAVTVSPYMGFDSMSPYLAYPGKGVIVLCRTSNPGGSDVQFLQVDGKPLYQVVAEAARERWNTNGQMGLVVGATFPNEIAKVRQIVGDMPLLIPGIGAQGGDIEATVKAGRTADGTGMMINSSRAILYASREKDFALAARNVALQTRETINRYRHG", "text": "SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily."}
{"protein": "MMLPADFFVPVSKMMLLALLLSIIICCGGAQRSEPMFTAVTDTVLPQDYDSNPTQLNYGVAITDVDNDGDFEVVVAGYNGPNLVLKYIKEKGHLVNIAVDERSSPYYALRDRQGNAIGVAACDIDGDGREEIYFLNTNNAFSGIATYSDKLFTFRNGRWEDLFSDEVNLRRGVANRFSGRSVACIDRKGSGRYSFYIANYANGNVGPHALIELDETASNLSRGIIVLSNVAAELGLNKYTGGRGIAVGPIVNSAASDIFCDNENGPNFLFQNKGDGTFVDIASSTGVDDVYQHGRGVALADFNRDGKVDIVYGNWNGPHRLFLQMNTNGKVRFRDIATQKFSMPSPIRTVIAADFDNDQELEVFFNNIAYRGPSANRMFRVGRREHADPFMEELNPGDASEPDGRGTGGAVTDFDGDGMLDLILSHGESMAQPLSVFKGKQGLKNNWLRVIPRTKFGAFARGAKVVLYTKKSGAHLRIIDGGSGYLCEMEPVAHFGLGKDEASSLEVTWPDGKIFTRSVAEGEINSVLDIAYPHEDDTVTKPTDIECGQGFSVNENGRCTDTDECIQFPFVCPREKPVCINTYGGYKCRPNRRCSRGFEPNEDGTACVAQVAYFGSYPSSASRSQALFLHCTASLLGLGFYFQIYTL", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
{"protein": "MEKYTVCLCGDCINKKNFLKHCQVIDNNCYIAISNELVDIKFDEYIEHGEFFGEKFYQKSHCIMIDFENILKFNSFMADNKLFTVISHCETPCNYSRFVINYLEYITKNNIINHIKYFLKNDYFNNIRWNCHLREKIFKYSNVSTIRSCLKYLPIEYIGEYFSYSLFRGDNIILDYLVDKIKIYLTSYFTGKKYKGNMFKITNKDKLIDISNIYTRLYNIIYYNKKNENIIEIYNQIINRFQELLESQENINVKKKLIFKHNELKLKLTYNEKVKNRLLGNILVYLNGKPSLIVKQLLMDGVNIHTINRDNGFTFLDYFIKIIIKKKNLDLLDILFEMKLIDQSKLNLILEKSIPPIDFKNDTELEIDKNFIRELSGYGADVDKCFDELIKTAKYYNNNKLVGYLKNLGDDLM", "text": "SIMILARITY: Belongs to the mimivirus L17x/L18x family."}
{"protein": "MSQLPLSGTFTALVTPFTPDGEAVDFDALDALVEAQIAGGVSGLVPCGTTGESPTLSEAETTAVIRRVVEAARGRVPVIAGTGSFSTKKTIEASRAALAAGAAGVMIVMPYYSKPSQDGLREHTLAVARAVPAPIVLYNIPGRTVVDLSAETTERICAAAPNVVAIKDASGNVFRCQELVRRLGDRLTILSGDDALTLAMMALGAQGVISVTSNVLPRETSAVTRRFLAGDLAGARAAHLALLELHGLLFVEPNPAPAKAALAALGRMSAAVRLPLVPAGEATRQQIAEAMRRLEARREAS", "text": "FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family."}
{"protein": "MEVAAPLLCLAAAVLVWGVLWVWGSWERMTRPEQAGLPGGGSRTLLVTAHPDDEAMFFAPTILGLARLRHQLFLLCFSAGNYYNQGEIRKKELLQSCDVLGIPPSNVMIIENRDFPDDPDVRWDPDRAADVLLQHVEANGIKLVVTFDEGGVSGHSNHVALNAAVRTLQAEGKLPKGCSVLTLQSVNLLRKYLCLLDLPCSLLLARDALFVLTQREAAQAQRAMSCHRSQLLWFRRLYMLFSRYMRINSLNFL", "text": "FUNCTION: Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PIGL family."}
{"protein": "MLYQWLYSMADEFSPLNVFRYITVRTFIAFFTAFLLCWIWGPHFIKRLQLKHFGQAIRDDGPQTHKKKAGTPTMGGGLILLSTLIPCLLWVDMMNPLVWGVLIVTWGFGLIGYMDDWLKVSKKNSKGLSGKIRLAGEFLISGLVVAALVHFHGLSTAVTIPFMKSVSIDLGYFYVIFAALVVVGTANAVNLTDGLDGLAIVPVMISAATLGLFAYVTGHFSIANYLQIPHVVGAGELSIVAATIVAAGMGFLWFNAYPAQVFMGDVGSLSLGGFLGSMAVITQNELLMLVLGGVFVVEALSVITQVISFKMTGKRVFKMAPIHHHFELGGLTETKIIVRFWIISILLAVLSLATLKLR", "text": "FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily."}
{"protein": "MEVERVQDISSSSLLTEAIPLEFIRSEKEQPAITTFRGPTPAIPVVDLSDPDEESVRRAVVKASEEWGLFQVVNHGIPTELIRRLQDVGRKFFELPSSEKESVAKPEDSKDIEGYGTKLQKDPEGKKAWVDHLFHRIWPPSCVNYRFWPKNPPEYREVNEEYAVHVKKLSETLLGILSDGLGLKRDALKEGLGGEMAEYMMKINYYPPCPRPDLALGVPAHTDLSGITLLVPNEVPGLQVFKDDHWFDAEYIPSAVIVHIGDQILRLSNGRYKNVLHRTTVDKEKTRMSWPVFLEPPREKIVGPLPELTGDDNPPKFKPFAFKDYSYRKLNKLPLD", "text": "FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin. In vitro catalyzes the oxidation of both enantiomers of naringenin to give both cis- and trans-dihydrokaempferol. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MTQSQVTPNAREALTETIVDAKVRKNLTFEAINEGTGLSLAYTTAALLGQHALPEKAAKLVAERLGLDDDAVRLLQTIPVRGSIPGGVPTDPTVYRFYEMVQVYGSTLKALVHEKFGDGIISAINFKLDIQKVPDPEGGERAVITLNGKYLPTKPF", "text": "FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. SIMILARITY: Belongs to the cyanase family."}
{"protein": "MKALSILGSTGSIGLSTLDVVRQHPGKFTITGLAEGHDVGLLNEQINEFRPDVVSVRDAASADQLRKLLGTHKPEIFYGIEGAATVAAAEGAEMVVSAIVGAAGLVPTVSAIKAGKHIALANKETLVVAGQLVSDLVKKHNVQLLPVDSEHSAIFQSLAGHRTEDIERIILTASGGPFRKTPAEELKLAGPEQALKHPQWTMGAKITIDSATLMNKGLEVIEAHWLFNMPAEKIGVVVHPQSIIHSMVEYIDGCVMAQMGVPDMRAPIAYALAWPERCGTGIGKLDLAKIGTLTFEEPDMERFPALRLAFDALKAGRTYPAVLNAANEIAVAAFLDKKIGFTDIADTVDKTMQAHEAYAPVELDEYLQADRWAREKAREIIG", "text": "FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP). SIMILARITY: Belongs to the DXR family."}
{"protein": "MQPALAPAPHPSMQTSAQDHADQVLHDSLLAAQHLSQHPQQPRPQQPNAQPHHLQPTATTSPRDQNNIDPAISGGAMLPPSQPPAQPEPTVEDETPKTYGKRPLSTSKRAAQNRAAQRAFRQRKESYIRKLEEQVKEYEVMSQEYKALQAENYQLREYVINLQSRLLDSQGEVPELPGNIDLNQPRTEISVPQPAPRPGQAGASAPPQGSPQSQVSIANDDMNSLNRIAEAGLGMRKHPNEEAFLSNNFQARRGRGDETADPSETKTEPPTHGLPMVS", "text": "FUNCTION: Putative transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MTERQIYTVSAEIAGRTLTLEAGRFAEQADGAVVARYGDTMLLATVVCAKEAREGTDFFPLTVDYEEKMYAVGKIPANFFKREGRPTTTAILISRLTDRPLRPLFPKGFYNEVQVIITTFSIDMENDPGPLAIIAASAALAISDIPFAGPVGAVQMGHLDGKLVVNPKMGEIEKSRLDLVVAGTKDAVLMVEAGAYELSEDEMLQAVIEGHAVCKQICELQEQLVQLCGKPKRPFTPPVVDTSLEEAISAWMGDRLRKAVRSPVKQEREAQTEALKAEVIAHFTADEPEEEIPNRTKEVSKAFEKLLKDEVRNAILDEGIRVDGRALDEIRPISIEVGVVPRVHGSALFTRGQTQVLTIATLGSPGDEQKVDDLGIETTKRYIHHYNFPPFSTGEIRRLGTPRRRDIGHGALAERSLYAVLPSEEEFPYTIRLVSEVLSSNGSSSMASVCGSSLSLMDAGVPIKAPVAGVAMGLITGEDGRWRVLTDIQGIEDALGDMDFKVAGTANGVTGLQMDIKTTGITYEIMRQAFAQARAGRLFILEKMNAVISAPRPELSIYAPRIMTIQIPVDKIGALIGPGGKTIRNICDTTGAQIDIEDDGRVFITAPDGEAAKKAISMIEGLTREAKVGDIFLGKVVSIKPFGAFVNILPGKDGMVHVSELDEKRVENVEDVVSLGDEINVMVIDIDRNTGKISLSRRAVLTGETPEARKAAGAAPRPRPREEQRGGREEPRSLREELRGPRRDGERPRPRRRDD", "text": "FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase family."}
{"protein": "MSTIPSEIINWTILNEIISMDDDDSDFSKGLIIQFIDQAQTTFAQMQRQLDGEKNLTELDNLGHFLKGSSAALGLQRIAWVCERIQNLGRKMEHFFPNKTELVNTLSDKSIINGINIDEDDEEIKIQVDDKDENSIYLILIAKALNQSRLEFKLARIELSKYYNTNL", "text": "FUNCTION: Phosphorelay intermediate protein that is part of the branched SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound osmosensing histidine kinase SLN1 to two distinct response regulator proteins, SSK1 in the cytoplasm, and transcription factor SKN7 in the nucleus. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes constitutively to the cytoplasm and the nucleus, independent on osmotic conditions and phosphorylation status of the protein. SIMILARITY: Belongs to the YPD1 family."}
{"protein": "MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ", "text": "FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. Also serves as the primary chemoreceptor for chemotaxis. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family."}
{"protein": "MNLVVLLILTLLLFIVSYVVDAGQVILVDSNITRSFVDMEADFSPSVTTVETGVVYVAEPLNACRNLRNKPEQSPYGTSPLVLIIRGGCSFEYKVRNAQRSGFKAAIVYDNVDRNFLSAMGGDSDGIKIQAVFVMKRAGEMLKKYAGSEEMEVMLVPPNTEDSVWSLYASIALILSLAIFCVMVTCVFFYRYCSTIRNSTSQFNGMCRRTVKAMPSVTFTCAKIDNTTGFSCAICLEDYIVGDKLRVLPCSHKFHVACVDSWLISWRTFCPVCKRDARTTADEPLATESTPFLSSSIATSSLVCIDSPPLGSSVSFSPAHVSSSFIHQFVRSSPMNGSRISENLRRQASPLQSSSQRSHLSMKSSHSLGYSTMSPLNAMGMSPYRPYPSNASPGLFSSTNHLLSNYTANTFSHFASAHSLPD", "text": "FUNCTION: Involved in the trafficking of vacuolar proteins. May function as a sorting receptor for protein trafficking to the protein storage vacuole (PSV) (By similarity). SUBCELLULAR LOCATION: Prevacuolar compartment membrane Protein storage vacuole membrane; Single-pass type I membrane protein."}
{"protein": "MSAAEGPLVVGVDTSTQSTKALVVDAATGRVVASGQAPHTVSSGTGRESDPRQWWDALGEALSQCGEAAREAAAVSVGGQQHGLVTLDARGEPVRPALLWNDVRSAPQARRLIDELGGAKAWAERTGSVPSASFTVTKWAWLTEHEPEAARAVKAVRLPHDYLTERLTGEGTTDRGDVSGTGWWASGTEAYDEEILARVALDPALLPRVVRPGEVAGTVRDGHGLPFSKGTLVAAGTGDNAAAALGLGLRPGVPVMSLGTSGTAYAVSQRRPADPTGTVAGFADARGDWLPLACTLNCTLAVDRVASLLGLDREAVEPGTDVTLLPFLDGERTPNLPHSSGLLHGLRHDTTAGQLLQAAYDGAVHSLLGALDLVLDADADPSAPLLLIGGGARGTAWQQTVRRLSGRPVQIPEARELVALGAAAQAAGLLTGEDAAAVARRWNTAAGPVLDAVERDEATLNRITGVLSDAAPLLERDAASR", "text": "FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5- phosphate. SIMILARITY: Belongs to the FGGY kinase family."}
{"protein": "MSSLLLFNDKSRALQADIVAVQSQVVYGSVGNSIAVPAIKQNGLNVFAVPTVLLSNTPHYDTFYGGAIPDEWFSGYLRALHERDALRQLRAVTTGYMGTASQIKILAEWLTALRKDHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQYLLPLAQGITPNIFELEILTGKNCRDLDSAIAAAKSLLSDTLKWVVITSASGNEENQEMQVVVVSADSVNVISHSRVKTDLKGTGDLFCAQLISGLLKGKALNDAVHRSGLRVLEVMRYTQQHESDELILPPLAEA", "text": "FUNCTION: B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP. SIMILARITY: Belongs to the pyridoxine kinase family. PdxK subfamily."}
{"protein": "MSQNKACDLCRLKKIKCSRGQPRCQTCTLFQADCHYSNRARRKRLVQRSKETFGGITLPVFDYAAGINGNEPEPSDHSIPNQENFALTTNGTISKNIEKPEDGEESVQRRLKLLEEKIDLLLDIATETSEFKRENKAIELPSLVTQIKDAESIVIKHRQGSPVDNTPTRILNVESLFPPQLPDWEKAFHDIPKKEVAHELVTSYFQHVNWWWPTFVYNDFMYEFERLYAFGFHSNNAWLISFYSILALSSIRKRLGNSKTLAESLFSTAWVFVQKSDFFLTPSIDKVQALIVMTQYAAYLSSSSLCRTLCGQACLMAQQLNLHRKQSTDVEPEKAESWKRIFWMCYILDKNISLIFGTPSVFNDKDIDCNLPDSKYELLFGVQSGGDLIFVPTVSLTIIQSEIRNRLYSVKSPTQMAAREKIIIPIHQKLKAWEENLPSEIKMYHEMLLNNTFSPTISLSDRFEFLTFAGMEVYFSYLNTLIILHRPSSSTENRRICINAAREAVQLLKNRLNIDLRVNVKADPLWIFLYCPFTPFLIIFNNLVHETDTETDSETLLNDLDLLHVIYDFFMEMEPVSDVALELVKIADKLLRVAKEVCSAKNNDVTDSTFKDIVEGFELNDLNSWDFDRVTNVMRNL", "text": "SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSNFTAKVPLSERMADVLISKDRWKDDEEGYLKVKYGLEIILINVMKFAIVYGIALVTGLLLQTVTVHLSYLWLRRYSFGLHATKTLNCTLISLTMFVLAPFIFQNIPSNNWIVLGTFAFILLNMFLFAPADTESLPLIGEEHRKKLKRKAMIGTLILTGIALLIPFAEMKTLIMVGSLFQVISINPLTYKLLKRRYRNYEKYE", "text": "FUNCTION: May be involved in the proteolytic processing of a quorum sensing system signal molecule precursor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AgrB family."}
{"protein": "MPVQLTTALRVVGTSLFALVVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGRPLKLHCSQRPRSVALCIAAYQEDPEYLRKCLRSAQRIAFPNLKVVMVVDGNRQEDTYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMERVRAVVWASTFSCIMQKWGGKREVMYTAFKALGNSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIGLIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCGKKPEQYSLAFAEV", "text": "FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of three isoenzymes responsible for cellular hyaluronan synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Cytoplasmic vesicle Note=Travels through endoplasmic reticulum (ER), Golgi, plasma membrane, and endocytic vesicles (PubMed:16014622). Actives only when present in plasma membrane (PubMed:16014622). O-GlcNAcylation controls its membrane localization (By similarity). A rapid recycling of HAS3 between plasma membrane and endosomes is controlled by the cytosolic levels of UDP-GlcUA and UDP- GlcNAc (By similarity). SIMILARITY: Belongs to the NodC/HAS family."}
{"protein": "MPNPLYRQHIISISDLSREQLECLLQTALKLKAHPRGDLLEGKLIGSCFFEPSTRTRLSFETAVQCLGGKVIGFSDGANTSAKKGETLADTARIISGYTDAIIQRHPKDGAARVAAEFSRVPVINAGDGTNQHPSQTLLDLVTIYETQGRLDKLKIAMAGDLKYGRTVHSLCQALKRWGCEFAFVSPPSLAMPDYITEELDEAGCRYRILGSLEEAAEWADILYMTRVQRERFDEQEFAKIQGKFNLEASMLARAKPNLRVLHPLPRVDEIHPDVDATPHAYYFEQATNGVYARMAILSLVLNEEV", "text": "SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."}
{"protein": "MKKKDRDSVFHRNIEIFITILINVVILKSFLLISSWVILVLLLVINDLPMYCYHHSLTYFLGCSKQTYFHRLGYPMQKLRHLLYFYYCYFLPRWKPRRRLTYHRYHPK", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MEKMHITNQEHDAFVKSHPNGDLLQLTKWAETKKLTGWYARRIAVGRDGEVQGVAQLLFKKVPKLPYTLCYISRGFVVDYSNKEALNALLDSAKEIAKAEKAYAIKIDPDVEVDKGTDALQNLKALGFKHKGFKEGLSKDYIQPRMTMITPIDKNDDELLNSFERRNRSKVRLALKRGTTVERSDREGLKTFAELMKITGERDGFLTRDISYFENIYDALHEDGDAELFLVKLDPKENIAKVNQELNELHAEIAKWQQKMKTSEKQAKKAQNMINDAQNKIAKNEDLKRDLEALEKEHPEGIYLSGALLMFAGSKSYYLYGASSNEFRDFLPNHHMQYTMMKYAREHGATTYDFGGTDNDPDKDSEHYGLWAFKKVWGTYLSEKIGEFDYVLNQPLYQLIEQVKPRLTKAKIKISRKLKRK", "text": "FUNCTION: Catalyzes the incorporation of the first glycine of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. This glycine is added to the epsilon-amino group of the L-lysine of the membrane-bound lipid II intermediate (GlcNAc-(beta-1,4)-N-acetylmuramic acid(-L-Ala-D-iGln-L-Lys-D-Ala-D- Ala)-pyrophosphoryl-undecaprenol), using glycyl-tRNA(Gly) as donor, in a ribosome-independent mechanism. Involved in methicillin resistance (By similarity). FUNCTION: Catalyzes the incorporation of the first glycine of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. This glycine is added to the epsilon-amino group of the L-lysine of the membrane-bound lipid II intermediate (GlcNAc-(beta-1,4)-N-acetylmuramic acid(-L-Ala-D-iGln-L-Lys-D-Ala-D- Ala)-pyrophosphoryl-undecaprenol), using glycyl-tRNA(Gly) as donor, in a ribosome-independent mechanism. Involved in methicillin resistance. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FemABX family."}
{"protein": "MKSYEVNFDGLVGPTHNYGGLSYGNVASQSNSQQGSNPREAALQGLAKMKALMEMGFQQGVLAPQERPDVAALRNLGFAGTDAQVIQQAAKQAMPLLVASCSASSMWVANAATVSPSADTADGRVHFTAANLNCKYHRSIEHPTTSRVLGAMFADQKHFAHHAALPAVAQFGDEGAANHTRFCRDYGQAGVEFFVFGRSAFDTRYPAPQKYPARQTLEASQAVARLHGLSEEGVVYAQQNPSVIDQGVFHNDVIAVGNGEVLFYHEDAFLETDKMLAELQGKLGKRGGNFQSICVPRSQVTVEDAVRSYLFNSQLLSRADGSMLLIVPEECRGNERVWQYLQSLTSSGGLIREVKVFDLKQSMQNGGGPACLRLRVALKETELAAVNPGVIMTAPLYDTLTQWVGKHYRDRLSESDLADPQLLLECRTALDELTQILKLGAVYPFQIN", "text": "FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)- succinylornithine, ammonia and CO(2). SIMILARITY: Belongs to the succinylarginine dihydrolase family."}
{"protein": "MYHLGDEYSQKAKREGYLARSVYKLIEINEKFSLFSSGNVLDIGASPGSFSQYAYKKLKRGVLVSVDINDISLRYVNNFYFIKGDIFSDDTASKINKFGPYSLVISDVAPKTTGNRLVDTSNSFNLNMRIIDLSFEVLLKKGNLLVKVFQGGDEMQIFKKFEKYFKFVKKIRPKAVRKNSFEIYFLGKSFGK", "text": "FUNCTION: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family."}
{"protein": "MQTLAQNLTSQGVDASLTQLIHTLANTSKEISHAVRHGALAGVLGATEQENVQGETQKKLDVITNDMLKDALKADNTVRGLASEEEDYIVEVGDKGEYLVCFDPLDGSSNIDINSLVGTIFSVLPAPTGELTESSFLQAGRKQVAAGYVLYGPSTMLALTTGKGVQLFTLNPETNEYLLTTEAMSISKDTGEFAINMSNQRFWEAPMQTYISDLLLGTIGPREKAFNMRWIAAMVGDVHRVLSRGGIFTYPTDNKNPQKPYKLRLMYEANPMSFLVEQAGGIASTGYEAIMDIEPSEIHQRVAVILGSANEVKACLEYHSLDYSEEPAL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family."}
{"protein": "MAGHRLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKDTYDYLKTLAGDVHVVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYHALENNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYKKS", "text": "FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. Retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) (By similarity). Acts also as component of the retriever complex. The retriever complex is an heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrins. In the endosomes, retriever complex drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the VPS29 family."}
{"protein": "MKNNRTFLEKLLEGSEVEWKPLDEVANIVNNARKPVKSSLRVSGNIPYYGANNIQDYVEGYTHEGEFVLIAEDGSASLENYSIQWAVGKFWANNHVHVVNGKEKLNNRFLYHYLTNMNFIPFLAGKERAKLTKAKLQQIPIPIPPLSVQTEIVKILDALTALTSELTSELTSELTSELILRQKQYEYYREKLLNIDEMNKVIELGDVGPVRMCKRILKNQTASSGDIPFYKIGTFGKKPDAYISNELFQEYKQKYSYPKKGDILISASGTIGRTVIFDGENSYFQDSNIVWIDNDETLVLNKYLYHFYKIAKWGIAEGGTIQRLYNDNLKKVKISIPPLKEQHRIVSILDKFETLTNSITEGLPLAIEQSQKRYEYYRELLLNFS", "text": "FUNCTION: A putative specificity subunit for a type I restriction enzyme; the corresponding endonuclease and methylase subunits have multiple frameshifts and are probably not expressed. SIMILARITY: Belongs to the type-I restriction system S methylase family."}
{"protein": "MPSIKIRENEPFEIAIRRFKRACEKAGVLSEVRRREYYEKPTEERKRKAAAAIKRHLKKLSRERFALQNLRKGRPQQ", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family."}
{"protein": "MVIGVLALQGAFIEHQKSLAACGVDSIQVRKPHQLEDIQGLIIPGGESTTMGKLMNQFELFEPIVEKAHNGLPLFGTCAGMIMLAKDIAGSTQPRLGLMDIEVERNAFGRQVESFETELTISELGEAPVRAVFIRAPYIKSVAANVKVLAKYNEKIVLAQQDHYLVAAFHPELTNDVRLHQHFLKMIK", "text": "FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. SIMILARITY: Belongs to the glutaminase PdxT/SNO family."}
{"protein": "MGAMAENLLVLCTILAARMALAAADDWIPATATFYGGNDGSGTMGGACGYGNLYDQGYGLENAALSTALFNDGAACGQCYLIVCDTDKAGRWCKPRGAVTVTATNLCPPNWALPSDGGGWCNPPRRHFDMSQPAWERIGVYRAGIVPVLYRRVRCWRRGGVRFTVGGFDHFELVLVANVAGSGSVAAVSVRGAGTGWLQMSRNWGANWQSLAGLAGQPLSFGVTTTGGQYILFQDVAPAGWKFGQTFSTSKQFDY", "text": "FUNCTION: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily."}
{"protein": "MIKLLYPEFWQKRNIIAYLLLPISLIYQFLGYLRASLARPIMLPAKVICVGNCSVGGTGKTQIVMYLAKLLKARNVSFVIVTKAYGSNLKSATTIHQGHTALEVGDEGVILAKYGAVIATKNIKEIVPLINELKPDIIIVDDFLQNPYFHKDFTIVSVDSQRLFGNGFLIPAGPLRQYPNKALDAADLIFLVSSHQDKIPQILTPYVNKLINAQIVPSNNIDKTKNYFAFSGIGNPERFFATLKNYGLNITGYKIFPDHYNYLQADLENLYSLAKEHNAILVTTRKDHVKFNDLNNNIVCLDVELSINHPDLLNEKIFKKA", "text": "FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). SIMILARITY: Belongs to the LpxK family."}
{"protein": "MIKLEKVSFTYKNRAALCDVNVDINEGEAVAIIGPNGSGKSTFLKVLNGILFPSSGRYVFDNNEINENTLKNNKFLKLFHKRVGFVFQNSDAQLFCSTVFDEVAFGIMQMGLEGEEVDKRVRDCLKLLNIEKLKEEHPYNLSGGEKKRVAIASVLAMNPEVITLDEPMNAIDPKGKRFLKELLIDLNKSGKTIICATHDFEYIEGVFNRAVVFSENHKIIRDDRYENIISDREFLMECNII", "text": "FUNCTION: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MASSQEKAKTGVLRNAAALLDEMQLMGETQGAKKVINSELWHACAGPLVCLPQRGSLVYYFPQGHSEQVAATTRKIPNSRIPNYPNLPSQLLCQVHNITLHADKDTDEVYAQMTLQPVNSETDVFPIPTLGAYTKSKHPTEYFCKNLTASDTSTHGGFSVPRRAAEKLFPQLDYSMQPPNQELIVRDLHDNMWTFRHIYRGQPKRHLLTTGWSLFVGAKRLKAGDSVLFIRDEKSQLLLGVRRATRQQTMLSSSVLSTDSMHIGVLAAAAHAASSGSSFTIYYNPRTSPSPFVIPVARYNKATYMQPSVGMRFAMMFETEESSKRRYTGTVVGISDYDPMRWPNSKWRNLQVEWDEHGYGERPERVSIWDIETPENTLVFPSSTLNSKRQCLPGYGVSVPGMEIGSANMSSFPRAQGNPYGSLQHIPAVGSELAIMLLNQSGQTLGSPLSFHQSSYSSIIQNVKQNYIPPLTVSTSACLTKQESLPSDDAQHQFHMANMQNGDLEGSEVQPVIDSISESKLNATSRDPRNTDSYTSRSTSEQNSKGEPRGKTRRSKKGLPHKTVSEKSDLSSAPSWICDNQQVGLESKLVGCDEQVNCGNIEDSSGALTQGNFVGQPHGHQVEQKGVLSPPKVESSKSPDGGKSVNSFPNQGCFSQFIDGLDWMTQPSYYQDSNVIQPAGVSENIFSSSADIPPSMIADTMETFQASCLSDCLPNSIQEFISSPDLNSLTFLSPDMQNLEVQLQHDGSNLPSTSNSFVQMSFSEESASQSANLSGLHMESTHRSINTTSCSQPMSTGGFDAGMYSKLPRLKESQILSLPEIHTNSMGTSACSMDATEYSLDRSAKPMKPPVRTYTKVQKQGSVGRSIDVTGFRNYHELRSAIACMFGLQGKLEHPGSSEWKLVYVDYENDVLLVGDDPWEEFINCVRCIRILSPSEVQQMSENGMHVLNDCIQAA", "text": "FUNCTION: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARF family."}
{"protein": "MNAPQENQASQDDADVLIIGAGPVGLTLANTLGMAGVRVIVAEKLPRIIDYPRAIGIDDESLRTLQAAGLSDQVQAHITPHHWMRFYTASGQCFASIEPRTDEYGWSRRNAFIQPQVDDILYRGLQRFDQVQVLLGHELHSFSQDDAGITATLKDADGVERTLRAKYLVASDGGNSLVRRMLNVAFEGRTKPNQWIVVDVRNDPLGTPHIDMHCDPQRPYVSAALPHGIRRFEFMVMPGETEEQLSRPENLAQLMRKVVADPDKVDYIRKRVYTHNARLAAQFRVDRILLAGDAAHIMPVWQGQGYNSGMRDASNLAWKLAMVVKGEARSDLLDSYEQERRDHARSMIHLSEVAGDIFAPESHTAAKVRDTVMLALNAVPPVKQYFAEMRFKPMPRYEQGVVLHHTGTGNQGVRTPFAGLLDRSGNTPLGRLLGLMAEKKESLVGRLVHGLETAASSPVGRMFIQPRVATANGHSGLLDDFVGLNFCILAWGTDPSYGMDEEALNFWQRLGARFIRAMPAGQLLHPTPTRDGVLTVGDEQGRLKDWFSAQGKSVVFVRPDRFVAALASPQEVSAVTRQMARVLHSPLEA", "text": "FUNCTION: Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI). SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family."}
{"protein": "MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNDRPYRITRGDLFYIRAEDKHSYTSVNDLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLKRHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQSD", "text": "FUNCTION: Activates expression of the rhaSR operon in response to L- rhamnose. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MQATIFSPRATLFPCKPLLPSHNVNSRRPSIISCSAQSVTADPSPPITDTNKLNKYSSRITEPKSQGGSQAILHGVGLSDDDLLKPQIGISSVWYEGNTCNMHLLKLSEAVKEGVENAGMVGFRFNTIGVSDAISMGTRGMCFSLQSRDLIADSIETVMSAQWYDGNISIPGCDKNMPGTIMAMGRLNRPGIMVYGGTIKPGHFQDKTYDIVSAFQSYGEFVSGSISDEQRKTVLHHSCPGAGACGGMYTANTMASAIEAMGMSLPYSSSIPAEDPLKLDECRLAGKYLLELLKMDLKPRDIITPKSLRNAMVSVMALGGSTNAVLHLIAIARSVGLELTLDDFQKVSDAVPFLADLKPSGKYVMEDIHKIGGTPAVLRYLLELGLMDGDCMTVTGQTLAQNLENVPSLTEGQEIIRPLSNPIKETGHIQILRGDLAPDGSVAKITGKEGLYFSGPALVFEGEESMLAAISADPMSFKGTVVVIRGEGPKGGPGMPEMLTPTSAIMGAGLGKECALLTDGRFSGGSHGFVVGHICPEAQEGGPIGLIKNGDIITIDIGKKRIDTQVSPEEMNDRRKKWTAPAYKVNRGVLYKYIKNVQSASDGCVTDE", "text": "FUNCTION: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the IlvD/Edd family."}
{"protein": "MTMCSGARLALLVYGILMHSSVYGSPAASGLRFPGIRPENEAYDEDGNPQQDFYDSEPPGVGSPASALRDAYALYYPAEERDVAHGILDKAYRKVLDQLSARRYLQTLMAKGLGGTPGGGADDDSEPLSKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIPYL", "text": "FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family."}
{"protein": "MAKEELIEFEGVVSEALPDNRFRVQLENGVEVWAYASGKMQKHRIRILAGDRVKLEMSPYDLTKGRINYRHK", "text": "FUNCTION: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IF-1 family."}
{"protein": "MSSDISNNDHLVLSDNPDHPANLIPSLCAKFWTLGWVTGTGGGCSIRENDLVYIAPSGVQKELMKAADIYVLSLAAQTASLRDRVYLRSPPCYKPSQCTPLFLAAFTKRRAGCCIHTHSQWAVLVTLILEAGGGPGGAEDAREFRINNIEQIKGFGKGFEKSGNLGYHDTLRIPVIENTAHEEDLTEFLEEAMDKYPDTYAVLVRRHGVYVWGDNVHKAKTQCESLDYLFQLAVEMKKMSLPWITDITPVKTRRS", "text": "FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily."}
{"protein": "MFWKFDLHSSSHIDTLLEREDVTLKELMDEEDVLQECKAQNRKLIEFLLKAECLEDLVSFIIEEPPQDMDEKIRYKYPNISCELLTSDVSQMNDRLGEDESLLMKLYSFLLNESPLNPLLASFFSKVLSILISRKPEQIVDFLKKKRDFVDLIIKHIGTSAIMDLLLRLLTCIEPPQPRQDVLNWLNEERIIQRLVEIVHPSQEEDRHSNASQSLCEIVRLSRDQMLQVQNSTEPDPLLATLEKQEIIEQLLSNIFHKEKNESAIVSAIQILLTLLETRRPTFEGHIEICPPGMSHSACSVNKSVLEAIRGRLGSFHELLLEPPKKSVMKTTWGILDPPVGNTRLNVIRLISSLLQTNTSSINGDLMELNSIGVILDMFFKYTWNNFLHTQVEICIALILASPFENAENGTITDQDSTGDNLLLKHLFQKCQLIERILEAWDTNEKKQAEGGRRHGYMGHLTRIANCIVHSTDKGPNSALVQQLIKDLPDEVRERWETFCTNSLGETNKRNTVDLAFSDYQMQQMTSNFIDQFGFNDEKFADQDDIGNVSFDRVSDINFTLNTNESGNIALFEACCKERIQQFDDGGSDEEDIWEEKHIAFTPESQRRSSSGSTDSEESTDSEEEDGAKQDLFESSSANTEDKMEVDLNEPPTWSANFDVPMETTHGAPLDSVGSDVWSTEEPMPTKETGWASFSEFTSSLSTKESLRSNSPVEMETSTESVDPLTPGAAALATQPEAPGSMAMEASSDGEEDAESTDKVTETVMNGGMKETLSLTVDAKTETAVFKSEEEKLSTSQDAACKDAEETPEPAEAKCTAPLTPSSSPEQRTDQPSMPSDPSVNGPV", "text": "FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the SAPS family."}
{"protein": "MEKRTSYCGELNEAHIGQSVVLHGWVQKRRDLGGLIFIDLRDREGIVQVVFNPEFSKEALEIADSVRNEFVVTIKGTVHARGEKAINDKLATGKVEVLAEEITILNTSKTPPFYIEDGVNVSDELRLKYRYLDLRRPEMNNIFKMRHTVTRTFRNKLDALGFFDIETPYLTKSTPEGARDYLVPSRVYPGNFYALPQSPQILKQLLMTAGFDKYYQIVRCFRDEDLRGDRQPEFTQIDLETSFLTKEEIQAITEDMLVDVVKEAKNITIDKPFPRMTYKEAMDRFGSDKPDIRFGLELVNVSDVVKDVDFKVFQSAIENGGEVKAINAKAAAANFSRKDLDALGVFVANYGAKGLAWLKVEAGELKGPIAKFFPEEKATELKASLQAEDGDLLLFAADKADIVAASLGALRNKLGKELNLINEEELAFLWVTDWPLFEYDEEAGRYVSAHHPFTLPKEEDIPLLETDSSKVMAEAYDIVLNGYEIGGGSLRIYKKEVQESMFRALGFTDESAKEQFGFLMDALEYGTPPHGGIALGLDRIVMILAGRNNLRDTIAFPKTGSAVDPLTNAPGEVSEAQLAELKLETVKKETN", "text": "FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily."}
{"protein": "MALLSPLLSLSSVPPITSIAVSSSSFPIKLQNVSVALLPSFGQRLVAHGPVIAQKRGTVVAMVSAAAEETAGEDGDQSKVEEANISVQNLPLESKLQLKLEQKIKMKMAKKIRLRRNRLMRKRKLRKRGAWPPSKMKKLKNV", "text": "FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cL37 family."}
{"protein": "GDLPVCGETCFGGTCNTPGCVCAWPVCTR", "text": "FUNCTION: Probably participates in a plant defense mechanism. SIMILARITY: Belongs to the cyclotide family. Moebius subfamily."}
{"protein": "MSNVKKVVLAYSGGLDTSAIVPWLKENYGCEVVAFVADVGQGAEELEGVEEKAKASGASECHVVDLKDEFVKNYVYPTLKTGAIYEGTYLLGTAMARPIIAKAQVEVARKVGADALSHGCTGKGNDQVRFESCYAALAPDLQVIAPWREWELSSRESLLGYLAERNIPCSASATKIYSRDANAWHISHEGGELEDPWCEPTEKVWTMTASPEQAPDKPEYLCVTVENGEIVAVNNQALSPFECLSVLNDVAAKHGVGRVDIVENRLVGMKSRGCYETPGGTVMMAALQAIDELVLDKVSRSWKTQLSEQFAQLLYDGRWFTPLQQSVMAAAQSLCATASGEVVLKLYKGSVTAVQKRSPHSLYSEDFATFGADEVYNQAHAEGFIRLFSLPSRIAALQKQQKG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily."}
{"protein": "MGAQARRERLAQLVAPILAEAGLDLEGLDITPVGKRRLVRVVVDSDDGVDLERIGEVSQKISTALDEVDVMGQSPYVLEVTSPGVDRPLTEPRHWRRARGRLVHAPLVAGGQVKGRVIDADETGVTFDVDGQSQVYAFSDLGRGKVQVEFRHDDAAD", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family."}
{"protein": "MKRIFVQNRELVVPGTLLAQGPYKNGRGTFREGSRIYSTVIGLVDIKGNTIRVIPLEGPYIPEVGDNVIGKIVDVKFSSWVVDIGAPYLANLKIQDFTDEKIDLLRTDLRKFFDIGDIIYGKVKAITEVNNIDLTTKGMPFNGGPLKGGQIVKITPSRVPRVIGRGGSMINMIKKLTMTRIIVGQNGWIWVNGKNEALEKLAIEAILKIDRESHTKGLTDRIKSLLLSRLQELKEKGVIEEIPELEEEPQEETEVNNNDGETRRT", "text": "FUNCTION: Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Confers strong poly(A) specificity to the exosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RRP4 family."}
{"protein": "MKDRIPFAVNNITCVILLSLFCNAASAVEFNTDVLDAADKKNIDFTRFSEAGYVLPGQYLLDVIVNGQSISPASLQISFVEPALSGDKAEKKLPQACLTSDMVRLMGLTAESLDKVVYWHDGQCADFHGLPGVDIRPDTGAGVLRINMPQAWLEYSDATWLPPSRWDDGIPGLMLDYNLNGTVSRNYQGGDSHQFSYNGTVGGNLGPWRLRADYQGSQEQSRYNGEKTTNRNFTWSRFYLFRAIPRWRANLTLGENNINSDIFRSWSYTGASLESDDRMLPPRLRGYAPQITGIAETNARVVVSQQGRVLYDSMVPAGPFSIQDLDSSVRGRLDVEVIEQNGRKKTFQVDTASVPYLTRPGQVRYKLVSGRSRGYGHETEGPVFATGEASWGLSNQWSLYGGAVLAGDYNALAAGAGWDLGVPGTLSADITQSVARIEGERTFQGKSWRLSYSKRFDNADADITFAGYRFSERNYMTMEQYLNARYRNDYSSREKEMYTVTLNKNVADWNTSFNLQYSRQTYWDIRKTDYYTVSVNRYFNVFGLQGVAVGLSASRSKYLGRDNDSAYLRISVPLGTGTASYSGSMSNDRYVNMAGYTDTFNDGLDSYSLNAGLNSGGGLTSQRQINAYYSHRSPLANLSANIASLQKGYTSFGVSASGGATITGKGAALHAGGMSGGTRLLVDTDGVGGVPVDGGQVVTNRWGTGVVTDISSYYRNTTSVDLKRLPDDVEATRSVVESALTEGAIGYRKFSVLKGKRLFAILRLADGSQPPFGASVTSEKGRELGMVADEGLAWLSGVTPGETLSVNWDGKIQCQVNVPETAISDQQLLLPCTPQK", "text": "FUNCTION: Involved in the export and assembly of pili subunits across the outer membrane. Forms a hexameric ring-shaped pore in the outer bacterial membrane. The 2 nanometer-diameter pore allows the passage of the thin tip fibrillum. As for the rod, it probably unwinds into linear fibers which would therefore be narrow enough to pass through the pore. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
{"protein": "MSRYRGPRFKKIRRLGALPGLTSKRPKAGSDLRNQSRSVKKSQYRIRLEEKQKLRFHYGLTERQLLKYVRIAGKAKGSTGQVLLQLLEMRLDNILFRLGMALTIPQARQLVNHGHILVNGRIVDIPSYRCKPRDIITVKDEQNSRTLVQNLIDSSAPEELPNHLTLHTFQYEGLVNQIIDRKCVGLKINELLVVEYYSRQT", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. FUNCTION: With S5 and S12 plays an important role in translational accuracy. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
{"protein": "MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLPAGTNSKGPPDFSSDEEREPTPVLGSGAAAAGRSRAAVGRKATKKTDKPRQEDKDDLDVTELTNEDLLDQLVKYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTISSSAENTRQNGSNDSDRYSDNEEGKKKEHKKVKSTRDIVPFSELGTTPSGGGFFQGISFPEISTRPPLGSTELQAAKKVHTSKGDLPREPLVATNLPGRGQLQKLASERNLFISCKSSHDRCLEKSSSSSSQPEHSAMLVSTAASPSLIKETTTGYYKDIVENICGREKSGIQPLCPERSHISDQSPLSSKRKALEESESSQLISPPLAQAIRDYVNSLLVQGGVGSLPGTSNSMPPLDVENIQKRIDQSKFQETEFLSPPRKVPRLSEKSVEERDSGSFVAFQNIPGSELMSSFAKTVVSHSLTTLGLEVAKQSQHDKIDASELSFPFHESILKVIEEEWQQVDRQLPSLACKYPVSSREATQILSVPKVDDEILGFISEATPLGGIQAASTESCNQQLDLALCRAYEAAASALQIATHTAFVAKAMQADISQAAQILSSDPSRTHQALGILSKTYDAASYICEAAFDEVKMAAHTMGNATVGRRYLWLKDCKINLASKNKLASTPFKGGTLFGGEVCKVIKKRGNKH", "text": "FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide. FUNCTION: May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Expressed diffusely throughout the nucleus. SIMILARITY: Belongs to the LEM family."}
{"protein": "MATSVQTGKAKQLTLLGFFAITASMVMAVYEYPTFATSGFSLVFFLLLGGILWFIPVGLCAAEMATVDGWEEGGVFAWVSNTLGPRWGFAAISFGYLQIAIGFIPMLYFVLGALSYILKWPALNEDPITKTIAALIILWALALTQFGGTKYTARIAKVGFFAGILLPAFILIALAAIYLHSGAPVAIEMDSKTFFPDFSKVGTLVVFVAFILSYMGVEASATHVNEMSNPGRDYPLAMLLLMVAAICLSSVGGLSIAMVIPGNEINLSAGVMQTFTVLMSHVAPEIEWTVRVISALLLLGVLAEIASWIVGPSRGMYVTAQKNLLPAAFAKMNKNGVPVTLVISQLVITSIALIILTNTGGGNNMSFLIALALTVVIYLCAYFMLFIGYIVLVLKHPDLKRTFNIPGGKGVKLVVAIVGLLTSIMAFIVSFLPPDNIQGDSTDMYVELLVVSFLVVLALPFILYAVHDRKSKANTGVTLEPINSQNAPKGHFFLHPRARSPHYIVMNDKKH", "text": "FUNCTION: Involved in glutaminase-dependent acid resistance. Exchanges extracellular glutamate (Glu) for intracellular gamma-aminobutyric acid (GABA) under acidic conditions. The ability to survive the extremely acidic conditions of the stomach is essential for successful colonization of the host by commensal and pathogenic bacteria. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Glutamate:GABA antiporter (GGA) (TC 2.A.3.7) family."}
{"protein": "MKLKKLYIFYFDIYEYFLCDLQLSETNEILKYIKNNIDKYTNSFNSSYIILKDFNIITNEVELQSYYNFTEDSKIKLNNTDLILFMTPYKIERIYSKYNRNFNQYRWFYILNNIEPAGSYKINMSNLQNINIYDKNKTAYYCKNPKLLFLTPIEIDKFIPVSRVSIDIECQHFGEFPTPNKFPISHICIDWFMESNINPVKKIITLINYEIIKNYKGEQKDRFIYTEIDELLTKDKVYITIYCTEKYMLHFILYTLRKDFDYILTYNGHSFDFTYIQGRRKFYNLNELCLVNAHKSNELKIYSYNKDTTYEIDSNNGIIFLDLYNYIKKIYNYNSYKLGEIAKERFNILSKIIDNGDEYIIMPLDTADNKNKVSIFYDVIRTANYCFINNIPYKIKDKTKIINDKEKLYDPISIENSLYQQFKIYKNNTPISDETTKVMLSKDDVDIGNKNAYVNFTKDKSDDIAYYCTHDTVLCNCIFKYDMIHDKVIAFSNEYLLPQYMSFKYKSTTNISGLLLKTLFCNRSMIVSGNLEFEKFEGGYVLEPKQKYIDSITAVFDFNSEYPSNIIEANLSPEKVEKVIKLQDDEYAVDIVENYLKEKYPYPDYCYMLIKKDKTYKFIVMDRRKPGIITQMIDKGMKSKNEYKNLKNINKNNPVLYNYYTSALYSKKITINSLYGLLGSERFDFNSPYCAEYCTALGQKCIKYIKNLVDKSRYIDNNLYLNEQNNPFSNEPVITRYSGNLDVNFTFYIIYGDTDSLFINIKFDNKFDNKEDLVNKSHECFQFLSNIINDEKNIILSKNFNFEYEKMYIWMLLLAKKKYIGEVVSSMNPLQLISDSKGTALIRRDCTEIHKTILKNTIDILKEYLTNNCTIQDVNNKINNYLMFTFKNIIENIQNLDINEFKKSVKYTGIYKDPNFYIELCVKKYNSKNPNDKIVKGQRFDFIYAHEIDIWDIETKKWNTKYTS", "text": "FUNCTION: Catalyzes DNA synthesis. SIMILARITY: Belongs to the DNA polymerase type-B family."}
{"protein": "MKFDVCVPILGFENVKEVTLEKIDDAFMRMESSNDEHISFTLINPFALREYDFEIPDATQKLLEIDEKSNILILNIAIIQTPVEDTVVNFIGPMIFNTDNNKAAQLVLSESTKYGVAEKISLYLKK", "text": "FUNCTION: Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FliW family."}
{"protein": "MVSVKKIVASALVGVLMFSAVGCNMVEKTQAAIDKTTVATVNGEKITLGEVDSHLKGVFAQMKSQYGDKYMDDPQVAQQILQQRQSVVQGLVTDKVLGIEADKLGIKPSEEEIKKKVDEQFENIKKGMGDNFDKALEAEGYTEDTFKDVIKNQVINQAVQDYIIKDVKVTDEDAQKYYDENKQQFVAKDSGVLTKHLLFENEEEAQKAYDEIQSGKTTFNDLFTKYQNNKSENKKPIAENLGVVPAENSGLVQEFVDGLKPLKEGEISKPIKTQFGYHIIQAGATYEKGAQLPFDEVKSQIIQILKQQKDSEKFKADMDQWKKDLNVKVYDDKLQEGLKISK", "text": "FUNCTION: Plays a major role in protein secretion by helping the post- translocational extracellular folding of several secreted proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the PrsA family."}
{"protein": "MATAVGMNIQLLLEAADYLERREREAEHGYASMLPYSKDRDAFKRRNKPKKNSTSSRSTHNEMEKNRRAHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRRLEKLGAERTRMDSVGSVVSSERSDSDREELDVDVDVDVDVDVEGTDYLNGDLGWSSSVSDSDERGSMQSLGSDEGYSSATVKRAKLQDGHKAGLGL", "text": "FUNCTION: Component of a transcriptional repressor complex together with MAX (By similarity). In complex with MAX binds to the core DNA sequence 5'-CAC[GA]TG-3' (By similarity). Antagonizes MYC transcriptional activity by competing with MYC for MAX binding (By similarity). Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MYKVALFDLDGTLINSEHKNREAWARLFRRHGVPYDDSVLRSFTGRPAKEAMADHVASFAGHSVDELCAEVAAYAALPDMPAAVTVDGAMELLHQLQQMRVPLGVVTSGPRDYAESALTTLGALQLLDVLITADDVSRGKPDPEGYSTACSALNVEPSQAIVFEDAPAGILAAKRAGIFCVGLTTTHDAEALAEADVLLKDLTEVRWPHIGPS", "text": "FUNCTION: Involved in the biosynthesis of the antifungal agent validamycin A (PubMed:16725283). Catalyzes the dephosphorylation of validoxylamine A 7'-phosphate to yield validoxylamine A (PubMed:21766819). VldH is also able to convert trehalose 6-phosphate to trehalose (PubMed:21766819). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family."}
{"protein": "MAVDFSMRQLLEAGAHFGHQAHRWNPKMQPYIFGTRNNIHIIDLAQTVPAMHQALQAVSDTVAKGGRVLFVGTKRQAADTIAEAAKRSAQYYVNSRWLGGMLTNWKTISGSISRLRKVTETLETGGPGLTKKERLMLSREKEKLEKALGGIKDMGGVPDLLFVIDTNKEQLAIKEANRLGIPVAAIVDTNCNPDGISYIVPANDDAGRAIALYCDLIAKAAIDGISRAQGSSGMDLGASEEPMAEELPANDDAAVTVESDALDPADVAMLAESTEHFELLAAPRGAPDDLTKLNGAGPQIVQKLNDAGIYHYWQLAAMTPEDVAKVDADLKLNGRIDRDSWVSQARGFVEAAAAA", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MLSIPSPQVLLALFSMTDLDDSTCKKYIKMITNIVILSLIICISLAFWIMSMTASTYYGSLRPVSPWRWLFSVVVSVVISCNGFKKKSLDHSGALGGLVVGFILTIANFSFFTSLLMFFLTSSKLTKWRGEMKKRLDSEYKEGGQRNWVQVFCNGGVPTELALLYMIENGPGEMPIDFAKQHTASWMCLSLLAALASSAGDTWASEVAPVLSKSSPRLITTWEKVPVGTNGGVTAVGLVSSLLGGTFVGLAYFLTQLVFVNDLDISAPQWPLIAFGGLAGLLGSIVDSFLGATMQFSGLDESTGLVVSSPTQETKHISGKPILDNNAVNLFSSVLVALLLPTAASGFWPTV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM19 family."}
{"protein": "MLQTSLTLPAPAKLNLFLHITGRRPDGYHNLQTVFQLLDFGDELTFTPNQSGEITITPAIEGVPLEQNLVYKAANILRSHVNRPELGATIHLTKRLPMGGGIGGGSSDAATTLVGLNYLWQTGVSPTTLAQLGRQLGADVPVFVEGNSAWAEGIGEQLIALDLPQYWYVVLTPACHVSTVEIFSHKDLTRDTLAITVAAFFEKGGKNDCQPLVERLFPQVRDAVDWLNKFGPAKLTGTGASVFAAFPSKDAAQKVFANKPKHLNGFVAQGVNESPLHQRLPEQCITGV", "text": "FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily."}
{"protein": "MAKLTKRMRVIRDKVDVTKQYDINEAVALLKELATAKFVESVDVAVNLGIDARKSDQNVRGATVLPHGTGRSVRVAVFAQGANAEAAKEAGAELVGMDDLADQIKKGEMNFDVVIASPDAMRVVGQLGQILGPRGLMPNPKVGTVTPNVAEAVKNAKAGQVRYRNDKNGIIHTTIGKVDFDSDKLKENLESLVVALKKAKPATAKGIYIKKISLSTTMGAGVAIDQSGLTAVVN", "text": "FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. SIMILARITY: Belongs to the universal ribosomal protein uL1 family."}
{"protein": "MSNGSIPVDEVIEHLRNWNFTWNIILTILLVVLQYGHYKYSVFLYGVKMAILWILWPLVLALSLFDAWASFQVNWVFFAFSILMACITLMLWIMYFVNSIRLWRRTHSWWSFNPETDALLTTSVMGRQVCIPVLGAPTGVTLTLLSGTLLVEGYKVATGVQVSQLPNFVTVAKATTTIVYGRVGRSVNASSGTGWAFYVRSKHGDYSAVSNPSAVLTDSEKVPHLV", "text": "FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Host Golgi apparatus membrane; Multi-pass membrane protein Note=Largely embedded in the lipid bilayer. SIMILARITY: Belongs to the alphacoronaviruses M protein family."}
{"protein": "MLHLYNSLTRKKEPFVSLRPGKIGMYVCGITVYDHCHLGHARSMVAFDVMVRYLRSQGFDVTYVRNITDIDDKIIARASERDVSIDELTAQYIDAMNNDTHALNILPPDHEPRATGHIETIIRLIQRLLEKGNAYVSENGDVCYEVDTFPEYGKLSHKDIEGLVSGSRVEIVKEKRSPLDFVLWKKAKPGEPSWPSPWGEGRPGWHIECSAMAMHELGEQFDIHGGGLDLQFPHHENEIAQSEAATGKPFANYWLHVGMLQVNGEKMAKSIGNFYTIADVLKEHHPEVIRYFLLSSHYRSPLNYSEENLLNAKKALIRLYQAVKDVPPQTADSKLDEYWQEQFNQAMNDDFNTPVALSVLFQLAHEVNKSNSPALAHTLKNLAGILGFLQKDPESFLQSGLAEEEKLVIEQLIAERLKARAERNWTKADQIRADLLSKGIELEDGATGTTWRRIAE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MVEERGSSRSSRGGSWGSGEDGGSSHGGKGVPKLSRTVAKKIHKYDVSADHSDYEDDGSVHSTSSSGSRRNPLSKSIIQQQSFRVGANFEEDLKTLYELIGVSKPADLAISASDWQSRGKSIAYSQPLSSPSLSQEHGEASHSNDLKPSIIDFRSEAPAASPRELPVAPVKLDAHERMTYRSDYVNSQPQNHYGRKNSPSQRSPPPESFPAFDSSPSRLGREGYGLHRMQSDPVMPTLGALSPLGTGNAHPESAGSTATRRWSFDLVPGNHEGDYANMSQVVRDNLPSAAVAMPKNGLVRRSPIIRDPNRSNSSVSNPYAQRQYPNLAEEAESSAKPESSAIPDSSAMPELPAKLESTAVPELSAKPESNAKPESEPEQDSSVEARTEHYGSVRKSKIPSALIIDKFEEPSIVSTGRSPGVVSKRPPWDTWFKGDFIGSGTFGSVYEGIDNNGMFFAVKEVSLKDQGKVGQEAIKQLEHEIALLSDIQHPNIVQYLGTERDDEKLYIFLELVSKGSLASLYKKYYFVYDQVRAYTKQILSGLKYLHDRKIIHRDIKCANILVDTNGVVKLADFGMAKQVDKLGLLKSFMGSAHWMAPEVVNPKRQYNFLADIWSLGCTVLEMATGDAPFGELECHSVLWKVGNGEGPLIPDDLEDEMKDFISKCLEVTVGNRPTCDMLLTHPFITGEPMTGPVKLVPMPELSTISEERSIDVSESPSIATSSQSGSSPSVAGDAVSPASVAVRPRSMRTLRSEFSMSSPESIAS", "text": "FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1a. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily."}
{"protein": "MARLRLTIAYKGTDLHGWQVQEHATRPRPRTVQGVLEPIVSRMAGEQVRLHAAGRTDAGVHADGQVAHVDIPDHKLDVDWQKAINAQLPDDICILDVRRAADDFHARFDALGKRYTYRLWLTRRFIPPKLHGQVWATGPLDVYAMDRAARHLAGTHDFAAFQNQGTDVTSTVRTVHAIRRCPSGTLPAGALLTYGEPYTSWRCTGTHPDQPPATAGHPLAGIGLELVWSFEGDGFLKQMVRNMMGLLVAVGRGALAADDVPGIMATLDRSRAPATAPACGLTLSEVYYPPCDYPYAR", "text": "FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family."}
{"protein": "MKNKLKILQIGSIDWSKEVVIPDNMDWYYFFSLTLRLAIKKVMEMEKINHFSAIIVDDLDLIPDLFLIESRIIPYTIFYSKKQQAIQEPIAFFLKRYCAQQIDLSDRPNLLRKLSKALFRGQYGDKMTPLDMVVSPGFKGRICHNGYENLELEGNFGSDFRPIVSWKYNIVASKKNPVEIWLEYEKDLSCELRLRIYNIQEGSAADLVRESVFSETDMEETIVLDNDFTSFLGITLEARGFGTLKIGAFHQRLTRYQFGKFVLGGKILKDSHRQEINYFFYPGDFKPPLVVYFSGYRRAEGFEGFGMMRGLGCPFLLISDQRLDGGVFYLGSDELEEGIRRIIQEHMELLGFSERELILSGISMGTYGAAYYGADFSPRAIILCKPLANLGTIAQRGRLRLPEVFPMALDILHRHTGGKDRENVMELDNRYWKKFKKADFSRTIFGLAYMKEEDYDPTAYEDLVQYLYPTETQLMSNGLSGRHNDDSTMVINWFMNYHRIILEKEFGRKK", "text": "FUNCTION: Part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon. SIMILARITY: Belongs to the accessory Sec system protein Asp2 family."}
{"protein": "MEVNIYGLTATALFIIIPTSFLLILYVKTASTQD", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbM family."}
{"protein": "MQCALYDAGRCRSCQWITQSVNEQLSAKTADLHRLLAGLPVEQWCAPIGGPEQHFRNKAKMVVSGSVEKPLFGMLHRDGTPVDLCGCPLYPASFAPVFSALKPFIARAGLTPYNVARKRGELKYLLLTESQFDGGMMLRFVLRSETKLTQLRAALPWLRAQLPQLRVITANIQPVHMAIMEGETEIYLTDQQALVERFNDVPLWIRPQSFFQTNPTVASRLYATARDWVGQLPVRHMWDLFCGVGGFGLHCATPQMQLTGIEIAPEAIACAKQSAAELGLTRLHFQALDSTQFAIAQGETPDLVLVNPPRRGIGKPLCDYLAQMAPRFIIYSSCNAQTMAQDIRHLPNYRIQRVQLFDMFPHTAHYEVLALLRRSI", "text": "FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfamily."}
{"protein": "MAQHTIDQTQVIHTKPSALSYKEKTLVMGILNVTPDSFSDGGKYDSLDKALLHAKEMIDDGAHIIDIGGESTRPGAECVSEDEEMSRVIPVIERITKELGVPISVDTYKASVADEAVKAGASIINDIWGAKHDPKMASVAAEHNVPIVLMHNRPERNYNDLLPDMLSDLMESVKIAVEAGVDEKNIILDPGIGFAKTYHDNLAVMNKLEIFSGLGYPVLLATSRKRFIGRVLDLPPEERAEGTGATVCLGIQKGCDIVRVHDVKQIARMAKMMDAMLNKGGVHHG", "text": "FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. SIMILARITY: Belongs to the DHPS family."}
{"protein": "MTRDDALPDSHSAQTFYENYEPKEILGRGVSSVVRRCIHKPTCQEYAVKIIDITGGGSFSSEEVQELREATLKEVDILQKVSGHPNIIQLKDTYETNTFFFLVFDLMKRGELFDYLTEKVTLTEKETRKIMRALLEVICTLHKLNIVHRDLKPENILLDDNMNIKLTDFGFSCQLQPGEKLREVCGTPSYLAPEIIQCSMDDGHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMDGKYQFGSPEWDDYSDTVKDLVSRFLVVQPQDRCSAEEALAHPFFQEYVVEEVRHFSPRGKFKVICLTVLASVKIYYQYRRVKPVTREIVIRDPYALRPLRRLIDAYAFRIYGHWVKKGQQQNRAALFENTPKAVLLSLAEEEDF", "text": "FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
{"protein": "MDSCDFRGLTSRRRTSNLKNYFVGATPLQKRLELVRRQNSDFPSPSRRKIPQCSQLQEDIDPQKVAFLLHKQWTIYSLTPLYKFSYSNLKDYSRLLSAFIVAEKQKGVAVEVGEDFNIKVIFSTLLGVKGTQRDHEAFLVQILSKSQSSREHREDKVLWTGWFCCVFGESLQETVSEDFTCLPLFLANGAESNTSLIRDWFQKTFDCCFSPLAISAFNLSWMAAMWTACKMDRYMATTEFLWSVPCSPQSLDISYAIHPEDAKALWESVHKTPGEVTQEEVDLFMNCLYSHFHRHFKIHLAATRLVRVSTSVASAHTDGKIKVSLNRSN", "text": "FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). SIMILARITY: Belongs to the CENP-L/IML3 family."}
{"protein": "MENCLSTLVFLLSIALVLFPKTGVSFLAAEGASDSDSKVYIVYLGEREHDDPELFTASHHQMLESLLQSKDDAHNSLIYSYQYGFSGFAALLTSSQAKKISEHPEVIHVIPNRILKLKTTRTWDHLGLSPNPTSFSSSSSAKGLLHETNMGSEAIIGVVDTGIWPESKVFNDHGLGPIPQRWRGKCESGEQFNAKIHCNNKLIGAKYYLSGLLAETGGKFNRTIIQDFKSNRDAIGHGTHTATIAGGSFVPNVSFYGLARGTVRGGAPRARIASYKVCWNVVGYDGICTVADMWKAFDDAIHDQVDVLSVSIGAGIPENSEVDSVDFIAAFHAVAKGITVVAAGGNDGPGAQNITNAAPWLLTVAATTLDRSFPTKITLGNNQTLFAESLFTGPEISTSLAFLDSDHNVDVKGKTILEFDSTHPSSIAGRGVVAVILAKKPDDLLARYNSIPYIFTDYEIGTHILQYIRTTRSPTVRISAATTLNGQPAMTKVAEFSSRGPNSVSPAILKPDIAAPGVSILAAVSPLDPDAFNGFGLYSGTSMSTPVVSGIIALLKSLHPNWSPAAMRSALVTTAWRTSPSGEPIFAQGSNKKLADPFDYGGGLVNPDKAAQPGLVYDMGIKDYINYMCSAGYIDSSISRVLGKKTKCTIPKPSILDINLPSITIPNLEKEVTLTRTVTNVGPIKSVYKAVIESPLGITLTVNPTTLVFNSAAKRVLTFSVKAKTSHKVNSGYFFGSLTWTDGVHDVIIPVSVKTTISM", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MHLNTTLLVSLALGAASVLASPAPPAITAPPTAEEIAKRATTCTFSGSNGASSASKSKTSCSTIVLSNVAVPSGTTLDLTKLNDGTHVIFSGETTFGYKEWSGPLISVSGSDLTITGASGHSINGDGSRWWDGEGGNGGKTKPKFFAAHSLTNSVISGLKIVNSPVQVFSVAGSDYLTLKDITIDNSDGDDNGGHNTDAFDIGTSTYVTISGATVYNQDDCVAVNSGENIYFSGGYCSGGHGLSIGSVGGRSDNTVKNVTFVDSTIINSDNGVRIKTNIDTTGSVSDVTYKDITLTSIAKYGIVVQQNYGDTSSTPTTGVPITDFVLDNVHGSVVSSGTNILISCGSGSCSDWTWTDVSVSGGKTSSKCTNVPSGASC", "text": "FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
{"protein": "MKTYSAKPAEVQRDWYLVDATDKTLGRLASEVAHRLRGKHKPVFTPHVDAGDYIVVINADKIRLTGRKERDKQYFWHTGFPGGIKSRSVAEVRERHPERLIESAVRGMMPKNRLGRAMLKKLKVYAGNEHRHHAQQPQPLEL", "text": "FUNCTION: This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. SIMILARITY: Belongs to the universal ribosomal protein uL13 family."}
{"protein": "MQFVQTSTLPQKTDQKFAVQKPIAIWLFVCCALVFAMVVVGGVTRLTDSGLSIVEWQPLVGTVPPLSQNDWDELFEKYHQTPQYKKVNLGMSLEEFKTIFWWEYFHRLLGRVIGLAFFIPFLYFLMKKAVDRPLGLKLSGIFLLGALQGGMGWYMVKSGLVDNPHVSQYRLTAHLGLAFAIYAAMFWVALDLLNPGRGLSANSGLRGLLNFSTMLSALVFIMVLSGGFVAGIRAGLAYNTFPLMDGHFIPPELFMLEPWYRNFFDNMTTVQFDHRLIAWTLAILVPIFWLKSRAVPLSGSARLACTLLLIMLAVQITLGISTLLLVVPLTLAAAHQAGALLLFTAALWVNHELRRQ", "text": "FUNCTION: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the COX15/CtaA family. Type 2 subfamily."}
{"protein": "MIHQPPAGARDLLPLEVVQKAWINDTLQQVFGQWGYQRIVTSTIERLDTLKAGGAIEDETVIQLHNNSREQLGLRPELTASVARAAVTRMANTSYPQRLCYRANVFRNPPSGHHGRQLEFYQAGVELLFSGGTLADAEILLLVAECLQKLQIPSWYLILGDAGLTRSLLSPFPEALRQEVRHCLATLDYVKLDNLSYPNEELKHRASLLFNLRGKPEDVLSKVVDLTLDQTGKHCLNNLKSLIELVNHSTSYKLPLTLDLSLIQTFDYYTGIIFKAIGQTNHKLQNLGQGGRYDQLLGVYHPQKKSAPGIGFSLNVGALHRCLLSTDILPQKPLLIDYLVVAKTSESQIEALKYAQQLRKDDNSLRVTIDLENRNEEEIKKYAQENGIKTIVWIEKGKEAIIN", "text": "FUNCTION: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily."}
{"protein": "MSFVVIIPARFASTRLPGKPLLDINGKPMIVHVLERARESGAERIIVATDHEDVARAVEAAGGEVCMTRADHQSGTERLAEVVEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAAPVHSAEEAFNPNVVKVVLDSEGYALYFSRATIPWDRDRFAKGLETVGDNFLRHLGIYGYRAGFIRRYVNWQPSPLEHIEMLEQLRVLWYGEKIHVAVAEQVPGTGVDTAEDLERVRAEMR", "text": "FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsB family."}
{"protein": "MRIGLTGGIASGKSLVATYLEKQGIPVVDADKLARQVVEPGEPALAQIVATFGEHVLQDDGTLDRKQLGAIIFGDEQKRKQLNEIVHPAVRQSMKKQADLYEQRGYTRVVLDIPLLYESNLFHMVNQVWLVYVDEATQLRRLIERDGLTETEAKQRIAAQMPLTAKKAQADVLIDNNGTKENTYRQVYDALAKTAHE", "text": "FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CoaE family."}
{"protein": "MNDETTPANKNPEKAELRCGWTTGACATAATKAALTALITGEFPDPVGIILPKGEVPYFQLANEGLGEGYAMAGIVKDAGDDPDVTHGATIISTVYPAPPGTGIIFRAGEGVGTVTREGLAIPPGEAAINPVPRRMMTEICEAICAEYGLPADLVITISVPGGEEIAQKTWNPRLGIIGGISILGTTGVVHPFYCSAWIHSIHRGIDVARAAGQKHVLGATGSTSEDAAQALYNLPDFAILDMGDFAGGVLKYLREHPIDRLTIAGGFAKLTKLAQGALDLHSSRSQVDKGFLWQIAERAGAPADMKERILLANTAMEVLELTQSIGIDIAGPIALEARQTALKTLRGAPVEVEIIVTDRKGNILARV", "text": "FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. SIMILARITY: Belongs to the CbiD family."}
{"protein": "MRHRCNVPQLGRPADQRKALLRSLTTEIIRNGTVTTTKARAKAVRSEVERMVTLAKDGSLAARRQALGYIYDKQLVHLLFEQAPERYAKRQGGYTRILRTVRRRGDNAEMAIIELT", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family."}
{"protein": "MIPPHRCLTDPLLQGSWPGYLPPMPKRARRMRLTTWRSPVTAVIAALLAAFLTPAAAHGAPRESAPVYSYENAIRESVWVDTRLDGDGDGKTDRVAVDVVRPRELARQGRKIPVIMDASPYYSCCGRGNESQKKTYDANGDVVRMPLFYDNYFVPRGYAFVGVDLAGTNRSDGCVDVGGRSDIQSAKAVIDWLNGRAHGYTSRTGTARAKATWTNGRTGMIGKSWDGTVANGVAATGVKGLKTIVPISAISSWYDYYFAKGAPLYDSGPDWLSDYVDSPDARTKCAAVQRKLVDEAPRTGDWTSLWTERDYVKDASKVRASVFLVHGMQDLNVRAKNFGQWWSALAKNGVERKIWLSQTGHVDPFDFRRTAWVDTLHRWFDHELLGYDNGVDREPTADIERHPDQWVTSTLWPPRGTDAVTLRPGTGTQAGVGTLGLRTGSGTETFTDDPRLSETDWAAHIDESTASKAGFVTAPLAGDVRLSGSSKVTVTATPTTSTAHLSAVLVDLGPDTIRDYADGGEGITTLTDRTCWGASTAGDSACFKNTRATTAAVDYTVLSRGWADLGNHASARKGVPLTPGKAYTITLDLAATDHVVPKGHRLALIVAGTDKDLIDPPSSTPTLTLDLARTSARVPLVGGAAAFTRATAQSGTAADATVLDGVREPHTAHRVPGGGL", "text": "SIMILARITY: Belongs to the peptidase S15 family."}
{"protein": "MTQMTPREIVHALDQYIIGQQEAKRSVAIALRNRWRRMQLDDSLRGEVVPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGYVGRDVESIIRDLVEMAMKMVREQAKEEVAHKAEDATEERILDALLPRPRGSEYDHARDESSTRQTFRKKLREGQLDDKEIDIEITPQGGGFDISAPPGMEEMTSQLQSMFSNMGKQKSETRRVTVEEARRLLHDEEAAKLVNEEQIKHRAIEAVEQNGIVFLDEIDKVAKRGDSGSGGDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFIASGAFHLSKPSDLIPELQGRLPIRVELQALTPDDFKRILTEPSAALTKQYQALLATDGLEVNFTDEGIARIAEIAWQVNDGTENIGARRLHTVMERLLEEPSFQGGDMASPLTIDAAYVDEQLGELATDEDLSRYIL", "text": "FUNCTION: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily."}
{"protein": "MSEKQSPKTSEAECSAMDLPEFEDEENWLFKVLGFQPGPSSALDDDTDDQADEPLSAAEFLHLQDILQEDRVSSTDDEDTCQAGCTEDDETSHSDRDIDNNVKVITGNIKASPSMYMEMFTDQNPQADQDLEETESDGAMNPTD", "text": "FUNCTION: May have an RNA/DNA binding role."}
{"protein": "MGKDTIADIITSIRNADMNRKGTVRIESTNITESIVKILLREGFIENVRKHRENNQYFLILTLRHRRNKKESYKTILNLKRISRPGLRIYSNSQRIPRILGGIGIVILSTSQGIMTDREARLKRIGGEILCYIW", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS8 family."}
{"protein": "MAPEMDQFYRSTMAIYKSILEQFNPALENLVYLGNNYLRAFHALSEAAEVYFNAIQKIGEQALQSSTSQILGEILVQMSDTQRHLNSDLEVVVQTFHGDLLQHMEKNTKLDMQFIKDSRQHYEMEYRHRAANLEKSMSQLWRMERKRDKNAREMKESVNRLHAQMQAFVSESQRAAELEEKRRYRFLAEKHLLLSNTFLQFFGRARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPVLGPPYPSGRLTPTRLDMPQRALGEFGSPRSRHGSGSYGPEPAEARSASQLEPDHRRSLPRTPSASSLYSSSTQRSRSNSFGERPGGGGGGGGARRVRALVSHSEGANHTLLRFSAGDVVEVLVPEAQNGWLYGKLEGSSSSGWFPEAYVKPLDELPVNPMNPLNPVTSMNPRSPVNELPSRLRSYPLRGSHSLDDLLDRPGNSTASSDYWDGQSRSRTPSHIPSRTPSPAPTPLPSSRRSSMGSMGVASDVKKLASWEQQPPELFPRGTNPFATVKLRPTVTNDRSAPLIR", "text": "FUNCTION: Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cell junction Cytoplasmic vesicle membrane Note=Localizes to RAB13-positive vesicles and to the plasma membrane at intercellular contacts."}
{"protein": "MKSSTQAVLEHTAIPKHIAVIMDGNGRWAKKRFLPRIMGHKRGLDALENMVKHCAKLGVQYLTVFAFSTENWRRPEDEVSFLMGLFLQALQKQVRRLHENNMRLKILGSRERFNRQILKGIEEAEALTANNTGLTLSIAADYGGRWDILQAANKLIAEGVSEITEDTLAKYLMLGDAPEPDLFIRTGGETRISNFLLWQMAYAELYFTDILWPDFDGKALDDAVASFQKRERRFGRTSEQLPIEQQRN", "text": "FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. SIMILARITY: Belongs to the UPP synthase family."}
{"protein": "MSGSGDREILLIAHPGRAEIVETAHRAAKIFTEAGIGLRVLADEAPSTRFDSRAEPAPVTGPAGDAVRVVEHSAAAAVGCEMVLALGGDGTFLRAAELARPASVPVLGINLGRIGFLTEAEAEHLDEALGQVVRGDYRVEDRMTIDVTVRVEDEVVESGWALNEASIENASRMGVLEVVLEVDGRPVSAFGCDGILIATPTGSTAYAFSAGGPVVWPELEALLVIPSNAHALFARPLVTSPESRIAVESVATGHDAIVFLDGRRTLALPRGGRVEAVRGSEPVRWVRLDSAPFADRMVRKFQLPVTGWRGRRRTESTRADRDQD", "text": "FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD kinase family."}
{"protein": "MLRRLVISIMLGMVSALIVWLFHQAMLGLEWLLFSRTDGSLVAAAASITGWRRALTPALGGLAAGLLLWAYQRYQHRKPSAPTDYMEAIEIGDGRLDVSASLVKSLASLLVVSSGSAIGREGAMVLLAALFASVFAQRYAKPKEWKLWVACGAAAGMASAYHAPLAGSLFIAEILFGTLMLASLGPVVIAAVSALLTTNLLQGGQETLYQVQTLPSPWPVQYFLMALLGLMAGFSGPLFLKAMAASSHAFRSLNLLPPLQLALGGIIVGLLSLIFPEVWGNGYSVVQSLLTTPPGVLLIGGILICKLLAVLASSGSGAPGGVFTPTLFVGAALGMLCGQIFSLWPVLGDNIGLLMALTGMATLLAATTHAPIMAALMVCEMTGEYTLLPGLLLSCVIATTIARWLRPISVYRSH", "text": "FUNCTION: Probably acts as an electrical shunt for an outwardly- directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcB subfamily."}
{"protein": "MKKIKEAEQRKIRRKKRIKDKIGRGIATRPRITIFKSNRYFYAQVIDDSKGHTVASISTIEKSLNLSKNIDDIKKLGEVLAKRLKEKNINNLIFDRNGYKYHGLIASFATSLREFGINI", "text": "FUNCTION: This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. SIMILARITY: Belongs to the universal ribosomal protein uL18 family."}
{"protein": "MDVRQSIHSAHAKTLDTQGLRNEFLVEEVFVADEYTMVYSHIDRIIVGGIMPITKTVSVGGEVGKQLGVSHFLERRELGVINIGGAGTITVDGQCYEIGHRDALYVGKGAKEVVFASIDTATPAKFYYNCAPAHTTYPTKKVTPDEVSPVTLGDNLTSNRRTINKYFVPDVLETCQLSMGLTELAPGNLWNTMPCHTHERRMEVYFYFNMDDDACVFHMMGQPQETRHIVMHNEQAVISPSWSIHSGVGTKAYTFIWGMVGENQVFDDMDHVAVKDLR", "text": "FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D- glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate. SIMILARITY: Belongs to the KduI family."}
{"protein": "MGLTSQLIPALVCLLVCTSHFVHGHKCDITLEEIIKMLNILTSQKNSCMELPVADVFAAPKNATEKETFCRAGIELRRIYRNHMCLNKFLGGLDRNLSSLASKTCSVNEAKTSTSTLRDLLERLKTIMKEKYSKC", "text": "FUNCTION: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-4/IL-13 family."}
{"protein": "MAVENNTQRSYSIIPCFIFVELVIMAGTVLLAYYFECTDTFQVHIQGFFCQDGDLMKPYPGTEEESFISPLVLYCVLAATPTAIIFIGEISMYFIKSTRESLIAEEKMILTGDCCYLSPLLRRIIRFIGVFAFGLFATDIFVNAGQVVTGHLTPYFLTVCQPNYTSTDCRAHQQFINNGNICTGDLEVIEKARRSFPSKHAALSIYSALYATMYITSTIKTKSSRLAKPVLCLGTLCTAFLTGLNRVSEYRNHCSDVIAGFILGTAVALFLGMCVVHNFRGTQGSPSKPKPEDPRGVPLMAFPRIESPLETLSAQNHSASMTEVT", "text": "FUNCTION: May play a role in neurite outgrowth and neurogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, neuron projection. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
{"protein": "MSVIKMTDLDLAGKRVLIREDLNVPVKDGKVTSDARIRASLPTIEHAMKAGAKVMLMSHLGRPEEGVFSEEDSLKPVAEHLSGLLGKEVRLVRDYLDGVDVADGEVVLLENVRFNKGEKKNEEGLSRKYAALCDVYVMDAFGTAHRAQASTHGAGQYAPVACAGPLLAAELEALGKALDNPKRPLVAIVGGSKVSTKLTVLESLSKVVDQLIVGGGIANTFIAAQGHPVGKSLYEADLVDEAKRLMAAAKAKGGDIPVPTDVVTGKEFSESTPASTKRVSEVAADDMIFDVGPDTAASYADMLRKAGTIVWNGPVGVFEFDQFAAGTKALGEAIADSDGFSIAGGGDTLAAIDKYGLASRISYISTGGGAFLEFLEGKKLPAVAMLEERAKG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MQTISLIRPDDWHLHVRDGAALATVVPHTARRFGRALIMPNLRPPVTTAAQALEYRARILAAVPPGQHFEPLMSLYLTDNTSPDEIDRAKASGAVVAVKLYPAGATTNSDAGVTAIEKVHAVLERMEKLGMVLCVHGEVTHGDVDVFDREQVFIEQVLAPLVARFPALRVVFEHITTAEAARFVQDAGPNVAATVTAHHLLLNRNAIFAGGIRPHHYCLPVLKRETHRRALVEAATSGNAKFFLGTDSAPHSRAAKETACGCAGCYTAHAAIELYAEAFEQAGALDRLEAFASLNGPAFYGLAPNAERITLAKDAWEVPGEYEYLHDDPLVPLRAGETVAWRVL", "text": "FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily."}
{"protein": "MENFDKTMKFNYDEIPKEDVKTVLQNVYHTLEERGYNPVNQIVGYLLSGDPAYIPRNNEARNQIRRIDRDDIMEELVSNYLQEKSN", "text": "SIMILARITY: Belongs to the UPF0297 family."}
{"protein": "MLPSALLRRPGLGRLVRQVRLYAEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIRIEANEALVKALE", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase epsilon chain family."}
{"protein": "MAREYPLELYRNFGIMAHIDAGKTTCSERILFYTGKSHNIGEVHDGAATMDWMEQEQERGITITSAATTTFWERTEDGETADTPKHRLNIIDTPGHVDFTIEVERSLAVLDGAVCVLDANAGVEPQTETVWRQADRYKVPRMVFVNKMDKIGADFFNCVRMIEDRTGARAVPVGIPIGAENELEGLIDLVTMKEWLWQGEDLGASWVQVDIRDSLKEMAEEWRGKMIEAAVEMDDDAMENYLMDGAEPDVATLRSLLRKGTLSLSFVPVLGGSAFKNKGVQPLLNAVIDYLPSPLDVVDYMGFKPGDEEEVRNIARRADDDMAFSGLAFKIMNDPFVGSLTFTRIYSGVLNKGDSILNSTKGKKERIGRMMMMHSNNREEIEEAFAGDIIALAGLKDTTTGDTLCDAKEPVVLETMTFPDPVIEIAVEPKTKGDQEKMSQGLARLAAEDPSFRVETDLESGQTIMKGMGELHLDILVDRLKREFKVEANIGAPQVAYRETIGHEVEHTYTHKKQSGGSGQFAEVKMIISPTEAGEGYSFESRIVGGSVPKEYIPGVEKGINSVMDSGPLAGFPVIDFKVALIDGKFHDVDSSVLAFEIAARMCMREGMRKAGAKLLEPIMKVEVITPEEYTGGIIGDLTSRRGQVSGQEPRGNAIAIDANVPLANMFGYINTLRSMSSGRAQFTMQFSHYDPVPQNISEEIQAKYA", "text": "FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MNGFSTEEDSREGPPAAPAAAAPGYGQSCCLIEDGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSVRHLYICDFHKNFIQSVRNKRKRKTSDDGGDSPEHDTDIPEVDLFQLQVNTLRRYKRHYKLQTRPGFNKAQLAETVSRHFRNIPVNEKETLAYFIYMVKSNKSRLDQKSEGGKQLE", "text": "FUNCTION: [Isoform 2]: Functions as transcription repressor; isoform 2 has lower transcription repressor activity than isoform 1 and isoform 3. FUNCTION: [Isoform 1]: Functions as transcription repressor, probably via its interaction with histone deacetylase complexes (PubMed:16820529, PubMed:18070604). Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus (PubMed:16820529). Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA (PubMed:19015240). Binds phosphoinositol phosphates (phosphoinositol 3- phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) via the same basic sequence motif that mediates DNA binding and nuclear import (PubMed:19015240, PubMed:26609676). FUNCTION: [Isoform 3]: Functions as transcription repressor; its activity is marginally lower than that of isoform 1. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus. SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleolus. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleolus. SIMILARITY: Belongs to the SAP30 family."}
{"protein": "MAAAAEGVPATRREEPPRDDAAVETAEEAKEPAEADINELCRDMFSKMATYLTGELTATSEDYKLLENMNKLTSLKYLEMKDIAINISRNLKDLNQKYAGLQPYLDQINVIEEQVAALEQAAYKLDAYSKKLEAKYKKLEKR", "text": "FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. May play a role in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Lysosome membrane Note=Localizes to the centrosomes in a microtubule-dependent manner. SIMILARITY: Belongs to the BLOC1S2 family."}
{"protein": "MEIEVVLGIGEDAGPKPCSAEIESAEKTLKDDGVVQENGVRVSDNGEKKSDVVVDVDEKNEKNLNESGVIEDCVMNGVSSLLKLKEDVEEEEEEEEEEEEEEEDGEDEEEEEEEEEEEEEEEHGYCVGDFVWGKIKNHPWWPGQIYDPSDASDLALKIKQKGKLLVACFGDGTFAWCGASQLKPFAESFKECSKVSNSRSFLGAVEEAVEEIGRHIERVLVCDCAEEKKHEFDSPLVNNAGIKEGVLVRDVRREMISSLLIGKHGEILKDVKSFAETVSFSGLLELEILKRKVSAFYRSNRGYGLTEYHEPQSVPGLEDKNNDDDDDDEEKNVNDGLQWRAKRSRVEEVAALDHEESSSLQRSLEKCSGFPDHRLPHRRKEKSITEIIEKESAAKVRFETEPADGDVKSNVKSGRKKTKRHDEVNGDLENVTTTALWRRRKSEVATIEDGGNKQVVESSKGKTSRKKKKMDVDDGDDDGSGDKEESEEKEISDLEINIDSTSLASLRKKVRFDDSVVERSTENGETATQTSKRERKKSKYLSPDFLSDFSRKGRKKSTIESESSKVSSQSQVDERVTDASDSLMEVEEDTLDKPCEPSSDNGLGQEELSRELSNAVDFLRLGATPKEMQDLIRVAALGTQYPKDSSSRDMVREFMTIYRSFTYHDGANHKFLGSYDSSDKEKEELSEMGKPVTKGKEKKDKKGKAKQKAEEIEVTGKEENETDKHGKMKKERKRKKSESKKEGGEGEETQKEANESTKKERKRKKSESKKQSDGEEETQKEPSESTKKERKRKNPESKKKAEAVEEEETRKESVESTKKERKRKKPKHDEEEVPNETEKPEKKKKKKREGKSKKKETETEFSGAELYVTFGPGSSLPKKEDLIEIYEKFGALDKERTDTVDNNFSAHVAFLDVADGEKAFESSLEKCPFTSNSTVKFRLKYPNERTEEKKTEAEVAETTMEVEYLKKKLDEMKLLLDGCEGGMTEEVKVKLEGEMVNLLEKVIEMRSS", "text": "FUNCTION: Together with PDP1, PDP2 and PDP6, interacts with MSI4/FVE and MSI5 to suppress FLC, MAF4 and MAF5 expression by regulating the function of the PRC2 complex and modulating H3K27me3 level, thereby promoting flowering. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PDP family."}
{"protein": "MSSTTTVAEFAAELNKSPATLIEQLTSAGVAKVQASDPLSESDKQKLLGYLHASHGTVAADRKKITLVKKSTSEIKQADSTGRARIIPVQTIKKRTFIKRDDGSDMPVEEAQPEVLVAPQVQAAADAELVRREDEANRHAELLRRQEAELTEKRRLRDEQAAQEAAREREREAAAQKAQAEAVAQAAAAAQAAALAAEAAKKVKPTIGKIFKPAPVAPTAPAITVEAQKVIDTAAAEKTSKAAEAATAKAAETASLQAAAKAKATAEFQADAAKAVDLQERRRKAEAEAAGIRAMLSAPKRVLVPHVDPKIAMKGTLHKPVVAPGAAKPAVPAAAAPAAPGAAGKKEVKSENLSSTWKDDAAKKKGIPSRGAPVVPGRGNFRAGPRGRRSSGRDVRPESNFVAPTEFKVLEVHVPETITVSELAHKMSIKSSEVIKHLMKLGQMVTINQPLDQDTAMIVVEEMGHTALTAALDDPEAFTADDVQGQQAEALPRAPVVTVMGHVDHGKTSLLDYIRRAKVASGEAGGITQHIGAYHVQTPRGMVSFLDTPGHEAFTAMRARGAQATDIVILVVAADDGVMPQTKEAIKHARAAGVPIVVAINKIDKPGINLERVKGELVTEGVVPEEFGGDSPFVPVSAHTGAGIDDLLEQVLLQAEVLELKASVDSLAKGLVIEARLDKGRGPVATVLVQSGTLKAGDVVLAGSTYGRVRAMLDENGKPIKTAGPSIPVEIQGLTEVPQAGDDFMVMTDERRVREIATYRAGKFRNTKLAKQQASKLENMFSDINAGEVKMLPIIIKADVQGSQEALAQSLLKLSTDEVKVQLVYSGVGGISESDVNLAIASKAVLIGFNTRADAQARKQAENNGIDIRYYNIIYDAVDELKAAMSGMLTPDKKEEIIGNAEIRNIFKVSKIGSIAGCMVTAGVVRRTAKVRLLRGNVVIFTGELDSLKRFKDDAKEVKEGFECGLNLKNYNDIEVGDILEFFEIKEVARTL", "text": "FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily."}
{"protein": "MPKKPARTRRPAPLAGRARKKNLLDSLGLRTVDYKDTATLRVFISERGKIRSRQVTGLSVQQQRQVATAIKNAREMALLPYPGQGIKP", "text": "FUNCTION: Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
{"protein": "MSVARNLWRVADAPHIVPADSVERQTAERLINACPAGLFSLTPEGNLRIDYRSCLECGTCRLLCDESTLQQWRYPPSGFGITYRFG", "text": "FUNCTION: Could be a 3Fe-4S cluster-containing protein. Probably participates in a redox process with YgcN, YgcQ and YgcR. SIMILARITY: Belongs to the bacterial-type ferredoxin family. FixX subfamily."}
{"protein": "MKLHEYEAKNIFKKYGIPVPESFLVSKEDDLNSINVDKEVVLKAQVLVGGRGKAGGILFASNKEEFIKKAEELFNKEVKGEKVEKILVEEKLPIEKEYYVSIIIDRDAKKPLIIFSTEGGVDIEEVAEKNPEKIIKYHIDVRKPFLPYIARWIVKEAKLPSNEIGKVADVIYKLYKIFKELDATMVEINPLVITKDGNVYAADAVLHLDDDAAFRHNYEEFEEYKNKEKLPFAYVELDGDVAVIGNGAGLTLASMDIINNLGRKPACFLDIGGGADAETVKLALRKVLENKNVKGIFINILGGITRCDEVAKGIVEVLKEHPNVKFAVRMMGTNEEIGRKILEEHGIPYETSMEEAGRKLIEQL", "text": "FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family."}
{"protein": "MTAIIKEFVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTNKFSCRVAQYPFEDHNPPQLELIKPFCEDLDQLLSENENVAAIHCKAGKGRTGVMICAYLLHRGKFPRAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNSLEYRPVPLLFHKIEFETIPMFSGSTCNPQFVVYQLKVKIFTSTAGPKRAEKLMYFDFPQPLPVCGDIKVEFFHKQNKVMKKEKMFHFWVNTFFIPGPEEYSEKVENGTLVGEQELDGIYSTERSDNDKEYLTLALTKNDLDKANKDKANRLFSPNFKVKLFFTKTVEESSNSEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQITQITKV", "text": "FUNCTION: Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5- trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, PML body Cell projection, dendritic spine Postsynaptic density. SIMILARITY: Belongs to the PTEN phosphatase protein family."}
{"protein": "MRKLKKFFKNPGIFIRDHLNKKYPVIRNEIECAENEEDILMRHDLALESKIDIDFPIDVVFTWVDDTDPTWQLRYQQHKLQVNAEHVGRYATDPARFSNHDELRYSLGSVLKFLPWVRRIYIVTDQQCPKWLTPSDKIRIVDHTDIIDRQYLPTFNSHVIEAHLHKIPDLAEHFIYFNDDVFVARPLPAGHFFRSNGIASLFMSNKSLAIMQKKGTDTPTLSASLKSASILNQDFSFLIDHPLVHTYVPLRKSIFEESWRLYRADLKSFLSHRFRTNHDLNLATFFVPWLSYIRGVAVPSRDICYYFNARSPAAATYFKALEIAKQKGTLPHSFCANDFNSKEKTKDSNVTLLLSRYFKDAITG", "text": "FUNCTION: Part of a group II capsule biosynthesis locus. SIMILARITY: Belongs to the stealth family."}
{"protein": "MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKKRKSSSSVHLMPQSNNKNSLVSPAQEPAPLQTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKVRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSGAPAAPLQ", "text": "FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity (By similarity). In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin (By similarity). In the central nervous system, it is involved in the regulation of neurite formation and arborization (PubMed:30184290). It may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning (PubMed:30184290). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK- STAT signaling pathway (PubMed:11972023). SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily."}
{"protein": "MGFPVTKLTHVIAGVGLLLAGREVAAQCALPSSYSWSSTNALASPKSGWAAIKDFTSVIYNGQHLVYASFADTSGNYGSMNFSPFSDWSDMASASQNAMSQAAVAPTLFYFAPKDIWILAYQWGPTSFSYKTSSDPTNPNGWSTPQPLFSGTISDSATGCIDQTLIGDSSNMYLFFAGDNGKIYRASMPIDNFPGDFGTESEIIMSDTSNNLFEAVQVYTVDGQNQYLMIVEAIGANGRYFRSFTADSLDGAWTAQAATESQPFAGKANSGASWTNDISHGDLVRSNPDQTMTIDPCNLQLLYQGRDPNASGDYNLLPWVPGVLTLQ", "text": "FUNCTION: Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 62 family."}
{"protein": "MRGAFLATAAAIAGTAMADIAHMRRHGHDSFHQRRAVEQPAPEADATCGCTTEVVTSWGPPTLIPIATSSPSSTVTSEVVTTLHSTSYSTVTLVVTPSGASPNRESAPATPAVTLPTPGVTSFSTTGTYTIPATTLTVTHSTTVCGATTTELPSGTHTYGGVTTVVDRHTTVVCPYATVEPSGSTVTSVIRTTTYVCPSAGTYTIAPTTTYVPTSTVIVYPTPATITPGTYTQPAQTITVTRDNYIYVCPFTGQQLPTTAPVAPATTAVPATTTAVPATTTAVPATSSVAPSSSPSKPAAPSGAVSGQMGMTYSPYTNEGGCKDKASIISEVALLKSKGFTHVRVYSTDCGSLEFIGEAARTSGLRMIIGVFIKQSGVAGAQDQVTAISKWAQWDLVSLIVVGNESIQNHFCDASTLAGFIVSAKQSFKAAGYSGQVTTTEPINVWQANGDALCGAVDIIGANIHPFFNADVSAAEAGKFVAQEFKTLKGICPGKDVINLETGWPHSGEANGKAIPSREEQAIAIKAIADEVGSMSVFFSYFDDLWKQPGAFGVERYWGCIENF", "text": "FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Note=Covalently-linked to the cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
{"protein": "MQSSSPSTSHCSQIPIKIQHHIAKKRQVRRRRVDLDCGCSYYIHLDCINHGFTHRGVHHCASSNEWRLYLRDNKSPIFHDNQTQSEPIQQQIQHTNIPNQIQPQLEEGTGDSQMFSQLPHLDDLTVSDWSFFKSL", "text": "FUNCTION: Strong activator of the late viral genes promoters. Acts as a suppressor of RNA-mediated gene silencing, also known as post- transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. TrAP suppresses the host RNA silencing by inhibiting adenosine kinase 2 (ADK2), a kinase involved in a general methylation pathway. Also suppresses the host basal defense by interacting with and inhibiting SNF1 kinase, a key regulator of cell metabolism implicated in innate antiviral defense. Determines pathogenicity (By similarity). SUBCELLULAR LOCATION: Host nucleus Host cytoplasm Note=The phosphorylated form appears to accumulate almost exclusively in the nucleus, whereas the non-phosphorylated form is found in both nucleus and cytoplasm. SIMILARITY: Belongs to the geminiviridae transcriptional activator protein family."}
{"protein": "MTAQINLKDITVQFGPNKAVNNVNLEINKGDIYGVIGFSGAGKSTLVRTINLLQYPSAGSVEVNGTILFKEGKLQVSKKQLQEKRRKIGMIFQNFNLLNEETVIENVAFALQHTHLSDKELEEKSLHLLELVGLKDKSDFYPAQLSGGQRQRVAIARALANDPDILISDEATSALDPKTTNQILDLLYDLNKKLGLTIVLITHEMDAVKRVANKIAVMEKGKVIEKGDLREVFLHPQKQLTRQFVGGALQAQHILNTYNFDKLADNAELYQLVYSINDVTKSVVADLDVSLNTKASILYGNVEVLSGEPIGTLAILLNLDEQKQKEAIKFLESKNVVVTKLDKGVLTND", "text": "FUNCTION: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family."}
{"protein": "MAEASGLVTVCLLGYLLSAECAVFLDRENATKILSRPKRYNSGKLEEFVRGNLERECIEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNDGVCKDDINSYECWCRAGFEGKNCELDVTCNIKNGRCKQFCKLGPDNKVVCSCTTGYQLAEDQRSCEPAVPFPCGRVSVPHISMTRTRAETLFSNMDYENSTEVEKILDNVTQPLNDFTRVVGGKDAKPGQFPWQVLLNGKVDAFCGGSIINEKWVVTAAHCIEPDVKITIVAGEHNTEKREHTEQKRNVIRTILHHSYNATINKYNHDIALLELDEPLTLNSYVTPICIADREYSNIFLKFGSGYVSGWGRVFNKGRSASILQYLKVPLVDRATCLRSTKFTIYNNMFCAGFHEGGKDSCQGDSGGPHVTEVEGISFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT", "text": "FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MGPRVLPLLEPGCRPQAGKWYRMAPRGEWPRGRVGHGCLFVPGGSGRVLLLGGADPAGAFADAHFVELGAHLWAPAAWSGLRPRYEHATFLSACRPPRLWVFGGAHRAGNRSCVQVLDPEIGTWESPEVTGIPPLPRTFHTSSAAIGDCLYVFGGGDKGAEPVKDQQLHVFDTVALAWTQPDTHGDPPSPRHGHVVVAVGTKLFIHGGLAGDIFYNDLFCIDTTDMKWVKIAATGDVPGGRASHSSAVFKDHLYIFGGIGPDGTLDTTYKYHIEEQQWTLLQFDSPLPAGRLDHAMCVIPWRVGKNGDAAAVSKEDKAEPTASAGDRAGHLCRGQDKKACTEDTMMHLLLIFGGMDTQAEIYRDCIVSLIE", "text": "FUNCTION: Rab9 effector required for endosome to trans-Golgi network (TGN) transport."}
{"protein": "MPSLPPAIFLMGPTAAGKTDLAMALADALPCELISVDSALIYRGMDIGTAKPSRELLARYPHRLIDIRDPAESYSAAEFRADALAAMAEATARGRIPLLVGGTMLYYKALLEGLADMPGADPEVRAALEAEARAEGWEALHRQLAEVDPESAARIHPNDPQRLMRALEVYRVGGVSMSELRRRQSAEKADFDASGRNQLPYTVAQLAIAPEQRQVLHARIAQRFRQMLEQGFIAEVEALHARSDLHAGLPSIRAVGYRQVWDYLDGKLSYAEMTERGIIATRQLAKRQFTWLRSWSHLHWMDSLAGDNLPRALKYLKTVSILA", "text": "FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). SIMILARITY: Belongs to the IPP transferase family."}
{"protein": "MGLPNAEEVKAFLMQLQANICAGLERLDGQASFATDSWQRAEGGGGISRVLTDGAVFEQAGVNFSHVMGASMPASATAHRPELAGRSFEAMGVSLVIHPKNPYIPTTHANVRFFIARKEGADPVWWFGGGFDLTPYYPFESDVKEWHQSAKDLCAPFGNEVYPKYKEWCDKYFFLPHRGETRGVGGLFFDDLNHWEFDKCFDYMQAVGNGFLTAYAPIVERRKDTAYGERERDFQLYRRGRYVEFNLVYDRGTLFGLQTGGRTESILMSMPPLVRWQYAYSPEAGTPEAELYERFLKPQDWLAD", "text": "FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase family."}
{"protein": "MDTWKVGPVELKSRLILGSGKYEDFGVMREAIAAAKAEVVTVSVRRVELKAPGHVGLLEALEGVRLLPNTAGARTAEEAVRLARLGRLLTGERWVKLEVIPDPTYLLPDPLETLKAAERLIEEDFLVLPYMGPDLVLAKRLAALGTATVMPLAAPIGSGWGVRTRALLELFAREKASLPPVVVDAGLGLPSHAAEVMELGLDAVLVNTAIAEAQDPPAMAEAFRLAVEAGRKAYLAGPMRPREAASPSSPVEGVPFTPTGPRPGRGPQ", "text": "FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ThiG family."}
{"protein": "MNSNASNTPIAIGISQIFPCSYLDGQQEQLLVIQEETLDPILFDRLLAIGFRRSGSAIYKPRCPRCSACQPIRLPINEFMPSKRQKRTLAHNRDLTWRMTSEHTEAQYALYEKYIRERHFDGPMFPPSKSQYEQFLFCHWLPPTFIEVYDGNRLLAVAVTDTLPNSLSAIYSYFDPDEERRSLGSLLILLQCRLAKLQDKEFLYLGYQIDANRKMSYKRLYRPYQILTPQGWEYSQVC", "text": "FUNCTION: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the R-transferase family. Bpt subfamily."}
{"protein": "MANAASGMAVHDDCKLKFMELKAKRTFRTIVYKIEDKQVIVEKLGEPEQSYDDFAASLPADDCRYCIYDFDFVTAENCQKSKIFFIAWSPDTAKVRDKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVFKSRTN", "text": "FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (PubMed:15563618, PubMed:19794115). Required for normal cell growth, plant development, cell organ expansion and flowering. Essential for root-knot nematode infection (PubMed:19794115). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
{"protein": "MAGGKGGKGMGKVGAKRHSRKSNKASIEGITKPAIRRLARRGGVKRISSFIYDDSRQVLKSFLENVVRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H4 family."}
{"protein": "MIQPQTHLNVADNSGARELMCIRIIGTSNRRYAHIGDVIVAVIKEVVPNMPLERSEVIRAVIVRTCKELKRDNGMIIRYDDNAAVIIDQEGNPKGTRIFGAIVRELRQLNFTKIVSLAPEVL", "text": "FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
{"protein": "MATLKIKKGDTVQIITGKDRGLKGKVIRAYPEQNKVLVEGANRITRHTRVQQGTRGSQSGGIITQEAPIHVSNVMIVDPSDGKPTRIGYRINDDGTKVRVSRRTGTEL", "text": "FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
{"protein": "MTKHYDYIAIGGGSGGIASLNRAASYGKKCAIIEAKHLGGTCVNVGCVPKKVMFYGAHIAEAINNYAPDYGFDVEVKKFDFSKLIESRQAYISRIHTSYNNVLAKNNIDVINGFGKFVDAHTIEVTLADGTKEQVTADHILIATGGRPYRPNIKGQEYGIDSDGFFALTELPKRAAVIGAGYIAVELSGVLNSLGVETHLLVRRHAPMRNQDPLIVETLVEVLAQDGIQLHTNSTPSEIVKNADGSLTVRCDGQSDVTVDCVIWAAGRVPTTDKIGLENAGVETNEHGYVKVDKYQNTNVKGIYAVGDIIENGIELTPVAVAAGRRLSERLFNNKPTEYLDYSLVPTVVFSHPPIGTVGLTEPQAIEQYGAENVKVYKSSFTAMYTAVTQHRQPCKMKLVCVGKDEKVVGLHGIGFGVDEMIQGFAVAIKMGATKADFDNTVAIHPTGSEEFVTMR", "text": "FUNCTION: Maintains high levels of reduced glutathione in the cytosol. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "YPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY", "text": "FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
{"protein": "MPVTDRSVPSLLQERADQQPDSTAYTYIDYGSDPKGFADSLTWSQVYSRACIIAEELKLCGLPGDRVAVLAPQGLEYVLAFLGALQAGFIAVPLSTPQYGIHDDRVSAVLQDSKPVAILTTSSVVGDVTKYAASHDGQPAPVVVEVDLLDLDSPRQMPAFSRQHTGAAYLQYTSGSTRTPAGVIVSHTNVIANVTQSMYGYFGDPAKIPTGTVVSWLPLYHDMGLILGICAPLVARRRAMLMSPMSFLRRPARWMQLLATSGRCFSAAPNFAFELAVRRTSDQDMAGLDLRDVVGIVSGSERIHVATVRRFIERFAPYNLSPTAIRPSYGLAEATLYVAAPEAGAAPKTVRFDYEQLTAGQARPCGTDGSVGTELISYGSPDPSSVRIVNPETMVENPPGVVGEIWVHGDHVTMGYWQKPKQTAQVFDAKLVDPAPAAPEGPWLRTGDLGVISDGELFIMGRIKDLLIVDGRNHYPDDIEATIQEITGGRAAAIAVPDDITEQLVAIIEFKRRGSTAEEVMLKLRSVKREVTSAISKSHSLRVADLVLVSPGSIPITTSGKIRRSACVERYRSDGFKRLDVAV", "text": "FUNCTION: Catalyzes the activation of long-chain fatty acids as acyl- adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase PpsA for further chain extension (PubMed:15042094, PubMed:15749014, PubMed:20553505). Catalyzes the adenylation of the long-chain fatty acids eicosanoate (C20) or docosanoate (C22), and potentially the very-long-chain fatty acid lignocerate (C24) (PubMed:15749014, PubMed:20553505). Involved in the biosynthesis of phthiocerol dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B) (PubMed:11279114, PubMed:20553505). FUNCTION: Catalyzes the activation of long-chain fatty acids as acyl- adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase PpsA for further chain extension. Catalyzes the adenylation of the long-chain fatty acids eicosanoate (C20) or docosanoate (C22), and potentially the very-long-chain fatty acid lignocerate (C24). Involved in the biosynthesis of phthiocerol dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MSRRHKAEKREINPDPKFGDLVVTKFMNAIMLDGKKSVAENIVYGAFDAVQGKSKQEPLSVFHSALDNIAPHVEVRSRRVGGATYQVPVDVRPERRQALAIRWLIAAARKRNETTMIDRLSGELLDASNNRGSAVKKREDTHKMADANRAFSHYRW", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MSYTITDPSKLAYLSSAWADPNSLINLCTNSLGNQFQTQQARTTVQQQFADVWQPVPTLTSRFPAGAGHFRVYRYEPILEPLITFLMGTFDTRNRIIEVRNPQNPTTTETLDATRRVDDATVAIRSAINNLLNELVRGNGMYNQVSFETMSGLTWTSS", "text": "FUNCTION: Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the virgaviridae capsid protein family."}
{"protein": "MQFGADTEFSNMCGVTLMNTPIGRVVADVMGAKDGVELTEYPSMIRVDGVNRLDFDYDELTDALGQDFDGSIFEEISSTHYGRMVHLDDKTILFASPEDAAEFIGFDLTAS", "text": "FUNCTION: Effector component of the propane 2-monooxygenase multicomponent enzyme system which is involved in the degradation of propane via the O2-dependent hydroxylation of propane. SIMILARITY: Belongs to the TmoD/XamoD family."}
{"protein": "MKRVAFIFSSAPHGSAAGREGLDALLATSALTDEIGVFFVGDGVFQLLPDQRPGAVLARDYIATFKLLSLYDIDQCWLCADSARERGLDPATPWVVDVECLAPDALRARLHEFDVILRF", "text": "FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrF/TusC family."}
{"protein": "MSRLQTRFAQLKQDNRAALVTFVTAGDPDYDASLEILKGLPAAGADVIELGMPFTDPMADGPAIQLANIRALQGGQTLAKTLRMVREFRAGDSDTPLVLMGYFNPIHHYGVERFVTEAKEAGVDGLIVVDLPPEHNEDLCHPAQAAGIDFIRLTTPTTGDERLPTVLEGSSGFVYYVSVAGVTGANAATLEHVEEAVARLRRHTDLPIGIGFGIRSAEHAAAVARLADGVVVGSALIERIAKAGDTARAVKDVLALCGELAEGVRNAR", "text": "FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. SIMILARITY: Belongs to the TrpA family."}
{"protein": "YITCLFRGARCRVYSGRSCCFGYYCRRDFPGSIFGTCSRRNF", "text": "FUNCTION: Exhibits stronger antimicrobial activity against the Gram- positive bacteria (S.aureus (IC(50) is 7.4 ug/ml)) and fungi (C.albicans (IC(50) is 3.0 ug/ml) and P.pastoris (IC(50) is 0.1 ug/ml)) than Gram-negative bacteria (E.coli no inhibition at 100 ug/ml). Binds to chitin (4.3 uM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTTAARPTFEPARGGRGKGEGDLSQLSKQYSSRDLPSHTKIKYRQTTQDAPEEVRNRDFRRELEERERAAARDKNRDRPTREHTTSSSVSKKPRLDQIPAANLDADDPLTDEEDEDFEEESDDDDTAALLAELEKIKKERAEEQARKEQEQKAEEERIRMENILSGNPLLNLTGPSQPQANFKVKRRWDDDVVFKNCAKGIDDQKKDKRFVNDTLRSEFHKKFMEKYIK", "text": "FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre- mRNA splicing. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC15 family."}
{"protein": "MDIRKVKKLIELLEESGIDELEIREGEESVRISRHSKTAAQPVYAQAPAFAAPVAAPAPAAAAPAAAAAESAPAAPKLNGNVVRSPMVGTFYRAASPTSANFVEVGQSVKKGDILCIVEAMKMMNHIEAEVSGTIESILVENGQPVEFDQPLFTIV", "text": "FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA."}
{"protein": "MPPKARAPLPPGDAARGEKLFKGRAAQCHTANQGGANGVGPNLYGLVGRHSGTIEGYAYSKANAESGVVWTPDVLDVYLENPKKFMPGTKMSFAGMKKPQERADVIAYLETLKG", "text": "FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MAARPVSSTTSTCRPCRPAQAAASKPSTSSSPGTGVLVGVPRERGSSVSKAAIRGARLEAAARCSLVRQRPMLLATVAVGSLVAAGAANATEIGDSLLGSSGLALADLSIGDWFGNLLYSAGQQANEAVQDQLSALSFTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKDRSEVVGNSVAFSLGLATTLAILGVAASFAGKAYGQVGQGLPVAASGLAVIMGLNLLEVIELQLPSFFSDYDPRAAAANLPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPIVGGSLLLTYTTGYVAPLLIAASFAGALQSLLSFRRYSAWINPISGAFLLGGGVYTLLDRLFPATSMVM", "text": "FUNCTION: Probably involved in the transfer of reducing equivalents from stroma to thylakoid lumen and required for the biogenesis of the plastid cytochrome b6f complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbD family."}
{"protein": "MNLRLELTRFLKLCFVLSSAFMFWKGLSIATNSHSPIVVVLSGSMEPAFQRGDVLFLWNRNERSKVGDVVIYEVQDKSIPIVHRVLREHHNDKNKQLLLTKGDNNAGDDIPLYGRKKIYLQKERDIVGTVKGYVPQLGYVTIWISENKYAKLALMGFLGISALLSNE", "text": "FUNCTION: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S26B family."}
{"protein": "MRRGPWERWSLASHRLDAGLCTCPREESREIRAGQIVLKAMAQGLVTFRDVAIEFSLEEWKCLEPAQRDLYREVTLENFGHLASLGLSISKPDVVSLLEQGKEPWMIANDVTGPWCPDLESRCEKFLQKDIFEIGAFNWEIMESLKCSDLEGSDFRADWECEGQFERQVNEECYFKQVNVTYGHMPVFQHHTSHTVRQSRETGEKLMECHECGKAFSRGSHLIQHQKIHTGEKPFGCKECGKAFSRASHLVQHQRIHTGEKPYDCKDCGKAFGRTSELILHQRLHTGVKPYECKECGKTFRQHSQLILHQRTHTGEKPYVCKDCGKAFIRGSQLTVHRRIHTGARPYECKECGKAFRQHSQLTVHQRIHTGEKPYECKECGKGFIHSSEVTRHQRIHSGEKPYECKECGKAFRQHAQLTRHQRVHTGDRPYECKDCGKAFSRSSYLIQHQRIHTGDKPYECKECGKAFIRVSQLTHHQRIHTCEKPYECRECGMAFIRSSQLTEHQRIHPGIKPYECRECGQAFILGSQLIEHYRIHTG", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MIRIAIDAMGGDFGPEPIIAGVVEALKDTKFSAVLVGDSNAIKPLIPEMYLKNIAFLEAAEVISMAEGATDALKRKESSIYKAIELLKNKEVDAVVSAGHSGATMSLATLRVGRLKNVARPAIATLMPNSKESTTLVLDVGANVDCRSEHLFQFAVMGEAYAKEILNRKLPRVGLLSNGEEACKGNEVSKEAFELVSRLDSFVGNAEGNQVFDGSVDVIVCDGFIGNILLKTSEGVADAIGKIIKKQVKKSPLAIAGSVLMKKVFRTLKKQVSYDEYGGAPLLGINGCVIISHGKSNSKAIKNAIFQAINFANSNINKVIEEELSHFAR", "text": "FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with the membrane possibly through PlsY. SIMILARITY: Belongs to the PlsX family."}
{"protein": "MSVVGKRVVDELCRVVSSYLGQSGQSLDLERCIDGAPVYAKGGATAICTVRMQHGCVYHLEFVYKFWAHLLEEMHYPFSPCFVISNNGLSTTLKCFLCRPSDAVSQFGHVLPVESDVYLAKNTSVVLGQDDFTKFKASLVFSKNLGVYNSMVICRTYFTDYRQVLQFLVVTPKSHKRLKSLLETVYCLAAPVADSAAQGGAGFPTNGRDARACTSDVTAVYWAGQGGRTVRILGAFQWSLGRAVALVRRSWPWISAGIAFLCLGLVWMRPS", "text": "FUNCTION: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. SUBCELLULAR LOCATION: Host nucleus inner membrane; Single-pass membrane protein Note=Localizes also at the transient membrane of perinuclear virions. SIMILARITY: Belongs to the herpesviridae NEC2 protein family."}
{"protein": "MSSAAASATAGSVTGKTPRILACVLCQHRKIKCDRSFPCANCQRANVQCTPSTPAPARKRRRPNQDLQERLARCEELLKEYAPDGKPDIARLTTKRSSLSQSPPKGEEPLPEWNRHGKLIHEDGSVRFVDSYMLSTIYDELRAMRDIIDHDESTPEDESSDYMTPDTNADLLFGGDTPQPAGNSMELQPSPGHIFRLWQVFLDRVNPLIKLVHVPSLQPYFVEATAGAPLPKNIEALLFSIYTLAAVSLSDAECTSILGYGREAALHRFSSGVRASLIRIGFLKTHDLTTLQALVHYLISLQGRYNRHAAWVLNGVVIRIAQKMGIHRDGTMLGLPPFETEMRRRLWFQILSMEFKTALMSGLGHSLLPRVWDTQEPKNVNDADLHPSATEPVKDREGPTEMIFVLITNKVARFIVESPGIEPIFLYHDEKVKKIPGAPSEEKIKEFRGLIDGLSKSLLELTDKYCDPAAGPLHQYTIEFQDIIMQRIRESLEPGDATIETHIDHMFKMAVESFESTVVSYRNSCKVAYLWFLRLQFHNDLFTFLAGQLSQRPSGPLVDRAWETVENILPYHPELLKVNASKENLLLASLLVKGWNMREEYCSTQMGITLNTPPYIEHLRSVVPQDYVKSENSSPSALSRIPKANRMVTREAASDQLSVSGPMDPTFDEFIGNYLDGADWDVFSRINLENPAFPGVPATGITPQVNATASDILPSTRIDHTDPNQTSHQFAMYGIDPQSAWQ", "text": "FUNCTION: Transcriptional regulator; part of the gene cluster that mediates the biosynthesis of pyriculol and pyriculariol, two heptaketides that induce lesion formation upon application on rice leaves but are dispensable for pathogenicity (PubMed:27902426). With TRF2, negatively regulates the expression of the gene cluster and the subsequent pyriculol and pyriculariol production (PubMed:27902426). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSRIGKNPVVLPAGVEVTVGEQIVVKGPLGSLKTAAHSAVNVAVEGQNVTVSKVAGAANAAAMWGTMRANLNNMVTGVSKGFERKLQLVGVGYRAQAQGDTLNLSLGFSHPVAHKMPAGVKVECPTQTEILIKGSDKQQVGQVAAEIRAYRKPEPYKGKGVRYADEVVVIKETKKK", "text": "FUNCTION: This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. SIMILARITY: Belongs to the universal ribosomal protein uL6 family."}
{"protein": "MSTKDFNLDLVSVSKKDSGASPRITSISLCTPGCKTGALMGCNMKTATCNCSIHVSK", "text": "FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. SIMILARITY: Belongs to the type A lantibiotic family."}
{"protein": "MLLHFDIVIQLLSSHTLKSHQVEPPMDFETSFEEFVEDKRFIALEVSDNDDDCDTDLTADTADELESSAILKMRESDASLNVTTGNNTSRKTTSNSKKRWSLLSNHSAVSSSKSKKRWSVLSSSFTSESHKDRESRNVLQQKRKSLQSYSSLDTVASNSSISASSSLKRSSTGLSLRQLFTKIGINDDISQPGIGIPQGKENLPPTMGKKNSSIASTSSENRLRTPLKPLVNHSKRPTSQPQQQQPLYNASLSSRRSSISSTVSSSSSSKWRFWKRNKNQTPALLQPDHHSLKTFPAVNRRDSMTPVEPRNMVKHKTSFSDFHKTIFSSNTYSESSDTISSMEITLKNKASSSSLSLNVLKKRNSQSSLKHKSSHASLQKFKRNKGKSSMIAPSTATNSSNDDSCSYSSKNSTLSHRISLPVPDQVSRDKIQNKLRYSTSLLSLNSKSSLPMNKNDHDETLLRQILLNCDIKRILNPAKGDVLPLINDVNHLSSIQLTSNVWQIGEVICKKVSLGTIDDITWDRKFLSLQELEKLKIMQQKFDGIPQLLKSFVVKEANGGLYLYLLFKDHGTPISLISLKNWKQILKIFWSCAGIIHGLEKNLKFEHRNLTLDNILIDGNGNITIIDFKCSRLQTPQDDVLYLRLDHPLFFLNGKDKSKINEYQYQFEFEIYQSMRILLNMDASAFEPMTNLYWLYYLSRVLLKFGDRKLGKNDANRDKMARVINHLEMNLAVHKRGGQLFKRLETEDIKNTGDLLKLYK", "text": "FUNCTION: Serine/threonine haspin-like protein kinase involved in cell cycle regulation. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Haspin subfamily."}
{"protein": "MERLQGLLLWLLLSPSVVWASRGPLRPLCRPVNATLAAENEFCPVCITFTTSICAGYCPSMVRVLPAALPPVPQPVCTYRELRFASVRLPGCPPGVDPIVSFPVALSCRCGPCRLSSSDCGGPRTQPMTCDLPHLPGLLLF", "text": "FUNCTION: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
{"protein": "MMTALETRLSVADGTHAAALRQRLQAALAECRRELARGACPEHFQFLQQQARALEGGLGILSQLTED", "text": "FUNCTION: Chaperone of the type III secretion (T3S) injectisome that translocates effector toxins into host cells, facilitating the establishment and dissemination of infection. Prevents premature polymerization of PscF, along with PscG, within the cytoplasm (PubMed:20494986). Required for type III secretion needle assembly. Also required for cytotoxicity by influencing PscF levels. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YscE family."}
{"protein": "MLKSVHQKVARRTGPLLAWLKLLWVRIDEDHMTTLAGNLAYVSLLSLVPFVAVIFALFAAFPMFSDVSVQLRHFVFANFMPATGDIIQRYIEQFVANSSKMTAVGALGLIVTSLLLMYAIDSALNTIWRSTRQRPKVYSFAVYWMILTLGPLLAGASLVISSYLLSLRWASGFNTMIDDVLRIFPLLLSWLSFWLLYSVVPTTRVPARDALIGSLVAALLFELGKKGFALYITMFPSYQLIYGVLAVIPILFLWVYWTWCIVLLGAEITVTLGDYRKLRQAAREEAESV", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0761 family."}
{"protein": "MVGREKELSIHFVPGDCRLVEEEVNIPNRRVLITGATGLLGRAVYKEFQQNNWHAVGCGFRRARPKFEQVNLLDSNAVHHIIYDFQPHVIVHCAAERRPDVVENHPDAASQLNVDASGNLAKEAAAIGAFLIYISSDYVFDGTNPPYREEDIPNPLNLYGKTKLEGEKAVLENNLGAAVLRIPVLYGEVERLEESAVTIMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVVGAQRPRNAQLDCSRLETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH", "text": "FUNCTION: Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine. Can bind NADP (in vitro). SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family. MAT2B subfamily."}
{"protein": "MKIDLNADLGEGCASDAELLTLVSSANIACGFHAGDAQTMQACVREAIKNGVAIGAHPSFPDRENFGRSAMQLPPETVYAQTLYQIGALATIARAQGGVMRHVKPHGMLYNQTAKEAQLADAIARAVYACDPALVLVGLAGSELIRAGKQYGLTTREEVFADRGYQADGSLVPRSQPGALIENEEQALAQTLEMVQHGRVKSITGEWATVTAQTVCLHGDGEHALAFARRLRSTFAEKEIVVAA", "text": "FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. SIMILARITY: Belongs to the LamB/PxpA family."}
{"protein": "MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGGKVQSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILIGDKSENVQDLLLLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNAVESYTYNIKQTVEDEKLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQKELERVCNPIISKLYQGGPGGGGSSGGPTIEEVD", "text": "FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). Plays a role in spermatogenesis (PubMed:24557841). In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (PubMed:24557841). FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. In the ATP- bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Note=Colocalizes with SHCBP1L at spindle during the meiosis process. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Note=Colocalizes with SHCBP1L at spindle during the meiosis process (PubMed:24557841). SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MPFHNPFIKDGQIKFPDGSSIVAHVERWAKVRGDKLAYRFLDFSTERDGVPRDLTWAQFSARNRAVAARLQQVTQPGDRVAILCPQNLDYLVAFFGALYAGRIAVPLFDPSEPGHVGRLHAVLDNCHPSAILTTTEAAEGVRKFFRTRPANQRPRVIAVDAVPDDVASTWVNPDEPDETTIAYLQYTSGSTRIPTGVQITHLNLATNVVQVIEALEGEEGDRGLSWLPFFHDMGLITALLAPMIGHYFTFMTPAAFVRRPERWIRELARKEGDTGGTISVAPNFAFDHAAARGVPKPGSPPLDLSNVKAVLNGSEPISAATVRRFNEAFGPFGFPPKAIKPSYGLAEATLFVSTTPSAEEPKIITVDRDQLNSGRIVEVDADSPKAVAQASAGKVGIAEWAVIVDAESATELPDGQVGEIWISGQNMGTGYWGKPEESVATFQNILKSRTNPSHAEGATDDATWVRTGDYGAFYDGDLYITGRVKDLVIIDGRNHYPQDLEYSAQEASKAIRTGYVAAFSVPANQLPDEVFENAHSGIKRDPDDTSEQLVIVAERAPGAHKLDIGPITDDIRAAIAVRHGVTVRDVLLTAAGAIPRTSSGKIGRRACRAAYLDGSLRAGKVANDFPDATD", "text": "FUNCTION: Involved in the biosynthesis of mycolic acids (By similarity). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (By similarity). Can use decanoate (C10), dodecanoate (C12) and tetradecanoate (C14) (PubMed:23364516, PubMed:26900152). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MSRPLIADIDLDALRRNYCLARDQAPHSRAIAVVKADAYGHGAVACADALRDLAPAFAVACLEEALTLREAGITQPIVLLEGFFDAAELSLIDAHRLWTAVHSDWQIDALLAYRPRQPIPTWLKLDSGMHRLGFAPEAFEARWQRLAAATEHVTDLHLMTHFATADALDAAYFRRQMACIASLRQRLEAPVCLANSPATLAWPEAHGDWNRPGVMLYGSDPLEGANDASRALEPVMTLRSEIIAVRELAEGEAVGYGGRWRASRPSRIGVVAGGYGDGYDRHARDGTPVLVEGQRVPLAGKVSMDMLTVDLTELPEAGIGSPVVLWGEGLPIDEVARHCDTISYTLMTGVLPRVPRRYRNAETG", "text": "FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. SIMILARITY: Belongs to the alanine racemase family."}
{"protein": "METSMPEYYEVFGDFHGVLVDKLFTKYWEDVETFSARPDDLLVVTYPKSGSTWIGEIVDMIYKEGDVEKCKEDAIFNRIPYLECRNEDLINGIKQLKEKESPRIVKTHLPAKLLPASFWEKNCKIIYLCRNAKDVVVSYYYFFLIIKSYPNPKSFSEFVEKFMEGQVPYGSWYDHVKSWWEKSKNSRVLFMFYEDMKEDIRREVVKLIEFLERDPLAELVDKIIQHTSFQEMKNNPCTNYSMLPETMIDLKVSPFMRKGIVGDWRNHFPEALRERFEEHYQRHMKDCPVTFRAEL", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. May play a role in the regulation of estrogen receptor activity by metabolizing free estradiol (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfotransferase 1 family."}
{"protein": "MAKTIVIKQIGSPIRRPAKQRATLIGLGLNKMHKTRELEDTPSVRGMINSIPHMVEIVEEKG", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MSNTIVVVGAGVIGLTSALLLSKNKGNKITVVAKHMPGDYDVEYASPFAGANHSPMATEESSEWERRTWYEFKRLVEEVPEAGVHFQKSRIQRRNVDTEKAQRSGFPDALFSKEPWFKNMFEDFREQHPSEVIPGYDSGCEFTSVCINTAIYLPWLLGQCIKNGVIVKRAILNDISEAKKLSHAGKTPNIIVNATGLGSYKLGGVEDKTMAPARGQIVVVRNESSPMLLTSGVEDGGADVMYLMQRAAGGGTILGGTYDVGNWESQPDPNIANRIMQRIVEVRPEIANGKGVKGLSVIRHAVGMRPWRKDGVRIEEEKLDDETWIVHNYGHSGWGYQGSYGCAENVVQLVDKVGKAAKSKL", "text": "FUNCTION: This enzyme can effectively convert cephalosporin C into 7- beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the DAMOX/DASOX family."}
{"protein": "MDLQQLEEQARQAALKDIQNMLQRPGQLEKVEQYRHRIARKKASVEALLKTGMQGQLDGVRVGLKQLETCMQDVREVRRRMDEVERLLRGVPEVYDALEVVREENTKHSQYATAMENLKHIFNVDASVQKTMALIEDDKLLNAHQCLADLENSRDDLLYELHKQPKQHASDKITLKRHFEKVDTVSQELEKKLRLILSRTLNTLRKKPTIIVTALRIIEREEKNDQFALQQQKVTGFLPPGRPKAWRRMIMDVLQQSVITRIEGSKLEERADNKMWLVRDLEILRQIILEDLRVVKSLCVPCFPPHYDIFGEYVKFYHEGLSSYLDNIVRSGLEGNEYVSMMAWVTHTYPGVELMSHPDLNVDVHRQIGTLLRPEHLKALEDEYLQNMQRNFQEWMTKAAETEKQEWFTETVPDQDEEYYHTSAPVIIFQMIDQHLQVTNTIHQELTFKALVMSIQQVEIFGQTYLKNVIELKEHHFRNRDQIKYFTHYIITIVNNSQQMVELAQQMKQLYWPKSRTEHYEDFERLLATFQRIRAHAASYLLEEAFLDMECHFNDLFTAKWLASNIAVDTICVTLDDYFQDYNHLRPNNFEMVINEAQKLLAKRYIRALLSKRLSKPRAECDAITRKIKTEAKRFKLFFEKIAPKISLSDSPLDLISTLSALLSSDIELLVLDLHTLLGSYPSLNEDHLVRLFYIRNDVKAAEVREKVQDAMKSKKAMVSIAKQDCIFKEIVFSDKLW", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SIMILARITY: Belongs to the SEC6 family."}
{"protein": "MSFIKKIFLSSRSSEDGLFFSKLEKILGFKPLNLTHFRRAFTHRSMNKLDEKGNPMNYERLEFMGDAMLGSVIAAHLFNMSPTGDEGYLTKMRSKIVSREHLNELGKDLNLIQFLESKVTLQNFGENIHGNLFEAFVGAIYLDRGFVYCEKFIHKKVIKPYVDIDKLEGKVISYKSLLIEWCQKEKRVFHYDIYEDEDAGKLKYFGVKLSIDGKVVAKARATSKKKAEEIASKRGYFVFQSEIDGK", "text": "FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease III family."}
{"protein": "MYIDTGIMSNNIFLFAFFALVGLTRIEAMPTKGSEGTWNVDYEDQEHTGITCRENEHYNSTRIECEDECNDRNNKLCYRFQQFCWCNEGYIRNSSHICVKLEDCLKDEEQKSETLASSANNDSSKRLEDDLKLFSHDSVSHTSLEPETQAQKFNGIIDQETLDLVFGKPENSSADNKPLETKTQAQKFNGIINEETLDLVFGKPENSWAENKPLETKTQAQKFNGIINEETLDLVFGKPENSWAENKPLETETQAQKFNGIINEETLDLVFGKPENSWAENKPLETKTQAQKFNGIINEETLDLVFGKPENSWAENKPLETKTQTQKFNGIIDQYTRRIVFVFSNI", "text": "FUNCTION: Counteracts the host humoral immune response by inhibiting the processing and the amidolytic activity of host PAP1 and PAP3. Thereby, melanization of host hemolymph, normally producing several reactive intermediates toxic for viruses, is deregulated and proper immune response cannot occur (By similarity). SIMILARITY: Belongs to the polydnaviridae EGF-like motif protein family."}
{"protein": "MSKSDVFHLGLTKNDLQGATLAIVPGDPERVEKIAALMDKPVKLASHREFTSWRAELDGKSLIVCSTGIGGPSTSIRVEELASTLGVDSRTLTPRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPMEFPAVETSTATRAGEARKSIGATTIGVTASDTFYPGQERYDTSGRERNSRSHIVRTLSILYQQQTYDTYSRVERFKGSMEEWQAMGVMNYEMESATVLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKSTESQFAVKIVVEAARRLL", "text": "FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PNP/UDP phosphorylase family."}
{"protein": "MVLTAGDKANVKTVWSKVGSHLEEYGSETLERLFIVYPSTKTYFPHFDLHHDSAQVRAHGRKVLSALGEAVNHIDDIPGALSKLSDLHAQTLRVDPVNFKLLNLCFVVVVGRHHPTILTPEVHVSLDKFLSAVATALTSKYR", "text": "FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SIMILARITY: Belongs to the globin family."}
{"protein": "MKSTAISRRYAKSLVNLAAPDGQLESTYTQLEQIQQAFACEPRLYKLLASPTLAADKIAGLLEGIGNYLQLSTTLRNLLGLLQQRQRLEYFDALVADYRELADVQLGLVRARVCSAAPLDAEVQQAISAQLQKRYGKQAVLELAVEPELLGGVRIEVAGQVLDGTIRSGLRRMAGYLNS", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase delta chain family."}
{"protein": "MPPRTAAERGGRRKSVKAPPPVDPLVELTTLESVHDALAKAERLRNYFQVERDKVNDFWTITKGEVETYRNRLFNAEASIEELERSHQVEMKVYKQRVRHLIYERKKKAQACQDESDRLLREAEDRHLQRMNEIQAKLQQQDQQLRAAAADHEMNVYEKRDSHSYMVTVTKTQSHEKELARLQVSCEAKLKVLRDELELRRRAEIHEIEERKNEHINALIKQHEEKFHEMKTYYNQITTNNLEIIHSLKEEIAQMKQNDEHNETLMYDIDRENQNLVAPLEEAQREVAELQQKRKQNEQNKRGLEVTRVKLRSLREEIRRQREEHQALEERYACVHREREELKGKFESALRQAVMVVEERNEVLQQKLIESHALVEERDVQLEGVLRAMNLEPKTLELIATEVDEWLQRKNQLIKDLHFELKKGEKLYSATLLEMERRCQTANIASLPRSNFE", "text": "FUNCTION: Cytoskeletal linker that plays a central role in the flagellum cell motility. Required for directional cell motility. Plays a role as part of a dynein regulatory system that regulates flagellar beat in response to signals from the central pair apparatus and radial spokes in procyclic cells. Also plays an essential role in the bloodstream form of the trypanosomes as its silencing is lethal for the circulating form. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, cilium, flagellum. Note=Associated with the cytoskeleton. Localized to the site of attachment of the flagellum to the subpellicular cytoskeleton. Also localized in the flagellum of the bloodstream form trypanosomes. SIMILARITY: Belongs to the DRC4 family."}
{"protein": "MTFLQLLIIAVVQGITEFLPISSSGHLILIPNFTEFPDQGPLIDVAVHVGSLLAIIVYFFKDVLTLARGGFASIGIGTDRPDAPSERRLFWWIVLGTIPAVAFGLAIKLGAFNSIAETWFNITVIDDDLMSSIRFTDLIAFNLIVYGIALGLADWLGKEVKKFEDMSWRDGLIVGIAQALAIIPGTSRSGVTMTAARALGYSRYESARFSFLLSIPAVAGAGVLIVPEIFEAGATLAMDALIAGVLTFIAAFLTMAFLMNFLKRASMLVFVFYRVAMGCALLAFF", "text": "FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family."}
{"protein": "MPTKAGTKSTANKKTTKGSSKSGSPRGHTGKTHAPPSMHSGMLYKDMVNIARSKGIPIYQNGTRLTKSELEKKIRRSK", "text": "FUNCTION: May play a role in genome packaging through direct interaction with viral DNA. Binds to ssDNA and dsDNA with the same apparent affinity in vitro. SUBCELLULAR LOCATION: Virion Note=Found in association with the viral nucleoid. SIMILARITY: Belongs to the asfivirus P10 family."}
{"protein": "MAENKKAVQRRIRAVKSTQQITKAMKMVDAAKLRRAQEKVQNARPYSRELAKTLGRLIQAGAGIDHPLLHRRTEGTPTVAYVLLTADRGLAGAFNINVIRKAHQALQKESRPTKLITIGRKGRDYFVKRKIQPVLEFVNLGDNITFALARSVLSKIVDLYLSGEVDEVRVIYTEFVNAVTQRPKEMQLLPIQPAQADGAHTHVEYIYEPSPERVLDTLVPRYAETMFYQLMLESKASEHGARMTAMGNATDNAEEMIAKLTLAYNRARQAAITREISEIVGGANALQG", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family."}
{"protein": "MAALVALCSGIGRKNLTTAAGCFTDRGTQAVSVIWRRCFSQFEQVTSNEDLPVPMENPYKEPLKKCVLCEKRVDYKNVQLLSQFISPFTGCIYGRHITGLCGKKQREITKAIKRAQKMGFMPVTYKDPAYLKDPRVCNIRYRE", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
{"protein": "MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNVLTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDADLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLSRAEERVLVRPHEPPPPPPMHAAGDARPTPTCVSSAAGLIENRPQSPAAGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPAPALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVTVAALAHPPSGLHPTPSPAPGPHAPLMPPSPPSQVLPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE", "text": "FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). Also involved in the regulation of mitochondrial dynamics (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Synapse Cell junction, focal adhesion Note=Dot- like pattern in the cytoplasm. Concentrated in Rac-regulated membrane- ruffling areas. Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2. In neurons, colocalizes with activated NTRK2 after BDNF addition in endocytic sites through the association with TMEM108 (By similarity). SIMILARITY: Belongs to the SCAR/WAVE family."}
{"protein": "MRAWLLLLAVLATFQTIVRVASTEDISQRFIAAIAPVAAEIPLASASGSGSGPGRSGSRSGGASTSTALAKAFNPFSEPASFSDSDKSHRSKTNKKPSKSDANRQFNEVHKPRTGQLENSKNKSKQLVNKPNHNNHNKMAVKEQRSHHKKSHHHRSHQPKQASASTESHQSSSIESIFVEEPTLVLDREVASINVPANAKAIIAEQGPSTYSKEALIKDKLKPDPSTLVEIEKSLLSLFNMKRPPKIDRSKIIIPEPMKKLYAEIMGHELDSVNIPKPGLLTKSANTVRSFTHKDSKIDDRFPHHHRFRLHFDVKSIPADEKLKAAELQLTRDALSPQVVASRSSANRTRYQVLVYDITRVGVRGQREPSYLLLDTKTVRLNSTDTVSLDVQPAVDRWLASPQRNYGLLVEVRTVRSLKPAPHHHVRLRRSADEAHERWQHKQPLLFTYTDDGRHKARSIRDVSGGEGGGKGGRNKRQPRRPTRRKNHDDTCRRHSLYVDFSDVGWDDWIVAPLGYDAYYCHGKCPFPLADHFNSTNHAVVQTLVNNMNPGKVPKACCVPTQLDSVAMLYLNDQSTVVLKNYQEMTVVGCGCR", "text": "FUNCTION: Acts as an extracellular morphogen to establish at least two cellular response thresholds within the dorsal half of the drosophila embryo. Required for the proper development of the embryonic dorsal hypoderm, for viability of larvae and for cell viability of the epithelial cells in the imaginal disks. Acts together with scw (By similarity). SUBCELLULAR LOCATION: Secreted. Note=Is internalized by receptor- mediated endocytosis. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MGIPWVEKYRPKAFSEIVNQEEAKTLLASWICARFRAPKEFCARWAKKREKEVAEAKAVLLAGPPGIGKTTVVHALAREIRYELIELNASDIRTGERIKLVVGRGLKESSLFGYEGKLVLFDEVDGLHVKEDEGGLEAIVEIVETAKVPIVMTANNPYDPKFRPLRDISLVVNLKRLSEEEVVEVLRRICTAEGAKCEEEALRSIAKSSLGDLRAAINDLQMYLSGGRKTLTVDDIKRVGERNPQLSMFEVLDRVYRARWFDEARAVSFNPSFDWEQYFLWALETVPVVYKDVETAAAAYDRLSKADMFLGRIKRMQEWELLPYALELALGGVSQVKNKPRLPPFIKYGFPQRLLLLAKSREARRRREALVEYLAQNLHISRSLARSDIIYVLSALARRDPKVVERLSRALGINAIDVKNLL", "text": "FUNCTION: Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. SIMILARITY: Belongs to the activator 1 small subunits family. RfcL subfamily."}
{"protein": "MDNTIPGGINITILIPNLMIIIFGLVGLTGNGIVFWLLGFCLHRNAFSVYILNLALADFFFLLGHIIDSILLLLNVFYPITFLLCFYTIMMVLYIAGLSMLSAISTERCLSVLCPIWYHCHRPEHTSTVMCAVIWVLSLLICILNSYFCGFLNTQYKNENGCLALNFFTAAYLMFLFVVLCLSSLALVARLFCGTGQIKLTRLYVTIILSILVFLLCGLPFGIHWFLLFKIKDDFHVFDLGFYLASVVLTAINSCANPIIYFFVGSFRHRLKHQTLKMVLQNALQDTPETAKIMVEMSRSKSEP", "text": "FUNCTION: Orphan receptor activated by a subset of RFamide-family neuropeptides such as FLRF-amide and FMRF-amide. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. May regulate the function of nociceptive neurons by modulation of pain perception. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily."}
{"protein": "MSEISIATSVPSGPGPLIGNQPDGPAKVIVRDLNFYYGQNHALKHINLSLAANRVTAFIGPSGCGKSTLLRVFNRMYDLYPGQRAEGQVMLDGNNILDPKLDLNLLRARVGMVFQKPTPFPMTIYENIAFGIRLYEKISKSEMDGRVEKALRSAALWNEVKDKLNASGLSLSGGQQQRLCIARTIAVRPEVILFDEPCSALDPISTAKIEELIDELKEDYTIAIVTHNMQQAARVSESTAFMYLGELIEFGPTNKIFTSPNDRRTQDYITGRFG", "text": "FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family."}
{"protein": "MGRLIFVSFGLLVVFLSLSGTAADCLSGWSSYEGHCYKPFNELKNWADAENFCTQQHAGGHLVSFQSSEEADFVVKLAFETFGHSIFWMGLSNVWNQCNWQWSNAAMLRYKAWAEESYCVYFKSTNNKWRSRSCRMMANFVCEFQV", "text": "FUNCTION: Anticoagulant protein which binds to the gamma- carboxyglutamic acid-domain regions of factors IX (F9) and factor X (F10) in the presence of calcium with a 1 to 1 stoichiometry. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
{"protein": "VNCGQVNKALSSCVPFLTGFDTTPSLTCCAGVMELKRLAPTVKDKRIACECVKTAAARYPNIREDAASSLPYKCGVVINVPISKTTNCHEIN", "text": "FUNCTION: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. SIMILARITY: Belongs to the plant LTP family."}
{"protein": "MAMNVSTTIGLLNATSFASSSSINTVKILFVTLFISIVSTIVKLQKSAANKEGSKKLPLPPGPTPWPLIGNIPEMIRYRPTFRWIHQLMKDMNTDICLIRFGRTNFVPISCPVLAREILKKNDAIFSNRPKTLSAKSMSGGYLTTIVVPYNDQWKKMRKILTSEIISPARHKWLHDKRAEEADNLVFYIHNQFKANKNVNLRTATRHYGGNVIRKMVFSKRYFGKGMPDGGPGPEEIEHIDAVFTALKYLYGFCISDFLPFLLGLDLDGQEKFVLDANKTIRDYQNPLIDERIQQWKSGERKEMEDLLDVFITLKDSDGNPLLTPDEIKNQIAEIMIATVDNPSNAIEWAMGEMLNQPEILKKATEELDRVVGKDRLVQESDIPNLDYVKACAREAFRLHPVAHFNVPHVAMEDTVIGDYFIPKGSWAVLSRYGLGRNPKTWSDPLKYDPERHMNEGEVVLTEHELRFVTFSTGRRGCVASLLGSCMTTMLLARMLQCFTWTPPANVSKIDLAETLDELTPATPISAFAKPRLAPHLYPTSP", "text": "FUNCTION: Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Can use L-valine or L-isoleucine as substrate, but not L-leucine, L-phenylalanine, L-tyrosine, D-valine or D-isoleucine. SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MIPGELMPLDGEIELNAGRPTVTVTVANTGDRPVQVGSHFHFYETNAALSFDREAARGYRLDIAAGTAVRFEPGQSRTVQLVALDGDRIVYGFNGRIMGAL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease beta subunit family."}
{"protein": "GLLSVLGSVAKHVLPHVVPVIAEKL", "text": "FUNCTION: Antibacterial peptide with wide spectrum of activity. Active against L.lactis, L.innocua, M.luteus, S.uberis and less against P.multocida and S.epidermidis. FUNCTION: Antibacterial peptide with wide spectrum of activity. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily."}
{"protein": "MSEWTKEQRYQKYEDVDQQTIEKLTEQVNQSEYRQTFHIQPQIGLLNDPNGLIYFKGNYYVSHQWFPLGPVHGLKYWYTYQSKDLVDFKAIGPTIKPDTKDDSHGVYSGSAFEYHDHLYYMYTANHRDSDWNRISTQHIAKMSKDGSINKFPKAVISAPPSGYTQHFRDPKVHVQDGVYYAMIAAQNIKKQGRILQYRSTDIVNWEFQGEVQTNLDDFGYMWECPDYFNLNGYDMLLFCPQGIDSEGERFKNIYQSGYIMGQYDINNLTMNHADFHELDYGFDFYAPQTFLDENGQRILIGWMGLPDINYPSDADGWAHCLTIPRVLTIESGNLKQRPIKALEKLRTNEETALGYANKFTRQLHPYEGKQFELIIDILENEATEVYFEVRTSKTESTLITYNKREQKLTLDRSESGQLPEPVEGTTRSTYLDTPLSKLQLFVDTSSVEIFCNDGERVMTARIFTDENATGIKTSTESGQTYLKFTKYDLKGDTI", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 32 family."}
{"protein": "MNKLSTKLVVAIGIGAALYGILGLWGFSIAPNTFIKPALAILTVFGALFGPVAGLLIGLIGHTVTDTIAGWGIWWGWVISSGIIGFSMGLIQKRVGFSVKNGSFNKGDISYLAITGLVGIVIAIIFAGAFDIIVMGEPFDKIVIQVLGATISDVIVFLVLGLPLTIGLAKSNKKHTHLKIEK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0397 family."}
{"protein": "MQLDEQRLRFRDAMASLSAAVNIITTEGDAGQCGITATAVCSVTDTPPSLMVCINANSAMNPVFQGNGKLCVNVLNHEQELMARHFAGMTGMAMEERFSLSCWQKGPLAQPVLKGSLASLEGEIRDVQAIGTHLVYLVEIKNIILSAEGHGLIYFKRRFHPVMLEMEAAI", "text": "FUNCTION: Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component or to other electron acceptors such as cytochrome c and Fe(3+) ion. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family. HpaC subfamily."}
{"protein": "MEQTYQYAWIIPFLPLPVPMLIGLGLLLFPTATKSLRRMWAFQSVLLLSIVMIFSINLSIQQINSSSVYQYVWSWIINNDFSLEFGYLIDPLTSIMSILITTVGILVLIYSDNYMSHDHGYLRFFAYMSFFSTSMLGLVTSSNLIQIYIFWELVGMCSYLLIGFWFTRPVAAKACQKAFVTNRVGDFGLLLGILGFYWITGSFEFRDLFQIFNNLISNNEVNFFFVTLCAVLLFGGAIAKSAQFPLHVWLPDAMEGPTPISALIRAATMVAAGIFLVARLMPLFIVIPHIMNFISLIGIITVFLGATLALAQKDIKRGLAYSTMSQLGYMMLALGMGSYRSALFHLITHAYSKALLFLGSGSVIHSMETLVGYCPEKSQNMVLMGGLTKHVPITKNSFLLGTLSLCGIPPLACFWSKDEILNDSWLYSPIFATIAWSTAGLTAFYMCRIYLLTFEGHLNVHFQNYSGKMNTPLYSISLWGKEGSKISNKNFPLVTLLKMKKNERTYFFSNKVYKIDENVRNQIQPFLSIPNFGNTKTSLYPYESDNTMLFPILILIIFTLFVGFLGIHFNQDVDILTKWLTPSINLLHKNSNNSIDWYEFSKDAVFSVSIASFGIFIAFFLYKPVYSSFQNLDLINSFVKISPKRIFYDKIKNAIYDWSYNRGYIDAFYGTFLTAGMRKLAEFTHFFDRRIIDGIPNGVGLMSFFVAEVIKSVGGGRISSYLFFYFSYVSIFLLIYYFVNL", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 5 family."}
{"protein": "MASSSSFTYYCPPSSSPVWSEPLYSLRPEHVRERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLILQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDMVMGVPENVLQPTHPVYNIGPEKVIQATTHFLQKPVPGFEECEDEVTSDPATD", "text": "FUNCTION: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. SIMILARITY: Belongs to the protein prenyltransferase subunit beta family."}
{"protein": "ANLLILQVSYAQKSSELVIGGDECNINEHRFLAFTYSRGFFCGGTLINQEWVLTATHCDRIFMRIYLGLHNQSVRYDDQQIRYPKEKYFFPCSKNFTKWDKDIMLIRLDRPVKNSEHIAPLSLPSNPPSVGSVCRVMGWGTITAPNDTYPDVPHCANINLFNYTVCRGAYKGLPATSRTLCAGVLQGGIDTCVGDSGGPLICNGQFQGIVFWGGDPCAQPRKPALYTKVFDHLHWILSIIAGNTTATCPP", "text": "FUNCTION: Snake venom serine protease that may impair the hemostatic system of the prey. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MDDLAQLQSCSNELATAITSLASYAGSGNTQQAINNQSPFEPEEVQRAKGNILAVATKLRTLICGPTDFLQHLASQVSEILACLRWLGEFQILACIPLMGSAPIKDIADLTNVPESRLRRIIRLTATAGFLREPERDHVAHTPLSASFFSNPSLLDAAMFLSESAAPIALQMPQTAQVKEKSSSPPSNGTPCDLALPRGTEFHTACKRRPKLNRQWLAYLHHAAGLHTADDIAAVLTQLDWPKLTNGRDGSIIEYAISRVDHCHAQVGVSSWSTSIARRLAHFYPALHFTVQISDPAVAITQEEFHPRITATSRILGTRQTAAGAAVYILHLPFASSSPSAVMTELAVHLDVLRSRSGILLILTPRLLPQPGSLPDPEVEATARSRDLALGQMADEGEMEMLELLETIDTVRDSLGKLVVTSKLRSRNNLVVAVTVEYQRDLPS", "text": "FUNCTION: Transcriptional coactivator; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer neosartorin, which exhibits antibacterial activity. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAIDAATVRKVARLARIATPEDRLEPLAQELNGIMTWIEQLAQVDTDGVEPLTSVVHAGLPLREDVVTMGGDADLITANAPKSTGGFFVVPKVVE", "text": "FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln). SIMILARITY: Belongs to the GatC family."}
{"protein": "MPQLVPFYFTNLLTFGMLAISMLLYLVSTIILPNILRLLVARTTMTKL", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase protein 8 family."}
{"protein": "MSDITTLSLTALRDKLARKELSAVEAASACLARIEATEPKIHALLHCDAEAALAAAKALDAAGPNPDQRLWGVPVLVKDAICVKDAPTTCGSKILENFTPFYDASCIEKMRAAGAVILGKANMDEFAMGSSTENSAYKVTANPWDLGKVPGGSSGGSAAAVAAGQCFAALGTDTGGSIRQPAAFCGTVGIKPTYGRVSRYGLVAYGSSLDQIGPLTRTADDAAAVLGVIAGPDPKDSTCAPRDVPDFEAALAGAADLAGLTIGLPDEYWGEGVDAEVRDACRAAVDTAKSLGANVVPVSLPHTPYAVATYYIVAMAEASSNLARFDGVRYGYRAPEAQSLEELYELSRSKGFGPEVQRRIVIGAYVLSAGYYDAYYRKAAQVRRLIRQDFLNAFEKCDVICGPTSPFAAFTIGQMSDDPLQMYLSDIFTISLNLAGLPGLSMPVGLGTTSAMPIGMQLFGRAFDEATILRTAKVLGNALPPLPQPAAV", "text": "FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). SIMILARITY: Belongs to the amidase family. GatA subfamily."}
{"protein": "MPRHCSAAGCCTRDTRETRNRGISFHRLPKKDNPRRGLWLANCQRLDPSGQGLWDPASEYIYFCSKHFEEDCFELVGISGYHRLKEGAVPTIFESFSKLRRTTKTKGHSYPPGPAEVSRLRRCRKRCSEGRGPTTPFSPPPPADVTCFPVEEASAPATLPASPAGRLEPGLSSPFSDLLGPLGAQADEAGCSAQPSPERQPSPLEPRPVSPSAYMLRLPPPAGAYIQNEHSYQVGSALLWKRRAEAALDALDKAQRQLQACKRREQRLRLRLTKLQQERAREKRAQADARQTLKEHVQDFAMQLSSSMA", "text": "FUNCTION: Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors. SUBCELLULAR LOCATION: Nucleus. Chromosome."}
{"protein": "GVPCRCDSDGPSVHGNTLSGTVWVGSCASGWHKCNTEHNIFHECCKE", "text": "FUNCTION: Binds voltage-dependently at site 3 of sodium channels (Nav) and inhibits the inactivation, thereby blocking neuronal transmission (By similarity). The minimum lethal dose against crabs is 7.3 mg/kg (Ref.1). SUBCELLULAR LOCATION: Secreted. Nematocyst. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type I subfamily."}
{"protein": "MKPLVLLSALVLLSFQVQADPIQNTDEETKTEEQSGEEDQAVSVSFGDREGASLQEESLRDLVCYCRTRGCKRRERMNGTCRKGHLMYTLCCR", "text": "FUNCTION: Has broad-spectrum antimicrobial properties. Has antibacterial activity against the Gram-positive bacterium L.monocytogenes EGD and the Gram-negative bacteria E.coli ML-35p and avirulent S.typhimurium 7953, but not against the mouse-virulent S.typhimurium 14028S. Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
{"protein": "MRKVKPKLNLTSQTARIVNLSHDGRGIARVNGKATFIQGALPGEMVEFQYTRVKKDFDEGKLLSIIEPSTLRVEPKCPHYQMCGGCSLQHMSAEEQIRFKQSHLLDLLSRYGHTEPQSMLSPLTSHHWNYRNKARLSTRFVEKKQSTMVGFRERNNPRFITEINQCPILNSKIDTDIVHLRKLIDTMEDKQCIAQIEVAAGDNEVALIFRNLTPLTEQDELKIRKFAEQFQYKVFLQPGGLDSVFCFYPSDAHAYLSYELPDYQITFQFHPNDFTQVNAELNRKMVTQAIQLMELKNSDIVLDLFCGLGNFSLPMAKHCSRVIGVEGNKNMVERAYMNAKSNHITNVDFYAANLDDVMEVRNLVNTSFSKVLIDPPRSGALEIVKQIDSIDPERIVYVSCNPITLARDTDILVNQKGYVLITAGVMDMFPHTAHVESIALFQKG", "text": "FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily."}
{"protein": "MPSSLPGSQVPHPTLDAVDLVEKTLRNEGTSSSAPVLEEGDTDPWTLPQLKDTSQPWKELRVAGRLRRVAGSVLKACGLLGSLYFFICSLDVLSSAFQLLGSKVAGDIFKDNVVLSNPVAGLVIGVLVTALVQSSSTSSSIVVSMVAAKLLTVRVSVPIIMGVNVGTSITSTLVSMAQSGDRDEFQRAFSGSAVHGIFNWLTVLVLLPLESATALLERLSELALGAASLTPRAQAPDILKVLTKPLTHLIVQLDSDMIMSSATGNATNSSLIKHWCGTTGQPTQENSSCGAFGPCTEKNSTAPADRLPCRHLFAGTELTDLAVGCILLAGSLLVLCGCLVLIVKLLNSVLRGRVAQVVRTVINADFPFPLGWLGGYLAVLAGAGLTFALQSSSVFTAAVVPLMGVGVISLDRAYPLLLGSNIGTTTTALLAALASPADRMLSALQVALIHFFFNLAGILLWYLVPALRLPIPLARHFGVVTARYRWVAGVYLLLGFLLLPLAAFGLSLAGGMELAAVGGPLVGLVLLVILVTVLQRRRPAWLPVRLRSWAWLPVWLHSLEPWDRLVTRCCPCNVCSPPKATTKEAYCYENPEILASQQL", "text": "FUNCTION: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane (PubMed:11880379). The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=ocalized at the brush border membrane in the kidney. SIMILARITY: Belongs to the SLC34A transporter family."}
{"protein": "MTGLLASRLRAEGARSPTKGTDIPMRQPSAEDLDAAHQLVSSARGGRDNVMNFRSDRQEMTGKALDNTQGDGSRNMDSQLQNGHKAPVEQRAGESPPESGANPIDHPTSSKKSPKAQSKEQAFTGHSCSNCGTKRTPLWRRSPTGATICNACGLYLKARNTDRPTHRSRSLLTPYGSSSAQTLDKSRSSTSPTNDGNDPRLTDTWSNYAVKECTPSGSCPGGGSCNGTGGAEGCDGCPAYNNRVYKSAARNAMALHTPRTSPQVSTQGGPGSTEGDAGSSNPETMTLHIACQNCQTTVTPLWRRDENGHPICNACGLYHKLHGAYRPPTMKKSIIKRRKRVVPAMREQSPPSATQSSNGSVSPEASPAALAHNHDSHRQYQNVEHGNGHPPPHTRPLYSHAYHAPPPADFTGYTSNVISLPHHPPSTSQQLRPYDNNHNNGETTNTHRAPMPALHNPKKRTISESSIEDSQRPQASQILTHIPQINPPTPPSSSSASFPNNNPGRFNSISSLLNHPGEAATVTAHDRDDSRVDPALSSAVAPRTQQPQQEHQHASAGSHSPPRFSPSLSPAPPSTTAVPVGGGSGSGAAAVAGVVDHRDAKAERRARLQREAQDMREALKAKERELALLE", "text": "FUNCTION: GATA-type transcription repressor that regulates iron- acquisition genes through specific binding the GATA sequence element 5'-(G/A)ATC(T/A)GATAA-3' of target promoters in an iron- and zinc-dependent manner (PubMed:18549241, PubMed:22117028). Regulation occurs via direct binding of iron ions (PubMed:18549241). Iron acquisition regulation is critical for survival under both iron- limiting conditions (to acquire essential iron) and iron-replete conditions (to limit iron toxicity) (PubMed:22117028). SRE1 targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis, presumed ferric reductase activity, iron-responsive transcriptional regulation, oxidative stress response, as well as genes encoding a number of putative oxidoreductases, metabolic and mitochondrial enzymes, superoxide dismutase, and genes previously identified as induced during nitrosative stress (PubMed:22117028). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRGIILALLLAIAGSERTQIEPVFSESKTSVYNYEAVILNGFPESGLSRAGIKINCKVEISAYAQRSYFLK", "text": "FUNCTION: Precursor of the major egg-yolk proteins that are sources of nutrients during early development of oviparous organisms."}
{"protein": "MRLVFAGTPEPALPSLQRLIASPRHEVVAVLTRPDAAAGRRGRPTPSPVARLALDHDIPVLRPPKPNSEEFVAELRELAPDCCAVVAYGALLSERLLAVPPHGWINLHFSLLPAWRGAAPVQAAIAAGDAVTGATTFLIEPALDSGPVYGVVTETIRANDTAGELLTRLAESGAHLLESTLDGIADGRLQAVPQPADGVTVAPKITVDEARVRWDLPAHVVDRRIRAVTPNPGAWTVIGDARVKLGPVAPESAEPLAPGAIRVLKNAVHVGTATEPVRLGTVQPPGKKPMNAADWARGARLDASVSAQ", "text": "FUNCTION: Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. SIMILARITY: Belongs to the Fmt family."}
{"protein": "MIDKAYEELIKMKEKIMRDSYTIHKELSESVESILNELWINYSPESVEHSKKLLAIDGGMWVKETRQGVIFIVNAKAIVFEGINEINSEGKVLVHIFSPGNYAKERIELLMQLLELQLALKLVENVDYVLLDGSFSKKLGRHKSELKVDLLDDIVSIDKILSLEEKDEDNMLRFLIAENQLVLSELVSRYKDKLLFISKNSKSSDLFKQAYSDITILELFTQNCGYSKILEKKIDENYILSRKASKLLSGLNYYFTNLRLEPSERLFRLDFFNADKIFEYLKVLKPVSLKGYPYPLIKVHKDVRVGKEDRERIYSILEMKRKDISWWPSQFY", "text": "FUNCTION: Involved in DNA double-strand break (DSB) repair (PubMed:12052775). Acts probably with HerA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits both single-stranded endonuclease activity and 5'-3' exonuclease activity on single-stranded and double-stranded DNA (PubMed:12052775). SIMILARITY: Belongs to the NurA family."}
{"protein": "MKRRELIRTAFSTIVATAALSSVSARARSEDLHGLTLKKVPPDAIPKNDVPIFSPDDVFTMPEQFWRDFKGKLYIGKAGTDPTLPQNLIDVFVKNANGGTALLSQPIDLNSETLKTFVAAKGALWSASEYSMALHNDNDEQIFYVPDVKNNGVSEFSRRLSQPGGYQLIGEISSFASLRQTRPLFSGAKVRLKGWHDGTEVGGGAFVGEMTPSEDDGGYIASSGQDFHWRRVSDDMNRITLFDFGAVADGKKDCLPAVMAMYHWAQNNNQKLSIQFPAGRFFISSFDISAKYIRFLRLAGAPVNFGYFPATTLVSDGKSEFLFKVNARWVELSNISFEGQIEHSPNGQGFFHNICPAGQYFRGSCLRFTGVGGVSLSLIDTLDCKIDQWYASKCTGDVIRGSWSFTKKGNWDHNTAIELSNFNVQHCRQGKVLNLPRCTQSIIHNGWIEHSEFPGDLSNGQWIVDALSLEGCKNPLIAHCSRLNMRQTNLQSGSWIDNSLANDEWLSSFERGSTRVESYGIAVDGSMKYNYLTSRFRIENHSSQEKWYELGNIHTPDVGDSWEIEVFGQSQFSNGSGTKALMSVTDDRHTGGKAIINLQRKIHGFEASWSVEGSSPINDVVYTTSNDSDTRVFVKLAQWLGSAGVMIKTTAKDRFVTGHCARFDSRMVHSEPPKGEKVHSAVRRFSLHNGLAGIGANEQGDLLVESRHIDAAKVETSRAEGYISLVINGQQVAVPYFALKQNS", "text": "FUNCTION: Involved in the biosynthesis of amylovoran which functions as a virulence factor. May be involved in the polymerization or late modification of the repeating units. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: To R.meliloti ExoP."}
{"protein": "MNFNNKTKYGKIQEFLRSNNEPDYRIKQITNAIFKQRISRFEDMKVLPKLLREDLINNFGETVLNIKLLAEQNSEQVTKVLFEVSKNERVETVNMKYKAGWESFCISSQCGCNFGCKFCATGDIGLKKNLTVDEITDQVLYFHLLGHQIDSISFMGMGEALANRQVFDALDSFTDPNLFALSPRRLSISTIGIIPSIKKITQEYPQVNLTFSLHSPYSEERSKLMPINDRYPIDEVMNILDEHIRLTSRKVYIAYIMLPGVNDSLEHANEVVSLLKSRYKSGKLYHVNLIRYNPTISAPEMYGEANEGQVEAFYKVLKSAGIHVTIRSQFGIDIDAACGQLYGNYQNSQ", "text": "FUNCTION: Specifically methylates position 8 of adenine 2503 in 23S rRNA. Confers resistance to some classes of antibiotics. FUNCTION: Specifically methylates position 8 of adenine 2503 in 23S rRNA. Confers resistance to some classes of antibiotics, such as chloramphenicol, florfenicol, clindamycin and linezolid. FUNCTION: Specifically methylates position 8 of adenine 2503 in 23S rRNA. Can also methylate position 2 of A2503 after the primary methylation at position 8 is complete, to form 2,8-dimethyladenosine; however, C8 is its preferred target. Confers resistance to several classes of antibiotics such as phenicols, lincosamides, oxazolidinones, pleuromutilins, and streptogramin A. The antibiotic resistance conferred by Cfr is provided by methylation at the 8 position and is independent of methylation at the 2 position of A2503. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. Cfr subfamily. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. Cfr subfamily."}
{"protein": "METPAFFFTTFLGCLLLSITGYSIYVGFGPPSKQLRDPFEEHED", "text": "FUNCTION: May play a role in photosystem I and II biogenesis. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbN family."}
{"protein": "MLAIFNIYLDNAFHLNGIILAKLPEAYAIFDPIVDVMPIIPVFFFLLAFVWQASVSFR", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbK family."}
{"protein": "MLGKRKRVVLTIKDKLDIIKKLEEGISFKKLSVVYGIGESTVRDIKKNKERIINYANSSDPTSGVSKRKSMKSSTYEELDRVMIEWFNQQKTDGIPVSGTICAKQAKFFFDALGMEGDFNASSGWLTRFKQRHGIPKAAGKGTKLKGDETAAREFCGSFQEFVEKENLQPEQIYGADQTGLFWKCLPSRTLTLETDQSTSGCRSSRERIIIMCCANATGLHKLNLCVVGKAKKPRAFKGTDLSNLPVTYYSQKGAWIEQSVFRQWFEKYFVPQVQKHLKSKGLLEKAVLLLDFPPARPNEEMLSSDDGRIIVKYLPPNVTSLIQPMSQGVLATVKRYYRAGLLQKYMDEGNDPKIFWKNLTVLDAIYEVSRAWNMVKSSTITKAWKKLFPGNEENSGMNIDEGAILAANLATVLQNTEECEHVDIENIDQWFDSRSSDSSCQVLTDSESAEDQTKAAEQKPSSKSRKTELNPEKHISHKAALEWTENLLDYLEQQDDMLLSDKLVLRRLRTIIRKKQKIQNNKNH", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the tigger transposable element derived protein family."}
{"protein": "MRVKEIRKNYQHLWRWGIMLRWGTMLLGMLMICSAAEQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEAHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNNMVEQMHENIISLWDQSLKPCVKLTPLCVTLHCTDLRNTTNNNSSIEEKMKGEIKNCSFNVTTNIRDKVQKEYALFYKLDVVPIDNDNNSTNTCYRLISCDTSVITQACPKVSFEPIPIHYCTPAGFALLKCNNKTFNGTGPCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEGVVIRSENFTDNVKTIIVQLNETVKINCIRPNNKTRKRVTMGPGRVYYTTGEIIGDIRQAHCNISRAEWNKTLEQIANKLRKQFENKTIVFNQSSGGDPEIVMHNFNCGGEFFYCDSSQLFNSTHLSNGTWWNGTGPENITLPCRIKQIVNMWQEVGKAMYAPPIRGQIRCSSNITGLLLTRDGGNTQNNNTNSSIEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRAKRRVVQREKRAVGIGAVFLGFLGAAGSTMGAAAVTLTVQARQLLPGIVQQQNNLLRAIDAQQHLLQLTVWGIKQLQARVLAVERYLKDQQLMGIWGCSGKFICTTAVPWNTSWSNKSFNEIWDNMTWMEWEREINNYTNLIYNLIEESQNQQEKNEQDLLALDKWDSLWNWFSITKWLWYIKIFIMIVGGLVGLRIVFTVLSIVNRVRQGYSPLSFQTRLPARGPDRPEGIEEEGGERDRDRSGPLVDGLLALIWVDLRSLCLFSYHRLRDLLLIVTRTVELLGRKGWEVLKYLWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEILQRTYRAILHIPVKIRQGLERALL", "text": "FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Host endosome membrane; Single-pass type I membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. SIMILARITY: Belongs to the HIV-1 env protein family."}
{"protein": "MNIEQFQSMLGERGISLSPRQLEQFEMYFETLVEWNEKMNLTAITEKEEVYLKHFFDSITAAFYYDFSNPLSICDVGAGAGFPSIPLKICFPHLKVTIVDSLQKRINFLNHLAQKLELSDVAFCHDRAETFGKKEHVRESYDIVMARAVARLSVLSELCLPLVKVGGTFIAMKGAAANEEIENGKYAVEVLGGQLEEVSTFQLPFEESERNILLIKKKRKTPKKYPRKPGTPNKLPIEK", "text": "FUNCTION: Specifically methylates the N7 position of guanine in position 535 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family."}
{"protein": "MKQILFMDTTLRDGEQSPGVNLNEQEKLQIARQLEKLGIDVMEAGFAAASEGDFQSVKRIAESIQNASVMSLARAKESDIRKAYEAVKRAVSPRLHVFLATSDIHMKYKLCMSKEDVLDSIHRSVILGKSLFPTVQFSAEDATRTAQPFLAEAVEVAIRAGADVINIPDTVGYTHPEEYYSLFQYLQESVPSYEKAIFSCHCHDDLGMAVANSLAAIEGGALQVEGTINGIGERAGNAALEEVAVALHIRKDHYKTQSSIILKEIKATSTLVSRLTGMMIPKNKAIVGANAFAHESGIHQDGVLKEVTTYEIIAPELIGESQNLFVLGKHSGRHAFTERMKELGYELTQKERDAAFEAFKALADRKKEITDEDLRALMLGEAALLTQQYNIKQLQVHFVSNHIQCATVVLQDGKGNKYEDAATGAGSIEAIYHAIQRILEMECKLVDYRIQSITQGQDALAHVHVELKEGPHQVSGFGVAQDVLEASARAYVHAAGKLKALLTLVK", "text": "FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily."}
{"protein": "MKLTKLLTYLKNVPSYAGQEDPDITSIEMDSREVKTGSLFVCIKGYTVDGHDYARQAAEKGAAAIVAEREVDADVPVIIIRHTKRALAVLSDAFYGQPTKQLRLIGITGTNGKTSTSHMVEEIFRKAGSRTGLIGTMYTKIHDETFEAKNTTPESVTLQKTFRKMVDQGVDTAVMEVSSHALHMGRVHGCDYDIAAFTNLTQDHLDYHETMEEYKHAKSLLFSQLGGSFNHETPKWAVLNADDPASAYFAQVTSAHLLTYGIQNDADVMAENIKMAPKGTTFDLVTPKGSAQVTIPLVGLFNVYNVLTAAAIAIAADIPFATITEGIEGLKGVRGRFELVDAGQDFPVIVDYAHTPDSLENVLNTCRGLTEGKLFVVVGCGGDRDKTKRPKMAKIAVDLADEPVFTADNPRSENPLAILNDMEEGVKGAYYHSIVNREQAIFFAIANAKKGDVVLIAGKGHETYQQIGGQTFDFDDAEVAKRAILELK", "text": "FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family. MurE subfamily."}
{"protein": "MLISKTLIFYQVVNIVSQKGSGKRRWKMENGDRYVYVVDVSKCYGCLSCVAACAAENNVPVGYFRTWVERYAMNGRVAFVPKICNHCDNPSCVHACPVNATYKTEEGLVLIDDEICIGCGACIQACPYGARFRNPVKGTADKCTLCNHRIPERLPACVESCPTSARVYGKMSDKAVKEILSKKNAVVLKAYTGNEPHTYYVSLTGVE", "text": "FUNCTION: Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrB is probably involved in transfer of electrons from TtrC to TtrA (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein."}
{"protein": "MNGEQSANGARTLPDDAVVVVPVSNVIFPGVVFPIVLDRPSAVAAAQQALREQHPLVLVLQQDVQAPDPGPQSLHRMGTLANVLRYVTGPDGAPHVACQGVERFEIDEWVEGFPFLVARGRRIPEPEAEGAAIEARFLHLRSQALEALQLLPQSPPGELVAAVEGASSPAALADLVAAYLDLQPPEKQQILETIDLEARLDKVSAFLAQRLEVLRLTSEIAQRTRQSLGERQRETLLREQMAAIQRELGEGEREELVELEAAIENAGMPEEVVQQARKELRRLARTPEAAAEYGMVRTYLEWLVELPWGVPEAAPIDLAEARRILDEDHFGLEKIKQRIIEHLAVRRLAPEGKAPILCFVGPPGVGKTSLGQSIARAMHRPFVRVSLGGVHDESEIRGHRRTYVGALPGNIIQAIRKAGRRDCVMMLDEIDKMSAGIHGDPSAALLEVLDPEQNVAFRDNYLAVPFDLSRVVFIATANMLDTIPGPLRDRMEVIQLSGYTAGEKRQIAERYLVRRQLEANGLTAEQVQIEPAALETLIARYTREAGVRSLEREIGRLLRHVAVRFAEGHTEPVRIGPTNLEPILGPPRVENEVAMRTSVPGVATGLAWTPVGGEILFIEATRTPGDGRLILTGQLGEVMRESAQTALSLVKSRAEALGVTPSLFKESDIHIHVPAGATPKDGPSAGVAMTMALISLLTDRTVRSDTAMTGEISLRGLVLPVGGIKEKVVAAATAGVRRVLLPARNRADERDIPEETRQTLELIWLERIEDAIEAGLDPRRGDVRQTQVRAAS", "text": "FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S16 family."}
{"protein": "MLILGSHVSLKGNDMFYGSVLEALEYNANTMMVYTGAPQNTIRKPIETMKIEEAHALMKEKGIDLNHVVVHAPYIINLCNPDPERRAFAVEFLTKEVIRVGQMGINQMVLHPGSAVGGNREEAVQWISEGLNQIIDNTKSYNVRIALETMAGKGNEIGKTFEEIKAIIDGVDDKSRVSVCFDTCHVHDAGYDVIHDLDKTLQLFDDIVGLNYISVVHVNDSKNELGASKDRHENIGFGYIGYDALLKVIYHEAFKEIPKILETPYVNDKPPYKLEIQMIKDRVFDNELKTKLEK", "text": "FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. SIMILARITY: Belongs to the AP endonuclease 2 family."}
{"protein": "MPKSEIHPKWYPDAKVICNGEVVMTTGSTQPELHVDVWSGNHPFFTGTQKILDTEGRVDRFMKKYGMGSANSATSKEQKEEKDSNK", "text": "FUNCTION: Binds the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily."}
{"protein": "MSDPFAQAQHQLDALGLRCPEPVMMVRKSVRKMNEGETLLIIADDPATTRDIPSFCEFMDHTLIASQTESTPYQYLIKKGL", "text": "FUNCTION: Sulfur carrier protein which probably makes part of a sulfur- relay system. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfur carrier protein TusA family."}
{"protein": "MAETSLLEAGASAASTAAALENLQVEASCSVCLEYLKEPVIIECGHNFCKACITRWWEDLERDFPCPVCRKTSRYRSLRPNRQLGSMVEIAKQLQTVKRKIRDESLCSQHHEPLSLFCYEDQEAVCLICAISHTHRPHTVVPMDDATQEYKEKLQKCLEPLEQKLQEITCCKASEEKKPGELKRLVESRRQQILKEFEELHRRLDEEQQTLLSRLEEEEQDILQRLRENAAHLGDRRRDLAHLAAEVEGKCLQSGFEMLKDVKSTLEKCEKVKTMEVTSVSIELEKNFSNFPRQYFALRKILKQLIADVTLDPETAHPNLVLSEDRKSVKFVETRLRDLPDTPQRFTFYPCVLATEGFTSGRHYWEVEVGDKTHWAVGVCRDSVSRKGELTPLPETGYWRVRLWNGDKYAATTTPFTPLHIKVKPKRVGIFLDYEAGTLSFYNVTDRSHIYTFTDTFTEKLWPLFYPGIRAGRKNAAPLTIRPPTDWE", "text": "FUNCTION: E3 ubiquitin-protein ligase (By similarity). May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1 (By similarity). Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (By similarity). Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Mitochondrion Nucleus Note=Found predominantly in the cytosol. Partial shift from the cytosol to the mitochondria when colocalized with MOAP1. Colocalizes with CDKN1A in the nucleus. SIMILARITY: Belongs to the TRIM/RBCC family."}
{"protein": "MTATIDNTQSQATTGGVGRVARVIGPVVDVEFAADELPEIYNALTVDVDFATASEQVEGETKRTLTLEVAQHIGDNMVRAISLQPTDGLVRGALVRDTGAPISVPVGDVTKGHVFNVLGQTLDVPRIEVTERWPIHRPAPAFDQLEAKTEMLETGIKVIDLLTPYVRGGKIGLFGGAGVGKTVLIQEMIHRVAKNFGGVSVFAGVGERTREGNDLFLEMTESGVINDTVLVFGQMDEPPGCRLRVGLAALTMAEYFRDVKRQDVLLFIDNIFRFVQAGSEVSTLLGRMPSAVGYQPTLADEMGALQERITSTRGHSITSVQAIYVPADDITDPAPHTTFTHLDATTVLSRPISEKGIYPAVDPLDSTSRILDPQFIGEEHFRVANQVKQILQRYKDLQDIIAILGIDELSEEDKVIVGRARRIERFLSQNMFVAEAFTGQPGSFVPLDETIDAFRRLCEGELDHLPEQAFFMCGGLDDVQAKAKRLAERS", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MSRFFSSNYEYDVASSSSEEDLLSSSEEDLLSSSSSESELDQESDDSFFNESESESEADVDSDDSDAKPYGPDWFKKSEFRKQGGGSNKFLKSSNYDSSDEESDEEDGKKVVKSAKEKLLDEMQDVYNKISQAENSDDWLTISNEFDLISRLLVRAQQQNWGTPNIFIKVVAQVEDAVNNTQQADLKNKAVARAYNTTKQRVKKVSRENEDSMAKFRNDPESFDKEPTADLDISANGFTISSSQGNDQAVQEDFFTRLQTIIDSRGKKTVNQQSLISTLEELLTVAEKPYEFIMAYLTLIPSRFDASANLSYQPIDQWKSSFNDISKLLSILDQTIDTYQVNEFADPIDFIEDEPKEDSDGVKRILGSIFSFVERLDDEFMKSLLNIDPHSSDYLIRLRDEQSIYNLILRTQLYFEATLKDEHDLERALTRPFVKRLDHIYYKSENLIKIMETAAWNIIPAQFKSKFTSKDQLDSADYVDNLIDGLSTILSKQNNIAVQKRAILYNIYYTALNKDFQTAKDMLLTSQVQTNINQFDSSLQILFNRVVVQLGLSAFKLCLIEECHQILNDLLSSSHLREILGQQSLHRISLNSSNNASADERARQCLPYHQHINLDLIDVVFLTCSLLIEIPRMTAFYSGIKVKRIPYSPKSIRRSLEHYDKLSFQGPPETLRDYVLFAAKSMQKGNWRDSVKYLREIKSWALLPNMETVLNSLTERVQVESLKTYFFSFKRFYSSFSVAKLAELFDLPENKVVEVLQSVIAELEIPAKLNDEKTIFVVEKGDEITKLEEAMVKLNKEYKIAKERLNPPSNRR", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm Note=Mainly cytoplasmic. SIMILARITY: Belongs to the eIF-3 subunit C family."}
{"protein": "MSTWGFASPTPDRFAVSAEAEDKVREQQTRLERIFNVGMSVLSKDCPENPHIWLQLEGPKENVCRAKEYLKGLCSPELQSEIHYPPRLHCIFLGAHGFFLDCLAWSTSAHLVPLLPGSLMISGLTEAFVMAQSRVEELVQRLSWDLQLQSCPGAPDNGGVLRDFSALLQTREDAYTEALLRLPLAVQEELLSLVQEASRGQGPSREVGSSGLLSPQFQGVRAPLNEGREFVGTRVAGSGKSPAVRGQSHTVEKEERKQDAVRDMGSGRKELSGEEVWEPGVAYRSQLAGGGAEEVAPLKGKASGKQEVPQQRGGFSVQGEPSGAHVPCQRAAPIRGASLLQRLHNGSASPPRVPSPPPAPEPPWPCGDRDRDRDRGDRGDKQQAGARGRGSPWKRGTRGGNLVTGTQRFQEALQDPFTLCLANVPGQPDLRHIVIDGSNVAMVHGLQHYFSSRGIALAVQYFWDRGHRDITVFVPQWRFSKDSKVRESHFLQKLYSLSLLSLTPSRVMDGKRISSYDDRFMVKLAEETDGIIVSNDQFRDLAEESDKWMAIIRERLLPFTFVGNLFMVPDDPLGRNGPTLDEFLKKPVRKQGSSKTQQPSKGSTEQANQQQGKDADRSNGGIRKTRETERLRRQLLEVFWGQDHKVDFILQREPYCRDINQLSEALLSLNF", "text": "SIMILARITY: Belongs to the N4BP1 family."}
{"protein": "MTNDNSGIWVLGYGSLIYKPPSHYTHRIPAIIHGFARRFWQSSTDHRGTPANPGRVATLIPYEDIIRQTAFLKNVNLYSESAPIQDPDDLVTIGVVYYIPPEHAQEVREYLNVREQNGYTLHEVEVHLETNREHEAELGEALEQLPRHNKSGKRVLLTSVYIGTIDNEAFVGPETVDETAKVIAVSHGPSGSNYEYLAKLEQALAQMPIMKERGRITDHYLTALLETVNKYR", "text": "FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Allows utilization of gluthathione through subsequent cleavage of the Cys-Gly dipeptide by Cys-Gly metallodipeptidase DUG1. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC subfamily."}
{"protein": "MLIPKRVKYRKQHRGRMTGKAKRGNRITFGEYGLQALEPAWITNRQIEAARVAITRSLKRGGKVWIKIFPDKPVTAKPAETRMGGGKGAPEKWVAVVKPGRIMFEVAGVSEELAREAIRLASHKLPIKTRFVKREEMDGEANES", "text": "FUNCTION: Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. SIMILARITY: Belongs to the universal ribosomal protein uL16 family."}
{"protein": "MSIVCTFFLFLLNTSFAFAFAIPKPPIVRRLSTTVTSNSTASSCSANGNPIDECWRCDENWKDNRKNLADCAVGFGRDSIGGRAGEFYTVTDSGDDNPLNPTPGTLRYAATQDQPLWIIFDRDMVIQLKQDLQVASYKTIDGRGNNVQIAYGPCLTLYKVSNIIINNLYIHDCVPVKRNALSSLGGYSDGDGISIFESRDIWIDHCTLEKCYDGLIDAVNGSTDITISNSYMLNHNEVMLLGHSDEYSGDRDMRVTIAFNYFGEGLVQRMPRCRHGYFHIVNNIYRDWKMYAIGGSANPTIFSQGNVFIASNNQFTKEVTKRESADGDEEWKEWNWKSEGDEMVNGAFFTPSGKEDSPSYAKFSSMVARPASLLKTTHPSVGVLSCEIDQAC", "text": "SIMILARITY: Belongs to the polysaccharide lyase 1 family."}
{"protein": "MAEGGSPDGRAGPGSAGRNLKEWLREQFCDHPLEHCEDTRLHDAAYVGDLQTLRSLLQEESYRSRINEKSVWCCGWLPCTPLRIAATAGHGSCVDFLIRKGAEVDLVDVKGQTALYVAVVNGHLESTQILLEAGADPNGSRHHRSTPVYHASRVGRADILKALIRYGADVDVNHHLTPDVQPRFSRRLTSLVVCPLYISAAYHNLQCFRLLLLAGANPDFNCNGPVNTQGFYRGSPGCVMDAVLRHGCEAAFVSLLVEFGANLNLVKWESLGPESRGRRKVDPEALQVFKEARSVPRTLLCLCRVAVRRALGKHRLHLIPSLPLPDPIKKFLLHE", "text": "FUNCTION: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:16325183). Mediates Notch-induced ubiquitination and degradation of TCF3/E2A and JAK2 (PubMed:21119685). May play a role in testis development (By similarity). SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family."}
{"protein": "MRNYELTTITRVSSREVAKSEIQETLKKHSVSVTAEEDWGQRKLWHPIKHEEQGIFHHYKCSADPNAIEKVEKEFLINQNILRSMVVRLHG", "text": "FUNCTION: Binds together with bS18 to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS6 family."}
{"protein": "MGLRASGTGFVVLVLLQSCAAYKLICYYTSWSQYREGDGSCFPDAIDPFLCTHIIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNFGPERFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTGLVKEMKAEFAREAQAGTERLLLSAAVSAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYAVSYMLRLGAPANKLVMGIPTFGRSFTLASSKTDVGAPISGPGIPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLAEV", "text": "FUNCTION: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm Cytoplasm, perinuclear region Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyl hydrolase 18 family."}
{"protein": "MLVLGSLRSALSCSSTASLISKRNPCYPYGILCRTLSQSVKLWQENTSKDDSSLNITPRLLKIIPNDTDIVTLEKQDELIKRRRKLSKEVTQMKRLKPVSPGLRWYRSPIYPYLYKGRPVRALTVVRKKHGGRNNSGKITVRHQGGGHRNRTRLIDFNRWEGGAQTVQRIEYDPGRSSHIALLKHNTTGELSYIIACDGLRPGDVVESFRRGIPQTLLNEMGGKVDPAILSVKTTQRGNCLPISMIPIGTIIHNVGITPVGPGKFCRSAGTYARVLAKLPEKKKAIVRLQSGEHRYVSLEAVATIGVVSNIDHQNRSLGKAGRSRWLGIRPTVRGVAMNKCDHPHGGGRGKSKSNKLSMSPWGQLAKGYKTRRGKNQNRMKVKDRPRGKDARL", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
{"protein": "MEWDSDSEGSGDEEEEEEEEEEEGVEVGGGGDGGVGVGVGGGFALAIEGVLGACGLVVSDALEPDFPIIYVNRGFEDATGYRAEEVLGRNCRFLQCRGPFAKRRHPLVDTTVVTDIRRCLEEGTVFQGDLLNFRKDGSPFMAKLQLTPIYGDDETITHYMGMQFFNDSNVDLGPLSVSTTKEIVRSTLITPDNTIRPSPMGKGFCSEHSDLFLLSDEVLCQKILSRLSPRDIASVNSVCKRLYHLTRNDDLWRMVCQNAWGSEATQVLETVAGTRSLAWGRLARELTTLEAVTWRKLTVGGAVEPSRCNFSACAAGNRVVLFGGEGVNMQPMNDTFVLDLNASKPEWRHINVRSAPPGRWGHTLSCLNGSRLVLFGGCGRQGLLNDVFMLDLDAQQPTWREIPGLAPPVPRSWHSSCTLDGTKLVVSGGCADSGVLLSDTYLLDVTMERPVWREIPASWTPPCRLGHSLSVYDGRKILMFGGLAKSGPLRLRSNDVFTLDLSENKPCWRCITGSGMPGASNPAGVGPPPRLDHVAVSLPGGRILIFGGSVAGLHSASKLYLLDPTEEKPTWRILNVPGRPPRFAWGHSTCVVGGTKAIVLGGQTGEEWTLTELHELSLMFPTLNQKDLELYSWKL", "text": "FUNCTION: Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light- regulated protein degradation of critical clock components by targeting them to the proteasome complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ADAGIO family."}
{"protein": "METDLNDYTVIKEGEAEILMHKKNQVFFNKAQVNNRDMSIAVLREFLSKRKQEHEAKSSKRTRPASKVIEKDASEASKEETPSENGMNNGDHEVASEDGPSSVSKDPAKTTERFAPREPKPPKVLEALSASGLRALRYAREIEGIGQVVALDNDLASVEACQRNIKFNGSVAISKVESHHTDARVHMLTHPKEFDVVDLDPYGSPSIFLDSAIQSVTDGGLLMCTATDMAVLCGGNGEVCYSKYGSYPLRAKYCHEMALRILLASIESHANRYKRYIVPVLSVQMDFYVRVFVRVYTSASAMKNTPLKLSYVYQCIGCDSFHLQPVGRSLPKNNSVRYLPAIGPVVKQDCNHCGKKYNMGGPIWSAPMHDPEWVTSILNSVKSMKDRYPAYDRISAVLTTVSEELLDVPLFLSLHNLCATLKCISPSAAMFRSAVINANYRISGTHVNPLGMKTDAPMEVIWDIMRCWVKNHPIKAQSPEQPGSVILSKEPSHEVDFSRHIGSLSKAQAKKVARFLPNPEKHWGPKLRAGRQITSKHVSLIGHEAVNGHLSQHHEELKEEDEEAEPEDNVQDKVDPKRQKTATDNITST", "text": "FUNCTION: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family."}
{"protein": "MLQLSSTQVTPVIAQGGVIAYPTEAVYGLGCDPDNDQAIEKLLAVKQRPWQKGLILVASSFEQLLPYVDVAQLTQAQLDFAHSKWPGPFTFVMPVKSHVSNKLRGEFDSIAVRVSAHPIVRELCDSLNKPLVSTSANLAGQDPVLTSRQILTDFADKIDALVLGDLGQQAQPSTIIDARSGLVLRNGQ", "text": "FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SUA5 family. TsaC subfamily."}
{"protein": "MKFYKYCASGNDFVITNADRKEDRSALAKELCNRYEGIGADGFIVILPHEKYDFEWEFYNNDGSRAAMCGNGSRAAAHFAHHINKINPNMSFLTGAGVIKAKVNQDKVEVSLGKIKSVQNTFEELGKTWQLCNTGVPHLVHFCQNLDEFDTMLCQKMRQKYNANVNFVKILDENHLKVRTYERGVEDETLACGTGMGACFYLAFLNKKVQNKVKITPKSGEEVGFAYKNEELFFEGKVKYCFEANYNFS", "text": "FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diaminopimelate epimerase family."}
{"protein": "MKPRACVVVYPGSNCDRDAYHALEINGFEPSYVGLDDKLDDYELIILPGGFSYGDYLRPGAVAAREKIAFEIAKAAERGKLIMGICNGFQILIEMGLLKGALLQNSSGKFICKWVDLIVENNDTPFTNAFEKGEKIRIPIAHGFGRYVKIDDVNVVLRYVKDVNGSDERIAGVLNESGNVFGLMPHPERAVEELIGGEDGKKVFQSILNYLKR", "text": "FUNCTION: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MPVLTDPLQILQALIRCPSVTPHEAGALSTLEQFLTKMGFHVERPIFADKNTEDVENLYAKMGKEGPHLMFAGHTDVVPPGDLENWKYPPFEGVIDQGKLYGRGAVDMKGGIACFVAAFARVLEKRTIKGRVSLLITGDEEGPALNGTVKLLKWAEQKGEKWTAALVGEPTSVKTVGDVIKIGRRGSISGIMTVKGRQGHVAFPERAANPLPLASKLIQSLIQTTLDEGTENFQPSNLELTAIDTGNPAMNVIPAQATVHFNIRYNDLWTKEMLMAEIENRLALVQSKNNNGQYPYYQLEWIPSLGDVFLTKNDKLINTLSNAIKSVTGNIPECSTSGGTSDARFIKDYCPVIEFGLPGQTMHMVDECVTVDAMETLTSIYECFIVDFFA", "text": "FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily."}
{"protein": "AQNVIAPNTLSNSIRMLGSQSPLIQAYG", "text": "FUNCTION: One of 3 components required for cytotoxicity (tested in African green monkey Vero cells); the complex is not hemolytic."}
{"protein": "MNQSLLSEFGDPIARVEAALAALRAGRGVLVADDEDRENEGDLIFAAESMTNEQMAMMIRECSGIVCLCLTDERVRQLELPMMVEANSSHYQTAFTVTIEAAQGVTTGVSAADRITTIRAAIADGARPSDLHRPGHVFPLRARTGGVLTRRGHTEATVDLMQLAGLKPFGVLCELTKEDGSMARLPDLVAFGRQHQMPVLTIEDLVQYRQLLSERSA", "text": "FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. SIMILARITY: Belongs to the DHBP synthase family."}
{"protein": "MAKATGRYNLISPKKDLEKGVVLSDLCNFLVSQTIQGWKVYWAGIEFDVTHKGMALLQRLKTNDFAPAWSMTRNLFPHLFQNPNSTIESPLWALRVILAAGIQDQLIDQSLIEPLAGALGLISDWLLTTNTNHFNMRTQRVKEQLSLKMLSLIRSNILKFINRLDALHVVNYNGLLSSIEIGTQNHTIIITRTNMGFLVELQEPDKSAMNRKKPGPAKFSLLHESTLKAFTQGSSTRMQSLILEFNSSLAI", "text": "FUNCTION: Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. Blocks the IFN-induced nuclear accumulation of host phosphorylated STAT1 by interacting with the STAT1-binding region of host importins. Alternatively interacts also directly with host STAT1 and may additionally inhibit its non-phosphorylated form. Plays a role in assembly of viral nucleocapsid and virion budding. May act as a minor matrix protein that plays a role in assembly of viral nucleocapsid and virion budding. SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein; Cytoplasmic side Host endomembrane system; Peripheral membrane protein Note=In virion, localizes on the intravirional side of the membrane. In the host cell, it is found associated with virus-induced membrane proliferation foci and to the plasma membrane where budding takes place (By similarity). SIMILARITY: Belongs to the filoviridae membrane-associated protein VP24 family."}
{"protein": "MANIKSQVKRIRTNEAARLRNQSVKSSLRTAIRSFREAAAAGDKDKANELLVATSRKLDKAASKGVIHANQAANKKSALAQAVNKI", "text": "FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family."}
{"protein": "MFIISSKNMLLKAQRLGYAVPAFNIHNLETMQVVVETAAELRSPLILAGTPGTYSYAGTGNVVAIARDLAKIWDLPLAVHLDHHEDLADITRKVQAGIRSVMIDGSHSPFEENVALVKSVVELSHRYDASVEAELGRLGGVEDDLGVDAKDALYTNPEQGREFVARTGIDSLAVVIGTAHGLYAAEPKLGFAALPPISERVDVPLVLHGASKLPDSDIRRAISLGVCKVNVATELKIAFSDALKHYFEENPDANEPRHYMKPAKAAMKDVVRKVIHVCGCEGQL", "text": "FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol and D-tagatose. SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase family. TagBP aldolase GatY subfamily."}
{"protein": "MTDLKTIIEEAYQNKDNFTTDTVPKKIYQAIHQTIELLDNGELRIAEKQNGQWNTNEWAKMAILLYFKTEPLKTFDAGYTFFYDKIPLKYTNNTSQPQSGVRVVPHAIVRKGAYLAPNTVLMPSYINIGAYVDSGTLIDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQAHPTIIEDDCFIGARSEIVEGVMVEKGSVISMGVFVGQSTPIYNRQTQEITYGRIPAGSVVIPGSLPSKDGHYNRYSAIIVKQVDEKTRSKVSLNELLREG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
{"protein": "MACLGLRRYKAQLQLPSRTWPFVALLTLLFIPVFSEAIQVTQPSVVLASSHGVASFPCEYSPSHNTDEVRVTVLRQTNDQMTEVCATTFTEKNTVGFLDYPFCSGTFNESRVNLTIQGLRAVDTGLYLCKVELMYPPPYFVGMGNGTQIYVIDPEPCPDSDFLLWILVAVSLGLFFYSFLVSAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN", "text": "FUNCTION: Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Exists primarily an intracellular antigen whose surface expression is tightly regulated by restricted trafficking to the cell surface and rapid internalization."}
{"protein": "MSISNMTSTVWPDLQVPAVEYNHLPILTVALLTVIASAVYINVSSAQDPYKVSSIPTVKRPRVLDAYRSGVWWRIFVPRLVPYIEEGYHKYNKNDQPFRIWLGGFQTYAYVLPERYLEKIKNMPESEASFAAMANKYFHTGLPTGEVNNLVLQVASKLVNGNLATIKTLMQGEVQKALAREIGSPRQWTKINAWQVARKTTEAPGLRVVFGEELANDKTFVTGVSEFVSNITVYAFTLRYINLGPLRDFILYLVHWRHRRSLPAVLTPLNNVITERKKVRSNRHISDDEESFDCIQWALDQPVSDDCKTAEAIARRLVVISLGTIDTVAGVLVKQLTHLASHPECHEAIRAEIRECLAEDDKGWTLKSSARMKKLESFIQESLRMSSGAISLSGMRIVTGPGFRLDDNTILPRDSFIAIPTRNILYDPEVFPEPEKFDPFRFYKIKEDEKNAGPLSNRRDIRASWLAFGYGRQACPGRFYAINAMKAILGEILLKYDIRLAEKQAPSIDIDLDPMLAPARSTDLEFRVRA", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspterpenacids (PubMed:28604695, PubMed:34085529). Performs the C22-oxidative modification of the terpene synthase sttA product preaspterpenacid I to produce preaspterpenacid II (PubMed:34085529). It has still to be determined how preaspterpenacid II is further modified to produce aspterpenacids (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSSSRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVHNCIQKDSKDSLHANTANRRTTPV", "text": "FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Synapse, synaptosome. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Synapse, synaptosome. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily."}
{"protein": "MSNNDLLNYYHRANELVFKGLIEFSCMKAAIELDLFSHMAEGPKDLATLAADTGSVPPRLEMLLETLRQMRVINLEDGKWSLTEFADYMFSPTPKEPNLHQTPVAKAMAFLADDFYMGLSQAVRGQKNFKGQVPYPPVTREDNLYFEEIHRSNAKFAIQLLLEEAKLDGVKKMIDVGGGIGDISAAMLKHFPELDSTILNLPGAIDLVNENAAEKGVADRMRGIAVDIYKESYPEADAVLFCRILYSANEQLSTIMCKKAFDAMRSGGRLLILDMVIDDPENPNFDYLSHYILGAGMPFSVLGFKEQARYKEILESLGYKDVTMVRKYDHLLVQAVKP", "text": "FUNCTION: Involved in the biosynthesis of the major light-harvesting pigment bacteriochlorophyll c (BChlc), which confers a significant competitive advantage to green sulfur bacteria living at limiting red and near-infrared light intensities (PubMed:15090495). Catalyzes the methylation at the C-20 position of the cyclic tetrapyrrole chlorin of bacteriochlorophyll d (BChld) to produce bacteriochlorophyll c (BChlc) using S-adenosylmethionine (SAM) as a methyl source (PubMed:15090495, PubMed:16797589). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MTDFNHPPRILFLYGSLRERSYSRLLAEEAGRIITTMGAETKFFDPRELPLRGQVLDSHPKVQELLELSQWSEGQVWSSPEMHGNITGILKNQIDWIPLEIGSIRPTQGRTLAVMQVSGGSQSFNAVNTMRILGRWMRMFTIPNQSSVAKAYQEFHEDGTMKDSPYRDRVVDVMEELYKFTLLLRDKVDYLTDRHSERKAKVNTDG", "text": "FUNCTION: Has high NADPH-dependent quinone reductase activity with a preference for quinones with hydrophobic substituents. Reduces also CrO4(2-) and Fe(3+). Somewhat active with NADH. May be involved in response to oxidative stress caused by arsenic. SIMILARITY: Belongs to the ArsH family."}
{"protein": "MSDVSVPLTFSDVAAAKVKTLIAEEENPNLKLRVYITGGGCSGFQYGFTFDEDVNEGDMTIENDGVTLVVDPMSLQYLIGGKVDYTEGLEGSRFFIDNPNATTTCGCGASFSV", "text": "FUNCTION: Required for insertion of 4Fe-4S clusters for at least IspG. SIMILARITY: Belongs to the HesB/IscA family."}
{"protein": "MSKFTTEEIRSKFISYFKANNHTHVSSSPLIPHNDPSLMFVNSGMVQFKNVFTGQEKRPYDKAVTSQKSLRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKEQAIYYAWNLLTKEFELPKDKLYATVYHTDDEAASYWKKIAGFSDDRIIRIKTNDNFWSMGDLGPCGPCSEIFYDHGEQIYGGLPGTKDEDGDRFIEIWNMVFMQYEQINKDTRIDLPKKSIDTGMGLERMTAVLQHVNNNYDIDLFQEIISFTENILKVKVEAEAKFSYRVIADHLRACSFLIADGVVPSSEGRGYVLRRIMRRAMRHAHILGSKEPLMYKLLPKLVDLMGNTYPELKRAESFISSILEQEEIRFKTTLERGLKLLSEETENLNAGGRLSGEVAFKLYDTYGFPLDLTEDILKNRNIAVDHQGFEQQMLEQKECARKSWLGSGESKTDQLWFDIKAKYGSTEFLGYNLNEADGKIVALIKDNALVNDISEIDTQFLLIANQTPFYGESGGQMGDIGVIKTQNCEIEVIDTLKYLGFIIVHKCVLKKGKVITDENANFSIDVKYRQNLRIHHSATHLLHAVLHQILGKHVTQKGSLVATSYLRFDISHPKALTPEEIVLIEDKVNEIIRDNHEVDTTLMSTEDAVKQGAMALFGEKYDSEVRVVKMGETSLELCGGTHVRHTGDIGCFKITSESAIAAGIRRIEAVCGEFVIKLIREKEGLLKNIENSLKTNKNELVSKVNNILERNKELEKELEKTYLASLDLSVEQIEKQAEKIKEIKLIYCHVENLDNKILRQAAENLTKKVEDLVVVYVGNNSSKLSITVGISRAITDKFNAGFIAKELSLFLGGSGGGGQPSIAQAGGSDLAKLPKVKDQLQSLLDA", "text": "FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MSKVCIVTGKRPAVGNNRSHAKNSTRRRFLPNLQTHRFWVESENRFVKLRLSAKGMRIIDKKGIDSVLTDIRANGVKI", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MAQILAPSVQWQMRFTKNSTEVSSMTSKMWGSLFLKQNKKAPARSSTKYRALAVKSEDGTINRMEDLLNLDVTPYTDKIIAEYIWIGGTGIDVRSKSRTISKPVEHPSELPKWNYDGSSTGQAPGDDSEVILYPQAIFKDPFRGGNNILVICDTYTPQGEPIPTNKRHKAAQIFSDAKVLGEVPWFGIEQEYTLMQQDVNWPLGWNVGGYPGPQGPYYCAAGADKSFGRDISDAHYKACLYAGINISGTNGEVMPGQWEFQVGPSVGIEAGDHIWCARYLLERITEQAGVVLTLDPKPIDGDWNGAGCHTNYSTKSMREEGGFEVIKKAILNLSLRHKEHISAYGEGNERRLTGKHETASIDSFSWGVADRGCSIRVGRDTEKEGKGYLEDRRPASNMDPYVVTGLLAETTLLWEPTLEAEALAAQKLSLNV", "text": "FUNCTION: The light-modulated chloroplast enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the glutamine synthetase family."}
{"protein": "MAESFVRLEHVFYKYEDAEKYAVKDVSISAEKGEWVALVGHNGSGKSTIAKLLNGLLFPEEGLIKIGHFVLSEKNIWEIRRQVGMVFQNPDNQFVGATVQDDVAFGLENHGVPHDTMVKRVESALNEVGMQSYALHEPARLSGGQKQRVAIAGVLALQPDVIILDEATSMLDPRGRAEVMETIRIMREQEDITVISITHDLDEVLFADRVIVMNNGEIHSEGTPQEIFQQADAMREIGLGVPFIIELQEKLVAGGFETESTVLSEGALLDQLWKLNSNN", "text": "FUNCTION: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family."}
{"protein": "MLLEAELDCHRERPGAPGASALCTFSRTPEIPMCAGCDQHILDRFILKALDRHWHSKCLKCSDCHVPLAERCFSRGESVYCKDDFFKRFGTKCAACQLGIPPTQVVRRAQDFVYHLHCFACVVCKRQLATGDEFYLMEDSRLVCKADYETAKQREAEATAKRPRTTITAKQLETLKSAYNTSPKPARHVREQLSSETGLDMRVVQVWFQNRRAKEKRLKKDAGRQRWGQYFRNMKRSRGSSKSDKDSIQEGQDSDAEVSFTDEPSMADMGPANGLYSSLGEPAPALGRPVGGLGSFTLDHGGLTGPEQYRELRPGSPYGIPPSPAAPQSLPGPQPLLSSLVYPDTNLSLVPSGPPGGPPPMRVLAGNGPSSDLSTESSSGYPDFPASPASWLDEVDHAQF", "text": "FUNCTION: Transcription factor (PubMed:18539116, PubMed:10593900, PubMed:12150931). Recognizes and binds to the consensus sequence motif 5'-AATTAATTA-3' in the regulatory elements of target genes, such as glycoprotein hormones alpha chain CGA and visual system homeobox CHX10, positively modulating transcription; transcription can be co-activated by LDB2 (PubMed:18539116, PubMed:10593900, PubMed:9192866). Synergistically enhances transcription from the prolactin promoter in cooperation with POU1F1/Pit-1 (PubMed:7708713). Required for the establishment of the specialized cells of the pituitary gland and the nervous system (By similarity). Involved in the development of interneurons and motor neurons in cooperation with LDB1 and ISL1 (PubMed:12150931, PubMed:18539116). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNFVLILMTNTLLALLLMIITFWLPQLNSYMEKSNPYECGFDPMSPARVPFSMKFFLVAITFLLFDLEIALLLPLPWALQTANLPLMVMSSLLLITILALSLAYEWLQKGLDWAE", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family."}
{"protein": "MSFKSLLKNLPKFFFLGLIHIYRWTISPLLGSPCRFFPTCSQYALQALKHHGCIKGLGFTIKRIGKCGPWHPGGVDLVPMTTLEESLDISPATNDDDSCDSQA", "text": "FUNCTION: Could be involved in insertion of integral membrane proteins into the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the UPF0161 family."}
{"protein": "MVATLERREEKRDWGTFATWITSTENRLYIGWFGCLMIPTLLTAASCYIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVIPSSNAIGIHFYPIWEAASIEEWLYNGGPYQLIVFHFLIGVACWMGREWELSYRLGMRPWIFVAFSAPVAAASAVFLVYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMRPFHMAGVAGVFGGSLFSAMHGSLVTSSLIRETSEVESVNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRALHFFLAAWPVVGIWLTALGVSTMAFNLNGFNFNQSVVDSEGRVINTWADIINRADLGMEVMHERNAHNFPLDLASNEILPVAISAPSVVG", "text": "FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family."}
{"protein": "MNMKILVLVAVLCLVVSTHAERHSKTDMEDSPMIQERKCLPPGKPCYGATQKIPCCGVCSHNNCT", "text": "FUNCTION: Reversibly blocks N-type calcium channels (Cav2.2/CACNA1B) in rat dorsal root ganglion cells. Elicits no toxic symptoms in either vertebrates or invertebrates during a period of 48 hours post- injection, when it was assayed in vivo by direct injection into mice and cockroaches (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 36 family. 02 subfamily."}
{"protein": "MTNFYKVFLAVFILVCCNISHAAVSFIGSTENDVGPSQGSYSSTHAMDNLPFVYNTGHNIGYQNANVWRISGGFCVGLDGKVDLPVVGSLDGQSIYGLTEEVGLLIWMGDTNYSRGTAMSGNSWENVFSGWCVGNYVSTQGLSVHVRPVILKRNSSAQYSVQKTSIGSIRMRPYNGSSAGSVQTTVNFSLNPFTLNDTVTSCRLLTPSAVNVSLAAISAGQLPSSGDEVVAGTTSLKLQCDAGVTVWATLTDATTPSNRSDILTLTGASTATGVGLRIYKNTDSTPLKFGPDSPVKGNENQWQLSTGTETSPSVRLYVKYVNTGEGINPGTVNGISTFTFSYQ", "text": "FUNCTION: Essential fimbrial adhesion factor that mediates binding to N-acetylglucosamine-containing receptors in the host intestinal microvilli, leading to colonization of the intestinal tissue, and diarrhea or septicemia. Also confers adhesiveness to laminin and basement membranes (By similarity). SUBCELLULAR LOCATION: Fimbrium Note=Attached to the tip of the fimbrial filaments. SIMILARITY: Belongs to the fimbrial protein family."}
{"protein": "MNDQKTTNTGLLTSTLKTKPKHNLKPSSEAIKKAVSKKEGHYKNKRFQKHNFNNKSEFEERIVKLKRISKTTKGGRNMRFSVLVVVGNKKGKVGYGIAKALEVPLAIKKAIKKAHNSIHTVEIHKGSIYHEVIGRKGASKVLLKPAPLGTGIIAGGAIRAIVELAGFSDIYTKNLGRNTPINMIHATMDGILKQLSPKKVALLRNKPISDL", "text": "FUNCTION: Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. FUNCTION: With S4 and S12 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
{"protein": "MLFPDDFSTWEQTFQELMQEEKPGAKWSLHLDKNIVPDGAALGWRQHQQTVLGRFQCSRCCRSWTSAQVMILCHMYPDTLKSQGQARMRIFGQKCQKCFGCQFETPKFSTEIIKRILNNLVNYILQRYYGHRKIALTSNASLGEKVTLDGPHDTRNCEACSLNSHGRCALAHKVKPPRSPSPLPKSSSPSKSCPPPPQTRNTDFGNKTFQDFGNRTFQGCREPPQREIEPPLFLFLSIAAFALFSLFTR", "text": "FUNCTION: Probable chaperone protein which facilitates trafficking and functional cell surface expression of some G-protein coupled receptors (GPCRs). Promotes functional expression of the bitter taste receptor TAS2R16 (By similarity). Also promotes functional expression of the opioid receptor heterodimer OPRD1-OPRM1 (PubMed:18836069). SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the TMEM7 family."}
{"protein": "MAGGHKKNEATRQTDEVIQQKYDESLSKHKNRCELSLTFEYKLSNKLRARLKAAFFKVDHGWEDQTLDQVETLVRKENHVHRRSRSINDLDSSKLRRPHHPNSIMGSNTGKLRASSFTRLVSPREGFAQLPYKKPVSPYSSSSAVSSTSSSFDRTSPPWLNYVEPHTELPRLPFELSHASTASAKSPLFGMNYHISRPEETDESLRLGTANLSRIRKSTSLPFPTAYPLSADDCKAAEVMLTLVNSMPSKKP", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the WHI5/NRM1 family."}
{"protein": "MYLELQIKKTHIFDLKGNKVEEIELPIFFSYPVRKDLIRRVFISEFTKALQPKGRDPMAGKRTSALSFGINLGLARVPRVKTTGEAALAPNTVGGRLAFPPTVEKKLVEEVNKKEKKLAIISALSATANMNFVKNRGHVFSIDTLPIIVVDDITKLTKTKEIIEVLESLKVYEDVERVKDRIRIRSGKGKMRGRRYKEPKGPLFVIHENNPVFVKAASNIPGVDVILASDLSVIHLAPGGHPGRLTIYTKSSIDVLRKRFEGRLAL", "text": "FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. FUNCTION: Forms part of the polypeptide exit tunnel. SIMILARITY: Belongs to the universal ribosomal protein uL4 family."}
{"protein": "MTIQLINESSNTEKFQQICDKWRLVHDRSAILALVLTDERLELRKLDEPKLGAIAVNFVDGTMAHRRKFGGGRGEAVAKAVGIKGDYLPTIIDATAGLGRDAFVLASVGCKVLLVERNPIVAALLEDGLVRAYADPEIGAFMQERMILADVRNISLLDVAQQAADVVYLDPMYPHKQKSALVKKEMRVFQHLVGADLDSDNFFVPAKALARKRVVVKRPDYAPFLAEQKPDFSQTTKNHRFDVYLSHLKSA", "text": "FUNCTION: Specifically methylates the guanosine in position 1516 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family."}
{"protein": "MGLITLILALIVVLFVCVFASNSSKPANNASFADNGAQRTAREFGPAARGGELLEFERWFKDTLATVFAQKAEKVANPTRAWNAETVFDNLSPWTSAADFGTVCHTLIGYCVRYNSPGDALHHSPDLANNLISGLRAICARLPDPPPHQQAPWGPVADWYHFTITMPEVFMTVTIVLDNTPHYDEAAALTRHWLALYLPTAVTSMGWHRTAGNAMRMGVPYAYGQLLRGYSAQQIAQEPGVQETLKTVAFPYVAAGNGLHPDSIYIDHLDVRAYGYLINSFFTFAYYTRLFGADVVNTEGLTRAIENVGSPEGVVVPGVMSRNGTLYSNVIGNFVDYPIAVHSADLSKVLTKLSDSYYGAVVGATTRLAYYEADPTNNTQAPLWTMTRRIWNRRARVINYNANTVMFESGIILQSLNGVLRVPSTTTSTQSFRPAVGKTALAKTRTAGAILVHARFAEMNNLQFKSCTLFYDHGMFQLYYNIGVEPNSLNNVNGRVVVLSRDTSVNTNDLSFEAQRLNNNNSSDGSAFNGVVCQRVPITNFNVPSLTVRSPSASVELVEQIISFQNMYTASAVACYKLNVEGHSDALRAYRINMDEVVYVTTGEGVKALFAYPWLMLKEDAAVVFMSANEDLVVPMSVINNAFSAIDEPGLQYAPVNCFLYGNGFRLNDSLANLQFQFEIIN", "text": "FUNCTION: Component of the polyhedra envelope. SUBCELLULAR LOCATION: Virion membrane. SIMILARITY: Belongs to the baculoviridae E66 family."}
{"protein": "MKNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREADCKNGFLLDGFPRTVEQAEALDTLLKNEGKSIDKAINLQVPDAELLKRLLGRAEIEGRADDNEVTIKNRLDNYNKKTLPLLDFYATRKKLSQVNGVGSLEEVTSLIQKELA", "text": "FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylate kinase family."}
{"protein": "MGFWKFSPFLVLGILALYQVGFLQAAPFRSALENPPDSGVRNEEELRLLLAAVMKDYMQMKTHELEQEQETEGSRVAVQKRSCNSATCVAHWLGGLLSRAGSVANTNLLPTSMGFKVYNRRRRELKA", "text": "FUNCTION: Stimulates cAMP production in porcine kidney cell line LLC- PK1 via the calcitonin receptor (CT) but not via the CT-like (CL) receptor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calcitonin family."}
{"protein": "MMEDKITIEKLNLYYSDFHALHDINMHIQKNEITAFIGPSGCGKSTLLRSLNRMNDLVEGCRIDGSIKLDGTDIYNGDLDVTVLRQRVGMVFQRPNPFPMSVYDNVAYGPRIHGITDKKELDEIVETSLKQAAIWDDLKDRLKKSALGLSGGQQQRLCIARALAVKPEVLLMDEPTSALDPISTSKIEELALELKKNYTIVIVTHNMQQAVRISDKTGFFLLGDLVEFGETDQLFSMPKDERTEKYITGRFG", "text": "FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family."}
{"protein": "MDIDIIEEDENPMLHRTDVRFEVVHDEATPSRLSVRDSLAATLNKDAEEVVIHKLDTKFGMRKTVGYAKVYDNPEYARDVEQDHMLERNKIVADGEEEAEEA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS24 family."}
{"protein": "MDGDRGKRDSYWSTSPSGSTTKLASGWERSSKVDTWLLILSFTQWALSIATVIICIIISARQGYSMKEYSMTVEALNMSSREVKESLTSLIRQEVIARAVNIQSSVQTGIPVLLNKNSRDVIQMIDKSCSRQELTQLCESTIAVHHAEGIAPLEPHSFWRCPVGEPYLSSDPKISLLPGPSLLSGSTTISGCVRLPSLSIGEAIYAYSSNLITQGCADIGKSYQVLQLGYISLNSDMFPDLNPVVSHTYDINDNRKSCSVVATGTRGYQLCSMPTVDERTDYSSDGIEDLVLDVLDLKGSTKSHRYRNSEVDLDHPFSALYPSVGNGIATEGSLIFLGYGGLTTPLQGDTKCRTQGCQQVSQDTCNEALKITWLGGKQVVSVIIQVNDYLSERPKIRVTTIPITQNYLGAEGRLLKLGDRVYIYTRSSGWHSQLQIGVLDVSHPLTINWTPHEALSRPGNEECNWYNTCPKECISGVYTDAYPLSPDAANVATVTLYANTSRVNPTIMYSNTTNIINMLRIKDVQLEAAYTTTSCITHFGKGYCFHIIEINQKSLNTLQPMLFKTSIPKLCKAES", "text": "FUNCTION: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). FUNCTION: Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins. SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Host cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase family."}
{"protein": "MQMDSPKSPLQPPTYGNLVTILSIDGGGIRGLIPAVILGFLESELQKLDGEEARLADYFDVIAGTSTGGLVTAMLTAPNKEGRPLFAASEIKDFYLEQCPKIFPQDHFPFSAAKKLVKSLTGPKYDGKYLHQLIHAKLGDTKLSQTLTNVVIPTFDIKHLQPTIFSSYEVKNHPLKDATLADIAISTSAAPTYLPAHFFKVEDLNGNAKEYNLIDGGVAANNPALLAIGEVTNEISGGSSDFFPIRPNDYGRFLVLSLGTGNHKAEEKFNAKEVAGWGLLNWLTHDNSTPIIDAFSQASSDMVDFHLSAVFRALHSEANYIRIQDDTLTGDAASVDIATVENLDILAKTGDELLKKPVARVNLDSGCNENAYETTNEHALIKLAGILSKEKKIRDIRSPHAKAPIRI", "text": "FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), and less efficiently the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidic acid (PA), phosphatidylserine (PS) and phosphatidylinositol (PI). Favors the release of fatty acid at the sn-1 position for PC or PE and the sn-2 position for PG, PA, PS and PI. Negatively affects disease resistance to the necrotic fungal pathogen Botrytis cinerea and the avirulent bacteria Pseudomonas syringae by promoting cell death and reducing the efficiency of the hypersensitive response, respectively. However, PLP2 contributes to resistance to cucumber mosaic virus (CMV), an obligate parasite inducing hypersensitive response. May negatively regulate oxylipin production, possibly via participating in membrane repair that includes removal of oxidatively modified lipids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the patatin family."}
{"protein": "MESWQAPDLKRLGGQAVPLRLYDTARQAVHATEPHPDGARMYVCGITPYDATHLGHAATMVTFDVINRVWRDNGHDVAYVQNVTDVDEPLFERAERDGEDWVVLGMRETALFREDMEALSIIPPKAYVGAVESMPTIAALVERLVDAGAAYTVDDGTGDVYFPVTATEGFGSESHYDRDTMLRFFGERGGDPDRSGKRDPLDALLWRGEREGEPSWESRLGRGRPGWHIECAAIALAHLGDRIDVNGGGNDLIFPHHEFSAAHAEAATKAVPFAKHYVHAGMIGLDGEKMSKSRGNLVFVSRLRADGVDPAVIRLALLDGHYREDRPWTAELHAAAADRLARWREAMGMSSGASGTTTAQRVRERLSDDLDTPGALRAVDEWAAASLTGAHHDAHAPALVRDTVESLLGVTLLRAVFRQRTTSATTLDRSR", "text": "FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and L- cysteine to form L-Cys-GlcN-Ins. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MshC subfamily."}
{"protein": "MSSSLASDTPRLPSIDTLLRHQACLPLIDRHGREGVLATLRQLLDDLRNLVRNGELTPAELAPEILLGRTGERLAAQQRSQVRRVFNLTGTVLHTNLGRALLPEAAIEAMQTAARYPLNLEFDLATGKRGDRDDLIEGLIRELTGAEAVTVVNNNAAAVLLALNSLGARKEGIISRGELIEIGGAFRIPDIMARAGVKLHEIGTTNRTHARDYEAAIGPRTGLLMRVHCSNYSIQGFTTQVPTAELASIAHQRDLPLLEDLGSGSLLDLTRWGLPAEPTVRQALADGADIVTFSGDKLLGGPQAGIIVGRKDLIARIKKNPLKRALRVDKITLAALEAVLALYRNPDRLAERLPTLRLLTRSQAEIQAQAERLAPEVKAHLGEQWAVSVAPALGMIGSGSQPVARLPSAALCLRPQVSKKLRGRSLHVLERALRDLPVPVLGRLDDDALWLDLRQLDDEAQWLAQLPALQLGPVQ", "text": "FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SelA family."}
{"protein": "MKTRVTRLTVAAPNDVSALAQAIESGEVDPTRVIAVLGKTEGNGCVNDFTRAFATSTLKRFFAERLALNETEVDERIAFVMSGGTEGGLSPHWLVFEVDDSAPSRDTTTPGLAAGVAFTRDLRPEEIGRTSQVELTRDAVLRAMAAAGIQRVEDVHFVQIKCPLLTAARINEAAARGQSVACHDTYESMGYSRGASALGVAAALGDLPGDVRDEQICREWSLYSSRASSSAGIELLRNEVLVLGNAPGWDPEYRIGHAVMEDALDAQAIERALASVPGGDKIKLTPERLAGLLVKAEPSASGSIRGNRHVMSDDSDINGSRHARALVGGVLAGQLGDTRLFVSGGAEHQGPNGGGPLALIVRS", "text": "FUNCTION: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6- trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family."}
{"protein": "MSGKNEFNIFKHVLVPEHRILSEEEKKALLEKYKITPAQLPQIRASDPAVKALGAKPGDIIEIKRRSPTAGVYYYYRVVVED", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family."}
{"protein": "MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM", "text": "FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:20949621). Plays an important role in the regulation of cell proliferation (PubMed:23698361, PubMed:22711838). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (PubMed:24623306). SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane; Lipid-anchor. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Endomembrane system Cytoplasm, cytosol. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
{"protein": "MPYDTMQQVIGLAPKKRGTLIQKGINFSYVPLNEEGGVDYEEAEKVLKRDQPHIVVIQRSRGYDTRQSYTVDQIKKMTAFVKKVSPESLVFVDNCYGEFSEKHEPTEYGVDFTAGSLIKNAGGGIAQTGGYIVGKEELVENAAIRLTAPGIGKEEGATLTNMHEFYEGFFLAPHTTGEAIKGMIFSAALLEKMGCEVTPKWHEPRTDLIQTIIFNVPEKMINFTKEVQKNSPIDSFVEPIPSDMPGYEDKVIMAAGNFVSGSTMEFSADGPIRPPYALYMQCGLTYAHDRIAVTNAVNHLFFKENG", "text": "SIMILARITY: To L.delbrueckii similar ORF in glnA 5'region."}
{"protein": "MASKPEKRVASSVFITLAPLRRDVAMAEEVRQAVCEARRGRPWEAPAPMKTPEAGLEGRPSPWTPPGRAAATVPAAPMQLSNGGCPPPPPVLDGEDALPDLDLFPPPPPPPPVLLPSEEEAPAPMGASLIADLEQLHLSPPLPPPPPQAPAERPSVQPSPLRPMEEELPPPPAERVEKGASTDICAFCHKTVSPRELAVEAMKRQYHAQCFTCRTCRRQLAGQSFYQKDGRPLCEPCYQDTLERCGKCGEVVRDHIIRALGQAFHPSCFTCVTCARCIGDESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRSFHENCYRCEDCRILLSVEPTDQGCYPLNNRLFCKPCHVKRSAAGCC", "text": "FUNCTION: Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion (By similarity). SUBCELLULAR LOCATION: Cell junction, focal adhesion Cytoplasm, cytoskeleton, stress fiber Note=Associated with actin stress fiber at cell-ECM focal adhesion sites. Recruited and localized at actin stress fibers and clustered at cell-EMC adhesion sites through interaction with FERMT2."}
{"protein": "MGAYKYMQELWRKKQSDVMRFLLRVRCWQYRQLSGLHRAPRPTRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGATYGKPVHHGVNQIKFARSLQSTAEERAGRHCGALRVLNSYWVGEDSTYKFFEVILIDPFHKAVRRDPDAQWITKAVHKHREMRGLTSAGKKSRGLGKGHKFHLTIGGSRRAAWRRRNTLQLHRYR", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family."}
{"protein": "MRPGTGAERGGLMVSEMESHPPSQGPGDGERRLSGSSLCSGSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMPGMMMSHMSQASMQPALPPGVNSMDVAAGTASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGSLITKSNLHAMIKAEESSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTVPVVPEPEVTSIVATVVDNENTVTISTEEQAQLTSTPAIQDQSVEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAAPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ", "text": "FUNCTION: Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus speckle Nucleus matrix Note=Colocalizes with AKAP8L in the nuclear matrix. SIMILARITY: Belongs to the PRPF40 family."}
{"protein": "MNSLVATPPVPPHFYETSCRSASYSMSSTNASVNRKRKAEDDCLPSDDTRMSASPSGSPALHPRPLAPRHLKRSRPNVSGRPLSLPRLMETLDTDALRSVLRSLCDRHPEIASEVMHTAPRPSVSAALEVLNNYQSTLQSSFPLGGNPSSDYAYNRVRQHLTNLLEALNDFTPHFLPPNESQPSTSLNYLDGATDIIHRLPRWTTPQHNLEKYAAYEEMSKAWCLVIREAAKRGGGIQLQYGGWDQKLAKHNETAGGKLQDAVNELNQSLGWIGGNVGNPSYPGGSNSQGDMSIRQQLMSGTYGAGLPLKVGPW", "text": "FUNCTION: Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cut8/STS1 family."}
{"protein": "LGALTQLLLNLGKL", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
{"protein": "MSKKQSTICQKVGIADLEIPIILGQKDGKLQHSIASCKITATIKETLKGDISGEVQRLLPSFTKEIEPKSWHRLLEEFKENIGVEKITLSLSCPFFVSKKAPVSELRGLMEYNCTFSASTGESGITTSLYVPVTTLCPCSKEISDGGAHNQRAEAIFRVEMKEHLWLEDLIQLVEESASCQVYSVLKRPDEKYVTEKAFDNPMFVEDVVRKIAVRAGEHPLIHAFSISVESFESIHKHNAYAYVNSEDLNL", "text": "FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. SIMILARITY: Belongs to the GTP cyclohydrolase IV family."}
{"protein": "MVEKIPMTASGYKKLEDELSTLKVKRIDVIEEMRLAAMDKDMRENAPYHAAKEQRGQIEGRIKEIEHELKYADVSEYTDTNTSKVNMGSTVKLRDPKNGECCTYTLVSPKEIEPLKGKISASSPIGKAVFNRNKGEQIEIEVPSGTLQYIIEDISF", "text": "FUNCTION: Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. SIMILARITY: Belongs to the GreA/GreB family."}
{"protein": "MIREKVTVSTRTLQWKCVESRTDSKRLYYGRFILSPLMKGQADTIGIAMRRALLGEIEGTCITRVKSEKAPHEYSTIAGIQESVHEILMNLKEIVLRSNLYGTCDASICVKGPGCVTAEDIILPPSVEIVDNTQHIAWLTEPIDFCIGLQIERNRGYILKTHHNFEDGSYPIDAVFMPVRNANHSIHSYGNGNEKQEILFLEIWTNGSLTPKEALHEASRNLIDLFIPFLHMEEENLHLEDGEHTIPLSPLSFHDKVAKLRKNKKKLALKSIFIDQLEFPPKIYNCLKKSNISTLLDLLNKSQEDLMKIEHFHIEDVKQILGILEKHFAIDLPKNQF", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RNA polymerase alpha chain family."}
{"protein": "MNSSTDPTFSELNASFTNTPDTLFATSVSSDPSHGFGEEDYACGTFNCSPKEFVAFVLGPQTLPLYKAVLITIIFGGIFITGVVGNLLVCIVIIRHSAMHTATNYYLFSLAVSDLLYLLFGLPTEVFLYWHQYPDLFGMPFCKIRAFISEACTYVSVFTIVAFSMERFLAICHPLHLYAMVGFKRAIRIITALWIVSFISAIPFGLLSDIQYLNYPLDHSRIEESAFCSMSPKIVNEIPVFEVSFCIFFVIPMILIILLYGRMGAKIRSRTNQKLGVQQGTNNRETRNSQMRKKTVIRMLAAVVITFFVCWFPFHLQRLIFLYAKNMDNYLDINEALFSIAGFAYYVSCTVNPIVYSVMSRRYRVAFRELLCGKAVGAYYNSGFARDHSSFRESSAYDRVHSVHVRASQHPNKFETDSSSANRVLIKKTYSLPLPKNADSTVLSTTDIVIVLENSHTVCEEPKVENDIWIENEETCI", "text": "FUNCTION: Acts as a receptor for the neuropeptides CAP-1 and CAP-2, but not CAP-3. Probably a component of signal transduction pathway that leads to Malpighian tubule fluid secretion in response to these ligands. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSVEDLELEDVLQIGYGDVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAANNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRTLAQKIVNNTMKVVPTPCTMDELESLLMEFGIMEEEDTSIIGKTAAEENAA", "text": "FUNCTION: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein. SIMILARITY: Belongs to the NifH/BchL/ChlL family."}
{"protein": "MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGAEQLEALKAFVESMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEIYHFTLEKIQPRVISFEEQVASIRQHLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ", "text": "FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By similarity). Also involved in the deneddylation of non-cullin subunits such as STON2 (By similarity). The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the CSN4 family."}
{"protein": "MEQGYGGYGAWSAGPANTQGTYGSGMTSWQGYENYNYYNAQNTSVPAGTPYSYGPASWEATKTNDGGLAAGSPAMHVASFAPEPCTDNSDSLIAKINQRLDMLSKEGGRGGISSGGEGVQDRDSSFRFQPYESYDARPCIPEHNPYRPGYGYDYDFDLGTDRNGSFGGTFNDCRDPAPERGSLDGFLRGRGQGRFQDRSNSSTFIRSDPFMPPSASEPLSTTWNELNYMGGRGLGGPSTSRPPPSLFSQSMAPDYSMMGMQGVGGFGGTMPYGCGRSQTRIRDWPRRRGFERFGPDNMGRKRKQFPLYEEPDAKLARADSDGDLSENDDGAGDLRSGDEEFRGEDDLCDSRKQRGEKEDEDEDVKKRREKQRRRDRMRDRAADRIQFACSVCKFRSFEDEEIQKHLQSKFHKETLRFISTKLPDKTVEFLQEYIINRNKKIEKRRQELLEKESPKPKPDPFKGIGQEHFFKKIEAAHCLACDMLIPAQHQLLQRHLHSVDHNHNRRLAAEQFKKTSLHVAKSVLNNKHIVKMLEKYLKGEDPFVNETADLETEGDENVGEEKEETPEEVAAEVLAEVITAAVKAVEGEGEPAAAHSDVLTEVEGPVDTAEASSDPHTEKLLEEQTCEAASETRSIEDKTRGEAAEARNEAAMPTADAGSTLPVIAIPGIMEDELEQTGAEAKDIPTE", "text": "FUNCTION: Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II). Acts as an anchor for a PKA-signaling complex onto mitotic chromosomes, which is required for maintenance of chromosomes in a condensed form throughout mitosis. Recruits condensin complex subunit NCAPD2 to chromosomes required for chromatin condensation; the function appears to be independent from PKA-anchoring (By similarity). Specifically involved in recruitment of CAPD2 to, and condensation of maternal but not paternal chromosomes (PubMed:12082153). May help to deliver cyclin D/E to CDK4 to facilitate cell cycle progression (PubMed:14641107). Required for cell cycle G2/M transition and histone deacetylation during mitosis. In mitotic cells recruits HDAC3 to the vicinity of chromatin leading to deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3; in this function may act redundantly with AKAP8L. Involved in nuclear retention of RPS6KA1 upon ERK activation thus inducing cell proliferation. May be involved in regulation of DNA replication by acting as scaffold for MCM2. Enhances HMT activity of the KMT2 family MLL4/WBP7 complex and is involved in transcriptional regulation. In a teratocarcinoma cell line is involved in retinoic acid-mediated induction of developmental genes implicating H3 'Lys-4' methylation. May be involved in recruitment of active CASP3 to the nucleus in apoptotic cells. May act as a carrier protein of GJA1 for its transport to the nucleus. May play a repressive role in the regulation of rDNA transcription. Preferentially binds GC-rich DNA in vitro. In cells, associates with ribosomal RNA (rRNA) chromatin, preferentially with rRNA promoter and transcribed regions (By similarity). Involved in modulation of Toll-like receptor signaling. Required for the cAMP-dependent suppression of TNF-alpha in early stages of LPS-induced macrophage activation; the function probably implicates targeting of PKA to NFKB1 (PubMed:19531803). SUBCELLULAR LOCATION: Nucleus matrix Nucleus, nucleolus Cytoplasm Note=Associated with the nuclear matrix (By similarity). Exhibits partial localization to the nucleolus in interphase, possibly to the fibrillary center and/or to the dense fibrillary component (By similarity). Redistributed and detached from condensed chromatin during mitosis (By similarity). Localizes specifically to the vicinity of the meiotic spindle in metaphase II oocytes (PubMed:12082153). SIMILARITY: Belongs to the AKAP95 family."}
{"protein": "MDLDKPSVWGSLKQRTRPLLINLSKKKVKKNPSKPPDLRARHHLDRRLSLSVPDLLEAEALAPEGRPYSGPQSSYTSVPSSLSTAGIFPKSSSSSLKQSEEELDWSQEEASHLHVVETDSEEAYASPAERRRVSSNGIFDLQKTSLGGDAPEEPEKLCGSSDLNASMTSQHFEEQSVPGEASDGLSNLPSPFAYLLTIHLKEGRNLVVRDRCGTSDPYVKFKLNGKTLYKSKVIYKNLNPVWDEIVVLPIQSLDQKLRVKVYDRDLTTSDFMGSAFVILSDLELNRTTEHILKLEDPNSLEDDMGVIVLNLNLVVKQGDFKRHRWSNRKRLSASKSSLIRNLRLSESLKKNQLWNGIISITLLEGKNVSGGSMTEMFVQLKLGDQRYKSKTLCKSANPQWQEQFDFHYFSDRMGILDIEVWGKDNKKHEERLGTCKVDISALPLKQANCLELPLDSCLGALLMLVTLTPCAGVSVSDLCVCPLADLSERKQITQRYCLQNSLKDVKDVGILQVKVLKAADLLAADFSGKSDPFCLLELGNDRLQTHTVYKNLNPEWNKVFTFPIKDIHDVLEVTVFDEDGDKPPDFLGKVAIPLLSIRDGQPNCYVLKNKDLEQAFKGVIYLEMDLIYNPVKASIRTFTPREKRFVEDSRKLSKKILSRDVDRVKRITMAIWNTMQFLKSCFQWESTLRSTIAFAVFLITVWNFELYMIPLALLLIFVYNFIRPVKGKVSSIQDSQESTDIDDEEDEDDKESEKKGLIERIYMVQDIVSTVQNVLEEIASFGERIKNTFNWTVPFLSSLACLILAAATIILYFIPLRYIILIWGINKFTKKLRNPYSIDNNELLDFLSRVPSDVQKVQYAELKLCSSHSPLRKKRSAL", "text": "FUNCTION: Might play a role in the development of cardiac outflow tract. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MCTP family."}
{"protein": "MNDQTPDRYVTFMGIACDTNADRLCEMLAARMAGNDSRWVAYFEKKLAENAQMGHDRLRFIGAQVNALMSFFEEEDDEAALALLWHIEHHCL", "text": "FUNCTION: Is required to sustain N(2)-dependent growth in the presence of low levels of carbon monoxide (CO). Probably acts by protecting the N(2) fixation ability of the nitrogenase complex, which is inactivated in the presence of CO. SIMILARITY: Belongs to the CowN family."}
{"protein": "MEVRHNWTVVEVKALMDKPFMDLVFEAQLVHRQYQEANYVQVSTLLSIKTGACPEDCKYCPQSAHYRTDVDRERLMEVESVLDAAKKAKDSGSTRFCMGAAWKNPKERDMPYLLDMIKGVKDIGLETCMTLGMITSDQAGELSGAGLDYYNHNLDTSPEFYGNIITTRTYQDRLDTLSHVRDAGMKICSGGIIGMGESVNDRAGLFVELANLPQHPESVPVNMLVKVKGTPLEDAEDVDPFDFIRLIAVARIMMPESAVRLSAGRESMNEQMQALCFMAGTNSVFYGCKLLTTPNPDEDSDMQLFKKLGVNSHQVAQKPDEVQEHELLDRVAERVASRPDKNDLFYEASV", "text": "FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase family."}
{"protein": "MEPSVGIVKTRHIDFNGDLRLESGRLLAAPITLAYETYGQLNADRSNGILVTHAWTGDAHAAGRHTPEDRKPGWWDDMIGPGKVLDTNRYFVICSNVIGSCGGSTGPTSINPRTGRPYNLSFPVIMVRDMVRAQKRLIDHLDLPSLVTVIGGSMGAMQALEWGVLFPDTVRSIIPIAGTGRTSPMAIALNALARQAIFNDPMWKKGNYRPEHPPADGLALGRAIGHISFLSNASMHLKFGRRFSARDGMFDFFGQFEVERYLEYNGRAFIDRFDTNAFLYLAKALDLYDVAWNYDSREQALDRIQCPSLWFTFSSDWLYPPQEAEDIVNILQKLGKPAEYHPIQSDYGHDSFLVEPEKFTHHITEFLNRLTV", "text": "FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family."}
{"protein": "MSLNIETTQGLERRVAITVPTEIVSKAVREEFKRAAKNVRVDGFRKGHVPAHIIEQRFGASIRQDVLNDLLPRHFFDAVIAEKINIAGRPTFAIETFEEGKDLVFTATFEVYPEVKLQGLENIKVEKPTVEITEADIDKMIDVLRKQQATWAESQDVVKADDRVTIDFVGSVDGEEFEGGKATDFVLFMGQGRMIPGFEEGIVGHKAGEQFDIDVTFPAEYHAENLKGKAAKFAITLKKIENMVLPELTDEFVAKFGPNTKSVADLRAEIRKNMERELKNALVSRVKQQVINGLIEQNPIDVPASAVEEEINVLRNQAAQRFGGNAQQTAQLPRELFEAEATRRVQVGLLFSEVIKSNELKADEERAKAMIADIASAYEQPAEVVEYYSKNEELMNNIRNVVLEEQAVDAVLAKAQVTEKVSSFDEIMNPQA", "text": "FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily."}
{"protein": "MSMSKLLSPPPTSPPGPALSRLPCRRVAPPPVLPFPFPLRRLTSRRVFATSCSSSDSEHAPSASSTALAGAGDDLSAGVTQEREGALPFVQLSSGIVLRTEEQSLLGDHAPAPAPASAASSFALLDELNGGCREDDHLGETPAYPAAMNALYAACLAGNATEQLWNFTWPAAVAVLHPASILPVAVLGFFTKLVVFAAGPLVGELISSLPRIPAYRSLAAIQTAAHLVSVATITYAFAVHRAAAASLLLRPWFAVLVASTAVDRLACVALGIIAERDFVVQLAGAGRPVALAKANATLSRVDLLCETVGASIFALLLSKNNPLTCIKLSCVISLCALPLLIFLCGEMNRLADGIFDHSENTTSHAEKTSSFSIRKTVEEAVATVRNGWSEYMRQPVLPASLAYVFVCFNVALAPGALMTTFLIHQGVRPSVIGAFGGSSGAVGILATFATARLVKELGILKAGAAGLIAQSALLGAAVVVYLTGAVSRRAGALFAFLGLIVASRAGHMAYSAIGLQVVQTGNPASKAKLIGATEIAVASLAELAMMAVAVVASDASHFGALAALSATAVTAAAGMYCRWLANPSDELRRIFPS", "text": "FUNCTION: May be involved in iron transport and iron homeostasis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Plastid, chloroplast envelope. SIMILARITY: Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A subfamily."}
{"protein": "MSVVHHLPPGWLLDHLSFINKVNYQLCQHQESFCSKNNPTSSVYMDSLQLDPGSPFGAPAMCFAPDFTTVSGNDDEGSCEVITEKYVFRSELFNVTKPYIVPAVHKERQQSNKNENLVTDYKQEVSVSVGKKRKRCIAFNQGELDAMEYHTKIRELILDGSSKLIQEGLRSGFLYPLVEKQDGSSGCITLPLDACNLSELCEMAKHLPSLNEMELQTLQLMGDDVSVIELDLSSQIIENNSSFSKMITLMGQKYLLPPQSSFLLSDISCMQPLLNCGKTFDAIVIDPPWENKSVKRSNRYSSLSPQQIKRMPIPKLAAADCLIVTWVTNRQKHLCFVKEELYPSWSVEVVAEWYWVKITNSGEFVFPLDSPHKKPYECLVLGRVKEKTPLALRNPDVRIPPVPDQKLIVSVPCVLHSHKPPLTEVLRDYIKPGGQCLELFARNLQPGWMSWGNEVLKFQHMDYFIALESGC", "text": "FUNCTION: N(6)-adenine-specific methyltransferase that can methylate both RNAs and DNA (PubMed:30982744). Acts as a N(6)-adenine-specific RNA methyltransferase by catalyzing formation of N6,2'-O- dimethyladenosine (m6A(m)) on internal positions of U2 small nuclear RNA (snRNA): methylates the 6th position of adenine residues with a pre-deposited 2'-O-methylation (By similarity). Internal m6A(m) methylation of snRNAs regulates RNA splicing (By similarity). Also able to act as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)- methyladenosine) (PubMed:30982744). The existence of N(6)- methyladenosine (m6A) on DNA is however unclear in mammals, and additional evidences are required to confirm the role of the N(6)- adenine-specific DNA methyltransferase activity of METTL4 in vivo (By similarity). Acts as a regulator of mitochondrial transcript levels and mitochondrial DNA (mtDNA) copy number by mediating mtDNA N(6)- methylation: m6A on mtDNA reduces transcription by repressing TFAM DNA- binding and bending (By similarity). N(6)-methyladenosine deposition by METTL4 regulates Polycomb silencing by triggering ubiquitination and degradation of sensor proteins ASXL1 and MPND, leading to inactivation of the PR-DUB complex and subsequent preservation of Polycomb silencing (PubMed:30982744). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MT-A70-like family."}
{"protein": "MLPLPRRQQQVLQATVQHYVDTVEPVGSRTLVRRFGLDASPATVRSAMGALEQKGLLTQPHTSAGRVPSPKGYRQFVDALLPEPGAAVVQLQRELAELSLQWAALDDLLHHLARRLADLTGLMSIITRPQRQEPRLKALRLVRSGDRLLVFLVESSAASSSLNLRLPPDSSAQLQALEHWLNDQLSKSAINWSGLPSHLQSVGAPLKQALASHNRGRNRQAEGALTTGLAGLLCQPEFQLTTSLRPLLQLVEQQPHELLNPAAATASGGVWIGQEHPHPALSGCAVVQAPYATASGGEGSVALVGPMRMAYATALAAVEAVAGTLSRLLA", "text": "FUNCTION: Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. SIMILARITY: Belongs to the HrcA family."}
{"protein": "MAEEEACLFAMSLASASVLPMVLKSAIELDLLELIAKAGPGAYVSPSELAAQLPTHNPEAPIMLDRILRLLATYSVLDCKLNNLADGGVERLYGLAPVCKFLTKNADGVSMAPLLLMNQDKVLMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGTDPRFNKVFNQGMSNHSTITMKKILEVYRGFEGLKTVVDVGGGTGATLNMIISKYPTIKGINFELPHVVEDAPSHSGVEHVGGDMFVSVPKGDAIFMKWICHDWSDDHCRKLLKNCYQALPDNGKVILAECVLPEAPDTSLATQNVVHVDVVMLAHNPGGKERTEKEFEALAKGAGFKEFRKVCSAVNTWIMELCK", "text": "FUNCTION: Catalyzes the conversion of caffeic acid to ferulic acid and of 5-hydroxyferulic acid to sinapic acid. The resulting products may subsequently be converted to the corresponding alcohols that are incorporated into lignins. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
{"protein": "MTTKRKAYVRTMAPNWWQQLGFYRFYMLREGTSIPAVWFSVLLIYGVFALKSGPAGWEGFVSFLQNPLVLFLNILTLFAALLHTKTWFELAPKAVNIIVKSEKMGPEPMIKALWVVTVVASAIILAVALL", "text": "FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FrdC family."}
{"protein": "MATTTTPRLKTKYREEIAGKLREEFSYENVMQIPGLVKIVVNMGVGDAARDSKLIEGAIRDLTTITGQKPAVTKARKSIAQFKLREGQPIGAHVTLRGDRMWEFLDRTLSLALPRIRDFRGLSPKQFDGRGNYTFGLTEQVMFHEIDQDKIDRTRGMDITVVTTATNDAEGRALLRHLGFPFKEA", "text": "FUNCTION: This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
{"protein": "MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLAIRCIHSEEGCRWSGPLRHLQGHLNTCSFNVVPCPNRCPAKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGVCPQESVYCENKCGARMMRRLLAQHATSECPKRTQPCAYCTKEFVYDTIQSHQYQCPRLPVPCPNQCGVGTVAREDLPTHLKDSCSTAFVLCPFKESGCKHRCPKLAMGRHVEESVKPHLAMMCALVSRQRQELQELRRELEELSIGSDGVLIWKIGSYGRRLQEAKAKPNLECFSPAFYTHKYGYKLQVSAFLNGNGSGEGTHLSIYIRVLPGAFDNLLEWPFARRVTFSLLDQSDPGLAKPQHVTETFHPDPNWKNFQKPGTWRGSLDESSLGFGYPKFISHQDIRKRNYVRDDAVFIRASVELPRKILS", "text": "FUNCTION: Adapter protein with E3 ligase activity that is involved in many diverse biological processes including cell proliferation, migration, differentiation, DNA repair, platelet activation or apoptosis. Promotes EGFR-mediated signaling by facilitating the dimerization of EGFR and downstream AKT activation thereby promoting cell proliferation. Ubiquitinates SMURF2 through 'Lys-48'-linked ubiquitin chain leading to SMURF2 degradation through the proteasome and subsequently osteogenic differentiation. Promotes 'Lys-63'-mediated ubiquitination of CHK1 which in turn activates cell cycle arrest and activation of DNA repair. In addition, promotes an atypical 'Lys-29'- linked ubiquitination at the C-terminal end of IRS1 which is crucial for insulin-like growth factor (IGF) signal transduction (By similarity). Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract. Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions. Inhibits adipogenic differentiation by activating pyruvate kinase PKM activity and subsequently the beta- catenin signaling pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, perinuclear region Cell junction, tight junction Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TNF receptor-associated factor family. B subfamily."}
{"protein": "MMFLSFNMISGGNTLQRFDPVACVSSVPLLLAPTTRPTFHFPSPFLSKPKPTYLFTSFSSSSSSSSSFFSSTTPPRSTMLHHDPLVSDVYATAISGVVALSFLRLFQETAKRDLFDQKLNRKLVHISIGLIFMLCXPLFSTETWASFFAALIPGINIFRMLVIGLGILKDEATVKSMSRFGDYRELLKGPLYYAATITLAAIIYWRTSPISIAAICNLCAGDGMADIVGRRLGGEKIPYNKNKSFAGSIAMATAGFLTSIGYMWYFSSFGFIEGSWKLVLGFLLVSIVTAFVESLPISTELDDNLTVPLTSILVGSIIL", "text": "FUNCTION: Involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the polyprenol kinase family."}
{"protein": "MERPQSSIWVFMLLLFMVLLQSPAWHVAAQRCPQTCVCDNSRRHVTCRHQNLTEVPNTIPELTQRLDLQGNILKVLPAAAFQDLPHLTHLDLRNCQVEMVAEGAFRGLGRLLLLNLASNRLSTLPQEALDGLGSLRRLELEGNMLEELRPGTFGALGSLTTLNLAHNALVYLPAMAFQGLLRTRWLQLSHNALSVLAPEALAGLPALRRLSLHHNELQALPGAALSQARSLARLELGHNPLTYTGEEDGLALPGLRELALDHGSLQALGPRAFAHCPRLHTLDLRGNQLTTLPPLQVPGQLRRLRLQGNPLWCACHARPLLEWLVRARVRSDGACRGPRRLRGEALDTLRPSDLRCPGDAAAGDGDGDEDEDRPAGPRAPPLRSPHGEAAWATPCPPACACVAETRHSTCDGRGLQAVPRGFPNDTQLLDLRRNHFPSVPRAAFPGLRHLVSLHLQHCGVAELEPGALAGLDRLLYLYLSHNQLSGLSAAALEGAPNLGYLYLEHNRFLRIPGTALRALPTLVSLHLQDNAVDRLAPGDLAGARALRCLYLSGNHITQVSPGALGPARELEKLHLDRNRLREVPTGALEGLPALKELQLSGNPLRALPDGAFQPVGRSLQQLFLNSSDLEQISPRAFSGLGKGLRSLYLHKNQLQSLPAPLGLSGLELVDLSGNPFHCDCQLLPLHRWLTGLNLRVGATCATPPSVRGQKVKVAAPVFEACPGWTARKAKRTPTSRGSARRTPSLSRH", "text": "FUNCTION: Potential negative modulator of chondrocyte differentiation. Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's differentiation by acting on its cellular collagenous microenvironment. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class IV subfamily."}
{"protein": "MNLLRTFNATLARRPLATQVIVSGAVCGAGDAFTQYLTGQKSWDYKRTARFTCLAAVFIAPPLNVWFRVLERVRHSNRHAQVFSRMSIDQFMFSPFFNAIILVNLRLLEGFSFSKSVDKMKNDWYDVYTSSLRLWPAVQLINFYFVPLNYRVILIQVVAFFWNSWLSFKTQTPALEDPTIE", "text": "FUNCTION: Involved in mitochondria homeostasis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family."}
{"protein": "MSGKGKVHGGKGKSSEIAKSSTSHSARAGLQFPVGRVKRYLKRNAQNKIRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDNLIKATIAYGGVLPHINKALLLKVEKKKGQK", "text": "FUNCTION: Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes. Involved in chromosome stability (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H2A family."}
{"protein": "MPYSADLDIRVTDSSLRDGSHAKRHQFTVEHVRSIVGALDAAGVPVIEVTHGDGLGGSSFNYGFSHTPEQELIKAAVETAERARIAFLMLPGLGVQSDIREAADNGASICRIATHCTEADISVQHFGLARELGLETVGFLMMSHSQPPEVLAKQARIMADAGCQCVYVVDSAGALILNAVSDRVSALVAELGDDAQVGFHGHENLGLGVANSVLAVEAGALQIDGSTRRFGAGAGNTPVEAFAAVTEKLGIRTGIDTLKIIDAAEDVVRPIMDGDCQLDRLSLMMGYAGVYSSFLKHADSHARRYGVSGAEILIEAGRRKLVGGQEDQLIEIALGLADRGPAGSAVAEKKSA", "text": "SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family."}
{"protein": "MSYGFVAYNLPKVQGTYRRGVKMHNATWFNVGGVAEVVFKPSSVEDLAAFVRDTNLPISVVGVASNLIVRDGIVKGVVVKLGREFSYINCNGNIITAGCATLLSNLAVAAQESGISGLEFFVGIPGTVGGAIEMNAGAYGGDVASVLRSVRAVNEHGEICTLSNDDMRYSYREHGLVGKWIFVDATFVGACGDRDAIKGTMREFIARRNDSQPVRGRTGGSTFKNPEGHQAWELIDKAGCRGLQIGGAQVSEKHCNFLLNCGGATAKDLEDLGNEIRCRVHSMFGIKLEWEIRFLGCGL", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurB family."}
{"protein": "MRFYNRYNSSLKNYLLCSINSFNTNTLKIPLKPTLSAVFNTFRGERSLKFIKLYLMILYISNQKPFIKKVKFSYIKKKILKRFFISVSLNKKNSFNFFMYMLNFYNYFFHIYYQKCLKYNRFENSLILYIDNIQFFFKNYNKQNQKTQIKCQLNLRNSQASILFKYLNNMFLIKVKN", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
{"protein": "MNYPGRGSPRSPEHNGRGGGGGAWELGSDARPAFGGGVCCFEHLPGGDPDDGDVPLALLRGEPGLHLAPGTDDHNHHLALDPCLSDENYDFSSAESGSSLRYYSEGESGGGGSSLSLHPPQQPPLVPTNSGGGGATGGSPGERKRTRLGGPAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQTTGARPQGGDRDGDHVCSPTGPASSSGEDDDEDRACGFCQSTTGHEPEMVELVNIEPVCVRGGLYEVDVTQGECYPVYWNQADKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLNCFRGQQMQENFDIEVSKSIDGKDAVHSFKLSRNHVDWHSVDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTTHIVFVVHGIGQKMDQGRIIKNTAMMREAARKIEERHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPDFEEKGGKVSIVSHSLGCVITYDIMTGWNPVRLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLKEIEERLHGLKASSMTQTPALKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEHMKPSFLNPAKEPTSVSENEGISTIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSTTQSSETSKDSMEDEKKPVASPSATTVGTQTLPHSSSGFLDSAYFRLQESFFNLPQLLFPENVMQNKDNALVELDHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDDDAKPNLDPI", "text": "FUNCTION: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid (PubMed:20359546, PubMed:22922100). Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl- sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2- diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2- diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2- diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (PubMed:20359546) (By similarity). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology (PubMed:24599962). These dynamic changes may be due to PA hydrolysis at the mitochondrial surface (PubMed:24599962). May play a regulatory role in spermatogenesis or sperm function (PubMed:24599962). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PA-PLA1 family."}
{"protein": "MKASDLNKSTVDELRSTEAELTKELFNLKFQLHTGRLEDTSKPARIKKDIARVKSVLRAKRG", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MSGTELDEPGKLKRAVIDASAGGVAGAISRMVTSPLDVIKIRFQVQLEPTATWALKDSQLKPKYNGLFRTTKDIFREEGLSGFWRGNVPALLMVVPYTSIQFAVLHKVKSFAAGSSKAENHAQLSPYLSYISGALAGCAATVGSYPFDLLRTVLASQGEPKVYPNMRSAFLSIVQTRGIKGLYAGLSPTLIEIIPYAGLQFGTYDTFKRWSMVYNKRYRSSSSSSTNPSDSLSSFQLFLCGLASGTVSKLVCHPLDVVKKRFQVEGLQRHPKYGARVELNAYKNMFDGLGQILRSEGWHGLYKGIVPSTIKAAPAGAVTFVAYELASDWFEANLT", "text": "FUNCTION: Mitochondrial transporter that mediates uptake of thiamine diphosphate (ThDP) into mitochondria. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MRALWIVAVCLIGVEGSMIEFGKMIQEETEKNPITSYSLYGCHCGLGSKGKPKDATDRCCFVHSCCYAKLSDCSPKTNRYEYHRENGTIVCGSSTFCKKQICECDRAAAICFRENLKTYNKKYKVYLRFKCKGVPEKC", "text": "FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic activity (PubMed:25522251). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)=2.18 uM) (PubMed:25522251). This activity is only partially reversible and seems to be non-competitive (PubMed:25522251). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. S49 sub-subfamily."}
{"protein": "MSGHNKWSTIKHKKGAADAKRGKIFTKIIKEISVAAKLGGGDPAANPRLRTAIDKAKGENMPKDNIERAIKKGTGGMEGVVYEEIVYEGYGPGGVAVLVEVMTDNRNRTVSEVRSIFTKCNGNMGEAGCVAWMFDKKGVISYDTSLDFDQLFEAALEAGAEDVVEEDEQIEVYTEPSSFIEVRDALEAKGFKFQSAEITMIPQTQVALEGKQAESMLKMMDRLEDCDDVQNVYANFDISADEMEKMM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TACO1 family."}
{"protein": "MEGVLYKWTNYLTGWQPRWFVLDNGILSYYDSQDDVCKGSKGSIKMAVCEIKVHPADNTRMELIIPGEQHFYMKAVNAAERQRWLVALGSSKACLTDTRTAKEKEISETSESLKTKMSELRLYCDLLMQQVHTIQEFVHRDERHPSPSVENMNEASSLLSATCNTFITTLEECVKIANAKFKPEMFQLPHPDPLVSPVSPSPVQMMKRSASHPGSCSSERSSCSIKEPASALHRLPQRRRRTYSDTDSCNDVPPEDPERPLHCSGNTLNGDLASATIPEESRLMAKTQSEEPLLPFS", "text": "FUNCTION: Plays a role in regulation of vesicular cargo transport from the trans-Golgi network (TGN) to the plasma membrane (By similarity). Regulates Golgi phosphatidylinositol 4-phosphate (PtdIns(4)P) levels and activates the PtdIns(4)P phosphatase activity of SACM1L when it binds PtdIns(4)P in 'trans' configuration (By similarity). Binds preferentially to PtdIns(4)P (By similarity). Negatively regulates APOB secretion from hepatocytes (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Note=Localizes to ER-trans Golgi network (TGN) contacts sites."}
{"protein": "MSSWTSKENINGVYIPSALLIFGTTIIKKEWIAYATALAVVLSAWKLFSNKPRKVLNPTEFQNFVLKDKTIVSHNVCIYRFALPRPTDILGLPIGQHISLAATIPGQSKEIVRSYTPISSDDDAGYFDLLVKSYPQGNISKHLTTLRIGDKMKVRGPKGAMVYTPNMVRHIGMIAGGTGITPMLQVIKAIIKGRPRNGGNDTTQIDLIFANVNPDDILLKEELDQLAKEDDAFRIYYVLNNPPEKWNGGVGFVTPDMIKAKLPAPAGDIKVLICGPPPMVSAMKKATESLGYKKANLVSKLEDQVFCF", "text": "FUNCTION: NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L- methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2- thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
{"protein": "MQLSSTKPSSKTREPSTAQDIVTMQNILEKLYRAESISRQESQALFGAIIRGELEASQLAAALISMKVRGEHPDEIAGAATALLADAQPFPRPDYLFADIVGTGGDGTNSINISTASAFVAASCGLKIAKHGNRSVSSRSGSSDLLSAFGIKLDMSAQDSRQALDDLGVCFLFAPQYHLGFRHAMPVRQQLKTRTVFNVLGPLVNPARPPLALIGVYSPELVRPIAETLKVLGYQRAAVVHGGGMDEVAIHAPTQVAELNNGEIETYELTHRDFGLDTYSLSALQGGTPEENRDILASLLQGKGERAHAAAVAANVALLLRLFGQENLRQNAQQALEVIHSGQAYQRVIALSARG", "text": "FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase family."}
{"protein": "MVKTVAVMVGSLRKDSLAHKLMKVLQK", "text": "FUNCTION: Reductase activity that acts on Fe(3+)-chelates and uses both NADH and NADPH as electron donors. May play a role in iron uptake."}
{"protein": "MSTDWKDLPVAPWLIDTMEQFGFTDMTPVQASVIPMFAGNKDVIVEAVTGSGKTIAFLVPLIQRMLNLLKEGPAVSGRVYSVVVSPTRELARQTYEVLQSILEMGCPEADASDKITLEKKKKGKAAPTMPKKIRGQLIMGGDLPSHMDLKNFLRDKPQIIVATPGRLLELLRAPQIKTSAFDSLVLDEADRLLDLGFGRDITSIINILPKQRRTGLFSATITDAIQNLVKIGLRNPVKIVVKVGGKKEQKTPLSLGLSYVVLEPREKLAYALNLLSIYPYRKAIVYLPTCAAVTYYQQMFSHLNEGREEPYEIYGLHGKLPSSTRIKILNKYQKTGAQAILMTTDIAARGLDIPEVDLVVQLDPPSDADTFQHRCGRAGRAGRQGQAIVLLHKGREEEYVDLMRVRKVKLRPYTGPGSELEGEKLDQEATELYTKLRKWVLEDRQRHDQALLSFVSFVRFYSKHVAQSIFRIQSLDLPGLAASYGLLRLPKMPELRTKDNERPENTWLGEVIDFDTYSYKNPAKEEARLKELEAHKEAMKNKVKIHKTKNDVQKANRAWSSTLQKKEEKSERHQKKQTRINEKIKRDFEEAKDLKQEESKEVVNDWKDMVKKSKKRKVDLPTFDDL", "text": "FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre- rRNAs at sites C1 and C2 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4 subfamily."}
{"protein": "MADLAKIEEQLSSLTLMQAAELVKMLEEKWGVSAAAPVAVAAVGAAAPAAEAVAEKTEFEVVLTAAGDKKVEVIKVVKDITGLGLIEAKKLVDEAPKPIKSNVKKAEADEIKGKLEAAGAKVELK", "text": "FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family."}
{"protein": "MAPMKLYGSTLSWNVTRCVAVLEEAGAEYEIVPLDFSKGEHKAPDHLARNPFGQVPALQDGDLFLWESRAICKYVCRKNKPELLKDGDLKESAMVDVWLEVESNQYTPALNPILFQCLIRPMMFGAPPDEKVVEENLEKLKKVLEVYEARLTKCKYLAGDYISVADLSHVAGTVCLGATPHASVLDAYPHVKAWWTDLMARPSSQKVASLMKPPA", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SIMILARITY: Belongs to the GST superfamily. Phi family."}
{"protein": "MAKIIGIDLGTTNSCVSVMEGGEPVVIPNAEGSRTTPSVVSFQANGERLIGQVAKRQAITNPEKTIISIKRYMGTDHKVNIDSTEYTPQQISAMVLQKLKADAEAYLGEKVTQAVITVPAYFNDSQRQATKDAGKIAGLEVLRIINEPTAASLAYGLDKMDTNEKILVYDLGGGTFDVSILELGDGVFEVKATNGDTKLGGDDFDQKLIDYIAETFKAENGIDLRNDKMAIQRLKEAAEKAKIELSSATQTNINLPFITADATGPKHIDMNLTRAKFNELTHDLVQRTLEPIKKSLEGSGYAMSDIDKIIMVGGSTRIPAVQDAVKDFTGKELSKGVNPDEVVAMGAAIQAGVLTGEVKDVLLLDVTPLTLGIETFGGVSTTLIEKNTTIPTRKSQVFSTAADGQTSVEIHVVQGERSMAADNKTLGRFTLSGIAPAPRGIPQIEVTFDIDANGIVNVSAKDKGTGKEANITITASTNLTDDEIEKAVNEAKKFEAEDKKRKESIEIKNNADQIVYQTEKTLTDLGDKVSAEDKAQIEEKVKAVKDVKDGEDLEAIKKATEDLTQTFYGISSKIYQQANPEGAQGAGFDPNNMGGANAGNASAGNDKKDDNVVDADFKVEDDK", "text": "FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "EIGSTIPNATFAYVPYSPELEDHKVCGMPTSFQSHERWKGKKVVIVAVPGAFTPTCTANHVPPYVEKIQELKSKGVDEVVVISANDPFVLSAWGITEHAKDNLTFAQDVNCEFSKHFNATLDLSSKGMGLRTARYALIANDLKVEYFGIDEGEPKQSSAATVLSKL", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily."}
{"protein": "MKLIEQHQIFGGSQQVWAHNAQTLQCEMKFAVYLPNNPENRPLGVIYWLSGLTCTEQNFITKSGFQRYAAEHQVIVVAPDTSPRGEQVPNDAAYDLGQGAGFYLNATEQPWATNYQMYDYILNELPDLIEANFPTNGKRSIMGHSMGGHGALVLALRNRERYQSVSAFSPILSPSLVPWGEKAFSAYLGEDREKWQQYDASSLIQQGYKVQGMRIDQGLEDEFLPTQLRTEDFIETCRVANQPVDVRFHKGYDHSYYFIASFIGEHIAYHAEFLK", "text": "FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate (By similarity). SIMILARITY: Belongs to the esterase D family."}
{"protein": "MLSALRTAGALSTRRLASTQAIASNSEAPKGIATTGTPFLNPSSKAEYALARLDDVMNLAQRGSIWPLTFGLACCAVEMMHFAAPRYDMDRYGVVFRASPRQADLIFVAGTVTNKMAPALRRIYDQMPEAKWVISMGSCANGGGYYHYAYSVLRGCDRVIPVDIYVPGCPPTAEALLYGVLQLQKKIKRKREAQLWYRR", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MKRTPHLLAIQSHVVFGHAGNSAAVFPMQRIGVNVWPLNTVQFSNHTQYGQWAGEVLAPAQIPALVEGISNIGELGHCDAVLSGYLGSAEQGRAILAGVERIKAVNPKALYLCDPVMGHAEKGCIVPQEVSEFLLDDAVAQADILCPNQLELDSFCGRRAQSLEDCVRMARGLLERGPQVVLVKHLAYPGRCEDMFEMLLVTRDHSWHLRRPLLAFPRQPVGVGDLTSGLFLARVLLGDSWVQAFEYTAAAVHEVLLETQACASYELQLVRAQDRIAYPRVRFEAQRLAF", "text": "FUNCTION: Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP. SIMILARITY: Belongs to the pyridoxine kinase family. PdxY subfamily."}
{"protein": "MDRYSRRNLEDLVVPNYQETSDSYPSPDMWGTGWSMNSSEAAEKCFDYDVIHNGFSGGLYSQMEMDMGTSEQVEEETKKLKASGCFDRSLHDFDEIQHMDDMFLSSILEDVPGNENFLSFKESDNNNSSSSSYLDTTDGREVPLFHYNWETCQDMPLMEEDAPMNLCEENKEEASAEEVVLQDLQRATEMLTDDTRKCFRDTFYRLAKNSQQKSDSNSDEFLEDRTRETEFETKLNRQSRGQSHIQQDGIQHEKYASTEETFFCSRIREFHHIW", "text": "FUNCTION: Probable transcriptional coactivator."}
{"protein": "MKLLIDVGNTSLKAKLWQNEQVQACDLNNLPWHAITHVIYACVGRSELLNAILAQAAFNSISCFEAKVTKTLGGLTCAYEHFNNLGIDRWLALIASFTLYPNKACIVVDAGTATTIDVLNCDGQHLGGWILPGLDLMTRSLTQNTQRVFDDENTPFTNQLGINTPNGLKNGALVATIGAINQAKPYLNDKNTQIIFAGGYGSLLQQQFKESIFDPMLVIKGLNYWYELDENSNKL", "text": "FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type III pantothenate kinase family."}
{"protein": "MKGVKKEGWISYKVDGLFSFLWQKRYLVLNDSYLAFYKSDKCNEEPVLSVPLTSITNVSRIQLKQNCFEILRATDQKENISPINSYFYESNSKRSIFISTRTERDLHGWLDAIFAKCPLLSGVSSPTNFTHKVHVGFDPKVGNFVGVPDSWAKLLQTSEITYDDWNRNSKAVIKALQFYEDYNGLDTMQFNDHLNTSLDLKPLKSPTRYIINKRTNSIKRSVSRTLRKGKTDSILPVYQSELKPFPRPSDDDYKFTNIEDNKVREEGRVHVSKESTADSQTKQLGKKEQKVIQSHLRRHDNNSTFRPHRLAPSAPATKNHDSKTKWHKEDLLELKNNDDSNEIIMKMKTVAIDVNPRPYFQLVEKAGQGASGAVYLSKRIKLPQENDPRFLKSHCHRVVGERVAIKQIRLSEQPKKQLIMNELLVMNDSRQENIVNFLEAYIIDDEELWVIMEYMEGGCLTDILDAVARSNTGEHSSPLNENQMAYIVKETCQGLKFLHNKKIIHRDIKSDNILLNSQGLVKITDFGFCVELTEKRSKRATMVGTPYWMAPEIVNQKGYDEKVDVWSLGIMLIEMIEGEPPYLNEDPLKALYLIANNGSPKLRHPESVSKQTKQFLDACLQVNVESRASVRKLLTFEFLSMACSPEQLKVSLKWH", "text": "FUNCTION: May be involved in cellular signaling or cytoskeletal functions. May play a role in morphogenetic control. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MLTRKIKLWDINAHITCRLCSGYLIDATTVTECLHTFCRSCLVKYLEENNTCPTCRIVIHQSHPLQYIGHDRTMQDIVYKLVPGLQEAEMRKQREFYHKLGLEVPGDIKGETCSAKQHLDPHRNGETKADDSSNKEAAEEKQEEDGDYHRSDEQVSICLECNSSKLRGLKRKWIRCSAQATVLHLKKFIAKKLNLSSFNELDILCNEEILGKDHTLKFVVVTRWRFKKAPLLLHYRPKMDLL", "text": "FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (By similarity). Plays a redundant role with PCGF5 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Note=Recruited by the non- coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome."}
{"protein": "MVESTTLVNQTWWYNPTVDIHPHWAKFDPIPDAVYYSVGIFIGVVGIIGILGNGVVIYLFSKTKSLQTPANMFIINLAMSDLSFSAINGFPLKTISAFMKKWIFGKVACQLYGLLGGIFGFMSINTMAMISIDRYNVIGRPMAASKKMSHRRAFLMIIFVWMWSIVWSVGPVFNWGAYVPEGILTSCSFDYLSTDPSTRSFILCMYFCGFMLPIIIIAFCYFNIVMSVSNHEKEMAAMAKRLNAKELRKAQAGASAEMKLAKISMVIITQFMLSWSPYAIIALLAQFGPAEWVTPYAAELPVLFAKASAIHNPIVYSVSHPKFREAIQTTFPWLLTCCQFDEKECEDANDAEEEVVASERGGESRDAAQMKEMMAMMQKMQAQQAAYQPPPPPQGYPPQGYPPQGAYPPPQGYPPQGYPPQGYPPQGYPPQGAPPQVEAPQGAPPQGVDNQAYQA", "text": "FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G- proteins. Signaling mediates the activation of phospholipase C (By similarity). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Note=Detected on the rhabdomere membrane in the photoreceptor outer segment. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MADEQTLDTQNLDANQAPEASGDDLAARVQVLEEQLAGAQDQALRVAADLQNVRRRAEQDVEKAHKFALEKFAGDLLPVIDSLERGLELSNPDDESIRPMREGIELTLKMFHDTLKRYQLEAIDPHGEPFNAEQHQAMAMQESADVEPNSVLKVFQKGYQLNGRLLRPAMVVVSKAPAPVSPSIDEKA", "text": "FUNCTION: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GrpE family."}
{"protein": "MAFDDKMKPVNGQPDQKSCGKKPKGLHLLSSTWWCPAAVTLAILCLVLSVTLIVQQTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANSSGPCPQDWIWHKENCYLFHGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSPFWMGLHRKNPNHPWLWENGSPLSFQFFRTRGVSLQMYSSGTCAYIQGGVVFAENCILTAFSICQKKANLLLTQ", "text": "FUNCTION: Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Cell membrane; Single-pass type II membrane protein Membrane raft Secreted Note=A secreted form also exists. Localization to membrane rafts requires palmitoylation (By similarity)."}
{"protein": "MAGGGVWVFRNNGVMELEEQATSRKALVHVATSEVIRSTEALERRLGALGWERYYEDRATLQLHRRDGSADLISIPRDFSRFRSTHMYDVVVKNRDHFKVVDLHT", "text": "SIMILARITY: Belongs to the FPF1 family."}
{"protein": "MGLQQEISLQPWCHHPAESCQTTTDMTERLSAEQIKEYKGVFEMFDEEGNGEVKTGELEWLMSLLGINPTKSELASMAKDVDRDNKGFFNCDGFLALMGVYHEKAQNQESELRAAFRVFDKEGKGYIDWNTLKYVLMNAGEPLNEVEAEQMMKEADKDGDRTIDYEEFVAMMTGESFKLIQ", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the calmodulin family. Calglandulin subfamily."}
{"protein": "MGIGVNTDLPRNEQIKAPKVRVVDENGKMIGVMPTRKALELAREKGLDLVLVAPNENPPVARIMDYGKYKYQLTKKQKENKKKPVQMKQMKFRLKIDEHDYQTKVKHIRRFLEDGHKVRVVVMFIGREMMFAEKGKEILERVIKDTEDLATVESPPKMEGRDMWMVLKPKNS", "text": "FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IF-3 family."}
{"protein": "MRSGAERRGSSAAAPPSSPPPGRARPAGSDVSPALPPPAASQPRARDAGDARAQPRPLFQWSKWKKRMSMSSISSGSARRPVFDDKEDVNFDHFQILRAIGKGSFGKVCIVQKRDTEKMYAMKYMNKQQCIERDEVRNVFRELEILQEIEHVFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQQNVQFSEDTVRLYICEMALALDYLRSQHIIHRDVKPDNILLDEQGHAHLTDFNIATIIKDGERATALAGTKPYMAPEIFHSFVNGGTGYSFEVDWWSVGVMAYELLRGWRPYDIHSSNAVESLVQLFSTVSVQYVPTWSKEMVALLRKLLTVNPEHRFSSLQDMQTAPSLAHVLWDDLSEKKVEPGFVPNKGRLHCDPTFELEEMILESRPLHKKKKRLAKNKSRDSSRDSSQSENDYLQDCLDAIQQDFVIFNREKLKRSQELMSEPPPGPETSDMTDSTADSEAEPTALPMCGSICPSSGSS", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MEHFQQVEPFDYVIFGATGDLTMRKLLPALYNRLRMGQIPDDACIIGAARTELDREAYVARARDALERFLPSDILGPGLVERFLARLDYVTLDSSREGPQWDALKSLLAKAQPDRVRVYYFATAPQLYGSICENLNRYELITPTSRVVLEKPIGTNMATATAINDGVGQYFPEKQIYRIDHYLGKETVQNVLALRFANPLMNAAWSGEHIESVQITAVETVGVEGRAAYYDTSGALRDMIQNHLLQVLCLVAMEAPDSLEADAVRNAKLAVLNALRPITDATAATETVRAQYTAGVVDGENVPGYLEELGKPSATETYAAIRAWVDTPRWKNVPFYIRTAKRSGKKVSEIVVTFRPAATTMFGATPASNRLVLRIQPNEGVDLRLNVKNPALDVFNLRTADLDTSIRMEGGLPFPDSYERLLLDAVRGDPVLFIRRDEVEAAWRWVEPILEAWKHDKAPMQTYSAGSYGPEQATQLLASHGDTWHEASE", "text": "FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family."}
{"protein": "MLRAQRPRLARLRACLSRGLHHKPVMALRREDVNAWERRAPLAPKHIKGITKLGYKVLIQPSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEKLMSKKTYAFFSHTIKAQEANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHLGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPCEYVEPHELREVSKTGDLRKVYGTVLSRHHHLVRKTDGVYDPVEYEKYPERYTSRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLVPVKSSVVPVEGCPELPHKLVAICDISADTGGSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPYVEEMLLSDASQPLESQNFSPVVRDAVITSNGLLTDKYKYIQKLRESRERIQFLSMSTKKKVLVLGSGYVSGPVLEYLSRDNNIEITLGSDMTNQMQQLSKKYNINPVSLTVGKQEAKLQSLVESQDLVISLLPYVLHPVVAKACIESRVNMVTASYITPAMKELEKSVDDAGITVIGELGLDPGLDHMLAMETIDTAKELGATVESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPASYLLNGKVVNVTGGVSFLNSVTPMDYFPGLNLEGYPNRDSIKYAEIYGISSAHTLLRGTLRYKGYSKALNGFVKLGLINREAYPALRPEANPLTWKQLLCDLVGISRSSPCEKLKEVVFTKLGGDNTQLEAAEWLGLLGDEQVPQAESIVDAFSKHLVSKLSYGPEEKDMIVMRDSFGIRHPSGHLENKTIDLVVYGDFNGFSAMAKTVGLPTAMAAKMLLDGEIEAKGLMGPFTKEIYGPILERIKAEGIVFNTQSTIKL", "text": "FUNCTION: Bifunctional enzyme that catalyzes the first two steps in lysine degradation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: In the C-terminal section; belongs to the saccharopine dehydrogenase family. SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family."}
{"protein": "MSEIKLIVGLGNPGDKYADTRHNAGEWLINRLARQFHFSLTPESKFSGKTARTVINGNEIRFLVPTTFMNLSGKAISSLANFYRIKPEEILVIHDELDLPPGVAKIKQGGGHGGHNGLRDTIAQLGNNKNFYRLRVGIGHPGDKNLVSAYVLNKPSLTDWQLIDKALDEATSCVDILIKDGITKATNRLNAFKA", "text": "FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PTH family."}
{"protein": "MPDHSHIYIGSAFVAGVVLTIAFKDLFYPEIEERIRDYRARHSSKSYQNASVDSLAVRHGPPAIVDGIEGCIGNTPLLRIKSLSEATGCEILAKAEFLNGAGQSSKDRVALSMIELAEERGLMTPHSGDTIYEGTSGSTGISLATLARAKGYLAHICMPSDQAIEKSNLLLKLGAIVDRVPPAPIVEKDNFVNRARALAQAHTNSTASESSVGTASQRGRGYFADQFENEANWRAHYNGTGPEIYAQCNGSLDAFVAGAGTGGTISGVALYLKPRIPNMTVVVADPQGSGLYNRVRYGVMFDTKEKEGTRRRRQVDTIVEGIGINRVTANFEAGRELVDDAVRVTDAQALAMARWLVEKDGIFAGSSSAVNCFAAVKTALKLGPGHRIVTMLSDSGSRHLSRFWAKAGNVGGAVDTKLEDVLNAKEDQ", "text": "FUNCTION: Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, in contrast to cysteine synthase cysB, this CS-like protein seems not to function in cysteine biosynthesis. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family."}
{"protein": "MLRLQMTDGHISCTAVEFSYMSKISLNTPPGTKVKLSGIVDIKNGFLLLNDSNTTVLGGEVEHLIEKWELQRSLSKHNRSNIGTEGGPPPFVPFGQKCVSHVQVDSRELDRRKTLQVTMPVKPTNDNDEFEKQRTAAIAEVAKSKETKTFGGGGGGARSNLNMNAAGNRNREVLQKEKSTKSEGKHEGVYRELVDEKALKHITEMGFSKEASRQALMDNGNNLEAALNVLLTSNKQKPVMGPPLRGRGKGRGRIRSEDEEDLGNARPSAPSTLFDFLESKMGTLNVEEPKSQPQQLHQGQYRSSNTEQNGVKDNNHLRHPPRNDTRQPRNEKPPRFQRDSQNSKSVLEGSGLPRNRGSERPSTSSVSEVWAEDRIKCDRPYSRYDRTKDTSYPLGSQHSDGAFKKRDNSMQSRSGKGPSFAEAKENPLPQGSVDYNNQKRGKRESQTSIPDYFYDRKSQTINNEAFSGIKIEKHFNVNTDYQNPVRSNSFIGVPNGEVEMPLKGRRIGPIKPAGPVTAVPCDDKIFYNSGPKRRSGPIKPEKILESSIPMEYAKMWKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFIDYGNYEEVLLSNIKPIQTEAWEEEGTYDQTLEFRRGGDGQPRRSTRPTQQFYQPPRARN", "text": "FUNCTION: Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins (PubMed:15955813). Plays a role in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine- methylated loci (PubMed:21172665). In cytoplasm, acts as an antiviral factor that participates in the assembly of stress granules together with G3BP1 (PubMed:35085371). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. Associated with actively translating polyribosomes. Component of stress granules (PubMed:18664458, PubMed:35085371)."}
{"protein": "MPFEIVFEGAKEFAQLIDTASKLIDEAAFKVTEDGISMRAMDPSRVVLIDLNLPSSIFSKYEVVEPETIGVNMDHLKKILKRGKAKDTLILKKGEENFLEITIQGTATRTFRVPLIDVEEMEVDLPELPFTAKVVVLGEVLKDAVKDASLVSDSIKFIARENEFIMKAEGETQEVEIKLTLEDEGLLDIEVQEETKSAYGVSYLSDMVKGLGKADEVTIKFGNEMPMQMEYYIRDEGRLTFLLAPRVEE", "text": "FUNCTION: Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. Unlike its eukaryotic paralog, loads on circular DNA without the replication factor C (RFC) clamp loader, although RFC greatly increases loading efficiency. Stimulates the ATPase activity of replication factor C (RFC) in the presence of ssDNA. Stimulates the helicase activity of Hel308 and may alter its substrate specificity. SIMILARITY: Belongs to the PCNA family."}
{"protein": "MMNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSAGVNNNNNNSSSSNNNNNNNNNAQNNNSGRNGSQSNDNGNNIKDTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYTLFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWESGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE", "text": "FUNCTION: Plays an important role in the cellular response to the nitrogen source. URE2 gene plays a major part in the repression of GLN1 and GDH2 genes by glutamine, and is required for the inactivation of glutamine synthetase. URE2 gene product may catalytically inactivate GLN3 in response to an increase in the intracellular concentration of glutamine (By similarity). SIMILARITY: Belongs to the GST superfamily."}
{"protein": "MGFVDGFSAFLHSSGAVKFGDFELSGGGRSPYYFDLRSVPSHPHQFRGMIRGLLDSVISEVGLDRFDTLASIPTGGLVVASALAIEAVKPLVYARAAAKGHGTGRTVEGIVRYGARALIIDDVATTGGSVIRAAESLRAAGAIVTDAFVVIDRMEGAEGRLGAEGIKLHRLAGALEVARSLHAAGLIPGDVMRQVEGRTR", "text": "FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily."}
{"protein": "MRSNYIVIEGLEGAGKTTARNVVVETLEQLGIREMIFTREPGGTQLAEKLRSLVLDIKSVGDEVITEKAEVLMFYAARVQLVETVIKPALAKGTWVIGDRHDLSTQAYQGGGRGVDQTMLATLRDAVLGDFRPDLTLYLDVTPEVGLKRARARGELDRIEQESFDFFNRTRARYLELAAQDASIRTIDATQSLECVMADIRQTVTTWVKEQGA", "text": "FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. SIMILARITY: Belongs to the thymidylate kinase family."}
{"protein": "MKAFGPPHEGPLQGLVASRIETYGGRHRASAQSTAGRLYPRGYPVLDPSRRRLQQYVPFARGSGQARGLSPMRLRDPEPEKRHGGHVGAGLLHSPKLKELTKAHELEVRLHTFSMFGMPRLPPEDRRHWEIGEGGDSGLTIEKSWRELVPGHKEMSQELCHQQEALWELLTTELIYVRKLKIMTDLLAAGLLNLQRVGLLMEVSAETLFGNVPSLIRTHRSFWDEVLGPTLEETRASGQPLDPIGLQSGFLTFGQRFHPYVQYCLRVKQTMAYAREQQETNPLFHAFVQWCEKHKRSGRQMLCDLLIKPHQRITKYPLLLHAVLKRSPEARAQEALNAMIEAVESFLRHINGQVRQGEEQESLAAAAQRIGPYEVLEPPSDEVEKNLRPFSTLDLTSPMLGVASEHTRQLLLEGPVRVKEGREGKLDVYLFLFSDVLLVTKPQRKADKAKVIRPPLMLEKLVCQPLRDPNSFLLIHLTEFQCVSSALLVHCPSPTDRAQWLEKTQQAQAALQKLKAEEYVQQKRELLTLYRDQDRESPSTRPSTPSLEGSQSSAEGRTPEFSTIIPHLVVTEDTDEDAPLVPDDTSDSGYGTLIPGTPTGSRSPLSRLRQRALRRDPRLTFSTLELRDIPLRPHPPDPQAPQRRSAPELPEGILKGGSLPQEDPPTWSEEEDGASERGNVVVETLHRARLRGQLPSSPTHADSAGESPWESSGEEEEEGPLFLKAGHTSLRPMRAEDMLREIREELASQRIEGAEEPRDSRPRKLTRAQLQRMRGPHIIQLDTPLSASEV", "text": "FUNCTION: Guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Also activates RHOG. Does not activate RAC1, or to a much lower extent than RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and RHOA, at the cleavage furrow to advance furrow ingression during cytokinesis. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with EZR, required for normal macropinocytosis. SUBCELLULAR LOCATION: Cell projection, microvillus Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Cleavage furrow Note=During mitosis, localizes to the spindle pole, central spindle and cleavage furrow (PubMed:16721066). In epithelial cells, recruited to the apical membrane by EZR where it participates in macropinocytosis (PubMed:17881735)."}
{"protein": "MRIDIITVLPEMIENTLNCSIIGRAQERGLLELKLHQLRDYSTDKWKRVDDYPFGGEPGMVMQVEPIDRIITELKTQREYDEVIFTSPDGERFDQPMANELSLLSNLIILCGHYKGIDYRIREHLITREISIGDYVLTGGELAAAVMTDAIARLIPGVLNDAGSALSDTFQDNLLAPPVYTRPAEYKGWRVPDILLSGHEANIAKWRLEQAVERTKRLRPDLIKD", "text": "FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family."}
{"protein": "MEEKGSRMVQQGNQEAAAAPDTMAQPYASAQFAPPQNGIPAEYTAPHPHPAPEYTGQTTVPEHTLNLYPPAQTHSEQSPADTNAQTVSGTATQTDDAAPTDGQPQTQPSENTENKSQPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKTVNPYTNGWKLNPVVGAVYSPEFYAGTVLLCQANQEGSSMYSAPSSLVYTSAMPGFPYPAATAAAAYRGAHLRGRGRTVYNTFRAAAPPPPIPAYGGVVYQDGFYGADIYGGYAAYRYAQPTPATAAAYSDRNQFVFVAADEISCNTSAVTDEFMLPTPTTTHLLQPPPTALVP", "text": "FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue- specific exons and of differentially spliced exons during erythropoiesis (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MGLPWYRVHTVVLNDPGRLISVHIMHTGLVSGWAGSMAFYELAVFDPSDPVLNPMWRQGMFVLPFMTRLGISKSWGGWDINGDSITDPGLWSYEGVAATHIILAGLMFLASMWHWVYWDLELFRDPRTGKPALDLPKIFGIHLFLSGLLCFGFGAFHVTGLFGPGIWVSDPYGITGRVQPIEPSWGADGFDPFNPGGIASHHIAAGILGILAGLFHLSVRPSFRLYKALRMGNVETVLSSSIAAVFWAAFVVSGTMWYGSAATPIELFGPTRYQWDLGYFNKEINKRVQASIASGSTASEAWSRIPEKLAFYDYIGNNPAKGGLFRAGAMNNGDGIAAGWLGHAVFKDKEGRELFVRRMPTFFETFPVVLLDKDGIVRADIPFRRAESKYSIEQVGVSVAFYGGELDGVTFKDPTTVKKYARRAQLGEIFEFDRARLKSDGVFRSSPRGWFTFGHLCFALLFFFGHIWHGARTIFRDVFAGIDPDLDEQVEFGAFQKLGDASTRKQAV", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily."}
{"protein": "MANYTAADVKRLRELTGAGMLDSKNALVEAEGDFDKAVELLRIKGAKDVGKRAERATAEGLVAAKDGALIELNSETDFVAKNGEFQALADQIVAAAAAAKAADVDALKAVKLGDTTVEQAIADLSAKIGEKLELRRATYFDGTTETYLHKRAADLPPAVGVLVEYTGGDTSAAHAVALQIAALKAKYLTREDVPADIVANERRIAEETARNEGKPEQALSKIVEGRVTGFYKDVVLLDQPAVSDNKKSVKALLDEAGVTVTRFVRFEVGQA", "text": "FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EF-Ts family."}
{"protein": "MAMTAQVKAELASTQVTKTCCRKAEVASMLRFAGGLHIVSGRIVVEAEFDTGAAARRLRTNIAEVYGHQSDVVMVQGNGIRKGSRYIVRVVKDGEALARQTGLLDQRGRPVRGLPPAVVSGGGCDAVAAWRGAFLAHGSLTEPGRSSALEVTCPGPEAALALVGVARRLGIHAKAREVRGVDRVVIRDGDAIGQLLTRLGAHESLMAWEERRMRREVRATANRLANFDDANLRRSARAAVAAGARVDRAMEILGEEVPDHLRMAGQLRLEHKQASLEELGQLHDPVLTKDAIAGRIRRLLAMADKRAEELGIPDTESSLTPDMLADEG", "text": "FUNCTION: Involved in cell division and chromosome segregation. SIMILARITY: Belongs to the WhiA family."}
{"protein": "MSLWYIIVAFVFFSTIIIVRNTRKTKKNLPPGPPRLPIIGNLHQLGSKPHSSMFKLSEKYGPLMALRFGSVSTVVASTPETVKEVLKTFDAECCSRPYMTYPARLTYNLKDIGFCPYTKYWREVRKMTVVELYTAKRVQSFQHTRKEEVASLVDFITQAASLEKPVNLNTKLMKLSGSVICRVVFGINLKGSKLENLYEEVIQGTMEVVGSFAAADYFPIIGRIIDRITGLHSKCEKIFKAMDAFFDQSIKHHLEDESIKDDIIDLLLKMERGEIELGEFQLTRDNTKGILFNILNAGIDTSAQVMTWVMTYLISNPRVMKKAQAEVREVIKNKDDIIEEDIERLEYLKMVVKETFRVLPLVPLLIPREASKDVKIGGYDIPKKTWIHVNIWAIHRNPNVWKDPEAFIPERFMDNQIDYKGLNFEFLPFGSGRRMCPGIGMGMALVHLTLINLLYRFDWKLPEGMEVEDVDLEESYGLVCPKKVPLQLIPVLTQWS", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MPSSALLYCLILLAGVRPSRGEYPRNESNCTHFPVSQTHMLRELRAAFSQVKTFFQKKDQLDNILLTDSLQQDFKGYLGCQALSEMIQFYLVEVMPQAENHGPEIKENLNSLGEKLKTLRMQLRRCHRFLPCENKSKAVEQVKNDFNKLQEKGVYKAMNEFDIFINCIEAYMTIKMKS", "text": "FUNCTION: Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Interferes also with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation (By similarity). In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-10 family."}
{"protein": "MASAVSERLFSLELLVDWVCLEAGLPQPPVVAEEEQKEEGEGASPPRPSRSLCPAVAFRLLDFPTLLIYPPAGPAAPAQESRPGLVSFRRGKSCLFRLQPATLHRLLLRTPLYTLLLQLPPGHPTPAPQLLGACSISLAAAVHKVLGFAAPGSSQSHRGSFPLCNRDGERIGDIALGYRLSDLGSSLLGHLERPVASPGGGVEGMEVQKSVEVSPQTWQENQQLQQPDSEPSPGDADKPLVDVKISRAGKDLKGRAFHSKADSDYTDSMENGKTNSDMCSKGSSERSVSPPNQEGTEVELETNIICPPPLYYTHLTQEKTPPKQGKITIEPQINASEEWDDGTFLKENVNPPTHTNPPEHTNSATGESCSVLINPASVQDTGASNQTTDHPPTEQNRINTIRQLPLLNALLVELSLLYNQPMANPTHIHPHLAWLYRTEDKKSPESSVKSTCKSESKKDKLSVGENEKSVSLQYKKNQTENLKKGKYFEKKGGAPQKRVSRGKLLYGLTNTLKLRLKQTNPDMLVEYEKKEQYKKMQTQMLGAKLRIPSSKVKILSFAELYQKPHELPKDKCLESDASFAENSNTSKQISVVVDDPSTTTETKLNCATEKTVDCDENRSNNGFLGEILSPANSVVSERFICTNTLEGKVFGRKSIQSPGVFQQVAVVDRTVVDKEIDDKQVKITGDDILTVDINEKNPSTSSCSESISELKYSDDFTSPCSSEDTSRILRACDSSPGTENPKNSQHTSTSSETRLSIRKNSSAKSSILSPPFSAGSPVLSHKRFPVSKTQDKSLEEASSSDFSSSQWTEEKENQRDQNSMHNSKVIKQDHDISAKPKTRTGCKSSEKSQSPRTSQVSSYLPSNLSELELNVLDCSTLDHFEEDCDDLGSLNISKQCKDICELVINKLPGYTV", "text": "FUNCTION: Microtubule-associated protein (MAP) that plays a role in the regulation of cell division; promotes microtubule stability and participates in the organization of the spindle midzone and normal progress of cytokinesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Midbody Note=Localized at stabilized microtubules (MTs) during interphase and to the mitotic apparatus during mitosis. Localized at spindle poles in metaphase and spindle midzone during telophase. Colocalized with Polo-like kinase PLK1 to the center of spindle midzone. Localized at the midbody during cytokinesis. Colocalized with acetylated-tubulin at MTs (By similarity)."}
{"protein": "MYAVFQSGGKQHRVSEGQVVRLEKLEVATGEKVEFDSVLMVVNGEDVKIGTPVVAGGKVVAEVVAHGRGEKVRIVKFRRRKHSRKQQGHRQWFTEVKITGIQA", "text": "FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MERSSTSFNFDKIPKFIMKLYKATNNEKYKGICWTPDGLKIHIYDRDVFVKETLPLISKTREFGTFVRMLNSYGFVKSKDIEEEDIYYNKNFRKGREDLLGFDDSLRMIKRKKSSDIRMRIGDGSLKEIVEYLYVQNQELYTELSVCKERIERQERALNGLIEILSRVFRTNSQDLGARIKPSGHNPHNEMDFFLGELSGPLKEGCEPASPPLQDKGIPELSFKPGGIPHADSDTKDDNYDPFF", "text": "FUNCTION: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HSF family."}
{"protein": "MNPDLDTGHNTSAPAHWGELKDDNFTGPNQTSSNSTLPQLDVTRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAIADLLLSFTVLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRGGRRRRRRRRLGACAYTYRPWTRGGSLERSQSRKDSLDDSGSCMSGTQRTLPSASPSPGYLGRGTQPPVELCAFPEWKPGALLSLPEPPGRRGRLDSGPLFTFKLLGDPESPGTEGDTSNGGCDTTTDLANGQPGFKSNMPLAPGHF", "text": "FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Cytoplasm Membrane, caveola Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1B sub-subfamily."}
{"protein": "MSNGGNAGKKSSSYFHFTAGLGSGILSAVLLQPADLLKTRLQQSNHASLLTTIRELSQSPNTIRSFWRGTVPSALRTGFGSAIYFTSLNALRQNVARSNLLRTIGVVDAKNGPVHSSSLPKLSNLANLTTGAVARAGAGFVLMPMTIIKVRYESNLYAYKSIMGAGRDIFLTEGFRGFFSGFGATAIRDAPYAGLYVLFYEQLKKRLSHIVHSVPQAEELVENLGVRKNMKGSTSASINFGSGVLAAGLATAITNPFDAIKTRIQLQPKKYTNLVMAGRKMVGEEGVKSLFDGLGLRMGRKAVSSALAWTIYEELIRRAELAWKGEEVIV", "text": "FUNCTION: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily."}
{"protein": "MNYFELFKFSPAFDIDTALLAERYRELQRAVHPDKFANDTEQQKLLSVQRTAQVNDGFQTLKDPIRRAEHMLSLRGIELSHETTTVKDTGFLMQQMEWREALEDIRDSADPQASIDALYQSFAEYRAQLTQQLTQLLTSEQAEDALLAADQVRKLKFMAKLHDELTRVEDALLD", "text": "FUNCTION: Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA. SIMILARITY: Belongs to the HscB family."}
{"protein": "MEVQRNFFIFAFLFVSFLLWQAWQSQMFLNKKTNEKIDPIFHFIDVKKNKKKIFIKNDVISLVVNMYGGDVEEASLLAYKDTLYSSRPFKLLETGSDFIYQAQSGLIGKDGPDSSINDSRPLYSANKNFFVLGPNEKELRVPIKWLSKNGVIYKKTFILKPNRYDVQIEYDVYNPSKESLNMNIFGQIKQTINLPKKRNVYSGNFALQTFRGAAYSSDDNKYEKYKFDMIANNKNLHIMTESGWIAMLQQYFAVAWIPDNLGKNTIYTSSLDHDTAVIGYKSPIINIPPNSRSIIKSKLWIGPKIQKEMKLVAPNLDLTVDYGWLWFLSQPLFKLLTILYSIIGNWGFSIILITFIMRGLTYPLTKAQYISMAKMRALQPKIQEIKEKFSKDKQRISQEMILLYKKEKINPLGGFLPIFIQMPIFLSLYYMLIGSVELRHAPFLLWIHDLSSQDPYYVLPVIMGLTMFFIQKISSTNHISDPLQKKIMNFMPVIFTAFFLWFPSGLVLYYIISNLVTIIQQKFILSNLEKNR", "text": "FUNCTION: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily."}
{"protein": "MHHTTKKKYGQNFLTDVNLLNKIVTKASITDKNVLEIGPGKGALTKIIVPQAKHVLAYEIDATLKPFLNFENHNNVNIIYDDFLKRDLLKDFDHYFSPNSQLSLIGNLPYYITSPILFKIIDTPQINDATIMIQKEVGMRLLAQPNNKNYNALSVIIQFLFSIEKIQEVKRHMFFPAPKVDSIVIKLTKNNNICPTFLQQFIKFVKASFKQKRKTLLNNLSCQFLLSKETIIPFFLQHHIPLQIRAEQVTLETFQKLTVKWFIFFNIS", "text": "FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily."}
{"protein": "MNLKILGIDPGSRNCGYAIMEANKGKNILIEAGLIKIKPSTLQYQITELCEGLDLIFKNHSFDEVAIEDIFFAYNPKTVLKLAQFRGALSLKILQIHGDFAEYTPLQVKKAVTGKAKATKEQVAFMVKRLLGLSKDIKPLDITDAIAVALTHAANLRVRV", "text": "FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single- stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuvC family."}
{"protein": "MPKMKTHRASAKRFKRTANGGLKRHHAFTGHRFHGKTKKQRRHLRKPAMVSRSDMKRIKQMVAQMH", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL35 family."}
{"protein": "MNFDYIGQALGYHGQPLQKIWDDERGVDDLRLMGLTQVNYGVYQERQKYFTFQERAKRLKMHQFLARKATDLYDRTLVANVMEDSLLAQGNTYMTQMAPFEFFLNVKDKRKGWAHRLSALKQGDIIYTQVTRLASGNRLIVKPLCTAEPKHAYLADIPIKAVILQDFWGPLPLDKQGNPRSFVQNDILRCEINNISADTERLSLNMIGMFNKVPDLKFGLCDFKELPKYYSKIHNLDHPSASHYEDELNKALEFENPNYDLLFQMNGLQPNENLSLMSYLRAGFPEEENAAELRQKQASQWAFRSVADGIEHFKNGQQVEAFQCLNKALNIDPRNVEALVARGALYANRGSFLKGLQDFEKALHLNKYHVNARKYMGETLVALGRSYEEENRIAEAVKAYSDCLNLLPLHEEARQSLDALHRSGDGKRRISTEPSNMTGGQSSDESSSSSASDSECEDSAGKPKSNISQPFYAQHKLKQSGDEKLAVIDAHKANEFRLDDDETVSSVRKLLREASKHKKAKKKGKKKKDKKERRRSRTKSETEDPIELLKKIDFQEALRQDNKLMNSTRSDEERKAKIKSYLKEGGKESPPPPPPMKKTAVSSRKSSFDNVGPSTSRHAASVVGFGGAQPPPAPKFLGQKKHPEPAPKLSFQIKKRPLQMDKLGMLRLAAPAEPLKGGRSSSSRSRSRSRSRSRSRSRNRRLGRSTRSSLRSRRSGSRSRSISRSRSRRRRTYSRSRSPSPRSYGNRFVIGRYRNRRTRRSRSFHRRRSPSPILKRRSPSPFVPRRTPSPASRYRRSRSRSRSRSRSRSPRRFQSRYMPRDRGSVNRSRYSWHNPHKRSVSRTVEPNGKDERAATPPKKGVADDRSGREERA", "text": "SIMILARITY: Belongs to the TTC14 family."}
{"protein": "MDPVPSTQTQKWPGKHADLDPEPSLLRYCDGRVHVGSGKLAEKKTLLTGGDSGIGKAAAVMFAREGSDLVISCLPEERDDAEVTRDLIEREGRNCWIWEGKLDKSDNCRDLVDFALKKLGWIDVLVNNIAYQQVAQSIEDIDDEQWDLTFKTNIFSFFWVTKAAISHMKSGSSIVNCSSINAYVGRPDLLDYTSTKGAITAFTRGLSNQYAQHGIRVNAVAPGPIYTPLVSSTFPKEKIELSDQVPLGRMGQPVEVASCYLFLACSDGGYMTGQTLHPNGGTVINN", "text": "SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MMKHMHIKIKKLHSHAVIPSYQTPQAAGFDLHAVEDSLIKARDRGLVGTGLAFEIESGFEVQVRPRSGLALHNGVSVLNTPGTIDSDYRGEIKVILINHSNEDFHIHRGDRIAQAVVSEVTQAVFTEVQELGQSVRGERGFGSSGVARKGHYQGKPLA", "text": "FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. SIMILARITY: Belongs to the dUTPase family."}
{"protein": "MDTQSSIGNEEWRIAGTSVVSGMALGKVFFLGTSPLHVRELTLPQEEVEHEIHRYYKALNRSKSDIVALEQEVTGQQGLQEVSSILQAHLEIMKDPLLTEEVVNTIRKDRKNAEYVFSSVMGKIEESLTAVRGMPSVVDRVQDIHDISNRVIGHLCCQHKSSLGESDQNLIIFSEELTPSEVASANSAYIRGFVSLVGAATSHTAIVSRAKSIPYLANISEELWNIAKRYNGKLVLIDGYRGELIFNPKPATLQSCYKKELSVVAHTSQRLVRKSLHPIVSSHAGSDKDVEDLLENFPQTSIGLFRSEFLAVILGRLPTLREQVDLYEKLARFPGDSPSVLRLFDFGEDKPCPGIKNKKERSIRWLLDYSVILEDQLQAIAKASLQGSIKVLIPGVSDVSEIIEVKKKWETIQTRFPKGHKVSWGTMIEFPSAVWMIEEILPECDFLSIGTNDLVQYTLGISRESALPKHLNVTLPPAVIRMIHHVLQAAKQNQVPVSICGEAAGQLSLTPLFIGLGVQELSVAMPVINRLRNHIALLELNSCLEITEALLQAKTCSEVEELLNRNNKITS", "text": "FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PEP-utilizing enzyme family."}
{"protein": "MKRAILLLPLGIFLIVAVFLFRGLWLDPSELPSALIGKPFPAFDLPSVQDPARRLTEADLKGKPALVNVWGTWCPSCRVEHPELTRLAEQGVVIYGINYKDDNAAAIKWLNELHNPYLLSISDADGTLGLDLGVYGAPETYLIDKQGIIRHKIVGVVDQKVWREQLAPLYQQLLDEPEAR", "text": "FUNCTION: Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein; Periplasmic side. SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily."}
{"protein": "SGHRHESXBSTBXASXSSKPCCBHCACTKSIPPQCRCSBLRLNSCHSECKGCICTFSIPAQCICTDTNNFCYEPCKSSHGPBBNN", "text": "SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor family."}
{"protein": "MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPSKYPVPENWLHKEAHQLFLKPEVLDPESVELKWSEPNEEELVKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK", "text": "FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site- terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Mitochondrion Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily."}
{"protein": "MAITAAASRLGTEPFSNAAKIELRSDASREEVEAVINAVYRHVLGNDYIMASERLVSAESLLRDGNLTVREFVRSVAKSELYKKKFFYNSFQTRFIELNYKHLLGRAPYDESEIVFHLDLYQNKGYDAEIDSYIDSVEYQNNFGDNIVPYYRGFETQPGQKTVGFNRMFRLYRGYANSDRAQIEGTKPRLARELATNKASSIVGPSGSNPAWGYRPSVDITPRKTLGNAVGENDRVYRIEVTGVRSPGYPSVRRSSYAIIVPYERLSEKIQQIHKLGGKIVSITSA", "text": "FUNCTION: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=This protein occurs in the rod, it is associated with phycocyanin. SIMILARITY: Belongs to the phycobilisome linker protein family."}
{"protein": "MASSMLSTAAVACINRASPAQASMVAPFTGLKSTSAFPTTRKTTTDITSIASNGGRVQCMQVWPPRGKKFYETLSYLPPLTREQLAKEVEYLLRKGWVPCLEFELEHGTVYREYHRSPGYYDGRYWTMWKLPMFGCTDAVQVLQELDEMIKAYPDCYGRIIGFDNVRQVQCISFLAYKPKGAE", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO small chain family."}
{"protein": "MADYGSDKKSRDNQMRSAINQQLVETGEREKLKELLRVRLAECGWRDQLKQLCKEIVRERGLEHVSVDDLVQDITPKARQLVPDTVKKELLQKIRNFLAQQANV", "text": "FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the ENY2 family."}
{"protein": "MANKKIRIRLKAYEHRTLDTAAGKIVENATRTGATVAGPVPLSTERSLYTIIRATHKYKDSREQFEMRTHKRLIDIINPTQKTVDALMKLDLPSGVNVEIKL", "text": "FUNCTION: Involved in the binding of tRNA to the ribosomes. SIMILARITY: Belongs to the universal ribosomal protein uS10 family."}
{"protein": "MERTFIMVKPDGVQRGLVGEIISRFEKRGFKLVGLKLMQISRELAETHYGEHKGKPFFEGLLNFITSGPVVAMVWEGKEVIATAREMMGATNPLKAQPGTIRGTYGIDVGRNVIHGSDSPESAAREIALFFKEEELLSYEKTLDTWIYE", "text": "FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NDK family."}
{"protein": "MDRALSTFPGDDDETNERNINHREKTSGEHGHYEDKLLDLSEEEPNMIKIKNDIKKIINERYSNYISIDDDEISDILKDSFISNEEMQIKDFVLRLLVLEKLFQTSVKECNSLKNIIKRLENHIETIRKNMIVLTKKVDFQTGRSTTL", "text": "SUBCELLULAR LOCATION: Virion membrane. SIMILARITY: Belongs to the poxviruses fusion protein family."}
{"protein": "MTELVYEQPLNEKIRSYLRLEYLDKQLQSNLNHDHQHRCFYPLFSLCELSERCDYRNEVLKDIERHLLQLSKWQELDHVDHQQIDLYINALTQAREPLQKPERFGSQLKQDRFISALRQRFGMPGACCNFDLPQLHYWLAKPWEEKQQDYRSWIAHFEPLLTPITLLLQLTRSTAHYDNAVAHAGFYQGDSAQALALVRVKVDASHGCYPTISGHKNRFAIHFVQFEQQRHSDRSIDFLLATCA", "text": "FUNCTION: Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to mid-cell in an FtsZ-dependent manner. SIMILARITY: Belongs to the ZapD family."}
{"protein": "MFCSAQKGSCSSRVSSSGAVGSRGCTGGSSFGGGSSCGLGGGSAWGFQGSSNSWSLSGGSKGSMGGGFGSCSVRGGFGAASSYGGGSGFGGSSGFGGGSGFGGGSGFGGGSSGGFSSYGGSMGCGLGGVSGYDGGLLSGSEKQTMQDLNDRLANYLDKVRALEEANTDLECKIKDWYGKHGSVKGGSGRDYSQYYSIIEDLKKQILSATCENARMTLQIDNARLAADDFRMKYEHELCLRECLEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRKNHEEEMKCMQGSSGGDVTVEMNAAPGVDLTKLLNDMRAQYEAMAEQNRQEAERQFNERSASLQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQLALKCSLEGTLADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLLNGDGGGCDYRNLVSKNVVLSDSGSCAGQGKDPSKTRVTKTIIEEVVDGRVVSSQVSNISEVKIK", "text": "SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MDHLLLKTQTQTEQVMNVTNPNSIYIKGRLYFKGYKKIELHCFVDTGASLCIASKFVIPEEHWVNAERPIMVKIADGSSITISKVCKDIDLIIAGEIFRIPTVYQQESGIDFIIGNNFCQLYEPFIQFTDRVIFTKNKSYPVHIAKLTRAVRVGTEGFLESMKKRSKTQQPEPVNISTNKIENPLEEIAILSEGRRLSEEKLFITQQRMQKIEELLEKVCSENPLDPNKTKQWMKASIKLSDPSKAIKVKPMKYSPMDREEFDKQIKELLDLKVIKPSKSPHMAPAFLVNNEAEKRRGKKRMVVNYKAMNKATVGDAYNLPNKDELLTLIRGKKIFSSFDCKSGFWQVLLDQESRPLTAFTCPQGHYEWNVVPFGLKQAPSIFQRHMDEAFRVFRKFCCVYVDDILVFSNNEEDHLLHVAMILQKCNQHGIILSKKKAQLFKKKINFLGLEIDEGTHKPQGHILEHINKFPDTLEDKKQLQRFLGILTYASDYIPKLAQIRKPLQAKLKENVPWRWTKEDTLYMQKVKKNLQGFPPLHHPLPEEKLIIETDASDDYWGGMLKAIKINEGTNTELICRYASGSFKAAEKNYHSNDKETLAVINTIKKFSIYLTPVHFLIRTDNTHFKSFVNLNYKGDSKLGRNIRWQAWLSHYSFDVEHIKGTDNHFADFLSREFNKVNS", "text": "FUNCTION: Encodes for at least two polypeptides: protease (PR) and reverse transcriptase (RT). The protease processes the polyprotein in cis. Reverse transcriptase is multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'- endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated, and reverse-transcribed inside the nucleocapsid. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA) (By similarity). SIMILARITY: Belongs to the caulimoviridae enzymatic polyprotein family."}
{"protein": "MPDLSLERACGGRVAGVDEVGRGPLAGPVVAAAVVIDAGRADPALLARLDDSKKLSAALRQRLATALLADPGVEVGLGEASVAEIDRINILQATFLAMGRALAKLAPPVDLALVDGNRLPPLPCPGQAVVRGDGLSLSIAAASIVAKVHRDAAMATLAQALPGYGWERNAGYGTAEHLAALDRLGATPHHRASFAPVREALARSALPGHKCVTALTFS", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family."}
{"protein": "MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFHCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEVNFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPRDQIGYWAVKIVTGVPEAIPIIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family. PetB subfamily."}
{"protein": "MNTKEISKVVDLVRESNPLVHNITNVVVTNFTANGLLALGASPVMAYAKEEVAEMTSIAGALVLNMGTLRPDEVEAMLLAGKSANMNDVPVLFDPVGAGATSYRTEVARHIPAEIELAIIRGNAAEIANVINEKWEIKGVDAGAGNGNVVSIAKQAADELNTVAVITGKEDVVTDGERTIVIRNGHSILTKVTGTGCLLTSVIGAFVAVEKDYAKAAVAALTFYGVAAELAAAKTVEKGPGSFQIEFLNQLANTTSSDIEKYGKIEVI", "text": "FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ). SIMILARITY: Belongs to the Thz kinase family."}
{"protein": "MAEFDARDLLDCYARGVFPMADAREDARVFLIDPERRGVIPLEAFHVPRRLARTVRGDPFEIRIDAAFHDVVLACAASGPGRTETWINRPIEQLYLELHELGFAHSVECWQGERLVGGLYGVSLQGAFFGESMFSRVRDASKVALVHLVARLIAGGFTLLDAQFMTEHLAQFGAREIPRREYHRRLDRALAAPADFYALGAAAPSADGAGRLALQLITQAS", "text": "FUNCTION: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the L/F-transferase family."}
{"protein": "MAHKKGQGSTQNNRDSIGRRLGVKKFGGEFVRAGNIIIRQRGTATHAGNNVGLGKDHTIFALVDGFVKFERLDKNRKKVSVYPAA", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
{"protein": "MPKPQSKRSSLPNYIKSRGELIASLQALLANDHVDLEILRSGVPWPSATEIVQLSQVSESNEDAPVAACHSSNEPVVVDPALGDDSHQAHIDLDVNWLSNLIPYNGDELSEQPDSSLFCSPPERMSVSDSSNNTDYLSHFSSSSICQWDNLLDSIGSQTFQDTINVLSPHCQDSGVSQPSNLADDTLGQGQPVSTVVQPQHPGSTERDESVSSIASSQESPRKRQRPHYAIEKRYRAGLQERFEALRDCVASLKKTQHEQRLPGTNEDLAEGDDGGSVSDRATVGRMNKAEVLNQATLCIRQLQEENEVVMEYIKLLIKQFRVMKQAMQQALKVDINS", "text": "FUNCTION: Transcription factor that specifically regulates the expression of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat leaves. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MYLSRPTGVARFAASSSSSSSASLFPGVDVDTTTKTGALHFEETKERIKKLFDKVELSVSAYDTAWVAMVPSPNSLNQPLFPECINWVLDSQHADGSWGLLHNDQLLMKANLLSTLACVLTLKRWNIGHDHMSKALDFIKSNIASATDENQRSPVGFDIIFPGMIEYAKDLNLNLPLAPTNVDALVRKKELELRSCRSNSEGGKAYLAYVSEGIGKLQDWDMVMQYQRKNGSLFNSPSTTAAAFMHRNDDGCFDYLRSLLQKFDGSVPTIYPLDIYARLHMVDSLQKFGIARHFKEEIRSVLDETYRCWMQGEENIFLDASTCAMAFRMLRVEGYDVSSDQLTQFSEDIFPNCLGGYLKDFGASLELYKASQIITHPDESVLENINSWTSRFLKHGLSSDSVWSDRTDSVVKQEAVNALEFPYNATLERLISKRAMESYSGDIVRISKSPYACLNFGHQDFLELAVEDFNTLQRIHLKELEELQRWVVENKLDELKFFRLHLGYCYFAAAATLTDPELHDARIAWAQNGVLTTVVDDFYDGGGSEEELDNLIELVEKWDPDGEVGYCSKDVEIVFLALHSTVCEIGRRALVWQGRSVMRNVIDGWLALLKVMRKEAEWSTNKVVPSMGEYMEQAHVSFALGPIILPMLFFVGPKLSEEMIGSCEYQKLYKLMSTAGRLKNDIRSYDRECKEGKLNILSLWMIDGGGNVTKEEAIEAIKGDFERAIRELLGLVLQENTTIPRACKDLFWKLMSIVNLFYMEDDGYTSNRLMNTVKAMFEQPMDLDALLNK", "text": "FUNCTION: Catalyzes the conversion of ent-copalyl diphosphate to the gibberellin precursor ent-kaur-16-ene. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MRADPASAAADIFEANRARGAVRFDVRLQDGMTRRHHLHESGSLRVRFPSPEDDGLSAMFVNTAGGIAGGDRFAVEVAAGEGSRVTLSSAAAEKVYRAPGKPAELDIALTAAAGAHIAWLPQETILFDRARIHRRIDIDLAATASLLLCEIVVFGRTAMGERMREGEFVDRWRLRRGGRLVFAETVRLDGDIGGKLAHPAIANGAAAIGTALIVPGDAALVERIRESLPAFRGEAGLSAWNGFAMARFCAQDAASLRADMMAVLGCASAVPLPRLWLN", "text": "FUNCTION: Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UreD family."}
{"protein": "MKLDTSGLETTMPVIGFGSNSEMLDGFSSAPSFDLPRTTDFDGFQKKAVEMVKPAKGTTTLAFIFKEGVMVAADSRASMGGYISSQSVKKIIEINPYMLGTMAGGAADCQFWHRNLGIKCRLHELANKRRISVSGASKLLANMLYSYRGMGLSVGTMIAGWDETGPGLYYVDNEGGRLKGDRFSVGSGSPYAYGVLDSGYKFDMSVEEASELARRSIYHATFRDGASGGVASVYHVGPQGWTKLSGDDVGELHYHYYPVAPITAEHVMEEAAE", "text": "FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MKSVYFVAGLFIMLAQGSWQRSLQDTEEKPRSVSASQTDMLDDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQQFLKWLLNVKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLATRDFINWLIQTKITDRK", "text": "FUNCTION: [Glucagon-like peptide 1]: Potent stimulator of glucose- dependent insulin release. Also stimulates insulin release in response to IL6. Plays important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Has growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis. FUNCTION: [Glicentin]: May modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life. FUNCTION: [Oxyntomodulin]: Significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness. FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. FUNCTION: [Glucagon-like peptide 2]: Stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted. SIMILARITY: Belongs to the glucagon family."}
{"protein": "MDRHHHHHHHHHHHMMSGGGQDPAAGDGGAGGATQDSFFLGPAAAAMFSGAGSSSSGAGTSAGGGGGGPSPSSSSPSLSRYESQKRRDWNTFGQYLRNHRPPLSLSRCSGAHVLEFLKYMDQFGKTKVHTPVCPFYGHPNPPAPCPCPLRQAWGSLDALIGRLRAAYEENGGTPEMNPFGARAVRLYLREVRETQARARGISYEKKKRKKPSSAGAGAGPSSEGSPPPPGGSASGGGDTSASPQFIIP", "text": "FUNCTION: Transcription factor required for lateral development of the lemma and palea (PubMed:22203474, Ref.9, PubMed:23526395, PubMed:25224972, PubMed:26486996, PubMed:29057928, PubMed:30725309). Involved in the regulation of grain hull development (PubMed:23526395). Possesses transactivation activity in yeast, and may determine grain shape and size by modifying gene expression in the grain hull (PubMed:23526395). Regulates the expression of cell proliferation and expansion related genes (PubMed:26486996). Acts as transcriptional repressor and regulates cell expansion during the lateral development of spikelet (PubMed:29057928). May act upstream of hormone-related genes and starch and sucrose metabolism-related genes, which may be responsible for lemma and palea development, and grain filling, respectively (PubMed:30725309). Does not seem to function at stages of floral-organ initiation and patterning (Ref.9). FUNCTION: Probable transcription regulator that acts as a developmental regulator by promoting cell growth in response to light. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the plant homeotic and developmental regulators ALOG protein family."}
{"protein": "MAFNTITFLQWAVFVAILFNMNLHSASAGSKGSSAQQSSHDSIKAEFCETNCTMKTGGKWTQCHGGCFCVHVGNETVGRCIKLDGDYDYPSSKHEE", "text": "FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL11 and CXCL13. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MALKKFNPVTPSTRQLVIVDRSGLYKGKPVKGLTEGLTKSGGRNNYGRITARFIGGGHKRSYRIIDFKRRKFDVVGTVERIEYDPNRTAFIALIKYDDGELSYIIAPQRLAAGDKIVAGEAVDVKPGNAMPLASMPVGTIVHNIELKPGKGGQVARSAGGYAQLVGRDQGMAILRLNSGEQRVVHGSCMATVGAVSNPDHGNINDGKAGRTVWRGKRPHNRGVTMNPVDHPHGGGEGRTSGGRHPVSPWGKPTKGKKTRSNKATDKFILRSRHQRKS", "text": "FUNCTION: One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
{"protein": "MPTYSKRKSRGSLEVSEKTNQPKFIKRSQSSETITSGETASELMQDEKEQSNGAVGSIEDEELQRLRENQASVEALSKKPESIDRELGVEALEIDNVVKSDEEKEDPNGASSKTVKARPLPAGSVHRVTTHMAPIPARSIGSHDTTTQRLIVVLDQACLEIYKVGKAKDAKYQLLNCDDHQGILKKLNRNIAQARPDITHQCLLTLLDSPLNKAGRLQVYIHTAKKVLIEVNPSVRIPRTFKRFSGLMVQLLHKLSIRSVNGNEKLLKVIKNPVTDYLPPNCRKATLSFDAPTVPPRKYLETLQPNQSVCIAIGAMAHGPDDFSDGWVDEKISISDYPLSASIACSKFLHSMEDFLGIV", "text": "FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)- methyltransferase that methylates the pseudouridine corresponding to position 1189 (Psi1189) in S.cerevisiae 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3- carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre- ribosomes (By similarity). Essential for cell growth. It also has a key role in promoting the mating function (PubMed:9133664). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family."}
{"protein": "MSIAAAPLTLALSKGRIFEETLPLLAEAGIGVVESPESSRKLILPTSDPGLRLIIVRASDVPTYVQYGAADFGIAGKDVLIEHAAGQAGRLYQPIDLNIAKCRLSVAVREDFDYAAAVHQGARLRVATKYVQSAREHFASKGVYVDLIKLYGSMELAPLVGLADAIVDLVSTGGTLRANGLREVETIMPISSRLIVNQASLKTRGASLQPLLDAFQRASQGQADSNS", "text": "FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short subfamily."}
{"protein": "MGRLRPEEISSILKGAITDYESRVRTEEVGQVLEVGDGIARVHGLSNVMYQEMVEFEDARGEKVIGLALNLEEDNVGVIIAGDDRYILEGSTVRRTGRLASVPVGQGVLGRVINALGQPIDGRGEIQAEETRPVEIIAPGIIRRKDVDTPLQTGIKAIDSMIPIGRGQRELIIGDRKTGKTALAVDTIINQHDQNVKCIYVAVGQKDSAVAGVVAQLEEYGAMEYTTVINASASQPAPLQYLAPYAGCAIGEYFMHRGEDALVIYDDLSKHAVAYRQMMLLLRRPPGREAYPGDIFYLHSRLLERAARMSEEYGGGSLTALPIIETKAGDISAYIPTNVISITDGQIFLDLDLFNANQRPAIDVGLSVSRVGSSAQIKAMKKVAGTLKLDLSQYRELASFAQFGSDLDKATQETLARGERLTALLKQRERDPMPVEEQVAVIFGGTQGLLREVEPDDVPDWEAQLREYLRSSHEDLLKDIREKKELTDETAERLREAIERFNEGFEPARSEVKVETRPQEEEGEEG", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "EVEEPKTKISASTAEASSSRISSAKMTADGTIKLGDQSPLKQSEKDHPVSWDFKLVQSLRNEYADERYISRSAMLDQEMNVVNLLELIDNLQRLGLSYHFEDKIRSILSGIYNTIKMRNPEGLYATALEFRLRRQHGFYVPQEIFESFKDENGDFNHSLCEDLKGLLYLYEASYLEKENESNLEMAREFTAKHLKKILKEKRIDQELEALVQHALELPLHWRMMRLEARWFIDIYEARSDRNPILLELAKLDFNIVQAIHQNDLECTLRWWSSTGLAEKLSFARDIMVENFFWTVGTISDPQHGNARRLLTKVAALVTAIDDVYDQYGTEDELELFTSVVERWDVNSIDQLPDYMKICFLALFNFVNEMAYDALKEEGVNIIPYLRKAWADLCKAYLQEAKWFFSGHIPTLQQYLNNAWTSISAPLVVVHAYFCVDYPINKDHVEYLEKCHKIIRCSSMIIRLANDLGTSPESEVLKSADVPKSIQCYVKETGACEEKAREYLRFLIIEAWKQMNEAQTVDSPFSSTFKGFAVNVARMGQCMYQHGDGHAHQNSEPRDRILSLLFEPISSFA", "text": "FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products, constituent of coffee beverage aroma (PubMed:23398891). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into linalool and beta-myrcene, and, as minor products, cis- ocimene and trans-ocimene (PubMed:23398891). Not able to use geranylgeranyl pyrophosphate (GGPP) and farnesyl pyrophosphate (FPP) as substrates (PubMed:23398891). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
{"protein": "MSSNNVPAPRRKCVGVKVGSVMIGGGAPIVVQSMTNTDTADELATVQQVEQLARAGSELVRITVNSMEAARTVPAIRARLDDMDCHVPLVGDFHFNGHKLLTAYPECAKALAKYRINPGNVGHGKKRDEQFSILIEMACKYDKPVRIGVNWGSLDPEMLARIMDENARSPDPLGASQVMHKALITSALESAARAEELGLGRDHIVLSCKVSGVQDLIAVYGELAAQCDYALHLGLTEAGMGSKGIVASTAALAVLLFKGIGDTIRISLTPEPGGDRAREVIVAQEILQTMGLRAFVPLVASCPGCGRTTSTYFQELAESIQIYVREQMIIWREQYEGVENMSLAVMGCVVNGPGESKHANIGISLPGSGETPVAPVFVDGQKTVTLKGDNIAGEFRVIVDEYVRTKYRKKVANA", "text": "FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. SIMILARITY: Belongs to the IspG family."}
{"protein": "MNEQHAQSDRPPTVRPMDFLLVTGLSGAGLQTAAKVLEDLGWYVADNLPPELISRMVDLSLESDSRLERLAVVIDVRSRLFTGDLGWVLTELESKPVHTRVLYLDASDEVLVRRFEQVRRSHPLSGGGAEGTLSEGIAAERDQLAKVKAAADLVIDTSSLAAHQLRQKIEDAFGDAENRTMQVTVQSFGFKYGLPMDADLVCDVRFLPNPHWIPELRPHTGQSEDVRDYVLSQDGAEDYLATYHHLLDLTIAGYRREGKRYMTIAVGCTGGKHRSVAMSEALASRLGKDSGLNVRVVHRDLGRE", "text": "FUNCTION: Displays ATPase and GTPase activities. SIMILARITY: Belongs to the RapZ-like family."}
{"protein": "MKPSLIIVTFIVVFMTISCVAADDEQETWIEKRGDCLPHLKRCKENNDCCSKKCKRRGANPEKRCR", "text": "FUNCTION: This toxin stabilizes ryanodine receptor 1 (RyR1) opening in a long-lasting subconductance state (40% of the full conductance state) (PubMed:27114612). Furthermore, it triggers calcium release from sarcoplasmic vesicles (64.2 nM are enough to induce a sharp release, and 50% of the total calcium is released after toxin (100 nM) addition) probably by acting as a cell-penetrating peptide (CPP) (PubMed:27114612). In addition, it has been shown to dose-dependently stimulate ryanodine binding to RyR1 (EC(50)=3.2 nM) (PubMed:27114612). It also augments the bell-shaped calcium-[3H]ryanodine binding curve that is maximal at about 10 uM calcium concentration (PubMed:27114612). It binds a different site as ryanodine (By similarity). It acts synergistically with caffeine (By similarity). In vivo, intracerebroventricular injection into mice induces neurotoxic symptoms, followed by death (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scorpion calcin family."}
{"protein": "MIFENTLAFAQQQDRNDPLAHYSDQFHHPVIDGKEVLYFTGNSLGLQPKTAKEHINQELEDWAKWGVEGHFHAVNPWVSYHEILTPASAELVGANESEVVCMNSLTTNLHLLFVSFYKPTAKRFKIISEAKMFPSDRYLLETQVRHHGLDPDDAIIEISPREGEYLIREEDIIAAVNDNADELALLFFGGVNYFTGQLFDMQRLTKAAHGVGALAGFDLAHAVGNVPMHLHDWDVDFAAWCTYKYLNSSAGNVGGIFVNDRHGNNTKINRFGGWWGHNKERRFLMENSFEPMTGAEGWQISNAPVMGMAILKSSLDIFHEAGIENLRAKSLKLTAYLEFVFNDIVNQFTDIKLEIITPTDPTQRGCQLSIKLVGTNKEFFEALTKAGVIADFREPDVIRLAPTPLYNSFEDVYLLGQTLKVLAQNWRQHG", "text": "FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. SIMILARITY: Belongs to the kynureninase family."}
{"protein": "MRKMIAVLRLGHRPERDKRITTHVALTARAFGADKIIIAAEEDEHVKESVEDVVNRWGGPFEIEFNPSWKKILREWKDRGIIVHLTMYGIHIDDAIPRIKDELKSGKDLLIVVGAEKVPREVYEMADYNVAVGNQPHSEVAALAVFLDRLLDGAGLRKEFHNAKLKIVPQERGKKVLQLE", "text": "FUNCTION: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aTrm56 family."}
{"protein": "MIKQRTLKNVVRATGVGVHTGEKVYLTLRPAPPNTGIIFCRTDLDPVVQIPARVNYIGDTSLSTCLTKGDVRIATVEHLLSALAGVGVDNLYIDLTSPELPIMDGSAGPFVFLIQSAGIEEQNAPKEFIRIKQRVKIEEADKSVMVEPYNGFKISFGIDFDHPLFNEHNQNATLDFSSTSYVKEVSRARTFGFLSDYEFIRKNNLALGASLDNALVLDEYKILNQDGLRYPDEFVKHKILDVIGDLYLLGRSLIGSFSGVKSGHTLNSQLLKQLLATKSAWEIVTFKDPSELPFAYTPVAMTA", "text": "FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. SIMILARITY: Belongs to the LpxC family."}
{"protein": "MASSTDVRPKITLACETCKHRNYITKKNRRNDPDRLEIKKFCPNCGSHQPHKESR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MSDRQQVTNAKGERIAIVAGLRTPFAKQATAFHGVSALDMGKMVVNELLARSELDPKLIEQLVYGQVVQMPAAPNIAREIVLGTGMDVSTDAYSVTRACATSFQSAVNVAESIMTGNIEIGIAGGADSSSVLPIGVSKKLAHALVDLNKARSFGQKLQIFRRLGIKDLLPVPPAVAEYSTGLSMGQTAEQMAKTYNISRADQDALAHRSHTLASETWASGHLRDEVMVAHVPPYKQFIERDNNIRENSDLSSYAKLRPAFDKKHGSVTAANSTPLTDGASAIILMSEGRAKALGYQPIGYIKSYAFTAIDVWQDMLMGPSYATPLALKRAGMELEDLTLIEMHEAFAAQTLANMQMFASKKFAEEKLGRNRAIGEIDMSKFNVLGGSLAYGHPFAATGTRLITQVCRELKRRGGGTGLATACAAGGLGAAMIVEVE", "text": "FUNCTION: Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MASLDVSDIAAQSAQLRAELKEWERAFAAANEGRKAERSDIKQAPEIAAKYKEYSRLKSLEKSVRYEKKHNPNSVNLEERPKKRKHASPPGSHEARLESTPRKAAKGPFTTPSKPRGHPSEFDPYDSPSALRRLFSPSTHQQSSSPLKTAIGPTPQRDGKALGLFDLLSESGGSTATPTAARLASVRGAAAQTPSKRKTLDTIAEEEEEEDGPRGDRTPASASKSYMLSALFATPTTWRYATMMDNRNDAIRREPSPQPSANDAGQGAPESETPAFLRRSNSARYAASNPNGEGLSPINVRKRPRFVGKGLSALVQGLRDMEEEHLDNELDVLREIEAEQAGMNTEATDSQAVEQDTVPTFKKKGQKRTTRRVRMKPVISKPKCESQLPASEDEDNTDNVDQSDDELAAVPETQQPGASGDETNGVPDAASLHSISEPELDSDSDYEEQSKPPARSKSFSERIRDAIGVVEPPPAEKQEKPQPKVKEKQTKPRERKVNPEAHANYRSLKLRNKNSKGRGAGRFGRRR", "text": "FUNCTION: Has a role in the initiation of DNA replication. Required at S-phase checkpoint (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the SLD2 family."}
{"protein": "MMIKLIVNADDFGLTEGTNYGIIDGHINGLVNSTTMMMNMPGTEHAVRLAKEYNLLGVGVHLVLTAGEPLLKDVPSLVGENGSFHKQSVVREGNINPEEVEREWTAQIEKFLSYGLTPTHLDSHHHVHGLPILHDVLERLAAKYNVPIRRCEEDRAVHPFSDVFYSDFYADGVTEDYFVKLKERVQGEQTVEIMVHPAYIDPELVKRSSYVMDRVKELRILTESELPEGIELVKF", "text": "FUNCTION: Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides. SIMILARITY: Belongs to the YdjC deacetylase family."}
{"protein": "MELSGEYVGCDGEPQRLRVSCEASGDADPLQSLSAGVVRMKELVAEFFGTLVEQDAQGLAEDPDDALDGDDEDDAEDENNSGRTNSDGPSAKRPKPAS", "text": "FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. GON7 plays a supporting role to the catalytic subunit OSGEP in the complex. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPLLDSFTVDHTRMQAPAVRVAKQMRTPHGDPITVFDLRFCVPNQEILPERGIHTLEHLFAGFMRDHLNGSDVEIIDISPMGCRTGFYMCLIGTPDEARVAAAWSAAMEDVLKVVDQAKIPELNEYQCGTYQMHSLEEAHEIARAILAHGVGVNKNAELALPSDKLASL", "text": "FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). SIMILARITY: Belongs to the LuxS family."}
{"protein": "MADQLTDDQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKVMMANRRRRRIEESKRSVNSNISRSNNGRKVRKRDRCTIL", "text": "FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. SIMILARITY: Belongs to the calmodulin family."}
{"protein": "MRKYNPRKIKNKVNIPIVLHKANSTIPFVQGTVDYKNVALLRKYISAEGKILSRRLTRLTSKQQRHISTAIKTARIAGLLPFINQ", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
{"protein": "MPSFDVVSELDKHELTNAVDNAIKELDRRFDLKGKCSFEAKDKSVTLTAEADFMLEQMLDILRSNLVKRKVDSQCMEVKDAYPSGKVVKQEVNFREGIDKDLAKKIVGLIKERKLKVQAAIQGEQVRVTGKKRDDLQEAIALLRGESLGMPLQFTNFRD", "text": "SIMILARITY: Belongs to the UPF0234 family."}
{"protein": "MKIGVFDSGVGGFSVLKSLLKAQLFDEIIYYGDSARVPYGTKDPTTIKQFGLEALDFFKPHQIKLLIVACNTASALALEEMQKHSKIPVVGVIEPSILAIKRQVKDKNAPILVLGTKATIQSNAYDNALKQQGYLNVSHLATSLFVPLIEESILEGELLETCMRYYFTPLEILPEVVILGCTHFPLIAQKIEGYFMEHFALSTPPLLIHSGDAIVEYLQQNYALKKNACAFPKVEFHASGDVVWLEKQAKEWLKL", "text": "FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. SIMILARITY: Belongs to the aspartate/glutamate racemases family."}
{"protein": "AVYVASPYAAGYGYAYPYAAAAYRAAPVVGAYAAYPYGVATYPYYY", "text": "FUNCTION: Component of the cuticle of migratory locust which contains more than 100 different structural proteins."}
{"protein": "MSERKAFVSRITNETKIQIAISLNGGHIEIKDSILCKKQQENGSDVAAQTTKSQVIDIQTGVGFLDHMIHALAKHSGWSLIVECIGDLHIDDHHTTEDCGIALGQAFKEALGQVRGVKRFGTGFAPLDEALSRAVVDLSNRPYAVIDLGLKREKIGDLSTEMIPHFLESFAEAARLTIHVDCLRGFNDHHRSESAFKALAVAIRESLAPNGTNDVPSTKGVLM", "text": "SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MEATTKKMAMIEIGKGWAASCLEARTCVISNEEDIYAEPRADTPVLKLDSTVRTALPPGYGIVISGTARNHKTAWEIVPGLVDSGYTGLLGLLLVPTDETPATGSAGGGIVSFSRGGVHARLTVIKLVPDDIMGACGAGAQRLPLKTAITSFKGDEDLLGNGFDHCMESLASIYPDILHVQLDCPVYFGCTGCKAFYRRLGSCLETRPLNELGSDHIYLRRGSAYESVNRFAAPDDVMFVAMYGKWLLIGMAETPNEKLTVELRDDDSSPAALIPFHDTFGQKEAEDAGYDIRAPENCTLPPGGSVRVILRQKLHMGKGRAAFVMGRSSMNLKGVLVEPERVVDDEWVSFNITNIRDAAAFFRKNDRIAQLVALEDKLELMGGVDALPWRVVQSVQEEKKNSSRGDKGFGSSGV", "text": "FUNCTION: Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP to avoid uracil incorporation into viral DNA. SIMILARITY: Belongs to the dUTPase family."}
{"protein": "MRTLVVDHPLVAHKLTVLRDKNTPSPVFRQLTEELVTLLAYEATREVKTQPVEIETPVTKTVGTAFTKPTPLVVPILRAGLGMLEGMTKLVPTAEVGFLGMARDEETLDIITYAERLPEDLTGRQIFVLDPMLATGGTLREAIKFLFKRGASDVTCICLLAAPEGLSKLEEELSDANVKIVLASIDEKLNEKSYIVPGLGDAGDRLYGVAG", "text": "FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. SIMILARITY: Belongs to the UPRTase family."}
{"protein": "MQAAHPIERAVGMEYYVSDADGVGGRLRSSPADFRVRELEAFDTEPVDADTGAYPHLVFRAELRNWETNDFASKLSDRLGISRERVSWAGTKDKRAVTTQLFSVKGVAAGDLPEIGGTDIEVIGRAGRPILFGDLAGNAFEIVVRDTENTDNAASVVADLRAFANGDDSVTSEGWSSDATLPDGDTTVGVPNYFGQQRFGSRRPVTHEVGLAIARGEWKDAVLAYVGNPNEREPESTQEARGYVDETHDWAGALDRLPGALGYERSICHRLVENGASEPADFREALEALPSNLQSLFVNAAQSYVFNRILSERLERGLPFDRPVEGDVVCFRDSDAPEDFPIPDADRTQEVTAKRLSTVERHCERGRAFVTAPLVGTDTELGSGEPGDIAREVLDDVGLEQGDFDLPGAFDSDGTRRAILLRTDLGVERDSADLTFSFSLPKGSYATVLLREFRKGDPDA", "text": "FUNCTION: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
{"protein": "MNQGKIWTVVNPSVGLPLLLGSVTVIAILVHAAVLSHTTWFPAYWQGGLKKAA", "text": "FUNCTION: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the antenna complex alpha subunit family."}
{"protein": "MQTLMSHSRITPLPGAITKEEIKNQLLVHERRFLSKPNRKDQWNVLPQSAHSKNTVNPVRKIADACAVPPHPEKKVIKLHLGDPSVGGKLPPSEIAVQAMHESVSSHMFDGYGPAVGALAAREAIVERYSSADNVFTADDVVLASGCSHALQMAIEAVANAGENILVPHPGFPLYSTLCRPHNIVDKPYKIDMTGEDVRIDLSYMATIIDDNTKAIIVNNPGNPTGGVFTKEHLEEILAFAHQYKLIIIADEIYGDLVYNGATFYPLASLSPKVPIITCDGIAKRWMVPGWRLGWLIIHNHFGVLTDVKNGIVALSQKIVGPCSLVQGALPKILRETPEDYFVYTRNVIETNANIVDSILADVPGMRVVKPKGAMYMMVNISRTAYGSDVSFCQNLIREESVFCLPGQAFSAPGYFRVVLTCGSEDMEEAALRIREFCYRNFNQHSDSEDSSDEGLDLSAMESD", "text": "FUNCTION: Transaminase involved in tyrosine breakdown (PubMed:24385923, PubMed:31043480). Converts tyrosine to p-hydroxyphenylpyruvate (PubMed:31043480). Has no transaminase activity towards phenylalanine (PubMed:31043480). Plays protective role against oxidative stress, metabolizing meta-tyrosine and negatively regulating its accumulation (PubMed:31043480). Plays a role in modulating the daf-2/insulin receptor-like transduction pathway through regulating tyrosine levels (PubMed:24385923). Negatively regulates dauer formation (PubMed:24385923). Plays a role in longevity (PubMed:24385923, PubMed:31043480). SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MNIAVVGLSHKTAPVEVREKLSIPEAKLEEVLAHLKSYPHIQEVAILSTCNRLEIYAVVTETEQGIIEISQFLSEKGHIPLHHLRRHLFILLHQDAVRHLMRVAAGLESLVLGEGQILAQVKNTHKLAQKYGGIGRLLDRLFKQAMTAGKRVRSETSIGTGAVSISSAAVELAQMKVIDICVCRVTIIGAGKMSRLLVQHLLSKGVSKIAIVNRSLRRAQELAGLFPEAQLQLHPLEEMINAVSVSDIVFTSTGATEPILNRSNLESIIAVNQSLMLVDISVPRNVDADVQQLEQIQSYNVDDLKAVVAANQESRRRLAQEAEGLLEEEVESFELWWRSLDTVPTISCLRDKVETIREQELEKALSRLGTEFAEKHQEVIEALTRGIVNKILHEPMVQLRAQQDIEARKRCLQSLQMLFDLDIEEQYT", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). SIMILARITY: Belongs to the glutamyl-tRNA reductase family."}
{"protein": "MELLSGPHAFLLLLLQVCWLRSVVSEPYRAGFIGEAGVTLEVEGTDLEPSQVLGKVALAGQGMHHADNGDIIMLTRGTVQGGKDAMHSPPTRILRRRKREWVMPPIFVPENGKGPFPQRLNQLKSNKDRGTKIFYSITGPGADSPPEGVFTIEKESGWLLLHMPLDREKIVKYELYGHAVSENGASVEEPMNISIIVTDQNDNKPKFTQDTFRGSVLEGVMPGTSVMQVTATDEDDAVNTYNGVVAYSIHSQEPKEPHDLMFTIHKSTGTISVISSGLDREKVPEYRLTVQATDMDGEGSTTTAEAVVQILDANDNAPEFEPQKYEAWVPENEVGHEVQRLTVTDLDVPNSPAWRATYHIVGGDDGDHFTITTHPETNQGVLTTKKGLDFEAQDQHTLYVEVTNEAPFAVKLPTATATVVVHVKDVNEAPVFVPPSKVIEAQEGISIGELVCIYTAQDPDKEDQKISYTISRDPANWLAVDPDSGQITAAGILDREDEQFVKNNVYEVMVLATDSGNPPTTGTGTLLLTLTDINDHGPIPEPRQIIICNQSPVPQVLNITDKDLSPNSSPFQAQLTHDSDIYWMAEVSEKGDTVALSLKKFLKQDTYDLHLSLSDHGNREQLTMIRATVCDCHGQVFNDCPRPWKGGFILPILGAVLALLTLLLALLLLVRKKRKVKEPLLLPEDDTRDNVFYYGEEGGGEEDQDYDITQLHRGLEARPEVVLRNDVVPTFIPTPMYRPRPANPDEIGNFIIENLKAANTDPTAPPYDSLLVFDYEGSGSDAASLSSLTTSASDQDQDYNYLNEWGSRFKKLADMYGGGEDD", "text": "FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MVVSKMNKDAQMRAAINQKLIETGERERLKELLRAKLIECGWKDQLKAHCKEVIKEKGLEHVTVDDLVAEITPKGRALVPDSVKKELLQRIRTFLAQHASL", "text": "FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor- mediated transactivation (PubMed:18206972, PubMed:21746879). As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:23591820). FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor- mediated transactivation. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Note=Localization at the nuclear pore complex requires NUP153 and TPR. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the ENY2 family."}
{"protein": "MAGNTIGQLFRVTTFGESHGIALGCIVDGVPPGIPLTEEDLQHDLDRRRPGTSRYTTPRREPDRVKILSGVFEGRTTGTSIGLLIENTDQRSQDYGAIKELYRPGHADFTYDGKYGFRDYRGGGRSSARETAMRVAAGAIAKKYLDMKHGIKVRGYLAQMGDVVCELKDWQQVEQNPFFSPDVDKLDALDELMRALKKEGDSIGAKVAVMAENVPVGLGEPVFDRLDADLAHALMSINAVKGVEIGDGFAVVNQRGSEHRDEIRANGFQSNHAGGILGGISSGQTITANLAMKPTSSITVPGKTITRSGEEVEMITKGRHDPCVGIRAVPIAEAMMAIVLMDHLLRHRAQNADVHVDMPHG", "text": "FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. SIMILARITY: Belongs to the chorismate synthase family."}
{"protein": "MTRHAEKRVVITGIGVRAPGGAGTAAFWDLLTAGRTATRTISLFDAAPYRSRIAGEIDFDPIGEGLSPRQASTYDRATQLAVVCAREALKDSGLDPAAVNPERIGVSIGTAVGCTTGLDREYARVSEGGSRWLVDHTLAVEQLFDYFVPTSICREVAWEAGAEGPVTVVSTGCTSGLDAVGYGTELIRDGRADVVVCGATDAPISPITVACFDAIKATSANNDDPAHASRPFDRNRDGFVLGEGSAVFVLEELSAARRRGAHAYAEVRGFATRSNAFHMTGLKPDGREMAEAITAALDQARRTGDDLHYINAHGSGTRQNDRHETAAFKRSLGQRAYDVPVSSIKSMIGHSLGAIGSLELAACALAIEHGVIPPTANYEEPDPECDLDYVPNVAREQRVDTVLSVGSGFGGFQSAAVLARPKETRS", "text": "FUNCTION: Involved in the biosynthesis of tetracenomycin C (TCM C) (PubMed:7814341, PubMed:9609708). Part of a type II polyketide synthase (PKS) that catalyzes the synthesis of tetracenomycin F2 (TCM F2), a precursor of TCM C, from malonyl-CoA (PubMed:8248801, PubMed:9609708). TcmK and TcmL form a heterodimeric alpha-beta complex that catalyzes the condensation reactions between the growing acyl-enzyme chain and the malonyl-CoA extender units (PubMed:9609708). SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family."}
{"protein": "MTAPLVGLIMGSDSDWPTVEPAAEVLDEFGVPFEVGVVSAHRTPEKMLDYAKQAHTRGIKVIVACAGGAAHLPGMVAAATPLPVIGIPRALKDLEGLDSLLSIVQMPAGVPVATVSIGGAKNAGLLAIRTLGVQYSELVERMADYQENMADYQPKIWPRKLSKKTPIFAPSSWGTRP", "text": "FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily."}
{"protein": "MPEVLLVATPGTRIYVRRGVVYAEAPSGEKAVVTADTELVVLATGSVSVSGRALRRLAELGVRLVVLGQRGQVVAEHRPVDRVNRTIEARMEQYRVKATGEALYYAAEMVYAKIVNQAKLLRYLAKSRREPWLRDAGYRVEGHADRLRQIIENEEPTTPEVIRSIEAQAARDYWDAIAQIAPTPFPGRQPRGEDHLNMALSYGYAILYSIAHDALTVAGLDPYAGFLHADRSGRPSLTYDYADTYKPIAVDKPLLTAPRKTDCLDTYMGALTYNARRCIATLVLENIYKTPYPDSRGRKKTLRDHIYTYAWNLAAAIRQHKPYKPFIVGRL", "text": "FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family."}
{"protein": "MAGHDDEEARIETVKDAVTDMKLERQSSTESVAPNGILDTITPKDEPNGHLSSKPSTPSLKPPKSRSRSSNSLAKDEVPEEKVGGDITIKQEPGQPPKLARSASQKLPPRAAPLFTDLPDKTTEATSTFQLMEVCTYANKYLGYTEHAMDCDCAEEWDAATCRNTACGEDSDCINRATKMECFGDCGCGDSCQNQRFQRREYAKVSVIKTEKKGYGLRADCDLRPNEFIFEYIGEVINEPQFRRRMIQYDEEGIKHFYFMSLNKGEFVDATKKGNLGRFCNHSCNPNCYVDKWVVGEKLRMGIFAERYIKAGEELVFNYNVDRYGADPQPCYCGEPNCTGFIGGKTQTERATKLSHATIEALGIDDPDGWDTAVARRPRKKKAGEDDEEYVDSLQPKSLDENGVTKVMAALMQCKEKWIAVKLLGRIQRCEDERVRHRVVRMHGYQILNSQLNTWKDDFNVVLQILDILDKFPRLTRNKIIDSKIEGTVSPLQECDDERVAEKAKALLEIWSALEVGYRIPRMKRDPAAVNNTPTANHYERRETAKDDRKPNSSKSRSRSRSRSRSVDVTRNAPRGPAALTRGGGKGHMHSYRPGQRPFRRPFNPLPKGWFAAESNGRTYYYSATGETTWSRPTAPAVQPPPPPKRESKEKTLQDIIDGIMNAKENTPKAKDKSATPATPADAKIPEKKEHKEKWRSYSEEKQKKLYENTLFPHVKYIVDKFKHKLPKDDLKRYAKEVAKKLVNSDFKNNRVEDPTKISDKQVKQVKKYCKEYFDKAVAKHRAYEEKKAERKSKGSVKATTSATIDKAETTSTKAPPQFDGAAETGDEDSDVQLSDAEYEDGQEESSHHSGLKRKRTDDEDFENDHENGGVSPTKRQRSASLPIIPPPPPPMSPSNLVLDDGSREALKRQRTEGAEDDEYGDSTISSGKRQRSETPPPPPPPPPPADIPPENIESENENDKDQEELQDYDVQEANWGKEDNIAIQSPSHSPFPAQSISNHSNTARETDSHS", "text": "FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys- 36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily."}
{"protein": "MGSSDQATAHARAQAASARLFDDACAVIPGGVNSPVRAFTAVGGTPPFITAARGCRLTDADGNHYVDLVCSWGPMILGHAHPAVVEAVAKAAASGLSFGAPTPAESELAAEMIARVAPVERIRLVNSGTEATMSAVRLARGFTGRAKIVKFSGCYHGHVDALLADAGSGVATLGLPSSPGVTGATAADTIVLPYNDIDAVRQAFAEFGDQIAAVITEASPGNMGVVPPAPGFNAALRALTAEHGALLIVDEVMTGFRVSRSGWYGIDPVDADLFTFGKVMSGGLPAAAFGGRAEVMERLAPLGPVYQAGTLSGNPVAVAAGLATLRHADAAAYAALDANADRLARLLSDALTNAGVPHQIPRAGNMLSVFFTDTPVTDFASARATQTWRYPPFFHALLDAGVYPPCSAFETWFVSTALDDDAFDRIAAALPAAARAAAGADEGNS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily."}
{"protein": "MNQADKNQEIPSYLSDEPPEGSMKDHPQQQPGMLSRVTGGIFSVTKGAVGATIGGVAWIGGKSLEVTKTAVTTVPSMGIGLVKGGVSAVAGGVTAVGSAVVNKVPLSGKKKDKSD", "text": "FUNCTION: May play a role in bone development. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM263 family."}
{"protein": "KQTAETLLSLSPAETANLKEGINFFRNKTTGKEYILYKEKNHLKACKNLCKHQGGLFIKDIEDLDGRSVKCTKHNWKLDVSTMKYINPPGSFCQDELVVEMDGNDGLFLIELNPPNPWDSDPRTPEELAFGEVQITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWWLLHEPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLSQRRPDIPIYVGDTERPVFWNLDQSGVQLTNINVVPFGVWQQVDKNLRFMILMDGVHPEMDTCIIVEYKGHKILNTVDCTRPNGGRLPEKAALMMSDFAGGASGFPMTFSGGKFTEEWKAQFIKAERRKLLNYKAQLVKDLQPRIYCPFAGYFVESHPSDKYIKETNIKNDPIQLNNLIKKNCDVVTWTPRPGATLDLGRMLKDPTDSQGIIEPPEGTKIYKDSWDFGPYLSTLHSAVGDEIFLHSSWIKEYFTWAGFKSYNLVVRMIETDEDFNPFPGGYDYLVDFLDLSFPKERPSREHPYEEIRSRVDVVRYVVKHGLLWDDLYIGFQTRLQRDPDIYHHLFWNHFQIKLPLTPP", "text": "FUNCTION: Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell- pathogen interactions. Catalyzes the conversion of CMP-N- acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family."}
{"protein": "MNSQGSAQKAGTLLLLLISNLLFCQNVQPLPICSAGDCQTSLRELFDRVVILSHYIHTLYTDMFIEFDKQYVQDREFMVKVINDCPTSSLATPEDKEQALKVPPEVLLNLILSLVQSSSDPLFQLITGVGGIQEAPEYILSRAKEIEEQNKQLLEGVEKIISQAYPEAKGNGIYFVWSQLPSLQGVDEESKILSLRNTIRCLRRDSHKVDNFLKVLRCQIAHQNNC", "text": "FUNCTION: Prolactin acts primarily on the mammary gland by promoting lactation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MRNRRNIFLIGPMGAGKTTVGRLLARALGMEFWDSDKEIERRTGVTVPMIFEYEGEAGFRRRESEVIADLTGKERIVLATGGGSVLAAENREHLAARGLVIYLQCSVQKQLERTHKDMNRPLLQTENPRQRLEELLRVRDPIYRELADYVVDTGQHSSRSAVRRIINAYEKSGTRLRTE", "text": "FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the shikimate kinase family."}
{"protein": "MKVIFTQDVKGKGKKGEVKEVPVGYANNFLLKKNYAVEATPGNLKQLELQKKRAKQERQQEIEDAKALKETLSNIEVEVSAKTGEGGKLFGSVSTKQIAEALKAQHDIKIDKRKMDLPNGIHSLGYTNVPVKLDKEVEGTIRVHTVEQ", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MSQSSVSAIRWANNQLILLDQRKLPLQEAYVNCVTHVEVADAIRQMVVRGAPAIGIAAAYGVALAAAEFGSDRDRLHRALETLADSRPTAVNLFWALRRMRGLIDGASVADLFPLLVEEATRIHEEDLQANLTMGELGADLIAESGRGALLTHCNTGSLATGGYGTALGVIRSAYRRDLVTEVFADETRPWLQGARLTAWELCQDDIPVKLIADSAAAHVMKTCAVKWVIVGADRITAHGDVANKIGTYGLAVLARHHGVKFMVAAPSSTIDFELFSGADIPIEERTSDELKFVQGTPLAPEKADAFNPVFDVTPAELIDAIVTERGVVLRPNAEKMLKLQ", "text": "FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily."}
{"protein": "MANRRGGGQGQPPSVSPSPGSSGNLSDDRTCTHNICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVITVTHAYGNRKGVRYLTNGLKVYYLPLRVMYNQSTATTLFHSLPLLRYIFVRERITIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSVITVVVVSRLVYRKGTDLLSGIIPELCQKYQELHFLIGGEGPKRIILEEVRERYQLHDRVQLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTKVGGIPEVLPESLIILCEPSVKSLCDGLEKAIFQVKSGTLPAPENIHNVVKTFYTWRNVAERTEKVYERVSKETVLPMHKRLDRLISHCGPVTGYMFALLAVLSYLFLIFLQWMTPDSFIDVAIDATGPRRAWTHQWPRDKKRDENDKISQSR", "text": "FUNCTION: Catalytic subunit of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MSSLEINNSCFSLETKLPSSHQSVEDSASEPSGYEAKDPPQDTLKDVDDVLEKPKDIIQFTAKKLSVGEVSQLVVSPLCGAVSLFVGTTRNNFEGKKVISLEYEAYLPMAENEIRKICNDIRQKWPVRHIAVFHRLGLVPVSEASTVIAVSSAHRAASLEAVSYAIDSLKAKVPIWKKEIYEESTSSWKRNKECFWAADD", "text": "FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily."}
{"protein": "MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLGGIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAILVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP", "text": "FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1- phosphate/C1P (PubMed:9305923, PubMed:9705349, PubMed:9607309, PubMed:10962286, PubMed:17379599). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (PubMed:10962286, PubMed:12909631, PubMed:15461590, PubMed:17379599). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (PubMed:17379599). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (PubMed:12909631, PubMed:15461590). May also have an intracellular activity to regulate phospholipid- mediated signaling pathways (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Membrane raft; Multi-pass membrane protein Membrane, caveola; Multi-pass membrane protein. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
{"protein": "MEALVYTFLLVGTLGIIFFAIFFREPPRIIK", "text": "FUNCTION: Seems to play a role in the dimerization of PSII. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbT family."}
{"protein": "MVVCLIGGVAGSLWPRPAGRLRGGCYFAFMGVAWVLLAISAIANAVKGSLWWDIWSLGLLVLIPAVVYGKMRRSRRISSDQDR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MIFLSHFSNLGDPVLLMAFLAFVLILVSLPFSFWSLSSNSNSSLVRLLIGVANLVLAFQLCTRWFLSGHFPVSNLYESLCFLTWTSTLVQLIIERRYLNPIIPAILTPFSLLTISFASFALPGELQIAGPLVPALRSSWLVMHVSVIMCSYSALLLGSLLSLAVLILSNSNELQIRGSSLGIGAYRTSNSTKSGYVNSRSLQQLFSNEENLDNLSYQTITVGFLLLTLGLVSGAVWANEAWGSWWSWDPKETWALISWLVYAAYLHARITRGWQGRKPAMIATFGFLIIVICYIGVNLLGVGLHSYGWFLS", "text": "FUNCTION: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family."}
{"protein": "MLKLFSAFRKDKIWDFDGGIHPPEMKTQSNGTPLRQVPLAPRFVIPLKQHIGAEGELCVSVGDRVLRGQALTRGRGRMLPVHAPTSGTVIAIAPHSTAHPSALAELSVIIDADGEDRWIEREGWSDYRAHSREALIERIHQYGVAGLGGAGFPTGVKLQGGGDKITTLIINAAECEPYITADDRLMQDCAAQIVEGIRILAHILQPREVLIGIEDNKPQAISMLRAVLADAHDISLRVIPTKYPSGGAKQLTQILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVVDGEPITERVVTLTGEAVSRPGNVWARLGTPVRHLLNDAGFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSVAEMGAPQEEKSCIRCSACADACPADLLPQQLYWFSKGQQHDKATAHHIADCIECGACAWVCPSNIPLVQYFRQEKAEINAIRLEEKRAAEAKARFEARQARLEREKAARLARHKSAAVQPAAKDQDAIAAALARVKEKQAQATQPVVIQAGSQPDNSAVIAAREARKAQARAKQAAHPMADSAIPGNDPSKAAVEAAIARAKARKQEQQAGSEPVEAVDPRKAAVEAAIARAKARKQEQQTGSEPAEPIDPRKAAVEAAIVRAKARKQEQQTGSEPAEPIDPRKAAVEAAIARAKARKQEQQTGSEPAEPADPRKAAVAAAIARVQAKKAAQQQVVNED", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily."}
{"protein": "MIAKLKGILDSITDSYLIIDINGVGYQVYSSGKTLMKLIKEEGSIVSLFIETHVREDRIHLFGFLDNTEKVAFNMLQSVSGIGTKMALHILSNLTPHQLQIAISSQNRHQLKAISGVGPKLIDRLMIELRDKVANINTIANNTSLATLSTDSNTHDNILSDAITALIALGISRAEATQILSDIYALSPSISVNELVRTALQRRAK", "text": "FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuvA family."}
{"protein": "MAVGWFYLSVLALCSLGSMCILFTIYWMRYWHGGFAWDGSMLMFNWHPVLMVTGMVVLYSAASLVYRLPQSWVGPRLPWKSGHAAMHLLAFLLTVLGLHAVFEFHNHAKIPHLYSLHSWLGITTVFLFACQWFLGFSVFLLPWASMWLRSLLKPIHVFFGASILSLAIASVVSGINEKLFFSLKNGTKTYSNLPSEAVFANCAGMLVVVFGLLVLYILLASSWKRPEPGMQAEREPTRTRGRAGTPEVMLEGERGLAEPLLQKRS", "text": "FUNCTION: Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce iron cations Fe(3+) into Fe(2+) in the lumen of the late endosome and lysosome. Reduced iron can then be extruded from the late endosome and lysosome to the cytoplasm by divalent metal-specific transporters. It is therefore most probably involved in endosomal and lysosomal cellular iron homeostasis. SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein."}
{"protein": "MDLIHTFLNLIAPPFTFFFLLFFLPPFQIFKFFLSILGTLFSEDVAGKVVVITGASSGIGESLAYEYAKRGACLVLAARRERSLQEVAERARDLGSPDVVVVRADVSKAEDCRKVVDQTMNRFGRLDHLVNNAGIMSVSMLEEVEDITGYRETMDINFWGYVYMTRFAAPYLRNSRGRIVVLSSSSSWMPTPRMSFYNASKAAISQFFETLRVEFGPDIGITLVTPGFIESELTQGKFYNAGERVIDQDMRDVQVSTTPILRVESAARSIVRSAIRGERYVTEPAWFRVTYWWKLFCPEVMEWVFRLMYLASPGEPEKETFGKKVLDYTGVKSLLYPETVQVPEPKND", "text": "FUNCTION: Has dehydrogenase activity against corticosterone (11 beta- hydroxysteroid) and estradiol (17 beta-hydroxysteroid), with higher activity against estradiol. Possesses higher dehydrogenase activity with NADP(+) than NAD(+) regardless of the sterol substrate. May be involved in signal transduction regulated by various sterols. SUBCELLULAR LOCATION: Lipid droplet Membrane; Single-pass type II membrane protein Note=Surface of oil bodies. Exists at a monolayer lipid/water interface. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MRLSIALGAVLTVLIAVQGEETTNSTTKYIDYSSLKKFTLAPTIQQSSTDGSQVQQIQIPISTRPDPRATEAPTPAPTLAPTPAPTPTPTPDPGPWTTITIDHDQVKPFAQPEPVTISEKTAVKFKPQLHITNGCHSYPAVDEAGETGGGLKTKGAPSAGCKGSGWGSQVYGRSGWYQDVWAIMYCWYFPKDEPSSGIGHRHDWEHVIVWIDNPAVENPKILAVTPSAHSGYHKYAPPNADTIDGVTTKVAYDSKWPMDHALDSTSEAGDFQDLIMWDQLSENARRALNSVNFGRPNTPMNDGNFQPKLAKAWPFQ", "text": "FUNCTION: Secreted effector that contributes moderately to virulence during infection by P.capsici. Does not cause visible reaction of C.annuum for several days after inoculation, but by 7 days after inoculation, small necrotic lesions become visible. Leads only to chlorotic areas, without necrosis at 7 days after non-host N.benthamiana leaves infection. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Necrosis inducing protein (NPP1) family."}
{"protein": "MKKSFIDQQKEISFVKNTFTQYLIDKLDVVEVQGPILSKVGDGMQDNLNGIENPVTVNVLQIPDATYEVVHSLAKWKRHTLARFGFNEGEGLVVNMKALRPDEDSLDATHSVYVDQWDWEKVIPDGHRNIAYLKETVETIYKVIRLTELAVEARYDIEAVLPKKITFIHSEELVEKYPDLTPKERENAITKEYGAVFLIGIGGVLPDGKPHDGRAPDYDDWTTESEKGYHGLNGDILVWNEQLGHAFELSSMGIRVDEDALKRQVEITGDQDRLKLDWHQALLQGQFPLTIGGGIGQSRMAMFLLRKKHIGEVQTSVWPDAVRETYENIL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily."}
{"protein": "MKPLLDVLMILDALEKEGSFAAASAKLYKTPSALSYTVHKLESDLNIQLLDRSGHRAKFTRTGKMLLEKGREVLHTVRELEKQAIKLHEGWENELVIGVDDTFPFSLLAPLIEAFYQHHSVTRLKFINGVLGGSWDALTQGRADIIVGAMHEPPSSSEFGFSRLGDLEQVFAVAPHHPLALEEEPLNRRIIKRYRAIVVGDTAQAGASTASQLLDEQEAITVFDFKTKLELQISGLGCGYLPRYLAQRFLDSGALIEKKVVAQTLFEPVWIGWNEQTAGLASGWWRDEILANSAIAGVYAKSDDGKSAI", "text": "SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MTAVTAAQRSVPAPFLSKTYQLVDDHSTDDVVSWNEEGTAFVVWKTAEFAKDLLPQYFKHNNFSSFIRQLNTYGFRKTVPDKWEFANDYFRRGGEDLLTDIRRRKSVIASTAGKCVVVGSPSESNSGGGDDHGSSSTSSPGSSKNPGSVENMVADLSGENEKLKRENNNLSSELAAAKKQRDELVTFLTGHLKVRPEQIDKMIKGGKFKPVESDEESECEGCDGGGGAEEGVGEGLKLFGVWLKGERKKRDRDEKNYVVSGSRMTEIKNVDFHAPLWKSSKVCN", "text": "FUNCTION: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HSF family. Class B subfamily."}
{"protein": "MIEFDNLTYLHGKPQGTGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGKEMPDLSAFQLEGCQVLEYARHKRKLRLGALKGNAFTLVLREVSNRDDVEQRLIDICVKGVPNYFGAQRFGIGGSNLQGALRWAQTNTPVRDRNKRSFWLSAARSALFNQIVAERLKKADVNQVVDGDALQLAGRGSWFVATTEELAELQRRVNDKELMITAALPGSGEWGTQREALAFEQAAVAAETELQALLVREKVEAARRAMLLYPQQLSWNWWDDVTVEIRFWLPAGSFATSVVRELINTTGDYAHIAE", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
{"protein": "MSLRLPSGSRRASPRPTTGSLRLSSGGASFGAGNACSMPGIGSSFSCAFGGSSSGGNALGGNPCAGFTVNEGGLLSGNEKVTMQNLNDRLASYLENVRALEEANADLEQKIKGWYEKFGPGSCRGLDHDYSRYFPIIEDLKNQIIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVESDVNGLRRVLDEITLCRTDLEIQYETLSEELTYLKKNHKEEMQVLQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQITEDVGATTSARNELTEMKRNLQTLEIELQSLLATKHSLECSLTETEGNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIETYCLLIGGDDGACKSGGYKSKDYGAGNVGNQMKDPVKAIVVKKVLEEVDQRSKILTPRLHSLEEKSQSN", "text": "FUNCTION: Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs) (By similarity). Plays a role in the cytoskeleton organization (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MTPSATKPLVSEAPKGIIDPSTGRPILSDDPFYKEINAELADKGFLVTTVDDLITWARTGSLMWMTFGLACCAVEMMQVSMPRYDVERFGFAPRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVISMGSCANGGGYYHYSYAVVRGCDRVVPVDIYVPGCPPTAEALLYGVLLLQRKIRRTGTIER", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MNKRKHMDIRRLIISLPAIMALWGGLASCDKMIYDNYDDCPRGVYVNFYSQTECAENPSYPAEVARLNVYAFDKDGILRSANVFEDVQLSAAKEWLIPLEKDGLYTIFAWGNIDDHYNIGEIKIGETTKQQVLMRLKQDGKWATNIDGTTLWYATSPVVELKNMEDGADQYIHTRANLREYTNRVTVSVDSLPHPENYEIKLASSNGSYRFDGTVAKADSTYYPGETKVVGDSTCRAFFTTLKLESGHENTLSVTHKPTGREIFRTDLVGAILSSQYAQNINLRCINDFDIRLVAHHCNCPDDTYVVVQIWINGWLIHSYEIEL", "text": "FUNCTION: Anchoring subunit of the minor fimbriae. Regulates fimbrial length (PubMed:19589838). These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. Fimbriae of P.gingivalis are major virulence factors (Probable). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily. FimB/Mfa2 family."}
{"protein": "MNYALLSNGITTALEKEGSIEWFPVPKFDSPSVFTKILDEDKGGYFLITPEKFNKVKQQYVEYSLILRTEFDDGNLILIDFLPLSLPAIIRLYEAKVPFNVEVKPLFNYGLVNAGTETRKDGIIYKNPESKEGLELLINGDYKIISPYRITVNSGKGYLYLLYSRDLRYGLFSQKGFVYSEPYEAYSKLLYYSRKELERARKPSIYENAFYRSLSVILGLIYKPSGGIIASPTTSIPEIVGDERNWDYRYVWVRDSSYAIEALVKANLLTHARRALDFLTNLLDPSSKSFDHPFYSVDGTPPPAEENLDWLSGFMNSKPVRIGNAAYLQIQMDIEGAYMNALYEYYKRTLDKDYISSIFWAVEAISDWVSSSWRGESTDIWEERGISRHYTHTKLMSWVALDRASKLAKDLGYNKLFEEWKSRANEIKIDILNNGVKDNHHFVRYYGGDEIDAALLTLPIYDFIPATDTLFMNTLKKIDEELRVADGLYLRYKKDFMGLAKNPFTLVTTWMARVYIRLKEFDRARWLLETLIKCNQDLGLIGEHVDPETCEARGNYPHLFPHSGMVLSILEFDEVR", "text": "FUNCTION: Catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose. SIMILARITY: Belongs to the glycosyl hydrolase 15 family."}
{"protein": "MVKIRPDEISSIIKQQIEQYQQEVKAVNVGTVFQVGDGIARIYGLDKVMAGELVEFEDGTVGIALNLEAKNVGAVLMGEGTRVQEGSSVRATGKIAQIPVGDGYLGRVVNSLARPIDGKGEIATKENRLIESPAPGIISRRSVHEPLQTGIVAIDAMIPIGRGQRELIIGDRQTGKTAIAVDTILNQKGKDVVCVYVAIGQKASSIAQVVNTLQERGAMDYTIIVAATADSPATLQYLSPYTGAALAEYFMYTGRHTLVIYDDLTKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDKLGSGSMTALPVVETQEGDVSAYIPTNVISITDGQIFLSADIFNAGIRPAINVGISVSRVGSAAQPKAMKQVAGKLKLELAQFAELEAFSQFASDLDQATQNQLARGQRLRELLKQSQSSPLSLEDQVASIYAGTNGYLDVLPADRVRAFLVGLRQYLATNKAKYGEILRSTNALTDEAQTLLKEALKEYTEEFLASAK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MRILLSNDDGYFAPGLAALAEALAPLAEVTVVAPERDRSGASNSLTLDRPLMLRQAPSGFYYVNGTPTDCVHLAVTGMLDHLPDMVISGINHGANMGDDTIYSGTVAAATEGYLLGIPSIAVSLANHNALYFDTAARVVSDLVRRLQNNPPTEPTLLNVNVPDRAWDAVRGISVTRLGKRHKAESVVKTSNPRGQTVYWVGAAGAAQDAGEGTDFHAVANGYVSITPLQMDLTRFSQMESVTAWLKP", "text": "FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SurE nucleotidase family."}
{"protein": "MWRLKVGAESVGEEDEKWVKSVSNHLGRQVWEFCADAAADTPHQLLQIQNARNHFHHNRFHRKQSSDLFLAIQYEKEIAKGAKGGAVKVKEGEEVGKEAVKSTLERALGFYSAVQTRDGNWASDLGGPLFLLPGLVIALHVTGVLNSVLSKHHRVEMCRYLYNHQNEDGGWGLHIEGTSTMFGSALNYVALRLLGEDADGGDGGAMTKARAWILERGGATAITSWGKLWLSVLGVYEWSGNNPLPPEFWLLPYSLPFHPGRMWCHCRMVYLPMSYLYGKRFVGPITPKVLSLRQELYTIPYHEIDWNKSRNTCAKEDLYYPHPKMQDILWGSIYHVYEPLFTRWPGKRLREKALQAAMKHIHYEDENSRYICLGPVNKVLNMLCCWVEDPYSDAFKLHLQRVHDYLWVAEDGMRMQGYNGSQLWDTAFSIQAIVATKLVDSYAPTLRKAHDFVKDSQIQEDCPGDPNVWFRHIHKGAWPLSTRDHGWLISDCTAEGLKASLMLSKLPSTMVGEPLEKNRLCDAVNVLLSLQNDNGGFASYELTRSYPWLELINPAETFGDIVIDYPYVECTAATMEALTLFKKLHPGHRTKEIDTAIGKAANFLEKMQRADGSWYGCWGVCFTYAGWFGIKGLVAAGRTYNSCLAIRKACEFLLSKELPGGGWGESYLSCQNKVYTNLEGNKPHLVNTAWVLMALIEAGQGERDPAPLHRAARLLMNSQLENGDFVQQEIMGVFNKNCMITYAAYRNIFPIWALGEYCHRVLTE", "text": "FUNCTION: Oxidosqualene cyclase involved in the biosynthesis of the highly oxygenated tetracyclic triterpenes cucurbitacins. Converts oxidosqualene to cucurbitadienol and does not produce lanosterol. SIMILARITY: Belongs to the terpene cyclase/mutase family."}
{"protein": "MSKGTLFDKVWDLHTVGTLPSGLTQLFIGLHLIHEVTSPQAFAMLRERGLKVLFPERTVATVDHIVPTENQARPFVDSLAEEMIQALENNCQENNITFYNIGSGSQGIVHVIAPELGLTQPGMTIACGDSHTSSHGAFGAIAFGIGTSQVRDVLASQTLALSKLKVRKIEVNGNLNPGVYAKDVILHIIRTLGVKGGVGYGYEFAGTTFEQMNMEERMTVCNMAIEGGARCGYVNPDRVTYDYLKGRDFAPKGADWDKAVAWWDSIKSDVDAQYDDVVVFDAAEISPTVTWGITPGQGIGVNQSVPQPEELLEEDRFIAEEAYRYMDLYPGQPIKGTKIDVCFIGSCTNGRISDLREAAKIAKGRHVAEGIKAFVVPGSERVKQEAETEGLDKIFQEAGFEWREPGCSMCLAMNPDKLQGRQISASSSNRNFKGRQGSSSGRTLLMSPAMVATAAIKGEVSDVRELL", "text": "FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily."}
{"protein": "MCTIISVNHHHVAILSKPKVKLFHTKNKRSASINLPWSLSPSSSAASRPISCSISSKLYTISSAQEETRRSGNYHPSVWDFDFIQSLDTDHYKEEKQLEREEELIMEVKKLLGAKMEATKQLELIDDLQNLGLSYFFRDEIKNILNSIYKIFQNNNSTKVGDLHFTSLGFRLLRQHGFNVSQGVFDCFKNEHGSDFEKTLIGEDTKGVLQLYEASFLLREGEDTLEVARKFSTEFLEEKLKAGIDGDNLSSSIGHSLEIPLHWRIQRLEERWFLDAYSRRKDMNPIIFELAKLDFNIIQATQQEELKDLSRWWNDSSLPQKLPFVRDRLVESYYWALGLFEAHKFGYERKTAAKIITLITALDDVYDIYGTLDELQLFTHVIRRWDTESATQLPYYLQLFYFVLYNFVSEVAYHILKEEGFISIPFLHRAWVDLVEGYLQEAKWYYTKYTPTMEEYLNYASITIGAPAVISQIYFMLAKSKEKPVIESFYEYDEIIRLSGMLVRLPDDLGTLPFEMKRGDVAKSIQIYMKEQNATREEAEEHVRFMIREAWKEMNTTMAANSDLRGDVVMAAANLGRDAQFMYLDGDGNHSQLQHRIANLLFKPYV", "text": "FUNCTION: Monoterpene synthase that catalyzes the formation of (3R)- linalool from geranyl diphosphate, but not from farnesyl diphosphate or geranylgeranyl diphosphate. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
{"protein": "MWFKNLQVHRFSAPWSLSADEVEASLAKHAFFPGTSLEMQTQGWASPRDNGQLVHTVGGQMLLTLRTEKKLLPTTVVNQVTRARAAEIEEQQGYKPGRKQMKELKEQVTEELLPRAFSIRRDTRVWIDPDNGWLAIDAAATAKADEVRGMLFKALDPLPLINLHVNQSPVAAMTEWLAGDAAPGGFTVDQEIELQSGAESKATVRYVRHPLDPEDLRRHIAAGKRCTRLAMTWNDRVSFVLTDGLVVKKVAPLDVIKEQADGTAHDEDERFDADFTMMAGELSGMLGDLTEALGGERKA", "text": "FUNCTION: May be involved in recombination. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the RdgC family."}
{"protein": "MVTKNSTRTEVKALAQNIHMSPFKARRVIDQIRGRSYEETLMILELMPYRAAFTILKLVYSAAANANNLGLNEAESFISKAEVNGGTVLKRLRPRARGRSYRIKRPTCHITIVLKDKSKNL", "text": "FUNCTION: This protein binds specifically to 23S rRNA. FUNCTION: The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL22 family."}
{"protein": "MATDDDSFPWDQDSILSRDLLSASSLQLCYENLNRSCVRSPYSPGSRLILYAVFGFGAVLAVCGNLLVMTSILHFRQLHSPANFLVASLACADLLVGLTVMPFSMVRSVEGCWYFGNTYCKFHSCFEGSFCYSSLFHLCFISLDRYIAVSDPLIYPTRFTASISGKCITFSWLLSIIYSFSLLYTGANEAGLEDLVSALTCVGGCQVAVNQSWVFINFLLFLVPALVMMTVYSKIFLIAKQQAQNIEKMSKQTARASESYKDRVAKRERKAAKTLGIAVAAFLLSWLPYFIDSIIDAFLGFITPTYMYEILVWIVYYNSAMNPLIYAFFYPWFRKAIKLIVTGKILRENSSTINLFPE", "text": "FUNCTION: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MATSILGEEPRFGTTPLAMLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATGGRGSGGLAGGSGAANSAFCLASTSPTSSAFSSDYGGLFSNSAAAAAAAAGVSPQEAGGQSAFISKVHTTAADGLYPRVGMAHPYESWYKSGFHSTLAAGEVTNGAASSWWDVHSSPGSWLEVQNPAGGLQSSLHSGAPQASLHSQLGTYNPDFSSLTHSAFSSTGLGSSAAAASHLLSTSQHLLAQDGFKPVLPSYSDSSAAVAAAAASAMISGAAAAAAGGSSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHSCHIPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACPVCNKRFMRSDHLSKHIKTHNGGGGGKKGSDSDTDASNLETPRSESPDLILHDSGVSAARAAAAAAAAAAAAAAAASAGGKEAASGPNDS", "text": "FUNCTION: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
{"protein": "MNTITLTARPEALTFAPEQSALIVVDMQNAYASQGGYLDLAGFDVSSTAPVIENIKTAVAAAREAGMTIVWFQNGWDSDYLEAGGPGSPNFHKSNALKTMRRCPELHGKLLAKGGWDYQLVDELTPLPGDIVLPKPRYSGFFNTPLDSMLRARNIRHLVFTGIATNVCVESTLRDGFFLEYFGVVLEDATHQAGPPFAQQAALFNIETFFGWVSDVQSFCDALSPEALARIA", "text": "FUNCTION: Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2. SIMILARITY: Belongs to the isochorismatase family. RutB subfamily."}
{"protein": "MAAMSLLRRVSVTAVAALSGRPLGTRLGFGGFLTRGFPKAAAPVRHSGAHGKRLFFIRPSRFYDRRFLKLLRFYIALTGIPVAIFITLVNVFIGQAELAEIPEGYIPEHWEYYKHPISRWIARNFYDSPEKIYERTMAVLQIEAETAELRLKELEVRKLMRVRGDGPWYYYETIDKELIDHSPKATPDN", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFB5 subunit family."}
{"protein": "MLDAFSRAVVSADSKTAPIGGDDLNQLRSFIASGNRRLDAVNAIASNASCMVSDAVAGMICENTGLIQAGGNCYPNRRMAACLRDAEIILRYVSYALLAGDASVLDDRCLNGLKETYTALGVPLQSTARAVAIMKAQAAAHIQDNPSEALAGAKLRKMGTPVVEDRCASLVAESSSYFDRVIAALS", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=Forms the periphery of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family."}
{"protein": "MITRLSTLFLRTLREDPADAEVPSHKLLVRAGYIRRVAPGIYSWLPLGLRAVRNIEAVVREEMDAIGGQELLFPALLPREPYETTQRWTEYGDSLFRLKDRKGADYLLGPTHEEMFAATVKDLYNSYKDFPVTLYQIQTKYRDEERPRAGVLRGREFVMKDSYSFDISDAGLDESYAKHRAAYQRIFDRLGLEYAICQATSGAMGGSASEEFLAVSENGEDTFVRSTSGNYAANVEAVVTQPGVERDIEGLPEAVTYETPVSETIDALVDWANSIDVQIEGREVTAADTLKCIVVKVREPGAEEAELTGILLPGDREVDMKRLEASLEPAEVELAVESDFADNPFLVKGYVGPVGLAKNGVKVLADPRVVTGTSWITGADEKERHVVGLVAGRDFTPDGFIEAAEIKEGDPAPAGEGTLTLARGIEIGHIFQLGRKYTEAFDVQILDENGKRAIPTMGSYGLGVTRLLAVLAEQRHDDAGLNWSVEVAPYQVHVVAANKDAAAIEAAERFAAELSAAGLDVLFDDRPKVSPGVKFKDAELLGMPFALILGRGYAEGKVELRVRGGEKSELDADQAVAQIVEMVAQARN", "text": "FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala- tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily."}
{"protein": "MATASVAFKSREDHRKKLELEEARKAGLAPAEVDEDGKEINPHIPEYMSKAPWYLKSEQPSLKHQKNWKIEPEPKKIWYDRGKKIYQAEQYRKGACINCGAMTHSSKACMDRPRKIGAKYTNMNIAADEKIESFELDYDGKRDRWNGYDTSTYRHVVDRYDAKEEARKKYLKEQQLKKLEEKNNNENGDDATSDGEEDLDDLRVDEAKVDESRQMDFAKVEKRVRTTGGGSTGTVRNLRIREDTAKYLLNLDVNSAHYDPKTRSMREDPLPDADPNEKFYLGDNQYRNSGQALEFKQINIHSCEAFDKGHDMHMQAAPSQAELLYKNFKVAKEKLKTQTKDTIMEKYGNAATEGEIPMELLLGQSERQIEYDRAGRIMKGQEVIIPKSKYEEDVHANNHTSVWGSWWKDHQWGYKCCQQTIRNSYCTGSAGIEAAEASIDLMKANIARKEASKESPKKVEEKKMATWGTDIPEDLELNEEALANALKKEDLSRREEKDERKRKYNVNYTNDVTSEEMEAYRMKRVHHEDPMRNFPG", "text": "FUNCTION: Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLU7 family."}
{"protein": "MSKSLRVGVVGAGAMGADHIDRINNRTSGAHISAIIEPDAARAAAAAENAPGAQAFTRIEDAIAADAVDAVLIAVPGQFHEPVLVPALEAGLPILCEKPLTPDSESSLRIVELEQKLDKPHIQVGFMRRFDPEYNNLRKLVESGEAGELLMLRGLHRNPSVGENYTQSMLITDSVVHEFDVIPWLAGSRVVSVEVKYPKTSSLAHSGLKEPILVIMELENGVLVDVEMNVNIQFGYQVATEAVFEKGLARIGQPSGMQRWRDGEFLINEHTDFTTRFATAYDRQIQSWVDAVHEGTLVAGPNAWDGYLVALSCEAGVKAFDGGVIPVDAAPRPDFYA", "text": "FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo- inositol (2KMI or 2-inosose). SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MKLYDNGVAVLGCGNLGNAIAKGLVASKQFKSNQIVLTKRNLSTIEPLKREGYHVTTSNHDAVSRCKIVIVCVVPAQLDDLLDSIKQSVTENHIIISVVSGASIEDIRSHLEKDVPIVRAMPNTAIQHCQSMTCLAIRSSHQKSTNSPSDKAKDNALEVAKKIFNCLGMSIVLSEEQIVPATALCACGIAFFCRAIRAAAQGGCEIGFHAEDAIRIAAQTAKGAATLLLENNFHPEYEIDKVTTPQGCTIAGLNQMEHAGFSSAMIKGIVTSSDKAASLYTQKQQNKKQQQLKQQQHQQHQHQQHQQHQQQVQQQEPHQYQQQQQQSHQQSQYNQGHNYGHQNQHHHNHDDQHQNYYNQDQKRRNNRKHRSNENYDNHHHHNQQYQQHQQPTQQESQEQTQQPEQTQSTNQSNQRRNSESRNGKSPQKQPQKQSQVQQPSSTTENTDQQQQQQPPQEQQQQQEQPQQPQEQQQQPNVVDEAERPKEQQQQPQQQQQTIDKKGYNNNRRGGRHYSYNNNYNSHHHRHNGINKNSSSMYHDEKRHEVKTEQIN", "text": "SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family."}
{"protein": "MSGVVALGHASSWGAALVRISPYTFSAIGIAISIGVSVLGAAWGIYITGSSLIGAAIEAPRITSKNLISVIFCEAVAIYGVIVAIILQTKLESVPSSKMYDAESLRAGYAIFASGIIVGFANLVCGLCVGIIGSSCALSDAQNSTLFVKILVIEIFGSALGLFGVIVGIIMSAQATWPTK", "text": "FUNCTION: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family."}
{"protein": "MATLDSDVTMIPAGEASSSVAASSSNKKAKRFEIKKWSAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNSEWEFQKYGH", "text": "FUNCTION: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The SCF complex plays a crucial role in regulating response to auxin and is essential for growth and development. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL1. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the RING-box family."}
{"protein": "MEKHDLLYEGKAKKIYRTDEEGLLWVEYKNSATAFNGEKKASIEGKARLNNEISSLIFSYLKEQGVDSHFVKRLSETEQLIHQVTIIPLEVVVRNVIAGSLAKRIGIEEGTPLEKPLVEFYYKDDDLGDPLVTEDHIAILQAATKEQVDILKVKAIEVNDALTTFFAGIGVKLVDFKLEFGVTADGAILLADEISPDTCRLWDAKTGERFDKDLFRRNLGNLQDGYEQILTRIEQKA", "text": "SIMILARITY: Belongs to the SAICAR synthetase family."}
{"protein": "MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYVYGPLPQSFDKEWVAKQTKRMLDMKVNPIQGLASKWDYEKNEWKK", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase IV family."}
{"protein": "MYRIIAVDLDGTLLTSENKITKYTKEIIQILIQKKFYFVFASGRHYIDIMKIKDSLKINIFIISSNGSKIYNLDNNLIFSDNLDENIASKLCRIKYSDKEIITQVYQNDQWYINNNKVENNFCSLLSSLQYKYFYPDDLNFKNISKIFFTSRNFQKLHILKRKIINFYGNKVHVNFSIPGCLEIVSGDHLKGYGLKLIANLLGVSLKNCIAFGDGMNDQDMLKVAGKAYIMKNSDPHLKIALPHLEIIESNDNDGVARCLNKIFIENNKEML", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family."}
{"protein": "MSAPIYLGVIGVGGVGTAFLNQLARLPNAPKLILLARSSQTLLSPTPSYSPTIPAAEWKTAVETPSLTKSGALTPDEIATYLASAPGRSILVDNTSDPALASNYPVFLRKGISVVTPNKKGFSSDLSLWKEIFAAAAEGKALVYHESTVGAGLPVISTLKDLVNTGDEVTRIEGVFSGTLSFLFNTFAPASGSSSAKWSEVVSQAKELGYTEPDPRDDLNGMDVARKLTILARIAGLDVQSPDSFPIESLIPAELTSLPSSADGIAQFMARLPEFDSQMAAIKEGAEKAGKVVRYVGSVDVAKKEVRVGLQQFDKDSAIAGLKGSDNIISFYTRRYGSNPLIVQGAGAGGDVTAMGVTADLLKVIERL", "text": "FUNCTION: Involved in osmoadaptation. SIMILARITY: Belongs to the homoserine dehydrogenase family."}
{"protein": "GLWEKIKEKANELVSGIVEGVK", "text": "FUNCTION: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily."}
{"protein": "MKAEIITVGDELLTGNTVDSNSAFIASKLTEKGYLVRRITTVGDDVEEIKSIILEALDRKPDVLVISGGLGPTHDDVTMLAVSKALNRELELCEECLERIRKFYVELHKKGLIDDPELNEARKKMAYLPKGATPLQNTEGAAPGAFIEHEGIKIFVLPGMPREMKAMLLNEVLPRLGERTFIQKKYLAEITDESKLAPILSEAIRKFNVRIHSSPKGFGKYIGIIIFGEDEEIIEKVIEFMQSRGISFKEGW", "text": "SIMILARITY: Belongs to the CinA family."}
{"protein": "MAARDATSGSLSEESSALDLPSACDIRDYVLQGPSQEANSEAFSSLEFHSFPYSSDVDPDTSNLNIEQNNSWTAENFWLDPAVKGQSEKEEDDGLRKSLDRFYEMFGHPQPGSANSLSASVCKCLSQKITQLRGQESQKYALRSFQMARVIFNRDGCSVLQRHSRDTHFYPLEEGSTSLDDEKPNPGLSKDITHFLLQQNVMKDL", "text": "FUNCTION: Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. SUBCELLULAR LOCATION: Chromosome."}
{"protein": "MTAELNFLDLFLKASIVVQLVIVILISFSIISWAIIIQRSRILTNALKEARTFEDRFWSGEDLNKLYEGLSNRRDGLTGSEQIFCVGFKEFSRLKQVNPDAPEAIIKGTMRAMNLAMNREIESLENRVPFLATVASVSPYIGLFGTVWGIMHAFMALSGAKQATLQMVAPGIAEALIATAIGLFAAIPAVMAYNRLSLRVNAIEQDYGNFIDEFTTILHRQAFGKAPH", "text": "FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ExbB/TolQ family."}
{"protein": "MVDKLTHLKQLEAESIHIIREVAAEFDNPVMLYSIGKDSAVMLHLARKAFFPGKLPFPVMHVDTQWKFQEMYKFRDRMVEELGLDLITHVNPDGVAQGINPFTHGSAKHTDIMKTEGLKQALDKHGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPELWNVYNGKVNKGESIRVFPLSNWTELDIWQYIYLEGIPIVPLYFAAEREVIEKNGTLIMIDDERILEHLSDEEKARIVKKKVRFRTLGCYPLTGAVESEAESLTDIIQEMLLTRTSERQGRVIDHDGAGSMEDKKRQGYF", "text": "FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric- sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily."}
{"protein": "MGIKIIIAGFKGKMGQAAYKMVTEDPELELVGLLDPFTDEKEVAGVPVFNAKEELAGLEAHVWVDFTTPKVAYDNTRFALEQGFCPVVGTTGFTPEQLEELITLSREKQLGGLIAPNFALGAVLLMQFAAQAAKYFPNVEIIELHHDQKKDAPSGTAIKTAELISQVRPSKQQGAADEEESIAGARGAYFDGMRIHSVRLPGLVAHQEVIFGSQGEGLTLRHDSYDRASFMTGVNLAIKEVVKRSELVYGLEHLL", "text": "FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapB family."}
{"protein": "MGVRMWLPFPMLLLSALPATLLSGAAGFTPSLDSDFTFTLPAGQKECFYQPMPLKASLEIEYQVLDGGELDIDFHLASPEGRTLVFEQRKSDGVHTVETEDGDYMFCFDNTFSTISEKVIFFELILDNMGEEVEGQEDWKKYITNTDVLEMKLEDILESINSIKSRLSKSGHIQTLLRAFEARDRNIQESNFDRVNFWSVVNLMVMVVVSAIQVYTLKSLFEDKRKSRT", "text": "FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Required for the maintenance of the Golgi apparatus; involved in protein exchange between Golgi stacks during assembly. Probably not required for COPI-vesicle-mediated retrograde transport (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein Note=Probably cycles between compartments of the early secretatory pathway. SIMILARITY: Belongs to the EMP24/GP25L family."}
{"protein": "MIDGIKQLGSLSLTRGASGVSSLTESLFGGEQQSTPAQQTGASFASVLGNVSMDAMNNLKKAEVASFEGIQGKANTREVVDAVLSAEQSLQTAIALRDKIVSAYLDITKMQI", "text": "SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the FliE family."}
{"protein": "MSKSRRIGILTSGGDCSGLNAVIRAVVHCASGKGWEVFGIRQATLGLMARPPQVSKLEIDQVDPLLTSGGTMLGTTNKGDPFAFPMPDGSFCDRSSEIIAGYHQLDLDALIGIGGDGSLAILRRLAQQGAINLVGIPKTIDNDIGITEHAIGFDTAVNIATEALDRLHFTAASHSRVMILEVMGRDAGHIALAAGIAGGADVILIPEILYSMDDICYHIKHRQEEGKNYCLIIVSEAVRTQDGEILTLTNRLGQSRYGGIGEYLADQISDRIGAETRVTVLGHIQRGGIASPLDRLVASAFGVAAVNLIEAAKYDYMVAWQNRQVITVPIEEAIAQYKAVNPEDALVKTARGLGIYLGE", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily."}
{"protein": "MAKKVQKKLPRRKEEFTYHGYKIDELRAMSLEDLLPVMPSRARRKVLRGWTIGEEKLLSDIRSNGSRIRTHQRDMIILPEMIGREIEIYNGKEFIRVELQPESVFHYLGEFALTRRRVTHGSAGIGATRSSKFVPLK", "text": "FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SIMILARITY: Belongs to the universal ribosomal protein uS19 family."}
{"protein": "MDLDKIGAETRQILQDVLDKASLDEGDVFVLGLSSSEVMGGHIGRNSSLEVGQVIVKTVLDILEEKGIFLAVQGCEHLNRALVVERSLAKKKDLEIVNVLPTLHAGGSGQLAAFQYMKDPVEVEFIVAQAGLDIGDTAIGMHVKHVQIPIRPKLKSVGAAHVTALASRPKLIGGSRAAYREDKIRKD", "text": "SIMILARITY: Belongs to the UPF0340 family."}
{"protein": "MFEINPVNNRIQDLTERTNVLRGYLDYDAKKERLEEVNAELEQPDVWNEPERAQALGKERSSLEAIVDTLDQMTQGLDDVSGLLELAVEADDEETFNEAVAELNTLEEKLAQLEFRRMFSGEYDSADCYLDIQAGSGGTEAQDWASMLLRMYLRWAEARGFKTEVIEESEGEVAGIKSATIKISGEYAYGWLRTETGVHRLVRKSPFDSGGRRHTSFSSAFVYPEVDDDIDIDINPADLRIDVYRASGAGGQHVNRTESAVRITHIPTGIVTQCQNDRSQHKNKDQAMKQMKAKLYELEMQKKNAEKQAMEDTKSDIGWGSQIRSYVLDDSRIKDLRTGVETRNTQAVLDGSLDQFIEASLKAGL", "text": "FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
{"protein": "MPLNFKPGDLVFAKMKGYPHWPARIDDVKDGAVKPPPNKYPIFFYGTHETAFLAPKDLFPYEKCKDKYGKPNKRKGFNEGLWEIQNNPQASYSLPPASVSSSDSDVPEEKSTARSDGEEEQETGQAILPTAGVSSSDEEGSDKGGVKRKGRTTTPPSAKRTKHSSSEQEPDSASSSEEENSDSDQDFTPEKSTPRIQRRTTNLGKKNKIFAESDSKSDESEDEKKEEEQKKSPSSSSASSPSLSSSDSEAPVKKTPRGRRPAEKPAPKPRGRGRKAEPIPSSDSSDSDSSVDRISEWKKRDEERRRELEERRKKEQEEQLRRLREEEREEEERKKREKAEKGDKSDSDSDSSKSEVIAPPKPKKSSSSSDSEEDKKPVKEVKPVASEIKKGKKEKVRAISDDSDSDKKVKKTIKKTRPSESARKTNQKEKRGERPRGRPSKVEKEKKKPEVITARKVVKKEPTVEEKLQKLHSEIKFALKVDNPDIQKCLDALEELGGLQVTSQILQKNTDVVATLKKIRRYKANQSVMDKAAEVYSRIKARILGPKLESQQKTVQKVNTAEKDPEEEKQTGKVEEDMDASVNGDFLSQRIETAGDKEQDGEGQNLDNKTEMETKQNNHAEHNSNPTEETIECRLISSENQTS", "text": "FUNCTION: May act as a regulator of myogenesis (By similarity). Promotes the repair of DNA double-strand breaks (DSBs) through the homologous recombination pathway by facilitating the recruitment of the DNA endonuclease RBBP8 to the DSBs (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the HDGF family."}
{"protein": "MKDPGLVAVGVAAAVAFGTALALGLPPIQRDKPRRKSWEVSAAFPTPVIAAGATVLVIRVIGYHPPIPLAIVGAVVGALSAAFTAYIEKVFPRPEAG", "text": "FUNCTION: One of the integral membrane subunits of multisubunit membrane-bound [NiFe]-hydrogenase eha. Eha is predicted to form large electron transfer complex and might catalyze energy-driven reduction of low-potential redox carriers (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EhaA family."}
{"protein": "MIGLNTAAIYILQTLGSLYLLIVLLRFILQLVRADFYNPLSQFIVRATKPLLNPLRRIIPGFGGIDLASLVLAILIQLVLMILILMLMGYGVGGFIMQLLIWSIIAVTSLFLKVFFFALIISVILSWVAPGSYNPGAQLVNQICEPLLMPFRKLLPNLGGLDLSPIFAFLALKLIDMLVINNLAAMTGMPQQLSIFL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the YggT family."}
{"protein": "MAYTPMIKQYKEIKEQNKDCILFFRLGDFYEMFFDDALIASKELEIVLTQRDCGENKKCPMCGIPYHVSDVYINKLVSKGYKVAICEQLEDPKLVKGLVKRGIIKIYTPATVIENENSDTGNFNYLMSISKKSNEVAISYIDISTGDVSYTNTTSDDIYKIIENEISKITPKEIIFNDHEFSTNSLETIASKFSIVLTTVNNGTDSIDFINSKITYDNTNSETTNICVANLLKYVFRYQDDLVHINSSRKYYINEFMEIDSNSVINLEIQKNLYTNSKNGSLFGVLNHTKTSMGSRLLHSYLERPLMDKEEILIRQNRVEEIFEDYELLVNLENCLDGIYDLDRLIAKLSYKSANAKDLIALKVSIEKIPYLKNLLNCNKKNVQLIGEKLDDLRDIYDLIDKSIVDDPPVILTEGNLIKPNFSNELDQLRYNRVNGKNELVEYEMSEKDRLGIKNLKIVFNKKLGYFIDVTKSNLNKVGEDYEKRQTLTNSSRFKTKQLEAIESKILDSEDEIFELEYKIFEDIRKIILENLSRIKKSADLIAIIDVSNSLAKCAYLNNYIKPDINTYGLIDVLESRHPIVELSVGQSEFITNDILIGSGKNDIQLITGPNMSGKSTYLRQVALICILNQIGSFVPATKANISIVDKIFTRIGSSDNLFKGESTFMVEMKEMSNIIKYATSNSLLVLDEIGRGTSTYDGLSLAWAIVEYISKDIKAKTLFATHYHELTELEKKLDNLINMKVDIKETNDSIIFLRKITRGSTDKSYGIEVAELAGMPKTLIKRAKSILKEIDKEDTKIDLPIADFAVQNEMEDDKNIHELKDFKDEIKNINVNEITPIQSLQLLNELVIKASKLGD", "text": "FUNCTION: This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. SIMILARITY: Belongs to the DNA mismatch repair MutS family."}
{"protein": "MKKLVLAALLASFTFGASAAEKINFGVSATYPPFESIGANNEIVGFDIDLAKALCKQMQAECTFTNHAFDSLIPSLKFRKYDAVISGMDITPERSKQVSFTTPYYENSAVVIAKKDTYKTFADLKGKRIGMENGTTHQKYIQDQHPEVKTVSYDSYQNAFIDLKNGRIDGVFGDTAVVNEWLKTNPQLGVATEKVTDPQYFGTGLGIAVRPDNKALLEKLNNALAAIKADGTYQKISDQWFPQ", "text": "FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 3 family."}
{"protein": "MPKLAVVLLVLLILPLSYFDAAGGQAAEGDRRGNGLARYLQRGGRDNEAECQINTPGSSWGKCCLTRMCGPMCCARSGCTCVYHWRRGHGCSCPG", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin specifically blocks mammalian neuronal nAChR of the alpha- 7/CHRNA7, alpha-3-beta-2/CHRNA3-CHRNB2 and alpha-4-beta-2/CHRNA4-CHRNB2 subtypes (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin D superfamily."}
{"protein": "MINTHVKLPGLDLKNPIMPASGTFGFGDVPAAKKFNLNDLGAMVIKTTTPHSTTGNPQPQIAVLNTGVLNSVGLTNPGVDAVIKDKLTPLRSEYPNLPIMASVGGEDEAGYLEVAKKLSDSGLVNALEINVSCPNVNQGGMSFGVHPDVVEELTKKIKSLVKIPIYVKLTPNVTDITQIAKAAENGGADGLSLINTLLGMEIDVETRKPVLGHNIGGLSGEAVKPIAIRMVHQVRESTTLPIIGMGGISSAKDVIEFILAGANAVAVGTAHFKDSLASKHIADDLPKELEKLGITDINQLVNKVNFN", "text": "FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily."}
{"protein": "MNNPSTPKAPLADYLAHLPLAEEERARLGESASFSELHARLAGEGAASEAGGDPALASVRARLQLGSPELDDAEMFGVDAQGRTFLKISPPIRRTKVIPEPWRTNILVRGWRRLTGRSNPPKPKRALPRARWQRVGSLRRFILLLLMLAQTSVATYYMKGILPYQGWAFVDLEELTRQSLLDTVQQVLPYVIQFGILALFAILFCWVSAGFWTALMGFWELLTGRDRYRISGSSAGSEPIAADARTAIVMPICNEDVPRVFAGLRATVESMAATGEMERFDFFVLSDTNDPDIAVAEQQAWLELCRETRGFGKIFYRRRRRRVKRKSGNIDDFCRRWGGDYRYMVVMDADSVMSGDCLAKLVRLMEANPEAGIIQTAPKASGMDTLYARMQQFATRVYGPLFTAGLHFWQLGESHYWGHNAIIRMQPFIDHCALAPLPGKGSFAGAILSHDFVEAALMRRAGWGVWIAYDLDGSYEELPPNLLDELKRDRRWCHGNLMNFRLFLVKGMHPVHRAVFLTGVMSYLSAPLWFFFLVLSTALLAVHQLMEPQYFLEPRQLFPIWPQWHPEKAIALFSTTLTLLFLPKLLSVMLIWAKGAKGFGGVIRVTLSMLLEMFFSVLLAPVRMLFHTRFVLAAFLGWSVQWNSPQRDDDATPWSEAIRRHGMQTLLGLAWTLLVAWLNPRFLWWLSPIVGSLMLSIPVSVISSRVKLGLRARDEKLFLIPEEYDTPRELRATDEYTYENRWHALKDGFLKAAVDPLLNALACAMGTARHNRAQAIETVRGERIGKAIEKGPEQLDGATRLALLSDPVALSRLHAQVWEENRDDWLGRWRKAEADDPHAASVPLAQVVPGDAGLLPAAQS", "text": "FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. OpgH subfamily."}
{"protein": "MIKYKRILIKLSGEGFANKEKNLAIDFELVAKIASQLKIIIEKGVQVSIVVGGGNFWRGVSAEKNGIPRNRADFIGMLATEMNALALQSGFEKAGLKARVQSSINIDQKVAENYINEKTLKYLNNGEVVIFAGGTGRPYFTTDTAATLFAAEIKAEVILMGKNKVDGVYDSDPKKNENAKHFSKITYDQILEKKLQVMDLTATSMARDNNINLIVFNLLEDNSIIKALEGKITHTEVTR", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UMP kinase family."}
{"protein": "MHRRITGKLVIATHNPGKLAEMRELLAPYGIEAISAGELGLAEPDETGDSFQANARIKAEAAAKAAQLPAFADDSGLAVDALDGAPGIYSARWAGDAKDFAGAMARIERLLQERGATAPERRTAHFVSALCVAWPDGHIEEVEARADGTLVWPPRGTAGFGYDPVFLPEGHSRTFGEMTSIEKHGLPPLGLGLSHRAKAFVKLAEICLAG", "text": "FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. SIMILARITY: Belongs to the HAM1 NTPase family."}
{"protein": "MPFPVPDPFVWDTSFQVFYFKLDDQHRAIFETLFNSTNDNTPGNLQLFYIVTANHFEEEEGWMVSASYGGYDAHKKLHEEFLAKVRSFSAPVSKENLFYAKDWLVQHIKTIDFKYKQLL", "text": "FUNCTION: Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms (By similarity). SIMILARITY: Belongs to the hemerythrin family."}
{"protein": "MAKITLDEAKKEAASLRTKLDEWADAYYSKDAPEVEDNVYDQSYNRLLELEKAFPEIVTPDSITQRVGGEIDSDFTKVNHPIPMLSMGDVFSKDELKEFDQRMQKLVGHPVEYNVELKIDGLSLSLEYQDGKLVRASTRGNGYIGEDVTANARYIADIPQVLPEPLTIEVRGECYMGKEAFAKLNQEREDEGLSVFANPRNAAAGSLRQLDPKVTKKRQLSTFIYTWVNPPREITSQHQAIERMHELGFHTNETGRKLANLDEVFDFIDEYTAKRNSLTYGIDGIVLKVDDLSLEQQLGNTVKVPRWEIAYKFPPEEQETIVRDIVWTVGRTGVVTPTAVMDPVQLAGTTVARASLHNPDYLNEKGVRIGDTVKLHKAGDIIPEISEVVLSKRPADSVPYEIPTTCPSCGQKLVHLEDEVALRCINPSCPAQVEEGIIHFASRPAMNIAGLGPKIVKQLIAKDLVHNVADLYHLTEDDLAQLDHFKEKSINNLLTAIDNSKKNSVELLITGLGIDHVGAKAARLIAQKFKNLEKIMSLGVQDIASIDTIGMTTAESMTTYFAQPEAQKLIEELRESGLNMDYLGADEPEEAPDNPFKDKTVVLTGKLEHYTRSEFTKKLQALGAKVTGSVSHKTDYVIYGKDAGSKYNKAEQLGVPLLTEEEAIAQIE", "text": "FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA subfamily."}
{"protein": "MTAIAPVITIDGPSGAGKGTLCKAMAEALQWHLLDSGAIYRVLALAALHHHVDVTSEDALVPLASHLDVRFVSTNGNLEVILEGEDVSGEIRTQEVANAASQVAAFPRVREALLRRQRAFRDAPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKGFSVNFERLLAEIKERDDRDRNRAVAPLVPAADALVLDSTRLSIEQVIEKALQYARQKLALA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily."}
{"protein": "MVKRNQRKKSAPKKRLTKAEVEKQRAIKRMILSVLMALLLIFAMLRLGVFGVTTYNMIRFLVGSLAYPFMFAWLIYLFCFKWLRQKDGMIAGVVIAFLGLLVEWHAFLFAMPRMLDQDIFLGTARLITRDLLALRVTEFVGGGMLGALLYKPIAFLFSNIGSYFIGFLFILLGLFLMTPWDIYDVSHFVKEAVDKLAVAYQENKEKRFIKREEHRLQAEKEALEKQAQEEEKRLAELTVDPETGEIVEDSQSQVSYDLAEDMPKEPEILAYDSHLKDDEASLFDQEDLAYAHEEIGAYDSLSALASSEDEMDMDEPVEVDFTPKTHLLYKLPTIDLFVPDKPKNQSKEKNLVRKNIKVLEDTFQSFGIDVKVERAEIGPSVTKYEIKPAVGVRVNRISNLADDLALALAAKDVRIEAPIPGKSLIGIEVPNSEIATVSFRELWEQSDANPENLLEVPLGKAVNGNARSFNLARMPHLLVAGSTGSGKSVAVNGIISSILMKARPDQVKFMMIDPKMVELSVYNDIPHLLIPVVTNPRKASKALQKVVDEMENRYELFSKIGVRNIAGYNTKVEEFNASSEQKQIPLPLIVVIVDELADLMMVASKEVEDAIIRLGQKARAAGIHMILATQRPSVDVISGLIKANVPSRMAFAVSSGTDSRTILDENGAEKLLGRGDMLFKPIDENHPVRLQGSFISDDDVERIVNFIKDQAEADYDDAFDPGEVSDNDPGFSGNGGAAEGDPLFEEAKALVLETQKASASMIQRRLSVGFNRATRLMDELEEAGVIGPAEGTKPRKVLQTN", "text": "FUNCTION: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the difSL recombination site, which is located within the replication terminus region. Required for activation of the XerS recombinase, allowing activation of chromosome unlinking by recombination (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Located at the septum. SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family."}
{"protein": "MKYFLDTADVSEIRRLNRLGIVDGVTTNPTIISREGRDFKEVINEICQIVDGPVSAEVTGLTCDEMVTEAREIAKWSPNVVVKIPMTEEGLAAVSQLSKEGIKTNVTLIFTVAQGLSAMKAGATFISPFVGRLEDIGTDAYALIRDLRHIIDFYGFQSEIIAASIRGLAHVEGVAKCGAHIATIPDKTFASLFTHPLTDKGIETFLKDWDSFKKK", "text": "FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily."}
{"protein": "MAVLDILTIPDERLKRKAQPVKDIEAIQGFIDDLIETMYHTDDGIGLASTQVGSTDAVIVIDLSETRDQPLVLVNPEIVEKSGEYVGEEGCLSIPGYRAKVTRFEKVKVTALDRQGKAIEIETDDFLAIVLQHEIDHLHGKVFIEHLSTLKQQIALKKVRKYA", "text": "FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. SIMILARITY: Belongs to the polypeptide deformylase family."}
{"protein": "MELLSRALFFFLLLSVLSSFSSSSFISDGVFESQSLVLGRNLLQTKKTCPVNFEFMNYTIITSKCKGPKYPPKECCGAFKDFACPYTDQLNDLSSDCATTMFSYINLYGKYPPGLFANQCKEGKEGLECPAGSQLPPETSAEVNAATTSSSRLWLTVSAALLVFVKLF", "text": "FUNCTION: Component of the FER-regulated Rho GTPase signaling complex. Acts as a chaperone and coreceptor for FER. Required for localization of FER to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor."}
{"protein": "MKTIIVFLSLLVLATKFGDAKEGVNQEQKKEVTQNEFRVEYLNEMAAMSLLQQLEAXESALFEKEAGRNSRQXRCAMGDVPCTKGKTNCCKGYECKPKSPSWWYDTDFCQPIHGGRPIGI", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 05 (ICK-7) subfamily. ICK-7 sub-subfamily."}
{"protein": "MEGWQRAFVLHSRPWSETSLMLDVFTEESGRVRLVAKGARSKRSNLKGALQPFTPLLLRYSGRGEVKTLRSAEAVSLALPLSGITLYSGLYINELLSRVLEYETRFSELFFDYLNCIQALAGTTGSPEPALRRFELALLGHLGYGVNFTHCAGSGERVDDTMTYRYREEKGFFASVVIDNNTFTGRHLKALEEREFPDVDTLRASKRFTRMALKPYLGGKPLKSRELFRQFMPKRTVKMKKD", "text": "FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family."}
{"protein": "MALKVAIAAGSAAKAIFKPALLCRPWEVLAAHEAPRRSISSQQTIPPSAKYGGRHTVTMIPGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNAIMAIRRNRVALKGNIETNHDLPPSHKSRNNILRTSLDLYANVIHCKSLPGVVTRHKDIDILIVRENTEGEYSSLEHESVAGVVESLKIITKAKSLRIAEYAFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVAARYPQITFDSMIVDNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYGHVYAVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVLASMDNENMHTPDIGGQGTTSQAIQDIIRHIRIINGRAVEA", "text": "FUNCTION: Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family."}
{"protein": "CISARYPCSNSKDCCSGSCGIFWTCYLRKDPCSKECLAP", "text": "FUNCTION: Causes paralysis to insect larvae (H.virescens). This toxin is active only on insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 13 (insecticidal toxin ABC) family. 02 (Calisoga) subfamily."}
{"protein": "MLERIKVCFTESIQTQIAAAEALPDAISRAALTVVQSLLNGNKILSCGNGTSSANAQHFAASMINRFETERPSLPAIALSADNVLLTAIGNDRLHEEIYAKQVRALGHTGDILLAISTRGNSRDIVKAVEAAVTRDMTIVALTGHDGGELAGLLGPQDVEIRIPSHRSARIQEMHMLTVNCLCDLIDNTLFPHQEV", "text": "FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. SIMILARITY: Belongs to the SIS family. DiaA subfamily."}
{"protein": "IEILLGGDDGSLAFVPNNFTVASGEKITFKNNAGFPHNVVFDEDEIPSGVDSGKISMNEEDLLBAPGZVYZVZLTZKGSYSFYCSPHQGAGMVGKVTVN", "text": "FUNCTION: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side. Note=Loosely bound to the inner thylakoid membrane surface in chloroplasts. SIMILARITY: Belongs to the plastocyanin family."}
{"protein": "MTSPTRRRTAKRRRRKLNKRGKLLFGLLAVMVCITIWNALHRNSEENEPSQETAAVSNTDQKKEVKKKTAKKSEEQIKTVDRNQKISNYLKEIGFSGTAMIVRNGEIVTNKGFGYADRKHYIQNNPLTSFYVGSSQKALIATAILQLEEKGKLQTSDPVSTYLPHFPNGQTITLKNLLTHTSGINGHIEGNGAITPDDLIKDIELQGIKRQPGVWDYKDSNYSVLAYIIAEVSGEPYEQYIKNHIFKPAGMTHAGFYKTYEKEPYPAVGYKMEGSKTVTPYIPDLSQLYGAGDIYMSAIDMYKFDQALIDGKLYSQKSYEKMFTPGSSSTYGMGFYVAPGSYSNHGVMPGFNILNSFSKSGQTIVILFSNIQNNAKLGQVNNKIYQLLNQE", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Localizes to the division septum during vegetative growth, and accumulates at the prespore during sporulation. SIMILARITY: Belongs to the beta-lactamase family."}
{"protein": "MARSFYSHIREAWKTPKEGKLAELQWQRQQEWRDQGAIERIERPTRLDKARSLGYKAKQGVVVARVSVRKGTARKQRFKAGRRSKRQGVNKITRRKNLQRIAEERSGRKFRNLRVLNSYWVGEDGSQKWFEVILLDPEHGAIQNDDDLSWICDDSQRGRAYRGRTSAGQRGRGQQKRGKGTEHTRPSIRANDKRGK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family."}
{"protein": "MSISIETITKRNQYRVDQPQRQPSRLSTVASISEYQSDYSKTVFEEIELEVIPNKQNISTRSFRNDGNDSDPQTLDPDAYPPKRSIAFVLLNSILSDMSMSTALPISAAYTEILGGTDAFSGLVIGIPTMISLVCLYPMLRFANPKSANGYTLYFRPLIVSCISQIIGHLLYSLAYRAQWLYLILIGRMCNGVGFTMFLYHKKYLTDKHFVGQNRSTFLATLNILAQTVGFMAGSFLGGLLAKACMHLTNPIWNQYTVGSWFMLFAWCIYGILLSIFFKEIRADGNDSSARKPENFNGQAVKLSYTHKFMLVFLSMVAFISYFNIAGYQASVPIYAKELYHYNAFQSGNFLSLSALVIAPLVFLSTFLSKWAEDRDMMLYGFILGILALVVHLVLDVLHKVRVQPYFVLYSAMQFGFSIGSAPLISLATKQLHPKYHILVGIIVQIGISAADTVGAICGGAIFDITTVGFIALNLGIAVLVFIQLLFLWNSIKTKTG", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MGNRSAADADGLLAGRGPGTGGGAGSPGAAAALVGGVLLIGAVLAGNALVCVSVAAERALQTPTNYFIVSLAAADLLLALLVLPLFVYSEVQGGVWQFSPGLCDALMAMDVMLCTASIFNLCAISADRFVAVAVPLSYNRQSGGGRQLLLIGATWLLSAAVAAPVLCGLNDARGRDPAVCRLEDRDYVVYSSVCSFFLPCPVMLLLYWATFRGLRRWEAARRTKLHGRRPRRPSGPGPPPPEAVETPEAPEAIPTPDATLAEPALPASEERRAKITGRERKAMRVLPVVVGAFLVCWTPFFVVHITGALCPACAVPPRLVSAVTWLGYVNSALNPLIYTVFNAEFRAVFRKALRLCC", "text": "FUNCTION: Dopamine receptor responsible for neuronal signaling in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior. Activated by dopamine, but also by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs. Agonist binding triggers signaling via G proteins that inhibit adenylyl cyclase. Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRVIIAGGGTGGHLFPGIALAESLIGKYPEAQIIFVGTPKGLEAKVIPKTGYELSFISIQGFVGKSFSEKAKSLKSLLKSMFESKNIINSFAPDIVFGVGGYASFPVVLAAFLKKIPTIILEQNTVPGLANKLLGKIASAVAITYPETIEYFSREKTYLTGTPIRKKILEGNKEKAKKLFDIEEGRITILILGGSLGARKINKAMTEGLSYLLPLKNRIQIIHQTGEADYNWVYNEYRNLSFRATVLPFIYDMVEAYSVADLVISRAGASTVAELTAIGKASILIPYPYAAYNHQEMNARRLLSRGACELILDRELNGEVLAKKINKILNKPEIMKEMEMASLAFGKPYAGEKIIEIAESLLRRKR", "text": "FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG subfamily."}
{"protein": "MENSHNESEEQPQSTPKVEEEQPAVEQSPENQCSEDDQSSEDLSSEEQSSDEEFFPEELLPELLPEMLLCEDRPPQECLPQKNAFEDRIPMEQPPCGIGKHKLEEGSFKERLARSRPQFRGDIHGRNLSNEEMIRAADELEEMKRVRNKLMIMHWKAKRSRPYPI", "text": "FUNCTION: May be involved in transcriptional regulation. Modulates various viral and cellular promoters in a promoter context-dependent manner. Does not bind DNA directly (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFS-II family. TFA subfamily."}
{"protein": "PGPCNCIETNVCICGTGCSGKCCRCGDACKCASGCGCSGCKVVCKCSGTCKCGCDCTGPTNCKCESGCSCK", "text": "FUNCTION: The metallothioneins are involved in the cellular sequestration of toxic metal ions. SIMILARITY: Belongs to the metallothionein superfamily. Type 2 family."}
{"protein": "MKISYLDFEQSVAELDAKVEELHALNQPGIADDISRLEVKARKELQRIYSKLGAWQTVQVARHPQRPYTMDYVQALFTEVQVLAGDRAFADDQAIIGGLARFNGQPIVWMGHQKGRDTKEKIQRNFGMPRPEGYRKALRLLRLAERFALPVFTFIDTPGAYPGIGAEERGQSEAIARNLAVMSDLAVPIICTVIGEGGSGGALAIGVGDRMLMLEYGVYSVISPEGCASILWKNAAMAAEAAETLGITARRLQGMGLVDEVLAEPLGGAHRDPEAVFALARERFAHHLQELQAMDTSKLLTTRYERLMHYGVVGAA", "text": "FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AccA family."}
{"protein": "MVAIRKEQSLSGVSSEIKKRAKRNTLSSLPQETQPLRKVRIIVNDPYATDDSSSDEEELKVPKPRKMKRIVREINFPSMEVSEQPSESSSQDSTKTDGKIAVSASPAVPRKKPVGVRQRKWGKWAAEIRDPIKKTRTWLGTFDTLEEAAKAYDAKKLEFDAIVAGNVSTTKRDVSSSETSQCSRSSPVVPVEQDDTSASALTCVNNPDDVSTVAPTAPTPNVPAGGNKETLFDFDFTNLQIPDFGFLAEEQQDLDFDCFLADDQFDDFGLLDDIQGFEDNGPSALPDFDFADVEDLQLADSSFGFLDQLAPINISCPLKSFAAS", "text": "FUNCTION: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
{"protein": "MAKITSLIGSGIVAATNQVGPHVKHIPAVGNLQKQIVSDQIQVRWSSTETSLKNDISATDVRGYKGHDMLAPFTAGWHSTDLEPLVIQKSEGSYVYDVNGKKYLDALAGLWCTSLGGNEPRLVAAATKQLNELAFYHSFWNRSTKPSLDLAKELLDLFTANKMAKAFFTNSGSEANDTQVKLVWYYNNALGRPDKKKFIARTKSYHGSTLISASLSGLPALHQQFDLPAPFVLHTDCPHFWRFHQPGETEEEFSTRLANNLENLILKEGPETIAAFIAEPVMGAGGVIPPPATYFEKVQAILKKYDILFIADEVICGFGRLGTMFGCEKYNIKPDLVSVAKALSSGYMPIGAVLVSPEVSDVIYSQSNKLGTFSHGFTYSGHPVSCAVALETLKIYKERNIIEQVNRISPKFQEGLKAFSDSPIIGEIRGTGLLHGTEFTDNKSPNDPFPPEWGIGAYFGARCEKHGVLVRVAGDNIMMSPPYILSLEEIDELIIKYGKALKDTENRVEELKSQKKIKSS", "text": "FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate or glyoxylate as amino-group acceptor. Cannot use beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MADSSNSSLNCTAIHDQTVLILGQVFNSVWLFISVIFLYIFACKLCFRPRIYLWLSFYTLGFMLWVLCKVLQEYVTGKFKCVITNCIGDFCLVFLSCIMLGIMLDRYLKIQGTLRGGMKDIHIGIFVSASCFGSLMIALLDGLHMGDSEKLQFNGTESFKCLPATSVSSYKAQLMFKSIFCIICIIMCLILTCLTAKKVLGTRLRKKYVIVGNVGLLSFVNILLWVMIACGLLKQALESNLSLCPTKQSTYIYPYTMPVTVIFVLVIYLFSSTHMKNAMRKSGQIRHSLSSPNQVQSSFRLV", "text": "FUNCTION: Acts as a viral G-protein coupled receptor that constitutively activates host alphai-type G-proteins, thereby inhibiting host forskolin-triggered CREB activation. SUBCELLULAR LOCATION: Host cell membrane Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSTMTDIGASGALHRTRSKPWYKVLYVQVLIAIVLGVLLGWVSPHLATNPWIKALGDGFVKLIKMVIAPIIFCTVVSGIAHIQDARKVGRVGVKALLYFEVVSSFALILGLIVGNLVPVGHGLAAKPDAGAVAKYVDQASHMSSVDFFLNIIPESVVGAFAKGDILQVLLFAILFGFALMALGERGHRLRDVIDDTAHAVFGVIAIVMKAAPVGAFGAMAFTIGKYGPAALGNLIGLVALFYATAALFVFVVLGLIAKFVGFNIFRFVGYIKDELLIVLGTSSSESALPQLMEKLERLGCSKSVVGLVVPTGYSFNLDGTNIYMTLATLFIAQALGIELTFTEQVTILLVAMLTSKGASGVTGAGFVTLAGTLAAVNPALVPGMAIVFSIDKFMSEVRALTNITGNGVATVFVSWWEGELDHDRLQANLNRTIDPSDVETAITTG", "text": "FUNCTION: Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family."}
{"protein": "MARGATWTRRLHLHGLFLAVLLLLTLPAGSTAAAGGGGGTVIGIDLGTTYSCVGVYRNGHVEIIANDQGNRITPSWVAFTGGGERLIGEAAKNQAAANPGRTVYDAKRLIGRRFADAEVQRDMRLLPFAVVDKGGKPHVRVEVRGGDVRLLSPEEVSAMVLARMKETAEAYLGEEVTRAVVTVPAYFNDAQRQATKDAATIAGLAVERILNEPTAAALAYGVGKEGAGGKNVLVFDLGGGTFDVSVLAIDGGVYEVLATNGDTHLGGEDFDQRVMEHFVELVRRKHGRDIAGDARALGKLRRECERAKRALSIQHQVRVEVESLFDGVDLSEPLSRARFEELNNDLFRKTMAPVRKAMADARLSNADIDEIVLVGGSTRIPKVRQLLRDYFGGKQPNQGVNPDEAVAYGAAIQANIVGGDTDNKTRDMVVLDVTPLTLGLETAGGVMATLIPRNTPVPTKRAQLFSTYKDKQTTVTVKVFEGERSMTRDNRLLGRFDLAGIAPAPRGAPQIEVAFEVDADGILSVSAADRATGRSERITISGDDRKTSREEIDRMLGEAEEFADEDRRHRERAGARNSLEAYVYGVKNAVVGGEMAGAMDGGEKEKVEAAVMEAYEWLDGNQDVGKEEYEEKLRELEDVCNPVMSAVYQRSGGSRRDGDGGGDDDHDEL", "text": "FUNCTION: Functions as chaperone during endoplasmic reticulum (ER) stress response. SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MSYYYGNYYGGLGYGLGGFGGFGGLGYGYGSSYGLGGYGGYGYFSPSFYGGYLSSGFY", "text": "FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SIMILARITY: Belongs to the KRTAP type 19 family."}
{"protein": "MRELVNIPLLQMLTLVAFSGTEKLPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWTRNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTANNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVLPCTTMGNPKPSVSWIKGDSALRENSRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGTAYSKLVKLEVEVFARILRAPESHNVTFGSFVTLRCTAIGMPVPTISWIENGNAVSSGSIQENVKDRVIDSRLQLFITKPGLYTCIATNKHGEKFSTAKAAATVSIAEWSKSQKESKGYCAQYRGEVCDAVLVKDSLVFFNTSYPDPEEAQELLIHTAWNELKAVSPLCRPAAEALLCNHLFQECSPGVLPTPMPICREYCLAVKELFCAKEWLAMEGKTHRGLYRSGMHFLPVPECSKLPSMHQDPTACTRLPYLDYKKENITTFPSITSSKPSVDIPNLPASTSSFAVSPAYSMTVIISIMSCFAVFALLTITTLYCCRRRREWKNKKRESAAVTLTTLPSELLLDRLHPNPMYQRMPLLLNPKLLSLEYPRNNIEYVRDIGEGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDNPNIVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRSMSPHTVCSLSHSDLSTRARVSSPGPPPLSCAEQLCIARQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKADGNDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGLQPYYGMAHEEVIYYVRDGNILACPENCPLELYNLMRLCWSKLPADRPSFCSIHRILQRMCERAEGTVGV", "text": "FUNCTION: Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle (PubMed:23326516). Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Single-pass type I membrane protein Note=Localizes to the postsynaptic cell membrane of the neuromuscular junction. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family."}
{"protein": "MIRIRFGMDVLLVLLLATCLLSPTHGTPLEWDFAVTLRTKIQFMDSSWQTIATAAHEFDELSALTFDESEELIYFNDLKHRNGSIFSLKRDLIAANHVVEQTIARTGNESVAGLAYDPLTTNLFWSDTEQRKIFFASIHGSATPKVLVDLSAEGGRPDGVAVDVCRRKLYWTNSNVTHPTVERIDLDGSNRTVIVNSDIDMPRGIVVDQLSDRLFWIDDLKGVFFSVESSKLDGSDRQVVLKDKHHEPLNLAVTNDAIYWTDRTTRSVWSHPKVPVIRVTTTSKPEEEDSTDATDFKDPEPVAEDCPLVRVANLSEEARGIVARTGFYQRLQKDHHCASIVRKVKQRVDEQSRKFEVSSLLDQKMKVLENERCMNNGEYKAATDLCICPTGFKGSRCEIRECHNYCVHGTCQMSESAYPKCYCQPGFTGERCEVSVCAGLCLNGGHCRASKEENEAPTCECPAKFGGARCEQNSTEICSLFCRLLKHEPEMYVPFGCHSICEELAQGNSTNIAVPQYQHLEVCLTPTVWTSSVIIILVVGIVSSLLLVAVIVHGIRRLYKPKRPRIRKTFVVRKQARTNSAGDTPLTNRPLATEQCEITIENCCNMNICETPCFDPKLVEQTLSKSSCKEDKKILIHNMEDDLY", "text": "FUNCTION: Has a role in spermatogenesis and oogenesis. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the cueball family."}
{"protein": "MNVFFMFSLLFLAALGSCADDGNPLEECFRETDYEEFLEIAKNGLSATSNPKHVVIVGAGMSGLSAAYVLANAGHQVTVLEASKRAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEVGKSAGQLYEESLQKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVRLNVRVIKIQQDVKEVTVTYQTSAKETLSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFPSGVGVIIAYGIGDDANFFQALDFKDCGDIVINDLSLIHQLPKEEIQAFCRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLTAARDVNRASE", "text": "FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:19135502). Is highly active on L-Met, L-Leu, L-Phe and L-Ile (PubMed:19135502). Exhibits diverse biological activities, such as antibacterial on both Gram-positive and Gram-negative bacteria and antiparasitic activities, as well as induction of platelet aggregation (PubMed:19135502). Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. This protein may also have activities in hemorrhage, hemolysis, edema, and apoptosis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
{"protein": "MDSITSAASVVAAGLAVGLAAIGPGIGQGSASQGAVEGIARQPEAEGKIRGTLLLSLAFMESLTIYGLVVALVLLFANPFA", "text": "FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family."}
{"protein": "MIQAETQLNAADNSGAKRLYCIKVLGGTRKRYASVGDIIVVSVKEAIPNAKVKKGDVLKAVVVRTQKEVRRPDGSYIKFDDNSAVLINQAKEPIGTRIFGPVARELRAKQFMKIISLAPEVL", "text": "FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
{"protein": "MAKKAKVQKELKRQELVAQYAEKRKELKEKGDYVALAKLPRDSAPSRLTRRCRKTGRPRGVLRDFELSRIAFRELAHKGQIPGVKKASW", "text": "FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. SIMILARITY: Belongs to the universal ribosomal protein uS14 family."}
{"protein": "MKNLPIIALDFDSTEAVDQFLDQFNEPLFVKIGMELFYQTGPQLIASIKDRGHDIFLDLKLHDIPNTVGKAMEGLSKLNIDLVNVHAAGGTEMMKQALNGLQKHNPDIKLIAVTQLTSTTETMLHKEQNIQTSIEEAVLNYATLAQSSGLDGIVCSPLEAKLVKNELGNDFLKVTPGIRPKDASSDDQKRITTPEDAKELGSTHIVVGRPITKSENPVASYHKIKESWLG", "text": "FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily."}
{"protein": "MVPEPGPVNSSTPAWGPGPPPAPGGSGWVAAALCVVIVLTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTAPRALALILGAWSLAALASFLPLLLGWHELGKARTSAPGQCRLLASLPYVLVASGVTFFLPSGAICFTYCRILLAARKQAVQVASLTTGTATAGQALETLQVPRTPRPGMESADSRRLTTKHSRKALKASLTLGILLSMFFVTWLPFFVASIAQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFVPCVHCPPEHRASPASPSMWTSHSGARPGLSLQQVLPLPLPPNSDSDSASGGTSGLQLTAQLLLPGEATRDPPPPTRAPTVVNFFVTDSVEPEIRQHPLGSPMN", "text": "FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that function as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. It has a high affinity for tricyclic psychotropic drugs (By similarity). Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity (PubMed:25078650). Is an activator of TOR signaling (PubMed:23027611). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSGVPFPSRVIGDLDYSNLLNIGQEEAIRCVLNAYPNIGLEATNLGRARRIVQRALNDNGMDGNKVMLAYTSNLISSGLRDTFACLARENRIGAVVTTAGGVEEDVIKCLGDTLVGDFALNDHALRNNGLNRVGNLLVPNDNYRNFEDFFVPLLRRLHEQQRDSRWTTKTTPSQIIAEIGAALESVRPNDCGSSLIYWCYRNDIPVFSPAFTDGSMGDMIYFYNYSRKGLVVDPVPDVRRLRQLGCKSTNVGRITCIVLGAGLPKHHLLRNVQADAVVYVTTGSDADGCESSCNVMADRANGLLSPNCDVVRVHGDATIISPLLLLRSSDGKEKVGVREDGN", "text": "FUNCTION: Required for the activation and stability of deoxyhypusine synthase DHSc. Required for cell growth and survival. SIMILARITY: Belongs to the deoxyhypusine synthase family."}
{"protein": "MKTFVLLSALVLLAFQVQADPIHKTDEETNTEEQPGEEDQAVSISFGGQEGSALHEELSKKLICYCRIRGCKRRERVFGTCRNLFLTFVFCCS", "text": "FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family."}
{"protein": "MHGLLLAGLAAALPLGVAGLPARQQSGLSPRGVDINPYRFASMAKYSEHKSTSQMVHSFSYSKDDDYVATATKLVKSTFPNMTFRTVKDHYIGTNGIGHVHFKQTAHGIDIDNADFNVNIGRDGKVFTFGNSFYEGEMPKTNPLTKRDFSDPVKALQGAIKTLKLPVKPQSAKAMPMKEAETFKFEGTSGALSDPMAKLVYIQKDGKLHLTWRVETDVGDNWLLSYVDSKETETVHNVVDYVASADYKVFAWGLNDPTEGQPTMIKDPWNTTGTGSPFTWHGDGQMDYTVTRGNNIAAQDNPSGGEQWENNYRPDSPELSFVYEYSEQMEPDQYKDFAITQLFYTTNTYHDVLYALGFTEEAGNFQMNNNGKGGEGNDFAICNAQDGSGTNNANFATPPDGQNGRMRMYTWTTAQPSRDGDLEAGIVIHEYTHGLSNRLCGGPANSNCLNELEAGGMGEGWGDFYATAIRLKQGDTHDTDYTMGEWAANMKGGIREYPYSTNMQTNPYTYADVQGMDEVHGIGTVWATILYEVLWNLIDEHGMSKNIMPKFVNGAPSDGRNLAMKLVLDGMTLMPCNPNFMQARDAIIDADQALTNGQNKCALMKAFSKRGLGANYKHGKNRVNNFDMPADC", "text": "FUNCTION: Secreted metalloproteinase probably acting as a virulence factor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M36 family."}
{"protein": "MPHNEYYNDDGELDRETCPRCGDTVLAEHEDRQHCGKCGYTEWK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS31 family."}
{"protein": "MTESSFKLAIVVSQFNRAVTEKLLNGVLQRLTELDVQANQIKTVWVPGAVEIPLLAKRLAKSKHYQAIVCLGAVIRGETDHYNYVCQQVSYGCQQVALEYEVPIIFGVLTTTTKEQAFARAGGERGNKGADWADAAVSMIKLMKEIEITDE", "text": "FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. SIMILARITY: Belongs to the DMRL synthase family."}
{"protein": "MQLNPAEISELIKSRIEGLAASSDIRNQGTVVSVTDGIVRIHGLSEVMQGEMLEFPATKDGQPSYGLALNLERDSVGAVILGEYEHISEGDTVKCTGRILEVPVGPELVGRVVNALGQPIDGKGPINAKLTDVIEKVAPGVIARQSVDQPLQTGIKSIDAMVPVGRGQRELIIGDRQTGKTAVAIDAIIAQKGQGVTCIYVAIGQKASSIKNVVRALEQAGAMEYTIVVAASASESAAMQYVSAYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQVSLLLRRPPGREAYPGDVFYLHSRLLERAARVNADYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETSLFNAGIRPAINAGISVSRVGGAAQTKLVKGLSGGIRTDLAQYRELAAFAQFASDLDEATRKQLDRGARVTELLKQPQYTPLPISLMGATLFAVNKGFMDDVDVKKVLAFESGLHQFLKTSHGALLERLEKNRAFDKEGKDEAELTQAITAFKKSFA", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MQRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTCGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDIVEAVAERLQRHHVRNVVLDTVMLAKSGDPLLSPSAIETLRVRLLPQVSLITPNLPEAAALLDAPHARTEQEMLAQGRALLAMGCEAVLMKGGHLEDAQSPDWLFTREGEQRFSAPRVNTKNTHGTGCTLSAALAALRPRHRSWGETVNEAKAWLSAALAQADTLEVGKGIGPVHHFHAWW", "text": "FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. SIMILARITY: Belongs to the ThiD family."}
{"protein": "MGICSSTCCGGRARDGLYEPVLADSEREAVADLLQYLENRGETDFFSGEPLRALSTLVFSENIDLQRSASLTFAEITERDVREVDRDTLEPILFLLQSPDIEVQRAASAALGNLAVDTENKVLIVQLGGLTPLIRQMMSPNVEVQCNAVGCITNLATHEENKAKIARSGALGPLTRLAKSRDMRVQRNATGALLNMTHSDENRQQLVNAGAIPVLVQLLSSPDVDVQYYCTTALSNIAVDASNRRKLAQSEPKLVQSLVNLMDSTSPKVQCQAALALRNLASDEKYQLDIVRANGLHPLLRLLQSSYLPLILSAVACIRNISIHPMNESPIIETNFLKPLVDLLGSTDNEEIQCHAISTLRNLAASSDRNKALVLDAGAVQKCKQLVLDVPITVQSEMTAAIAVLALSDDLKSHLLNLGVCGVLIPLTHSPSIEVQGNSAAALGNLSSKVGDYSIFVQNWTEPQGGIHGYLCRFLQSGDATFQHIAVWTLLQLFESEDKTLIGLIGKAEDIIEHIRSIANRQIEPDNEFEDEDEGEVVNLAQRCLELLGQSMSKAHIEG", "text": "FUNCTION: Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. SUBCELLULAR LOCATION: Vacuole membrane; Lipid-anchor. SIMILARITY: Belongs to the beta-catenin family."}
{"protein": "MEADGLGCAVCVLTGASRGFGRALAPQLARLLSPGSVMLVSARSESMLRQLKEELGAQQPDLKVVLAAADLGTEAGVQRLLSAVRELPRPEGLQRLLLINNAATLGDVSKGFLNVNDLAEVNNYWALNLTSMLCLTSGTLNAFQDSPGLSKTVVNISSLCALQPYKGWGLYCAGKAARDMLYQVLAAEEPSVRVLSYAPGPLDNDMQQLARETSKDPELRSKLQKLKSDGALVDCGTSAQKLLGLLQKDTFQSGAHVDFYD", "text": "FUNCTION: Catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sepiapterin reductase family."}
{"protein": "MKLVVQRVTEASVTVEGAVAGRIGPGIMALVGITHEDTEEDAAYLADKIVNLRIFDDESGKMNLSLLDTGGEILSVSQFTLYGETKKGRRPNFMNAAKPDQAVLLYEKWNELLREKGVKVETGIFGAMMDVQLTNSGPITLIMDSKQ", "text": "FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DTD family."}
{"protein": "MKVQRSTFLAVTGKSNLHHFHSSSQRIPITSEIDSREFVSKLLDRKWGLQCPASPIQQISVSSVKGIDKFSFLNNTRPHLGDEMSKSKQGSSFYILRDDLLHPLVNGNKARKLDALLPLVEDHKVTDLVTCGGCQSAHTAAVAVSCAERGLRSHLLLRGEQPDVLTGYNLVSTMYGNVQYVPRSRYANREEMLRTYADLVAGEDGTVLWAKDIVEGRDTMNVAKMDDFSSMKTSRRKVLIVNEGAGDALALLGMFRLVQHLSQDHLLGKKRPVKFVVDAGTGTTAVGLGVAAMSLGLPWEINAVMLADTLKNYKRHEDHLIAEFSRQFPGSVFCSGLDMNQMIKWIDRQHPRKFGKVLEGEVEMCRKIAQETGVLVDPMYTLAAWETATELVQDEKSSIVVMLHTGGTLGMFGLAQRYKTCFTNLKD", "text": "FUNCTION: Catalyzes the production of hydrogen sulfide (H2S) from cysteine. Can accept both D-cysteine and L-cysteine as substrate. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase family."}
{"protein": "MMLPRCFVTVLLMSSVLYIGGETSSEVLGPVVSTEAGSFQGMELTTHGERVIYAFLGIPYAKPPTGLLRFKKPQPADFIQGTYKATEKPPSCFQLDSDLQLPWADPDSPMKEDCLFLNLWTPASLSTEEEELKSVMVWIHGGGYTSGSSALDVYDGQTLSSSGDVVVVTMNYRLDAFGFLNSLTEDAPGNMALYDQLLALQWVHTNIKYFGGDPNKVTLFGESVGAFATSFLALSPLTKGLFQKIMLESGSAYNKLTVNSIDQAKNNNQLATLVGCANETFTLISNPEEVVACMREVAPAKFTQTYYKELGSEREKINFIFWPHFGDDILPTRTAELIKEKNLTALFAGVNSVEGSALSVFFFPEVYQMFVESNLTLTKAYATILMNEFFKVFNFQDSAKAIEFYLGDVEDDDEEGIRSALFGVVGDYIITCPTIYLADKYSERGANVQFYRFDRRPSTSQWPPEWMGAAHNDEIQFVFGMPVRYPEKYTEEERTLSEYMTRTWTNFVKSEDLKLKNGSQWPSYSLSEPQFATLQTNEQIIGSGQRKAECDFWRPYFDI", "text": "FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "MKPFVAIIFCFLILGVDSQRWFQFMKEAGQGTRDMWRAYTDMREANWKNSDKYFHARGNYDAAQRGPGGAWAAKVISDAREGFKRITGRGIEDSRADQFANEWGRSGKDPNFFRPPGLPSKY", "text": "FUNCTION: Major acute phase protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SAA family."}
{"protein": "MSQLEKIYGVHAVEALLRHHPKRVKHIWLAEGRNDPRVQTLVALASENRVTIGQAERREMDAWVEGVHQGVVADVSPSQVWGEAMLDELLDRSEGPPLLLVLDGVTDPHNLGACLRTADAAGALAVIVPKDKSATLTPAVRKVACGAAEVIPLVAVTNLARTLEKLQQRGLWVVGTAGEAEVELYQQDLTGPTIIIMGAEGKGMRRLTREHCDYLVRLPMAGSVSSLNVSVATGVCLFEALRQRSAKRKP", "text": "FUNCTION: Specifically methylates the ribose of guanosine 2251 in 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. RlmB subfamily."}
{"protein": "MVSTTTFLMLTSLATLTSARSHLTVTIGSNCTLKGPQGGHVFWWRIYDNGWFTKPCDQPGRFFCNGRDLTIINVTANDKGFYYGTDYKSSLDYNIIVLPSTTPPPRTTTFSSSSVANNTISNPTFAALLKRTVNNSTTSHTTISTSTISIIAAVTIGISILVFTITYYACCYRKDKHKGDPLLRFDI", "text": "SIMILARITY: Belongs to the adenoviridae E3_20 family."}
{"protein": "MAGTPNFDRRSFLRLAAAAGLTGMAGVTSATPGRSPGPKKDEILVGVTSTADSPRKAVADAVPGNAEIVHENETLSYAAVKFPSKAPKQARENFISAITKRDEVKYAEKNATHEALYTANDPKYGSQYAPQQVNADSAWDTTLGSSSVKIAVVDQGVKYDHPDLSSQFGSNKGRDFVDNDGDPYPDLLSDEYHGTHVAGIAAGTTDNNEGIGGISNSTLLSGRALSESGSGSTSDIADAIEWAADQGADVINLSLGGGGYSSTMKNAVSYATQQGSLVVAAAGNDGRQSVSYPAAYSECVAVSALDPDETLASYSNYGSEIDLAAPGTNVLSCWTTSTEYNEISGTSMATPVVSGVAGLALAVHNLSPADLRNHLKNTAVDIGLSSTKQGSGRVDAANAVTTDPGDGGGGGGGGSKETTYDGTLSSSSDSNCVSHSWNYSSPSQVVIDLSGPSSADFDLYATEGSGTCPTTRSYDYRSWSYDSTEQIVIDNPDTSADLGILVDSYSGSGSYTVTITEKE", "text": "FUNCTION: Probable secreted halophilic serine protease showing proteolytic activity toward the protease general substrate azocasein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "KRSLRDLGILVNQIIPEGGSLKCLKDLPRAWFNVVPYREVGLMTAIFLEKEYGMPYVSVTPMGILDTAEFVRQMERLVNAWASVLPEKQANYSSYIKDQTNFV", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ChlB/BchB/BchZ family."}
{"protein": "MESESSRRMGNACIPLKRIAYFLCLFSVVLLTEGKKPAKPKCPAVCTCSKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNAFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSPKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIDTQLYVIVAQLFGGSHIYKRDGFANKFIKIQDIEVLKIRKPNDIETFKIEDNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIARPPLALRTPHLILSSSSQRPVIYQWSKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRFIGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKFVKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQIYKHVIVDLSA", "text": "FUNCTION: Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors. Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway (By similarity). SUBCELLULAR LOCATION: Secreted Synapse Cytoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Endoplasmic reticulum. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm Golgi apparatus Secreted."}
{"protein": "MNEAAKTLDGWYCLHDFRTINWAELKTLSTEERQQIINEFLDLMEKWNDTEAQGEGSHAVYTIVGQKADVMLMILRPSMEELNEIETAFNKSRFAEFTVPAYSYVSVVELSNYMAGDSDDDPYQNPHVRARLYPQLPKAKHVCFYPMDKRRQGDDNWYMLPMDQRRELMKSHGMIGRSYAGKVKQIITGSVGFDDWEWGVTLFADDVLQFKKLVYEMRFDEVSARYGEFGSFFVGNLLTAEGIPSYFYV", "text": "FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway. The reaction occurs in a stepwise manner with a three-propionate intermediate. SIMILARITY: Belongs to the ChdC family. Type 1 subfamily."}
{"protein": "MVNMETCAMDCCVLKALLAERAHKCLILDCRSFFSFSSCSIVGSSNVRLSTIVKRRAKGSMGLEHIVPNEEQRCRLVAGMYEAVVLLDERTSELDMLRKDSTMMLAVNALCRDSRGSSIYFLKGGYETFSAQCPEFCTKNSPPVGLSLPLCANNVPGSADSNCTPCGTPLYDQGGPVEILPFLYLGSAYHASRKDMLDTLGITALINVSANCPNHFEGHFQYKSIPVEDSHKADISSWFNEAIDFIDSVKNSGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPSCSAEAGSPTISVLDRGTSTTTVFNFPVSIPVHSGANSLSYLQNPITTSPSC", "text": "FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-188' and 'Tyr-190', regulating its activity during the meiotic cell cycle. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "MAIFEWRHRRRPFDGGGTRRRRFFSPLYSRNFKRTILFAVIFLAIFPPLYFHFKLRRIRQIVAQKCDWLHHPPLVCAHGGDSTLAFPNTMDAYSFAIRSRVDCIEVDVSRSSDGVLFALHNRDLQRIARNSSVQVGDLSMKQIKELDVSEIVKGTLGSSRIPTLEEALALISNSVRKVILDAKVGPPMYEKGLAQDILSIIERAQCNNCIVWAKSDTLARDIIRRAPDTMVGYIVMVDPLTGARNSLLRMKGARVVGVYHPLIDEELVRVVRRRNKEVYAWTVDDADPMKRMLHLGVDAVVTSDPSMFQGLMEDLRTECLEEGFSIRT", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
{"protein": "MESGIDLQGQFISALQSLGLSHDLAKLLWLPLPMLMMLIVATVGVLVAVWLERKISAAVQQRIGPEYIGPLGILAPLADGLKLIFKEDVLPANSDRWLFTLGPAVVVIPVFLSYIIVPFGQNLLISNLAMGVFLWIALSSIAPIGLLMAGYASNNKYSLLGGLRAAAQSISYEIPLALAVLAVAMMSNGLGTVEIVEQQSQYGILSWNVWRQPIGFLVFWIAALAECERLPFDLPEAEEELVAGYQTEYAGMKFALFYLGAYVNLVLSALLVSVLYFGGWSFPIPLETIANLLGVSETNPFLQIAFAVLGITMTLIKAYFFVFLAILLRWTVPRVRIDQLLDLGWKFLLPVGLVNLLLTAGLKLAFPVAFGG", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MATNIGMMDSAYFVGRSEILAWINSTLQLNLSKVEEACSGAVHCQLMDSVHPGTVPMHKVNFDAKSEYEMIQNYKVLQDVFNKLKITKHIEVSKLVKGRPLDNLEFMQWMKKYCDSVNGGQHNYHALERREASKGGKEATKRAAATQQSGKSSSSSAPPRPSSSNGTRKHEPQSNNTGTHHSSTGNHHHSSKPSAKQSKPVPAYDEKITELKLYIDSLEKERDFYFSKLRDVEILCQNPDTEHLPLVGSIKRILYAADGEDVGAAETQTLSPIAEGSEERRNSVTESQKRKLIVNLDVDVAAITTLSPRQRLSDASDVKCSGSSPLLTC", "text": "FUNCTION: Plant-specific EB1 subtype that functions preferentially at early stages of plant mitosis by regulating spindle positioning and chromosome segregation. Accumulates in the prophase nucleus and is required to maintain spindle bipolarity during premetaphase and/or metaphase and for efficient segregation of chromosomes at anaphase. May play a role in the dynamics of microtubule network in elongating pollen tubes. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=During mitosis, accumulates in the prophase nucleus, and after the nuclear envelope disintegration is associated with whole spindle microtubules, plus end of microtubules, phragmoplast and finally is actively recruited to the nucleus. Localizes in the microtubule network in elongating pollen tubes. SIMILARITY: Belongs to the MAPRE family."}
{"protein": "MRMDKLTSRFQQALADAQSLAVGRDHNIIEPVHVLAALLDQSGGSTRPLLSQAGVNVPLLRERLGEALDTLPKVSGQEGNLSIGNDLNRLLNQTDKLAQQHGDAFIASEWFVLAAADDASPLGVALRAAGGDKKKIEAAIDKLRGGETVQSENAEEQRQALEKYTIDLTARAESGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLRGKRVLSLDMGALIAGAKFRGEFEERLKAVLSDLSKNEGQIILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEKDAALERRFQKVFVGEPTVEDTIAILRGLKERYAVHHGVEITDPAIVAAATLSNRYITDRQLPDKAIDLMDEAASRIRMEIDSKPEELDRLERRLIQLKIQREMLKKEKDDASRQRLADLETDIDKLEREFYDLNELWKSEKAALQGTTKVKEQIEHAKLELEAAQRRQDYAKMSEIQYGVLPQLEKQMALANEVEHHDFKLVQDRVTAEEIAEVVSRWTGIPVNKMLEGERDKLLRMEDELHHRVVGQNEAIKVVSDAVRRSRAGLSDPNRPSGSFLFLGPTGVGKTELCKALADFLFDSTEAMIRIDMSEFMEKHSVARLIGAPPGYVGYEEGGYLTEAVRRRPYSLILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVIVMTSNLGSHQIQELSGDDSAEAYTQMKAAVMGVVQAHFRPEFINRLDDIVVFHPLDKAQIKSIARIQLQGLEKRLAERGLKLDLDDAALEVLGSVGFDPVYGARPLKRAIQSQVENPLAQQILSGQYLSGDSVRVRADGGRLVFTKD", "text": "FUNCTION: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ClpA/ClpB family."}
{"protein": "MLKLLLGDPNTRKLKRYQPIVEEINFLEEEISKLTDDELRQETHNLKSQISSESDIKQQKELLDESLPKAFAIVREASKRVLDMRHFDVQLIGGMVLHECQIAEMKTGEGKTLVATLPCYLNALTGKGVHVVTVNDYLARRDAEWMGQVHRFLGLSVGLIQQDMSPVQRKKNYDCDITYATNSELGFDYLRDNMSTDINEVVQRPFNYCVIDEVDSILIDEARTPLIISGQVERPQEKYQKASELALALVKAKEIGKDGIDPEGDYEVDEKQRSCILTDQGFAKCEEYLAVSDLYNPKDPWAHYITNALKAKELFIKDVNYIIKNNEAVIVDEFTGRVMPGRRWSDGQHQAIEAKESLKIQPETQTLASITYQNFFLLYPGLAGMTGTAKTEEVEFEKTYKLESTVIPTNQIRKREDLPDQVFKTEIGKWKAVARETAQIHRAGRPVLVGTTSVEKSELLSSLLAEEKIPHNLLNAKPENVEREAEIVAQAGRAGAVTIATNMAGRGTDIILGGNSDYMARLKLKEILIPLLVKPNNEHKPPIPKQRSSKSKGGFSSKVGSNLTKNIPDYSTSLFPCKLDEEIQKKLSVLSDELVKNWGDRQLSVLDLDDRIATAAEKAPTEDKMIKLLRESLSRVKDEYEKVLTHEEKKVREVGGLHVIGTERHESRRVDNQLRGRAGRQGDFGSTRFFLSLEDNLLRIFGGERVANLMNAFRVDEDMPIESGMLTRSLESAQKKVETYYYDIRKQVFEYDEVMNNQRKAVYSERLRVLQGTDLKRQVIGYGERTMYEIVEAYINPDLPPEEWDIAQLISKVKEFIYLLDDLKADDVKLLSIEELKNYLQEQLRTAYDLKESQIEQIRPGLMREAERFFILQQIDNLWREHLQSMDSLRESVGLRGYGQKDPLIEYKNEGYDMFLEMMTNMRRNVIYSMFMFQPKTDKDDKN", "text": "FUNCTION: Probably participates in protein translocation into and across both the cytoplasmic and thylakoid membranes in cyanobacterial cells. FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm. SIMILARITY: Belongs to the SecA family."}
{"protein": "MINGWTGNILRINLTTGAIS", "text": "FUNCTION: Oxidoreductase with an extremely broad substrate specificity that can reduce reversibly 2-oxocarboxylates to (2R)- hydroxycarboxylates. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the AOR/FOR family."}
{"protein": "MPRLEDWEIKKYWEIFQGLNPVDNKITGDKASTVLKNSRLKDDQLSQIWDLSDIDSDGKLDFEEFCITMRLIFDLVNGNQQSLPSELPSWLVPASKAHLIQANMAVTTGSNNYQTNNNTITDDDDEDESLSDDFDWYISPTDKSIYETIYDSNSDSYGRVKFDSLTGLYQTLSKVPRSDISSAWNLVNPKSFEAIDKDQVLVFLHILNQRENGKRIPRYVPASLRATFSKDTPSYDLNQAPSKPINSAPVNNKNSFANSYLNKIGHANNATNEKGTDFSATEGTDWEEVRLRRELANLEDLLSKASQKDHTSNKSDDSESAMIKYEYEQLLKYKTNILSELESGSNHNNSKDLGDAKNDIELIENQVTILEEFLNERQNELNKTNEEIRALRT", "text": "FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Endosome membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, actin patch Note=Cytoplasmic and cortical actin patches. SIMILARITY: Belongs to the END3 family."}
{"protein": "MASRSLGGLSGIRGGGGGGGKKSLSARNAAVERRNLITVCRFSVKTLIDRSCFETIDDSSPEFNNFAAILEQILSHRLKGQVTWFGYESPRSFWDYIRVACRKVSQNCICSIENMENVSSSRAKGRAWIRVALMEKHLSEYISTALRDFKTTRRFYEDGAIVLGEEANMLAGMLLGLNAIDFSFCLKGEGLDGSFPAVIDYTPYLKYIQGSDSISSDEEELRTLGSSGSESSTPENVGPPFLMDENSWFNKCKRVKQKYQLTLEQKGYLEELLRLRENQLSESVSQNKILLQRIEDSDLAHKLEKEQLEYIIVELQDQLTVLKNNDLRSRQELTAHLTNQWPSPGALDVNAVALDTLLYRKHNKQWYEKSYQSLDQLSAEVSLSQTSLDPGQSQEGDGKQDTLNVMSEGKEDTPSLLGLCGSLTSVASYKSLTSLKSNDYLASPTTEMTSPGLTPS", "text": "SIMILARITY: Belongs to the RUNDC3 family."}
{"protein": "MPVDTKRIRGPEESQSPLLFLSPDKAPKAPSSRQGVRGNGDVRPVFARCGLVSQAKGSAYIEAGNTKIICSVYGPKETERRDETDMKTGRLVCDFRLAPFSCVKRGAWIQGSEERDLSATLMESLRPGVCLHRYPRSQIDVNVMVLENDGSVLAHAVTCASMALADAGIEMYDIVLGCTLRQSGNACLVDPSYAEECGSWQEGYGDNQGCVTLALLPNLNQVSGLNADGEMREDTLTEAMRTCMDGCHKLYPVVQQALTRAVKKKAPPPEK", "text": "FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus. SIMILARITY: Belongs to the RNase PH family."}
{"protein": "MGDDRPFVCNAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKNCEEVGLFNELASSFEHEFKKAADEDEKKAAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSPPLKEKEVTPKPVLISTPTPTIVRPGSLPLHLGYDPLHPTLPSPTSVITQAPPSNRQMGSPTGSLPLVMHLANGQTMPVLPGPPVQMPSVISLARPVSMVPNIPGIPGPPVNSSGSISPSGHPIPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQSQILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDERRQRFLERNRAAASRCRQKRKLWVSSLEKKAEELTSQNIQLSNEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQGYLESPKESSEPTGSPAPVIQHSSATAPSNGLSVRSAAEAVATSVLTQMASQRTELSMPIQSHVIMTPQSQSAGR", "text": "FUNCTION: [Isoform 5]: Acts as a negative regulator, inhibiting both ATF2 and ATF7 transcriptional activities. It may exert these effects by sequestrating in the cytoplasm the Thr-53 phosphorylating kinase, preventing activation. FUNCTION: Stress-responsive chromatin regulator that plays a role in various biological processes including innate immunological memory, adipocyte differentiation or telomerase regulation (PubMed:29490055). In absence of stress, contributes to the formation of heterochromatin and heterochromatin-like structure by recruiting histone H3K9 tri- and di-methyltransferases thus silencing the transcription of target genes such as STAT1 in adipocytes, or genes involved in innate immunity in macrophages and adipocytes (By similarity). Stress induces ATF7 phosphorylation that disrupts interactions with histone methyltransferase and enhances the association with coactivators containing histone acetyltransferase and/or histone demethylase, leading to disruption of the heterochromatin-like structure and subsequently transcriptional activation (By similarity). In response to TNF-alpha, which is induced by various stresses, phosphorylated ATF7 and telomerase are released from telomeres leading to telomere shortening (PubMed:29490055). Also plays a role in maintaining epithelial regenerative capacity and protecting against cell death during intestinal epithelial damage and repair (By similarity). FUNCTION: [Isoform 4]: Acts as a dominant repressor of the E- selectin/NF-ELAM1/delta-A promoter. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Chromosome, telomere Note=Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear periphery. SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MFDATTILAYKGKNKAVIGGDGQVTFGNTVLKGNATKIRTLYKDQILAGFAGSTADAFNLFDMFEGHLEACKGDLLKSVIAFSKEWRKDKVLRRLEAMMIVLNKEKIFILSGNGDVVEPEDGAIASIGSGGNFAISAARALAKHSSLDEEELVKESLMIAGELCIYTNQNIKILKLED", "text": "FUNCTION: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily."}
{"protein": "MDGIVPDIAVGTKRGSDELFSTCVTNGPFIMSSNSASAANGNDSKKFKGDSRSAGVPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGAPGIISASPYAGAGFPPTFAIPQAAGLSVPNVHGALAPLAIPSAAAAAAAAGRIAIPGLAGAGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI", "text": "FUNCTION: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre- mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre- mRNA. Represses the splicing of MAPT/Tau exon 10 (PubMed:15009664). Binds to polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon inclusion of CFTR exon 9 (PubMed:14966131). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to a polypyrimidine tract flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). In case of infection by picornaviruses, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES- mediated translation (PubMed:21518806). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MITITDAAQSHFAKLLANQEEGTQIRVFVINPGTPTAECGVSYCPPDAVEATDTELKFEQLSAYIDELSKPYLEDAEIDFVTDQLGSQLTLKAPNAKMRKVDDNAPLMERVEYVLQSQINPQLAGHGGRVTLMEITPDALAILQFGGGCNGCSMVDVTLKEGIEKELLQKFPELKGVRDLTEHQRGEHSYY", "text": "FUNCTION: Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. SIMILARITY: Belongs to the NfuA family."}
{"protein": "MTKSELIERIVTHQGLLSSKDVELAIKTMLEQMSQCLATGDRIEIRGFGSFSLHYRAPRVGRNPKTGQSVELEGKFVPHFKPGKELRDRVNEEEHEHP", "text": "FUNCTION: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. SIMILARITY: Belongs to the bacterial histone-like protein family."}
{"protein": "MATALGFRCLFRTRPAPLCRHVDRLWRNPRRGHRLSPADDELYQRTRISLLQSEFPQAVYIDSYSSRGFTICGNRVFGPCVLLPQTVVQWNVGSHQDITEESFSLFWMLEPRIEIVVVGTGNKTERLHPQVLQAMRQRGIAVEVQDTPNACATFNFLCHEGRVTGAALIPPPGETALASLGQASE", "text": "FUNCTION: Essential factor for the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). SUBCELLULAR LOCATION: Nucleus Mitochondrion inner membrane."}
{"protein": "MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVGFTDSERLIGDAAKNQVAMNPINTVFDAKRLIGRRFSDASVQSDMKLWPFKVIPGPGDKPMIVVNYKGEEKQFSAEEISSMVLIKMKEIAEAFLGTTVKNAVVTVPAYSNDSQRQATKDAGVISGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLYEGIDFYSTITRARFEELNMDLFRKCMEPVEKCLRDAKMDKSTVHDVVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIPRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERTRTRDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGTLNVSAEDKTTGQKNKITITNDKGRLSKEEIEKMVQEAEKYKSEDEEHKKKVEAKNALENYAYNMRNTIKDEKIASKLSADDRTKIEDAIEQAIQWLDGNQLAEAEEFEDKMKELESLCNPIIAKMYQGAGGDMDDEGPAPSGGGAGPKIEEVD", "text": "SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MHREDDSTSTGRREERLSTGKGDSLQPGPDQRIFQTALYRPQRHGLILFPQRLYGNCLAPLAYSNYVAPRELHSSIHAEGRTLSVRLIMLFVNTSKRSRTLPPVGSTVMRILVNLCQLLSAEFQLLQGSQRLIFKLCYRTCPDQRRGDTRVAQCPGDSHLSQCLTATFRNGVQRPDAPQQLFVLCTGLQGAALIRPRPFGDSVQIAGGQQSLSQRRKDNAAGSDLAKGIEQAIFDPAIEHVVIGLMNEKRNPLFLQDRGSLLRQFRRIAGNPHIKRLALTVQMRERSHRLFQRRGGVHTVRIEDVDIVEPHPLQRPGRGWRSGICDLPPMPPYGPGHMSQPAFEEMIISSR", "text": "FUNCTION: Confers an increase in glyphosate resistance when expressed in E.coli."}
{"protein": "MDLSRSAAWSALVSHRQEVEQLHMRDMFMSDHDRFKHFSIRWNGLLLDYSKNRINSRTMGLLVELARQANLIEARDGMFAGEKINFTENRAVLHTALRRQPGYTLNVDGLDVPAEVDSVLRQMKAFTDKVVGGEWKGYTGKRITDVVNIGIGGSDLGPCMVTEALRPFADGAIAVHFVSNIDGTHVSEVLKRVDAETTLFVIASKTFTTQETLTNSMTAREWFLSRAIDPAHIALHFAAVSTNRTKVVEFGIDPENMFRFWDWVGGRYSLWSAIGLSIALYLGFEAFQELLRGARAMDEHFQEAPLEENIPVILALLGVWYNNFFDVPSHAVIPYDQYLHRLPAYLQQLDMESNGKRVDRLGNTVEYPTGPIIWGEPGTNSQHAFFQLLHQGTGFIPADFILPLKTQNPIGEHHDILVANCFAQTEALMRGKSASEASEELAAAGVDEETMQMLVAHKVFPGNRPTNTLLLDEINPFTLGSLIAMYEHKVFVQGVIWQVNSFDQWGVELGKQLAKAILPELQSQKESDAHDASTNALINSYRSYREGQKVG", "text": "FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MSFSPLIRQLIDALRTLPGVGQKTAQRMALQLLERDRSGGLRLAQALSQAMEGVGHCRQCRTLTEDELCPQCADPRRDDTLLCVVEGPMDVYAVEQTGYRGRYFVLKGHLSPLDGLGPEAIGIPQLLARIEEQGSFSEVILATNPTVEGEATAHYIAQLLTNKGLITSRIAHGVPLGGELELVDGGTLAHSFAGRKPIAL", "text": "FUNCTION: May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. SIMILARITY: Belongs to the RecR family."}
{"protein": "MSYFTQEQKTQWKDNGFVHLKGFLNEALAQDIKDWTQELYEWEEAPGKWMKYFETSSDTGERLLCRVENFIDYHKGIKGFLCGEMIYGMVSELMGEQAVLFKEKINFKYPGGAGFAYHQDAPAFTSFGQKYHITMMVSVDASNEENGCLRMAHGFSEEKTLEQEPDGTVCKKLAAKLDWRPLETGPGDLVLFNSYVPHYSEANTSDRSRRAMFITYNRLSEGEKRLDYFKDKREKFPPEAERIEGKDYSSAESLYNLGNPIK", "text": "FUNCTION: Involved in the degradation of the organophosphonate 2- aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the hydroxylation of 2-aminoethylphosphonic acid to yield (2-amino-1- hydroxyethyl)phosphonic acid (PubMed:22564006). SIMILARITY: Belongs to the PhyH family."}
{"protein": "YYTPEYKTKDTDILAAFRMTPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVAGEENQYIAYVAYPLDLFEEGSVTNMLTSIVGNVFGFKALRALRLEDLRIPPAYSKTFMGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEALFKSQAETGEIKGHYLNATAGTCEEMMKRAVFARELGAPIVMHDYLTGGFTANTSLAFYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSMPGVFPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRD", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
{"protein": "MAVDRPQNLQDTFLNFVRKNKVPLTIFLVNGVKLQGVVTWFDNFCVLLRRDGHSQLVYKHAISTIMPGAPIQMFEPGDEAGHAG", "text": "FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. SIMILARITY: Belongs to the Hfq family."}
{"protein": "MKESTRTSTPSSGAKPKGDREICLRPSSSVFLGDQQLYFTQEYLATNSLNMKYVVYFAACQFSGPIAVIYAAPKSWFIWIRTISGRILKRDLPCTDPVFIDWTRAHCLLVLSKNGRAQVLSSIGEKVSEVFFDNQVSDVHECRTFATSRGDSGIAVMDVDGQVAVVNSVSEPVIWSMRPPYSELPTAWTAFQPHSQLTHILLIFEAVFLMGCQGESLQVQNHASVWVDSSTKYVKCVVDDARSRIAMMTENGKIQIVSIDLSTCFCTVEVTEHEIGKCINFGWVGNSVVFVQMSSSLTVFVNVSARRKPGDEVRFMSIKMTANARISVEPDGIRLFESTRVEFVEAASREKIAVLNRSLNEDGAYLYKAAQEMEQGTGHNSFAASTVIQDMYKAIDDCISTACDTWQPEEQKLLLKAARFGMAYTNTTPDTTKLMRAIKEIRVLNELRMVRTGIPLTHRQYRIIGDTCIINRLIDMGSYSVAIKVAQWLGGENCESVDRVLLEWVRRSISKVSRSNMKMDQPALEALDEKISAKLLQFPHVSMADAARRAIEAKLPELARLFIRRETDDESHVAVLLQLNDVSAALTKAAASQRPQLIHQVVRHLMTSESRSSYELAISRIPLAQCLYQDLVRQEGETRGISSRQMLALLEQASDFERQTLFHFDVAEIERNPSERLNALRRAKDAAKSMGDKAIEEILNDVSAFAPLQIQRGQADMSVRDTIIEIADDTAKVAQLKQQARLNDKQVLLWTIEGLAKKGKMEQLFDLAQKRSPIGYAPFVKACVRYKRNEEVNKYFAKANGYSDLVAANLAKKNYVDAAKLAYDRRDREVLHAIHMKSHDDPVQCPRVKQLLNSMDQA", "text": "FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the rab-5-to-rab-7 endosome conversion probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. Within the HOPS complex, contributes to the normal development of gut granules in the adult intestine. The CORVET complex is proposed to function as a rab-5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for recruitment of vps-33.1 to the HOPS complex. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with vps-33.1 but not vps-33.2. SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Note=Cytoplasmic, peripheral membrane protein associated with late endosomes/lysosomes. SIMILARITY: Belongs to the VPS16 family."}
{"protein": "MKQLLDFLPLIVFFVVYKLHDIFWATAALIVATALAVIYSWYKYRKVEKMTLVTFVLVAVFGGLTIYFHNAEFIKWKVTIIYALFAGALLIGQWVMKKPLIQSMLGKEITLPAHAWSRLNIAWALFFIFCGLLNIYVAFWLPEAVWMNFKVFGIPGLTLVFTLLSGVYIYRHMPQEEK", "text": "FUNCTION: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the YciB family."}
{"protein": "MEDSEGTDGTEEDGCRAGGWFHVEAIITHGQRQVSSDEDEDCTETGEDVDFIDNRVPGDGQEIPLQLYTQQIAQDDEATVQALKRKFVASPLSACSCIENDLSPRLDAISLNRKSEKAKRRLFETEPPDSGYGNTQMVVGTPEEVTGDENSEGGRPVEDKEEERQGGDGEADLTVQTPQSGTDAAGSVLTLLRSSNLKATLLSKFKELFGVGYYELVRQFKSSKTACADWVVCAFGVYYAVAEGIKQLIQPHTQYAHIQVLTCSWGMVVFMLLRYNCAKNRDTVSKNMSMLLNIPEKHMLIEPPKLRSTPAALYWYKTAMGNGSEVYGETPEWIVRQTLVGHSMEDEQFRLSVMVQFAYDHDIVEESVLAFEYAQLADVDANAAAFLNSNCQAKYVKDAVTMCRHYKRAERAQMSMSQWITFRGNKVLEEGDWKPIVKFLRHQGVEFVSFLAAFKLFLKGVPKKNCIVFYGPADTGKSYFCMSLLQFLGGAVISYANSSSHFWLQPLSDSKIGLLDDATPQCWSYIDTYLRNLLDGNPVSIDRKHKTLLQLKCPPLMITTNINPLEEDRWKYLRSRLTLFTFNNPFPFASPGEPLYPINNANWKCFFQRSWSRLDLNSPEEQDDNGNTSEPFRCVPGDVARTL", "text": "FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1- E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the papillomaviridae E1 protein family."}
{"protein": "MVNMEASMFLTFAGLVLLFVVCYASESEEKEFPKEMLSSIFAVDNDFKQEERDCAGYMRECKEKLCCSGYVCSSGWKWCVLPAPWRR", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 51 (Hntx-8) subfamily. Hntx-8 sub-subfamily."}
{"protein": "MEVTNGLNLKDTELRLGLPGAQEEQQLELSCVRSNNKRKNNDSTEESAPPPAKTQIVGWPPVRSNRKNNNNKNVSYVKVSMDGAPYLRKIDLKMYKNYPELLKALENMFKFTVGEYSEREGYKGSGFVPTYEDKDGDWMLVGDVPWDMFSSSCQKLRIMKGSEAPTAL", "text": "FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin- responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Aux/IAA family."}
{"protein": "MPRTSLLTLACALATGASAFSYGAAIPQSTQEKQFSQEFRDGYSILKHYGGNGPYSERVSYGIARDPPTSCEVDQVIMVKRHGERYPSPSAGKDIEEALAKVYSINTTEYKGDLAFLNDWTYYVPNECYYNAETTSGPYAGLLDAYNHGNDYKARYGHLWNGETVVPFFSSGYGRVIETARKFGEGFFGYNYSTNAALNIISESEVMGADSLTPTCDTDNDQTTCDNLTYQLPQFKVAAARLNSQNPGMNLTASDVYNLMVMASFELNARPFSNWINAFTQDEWVSFGYVEDLNYYYCAGPGDKNMAAVGAVYANASLTLLNQGPKEAGSLFFNFAHDTNITPILAALGVLIPNEDLPLDRVAFGNPYSIGNIVPMGGHLTIERLSCQATALSDEGTYVRLVLNEAVLPFNDCTSGPGYSCPLANYTSILNKNLPDYTTTCNVSASYPQYLSFWWNYNTTTELNYRSSPIACQEGDAMD", "text": "FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from phytate. SIMILARITY: Belongs to the histidine acid phosphatase family."}
{"protein": "MAPDRALAAQARPEQEFFCFRVGDLRLGVPSENVLEVLRAGLLTPLPRTPSFIMGVTGHRGEVLPVLDLLRFLSKGEARIGPRTRLFVGVTGSYVAGVVADTVLGLRRIPVADILPPPLGGDAAAEHLLGVVQASGNQEAINLLNFSKLLQTARQRAVAR", "text": "FUNCTION: Necessary for proper aggregation of cells to form fruiting bodies. FRZ genes define a system of signal transduction analogous to the enterobacterial chemotaxis systems."}
{"protein": "MLGRKLGKKTAQAKGRGAAAAKELGLFVDFSPEDMMLGIPDDPDDGDLEAELAALTGVKAVSKPKPKGKAPLPMEEIEKMAQDCMTDMTGEDDDDDLEEDEELLAELQDVVGEEEEVEQSQPSDTEESEPSASETQEHTEPEQQVNSSVAEIQHNLQVPAGGMLQVLEERIGNYKEAISNAKLSNESAKARRYERGLKTLESMLSAARQGRTVIEADIPPPVACGKPAVSPTTDVPTTDTSKQGLGDLNDVPMETTEAVTNLEKPEDPVSKATTNDGGAVEKTHVASENDTDSKTVLLLRQRDYKLAALKAKQTGDIEKAKEYMKISKKFSVVLEALESGQPVDLSNMPAAPEDHEAMVTESKIIAHPTPAPPVSNILNTQGSSVGSLLQALQQRMEKYKSAAQQAKSSGDDRKARMHERIAKQYQDTIRAQKAGRQVNLAELPVPPGFPPLPGMEQTEEEGSVEKALEAAQKLAKTAGEDVDDDEDECQAKPPGHPKPTQLVKPLVMPAISDNEERLLPIKAPVKVASEETFPPAVQEQLEFLEHRKKQYRKAALQAKQKNDLEQAKQHMRVAHTLQVSIDQVKSGKLVDISKVPSLPDDEESDFVVVEHEDIKSPQNSEDVYNMLMKLLHEQHEKCIRYSKQFTQMGNVAETTRFENMAEDCKKNCEILQLSQAQGLDPPPYHFEDKTLKIVRVFSELSSTEMLLIIVRGINLPAPSGVAPNDLDAYVKFEFPYPSSEQPQKNKTLVIKNTNSPEYEQSFKLNINRNHRGFKRVIQTKGIKFEIFHKGFFLVRSDKQVGSASVKLDKLETQCEIREIVEVFDGRKPTGGKLEIKVRLRDPLNGQDLQVVTEKWLVMGHVPRK", "text": "SIMILARITY: Belongs to the CC2D1 family."}
{"protein": "MAAVDSDIEPLPRGGFRCCLCHITTANQPSLDAHLGGRKHRHLVELRATRKAQGLRSVFVSGFPRDVDSTQLSEYFQAFGPVASVVMDKDKGVFAIVEMGDLGAREAVLSQPQHSLGGRRLRVRPREQIEFQSPASRSPKRVAPDSHQLIKALAEAPDVEAQMVKLVGLRELSEAERQLRSLVVALMQEVFAEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLDEPQPAPKAPESPSLDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFEAPSSSLAPRTPDSALASETLASPRSLPPASPLQEDQGDGDQGKAVELAEALKGEKAEGGAMLELVGSILRGCVPGVYRVQTVPSARCPVVKFCHRPSGLHGDISLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLNNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEQVEVDGWDCSFPRDASRLEPSTNKEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALSVAGGLPSNLSEGLRLGPMNLQDPFDLSHNVAANVTSRVAGRLQNCCRAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSILSATPIPLPPASFTQLTAVLAQVLREALGCHIEQGTKRLRSEGGGPGEPPQGGTSKRAKLDGQKKSCEEGPEEQQGCAGEHGEDGVEEMVIEVGESVQDWVMRSPGQLGELPLMTGKHLATREEGQSGTAALAKQGPRGPEAACEGSQAEAEKRVSLTVSWRCALWHRVWQGRRRARRRLQQQIKEGGGSGAGSGAEWLATEAQVTRELRGLSSTEQRPEAEPLLTFVASTSQADQSLTVTPLQDSQGLFPDLHHFLQVFLPQALRNLLK", "text": "FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus speckle. SIMILARITY: Belongs to the DNA polymerase type-B-like family."}
{"protein": "MVTSSSVIVLTLWAALVSASPVADPLVTPAPKLEDLEKRATSCTFSGSEGASSASKSKTSCSTIVLSDVAVPSGTTLDLTDLNDGTHVIFEGETTFGYEEWSGPLVSVSGTDITVTGADGAYLNGDGSRWWDGEGSNGGKTKPKFFYAHDLTSSTISGIYIQNSPVQVFSIDGSTYLTMEDITIDNTDGDDGEAANTDGFDIGDSTYITITGANVYNQDDCVAVNSGENIYFSGGVCSGGHGLSIGSVGGRSDNTVKNVTFYDSEIKSSQNGVRIKTIYGDTGSVSEVTYKEITLSDITDYGIVVEQNYDDTSKSPTDGITIEDFVLDNVQGSVESSGTNIYIVCGSDSCTDWTWTDVDVSGGKTSSDCENVPDDISC", "text": "FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
{"protein": "MKSLILAEKPSVARDIAEAMNIKGKRNGYIENEKYVVTWALGHLVTNAQPEHYDKAYKEWKLEDLPIIPKRMQTVVIGKTSKQFKTVKSLILDKKVKEVIIATDAGREGELVARLILDKVHNKKPIKRLWISSVTKKAIQEGFKKLKDGREFQHLYEAALARSEADWIVGINATRALTTKYDAQLSLGRVQTPTIQLVNARQQEINHFKAKKYYTLSTEIGGLTFQLSTNKQHMTMEDATQIANEIKHVEGNVDSVEKKVKKSHPKPLYNLTDLQQEAYQRYKMGPKETLNTIQNLYERHKVLTYPRTDSNYLTDDMVDTIKERLYALLATDYKSQVKSLLGQSYSSKMRIFKNHKVSDHHAIIPTEVRPDMQSLSNRESKIYMMVAERFLESLMAPHEYEAVRVNVTVGQHIFAFNEKVTRQLGYKALKMNNDNVVKKVAFQKGEKYHLQSLKVNEHETTPPDYFNEGSLLKAMENPQNYIQLKEKKHANTLRQTGGIGTVATRADIIEKLFNLNAIESRDGKIKVTSKGKQILDLAPQELTSPLLTAEWEEKLLLIEKGRYNSRHFIDEMKAFTQSIVNTIKNSEQKYKHDNLTTTECPTCGKFMIKVKTKNGQMLVCQDPTCKTKKNVQRKTNARCPNCKKKMTLFGRGKDAVYRCVCGHTETQEQMDKRFKNKSSGKVSKKEMKKYMNNEDSLENNPFKDALKNLKL", "text": "FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. SIMILARITY: Belongs to the type IA topoisomerase family."}
{"protein": "MWRGGRLSSRGVRFLETLGFACPSAVAEPPRVTSWTAFSGNQLTRNLQIKPWEFSGHRTMWLRSYRITFSCLTRLKTYRSSWKKLYSTSQTVDSKEVKTFQALAHSWWDEQGKFAPLHSMNDLRVPFIRDNLLKTSTNHDPGKPLSGMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVLDKRIQYRVCSLEETLNENAECFDAVVASEVVEHVNNLEMFIQCCYQVLKPGGSLFITTVNKTQLSYVLGIVFSEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGMVYNPFSGYWHWTENTSLNYAAHAVRARAQEHLEPAESA", "text": "FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family."}
{"protein": "MKTWYMVVVIGFLATLAQTSLALKEEDCEVCVKTVRRFADSLDDSTKKDYKQIETAFKKFCKAQKNKEHRFCYYLGGLEESATGILNELSKPLSWSMPAEKICEKLKKKDAQICDLRYEKQIDLNSVDLKKLKVRDLKKILNDWDESCDGCLEKGDFIKRIEELKPKYSRSEL", "text": "FUNCTION: Required during the maturation of the embryonic nervous system for maintenance of neuronal and cuticular connectivity. Essential for maintenance of dopaminergic neurons and dopamine levels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ARMET family."}
{"protein": "MRVIPLASESLGVRSLATFVEAGGIKILIDPGVALGPKRYGLPPAKIELETLQKMRRKIQGYARRADVVTISHYHYDHHTPFFEGLYESSSEEYAREIYAGKLLLIKHPRENINFSQRKRAWAFLKNAEPIARRIEFADGRAFDLGGVTLEFSPAVPHGSEGSRLGFVVMVLIDDGSERIIHASDIQLLNRKAVEWIIEKNPDLLITGGPPTYLGKRAEGSWETGIKNLNEIIRETNAEIILDHHIVRDKRYPEFFDELEKRPKTFAGFLKVEDKPLEAYRRELHKRERGESVELPFRVG", "text": "SIMILARITY: Belongs to the UPF0282 family."}
{"protein": "MNVFFMFSLLFLAALGSCADDRNPLGECFRETDYEEFLEIAKNGLRATSNPKHVVIVGAGMSGLSAAYVLAEAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFHQENDNAWHFIKNIRKRVGEVKEDPGLLQYPVKPSEEGKSAGQLYEESLGKVAEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVDGMDKLPTSMYQAIKEKVRFNARVIKIQQNDREVTVTYQTSANEMSPVTADYVIVCTTSRATRRITFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCGDIVINDLSLIHQLPKKDIQTFCYPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEL", "text": "FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:22963728). Is highly active on L-Met=L-Leu>>L-Phe>L- Trp>L-Tyr>L-Ile, and weakly or not active on L-His, L-Arg, L-Val, L- Gln, L-Thr, L-Lys, and L-Ser (PubMed:22963728). Exhibits a low myotoxicity (a mild myonecrosis is observed after injection in mice quadriceps muscle) (PubMed:22963728). In vitro, is cytotoxic to a lot of human cell lines, including AGS (IC(50)=22.7 ug/ml), MCF-7 (IC(50)=1.4 ug/ml), HL-60, HeLa and Jurkat cells, as well as to the parasite Leishmania brasiliensis (IC(50)=2.22 ug/ml) (PubMed:22963728). This cytotoxicity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger (PubMed:22963728). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
{"protein": "MQIKIGEIESKLNNIIEEEGAAYFVLIDPDEKNYREIANHVKDYADAIIIGGSIGIINLDEVTKEIKEITGLPVILFPGNVDGVTKEADAVLFMSLMNSKNTYWNMTAPTLGALTIKKYGLETLPMAYLGIEPISKTAVGFVGEVNEIPQKKPEIAGIYSLSASYFGMRWVYLEAGSGAEYPVNNEMIGVSKKLSGINIIVGGGIRTPEVAYEKVMSGADVIVTGTLTEKDPKAVEEMKKAIKKAGMDKLKMLSKK", "text": "FUNCTION: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II subfamily."}
{"protein": "MGKIRKLDDQLSNLIAAGEVVERPASVVKELVENSIDANSTSIEIHLEEAGLSKIRIIDNGDGIAEEDCIVAFERHATSKIKDENDLFRIRTLGFRGEALPSIASVSELELITSTGDAPGTHLIIKGGDIIKQEKTASRKGTDITVQNLFFNTPARLKYMKTIHTELGNITDIVYRIAMSHPEVSLKLFHNEKKLLHTSGNGDVRQVLASIYSIQVAKKLVPIEAESLDFTIKGYVTLPEVTRASRNYMSTIVNGRYVRNFVLMKAIQQGYHTLLPVGRYPIGFLSIEMDPMLVDVNVHPAKLEVRFSKEQELLKLIEETLQAAFKKIQLIPDAGVTTKKKEKDESVQEQFKFEHAKPKEPSMPEIVLPTGMDEKQEEPQAVKQPAQLWQPPKQEWQPPQSLVREEQSWQPSTKSIIEEPIREEKSWNSNDEDFELEELEEEVQEIEEIEMNGNDLPPLYPIGQMHGTYIFAQNDKGLYMIDQHAAQERINYEYFRDKVGRVAQEVQELLVPYRIDLSLTEFLRVEEQLEELKKVGLFLEQFGHQSFIVRSHPTWFPKGQETEIIDEMMEQVVKLKKVDIKKLREEAAIMMSCKASIKANQYLTNDQIFALLEELRTTTNPYTCPHGRPILVHHSTYELEKMFKRVM", "text": "FUNCTION: This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex. SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family."}
{"protein": "MQPSRTRVSFFETGETMKQRKKSYLSIFVIFFSLFFFGIFMYNDNLKSSIADFTSSNPFSSSFVELPPDECDLFTGQWVFDNKTYPLYKEEECEFLTEQVTCLRNGRKDSLFQNWRWQPRDCSLPKFNARVLLEKLRNKRLMFVGDSLNRNQWESMVCLVQSVIPPGRKSLNQTGSLTVFKIQDYNATVEFYWAPFLVESNSDDPEKHSIIDRIIMPESIEKHGVNWIGVDFLVFNSYIWWMNTVSIKVLRGSFDDGDTEYDEIKRPIAYERVLRTLGDWVDHNIDPLSTTVFFMSMSPLHIKSSDWANPEGIRCALETTPILNMSFNVAYGQFSAVGTDYRLFPVAENVTQSLKVPIHFLNITALSEYRKDAHTSVYTIKQGKLLTREQQNDPANFADCIHWCLPGLPDTWNEFLYTHIISRR", "text": "FUNCTION: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily."}
{"protein": "MQKDSGPLMPLHYFGFGYAALVATGGIIGYAKAGSVPSLAAGLFFGGLAGLGAYQLSQDPRNVWVFLATSGTLAGIMGMRFYNSGKFMPAGLIAGASLLMVAKVGISLLSSPHP", "text": "FUNCTION: Required for normal heme biosynthesis. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM14 family."}
{"protein": "MAIHRIVLFYAFAPVADPESVRLWQRALCEKHGLTGRILISRDGINATVGGELSAVKQYVKATKEYPAFNDIDVKWSEGSAADFPRLSVKVRDEIVSFGAPGELEVDQNGVVGGGTHLQPEELHELVAQKDVVFFDGRNAFEAQIGKFKNAVVPDVETTRDFIAELDSGKYDELKDQPIVTYCTGGIRCEVLSSLMVKRGFKEVYQLDGGIVRYGEKYRDAGLWEGSLYVFDKRMHLEFSDEAKTIGECSRCGAPTSDFHNCANLACRHLSLYCAECAASEDTLRCAGGCPAA", "text": "FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. SIMILARITY: Belongs to the TrhO family."}
{"protein": "MEKTFSLSRRDDGIALLTMDVPGETMNTLKAQFAPEITAILQEIKADSSIKGLVLISGKADSFVAGADISMLDACETAEDARLLSRQGHHVFAELEGLNIPVVAAIHGACLGGGLELALACHQRVCSDSSKTMLGVPEVQLGLLPGGGGTQRLPRLIGIAKALDLMLTGKQVRPKQAVKMGLVDDVVPESILLDTAIEMALAGKKTRKPLKQPLVTKLLEGTPVGRNIMFDQATKQVLKKTQGNYPSPLKIIDCVREGMAKGMEKGLEVEAAHFGALVATPESAALRSIFFATTEMKKETGAGDAKPRKVAKAVVLGGGLMGGGIASVTTTKAKVPVRVKDISDKGLSNALGYAYKLLDKGVKRRHMTSAERDKLMALMTTTTEYRGVKDADIVVEAVFEDLNLKHQMVRDIERECGEHTIFASNTSSLPITQIAAAASRPENVIGLHYFSPVEKMPLVEVIAHEKTSPETIATTVAFARKQGKTPIVVKDCAGFYVNRILALYMNEAAQLLLEGQAVDHLDKALVKFGFPVGPMTLLDEVGIDVGAKISPILEKELGERFKAPAAFDKLMADDRKGRKNGKGFYLYGKAAKKGKKVDESVYSLLGLTPATGKEAGEIAERCVVQMLNEAVRCLEEGIIASPRDGDIGAIFGIGFPPFLGGPFRYMDTLGAAKMVRLLEGYQSKYGDRFAPAALLKAMAAEGKTFY", "text": "FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family."}
{"protein": "MSILNPRTSLEAGDSEDACCAAMASVCCINTKEDADSPSAGLPSGTTQNLDVEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACILKSLRNAGHKCPVDNEILMEKQLFPDNFAKREILSLRVKCPNLGCTDTMELRHLEHHLVQCQFASVECSQCQGSFLKLLLDKHMEHECGRRRTFCDNCGLAMAYEDKSGHELICPMAYVTCDYCQTNLIREQMPAHYSMDCTMAPIPCMYCEFGCREKMQRHNLAGHLQDFTQAHMRMMAQTLRSFSTTPTSHISDISFCDPNQFEPVPLSVAPAHPSHMPSQQDCSQETRNLRETVEQLEGRLVRQDHQIRELIAKMETQCTYVNELKHTIHSLEDKVADMDAHRCNGVFIWRIKGFSGLQKSQEEEKPVVIHSPGFYTGDPGYKLCLRLHLQLPSAQRCANYISLFVHTMQGDYDSLLPWPLQGTIRLSILDQSESTARQDQVEVMDTKPDLLAFQRPTAPRNPKGFGYVTFMHLNTLKQRQYVKNDTLLVRCSVNIHLDLTSPRREGFQPRSGEGTL", "text": "FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cell cortex Nucleus Lipid droplet. SIMILARITY: Belongs to the TNF receptor-associated factor family. A subfamily."}
{"protein": "MDRITDFYFLDFRESVKTLIITGNSWRLQEMIDRFFTNISNFNRESLTEIQNIQIEEIAVNLWNWAVTKRVELSVRKNQAAKLCYIACKLVYMHGISVSSEEAIQRQILMNIKTGKEWLYTGNAQIADEFFQAAMTDLERLYVRLMQSCYTEANVCVYKMIVEKGIFHVLSYQAESAVAQGDFKKASMCVLRCKDMLMRLPNMTKYLHVLCYNLGIEASKRNKYKESSFWLGQSYEIGKMDRRSVEPQMLAKTLRLLATIYLNCGGEAYYTKAFIAILIANKEHLHPAGLFLKMRILMKGNSCNEELLEAAKEILYLAMPLEFYLSIIQFLIDNKRESVGFRFLRIISDNFKSPEDRKRILLFYIDTLLQKDQDMIAEEKIKDVLKGYQTRSRLSRDLVNWLHNILWGKASRSVKVQKYADALHWYSYSLKLYEYDKADLDLIKLKRNMVSCYLSLKQLDKAKEAIAEVEQKDPTHVFTRYYIFKIAIMEGDAFRALQVVSALKKSLMDGESEDRGLIEAGVSTLTILSLSIDFALENGQQFVAERALEYLCQLSKDPKEVLGGLKCLMRIILPQAFHMPESEYKKKEMGRLWNYLNTALLKFSEYFNEAPSTLDYMVNDANWFRKIAWNLAVQSEKDLEAMKNFFMVSYKLSLFCPLDQGLLIAQKTCLLVAAAVDLDRGRKAPTICEQNMLLRTALEQIKKCKKVWNLLKKTGDFSGDDCGVLLLLYEFEVKTKTNDPSLSRFVDSVWKMPDLECRTLETMALLAMDKPAYYPTIAHKAMKKLLLMYRKQEPVDVLKYSVCMHNLIKLLVADEVWNISLYPLKEVQSHFKNTLSIIRQNEGYPEEEIVWLMIKSWNIGILMSSKNKYISAERWAAMALDFLGHLSTLKTSYEAKVNLLYANLMEILDKKTDLRSTEMTEQLRALIVPPEDQGSVSSTNVAAQNHL", "text": "FUNCTION: Regulator of crossing-over during meiosis. Involved in initiation and/or maintenance of chromosome synapsis and formation of crossovers. SUBCELLULAR LOCATION: Chromosome Note=Forms arrays of discrete foci along synaptonemal complexes in spermatocytes and fetal oocytes. SIMILARITY: Belongs to the SPO22 family."}
{"protein": "MAVYDQSGDRNRTQIDTSRKRKSRSRGDGTTVAERLKRWKEYNETVEEVSTKKRKVPAKGSKKGCMKGKGGPENSRCSFRGVRQRIWGKWVAEIREPNRGSRLWLGTFPTAQEAASAYDEAAKAMYGPLARLNFPRSDASEVTSTSSQSEVCTVETPGCVHVKTEDPDCESKPFSGGVEPMYCLENGAEEMKRGVKADKHWLSEFEHNYWSDILKEKEKQKEQGIVETCQQQQQDSLSVADYGWPNDVDQSHLDSSDMFDVDELLRDLNGDDVFAGLNQDRYPGNSVANGSYRPESQQSGFDPLQSLNYGIPPFQLEGKDGNGFFDDLSYLDLEN", "text": "FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3' (PubMed:11798174). Binding to the C-repeat/DRE element mediates high salinity- and dehydration-inducible transcription (PubMed:11798174). Promotes the expression of heat stress-inducible genes by contributing to the formation of a heat stress-specific transcriptional complex with NF-Y subunits (e.g. DPB3-1, NF-YA2 and NF- YB3) at the promoter of target genes, thus promoting heat tolerance (PubMed:25490919). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
{"protein": "MSDILPLDVIGRRVEVNGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCRHPTGGSFVRPNIVNFGEDFLTALKKRYVLTDGPDDDEKSCSLKVGSKQVQTIGFEHITKKQSQLRSLQDISLWKCAVSCAGERGRIAEACPNIRVVDLSKNLLSTWDEVILIAEQLKDLEALDLSENKLQFPSDSPTLTRTFSTLKTLVLNKTGITWTEVLHCAPSWPVLQELYLKSNGISISERPVNALQNLRLLDLSSNPSIDESQLCLIAYLPRLEHLLLSDIGLSSIHFPDAEIGCKTSMFPALTYLIVNDNQISEWSFINELDKLQSLQALSCARNPLTKGDKAEEIIIAKIGQLKTLNRCQILPEERRGAELDYRKAFGKEWRKAGGHPDPDRNRPSAEFLSAHPRYQLLCCKYGAPEDEELKTQQPFMLKNQLLTLKIKCSNQPEQQILEKQLPDSMTIQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCLLVRW", "text": "FUNCTION: Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TBCE family."}
{"protein": "MGVHKLEPKDHLKPQNLEGISNEQIEPHFEAHYKGYVAKYNEIQEKLADQNFADRSKANQNYSEYRELKVEETFNYMGVVLHELYFGMLTPGGKGEPSEALKKKIEEDIGGLDACTNELKAAAMAFRGWAILGLDIFSGRLVVNGLDAHNVYNLTGLIPLIVIDTYEHAYYVDYKNKRPPYIDAFFKNINWDVVNERFEKAMKAYEALKDFIK", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MMDMTPTITTTTTPTPKSPEPESETPTRIQPAKPISFSNGIIKRHHHHHHPLLFTYKECLKNHAAALGGHALDGCGEFMPSPSSISSDPTSLKCAACGCHRNFHRRDPDNNNDSSQIPPPPSTAVEYQPHHRHHPPPPPPPPPPRSPNSASPPPISSSYMLLSLSGTNNNNNNLASFSDLNFSAGNNHHHHHQHTLHGSRKRFRTKFSQFQKEKMHEFAERVGWKMQKRDEDDVRDFCRQIGVDKSVLKVWMHNNKNTFNRRDIAGNEIRQIDNGGGNHTPILAGEINNHNNGHHGVGGGGELHQSVSSGGGGGGFDSDSGGANGGNVNGSSSS", "text": "FUNCTION: Putative transcription factor. Probably involved in establishing polarity during leaf development through the gibberellic acid (GA) signaling pathway. SUBCELLULAR LOCATION: Nucleus Note=Interactions with MIF proteins prevent nuclear subcellular location and leads to a scattered repartition throughout the cytoplasm."}
{"protein": "MKVSFFLLKFPLSSETFVLNQITAFIDMGHEVEIVALQKGDTQHTHAAWEKYGLAAKTRWLQDEPQGRLAKLRYRACKTLPGLHRAATWKALNFTRYGDESRNLILSAICAQVSQPFVADVFIAHFGPAGVTAAKLRELGVLRGKIATIFHGIDISSREVLSHYTPEYQQLFRRGDLMLPISDLWAGRLKSMGCPPEKIAVSRMGVDMTRFTHRSVKAPGMPLEMISVARLTEKKGLHVAIEACRQLKAQGVAFRYRILGIGPWERRLRTLIEQYQLEDVIEMPGFKPSHEVKAMLDDADVFLLPSITGTDGDMEGIPVALMEAMAVGIPVVSTVHSGIPELVEAGKSGWLVPENDAQALAARLAEFSRIDHDTLESVITRAREKVAQDFNQQAINRQLASLLQTI", "text": "SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MPLHIDAVILAGGMARRMGGDDKGLVELNGQPMIKHTIDRIKPQVKEILINANRNQTRYAEFGFKVISDEHSGFLGPLAGMLAALGQTKADYLLTVPCDSPQLPMDLVERMLNAIETKGADMAVASNGEQEQPVVLLMKPSLRDSMEAFLKAGDRKILLWYAKQNYAVATFADQPNAFMNINTLEEKQQFALDQT", "text": "FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MobA family."}
{"protein": "MVSDGQVFPVPADLARDAHIDAAAYDAALARVEADPEGYWRDIAARLDWITPPTKIKDVSYAKEDFRIRWYEDGVLNVSANCIDRHLPAKKDDVALVFEGDEPGTSSTLTYGQLHEEVCRMANVLKAQGVKKGDRVTIYLPMVPLAAVAMLACARIGAVHSVVFGGFSPDSIAGRIQDCASHFVITADEGRRGGRRVPLKANIDEALKHCPWVGKVLMIRWTGADVPLKAGRDIVWQDVRDTVSADCPPEPMNAEDPLFILYTSGSTGKPKGVLHTTGGYLAWASWTFWAVFDYKPGEVFWCTADVGWVTGHSYVVYGPLANGGTSLIFEGVPNYPTPSRFWEVIDKHQVSIFYTAPTALRALMREGDAHVTKNDLSSLRLLGSVGEPINPEAWLWYHRVVGKEKLPIVDTWWQTETGGMLITPLPGATALKPGSASKPLPGVKPQLVDAEGKFLDGATEGNLVITDSWPGQMRTVYGDHQRFFETYFSTYPGKYFTGDGCRRDADGYYWITGRVDDVINVSGHRLGTAEIESALVAHETVAEAAVVGYPHDIKGQGVYAYVTLKAGIEATDALRKDLVLWVRHEIGPFAAPDVIQWAPGLPKTRSGKIMRRILRKIAENELGSLGDTSTLADPSVVDDLVKNRAGT", "text": "FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MGTKPTEQVSWGLYSGYDEEAYSVGPLPELCYKADVQAFSRAFQPSVSLMVAVLGLAGNGLVLATHLAARRTTRSPTSVHLLQLALADLLLALTLPFAAAGALQGWNLGSTTCRAISGLYSASFHAGFLFLACISADRYVAIARALPAGQRPSTPSRAHLVSVFVWLLSLFLALPALLFSRDGPREGQRRCRLIFPESLTQTVKGASAVAQVVLGFALPLGVMAACYALLGRTLLAARGPERRRALRVVVALVVAFVVLQLPYSLALLLDTADLLAARERSCSSSKRKDLALLVTGGLTLVRCSLNPVLYAFLGLRFRRDLRRLLQGGGCSPKPNPRGRCPRRLRLSSCSAPTETHSLSWDN", "text": "FUNCTION: Receptor for chemokines SCYA27 and SCYA28. Subsequently transduces a signal by increasing the intracellular calcium ions level. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MVDALTYDDVYVNFTQEEWALLNPSQKSLYKDVMLETYRNLNAVGYNWEDSNIEEHCESSRRHGRHERNHTGEKPYEGIQYGEAFVHHSSLQMRKIIHTGEKRYKCNQCDKAYSRHSILQIHKRTHSGEKPYECNQCGKAFTQHSHLKIHMVTHTGEKPYKCDQCGKAFAFHSTLQVHKRTHTGEKPYECNQCSKAFAHHCHLRVHKRIHTGEKPYKCDQCGKAFVGQNDLKRHERVHTGEKPYKCNECGKAFVCNASLRTHKTTHTGVKPYECKQCTKSFASHGQLQKHERIHTGEKPYKCDQCGKAFASHDKFQKHERIHIGEKPYKCKQCTKSFASHDKLQKHERIHTGEKPYECKQCTKSFASHNKLQKHERIHTGEKPYKCDQCNKAFVYESYLQVHKKTHTGEKPYKCNECGKAFARHSHLKVHKITHTGEKPYKCNQCGKALAYHSTLQVHQRTHTGEKPYECEQCGKAFANQSYFQVHKRIHTGEKPYKCDQCGKAFVGSSDLKRHERVHTGRETLQM", "text": "FUNCTION: Sequence-specific DNA binding transcriptional repressor. Represses target gene transcription by recruiting HDAC1 and HDAC2 histone deacetylases. Acts as a specific transcriptional repressor for PTCH1 during embryonic development. Required for osteoblast differentiation and sonic hedgehog/SHH signaling response. Binds to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLTEASLSIWGWGSLGIVLFLITFGPFVIFYLTFYILCFVGGGLVVTLLFGKTNSEKYLEQCEHSFLPPTSPGVPKCLEEMKREARTIKIDRRLTGANIIDEPLQQVIQFSLRDYVQYWYYTLSDDESFLLEIRQTLQNALIQFATRSKEIDWQPYFTTRIVDDFGTHLRVFRKAQQKITEKDDQVKGTAEDLVDTFFEVEVEMEKEVCRDLVCTSPKDEEGFLRDLCEVLLYLLLPPGDFQNKIMRYFVREILARGILLPLINQLSDPDYINQYVIWMIRDSNCNYEAFMNIIKLSDNIGELEAVRDKAAEELQYLRSLDTAGDDINTIKNQINSLLFVKKVCDSRIQRLQSGKEINTVKLAANFGKLCTVPLDSILVDNVALQFFMDYMQQTGGQAHLFFWMTVEGYRVTAQQQLEVLLSRQRDGKHQTNQTKGLLRAAAVGIYEQYLSEKASPRVTVDDYLVAKLADTLNHEDPTPEIFDDIQRKVYELMLRDERFYPSFRQNALYVRMLAELDMLKDPSFRGSDDGDGESFNGSPTGSINLSLDDLSNVSSDDSVQLHAYISDTVYADYDPYAVAGVCNDHGKTYALYAITVHRRNLNSEEMWKTYRRYSDFHDFHMRITEQFESLSSILKLPGKKTFNNMDRDFLEKRKKDLNAYLQLLLAPEMMKASPALAHYVYDFLENKAYSKGKGDFARKMDTFVNPLRNSMRNVSNAVKSLPDSLAEGMTKMSDNMGKMSERLGQDIKQSFFKVPPLIPKTDSDPEHRRVSAQLDDNVDDNIPLRVMLLLMDEVFDLKERNQWLRRNIKNLLQQLIRATYGDTINRKIVDHVDWMTSPEQVADSVKRFRDAFWPNGILAEAVPCRDKSIRMRTRVAGKTKLLAIMPDELKHIIGAETTRKGILRVFEMFQHNQLNRRMVYVFLEGFLETLFPQYKFRELFNKLHSRSKQMQKYKQKLQTTQAPSLQKR", "text": "FUNCTION: May be involved in several stages of intracellular trafficking. May play a role in endosome homeostasis (By similarity). Acts as a GAP for Galphas. SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family."}
{"protein": "MNSLLMITTCLILIGTVLAEDGYLFDKRKRCTLECIDKTGDKNCDRNCKNEGGSFGKCSYFACWCKGLPGITPISRTPGKTCKI", "text": "FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MESQCRPNVDGVHNGVESHVKVVEKPRSVGSSSEFVLRILGLLLTLIAAVVAGVDKQTKIIPLTLIKTLPSLHVPVTAKWSDMSAFVYLVVSNAIACSYAAISLVLVTMLGRRGKGGRVLAVIVLDLHMVGLLFSANGAATAVGVLGQYGNSHVEWKKVCNVFDSFCHHLVASLALSFLGSLSFLGLVLLAILNLHKKSSTK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP) family."}
{"protein": "MSAFNLERFRFDKGKKIDTEFGEKGASSRPSTPNSQLEDHVTSIPETPEAKRVNNPSLFKKDKGVSFLDSDSENEDHQSKSKFSSTHQQSHPREENGTSDSVTDDSEDDYLAVKRPSASTAQVKDGSKYKNLQRLKEIFPKQNNDELLKLIESTSTLDGAVAAGVVLFNKEGSSRKRKLDEVPKDSSPVHEGINGQTKKKKKIDRVSSDNDSSLSEDDWEKQEASVKKLQRHFPDLDKEELREVLQEHDWSFHEALEALKLFAEDETDALQNAAKKEVSNGKEFSRSNKNDNKSSAKAKANQNSNKAMAQNGVKKKGKGKKYSENAKRDTRDLESEESASDAGSCLDEDYSSGDEKLEEEYKTKILSFLQDASLDELYLIPHCSHKKAQKITELRPFSSWESLFEKMTKSNGLSEDLIWDCQTLIKEREVVMKLMNKCEEISRTLTKQVTQLTEDGECGWNIEQPSIMSENLVLKPYQKIGLNWLALLHKHKVNMILADEMGLGKTVQAIAFLAHLYVTGDSGPHLVVVPASTMDNWIREFNQWCPSMNILLYYGSQEERKHLRYDILNKVVEFNVIVTTYNCAISSAEDRSLFRRLKLNFAVFDEGHMLKNMSAIRYQHLMTLNARSRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIKRLFSSKAKSTDEQTIFEKERIAHAKQIMKPFILRRVKSEVLKQLPPKQDKIKFCQMSKKQEQLYSDLLNKLKKSIDATEKNSELCNVMMHLRKMANHPLLHRQYYTADRLRTMSKLMLKEPTHCDANPDLIFEDMEVMTDFELHRLCNEFTTLSQYKLEKELILDSGKFNILEKLLSDIKKKGDRVVLFSQFTMMLDIIEVFLRHHQHRYVRLDGKTQISERIHLIDEFNTDMDIFIFLLSTKAGGLGINLTSANIVILHDIDCNPYNDKQAEDRCHRVGQTKEVKVIKLIGKGTIEESMLKISQQKLRLEQDMTTNDTGDEGTIPLDMATLLKTSLGL", "text": "FUNCTION: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double- strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage (By similarity). SIMILARITY: Belongs to the SNF2/RAD54 helicase family."}
{"protein": "MKAWIWFTFVACLFAASTEAASNLVCYYDSSSYTREGLGKLLNPDLEIALQFCSHLVYGYAGLRGENLQAYSMNENLDIYKHQFSEVTSLKRKYPHLKVLLSVGGDHDIDPDHPNKYIDLLEGEKVRQIGFIRSAYDLVKTYGFDGLDLAYQFPKNKPRKVHGDLGLAWKSIKKLFTGDFIVDPHAALHKEQFTALVRDVKDSLRADGFLLSLTVLPNVNSTWYFDIPALNGLVDFVNLATFDFLTPARNPEEADYSAPIYHPDGSKDRLAHLNADFQVEYWLSQGFPSNKINLGVATYGNAWKLTKDSGLEGVPVVPETSGPAPEGFQSQKPGLLSYAEICGKLSNPQNQFLKGNESPLRRVSDPTKRFGGIAYRPVDGQITEGIWVSYDDPDSASNKAAYARVKNLGGVALFDLSYDDFRGQCSGDKYPILRAIKYRL", "text": "FUNCTION: Cooperates with insulin-like peptides to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex. SUBCELLULAR LOCATION: Secreted Note=Secreted in hemolymph. It is probably transported to target tissues via hemolymph. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF subfamily."}
{"protein": "MSSPLSQAFAQNFLGHSPRWYKLTVLAFLLLNPLLLWLAGPVTSAWVLVGEFIFTLAMALKCYPLQPGGLLVLEALLLGLATPEALYAELQHNFPVLLLLMFMVAGIYFMKDLLLLLFSRLLLGVRSKTLLSLLFCLLAALLSAFLDALTVTAVVISVAVAFFAVYHRVASGQRASEDYDPATDRQVPELHRAHLEEFRAFLRSLLMHAAVGTALGGVCTLVGEPQNLLIGHEAGWHFVEFFRQVAPVSMPVLAAGLLTCVLLEKSRRFGYGAQLPAAVRQVLAEYAASESRKRGAQQKAALLVQALAALVLIVGLALHVAEVGLIGLLVIVLITAFTGVTDEHQIGRAFQEALPFTALLVVFFAVVAVIHQQHLFTPIIQAVLALPAERQPGMLFIANGLLSAISDNVFVATIYITEVKQALDAGHMSREHFDTLAVAINTGTNLPSVATPNGQAAFLFLLTSSIAPLVRLSYGRMVWMALPYTLVMGGLGWWAVSHWL", "text": "FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons (PubMed:15107534). Can also transport lithium (PubMed:15107534). FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter family. SIMILARITY: Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter family."}
{"protein": "MAAVAVLRNDSLQAFLQDRTPSASPDLGKHSPLALLAATCSRIGQPGAAAAPDFLQVPYDPALGSPSRLFHPWTADMPAHSPGALPPPHPSLGLTPQKTHLQPSFGAAHELPLTPPADPSYPYEFSPVKMLPSSMAALPASCAPAYVPYAAQAALPPGYSNLLPPPPPPPPPPTCRQLSPAPAPDDLPWWSIPQSGAGPGSSGVPGTSLSSACAGPPHAPRFPASAAAAAAAAAALQRGLVLGPSDFAQYQSQIAALLQTKAPLAATARRCRRCRCPNCQAAGGAPEAEPGKKKQHVCHVPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKSFTRSDELQRHLRTHTGEKRFACPECGKRFMRSDHLAKHVKTHQNKKLKVAEAGVKRENPRDL", "text": "FUNCTION: Binds to GC boxes promoters elements. Probable transcriptional activator that has a role in the coordination of changes in transcription required to generate pattern in the developing embryo. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family."}
{"protein": "MTHIIQESLAGQFLIAMPALNDPNFALSVTYICVHNQDGAFGLVINQSFDSVTGKTLFDQMDMPAVKAAENQTVHIGGPVHQGYVFVLHGRPMEWKASLQISDTVAMSNSTDILQAIASGVGPDPCMIFLGCAGWAPGQLEAELAENSWLTCPGNDDLLFRTPLEERWEKAAQSIGVDLNLLSGVAGHA", "text": "SIMILARITY: Belongs to the UPF0301 (AlgH) family."}
{"protein": "MERISLTIEKNLLKEVDEIINKERISRSEFIRRALEYYVKKYDWLSRIESKIGEITVIYNSKAVEDIVKLESQYKDIVIISLEIPFEGKIIRMIAIKGQRDRIIEFTNKLKGISSVELAQLTTISIE", "text": "SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family."}
{"protein": "MAPLKLNNKNLSQIAAAGETQVKVPTYKRGGDVKEGIVHVGVGGFHRAHLAVYVDQLMQKHGVTDYAICGVGLQPFDAAMRDALGSQDHLYTVIERSAKGSFAHVVGSINSYLFAPDNREAVIAKMAHPDTHIVSLTITESGYYYNENTHELQSEHPDIQFDLQPANEKSPRTTFGFLYAALARRYQQGLKPFTVMSCDNMQKNGSITRHMLESFARLRNPEIAKWIAEQGAFPNAMVDRITPQTSATDKTALADNFAIEDSWPVVTEPFMQWVIEDQFSDGRPPFEKVGAQVVKNVHDVEEFEKHKLRLLNGSHSAIGYPGQLAGFKYVHEVMENPLFSKFVWQMMQDEVKPLLPEIPGVNIDEYCKTLIERFSNPTIMDQLPRICLNASGKIPQFIMPSIAEAIWVTGPFRRLCFVAAAWFHYINGVDDSGKKFEVDDPMREELQAKARAGGTSPAELLSIKSLFGDDLRGDKRFLQEITKAMEDIARDGILKTLPKYID", "text": "FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose and D-mannitol in the mannitol metabolic pathway. SIMILARITY: Belongs to the mannitol dehydrogenase family."}
{"protein": "MSIKSDRWIRKMAEEHGMIEPFEAGQVRFNDAGERLVSYGTSSYGYDVRCAPEFKVFTNVHSVIVDPKNFDEKSFIDVIGDECIIPPNSFALARTMEYFRIPRDVLTICLGKSTYARCGIIVNVTPLEPEWEGHVTLEFSNTTNLPARIYAGEGVAQMLFFQSDADDVCETSYKDRGGKYQGQRGVTLPRT", "text": "FUNCTION: Catalyzes the deamination of dCTP to dUTP. SIMILARITY: Belongs to the dCTP deaminase family."}
{"protein": "MATKILALLALLALFVSATNAFIIPQCSLAPSAIIPQFLRPVTSMGFEHLAVQAYKLQQALAASVLQQPINQLQQQSLAHLTIQTIATQQQQQFLPALSQLDVVNPVAYLQQQVLASNPLALANVAAYQQQQQLQQFLPALSQLAMVNPAAYLQQQQLLSSSPLVVGNAPTYLQQQLLQQIVPALTQLAVANPAAYLQQLLPFNQLTVSNSAAYLQQRQQLLNPLAVPNPLVTAFLQQQQLLPYSQFSLMNPALSWQQPIVGGAIF", "text": "FUNCTION: Zeins are major seed storage proteins. SIMILARITY: Belongs to the zein family."}
{"protein": "MSTHESADQAGTPQYGTAHSAASAAPHYSAAFGATSLPGSQPVSAQEYDAVLRRLSAAEATRDNMSRQIRGAGEKNRKLVEAITSMRYQVERLRASLSQNVMPPLNSAIVLAVHEGQTMTYEQVADDKTPAEIDTYLDVQVSGRMMRIPVSPLIDLSTLTPGMTVLLNDKTEAVLALDTEPFGDVVTVREVLDEQRVLVDTSSGAQQVARVAGSLNIEQLRTGDAVTLDTRTRMLTSQVPASRSQELVLEEIPDVTYEQIGGLGAQIEQIRDAVELPYLHPEIFERYHLAPPKGILLYGPPGNGKTMIAKAVANSLAARAAALNPGSATRGYFLNIKGPELLDKFVGETERQIRDIFVAAREKAEAGHPVVVFFDEMESLFRMRGSGRSSDIETTIVPQLLAEIDGVESLQNVIVIGATNREDLIDAAVMRPGRLDLKIRINRPDAAGAAEIFGLYLTEDLPLDATEVAAAGSTRAALTAMIAAAAGQLYARTPSTAYAVATVDSSMVVGSGASANLSTHTLYRGDFASGAVIRNIVDRAKKAAIKEQLQALTAGADASSVGIGTRHLLEAVRAEFEDQVDLPPLPDIEDALTVAGVRGRLVSVEPPR", "text": "SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MAQLAKFDVPEELTNKALEALELARDTGKIKKGTNEATKAIERGNAKLVLIAEDIEPAEIVAHIGPLSEEKKAPYIYIKNQKDLGAASGLGVSCATVAIVDAGKAAEMIQDIAQKLDALK", "text": "FUNCTION: Multifunctional RNA-binding protein that recognizes the K- turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family."}
{"protein": "MSLLEFFRPQKKTSASLAKERLQIIVAERRSQNDPAPSYLPQLKEDILKVISKYVAIDPAMVDLTFEHKDDDISVLELNVKLPDEEK", "text": "FUNCTION: Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. SIMILARITY: Belongs to the MinE family."}
{"protein": "MKVTLISILTCAAVLVLHTTAAEELEAESQLMEVGMPDTELAAVDEERLFECSVSCEIEKEGNKDCKKKKCKGGWKCKFNMCVKV", "text": "FUNCTION: Neurotoxin active on both insects and mammals. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 02 (Hwtx-2) subfamily."}
{"protein": "MSSLGRLHLITDARAGRNPLTVVQAALSVARTELVVQVRVADDATDRQAYDLARRVIALCARYDATCLVNDRLHVALAVGAAGGHVGADDLPVGAARAVLGSAAVLGVTARDADTAVEAVAAGASYLGVGPVHPTTSKEGLPPAIGVAGVGVVAAAVSVPVIAIGAVTAADVPVLRAAGAYGVAVIGALSHAADPAGATAALLEALTW", "text": "FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). SIMILARITY: Belongs to the thiamine-phosphate synthase family."}
{"protein": "MSTRSKSVPVPAGGGAATVPLAVLLRREVVSEKTAAERPELQVGLFSQAKKGEDYTFLKPDCERLPGVPSSSFSAFGLFDGHNGNGAAIYTKENLLSNILTAIPADLNREDWLAALPRAMVAAFVKTDKDFQTKARSSGTTVTFVIIDGLFITVASVGDSRCVLEAEGSIYHLSADHRFDASKEEVDRVTESGGDVGRLNVVGGAEIGPLRCWPGGLCLSRSIGDQDVGQFIVPVPYVKQVKLSTAGGRLIISSDGVWDVLTAEVAFNCSRTLPPEAAAEQIVKEAVQQKGLRDDTTCIVVDILPDKANLTMPHTKKQPGMGVFKNMFRKKTPSDSSSHTDREYMDPDIVEEIFEDGCAFLSKRLDSEYPVRNMFKLFICAICQVELKPSQGISVHEDSSQPGNLRRWDGPFLCQGCQEKKEAMEGKRRSRDSSSRNSGSSE", "text": "SIMILARITY: Belongs to the PP2C family."}
{"protein": "MSTGLDMSLDDMIAKNRKSRGGAGPARGTGSGSGPGPTRRNNPNRKSTRSAPYQSAKAPESTWGHDMFSDRSEDHRSGRSSAGIETGTKLYISNLDYGVMNEDIKELFAEVGELKRYTVHFDRSGRSKGTAEVVYSRRGDALAAVKKYNDVQLDGKPMKIEIVGTNLQTAAAPSGRPANGNSNGAPWRGGQGRGGQQRGGGRGGGGRGGGGRGRRPGKGPAEKISAEDLDADLDKYHSGDMETN", "text": "FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the ALYREF family."}
{"protein": "MEQEQDTPWTQSTEHINIQKRGSGQQTRKLERTNLTQLMDHYLRTMNQVDMHKQTASWKQWLSLKNPTQESLKTRVLKRWKLFNKQEWTN", "text": "FUNCTION: Plays an important role in promoting lung pathology in both primary viral infection and secondary bacterial infection. Promotes alteration of mitochondrial morphology, dissipation of mitochondrial membrane potential, and cell death. Alternatively, inhibits the production of interferon in the infected cell at the level of host mitochondrial antiviral signaling MAVS. Its level of expression differs greatly depending on which cell type is infected, in a manner that is independent of the levels of expression of other viral proteins. Monocytic cells are more affected than epithelial cells. Seems to disable virus-infected monocytes or other host innate immune cells. During early stage of infection, predisposes the mitochondria to permeability transition through interaction with host SLC25A6/ANT3 and VDAC1. These proteins participate in the formation of the permeability transition pore complex (PTPC) responsible of the release of mitochondrial products that triggers apoptosis. SUBCELLULAR LOCATION: Host mitochondrion inner membrane Host nucleus Host cytoplasm, host cytosol Note=Inner mitochondrial membrane in most cells types. Otherwise is detected in the nucleus and cytosol. SIMILARITY: Belongs to the influenza viruses PB1-F2 family."}
{"protein": "MAISQERKNELIKEYRTHEADTGSPEVQIAVLTAEITALNEHLREHKKDHHSRRGLLKMVGRRRHLLNYLRDKDVQRYRELIKSLGIRR", "text": "FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MQSSLLGRMTGVTGSRSKRHTKFRLRRLQQPPTESTTRLASPDDAQPIEETKSQEHLEQSATQGLSEASGDNNAGGAHPTPAPNEGDAPTVAELQHGSNDRVDDGTSGSGTVSGWKLAAVLIGLSLAVFCMSLDSTVLSTAIPKITAEFNSLHDMAWYVSAYNLTISSFSLVYGKIYSLYRVKWVYLTTLFLFEAGSLVCGAAPSSLALIIGRAIAGVGGAGVFLGSMLIVHEIMPLHQVPLFIALISGLYGIASVVGPLLGGVFTDYVSWRWCFYINLPIGGLTAFIIVLFVRPRVREKATVKKTPWAQLLDLDPLGIILILPAVMCMLLVLQWGGAKYAWSNWRIIVLLVMAGSLALTFTAVQLWQGERATIPPRIVRNRSVWGAIAFSVCIYGSFTVFTYYLPIWFQAIKSVSATRSGVMNLPMILGVVVCSMLSGWGVSRVGYYVPFMYMAPVVGSIGAGLLTTLHVFSGPAAWITYQLLLGVGIGSGMALPLVAVQTALPTDDVSTGSAIITFTQSLSGALFNFVAQSVFQSRLVHNLNAALPGVDTARVADVSPREIRNAIEPEYLPQTLEAYSLAITQVFYAGTALCTLALFGVLPIKCLSVKGSRIPPMAHA", "text": "FUNCTION: MFS-type transporter; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
{"protein": "MARLAINVDHVATVRQARRASEPDPVTAAALAELAGAHGIVVHLREDRRHIQDRDVQVLRQTVKSKLNLEMAATREMIQIALNIKPEMVTLVPEKRQELTTEGGLDVVSFEGALEEAIKTLHEGGIAVSLFINPDPRHIKVAHRLEAEYVEIHTGMFAEADSYTRRQEEYERVVTSAKLARKLGLGAHAGHGIGYQNVLWLRNIPEIQEFSIGHAVIARAVLVGMERAVREMLALVNG", "text": "FUNCTION: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PNP synthase family."}
{"protein": "MRNSPVSPGPGYAPSRGAARTRKRGVARWLAYAGGVFAGAWLATQLYYVAQIAAWSVIDPGSSAFMRADAWRLSNAQPAVPIRHRWVPYDKISRNLKRAVIASEDADFANNSGYEVDAILQAWEKNRARGRIVSGGSTITQQLARNLFLSGERSYIRKGQELIITWMLETLLDKERIFEIYLNSVEFGRGVYGAEAAAQYYYRIPASRLSAWQSARLAVMLPNPKYFDAHRSSPYLAQRASVIARRMGAAELPASQ", "text": "FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 51 family."}
{"protein": "MSNLIPPHGGKGLVCCLLEGAELEAEKKKAATLPKLNISSRAKGDLIMMGIGGFSPLDGFMTKADWKGVCEDFLLADGTFWPIPVTLDASADDAAKINVGDEIALFDPEREEFMATMKVTEKYEMTEADKIFECEKVFMGEGTPTAEEFWKIAKDDHPGVQMVMNQGEFNLAGPVKVLSEAEYPEEYPGIYQRPAESRAIFEERGWKEIAAMQLRNPMHRSHEYLCKIAIEVCDGCFIHSLIGNLKPGDIPADVRVKCIDALVKNYFVEDKAVQGGYPLDMRYAGPREGLLHATFRQNYGCSRMIIGRDHAGVGDFYGMFEAQTIFDKIPTPEGEGKALLCTPLKIDWTFYCYKCDGMASLRTCPHAKEDRVLLSGTMLRKMLSEGGELPDHFGRDEVVAILREYYEGLTEKVEVKLHGAATGN", "text": "SIMILARITY: Belongs to the sulfate adenylyltransferase family."}
{"protein": "MSFSEQIQNLSLLLLEIGTIIGALGVVLLPNILYSGFLLGGVLICIAGIYLLLNAEFIAAAQVLIYVGAINVIILFAIMLVNKIENLNPSNNQMMRNGLSSFICFSFFILLSNMIFDTQWIDTVGVSTKYSISIIGNHIFSDFLLPFEIVSVLLLVTLVGAVFIARKEDASEIEISKISFLNLPDPSKK", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 6 family."}
{"protein": "MFEFVKLKNVCVNLSHRSILTDISLSLISNRVLTLIGPNGAGKSTLVRIILGLIKPNSGTIIRSNNLSVGYVPQKLHLNTLLPITVERFMKLSRKTNNIKIEEMLKRVKAESLKFCQLQKLSGGEMQRILFAKALLNNPNLLVLDEPTQGVDVMGQLALYKLINEIRHELQCAILIVSHDLNFVMAKTDDVICLNNHICCSGTPETVCNNLEFISIFGLKRVQELAIYHHNHNHIHNF", "text": "FUNCTION: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family."}
{"protein": "MKEYQVYLERARSRQQDFLYPLLFREYIYGLAYSHNLNRSIFLENVGYDNKYSLLIVKRLITRMYQQNHLIISANDSTKNPFWGYNKNLDSQIISEGFAIVVEIPFLRQLSSSLEEAEILQSYQNWRSIHSIFPFLEDKLTYLNYVSDIRIPYPIHLEILVQILRYWVKDAPFFHLLRLFLYNFSNWNSFLTTKKSISTFSKRNPRLFLFLHNFYVCEYEYIFVFLRTKSSHLRLKSFSVFFERIFFDAKREHLVKVFSKDFSYTLTFFKDPNIHYVRYQGKCILASKNVPFLMNKWKHYFIHLWQCFFDVWPQPRMININPLSEHSFQLLGYFLNVRLNRSVVRSQMLQNTFLIEIGIKKLDIIVPILPLIRSLAKAKFXBILGEPISKPVWADSSDFDIIDRFLRICRNLSHYYNGSSKKKSLYRIKYILRLSCIKTLACKHKSTVRAFLKRSGSEELLQEFFTEEXXILSLIFPXBSSTLQRNRIWYLDILFSNDLVHDE", "text": "FUNCTION: Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the intron maturase 2 family. MatK subfamily."}
{"protein": "MTEAPTEFPPEDGTPRRELGGDWVIRILGEIKEEALKHFDPRLLIALGNYIHSRHGDTPEGARELIRILQRALFVHLRAGCNRSRISQTRRRTPFPAAPTPRGMY", "text": "FUNCTION: Stimulates gene expression driven by the HIV-2 LTR. Prevents infected cells from undergoing mitosis and proliferating, by inducing arrest or delay in the G2 phase of the cell cycle. Cell cycle arrest creates a favorable environment for maximizing viral expression and production (By similarity). SUBCELLULAR LOCATION: Virion. Host nucleus."}
{"protein": "MTRSLLWQMVIVLGAILMVNYVLTTLTPQTQEPVVDVSYSRFKTELAADNVAAITFEGNNVVGNLRERTILNRVEGTEEVQSFLRFRTTMPPVTDTRLLDDLEQRKVDVKVRPESKPSPWATAMIYMLPWLLIVGVWWFVIKGMRTRQGPGGGMMGGFSKSGAKMYTKERSRVTFADVAGLDEAKQELMEIIEFLRNPKKFMRLGAKAPRGVLLVGPPGTGKTLMARAVAGEAEVPFFTISASQFIEMFVGVGASRVRDLFNNAKKNAPSIIFIDELDAVGRSRGTGLGGGNDEREQTLNQLLSEMDGFEAHDEVIVMSATNRPDVLDPALLRPGRFDRQVTVERPDWRAREEILKVHTRQVPIDEDVDLQIIARSTPGMCGADLENLVNEAALIAARENAQKVTMQHFEQAKDRVLMGTERKLVMSQQEKRITAYHEAGHTLLARLSPGADPIHKVSIIPRGQALGVTQQLPVDDRYHYSRSYLMTRIAVSLGGRAAEKAIFEEYSTGAQNDLKQATDLAEKMVCQWGMSERVGPMSINRGEEHPFLGRKLASDNAFSQHMAWIIDQEIEKVVKAGEQAADEIIANHLPVLKKLADALLEEEVLDRTRVDEVLRETGIEVQDDPAAHPDGDHVLQGELAGGAVEG", "text": "FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family. SIMILARITY: In the central section; belongs to the AAA ATPase family."}
{"protein": "MHENFDKRLEVLLEGLALTRRSLDPEGKENELKELEQQAVQDGFWDDVARAGKISERIARLKQQLSEFNELKNKVSTIQFFLEDEESSKDLEMQKELEKEFVFCEKKITEWETLRLLSGELDRNSCFLSINAGAGGTESCDWVEMVLRMYMRWASSHSWRVEVIDRLDGEVAGIKHITLKLVGEYAYGYAKAESGVHRLVRISPFDSNAKRHTSFASVEVFPEIDDKIEVEIHPGDIRIDTYRSSGAGGQHVNVTDSAVRITHFPTGIVVSCQNERSQIQNREACMNMLRARIYQKLLQERLEKQNIDRKNKKEISWGSQIRNYVFQPYTLVKDVRTGYEVGNIQAMMDGELLDAFIKAYLVDYGEIT", "text": "FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
{"protein": "MTTHNRPARVAEEFRHELSALLARGLKDPRITGFVTVTGSKMSPDLKEATVYVSIHGDERVRKDTFAGLQAAAGFLQREVSRALRLRNTPHLRFVYDESVARGDRIERLLREARTQGQEPAADVEPAPGAAPDDEAEE", "text": "FUNCTION: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RbfA family."}
{"protein": "MARTAATKLALVPLVAAMLLVAADAHHLRPGELCLGPLRRLRKRQRHQPSAGCCSGVKRLAGLARSTADKQATCRCLKSVPARTTPAGPQASPPGAASASPTRSAPVSTALRSTDRTRAPHISSDRRLVG", "text": "FUNCTION: Possible dehydrative stress responsive protein. Not shown to have lipid transfer activity. SIMILARITY: Belongs to the plant LTP family."}
{"protein": "MENETGSELNQTQLQPRAVVALEYQVVTILLVLIICGLGIVGNIMVVLVVMRTKHMRTPTNCYLVSLAVADLMVLVAAGLPNITDSIYGSWVYGYVGCLCITYLQYLGINASSCSITAFTIERYIAICHPIKAQFLCTFSRAKKIIIFVWAFTSIYCMLWFFLLDLNISTYKDAIVVSCGYKISRNYYSPIYLMDFGVFYVVPMILATVLYGFIARILFLNPIPSDPKENSNMWKNDSTHQNKNLNSKTSNRYFNSTVSSRKQVTKMLAVVVILFALLWMPYRTLVVVNSFLSSPFQENWFLLFCRICIYLNSAINPVIYNLMSQKFRAAFRKLCNCKQKPVEKPANYSVALSYSVIKESDRFSTELDDVTVTDTYLSATKVSFDDTCLASEITFNQS", "text": "FUNCTION: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MPTIQQLIRNARQPIENRKKSPALRGCPQRRGVCARVY", "text": "FUNCTION: With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
{"protein": "MAQLYYKYGTMNSGKTIEILKVAHNYEEQGKPVVIMTSALDTRDGFGIVSSRIGMRREAIPISNDMDIFTFIAQLEEKPYCVLIDESQFLSKQNVYDLARVVDELNVPVMAFGLKNDFQNNLFEGSKHLLLLADKIDEIKTICQYCSKKATMVLRTENGKPVYEGDQIQIGGNETYIPVCRKHYFNPDI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thymidine kinase family."}
{"protein": "MMSNRSDFIVPDEAAVKRAASVNFHLEPLRPWLDDPQITEVCVNRPGEVFCERASAWEYYAVPNLDYEHLISLGTATARFVDQDISDSRPVLSAILPMGERIQIVRPPACEHGTISVTIRKPSFTRRTLEDYAQQGFFKHVRPMSKSLTPFEQELLALKEAGDYMSFLRRAVQLERVIVVAGETGSGKTTLMKALMQEIPFDQRLITIEDVPELFLPDHPNHVHLFYPSEAKEEENAPVTAATLLRSCLRMKPTRILLAELRGGEAYDFINVAASGHGGSITSCHAGSCELTFERLALMVLQNRQGRQLPYEIIRRLLYLVVDVVVHVHNGVHDGTGRHISEVWYDPNTKRALSLQHSEKT", "text": "FUNCTION: The VirB system could be required for the establishment of the replication niche in the host. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GSP E family."}
{"protein": "MGDLPGIVRLSIALRIQPNDGPVFFKVDGQRFGQNRTIKLLTGSSYKVEVKIKPTTLQVENISIGGVLVPLELKCKEPDGERVVYTGIYDTEGVAPTKSGERQPIQITMPFTDIGTFETVWQVKFYNYHKRDHCQWGSPFSVIEYECKPNETRSLMWVNKESFL", "text": "FUNCTION: Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels. SIMILARITY: Belongs to the CNRIP family."}
{"protein": "MRFQVALLLLSVAVARALPPVYKRDADSGDSQNPPNQPSKQSSTPLPPESSNQVKTTRPTDGQGQKSDKKDQDKTTLAAVSSKAESGPPTAATDHSLGDSRRQPEKTDAELKETARPLSPVNPKLEKSDQSSTEDSGKPTGGNSGKPTGGDSGKPTGGDSDKPTEAGSNKATEDDSGKSTKVDLDKPTSKIFPDTETSKTDKVQPTEKGQKATLTSKTESGETLAGDSDFSLKPEKGDKSSEPTEDVETKEIEEGDTEPEEGSPLEEENEKVSGPSSSENQEGTLTDSMKNEKDDLYKDSSGNTSAESSHFFAYLVTAAVLVAVLYIAYHNKRKIIAFALEGKRSKVTRRPKASDYQRLNLKL", "text": "FUNCTION: May be involved in regulating membrane traffic to and from trans-Golgi network. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes (By similarity)."}
{"protein": "MMEEEELEFVEELEAVLQLTPEVQLAIEQVFPSQDPLDRADFNAVEYINTLFPTEQSLANIDEVVNKIRLKIRRLDDNIRTVVRGQTNVGQDGRQALEEAQKAIQQLFGKIKDIKDKAEKSEQMVKEITRDIKQLDHAKRHLTTSITTLNHLHMLAGGVDSLEAMTRRRQYGEVANLLQGVMNVLEHFHKYMGIPQIRQLSERVKAAQTELGQQILADFEEAFPSQGTKRPGGPSNVLRDACLVANILDPRIKQEIIKKFIKQHLSEYLVLFQENQDVAWLDKIDRRYAWIKRQLVDYEEKYGRMFPREWCMAERIAVEFCHVTRAELAKIMRTRAKEIEVKLLLFAIQRTTNFEGFLAKRFSGCTLTDGTLKKLESPPPSTNPFLEDEPTPEMEELATEKGDLDQPKKPKAPDNPFHGIVSKCFEPHLYVYIESQDKNLGELIDRFVADFKAQGPPKPNTDEGGAVLPSCADLFVYYKKCMVQCSQLSTGEPMIALTTIFQKYLREYAWKILSGNLPKTTTSSGGLTISSLLKEKEGSEVAKFTLEELCLICNILSTAEYCLATTQQLEEKLKEKVDVSLIERINLTGEMDTFSTVISSSIQLLVQDLDAACDPALTAMSKMQWQNVEHVGDQSPYVTSVILHIKQNVPIIRDNLASTRKYFTQFCVKFANSFIPKFITHLFKCKPISMVGAEQLLLDTHSLKMVLLDLPSISSQVVRKAPASYTKIVVKGMTRAEMILKVVMAPHEPLVVFVDNYIKLLTDCNTETFQKILDMKGLKRSEQSSMLELLRQRLPAPPSGAESSGSLSLTAPTPEQESSRIRKLEKLIKKRL", "text": "FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:15878329, PubMed:18367545). Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Recycling endosome Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex (PubMed:25799061). SIMILARITY: Belongs to the VPS53 family."}
{"protein": "MHFSTVTRDMEAFTASSLSSLGAAGGFPGAASPGADPYGPREPPPPPPRYDPCAAAAPGAPGPPPPPHAYPFAPAAGAATSAAAEPEGPGASCAAAAKAPVKKNAKVAGVSVQLEMKALWDEFNQLGTEMIVTKAGRRMFPTFQVKLFGMDPMADYMLLMDFVPVDDKRYRYAFHSSSWLVAGKADPATPGRVHYHPDSPAKGAQWMKQIVSFDKLKLTNNLLDDNGHIILNSMHRYQPRFHVVYVDPRKDSEKYAEENFKTFVFEETRFTAVTAYQNHRITQLKIASNPFAKGFRDCDPEDWPRNHRPGALPLMSAFARSRNPVASPTQPSGTEKGGHVLKDKEVKAETSRNTPEREVELLRDAGGCVNLGLPCPAECQPFNTQGLVAGRTAGDRLC", "text": "FUNCTION: Probable transcriptional regulator involved in developmental processes (By similarity). Binds to the palindromic T site 5'- TTCACACCTAGGTGTGAA-3' DNA sequence (PubMed:11111039). Is required for normal development of the pharyngeal arch arteries (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPILEKTPPKMAAKSPSSEEEPGLPKLPVPPLQQTLATYLRCMQHLVPEEQFRRSQAIVQQFGAPGGLGETLQQKLLERQEQTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFQDTNDQLRFAANLISGVLSYKALLDSHSIPIDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQKSSVMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVRMASNEDERLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGMELSDTNRALQLLHGGGCSKNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMVKSSKKMVRADSVSELPAPRRLRWKCSPEIQGLLASSAEKLQQIVKNLDFTVYKFDDYGKTFIKQQKCSPDAFIQVALQLAFYRLHGRLVPTYESASIRRFHEGRVDNIRSATPEALHFVKAITDHASAMPDSEKLLLLKDAIRAQTQYTVMAITGMAIDNHLLGLRELAREVCKELPEMFTDETYLMSNRFVLSTSQVPTTMEMFCCYGPVVPNGYGACYNPQPESILFCISSFHGCKETSSTKFAKAVEESFIEMKGLCSLSQSGMGKPLATKEKVTRPSQVHQP", "text": "FUNCTION: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family."}
{"protein": "MSSPIIIRAPKKQPPEPPCLISLLPEEIVVDIVARVPRCYYPTLSQVSRRFRSLVASPEIYKRRSFFGCTEQCLYIAISKDQTSDIHWFTLCRKPNGQQFSGTTASDHRLVHIPTLPPMPMHGSYVGIGSNIFVMGGFCNWKITSSVSLIDCRTHTAQTLPNMPKAVAFPVTELIDRKIYVIGGSDTLSPMKSPSRIMMVYDTDTEMWQLRARPDWEAGKKWFSSVVIGGKIYMRTYHNSFVCDPNDTSCDRDEVLHSKEWWSACVIDDVLYYYDVRENCLRAYDPKQRAWGVVKGFEGLLPVACKWSKTVSYTGGKLVLFLQKTEKTEIWCAEIAVERREGGEIWGKVEWCNVVLSGNFHIMDCVAVVL", "text": "FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAKTSMIVKQSRTPKFRVRAHNRCKICGRPHAYMRKFGMCRICFRNLAYKGEIPGVTKASW", "text": "FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. SIMILARITY: Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily."}
{"protein": "MTTQSEYDYIIIGAGSAGNTLAARLTEDAGVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGRRYNWAYETEPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDYDGWAKEPGLEDWSYLDCLPYFRKAETRDIGPNDYHGGEGPVSVTTPKAGNNPLFHAMVEAGVQAGFPRTDDLNGYQQEGFGPMDRTVTPNGRRASTARGYLDEAKKRSTLTIVTHALTDRILFEGKRAVGVAYLVGDSDTRIQARARKEVLLCGGAIASPQILQRSGVGPAEVLNKLDIPVVHDLPGVGQNLQDHLEMYLQYACTQPVSLYPSLKWWNQPAIGAEWMFLGTGIGASNQFEAGGFIRSSEAFEWPNIQYHFLPVAINYNGTKGVQEHGFQAHVGSMRSPSRGRVQVKSKDPREYPSILFNYMASEQDWQEFRDGIRLTREIMQQPALDPYRGREISPGIDVQSDEALDQFVREHAETAYHPSCSCKMGTDEMAVVDGQGRVHGLQSLRVVDASIMPIITTGNLNAPTIMIAEKIADKIRGRQPLPRSTADYFVAGDKPARGKPLREISHQA", "text": "FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MNRIIRGVIQYNQKIKAGLVKQFEHVSDHPNPTAVMFTCMDSRMLPTRFTQSAVGDMFVVRNAGNMIPAAPNYGSYSEVSINTEPAALELAVKRGKIRHVVVCGHSDCKAMNTLYQLHQCPTKFDVSSPMDQWLRRNGFESMKKLNERLHIGPKTMKFESEVAPSQSFEAIIDPMEKWSAEDKLSQINVLQQIMNISTHEFLKDYLEAGNLHLHGAWFNIYDGEVFLFSKDRKRFVVIDEKTVPSLSAELERRCPLPEDKAGDVVIQNLH", "text": "FUNCTION: Reversible hydration of carbon dioxide. SIMILARITY: Belongs to the beta-class carbonic anhydrase family."}
{"protein": "MASAMRGEKCERSRIRELVLILSLITMAGDSRATPFDPSFFIEGVQSEVVNPFNRTILNRFNLTEEQILSIQNRSNPNMRDDSAQSSNQQYLQQVATQRLNDIFKRVQKAISNEPNGSASKEKAGFPICNAETTNPEDWSLGNNVTLQFASSVFISNNDDRLSSALLRLYKTNPGQTREHNPGQASTQPISTENPGNTAPNCAEQPPVGPQIRVTVSIVHQQRKKQRKKRTCNTAMLSSSSTGWVEIDVKCALAYWEQQHRQQLRQQQPLQPQLTASVVGILMIEVHDDEENLLRPGLYFAPPTCDQADIAVPWSVYRTEPFKSHLASWTLPRKPRLDIFFNGSNSMKNSYNTPKSRAFIESTTSNSPTIDNQLDESGEYESQQRVHAPLVHHRRHHHNHQQPESESESAQLEAEIEAEELMSSASNSEQQMEPISNHHRHRTGHHHPHHQLHQHHHHHHRHTKHHRIPAHKQE", "text": "FUNCTION: Negatively regulates proliferation of neuronal precursor cells, thereby controlling the timing of postembryonic neurogenesis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKVLAAIALSATAFTGAVAAVLTQEAFLNNPRIHHDQEKYLIELAPYRTRWVTEEEKWALKLDGVNFIDITEEHNTGFYPTLHSASYVKYPPKMQYAEEVAALSKNLSKENMKANLERFTSFHTRYYKSQTGIQSATWLYDQVQRVVSESGAAEYGATVERFSHPWGQFSIIARIPGRTNKTVVLGAHQDSINLFLPSILAAPGADDDGSGTVTILEALRGLLQSDAIANGNASNTVEFHWYSAEEGGMLGSQAIFSSYKRDRREIKAMLQQDMTGYIQGALNAGVEEAIGIMVDYVDQGLTQFLRDVVTAYCSVGYLETKCGYACSDHTSASKYGYPAAMATEAEMENTNKKIHTTDDQIKYLSFDHMLEHAKLTLGFAFELAFAPF", "text": "FUNCTION: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily."}
{"protein": "MAEVKLLGFWYSPFSHRVEWALKIKGVKYEYIEEDRDNKSSLLLQSNPVYKKVPVLIHNGKPIVESMIILEYIDETFEGPSILPKDPYDRALARFWAKFLDDKVAAVVNTFFRKGEEQEKGKEEVYEMLKVLDNELKDKKFFAGDKFGFADIAANLVGFWLGVFEEGYGDVLVKSEKFPNFSKWRDEYINCSQVNESLPPRDELLAFFRARFQAVVASRSAPK", "text": "SIMILARITY: Belongs to the GST superfamily. HSP26 family."}
{"protein": "MPELPEVETTRRGIAPHILHHPITAVTLRHTQLRWPIDKALSRNLPGRTLVRADRRGKYLLLAVDDGRTLIWHLGMSGSLRIVEPTEPPGKHDHIDLRFAHGRVLRYHDPRRFGAFLATADDPAQHALICHLGPEPLTDDFNGEYLYERSRKRSTAVKSWIMDSRVVVGVGNIYANESLFLAKIHPLRAAGKLTRPACHRLADIIKAVLARSITQGGTTLRDFVGGDGKPGYFAQQLNVYGRGGEPCPVCAKPLTEKPLSQRTTVYCTHCQN", "text": "FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. SIMILARITY: Belongs to the FPG family."}
{"protein": "MSEDPKNIKRALISVYDKTGLEDLARALDNAGVEIVSTGSTAKKIADLGIDVTPVEKLTGFPECLEGRVKTLHPRVHAGILADTRKEDHLKQLEELEVEPFQLVVVNLYPFRETVASGADFDGCVEQIDIGGPSMVRAAAKNHPSVAVVVDPARYGDVADAVANGGFTLEERRGLARDAFLHTADYDAAVSAWFVDQLSDGDVTTPLRYGENSHQSATVTRIGTTGLANAKQFNGKEMSYNNYQDADAAWRAAWDHERPCVAIIKHANPCGIAVSEESIAAAHRAAHACDPMSAFGGVIAVNREVTVEMAEQVKEIFTEVIVAPSYEEGAIEVLKAKKNLRVLQAEHEAPKEEVKYISGGMLTQEPDTYQAEGDNPANWTLAAGEALNESDLAQLEFAWRSVRAVKSNAILLAKDNATVGVGMGQVNRVDSAKLAVERANTLADGANRAEGSFAASDAFFPFADGLEVLLEAGVKAVVQPGGSIRDEEVIEAAKKAGVTMYFTGTRHFFH", "text": "SIMILARITY: Belongs to the PurH family."}
{"protein": "MASTISAYKEKMKELSVLSLICSCFYTQPHPNTVYQYGDMEVKQLDKRASGQSFEVILKSPSDLSPESPMLSSPPKKKDTSLEELQKRLEAAEERRKTQEAQVLKQLAERREHEREVLHKALEENNNFSRQAEEKLNYKMELSKEIREAHLAALRERLREKELHAAEVRRNKEQREEMSG", "text": "FUNCTION: Exhibits microtubule-destabilizing activity, which is antagonized by STAT3. SUBCELLULAR LOCATION: Golgi apparatus Cell projection, growth cone Cell projection, axon Cytoplasm, cytosol. SUBCELLULAR LOCATION: Golgi apparatus Cell projection, growth cone Cell projection, axon Cytoplasm, cytosol. SIMILARITY: Belongs to the stathmin family."}
{"protein": "MRLFYRYQDLAPQLVPLDYTTSPKVKVPYELIGSMPELKDNPFRQRIAQVFSQDGDGHMTLENFLDMFSVMSEMAPRDLKAYYAFKIYDFNNDNYICAWDLEQTVTRLTRGELSAEEVTLVCEKVLDEADGDQDGRLSLEDFQNMILRAPDFLSTFHIRI", "text": "FUNCTION: Acts as an auxiliary subunit of the sensory mechanoelectrical transduction (MET) channel in hair cells (PubMed:34089643). Plays a role in regulating hair cell MET channel localization and function (PubMed:34089643)."}
{"protein": "MTWTYILRQSDLPPGEMQRYEGGSEPVMVCNVDGEFFAVQDTCTHGDWALSEGYLDGDVVECTLHFGKFCVRTGKVKALPACKPIKVYPIKIEGDEVHVDLDNGELK", "text": "FUNCTION: This protein seems to be a 2Fe-2S ferredoxin. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin component family."}
{"protein": "MSCARALAACCLWRLRTGALQPLSAYGRRISVRFCSSGMTLDNINREAVDRIIRVDHAGEYGANRIYAGQMAVLGRTSIGPVIQKMWDQEKDHLKKFNELMVAFRVRPTVLMPFWNVVGFALGAGTALLGKEGAMACTVAVEESIAHHYNNQIRTLMEKEPEKYEELLQVIKKFRDEELEHHDIGLEHDAELAPAYVVLKSVIQAGCKVAIYLSERL", "text": "FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6- methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Involved in lifespan determination in a ubiquinone- independent manner. Plays a role in modulating mitochondrial stress responses, acting in the nucleus, perhaps via regulating gene expression, independent of its characterized mitochondrial function in ubiquinone biosynthesis (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ7 family."}
{"protein": "MALEPSRYLDKKTWKMTPAMIRARQPYFKKNMIALGLLLGITTGVYVYTFNLSHKDNDFIDVPIPPIDEKELAVLQKEFNDKKN", "text": "FUNCTION: Required for assembly of cytochrome c oxidase (complex IV). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the COA3 family."}
{"protein": "MGRSMLPEQQEDVSRKSKKEKKSKKDKKRKLEAEAEVVVVEAAAATSTDEATKSSKKKRAKGDLGQGEEAENGGGKVVAVTGKGSADAKYAPLSSFAATALPPQVLDCCKGFERPSPIQAYAWPYLLDGRDFIGIAATGSGKTIAFGVPALMHVRRKMGEKSAKKGVPRVLVLSPTRELAQQIADVLCEAGAPCGISSVCLYGGTSKGPQISALKSGVDIVIGTPGRMKDLIEMGICRLNDVSFVVLDEADRMLDMGFEPEVRAILSQTASVRQTVMFSATWPPAVHQLAQEFMDPNPIKVVIGSEDLAANHDVMQIVEVLDDRSRDSRLVALLDKYHKAQRNRVLVFVLYKREATRVETMLQRRGWSAVSVHGDKAQHDRTKALSLFKEGSCPLMIATDVASRGLDIPDVEVVINYSYPLTTEDYVHRIGRTGRAGKKGVAHTFFTQENKGLAGELVNVLREAGQVVPPALTKFGTHVKKKESQIYGSHFKEIKADAPKSTKITFGDSDED", "text": "FUNCTION: ATP-dependent RNA helicase required for 60S ribosomal subunit synthesis. Involved in efficient pre-rRNA processing, predominantly at site A3, which is necessary for the normal formation of 25S and 5.8S rRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily."}
{"protein": "MSVDEKYDAACELLYRLDPTKVKTHLQNLIALEPEIAEGLLSSIDIPLTIKKDTDANNKEFLCCDYNRDIDSHRSPWSNQYFPELSAEDLKESPFPSEPLRELEVACNNSFELYRDLYYEGGYTSTYLWDVDESTDFAGVILFKKAESDDSKWDSIHVISATHDEEGMEVTYNVTTTVILHLENLSKEQQLSLSGNLTRENSKTVKLQNVSTVEQLVPAHSSSLGSMIEDIESKLRSMLEIVYFEKTLDIYNVLRERNDDSTKLQKEQHSELIENFQKL", "text": "FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus Note=Septum. SIMILARITY: Belongs to the F-actin-capping protein beta subunit family."}
{"protein": "MLILSRKENESIIIGEGIEIKVVQTGKGYAKIGIEAPKSLMILRKELVQQVKDENLHSVVQNDIKLDDLSKKLIK", "text": "FUNCTION: A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its function is probably anatagonized by FliW. Inhibits translation of flaA mRNA in vitro (PubMed:27353476). Involved in post-transcriptional regulation of flagellin biosynthesis (PubMed:27353476). FUNCTION: A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Binds mRNA; 77% of enriched bound RNA is for flagellin A (flaA) while another 13% encodes other flagellar or motility-related genes. Binds mRNA in 5'-UTR or intergenic regions, binds consensus 5'-AAGGA-3' in the loop of a predicted stem-loop structure. Binds at least 2 sites in the 5'-UTR of flaA mRNA and represses its translation; mutation of the binding sites abolishes binding and leads to increased amounts of FlaA protein. Translation repression is antagonized by FliW, probably by its direct binding to CsrA, which allows translation of FlaA and probably other flagellar proteins (PubMed:27229370). Influences the localization of flaA transcripts to poles of short, probably elongating, cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family."}
{"protein": "MAAAVNLELDPIFLKALGFLHSKSKDSAEKLKTLLDESLARGIDSSYRPSQKDVEPPKISSTKTVSVKQEPKTSSSLPSGNNNGKVLTTEKVKKEGEKRPADKMKSDITEGADVPKKPRLEKPETRSSPITVQTSKDLAMADLSSFEETSADDFAMEMGLACVVCRQMTVASGNQLVECQECHNLYHQDCHKPQVTDKEVTDPRLVWYCARCTRQMKRMAQKTQKPPQKPAPTVVSVAPAVKDPLVKKPETKLKPETTFLAFKRSEVKASTVVSGNSSSTNVSSSATSGLIGWAAFAAKTTSAGPSTAKLSSAAQNNSGKPATSSANQKPVGLTGLATTSKGGIGSKIGSSNSTSPTVPLKPPPPLTLGKTGLSRSVSCDNVSKVGLPSPSSLVPGSSSQLSGNGNSGTSGPSGSTTNKTASEPSTSPSASLKGPTSQESQLNAMKRLQMVKKKAAQKKLKK", "text": "FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'- box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Integrator subunit 12 family."}
{"protein": "MKIYSYNELKTRFAEYAKPGEFSITSADTFRIIRLHYDEKQGCLFAFCNTNIEKRVLQFYFKVKLNLYSYKQCYDKHIFPSCRNKCISYTTFVAPGVEGNCLNKINVIKYERNKAAPSDNAACLDKFLHNVNRVHMQTPFVEGAYMRFKKTQRCQNNYVGGSTTRMFNLQHFYEDFELVDEMTLTSGIMPVLSCYDIETHSDGHNMSKASVDCIMSIGFVVYKNDEYARFCFMYHKLPTEIPETHDDDTHVVMFQNEVDMITAFFDMIKITNPDVILDFNGDVFDLPYILGRLNKTKMLLKRYDLPAAAPTTKLFINKLGNKVDTYYFNYYIHIDLYKFFSSDSNQHKVENFQLNTISSYYLGENKIDLPWTEMVKMYNTRRLDVIAKYNVQDCMLPIKLFVKLKMADSVYSQCILHRLCTDDVICNISHLISVACFYAAITNTRINESTGKEEPDPYFFNKNDLSIISGQFNADKATAGISNLKRKLTPLKNIPKDAINLGPANQTVKYKGGKVLQPRASIYKNAFSLDFNSLYLTIMIAICACLSNLVLCEDGNVYLNHNSRAIVVKLLLKLLSERCKFKKNRDNQSESAFLYDLYDQKQNSVKRTANSIYGYYGIFYKVLANYITRVGRNQLRRAISLIEGLSNDPEILKKFNLNSIGFKVVYGDTDSTFVLPTFNYNEIFDETDTLKQICTHVETRVNSSFTDGYKMAFENLMKVLIILKKKKYCYLNSENKIVYKGWLVKKDMPVFMRIAFRTAVEQILRHLDINKCLQSLQASFYEYYDEFAKSKPMTDYSFSMTYNDNPGKKRKSADDNNEGPSPKRRVITVARHCREILVNKGTDFVPGNGDRIPYLLIDIEGKVTEKAYPLRLFDPVKMRISWIKHMGILCTFMNELLEIFGDEQKDNLAKCFTAIMQKYMQNQLYDRKEPVLVKINQKKCSVKRKRDDDDDNNDDDDDDGCDSSDSENDTQCANNTYKFCLYKIKK", "text": "FUNCTION: Replicates the viral genome, host DNA polymerases cannot substitute for the viral enzyme in this process. SIMILARITY: Belongs to the DNA polymerase type-B family."}
{"protein": "MVLVTQNAPNFIAPAILKNNQIVEQFDLKKYSNGQSTVLFFWPMDFTFVCPSEIIEFNKLHSEFKKRNVKIVGVSIDSVYVHQAWQNTLPKNGGIGKINFPMVSDVKHDIQKSYGIQHPNLGIALRASFLIDSNWIIRHQVVNDLPFGRNITDMIRMVDALDFHNKFGEVCPANWKKGEEGITASSEGVSQYLSKYS", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily."}
{"protein": "MRVYYDRDADLARILDRKIAIVGYGSQGHAHALNLRDSGIKNVAVALRAGSPTAKKAEGEGLKVMTVAEAAAWADLIMILAPDEHQAAIYKNEIALNIRDGAALLFAHGLNVHFGLIEPKDTIDVLMVAPKGPGHTVRGEYQKGGGVPCLIAVHHNATGNALDLGLAYASAIGGGRSGIIETNFREECETDLFGEQAVLCGGTVELVRAGFETLVEAGYAPEMAYFECLHELKLIVDLMYEGGIANMNYSISNTAEYGEYVTGPRIITPETKAEMKRVLEDIQSGKFVRDFMLENAVGQPSFKATRRRSAEHQIEEVGARLRGMMPWIAKNKLVDQAKN", "text": "FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. SIMILARITY: Belongs to the ketol-acid reductoisomerase family."}
{"protein": "MDKTTVYLPDELKAAVKRAARQRGVSEAQVIRESIRAAVGGAKPPPRGGLYAGSEPIARRVDELLAGFGER", "text": "FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin VapC26."}
{"protein": "MYMLSSDERARLKWACRRGMLELDVIIMPFFEECLDDLPDQEQRDFVSLLTSDDPDLFTWMMGHGRSENPAHAAMVDKIVAHNNSKLR", "text": "FUNCTION: An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins. Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH and other flavinylated proteins as well. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SdhE FAD assembly factor family."}
{"protein": "MASESSIPLYDCLIIGGGIAGLSSALSLVRTLHTAVVFDEGIHRNDQAPHLATVPTWDSQDPKRFRDAAKLNILSKYSTVEFANVKLEKFNKALGKPFLTKVFGHDYVVLPSKYFDDIKRASPQSLSFFQALSDGLNMEASVGHLYASTTEIDVVVKHLNPRLTQLTPLLCDEAEYAIEREVGALPDWKKFNVSNLIAAIVHRTTNRILVGKELCRNEEYLAITTKFSRSLFISGIFWNFVRLGPLRKLVAWLTIGLHLRDRNAAAKVLLPHVLARRQEKEAGVDVATKYPDALQWTIDTAPSFPGDDEPLHQVYHMLHLTFAASSASGVGVTQCLLNVLAYPEYLEPLRDEISTVVARHGGWTDKALSQMALLDSFIRETMRLHPAGSFMDDHFRFHDGLTLPKGTNIIAPALAIHYDPDNYEDAHRFDGFRFARYRQKQGENHRWLASTIDQKFLQFGYGNHACPGRFYAIRKIKLVLAKLIMDYDFKWAQPRPVHDRPEDFAIEAQLVAAPDAEILIRSRNLSN", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells (PubMed:25302411). The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues (PubMed:25302411). One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine (PubMed:25302411). After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT (PubMed:25302411). In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as tailoring enzymes to produce the intermediate dechloroaspirochlorine (PubMed:25302411). Ultimately, chlorination of dechloroaspirochlorine by the halogenase aclH is the last step in the aspirochlorine pathway (PubMed:25302411). SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "AFGTILKALAKIAAKVVKKLATKPGATYMLKQNLQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 02 subfamily."}
{"protein": "MAKELRFGDDARQQMLAGVNALADAVKATMGPSGRNVVLERSFGAPTVTKDGVSVAKEIEFENRFKNMGAQMVKEVAAKTSDTAGDGTTTATVLARAIVVEGHKAVAAGMNPMDLKRGIDKAVAAVTKKLQEMSKPCKDGKAIAQVGTISANSDQAIGSIIAEAMEKVGKEGVITVEDGNSLENELAVVEGMQFDRGYISPYFINNQQNMSAELEHPFILLVDKKISTIRDMLSVLEAVAKSGPSLLIIAEDVEGEALATLVVNNMRGIVKVCAVKAPGFGDRRKAMLQDIAILTAGEVISEEVGTSLESATLDSLGTAKRVVVTKENTTIIDGEGKAADINARITQIRAQMEETTSDYDREKLQERVAKLAGGVAVIKLVLLPNRMKRKARVEDALHATRAAVEEGIVAGGGVALIRAQKALDGLKGENADQDMGINILRRAIESPLRQIVANAGYEPSVIVNKVAESKDNFGFNAATGEYGDMVEMGILDPTKVTRTALQNAASVASLMLTTECMVADLPKKEEPMGAGEMGGMGGMGGMGGMM", "text": "FUNCTION: May play a protective role against the defense mechanisms generated by the infected macrophages. FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the chaperonin (HSP60) family."}
{"protein": "MSTPSPQLLVAAAQQTLGMGKRRGPPRAVCLHLAGEVLAVARGLKPALLYDCSSAGAPEIQSYLEKLRGLGFPTQGLHVLEIAENSLIVHPEYVRRHLEQVLLGSIAFVDVSGSQPYPAVCSLDQLQDFKALVVEIITHLQGLQRDRSLAVSCSRLCSSAWNLCTVFGILLGYPVPYTFHENQGEDNCLAQTPLRVFTARISWLCCQPPVLLYSFSVPESLFLSLRDILNTWEKDLRTRCRTQNDFADLSISSEIVTLPAVAL", "text": "SIMILARITY: Belongs to the UPF0739 family."}
{"protein": "MDVIGRQHLRQMWDDLAEVYDKKTALIFESAQGKVRQFSYSELNEEINRAANLFHACGIKKGDHVALHLDNCPEFFFCWFGLAKIGAVMVPINARFMYEESAWIINHCQAHFVVTSDNFSPIYQPMLHDKHSPLTQLFLITENCLPTEQGVVDFLSEKAKHPVTLNHHTPLSVDDTAEILFTSGTTSQPKGVVITHYNLRFAGYYSSWQNALREDDIYLTVMPAFHIDCQCTASLPAFSVGATFVLLEKYSARAFWKQILKYQATVTECIPMMMRTLMAQPVSPDEKQHKLREVMFYLNLADEEKDAFIERFNVRLLTSYGMTETIVGLIGDRPGDKRRWPSIGRPGFCYQAQIRDKQNQQVPNGVVGEICVKGEPGKTLFKEYYNRPDATEKALEPDGWLHTGDYGYQDDEGFFYFVDRSCNMIKRGGENVSCIEIENIIASHPKIQDVAVIGVPDDIRDEAIKAFVVLVDGETLSEEAFFAFCEQNMAKFKVPSAVEFKQGLPRNCSGKVIKKHLQ", "text": "FUNCTION: Catalyzes the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has activity toward crotonobetaine and gamma-butyrobetaine. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MAQNLSCENWLATEAILNKYYLSAFYAIEFIFGLLGNVTVVFGYLFCMKNWNSSNVYLFNLSISDFAFLCTLPILIKSYANDKGTYGDVLCISNRYVLHTNLYTSILFLTFISMDRYLLMKYPFREHFLQKKEFAILISLAVWALVTLEVLPMLTFINSVPKEEGSNCIDYASSGNPEHNLIYSLCLTLLGFLIPLSVMCFFYYKMVVFLKRRSQQQATALPLDKPQRLVVLAVVIFSILFTPYHIMRNLRIASRLDSWPQGCTQKAIKSIYTLTRPLAFLNSAINPIFYFLMGDHYREMLISKFRQYFKSLTSFRT", "text": "FUNCTION: Receptor for succinate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSIEEEDTNKITCTQDFLHQYFVTERVSIQFGLNNKTVKRINKDEFDKAVNCIMSWTNYPKPGLKRTASTYLLSNSFKKSATVSLPFILGDPVCMPKRVESNNNDTCLLYSDTLYDDPLIQRNDQAGDEIEDEFSFTLLRSEVNEIRPISSSSTAQILQSDYSALMYERQASNGSIFQFSSP", "text": "FUNCTION: Potential transcriptional regulator that is required to activate expression of a number of early meiotic genes including HOP1."}
{"protein": "MKYDNLLDRFIKYVKVNTRSDPDSETTPSTESQEAFALTILKPEMEAIGLQDVHYNPVNGYLIGTLPANNPTLTRKIGFIAHMDTADFNAENVNPQIIDNYQGGDITLGSSNYKLDPKAFPNLNNYIGQTLITTDGTTLLGADDKSGIAEIMTAIEFLTSQPQIEHCDIKVAFGPDEEIGVGADKFEVADFEVDFAYTMDGGPLGELQYETFSAAALEVTFLGRNVHPGTAKDQMINALELAIDFHEKLPAKERPEYTDGYQGFYHLTGLTGTVEEARASYIIRDFEEASFEARKVKVENIAQSMNAHLGTKRVLVELNDQYYNMKKVIEKDMTAIELAKEVMEELAIKPVIEPIRGGTDGSKISFMGIPTPNIFAGGENMHGRFEFVSLQTMERAVDVIIGLVCKA", "text": "FUNCTION: Cleaves the N-terminal amino acid of tripeptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20B family."}
{"protein": "MSTENTLSVADLARENVRNLVPYQSARRLGGNGDVWLNANEFPTAVEFQLTQQTLNRYPECQPKAVIENYAQYAGVKPEQVLVSRGADEGIELVIRAFCEPGKDAILYCPPTYGMYSVSAETLGVERRTVPALENWQLDLQGISDNLDGTKVVFVCSPNNPTGQLINPQDLRTLLELTRGKAIVVADEAYIEFCPQATLTGWLVEYPHLVILRTLSKAFALAGLRCGFTLANEEVINLLLKVIAPYPLSTPVADIAAQALSPQGINAMRDRVAQTVQERQYLVNALQQTACVEHVFDSETNYILARFTASSSVFKSLWDQGIILRDQNKQPSLSGCLRITVGTRQENQRVIDALRAEPV", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily."}
{"protein": "MLAAKRYAEALIKLGQEEGKLEIFYEQLFKMFEIIKNNNEFNTIWFDLEMKRSEKKQRIKVFFGGDIDSYILNLLYLLIDKRREIILTYIPFYYKEIYDKIVGNVDVQVIVAHEIGSDVLNKISKWLLKKYGVKNPRFIVKVDKSIIGGIKLLFNNIEVDASIKGALDSMRKELVKIAIL", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase delta chain family."}
{"protein": "MEWLIYIVILFVGIAAGAFFGISVGRKRAEEALEKKLKAAKEDAESIIKSAEKEASEIKKKAIIEAREEAHQIREEIEKERKKREEEIKQLEERLLKREEMLSKREELIDKRENYVENLKIELESKAKEIEEKAKEIERRFIELAGITHEQAREIVLQEAREKYEHEIAKFFVQIKTRYEDEADKYAKKIIADAIQRYAPEYIGEVTISTVALPNDDMKGRLIGREGRNIRTFEKITGVDLIIDDTPEMVTLSSFNPLRREVARRTIEKLVQDGRIHPARIEEMYEKAKAEVEREIKEAGQDAVITVGVGGLHPEIIKLLGRLKFRTSYGQNVLAHSVEVAQIAGLLAAELGLNVDKAKRGGLLHDIGKAIDHEVEGSHTDIGAEMLKRYGESDEIINMVMAHHGQEEPITPEAAIVAAADAISAARPGARREDVENYIKRLMKLEEIAKSYKYVENAYAIQAGREIRVIVQPDKTDDATIEKLAHDIATRIENELQYPGVLKVVVIREKRSVSYAK", "text": "FUNCTION: Endoribonuclease that initiates mRNA decay. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RNase Y family."}
{"protein": "MTTIAVIGGGQIGEALVSGLIAANMNPQNIRVTNRSEERGQELRDRYGILNMTDNSQAADEADVVFLCVKPKFIVEVLSEITGTLDNNSAQSVVVSMAAGISIAAMEESASAGLPVVRVMPNTPMLVGKGMSTVTKGRYVDAEQLEQVKDLLSTVGDVLEVAESDIDAVTAMSGSSPAYLFLVTEALIEAGVNLGLPRATAKKLAVASFEGAATMMKETGKEPSELRAGVSSPAGTTVAAIRELEESGIRGAFYRAAQACADRSEELGKH", "text": "FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family."}
{"protein": "MTMETLPKVLEVDEKSPEAKDLLPSQTASSLCISSRSESVWTTTPRSNWEIYRKPIVIMSVGGAILLFGVVITCLAYTLKLSDKSLSILKMVGPGFLSLGLMMLVCGLVWVPIIKKKQKHRQKSNFLRSLKSFFLTR", "text": "FUNCTION: Regulatory subunit of TRPV1, a molecular sensor of noxious heat and capsaicin. Positively regulates TRPV1 channel activity via phosphatidylinositol 4,5-bisphosphate (PIP2). Binds various phosphoinositide, including phosphatidylinositol 4,5-bisphosphate (PIP2), but not phosphatidylinositol (PI) (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MKVTFEELKGAFYRVLRSRNIAEDTADACAEMFARTTESGVYSHGVNRFPRFIQQLDNGDIIPDAKPQRVTSLGAIEQWDAQRAIGNLTAKKMMDRAIELASDHGIGLVALRNANHWMRGGSYGWQAAERGYIGICWTNSIAVMPPWGAKECRIGTNPLIVAIPSTPITMVDMSMSMFSYGMLEVNRLAGRELPVDGGFDDNGQLTKEPGVIEKNRRILPMGYWKGSGLSIVLDMIATLLSNGSSVAEVTQENSDEYGVSQIFIAIEVDKLIDGATRDAKLQRIMDFITTAERADDNVAIRLPGHEFTKLLDDNRRHGITIDDSVWAKIQAL", "text": "FUNCTION: Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family. DlgD subfamily."}
{"protein": "MKKLLPLFVSAALGTLSSAVWAENLAEIYNQAKENDPQLLSVAAQRDAAFEAVTSSRSALLPQINLTAGYNINRSDQAPRESDLLSAGINFSQELYQRSSWVSLDTAEKKARQADSQYAATQQGLILRVAKAYFEVLRAQDNLEFVRAEKAAVGRQLEQTKQRFEVGLSAITDVHDAQAQFDGVLADEVLAENSLTNSYEALREITGQEYSKLAVLDTKRFAASRTTESSEALIEKAQQQNLSLLAARISQDVARDNISLASSGHLPSLTLDGGYNYGNNSNDNAKNTSGEEYNDFKIGVNLKVPLYTGGNTTSLTKQAEFAYVAASQDLEAAYRSVVKDVRAYNNNINASIGALRAYEQAVISAKSALEATEAGFDVGTRTIVDVLDATRRLYDANKNLSNARYDYILSVLQLRQAIGTLSEQDVMDVNAGLKVAKK", "text": "FUNCTION: Outer membrane channel, which is required for the function of several efflux systems (By similarity). Required to export RtxA cytotoxin. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family."}
{"protein": "MSHDSDDKTFPYQKDDAELRRRLTPMQYEVTQHAATERAFTGEYTDTEDAGIYKCVVCSTPLFESGAKFHSGCGWPSYFKPLNGEVIDEKVDYSHGMVRVEVRCNNCGAHLGHVFEDGPRDKTGLRYCINSAALNFESRPENE", "text": "SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family."}
{"protein": "MSQQPEYTDWQQIVDLVKHSVEQKQHDMLLTMLMTPDEREALVSRVNIVRELLKGELSQRQISQMLGVGIATITRGSNELKLKSDEDKARLNQLLEGTKKGG", "text": "FUNCTION: This protein is an aporepressor. When complexed with L- tryptophan it binds the operator region of the trp operon and prevents the initiation of transcription. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TrpR family."}
{"protein": "MVFGENQDLIRTHFQKEADKVRQMKTNWGLFTRSRMIAQSDYDFVVTYEQAETEQDRSTVLSVFKEKAVYAFVHLMSQISKDDYVRYTLTIIDDMLREDVSRTKIFEEVAVLLKRSPFSFFLGLLHRQDQYIVHTTFSVLTKMAVFGNIKVTGDELDYFMGSLKEAITRGIANDYIATAVRCMQTLFRIDPYRVSFVNISGYESLSHALYSTRKCGFQIQYQIIFCMWLLTFNGHAAEVALCGNLIQTISTILGTSHKEKVIRIVLATLRNLIASNEDEYMKKQAARQMVQNQILVKLDHLENRKFQDVDLIDDMAFLQKELKKVVEVLTSFEEYESELRHGALFWSPPHKCEIFWTENAHKLNDNRQELLKMLITMLEKSNDPLVLCVAANDIGEFVRYYPRGKMHVEQLGGKEALMRLLTVPDPNVRYFALLAAQKLMVNHWKDLGLEI", "text": "FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity). SIMILARITY: Belongs to the V-ATPase H subunit family."}
{"protein": "MPQELVYTLQQLADLLKVEVQGNTETPISGVEEISEAQSHHVTFLDNEKYSRFIKNTEAGAIILSKAQAQKYGHLNKNFLIVSEFPSIAFQKCIELFIPPIDSGFPGIHPTAVIHPTAHIGKDVFLEPYAVICQHAQIGDSSHIGAGSVIGAFSTLGEHCYVHPKVVIRERVVIGKRVIVQPGAIIGACGFGYITNAFGRHKHLKHLGQVIIEDDVEIGANTTIDRGRFKNSVIREGTKIDNQVQIAHHVEVGKHSMIVAQAGIAGSTKIGNHVIIGGQTGITGHISITDHVIMMAQTGVTKSISSPGIYGGAPARPYQEIHRQVAKIRGLPKLEERLGMLEEKVKGLSAQSEEAQITP", "text": "FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3- hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD subfamily."}
{"protein": "MDLNLRHAVIANVSGNSQEELEHTIVDAIQSGEEKMLPGLGVLFEVIWQHATESDKTEMLETLEQGLKAK", "text": "SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspI family."}
{"protein": "MLGEEAEPQWISEEVKTGTTIIAIEFNGGVVLGSDSRVSAGDSVVNRVMNKLSPLHDKIYCALSGSAADAQTIAEMVNYQLDVHSLEIDEDPQVRSAATLVKNISYKYKEELSAHLIVAGWDRRDGGQVFATLGGLLTRQPFAIGGSGSSYVYGFVDAEYRRGMTKEECQKFVVNTLALAMNRDGSSGGVAYIVTIDEHSTDEKVILGNDLPTFFDQ", "text": "FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MLDPFSEKAKELLKEFGSINDFLNSIPRIVDVEEVIERVKIASDRKLLEGFVDIEDIKDLAQFYALLGALSYSPYGLELELVKKANILLYSERIRREKEIRPEEISLRINKAIEFPIDDLKKIERVFGKLPEYTIHLAEFLDLIPGERLSEYYIYNGNVYLRKEDLIKVWMKAFERNIEKSVNMLYEIRDELPGFFREVLGGIKEVAEQEFGKSGEVKAGTLRPDLFPPCVKNALKGVPQGLRNYAITVLLTSFLSYARICPNPPRRNVRVKDCIDDIRIITDEILPLIIEAANRCSPPLFEDQPNEIKNIWYHLGFGYTANPKLEDSGNSTWYFPPNCDKIRANAPQLCTPDKHCKYVRNPLTYYLRRLYLEGRKNASKGGNERGEKRVLQQ", "text": "FUNCTION: Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair. Displays gap-filling and strand-displacement activities. SIMILARITY: Belongs to the eukaryotic-type primase large subunit family."}
{"protein": "MMQSHIDFALATPEILLLVLALAVLLIDAVSSHPDRKTTYVLSLATLAILTVVSLFQWSNGVSGKTFNGMYVTDSFSHLLKITSYIAVAVTLIYGRVYAQSRDMLRGGELYVLTLLALLGQMVMISAGSLVSVYLGLELMSLALYALIALRRDDVVATEAAMKYFVLGALASGFLLYGMSMVYGSTGHLDLAEISRVIGSGQAKELPLVFGIVFLVAGLAFKLGAVPFHMWVPDVYQGSPTAVTLILGGAPKLAAFAMTLRLLVDGLHGLAADWQSMLMILAVLSLAIGNLTAIVQTNFKRMLAYSTISHMGFVLLGLASGVVVGKAEAASAAYGASLFYMITYVLTTLASFGIVLLLSRQGFECEQIDDLKGLNRRSPWHALIVLLLMFSLAGIPPLVGFYAKLAILQAVIESGHVALAVVAVLFSLIGAFYYLRVVKVVYFDEPVAEDAPLSATCVQRGLLSVNGALILILGILPGGLMALCVQVIKTSFAGL", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."}
{"protein": "MPVQGSQRRLLGSLNSTPTATPHLGLAANQTGARCLEVSVPDGLFLSLGLVSLVENVLVVTAIAKNRNLHSPMYCFICCLALSDLLVSGSNMLETAVTLLLEAGALAARAAVVQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVLCSTLFIAYYDHAAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRLAHQGFGLKGAATLTILLGIFFLCWGPFFLHLTLIVLCPQHPTCSCIFKNFNLFLALIICNAIIDPLIYAFRSQELRRTLKEVLLCSW", "text": "FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MAAVFDLDLETEEGSEGEGEPELSPADACPLAELRAAGLEPVGHYEEVELTETSVNVGPERIGPHCFELLRVLGKGGYGKVFQVRKVQGTNLGKIYAMKVLRKAKIVRNAKDTAHTRAERNILESVKHPFIVELAYAFQTGGKLYLILECLSGGELFTHLEREGIFLEDTACFYLAEITLALGHLHSQGIIYRDLKPENIMLSSQGHIKLTDFGLCKESIHEGAVTHTFCGTIEYMAPEILVRSGHNRAVDWWSLGALMYDMLTGSPPFTAENRKKTMDKIIRGKLALPPYLTPDARDLVKKFLKRNPSQRIGGGPGDAADVQRHPFFRHMNWDDLLAWRVDPPFRPCLQSEEDVSQFDTRFTRQTPVDSPDDTALSESANQAFLGFTYVAPSVLDSIKEGFSFQPKLRSPRRLNSSPRAPVSPLKFSPFEGFRPSPSLPEPTELPLPPLLPPPPPSTTAPLPIRPPSGTKKSKRGRGRPGR", "text": "FUNCTION: Phosphorylates specifically ribosomal protein S6 (PubMed:29750193). Seems to act downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression in an alternative pathway regulated by MEAK7 (PubMed:29750193). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily."}
{"protein": "MGLDKVVKDIMDKAEADSRDITAKAAAEAAEIKKSAEAEAKQIIAAENARAEQAISKMRQRELSSAKLDVKKAKLNSEKDVLAETHEAFVRQLSTLPREKKADLLQKLVKLAKKDIPQGKIFTNAADADLVKDSGYEYGGNVKCIGGIVVTSVDGSVNLDYTFDSILEDVWTSSMKPVSDILFGSR", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase E subunit family."}
{"protein": "MELTMASTMSLALLVLSAAYVLVALRRSRSSSSKPRRLPPSPPGWPVIGHLHLMSGMPHHALAELARTMRAPLFRMRLGSVPAVVISKPDLARAALTTNDAALASRPHLLSGQFLSFGCSDVTFAPAGPYHRMARRVVVSELLSARRVATYGAVRVKELRRLLAHLTKNTSPAKPVDLSECFLNLANDVLCRVAFGRRFPHGEGDKLGAVLAEAQDLFAGFTIGDFFPELEPVASTVTGLRRRLKKCLADLREACDVIVDEHISGNRQRIPGDRDEDFVDVLLRVQKSPDLEVPLTDDNLKALVLDMFVAGTDTTFATLEWVMTELVRHPRILKKAQEEVRRVVGDSGRVEESHLGELHYMRAIIKETFRLHPAVPLLVPRESVAPCTLGGYDIPARTRVFINTFAMGRDPEIWDNPLEYSPERFESAGGGGEIDLKDPDYKLLPFGGGRRGCPGYTFALATVQVSLASLLYHFEWALPAGVRAEDVNLDETFGLATRKKEPLFVAVRKSDAYEFKGEELSEV", "text": "FUNCTION: Involved in serotonin biosynthesis. Catalyzes the conversion of tryptamine to serotonin (PubMed:21080162, PubMed:23053415, PubMed:20150424, PubMed:23521226). Accumulation of serotonin may play a role in innate immunity (PubMed:20150424). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MDNASFSEPWPANASGPDPALSCSNASTLAPLPAPLAVAVPVVYAVICAVGLAGNSAVLYVLLRAPRMKTVTNLFILNLAIADELFTLVLPINIADFLLRQWPFGELMCKLIVAIDQYNTFSSLYFLTVMSADRYLVVLATAESRRVAGRTYSAARAVSLAVWGIVTLVVLPFAVFARLDDEQGRRQCVLVFPQPEAFWWRASRLYTLVLGFAIPVSTICVLYTTLLCRLHAMRLDSHAKALERAKKRVTFLVVAILAVCLLCWTPYHLSTVVALTTDLPQTPLVIAISYFITSLSYANSCLNPFLYAFLDASFRRNLRQLITCRAAA", "text": "FUNCTION: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals. Has a higher affinity for neuropeptide B. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRTVHDDELKKILKIMSPGTSLREGLDNILRAKTGGLIVLGDNEEILDLVDGGFNINSEYSPAYIYELAKMDGALVLTSDRKRILYANAQLMPNQSISTFETGTRHRTAQRVAKQTNKIAIAISQRRNIITVYKGDIKYVLRDSAVILSKANQAIQTLEKYVAVLERVTNNLNILEFQDLATLFDVTTAIQRTEMVMRIVEEIEGYIIELGNEGRLISMQLNELVRSIEQDGVLLIRDYCYDKMEYNDVYKEIQELSAEDLLDLDIIAKELGYVGKSLIDTLVSPRGYRISNKVPRIPSNVIENLVGHFGKLKYILEAGNEELDQVEGIGEARARAIKNGLRRIREQVALNKNL", "text": "FUNCTION: Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. DisA forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation. FUNCTION: Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome, operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis. SIMILARITY: Belongs to the DisA family."}
{"protein": "MRDSMSEADRSSPGSGKTDREDETAENATQDVIAVTPDDERTGLANRLDAHTGDGVRHRAFTCLLFDEDGRVLLAQRADRKRLWDTHWDGTVASHPIEGQSQVDATRQRLAEELGIEPHQYDKLEITDRFEYKRRYLDEGLEWEVCAVLQATLHDTSFDRDPEEVGGAMWVDYEDLYENPRYYRQLRLCPWFEIAMRRDFEGDADPVPDGTRA", "text": "FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IPP isomerase type 1 family."}
{"protein": "MAAAVAAALARLLAAFLLLAAQVACEYGMVHVVSQAGGPEGKDYCILYNPQWAHLPHDLSKASFLQLRNWTASLLCSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPPGGNKTQYDEIGIPVALLSYKDMLDIFTRFGRTVRAALYAPKEPVLDYNMVIIFIMAVGTVAIGGYWAGSRDVKKRYMKHKRDDGPEKQEDEAVDVTPVMTCVFVVMCCSMLVLLYYFYDLLVYVVIGIFCLASATGLYSCLAPCVRRLPFGKCRIPNNSLPYFHKRPQARMLLLALFCVAVSVVWGVFRNEDQWAWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFLTKSGSSIMVEVATGPSDSATREKLPMVLKVPRLNSSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGVGLLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWRRELGVFWTGSGFAKVLPPSPWAPAPADGPQPPKDSATPLSPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMREPGSPAESEGRDQAQPSPVTQPGASA", "text": "FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17965014, PubMed:19114711, PubMed:22194595). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952, PubMed:16829951). May play a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus processed leader peptide gp18 of the envelope glycoprotein gp130 dependently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Endosome membrane; Multi-pass membrane protein Membrane; Multi-pass membrane protein; Lumenal side Note=targeted through the entire secretory pathway to endosomes/lysosomes (PubMed:15998642). SIMILARITY: Belongs to the peptidase A22B family."}
{"protein": "MATQRKIIHIDMDCFYAAIEMRENPALIGKPVAVGGSVEGRGVLTTCNYEARKFGLHSAMPTAQALKRCPNLILVPVNMPLYKAVSEQIHQIFRRYTDIVEPLSLDEAYLDVTDCRQCSGSATWIAQEIRDAIWNELHLTASAGIAPLKFLAKIVSDQNKPNGQFVISPENMTAFIYDLPLKKIPGVGKVTNEKLAQLGLHTCGDIQHSDKAFIYKTFGKFGQRLWEFSHAIDNRKIEANRPRKSLAVENTLPTDIWHLAEAEQIVDELFKKLVFRLQRNWGERSLQEFKKLAIKLKFGDFTQTTLERTTDGLSRERFIELLQQVWQRTNRRSVRLIGLSVHYPTEKVKKQLNLWE", "text": "FUNCTION: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DNA polymerase type-Y family."}
{"protein": "MEAPGPAQAAAAESNSREVTEDAADWAPALCPSPEARSPEAPAYRLQDCDALVTMGTGTFGRVHLVKEKTAKHFFALKVMSIPDVIRRKQEQHVHNEKSVLKEVSHPFLIRLFWTWHEERFLYMLMEYVPGGELFSYLRNRGHFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILLDRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSGFPPFFDDNPFGIYQKILAGKLYFPRHLDFHVKTGRMM", "text": "SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily."}
{"protein": "MPIATPEVYNEMLDRAKAGKFAYPAINVTSSQTLHAALRGFAEAESDGIVQISTGGAEFLGGQHNKDMVTGAVALAEFAHIVAEKYDVTVALHTDHCPKDKLDGYVRPLIAVSEERVKAGRNPLFQSHMWDGSAETLADNLSIAQELLARARAARIILEVEITPTGGEEDGVSHEINDSLYTTVDDAVRTVEALGLGEKGRYLLAASFGNVHGVYKPGNVVLRPELLKELNEGIASKYGQPAGSKPFDFVFHGGSGSTAEEIATALENGVVKMNIDTDTQYAFTRPVVDHMFRNYDGVLKVDGEVGNKKTYDPRTWGKLAEAGMAARVVEACGHLRSAGQKIK", "text": "FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase family."}
{"protein": "MSRPRRRGRDINGVLLLDKPQGMSSNDALQKVKRIYNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGQIVEERPVTFSAEQLAAALDTFRGDIEQIPSMYSALKYQGKKLYEYARQGIEVPREARPITVYELLFIRHEGNELELEIHCSKGTYIRTIIDDLGEKLGCGAHVIYLRRLAVSKYPVERMVTLEHLRELVEQAEQQDIPAAELLDPLLMPMDSPASDYPVVNLPLTSSVYFKNGNPVRTSGAPLEGLVRVTEGENGKFIGMGEIDDEGRVAPRRLVVEYPA", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1 subfamily."}
{"protein": "FLPAVLRVAAKVVPTVFCLISKKC", "text": "FUNCTION: Has antibacterial activity against E.coli ATCC 25992 (MIC=49 uM), E.coli CIB 84492 (MIC=25 uM), S.aureus ATCC 25923 (MIC=6 uM) and S.aureus CIB 85462 (MIC=3 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MADDGMLLNFTFSDDVVKKSEPKLKGGTWRDRLSAKKIAQHRAQPRKPSDGTAAPRPVKNPNRIQVSGTRPAKRQRTDDDHDAGLRDHDRAGQSQHQHQHPRQFISSLFSKNPLPRNAEEPTDEAPAEDAKPTNAPLIDGLDTFTNLGLSPTLAAHLLTKLELKAPTAIQKASISQLLKEESDAFIQAETGSGKTLAYLLPLVQRIMALSHPTNRTDATSTTDAEGQPVVHRDSGLFAIVLAPTRELCKQISVVLEGLLRCAHWIVAGTVIGGEKKKSEKARLRKGLNILVATPGRLADHLENTQALDVSNVRWLVLDEGDRLMELGFEQELQGIIKKLDARQRPSRIPGVPTKRTTILCSATLKMNVQKLGEMSLKDAIHIKADPADEDGDAKPKNDDESAFTVPAQLKQSYAIVAAKLRLVTLTAFLKRTFMRKGSVMKAIVFVSCADSVDFHFEVFTRKLQDSDENAEDSDASDTKEKPAAFTHNTIARATAFSNPSNPVTLHRLHGSLPQHVRTSTLASFARNKDASVLVCTDVASRGLDLPNVDLVIEYDPAFSAEDHLHRIGRTARLGRDGRALIFLQPGCEEGYVEILKRGYRDGGKALTRTNADDILKRGFGGNVESENKDWEEKATDWQMDLERWALEKPESLEMARRAYQSHIRAYATHVASERSMFNIKELHLGHLAKAFALRDRPSKINVPGLRQGKDDTKKDYKAARAPAAGKKRKTPGGRDDDDIPAAADTASAAQKMRAKMKEHMAGASEFNLA", "text": "FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7 subfamily."}
{"protein": "MEQNSRALIDGFNRKIDYLRMSVTDRCDFRCVYCMAEDMQFLPRQQILSLEELFQVAERFVALGTRKIRLTGGEPLVRQGIVDLCGRIAALPGLRELCMTSNGSQLPRLAQPLFDAGLSRLNISLDSLDAERFKQLTRTGDLAQVIAGIDAARRAGFQRIKLNCVVLKGRNDDELVDLVRFAIDRELDITFIEEMPLGVISEHERGESFCSSDEVRARLAEQFTLIESTESSQGPARYWRLAEASSTRVGFISPHSHNFCATCNRVRLTVEGRLLLCLGNEHSMDLKQVLRAHPGDAERLEKAIRDSLHLKPYRHHFEVGGDVQILRFMNMTGG", "text": "FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. SIMILARITY: Belongs to the radical SAM superfamily. MoaA family."}
{"protein": "MEFDFDISQSLPDFITKVDNTLNPFNRQLDVTSRKRLQQNLIVIIDRMGMASAKARLLRRLTAQSLKGAITTAAKLGISDHRLYILKETEVNRGLGKVVGILKVGKKKLFVVDYTGAQHECLPLCVLDFYVHESQQRTGNGKLLFEYMLKAENVTPSHLAIDRPSFKFLSFLQKHYGLRDTLPKQVNNFVVFEDLFNLIRKKKSGGITQHQPTSLKPPIPPTGRRCMHFLNLTIWQTR", "text": "FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. SIMILARITY: Belongs to the acetyltransferase ATAT1 family."}
{"protein": "MATVIHSPRDPNTLSNYNNWVSTHITATFDILFEQKKLVGNVVHKLKSITDARSTEIILDTNHVDIGDVKVDGQASHWELLPPLEPYGAALKINLDQGVGLNEMVEVEISVKTTEKCTALQWLTPAQTSNRKHPYMFSQCQAIHARSIFPCQDTPDVKSTIDFNITSPLPVVASGLPVRGIIEKAQPGSKTLYQFHQKLPIPSYLFALASGDISEAAIGPRSVVATSPDKLSECQWELKADTENFIHAIEKIVYPYAWGEYNVLILPPSFPYGGMENPIFTFATPSIISKDRENVDVIAHELAHSWSGNLVTNASWEHFWLNEGWTTYLERRVSLHGEAYRHFSAIIGWKSLADSVEHFGHDHPFTKLVTDLKGKDPDDAFSSIPYEKGFNFLFHLENLLAKDKFDRFIPHYFTKFKGKSLDSYEFKATMLEFFQHDLEASNLLKNVDWDAWFYAPGLPPKPQFDTSLVDVVYELSSKWKSLPDSSFQPRTSDIEGLTANQIVVLLEQILLFERPLTPELSRVLGEVYSLAKSENIEVSNLYFQVGLRAGDDTVYKPTAELLGKIGRMKFVRPLYRNLQKVNRPLAIETFEKNKDFYHPICRAMVEKDLFGKREE", "text": "FUNCTION: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase M1 family."}
{"protein": "MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQPTSY", "text": "FUNCTION: Could accelerate the degradation of some genes transcripts potentially through selective RNA binding. Controls extracellular enzymes, N-(3-oxohexanoyl)-L-homoserine lactone, and pathogenicity (By similarity). Repressor of virulence factors (By similarity). FUNCTION: Could accelerate the degradation of some genes transcripts potentially through selective RNA binding. Controls extracellular enzymes, N-(3-oxohexanoyl)-L-homoserine lactone, and pathogenicity (By similarity). Repressor of virulence factors (By similarity). FUNCTION: Controls extracellular enzymes, N-(3-oxohexanoyl)-L- homoserine lactone, and pathogenicity. Repressor of virulence factors (By similarity). FUNCTION: A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family."}
{"protein": "MVLAKDLKSGMTFLNGEKLLRVMEASHHKPGKGNTIMRMKLKDVRSGSTFDDTYRPEDKFEQAVIETVTAQYLYSMDGIANFMNNETYEQYEIPVEQVKDELLYVLENTDVKIQFYGTEVIGIQLPTTVVLEVTETQPSIKGATVTGSGKPATMETGLVVNVPDFVEAGTKLEINTQTGEYLKRA", "text": "FUNCTION: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the elongation factor P family."}
{"protein": "MDGIKYAVFTDKSIRLLGKNQYTSNVESGSTRTEIKHWVELFFGVKVIAMNSHRLPGKGRRMGPIMGQTMHYRRMIITLQPGYSIPPLRKKRT", "text": "FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
{"protein": "MSEILPYSDEKMGHYGSDGEVGQISFSCRLQDTSSFFGGNQQKRPPKLGQIGRAKRVVIEDDRIDEVLKGVSDKSPSGV", "text": "FUNCTION: Potent and specific cellular inhibitor of CaM-kinase II (CAMK2). Traps Ca(2+)/calmodulin on CAMK2 (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the CAMK2N family."}
{"protein": "MKIFDYENIQLIPNKCIVNSRSECDTTVTLGRHTFKMPIVPANMQTIINDSIAEFLAENGYFYIMHRFDGAARIPFVKKMKERQWISSISVGVKKEEYLFIEELAKQKLASDYITIDIAHGHSNSVIEMIQHIKTHLPETFVIAGNVGTPEAVRELENAGADATKVGIGPGKACITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESSGETKIENGIAYKEYFGSASEFQKGEKKNIEGKKIWIQHKGSLKDTLIEMHQDLQSSISYAGGRDLEAIRKVDYVIVKNSIFNGDAI", "text": "FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily."}
{"protein": "MSGRFVRASKYRHIFGQTCKKELCYDNIKLSNNAWDSNLLSVNPFYLSVNWNAGAGGALAVIPLNERGKLPDQVNLFRGHTAAVLDTDWNPFHDQVLASGGDDSKIMIWKVPEDYTVMEPYEDVHPIAELKGHSRKVGLVQYHPTAANVLASSSADNTIKLWDCEKGVAHVSLKMDVMCQSMSFNADGTRLVTTSRDKKVRVWDPRTDKPVSVGNGHAGAKNPRVVWLGSLDRFATTGFSKMSDRQIALWDPTNLSEPIGGFTTLDTGSGILMPFWDDGTKVIYLAGKGDGNIRYYEYENDVFHYLSEFKSVDPQRGIAFLPKRGVNVSENEVMRAYKSVNDSIIEPISFIVPRRSESFQSDIYPPAPSGKPSLTAEEWASGKDAQPDLLDMSTLYESKGTVEKAVSATVPSAGAQVQKHNEEKVETPKPEAQPVSKPKESAEEQKPSKEPEVKPTTPSASKVEEPSKKRDEDNHQKEETVTQPKREKTPVEKSFPKPASSPVTFSEDVKKEPSEEKKLEVSDEAPKAAPLAESKKVEEKEPFYVSKDKKDISAVNLADLNKRFEGFEKRYEEELAIRDWKIAQLEDKLAKLTEAIKEKCN", "text": "SIMILARITY: Belongs to the WD repeat coronin family."}
{"protein": "MSRVGVLALGPAGVGKSTFCNSIITHMQSIGRRAHIVNLDPAAEPSEYEFTIDIRDLISLQDVMEEMDLGPNGALIYCFEFLMNNLDWLDEEIGDFNDEYLIFDCPGQIELYTHIPVLPTIVRHLQTSLNFNLCATYLLEAPFVIDRSKFFSGALSAMSAMILLELPHINILSKIDLIKNEVSKKELKKFLNPDPLLLNASSDNESNPKFAKLNKAIANLVDDFGMVQFLPLDCNKDSDSVATILSYIDDVTQWSESQEPKEPVEEIEEEVDFE", "text": "FUNCTION: Small GTPase required for proper nuclear import of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import. SIMILARITY: Belongs to the GPN-loop GTPase family."}
{"protein": "MKAMERWFNVGKIVNTHGIRGEVRVISRTDFPEERYKKGNKLYIFRERDTEPIEVTVKSHRVHKSFDLLSFEGYDSINDVERFKGAMLKVPESQLGELAEGEYYFHEIIGCTVVTEGGETIGAVKEILTPGANDVWVVRREDGSEALIPYIDEVVLHVDPERKTIIIRPMEGLLE", "text": "FUNCTION: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimM family."}
{"protein": "MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT", "text": "FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex. SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MAAIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK", "text": "FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
{"protein": "MSVRLVLAKGREKSLLRRHPWVFSGAVARMEGKANLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPSESIDIAFFTRRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVAVRKKEGMELTQGPITGELPPALLPIEEHGMKLLVDIQHGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSHEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKDINMLAIQLLNEGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM", "text": "FUNCTION: Specifically methylates the cytosine at position 1962 (m5C1962) of 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family."}
{"protein": "MSRTIFCTFLKKEAIGQDFQIYPGDIGRRIYDDISQEAWSLWLNKQTMLINEKKLSMIHHEDRALLEREMIQFLFEGKDVHVSGYIPPKD", "text": "FUNCTION: Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. SIMILARITY: Belongs to the Fe(2+)-trafficking protein family."}
{"protein": "MTQFAFVFPGQGSQSVGMLAEMAANYPIVEETFAEASAALGYDLWALTQQGPAEELNKTWQTQPALLTASVALWRVWQQQGGKMPALMAGHSLGEYSALVCAGVINFADAVRLVEMRGKFMQEAVPEGTGGMSAIIGLDDASIAKACEESAEGQVVSPVNFNSPGQVVIAGHKEAVERAGAACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFSAPTVPVVNNVDVKCETDAAAIRDALVRQLYNPVQWTKSVEFIAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASALNEPAALSAALTQ", "text": "SIMILARITY: Belongs to the FabD family."}
{"protein": "MASSTSNSAAARMQTHLQTEPQNRSQNQLQGSVTITQSQTHTSAPVLRLRGESTGESESSTNGERGLGRGRRIQWAEDVVDNEGLGRKKSKVCCIYHAPRPIDESSDESSSDSDDSSSDDDGGAKPSGGNGDKHDHGDECAHGHAHGKGKGKGKERKRSPNAYERQPNYKGKDKGKGGG", "text": "FUNCTION: Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the YPI1 family."}
{"protein": "MKIRPLHDRVVVRRMEEERTTAGGIVIPDSATEKPMRGEIIAVGAGKVLENGDVRALAVKVGDVVLFGKYSGTEVKVDGKELVVMREDDIMGVIEK", "text": "FUNCTION: Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GroES chaperonin family. SIMILARITY: Belongs to the GroES chaperonin family."}
{"protein": "MAVIAFIGLGQMGSPMASNLLKQGHQLSVFDVNPDAVQRLVDKGAQPASSPAQATIGAEFVITMLPNGDLVRSVLFGEQGVCETLSREALVIDMSTIHPLQTDNLIADMQSKGFSMMDVPIGRTSDNAITGTLLLLAGGTAEQVERATPVLMAMGNELVNTGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPNKVMKGDLSPAFMIDLAHKDLGIALDVANQLHVPMPLGAASREVYNLARAAGRGREDWSAILEQVRISAGLTANVKK", "text": "FUNCTION: Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1- sulfonate (DHPS). SIMILARITY: Belongs to the HIBADH-related family. 3-sulfolactaldehyde reductase subfamily."}
{"protein": "MKRREAVCAHRHFLGTGKPPHPLGRSIPVEPCPGLPAFAEVDLLSLLVPIKISSTPPSGSRLDPQIASSAFPGLGSLGGQDSSGSLVQRASCELESPYEL", "text": "SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MDYWILLVLAFLVADKSWHLTGLLATKLTSPERLQQLIRERQELHQQQQSLSAQDHYAKWTKNNRRLDVLDRDIARVRKNYLESVEATKARLAKLKLLVVTVPFTALKFYKGKLPVYALPKGMFPRFIEGTLEHGWLYMALAPLNMKQFSEGASVAVSLGIWLFALLRVLGAIEFVLETLREQNPQVATETAKVHARTAQAASAN", "text": "FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP- dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WRB/GET1 family."}
{"protein": "MATINQLVRKPRVKKVVKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRIRLTNGFEVISYIGGEGHNLQEHSVVLIRGGRVKDLPGVRYHTVRGALDCAGVKDRKQGRSKYGVKRPKA", "text": "FUNCTION: With S4 and S5 plays an important role in translational accuracy. FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
{"protein": "EDHPVHNLGEHSVCDSVSAWVTKTTATDIKGNTVTVMENVNLDNKVYKEYFFETKCKNPNPEPSGCRGIDSSHWNSYCTETDTFIKALTMEGNQASWRFIRIDTACVCVITKKTGN", "text": "FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons as well as basal forebrain cholinergic neurons in the brain. Its relevance in the snake venom is not clear. However, it has been shown to inhibit metalloproteinase-dependent proteolysis of platelet glycoprotein Ib alpha, suggesting a metalloproteinase inhibition to prevent metalloprotease autodigestion and/or protection against prey proteases (By similarity). Binds a lipid between the two protein chains in the homodimer. The lipid-bound form promotes histamine relase from mouse mast cells, contrary to the lipid-free form (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NGF-beta family."}
{"protein": "MLFTRSVARISSKFLRNRSFYGSSQSLASHRFAIIPDQGHSCSDSPHKGYVCRTTYSLKSPVFGGFSHQLYHQSSSLVEEELDPFSLVADELSLLSNKLREMVLAEVPKLASAAEYFFKRGVQGKQFRSTILLLMATALNVRVPEALIGESTDIVTSELRVRQRGIAEITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNKMSVLAGDFLLSRACGALAALKNTEVVALLATAVEHLVTGETMEITSSTEQRYSMDYYMQKTYYKTASLISNSCKAVAVLTGQTAEVAVLAFEYGRNLGLAFQLIDDILDFTGTSASLGKGSLSDIRHGVITAPILFAMEEFPQLREVVDQVEKDPRNVDIALEYLGKSKGIQRARELAMEHANLAAAAIGSLPETDNEDVKRSRRALIDLTHRVITRNK", "text": "FUNCTION: May be involved in the supply of solanesyl diphosphate for ubiquinone-9 (UQ-9) biosynthesis in mitochondria (PubMed:21950843). Synthesizes C25 to C45 medium / long-chain products depending on the type of substrate available (PubMed:21220764). Can use geranyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as substrates, but not dimethylallyl diphosphate (PubMed:11069698, PubMed:17877699, PubMed:21220764). SUBCELLULAR LOCATION: Plastid, chloroplast Mitochondrion. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
{"protein": "MREAYLRCWIFSWKNVWVRPCQRLHFKTVLLQGSLLYTALDSYSTVQAAPKSSSGSVKFQGLAETGIMKMDMEDADMTLWTEAEFEEKCTYIVNDHPWDSGADGGTSVQAEASLPRNLLFKYAANNSKEVIGVVSKEYIPKGTRFGPLIGEVYTNDTVPKNANRKYFWRIYSREEFHHFIDGFNEEKSNWMRYVNPAHSAREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYPYPGELTVINLTQTESNPKQYSSEKNELYPKSVPKREYSVKEILKLDSNPSKRKDIYRSNISPFTLEKDMDGFRKNGSPDMPFYPRVVYPIRAPLPEDFLKASLAYGMERPTYITHSPLPSSTTPSPPASSSPEQSLKSSSPHSSPGNTVSPLAPGLPEHRDSYSYLNVSYGSEGLGSYPGYAPAPHLPPAFIPSYNAHYPKFLLPPYGISSNGLSTMNNINGINNFSLFPRLYPVYSNLLSGSSLPHPMLNPASLPSSLPTDGARRLLPPEHPKEVLIPAPHSAFSLTGAAASMKDESSPPSGSPTAGTAATSEHVVQPKATSSVMAAPSTDGAMNLIKNKRNMTGYKTLPYPLKKQNGKIKYECNVCAKTFGQLSNLKVHLRVHSGERPFKCQTCNKGFTQLAHLQKHYLVHTGEKPHECQVCHKRFSSTSNLKTHLRLHSGEKPYQCKVCPAKFTQFVHLKLHKRLHTRERPHKCAQCHKSYIHLCSLKVHLKGNCPAGPAAGLPLEDLTRINEEIERFDISDNADRLEDMEDSVDVTSMVEKEILAVVRKEKEETSLKVSLQRNMGNGLLSSGCSLYESSDLSLMKLPHSNPLPLVPVKVKQETVEPMDP", "text": "FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs (PubMed:27102484). Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (PubMed:27102484). Binds specifically to the PRDI element in the promoter of the beta-interferon gene (By similarity). Drives the maturation of B-lymphocytes into Ig secreting cells (By similarity). Associates with the transcriptional repressor ZNF683 to chromatin at gene promoter regions (PubMed:27102484). Binds to the promoter and acts as a transcriptional repressor of IRF8, thereby promotes transcription of osteoclast differentiation factors such as NFATC1 and EEIG1 (PubMed:32741026). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
{"protein": "MWKGFLSKLPRKTSASGRGADLDSGQCSNGAGNGNPIQRTSSCGSIPSGRSTSTIKRMSSAIFPSSVVAGIEPLVSFKDVPNSEKQNLFVSKLNLCCAVFDFSDPNKSSAEKDIKRQTLLDLIDYVDSSSSRFSEAVIAASSRMFAVNLFRVFPPNYRSSSSGGGEGEEEEPMFEPAWCHLQLVYELLLKFIGSSSLDAKVGKKYFDHSFIVKLLNLLDSEDPRERDCLKTILHRIYGKFMVHRPFIRKAVSNIFYHFVFETDRHNGIAELLEVFGSVISGFALPLKEEHKIFLWRVLVPLHKPKSVGVYLQQLTYCVTQFIEKDPKLASSVIIGLLRYWPITNSQKEVMFLSEIEEILETISTAEFQKCMVPLFRRIAQCIKSSHFQVAERALFIWNNDNVISLIAQNRQMIMPIIVPALEHNSQNHWNQAVLNLTDNVKKMFSEMDDVLFSACLVKYKEDEERQASLESKRRLTWEKLESAASFQPVTGHTAVLVGRQPSANLIATLI", "text": "FUNCTION: B regulatory subunit of phosphatase 2A (PP2A) involved in salt stress response (PubMed:31221736). Under salt stress conditions, required for the catalytic activity of PP2A and the dephosphorylation of SIT1, a negative regulator of salt tolerance (PubMed:31221736). Dephosphorylation of SIT1 turns off salt-induced SIT1 activity directly, which has a positive effect on salt tolerance (PubMed:31221736). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane; Peripheral membrane protein Note=The partial localization to the plasma membrane may be due to its association with SIT1. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 family."}
{"protein": "MASTEEIVQMMQEASAEFAEADDVSFLDKMNSNIAQLEQQLREQMDESRQNIAKLEINLIDTEKSIGSLRELMKDATDEATIMKGSDKLNNLIDELQATENEIQMMNSEIEKKVSKLVEDEDNTSSEYEMISKELEQEYDPVFASNILKLKLYRSLGVRLDLDNNQILIQNKELGTIDTLPLEDELTEFFKVKYIWSRIGK", "text": "FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Note=Associated with kinetochores. SIMILARITY: Belongs to the SPC24 family."}
{"protein": "MTAENRPPVGDKQDKGQAVQEMFASIAPRYDLLNRVLSLGVDRGWRRAAAAEALAHSPRRVLDVATGTGDFAIELKERAPQVEIVGSDFVPQMLDLARQKAGAKQLSIRFEEGDALRLPYPDASFDAVTCAFGFRNFADYTQGLAEMWRVLTPGGRLVLLEFPPPASGLFGAVFRLYFQHVLPRIGALVSGNAGAYTYLPESVLAFPEPERLAQMMRATGFRTRYRALTFGIAGMWVGDKR", "text": "FUNCTION: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family."}
{"protein": "MGRRKSKRKPPPKRKAIEPLDQQFNCPFCNHEKSCEVKMDRAKNTAMIQCTVCLEDFHTTTNVLSEPIDVYNDWVDACESAN", "text": "FUNCTION: Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ELOF1 family."}
{"protein": "MAGTANCIDILIAIILPPLGVFLKFGCGHEFWICLLLTFLGYIPGIIYAIYAITK", "text": "FUNCTION: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0057 (PMP3) family."}
{"protein": "MSKLRIPILLVLFIVSCCSAEQCGTQAGGALCPGGLCCSKFGWCGSTSEYCGDGCQSQCSGSSGGGTLSSLISGDTFNNMLKHRNDNACQGKPFYTYDAFLSAAKAFPNFANKGDTATKKREIAAFLGQTSHETTGGWPTAPDGPYAWGYCFLREQNPSTYCQASSEFPCASGKQYYGRGPIQISWNYNYGQCGRAIGVDLLNNPDLVATDPVISFKTALWFWMTPQSPKPSCHDVITGGWTPSSADRAAGRLPGYGTVTNIINGGLECGRGQDSRVQDRIGFYKRYCDIFGIGYGDNLDCYSQRPFGSSLPLSSILLDTVAAA", "text": "FUNCTION: Defense against chitin-containing fungal pathogens. SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily."}
{"protein": "MSINLLHKDDTRIDLVFEGYPLEFVNAIRRASMLYVPIMAVDDVYFIENNSPLYDEILAHRLALIPFMSEEALDTYRWPEECIECTENCEKCYTKIYIEAEAPNEPRMIYSKDIKSEDPSVVPISGDIPIVLLGTNQKISLEARLRLGYGKEHAKFIPVSLSVVRYYPKVEILANCEKAVNVCPEGVFELKDGKLSVKNELSCTLCEECLRYCNGSIRISFVEDKYILEIESVGSLKPERILLEAGKSIIRKIEELEKKLVEVVK", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family."}
{"protein": "MKNISDYRNKKVLVLGLAKSGVNAARLLHKLGALVTVNDKQQFDDNKDAQELLADGMRVITGRHPVELLDEHFELMVKNPGIPYSNPMVKRAEALHMPIITEPELAYQVSEAQWIGITGTNGKTTTTTLIGLMLNQQRPHHAFDAGNIGIPVSQVAQKVGKDDTIVAELSSFQLCGIKTLHPHIAVLTNIYEAHLDWHGNRANYVAAKMRITMNQTPDDYFIMNWDLPEMHELAKQSKAQIVPFSRKNAEGARAQLIDGWLTFDGDRIMKASEMQIPGLHNIENALAAIAAVKLEGVGDDAIREVLRTFSGVKHRIQYLETIDGRRVYNDSKATNVEAATVALNAFDQPIVWLAGGLDRGLPMDALTPLVKKHVKSMVVFGQTAPLMAKIGKDAGVPVQTTENVMTAVPLAYEVSRPGDVILLSPAAASWDQYPNFEVRGDDFIKAVNQLKATVESGDK", "text": "FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family."}
{"protein": "SLFELEGKMILQETGKNPAKSYGVYGCNCGVGGRGKPKDATDRCCYVHKCCYKKLTGC", "text": "FUNCTION: Wasp venom phospholipase A2 homolog that lacks enzymatic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily."}
{"protein": "MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFEADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNKLSNMQPQIAMDRYLESMGDPDASDFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVSLDTATYVPIDNDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYKNGARTSGGDNDEYEDCTQESGCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDPSSAPSDVPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW", "text": "FUNCTION: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the BamA family."}
{"protein": "MFENDTIVAIATANGIGSISIVRVSGAKALEIATKISKKNNFKARLATLSTIYDSKNEIIDEALVIYFKSPFSFTGEDVVEFQCHGGVAISNMIVDEVLNAGARLANPGEFSKRAFFNNKIDLTKAEAISKIIEARSADAVKLLARQLKGELTNFVDEIREDLLFMLAYTEVSIDYAEEDLPTDIYEQIENKMQKISLKLSNTLEASRRREGMIEGFKVAIIGKPNVGKSSLLNKLLNFDRAIISDIAGTTRDTIEESVRIGTHIIKIVDTAGIRDASDVIEKIGIEKSIQAINEADIVIALFDNSKICDDEDKKILDLIKENSDKKVIVVLNKSDLQNQFDKNVLDSFIELSTKEDINPLIKELELILDSNTFGDDITLVSKRQVLAVENTLYNIGLAKEPLKSGELEFFAHFITQALEDISSITRPYDNDEMLDVMFGEFCLGK", "text": "FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family."}
{"protein": "MKFTKPNSRQNKPHVEQKTSRRSTNANAVASKNVKKVTEAQPKSVKASTHSVKPTVKNPLVEGEKLQKVLARAGQGSRREIEAMIAENRVSVDGKIATLGDRIDVHAGVKIRIDGHLINLLHAQKEVCRVLMYYKPEGELCTRHDPEGRPTVFDRLPRLTGSRWIAVGRLDINTSGLLLFTTDGELANRLMHPSREVEREYSVRVFGQVDEAMLHRLKKGVQLEDGPANFKEIKFAGGVGMNQWFDVTLMEGRNREVRRLWESQGVQVSRLIRTRYGNISLMKSLPRGGWEEMDLTNVNYLRELVGLPAEVETKLDVTKPRRRAKTGQIRKAVKRYAELNKRYKK", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-2605 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family."}
{"protein": "MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE", "text": "FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus membrane Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MEMEMSVLAMSSTLILALAMALIFLFKAKSSSAIKWPPGPKTLPIIGNLHQLGGDELHIVLAKLARVHGAIMTIWMAKKPVIVVSDVNSVWEVLVSKSSDYAARDAAEISKIVSASSHSINTSDSGPYWQTLRRGLTHGPLGPLNISAQIPIQQRDMQRVIREMQQDAAANGGIIKPLDHLKRSSTRLVSRLIFGDTFDNDPYNDSMHEVVQDLNRFGGIALLEQAFSFAKHLPSYKRGVKEFHIHKRKIDDLVRPVVASANPPSNSYLGFLQSQNYSEEIIIACIFELYLLAMDSSASTATWALAFMIRDQQVQEKLYQDIKRVIGDGVDLVKAEDLSKMHYLQAVVKETMRMKPIAPLAIPHKTAIDTTVMGTKVPKGTCVMVNLYALHHDESVWAKPYTFMPERFLQGEDGKSVTEQAFLPFGAGMRICGGMEVGKLQFSLALANLVNAFKWTSAAEGKLPDMSDELQFITVMKTPLEARIIPRNP", "text": "FUNCTION: Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:23161544, PubMed:26359402). Catalyzes the conversion of matairesinol to pluviatolide (PubMed:23161544, PubMed:26359402). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MLKYALHSGGMPRNRLLRQLSAYIFRRSYSSNIRNIGILAHIDAGKTTTTERMLFYSGKTRSLGEVHRGNTVTDYLTQERERGITICSSAVTFPWSGNRINLLDTPGHIDFTMEVEQSLYAVDGVVVVLDGTAGVEAQTVTVWTQADKHKLPRLAFVNKMDRPDADFDKCVNDLRTKLETQPVCIQYPSKNQDGLLAINDVITLEQLTWQPKDLGRSYSKTKLEPSDDLRQLQEKRNELIDQLSGLDDELADVVISTESFDNVSNALIERALRRATCQQKVVPVLLGSAYKNVGIQRLMDAVNTYLPAPEERNQIYDCFGNEVAGKVFKIVHDKQRGPLTLVRILRGEIKRGMRLICSRGQAEVVSKLYEPLADEYREVGAVQSGDVVICAGLKSTVTGDLLTSSQTALRNAQKRLKQSQGTVSADEDEELDTDELFGIDRQIPDAVYFCSIEPPSVSSQTAMEQALRQLQREDPSLRVSYDSVTGQTVLGGMGELHMDIIKSRILSEYKIDVDLGPLQIAYKETIESPSLTTLSVEKEIAGSKQNVSLTLEVVKDHDELFSLDKSPENLSNLNTLRPRTLQVIRKGSVSALERGPRVGGQVVDTQIRLHNAIIGRGTADSFVMATAAQCVQKLLSTSGTRLLEPIMALQIVAPSERISGIMADLSRRRALINDVLPKGERNKMILVNAPLAELSGYSSALRTISSGTASMTMQPSGFSGMNAVDESLAERRVQGLE", "text": "FUNCTION: Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Not involved in the GTP-dependent ribosomal translocation step during translation elongation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MEETALTKDQITEFKEAFCLFDKDGDGCITVEELATVIRSLDQNPTEQELHDIITEIDSDSNGTIEFAEFLNLMAKKLQESDAEEELKEAFKVFDKDQNGYISASELSHVMINLGEKLTDEEVEQMIKEADLDGDGQVNYDEFVKMMINID", "text": "FUNCTION: Potential calcium sensor. SIMILARITY: Belongs to the calmodulin family."}
{"protein": "MAIGRYGTLVFYILAGLAFVWSLEYFKHYTKNNYERFHCTAVVEPVQGTATVEKLSAVGGPPCDKRAELKLITQKLTQHFDPNKQPALFCIVENTSVESVHYPVSRTNKGPAGYIAYAGYEADRAAVHKYCEAHGAAVLHM", "text": "FUNCTION: Component of the ceramide synthase complex required for synthesis of ceramides. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the LIP1 family."}
{"protein": "MKLIKLKLASFRNLQNIELAPGKKFNVFYGNNGQGKTNLLESIYLLATMKSFKQARNAELIAFGGEFALVKGTVERDQVRREIAVLIEKQGKKAKVDAKLMTRLDDFFGNLNVVLFTPEEISMVRGGPDLRRRYLDRAVFTCDLGYLTAYHDYAKILKNRNALLKVNETAGIEVWTEQLVQAALLVIERRKAYLDRIGRLLQGFYSEISGNDETVQIEYRLHGVDARLFAEDPAEALNQALRAHAAEERRRGSTAIGPHRDDLYFGLNGRGARQFASQGQQRSFVLALKMAEIEHITRCFEAPPVLLLDDMTSELDRERNRNLMEFLKKREMQVFITTTSLHNVDVDELQDNRTFRIKEGKILD", "text": "FUNCTION: The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecF family."}
{"protein": "MYLEVSERQVLDASDFAFLLENSTSPYDYGENESDFSDSPPCPQDFSLNFDRTFLPALYSLLFLLGLLGNGAVAAVLLSQRTALSSTDTFLLHLAVADVLLVLTLPLWAVDAAVQWVFGPGLCKVAGALFNINFYAGAFLLACISFDRYLSIVHATQIYRRDPRVRVALTCIVVWGLCLLFALPDFIYLSANYDQRLNATHCQYNFPQVGRTALRVLQLVAGFLLPLLVMAYCYAHILAVLLVSRGQRRFRAMRLVVVVVAAFAVCWTPYHLVVLVDILMDVGVLARNCGRESHVDVAKSVTSGMGYMHCCLNPLLYAFVGVKFREQMWMLFTRLGRSDQRGPQRQPSSSRRESSWSETTEASYLGL", "text": "FUNCTION: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of mesangial cells through a heterotrimeric G-protein signaling pathway. Probably promotes cell chemotaxis response (By similarity). Binds to CCL21. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "NSELINSILGLPKVMNEA", "text": "FUNCTION: Causes the migration of the distal retinal pigment into the proximal end of the pigment chromatophore cells and thus decreases the amount of light entering the retinulas. May also function as a neurotransmitter and/or neuromodulator. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod PDH family."}
{"protein": "MANIFENCSYHSPYEPYYLNCTNTTNQCTLVQDVETIESIIFWIDFLIPCTLFVVACFLNAYYLSILVPEFTEMNDITKKQYIFMVSRAISALTACVIMLALRILQLITSSFTIYFLFFLIDDLSFYSLLGSYVGSAILLYLATIRPILYSNRISVRTVYKFAIANLITSVVLAITTAMFQAADLSDGPFQCDLKHCQPITNMIMLVLILTSFLIPIVTLSFVLVTLCFYKNRSESIGDFTTDNSVSKSARTRLAWTLFTFTLITLTEAIPSFYLVGTSIGQLLSTWILCAHCYSIPEYEKFGYNIQKS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. B0244 subfamily."}
{"protein": "MGIGKSKINSCPLSLSWGKRHSVDTSPGYHESDSKKSEDLSLCNVAEHSNTTEGPTGKQEGAQSVEEMFEEEAEEEVFLKFVILHAEDDTDEALRVQNLLQDDFGIKPGIIFAEMPCGRQHLQNLDDAVNGSAWTILLLTENFLRDTWCNFQFYTSLMNSVNRQHKYNSVIPMRPLNNPLPRERTPFALQTINALEEESRGFPTQVERIFQESVYKTQQTIWKETRNMVQRQFIA", "text": "FUNCTION: [Isoform 2]: Proposed to inhibit LPS-TLR4 signaling at the late endosome by interaction with isoform 1 thereby disrupting the association of isoform 1 with TICAM1. May be involved in TLR4 degradation in late endosomes. FUNCTION: Functions as sorting adapter in different signaling pathways to facilitate downstream signaling leading to type I interferon induction (PubMed:16603631, PubMed:16757566, PubMed:25385819, PubMed:25825441). In TLR4 signaling, physically bridges TLR4 and TICAM1 and functionally transmits signal to TICAM1 in early endosomes after endocytosis of TLR4. In TLR2 signaling, physically bridges TLR2 and MYD88 and is required for the TLR2-dependent movement of MYD88 to endosomes following ligand engagement (PubMed:25385819). Involved in IL-18 signaling and is proposed to function as a sorting adapter for MYD88 in IL-18 signaling during adaptive immune response (PubMed:22685567). Forms a complex with RAB11FIP2 that is recruited to the phagosomes to promote the activation of the actin-regulatory GTPases RAC1 and CDC42 and subsequent phagocytosis of Gram-negative bacteria (PubMed:30883606). SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum. Early endosome membrane. Late endosome membrane. Note=Translocates to late endosomes upon LPS stimulation where it colcoalizes with isoform 1. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm Golgi apparatus. Cell membrane Endoplasmic reticulum. Early endosome membrane. Late endosome membrane. Cell projection, phagocytic cup Note=Localized to the plasma membrane as a result of myristoylation. Phosphorylation on Ser-16 leads to its depletion from the membrane. Upon LPS stimulation colcoalizes with isoform 2 in late endosomes."}
{"protein": "MKNVTDSFVFLGHWPSAGSFGFNTDILATNPINLSVVLGVLIFFGKGVLSDLLDNRKQRILNTIRNSEELRDGAIEQLEKARARLRKVEMEAEQFRVNGYSEIEREKWNLINSTSKTLEQLENYKNETIQFEQQRAINQVRQRVFQQALQGAIGTLNSCLSNELHLRTINANIGMFGAMKEITD", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MGCGNSTATSAAAGRGKPGAVKDATEDSITEDDKRRNYGGVYVGLPSEAVNIASSQAKTVQKS", "text": "SIMILARITY: Belongs to the OCC1 family."}
{"protein": "MPKRPAENPEQSDDFVSKSQKKREMAERQELGTQLVNLTDSQLAKMPLDDELRDAVLLARKIRNKHEGYRRQLQFIGKLMRLRDIAPIEQALNNLKNAHQQQTSIFHEIETTRDKLLHEGDDALQEFIEEHPHADRQKLRQLIRLAEKQRAEQKPPVAARQLFVYLRELLG", "text": "SIMILARITY: Belongs to the UPF0307 family."}
{"protein": "MPNLLSRNPFHGHHNDHHHDRENSSNNPPQLIRSSKSFLNFIGRKQSNDSLRSEKSTDSMKSTTTTTNYTTTNLNNNTHSHSNATSISTNNYNNNYETNHHHNISHGLHDYTSPASPKQTHSMAELKRFFRPSVNKKLSMSQLRSKKHSTHSPPPSKSTSTVNLNNHYRAQHPHGFTDHYAHTQSAIPPSTDSILSLSNNINIYHDDCILAQKYGKLGKLLGSGAGGSVKVLVRPTDGATFAVKEFRPRKPNESVKEYAKKCTAEFCIGSTLHHPNVIETVDVFSDSKQNKYYEVMEYCPIDFFAVVMTGKMSRGEINCCLKQLTEGVKYLHSMGLAHRDLKLDNCVMTSQGILKLIDFGSAVVFRYPFEDGVTMAHGIVGSDPYLAPEVITSTKSYDPQCVDIWSIGIIYCCMVLKRFPWKAPRDSDDNFRLYCMPDDIEHDYVESARHHEELLKERKEKRQRFLNHSDCSAINQQQPAHESNLKTVQNQVPNTPASIQGKSDNKPDIVEEETEENKEDDSNNDKESTPDNDKESTIDIKISKNENKSTVVSANPKKVDADADADCDANGDSNGRVDCKANSDCNDKTDCNANNDCSNESDCNAKVDTNVNTAANANPDMVPQNNPQQQQQQQQQQQQQQQQQQQQHHHHQHQNQDKAHSIASDNKSSQQHRGPHHKKIIHGPYRLLRLLPHASRPIMSRILQVDPKKRATLDDIFNDEWFAAIAACTMDSKNKVIRAPGHHHTLVREENAHLETYKV", "text": "FUNCTION: Involved in regulating the activity of the plasma membrane proton pump PMA1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MADPIVHPGVHRPEFSAPLHARAEIIATLRAALGKPNTTLVGAAIGTGMAAQAASRGGADFILALNAGRLRSMGAPSIFSLLALRKSNDFVLDFAQSEILPFVKVPVFFGASAFDPRCSIEAELERIADAGFGAIVNFPTSIFLDGRFRADIEGAGLGFQRELEMLRAAQKRNMATLAYVRTVAEAQQAATAGVDIINLNLGWNVGGTVGSRTELSLRQAAEYAKIIFRQIRAISEDTLCVLEGGPIVSPDQMYEVSALSKADGYIGGSTIDRVPLEASMEQITSAFKSVGTLQKRIDELERQLEHVQREYSIVGRSPSIQQIKQRIEKLAASSLPVMITGQAGTGKKLLARGIHEAARRSGSKLISSEDASGESLFGFAPSEGGRKVLGLLQYHPKATLLIESVECLCVDAQERLIEVIETGAYRRLGDNERGRFEGRLILASTRPLPELGSSGQLIPALESRLAPGHVFLPPLCDRLEDLPLLAEHFLQALRKDRRSRKLSVDHSAYRVLMTYGWPENIRELRSVLETAAIRCEGDWIKSEHLPPLGDANADAPHPHPGEEREWILDALQRHRFRRGEAARYLGISRKTLYNKMRVYGLPLQPRERS", "text": "FUNCTION: Probable transcriptional regulator that acts in conjunction with sigma-54."}
{"protein": "MASTFRLSISFLTLILFSLWVVEAHTSRKLISIKEKEGQDISHLLKDGEFDDPSLYMYFTLNDLKLGTKLLIYFYKNDLQKLPPLLTRQQADLIPFTKSKLDFLLDHFSITKDSPQGKAIKETLGHCDAKAIEGEHKFCGTSLESLIDLVKKTMGYNVDLKVMTTKVMVPAQNSISYALHNYTFVEAPKELVGIKMLGCHRMPYPYAVYYCHGHKGGSRVFEVNLVTDDGRQRVVGPAVCHMDTSTWDADHVAFKVLKMEPRSAPVCHFFPLDNIVWVTK", "text": "FUNCTION: Associated with the protein storage vacuole formation. SUBCELLULAR LOCATION: Protein storage vacuole Golgi apparatus, Golgi stack Golgi apparatus, trans-Golgi network Prevacuolar compartment."}
{"protein": "MARGTALLGLTSLLLGLVNGQKPGETKEVHPQLTTFRCTKKGGCKPATNYIVLDSLSHPIHRAEGLGWGNCGDWGNPPPKDVCPDVESCAKNCIMEGIPDYSQYGVTTNGTSLRLQHILPDGRVPSPRVYLLDKTERRYEMLHLTGFEFTFDVDATKLPCGMNSALYLSEMHPTGAKSKHNPGGAYYGTGYCDAQCFVTPFINGLGNIEGKGSCCNEMDIWEANSRASHVAPHVCNKKGLYLCEGEECAFEGVCDKNGCGWNPYRVNVTDYYGRGEEFKVNTLKPFTVVTQFLANRKGKLEKIHRFYVQDGKIIESFYTNKEGIPYTNMIEDEFCAATGSRKYMELGATQGMGEALTRGMVLAMSIWWDQGGNMEWLDHGEAGPCAKGEGAPSNVVQVEPFPEVTYTNLRWGEIGSTYQEVQKPKPKPGPGPRSD", "text": "FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family."}
{"protein": "MFLQAVTSPISINSLMVLAAYALLGGLYLIVVPLLLYSWMNRRWHCMGKFERLSAYGLVFLFFPGLILFAPFLNLRLNGQGEV", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I NdhL subunit family."}
{"protein": "MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKFGIEIRGCLTQMGDIPLDIKDWSQVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKDGFQSNHAGGILGGISSGQQIIAHMALKPTSSITVPGRTINRFGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRQRAQNADVKTDIPRW", "text": "FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. SIMILARITY: Belongs to the chorismate synthase family. SIMILARITY: Belongs to the chorismate synthase family."}
{"protein": "MSTQKNARATAGEVEGSDALRMDADRAEQCVDALNADLANVYVLYHQLKKHHWNVEGAEFRDLHLFLGEAAETAEEVADELAERVQALGGVPHASPETLQAEASVDVEDEDVYDIRTSLANDMAIYGDIIEATREHTELAENLGDHATAHMLREGLIELEDDAHHIEHYLEDDTLVTQGALE", "text": "FUNCTION: Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Dps family."}
{"protein": "MPISQTYLGSAKAPAGIKSFYFIRHGATDLNEKEIVVNGEKLWGVQGSGTNIGLNAKGERQALLAGNVLRSLPISGVVCSPLLRALQTAFIANPGCPSFQIANDLQERDFGTHEGGFGPLQMFEDDYPDCESTEIFSIHVAKALKHACRENVLLVAHGGVLRVVAALLGVAITDEHTANGRVLHFSVVADNWSVRVIQSPVVMVSGVTRGIGKAIAEDLIRHGYRVSLGARNIQDLVAAFGDENEALHYARFDALDHSSMKDWVDTTIAKFNRIDGLVNNAGCGDHVDLEKEINVELLQKQWDINCVAPLIMTKLCMPYLIESGSGRIVNLNSMSGQRVANSLVGYNMTKHGLAGLTKTTQHVGWDHGVRAVDICPGFVATNMSSWTNLIGPDEMIQPEDIAKLVRAAMERPNRAFVPKNEVLCMKESTR", "text": "FUNCTION: Reduces deoxy-fructosyl-glutamine to mannopine. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "APVPGLSPFRVV", "text": "FUNCTION: Induces relaxation of mouse trachea that has been precontracted with methacholine. May induce relaxation of arterial smooth muscle. May target bradykinin receptors (BDKRB). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-related peptide family."}
{"protein": "MESLPKTLSTLARLRERDITLTFATGRHALEMQHILGALSLDAYLITGNGTRVHSLEGELLHRDDLPADVAELVLYQQWDTRASMHIFNDDGWFTGKEIPALLQAFVYSGFRYQIIDVKKMPLGSVTKICFCGDHDDLTRLQIQLYEALGERAHLCFSATDCLEVLPVGCNKGAALTVLTQHLGLSLRDCMAFGDAMNDREMLGSVGSGFIMGNAMPQLRAELPHLPVIGHCRNQAVSHYLTHWLDYPHLPYSPE", "text": "FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5- hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5- hydroxymethylpyrimidine phosphate (HMP-P). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family."}
{"protein": "MHSYDYWLILAFFAVVLLPAPFLGRFYYKVMEGQSTWLTPILGPVERGCYRIAGVNPQDEQSWQKYTLALLAFNLAGFLLLFAILLFQDHLPLNPQNLPGQEWTLAFNTAVSFMTNTNWQAYSGEASLSYLSQMVGLTVQNFVSAATGLAVLVALCRGIGRKSTKTLGNFWVDMTRATLYGLLPLCLLLALYLVWQGVPQTFAQYVNAVTMQGVDQVIPLGPAASQIAIKQLGTNGGGFFGVNSAHPFENPTAWSNLFEVASIILIPVALVFTFGHYVKDLRQSRAIIGCMLALFIIGGATSLWAEYQPNPALNNVTVEQAAPLEGKEARFGTTATVLWSVTTTAASNGSVNGMHDSLNPLSGMVALVNMMVGEVIFGGVGAGLYGMLLNVLIAVFLAGLMIGRTPEYLGKKLQAREVQLLVVTLLVMPVGVLVLGAIAASLPGPVAAVSNPGPHGFSQLLYAYTSASANNGSAFGGFGANTAFHNLMLGLGMLIGRFGYILPVLALAGSLAMKKTAPIGQNSFPTHGPLFVTLLTVTILLLGGLTFLPTLALGPIAEHLSMGF", "text": "FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KdpA family."}
{"protein": "MVRIPRRKLLPSCLCMTATVFLMVTVQVLVELGKFERKKFKNSDLQDGQKDVEGDPKHLNPLPKKDALALSGRNKVDAGSYPIVLWWSPLTGETGRLGQCGADACFFTINRTFQHHPMTKAFLFYGTDFNIDSLPLPRKAHHDWALFHEESPKNNYKLFHKPVITLFNHTATFSRHSDLPLTTQYLESVEVLKSLRYLVPLQSKNNLRQKLAPLVYVQSDCDPPSDRDSYVRELMAYIEVDSYGECLQNKHLPQQLKNPASMDADAFYRVLAQYKFILAFENAVCDDYITEKFWRPLKLGVVPVYYGSPTIADWLPSNRSAILVSEFSHPRELASFIRRLDYDDGLYETYVEWKLKGEISNQRLLTALREREWGVQDINQDNYIDTFECMVCRRVWANRRLQEQGLPPKQWKADVSHLHCPEPTLFAFSSPASPALRGRSLRELWLPSFQQSKKEAQALRWLVDRNQNFSSEEFWALVFKDSF", "text": "FUNCTION: Predominantly fucosylates the innermost N-acetyl glucosamine (GlcNAc) residue in biantennary N-glycan acceptors. Postulated to generate core alpha(1->3)-fucose epitope within the chitobiose unit of biantennary N-glycans, providing for a recognition signal to reorient aberrantly folded glycoproteins for degradation (By similarity). Involved in biosynthesis of Lewis X-carrying biantennary N-glycans that regulate neuron stem cell self-renewal during brain development (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 10 family."}
{"protein": "MPSSAHLQDPPPHLSRTLTQDEEQTSLRQSSSCGPSTTSASASESLSGSTKSRISQKKLLEGMLPKIIPTESAAKLLCCYAVFMALTVVVIALSIALSVKKTPQISAVNTYAACQRNWIGFGNKCYYFNETARNWTFSQTLCKEQEAELARFDNEEELNFLKRYKGSSGYWIGLHRESSADPWKWTDNTAYNNLVPIKGEEKHGFLSDNGLSSGKDYIKRKSICSKLNSYTSQCP", "text": "FUNCTION: Lectin-type cell surface receptor. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
{"protein": "MSDSEYLTRAEAVLAAIERSLDDADADIEFERSGNVLTLEFENGTKIIVNLQPPMQEIWIAAKSGGYHFRFVDGEWRDTRNGTEFYAALSEYATQQAGEPVEIAP", "text": "FUNCTION: Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. SIMILARITY: Belongs to the frataxin family."}
{"protein": "MLRSLKALKLNSLNAQKGIRQFCSDSKISGQVIGIDLGTTNSCVAVMQGAEARVLENAEGGRTTPSVVAFTEDNQKIVGLPAKRQMVTNAENTLFATKRLIGRRFDDPMTKKDMTMVPYKIVKGPNGDAWFEVKGKMISPSEAGAMVLQKMKETAETNLGGPVTDAVITVPAYFDDSQRQATRDAGTIAGLKVQRIINEPTAAALAYGFKKDEPKTVAVYDLGGGTFDISILEIVGGVFEVRATNGDTFLGGEDFDNALLEHFVAEFKKEKGIDLTKDTMATQRLREAAEKAKCELSSTLTTEINLPYISAGPSGPVHFNMKLTRSKFEQLVADLIQRTIGPCNICLKDAGLSTSEINEVILVGGMTRMPKVQELAKSTFNKEPFKGVNPDEAVAVGAAIQGGVLKGDTKGIVLVDVTPLSLGIETLGGVFTRLIKKNTNIPASKTDTFSTAADGQSEVEIKVFQGEREMAVDNKLLAKFTLFGLPPLPKGVPQIEVTFDIDVNGMLQVIAKDKATGKAQQVRIQTSGGLSKDDIARILKESEANAEVDRKRKELVEARNNGESVVYQVEKDLVEFKDYLSQPQTEEIKKAVQAVRDVLAKEDGSAIEAEIKKLHDLTRSSFETAYKAKLDSSASKSSSTENKENKDNTTEAEFTEKK", "text": "FUNCTION: May function in protein folding and assembly, and disassembly of protein complexes. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MNHAELRRLFAACDGNQSGRVEYEDFTTVCRELNVPADDIRTLFNKFDLDGDGYINFNDFSSSFQEVSEALNLASLGNCLHSQRRAWDEFENTLDGDVAFYLGRQWDALSELYEGIHSTSDELLLQQFEDLIRALVTEIREHRMESEQLETSLRRTEEVSSSQLAEMEEDLQQQLIHTERRVREEEQKKLDESIAMLQIKHENELADLQTTIERLTKQYQEESKLNTPREDSVKLRAQIKDLMEENEELRASLMKAQMNVSILQVELDKLKNAFTDQKRQHERESDDLKKMVMEFQSYSSHIEMLQEMNKSLYDSNDGLRSALSQENASTKRQLSPRNEVLPRKMKPIRQSTMNQSSFTNEEDTLALVKCWAEKYLDSGVSVQSEMDAMSGIDYDSDDSHHSVETVHHSYSCVPSELEVSEVKPEALRSVARSTVGSISSSLRRRLSAFPVKQNEEDLLDTQDLAPVYRLVLAGDAGSGKSSFLLRLSLNEFRGDIQTTLGVDFQIKKMLVDGEKTNLQIWDTAGQERFRSIARSYFRKAHGVLLLYDVTSESSFLNVREWVEQIRESTDEDIPMCIIGNKVDLRAARPEGSCVSSIHGEKLAMNYNALFCEASAKEGTNVIEAVLHLAREVKKHVKLGRRSESQVKLSLHKRRKTLSNCCGV", "text": "FUNCTION: Binds predominantly GDP, and also GTP. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MTDPRETVPPGNSGEETIGEAFAWLNRTVEAINREAVNHLPRELIFQVWQRSWRYWHDEQGMSESYTKYRYLCIIQKAVYMHVRKGCTCLGRGHGPGGWRPGPPPPPPPGLV", "text": "FUNCTION: Plays a role in nuclear translocation of the viral pre- integration complex (PIC), thus is required for the virus to infect non-dividing cells. Targets specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity results in the degradation of host SAMHD1. In turn, SAMHD1 depletion allows viral replication in host myeloid cells by preventing SAMHD1-mediated hydrolysis of intracellular dNTPs necessary for reverse transcription (By similarity). SUBCELLULAR LOCATION: Virion. Host nucleus. Note=Nuclear just after virion uncoating, or if expressed in the absence of unprocessed GAG. SIMILARITY: Belongs to the lentivirus VPX protein family."}
{"protein": "MSLRYYIKNILFGLYCTLIYIYLITKNSEEYYFLVTDKMLYAIVISTILCPYSKYAIEHIAFNFIKKHFFERRKNLNNAPVAKLNLFMLYNLLCLVLAIPFGLLGLFISIKNN", "text": "FUNCTION: This protein is able to protect a cell, which harbors the plasmid ColE1 encoding colicin E1, against colicin E1."}
{"protein": "MNITLGYIDPVAFSLGPIQVRWYGIIIACGILLGYFIAQAALKQVGLHKDTLIDIIFYSAIVGFIVARIYFVTFQWPYYMNHLSEIPKIWHGGIAIHGGLIGGLISGIIVCKIKNLHPFQIGDIVAPSIILAQGIGRWGNFMNHEAHGGPVSRAFLEHLHLPDFIIRNMYIEGQYYHPTFLYESIWDVIGFVILITLRKRLKLGETFFGYLIWYSVGRFFVEAMRTDSLMLTSHIRVAQLVSVVLILISVIFVIYRRVKYQPIKYENSGPLTWPIKKAK", "text": "FUNCTION: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Lgt family."}
{"protein": "MIRAFSFPVSPERGRLRGWLEGSLAGLCELHWLRERQEYRVQQALRLAQPGMGGAEAEDEEDAEEDEDAAAARRAAAALEEQLEALPGLIWDLGQQLGDLSLESGGLDQESGRSSGFYEDPSSTGGPDSPPSTFCGDSGFSGSGSYGRLGPSDPRGIYASERPKSLGDASPSAPESVGARVAVPRSFSAPYPTAAAGAETCSSAERRARAGPFLTPSPLHAVALRSPRPSGRVPCGSPDGAASRPLDGYISALLRRRRRRGAGQPRTSPGGADGGARRQNGARPRPPEASPPPGGARPAREPSTERAWAAAWEAEVPPEPAPPAAASPPSSPAEGRLVKAQYIPGAPAASRGLPGRAARRRAPPLTRGRSVEQSPPRERPRAAGRRGRLAEPSGRRGSPRARKAARSQSETSLLGRAHAAPPPKYPTAERDEPRPPRPRRGPAPTPTVQACRRWRSTAEIDAPDGRRPRARVPAPRGPAPSPSAPPRRLLYGCAGSDSECSAVGRPVPLGRRMPSGCAPGGYGESESSASEGESPAFSSASSDSDGSGGLVWPQQLVAAAGASPSGPGGAAGGGTPAGPAKVFVKIKASHALKKKILRFRSGSLKVMTTV", "text": "FUNCTION: May be involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins (By similarity). SIMILARITY: Belongs to the dapper family."}
{"protein": "MPAPADIQAATLNKFLAAWREGSAPDTMALWSDDFKQRLLPLSLGESSFRSRDQAALFYPGLVENLRNWELHIKEIVHDSARGTAAVYATSQADTPFSGEKWTNEYAIFLSFSEDGTKVCRLEEMMDSAFYQSFVPKFQRYLMGLGGLKK", "text": "FUNCTION: Monooxygenase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer neosartorin, which exhibits antibacterial activity (PubMed:30394754, PubMed:32105084, PubMed:33891392). The two different monomeric units appear to be synthesized by the same set of enzymes, among which the Baeyer-Villiger monooxygenase nsrF is the key enzyme for the divergence of the biosynthetic routes (PubMed:32105084). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase nsrB (PubMed:32105084). The atrochrysone carboxyl ACP thioesterase nsrC then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (PubMed:32105084). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase nsrE, and oxidized by the anthrone oxygenase nsrD to yield emodin (PubMed:32105084). Emodin is then reduced to emodin hydroquinone by the oxidoreductase nsrR (PubMed:32105084). A-ring reduction by the short chain dehydrogenase nsrJ, dehydration by the scytalone dehydratase-like protein nsrI and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:32105084). The Baeyer-Villiger monooxygenase nsrF accepts chrysophanol as a substrate to insert one oxygen atom at two different positions to yield the precursors of both monomric units (PubMed:30394754, PubMed:32105084, PubMed:33891392). NsrF is promiscuous/flexible in interacting with the 2 (non methylated and methylated) aromatic rings of chrysophanol, thus diverging the biosynthetic pathway at this point (PubMed:30394754, PubMed:32105084, PubMed:33891392). After the hydrolysis of the lactones, methylesterification by the methyltransferase nsrG yields respectively moniliphenone and 2,2',6'-trihydroxy-4-methyl-6-methoxya- cyldiphenylmethanone (PubMed:30394754, PubMed:32105084). The next steps are the hydroxylation by the FAD-dependent monooxygenase nsrK, followed by isomerization by the monooxygenase nsrQ (PubMed:32105084). The short chain dehydrogenase/reductase nsrO then catalyzes the C-5 ketoreduction to give the xanthone skeleton of blennolide C and 5-acetylblennolide A (PubMed:32105084). The acetyltransferase nsrL has a strict substrate specificity and uses only blennolide A but not blennolide C to yield 5- acetylblennolide A as the single-acetylated product (PubMed:30394754). In the final step of the biosynthesis, the heterodimerization of the 2 xanthones, blennolide C and 5-acetylblennolide A, is catalyzed by the cytochrome P450 monooxygenase nsrP (PubMed:30394754). NsrP can utilize at least three different xanthones as its substrates to perform the dimerization reaction (PubMed:30394754). SIMILARITY: Belongs to the avfA family."}
{"protein": "MVSIPEYYEGKNILLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEILSGKLFDRLRDENPDFRQKIIAINSELTQPKLALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPPPVDPKKLIDSLEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGPSGLFIAAGKGILRTMRASNNALADLVPVDVVVNTSLAAAWYSGVNRPRNIMVYNCTTGSTNPFHWGEVGDYLNHSFKTNPLNQVFRHPYVKFYSNNLMLHYWKGVKHTVPALLLDLALRLTGQKPWMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYIENYCMGTKKYVLNEEMSGLPAARKHLNKLRNIRYGFNTILVILIWRIFIARSQMARNIWYFVVSLCYKFLSYFRASSTMRY", "text": "FUNCTION: Catalyzes the reduction of saturated and unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols. It plays an essential role in the production of ether lipids/plasmalogens which synthesis requires fatty alcohols. In parallel, it is also required for wax monoesters production since fatty alcohols also constitute a substrate for their synthesis. SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the fatty acyl-CoA reductase family."}
{"protein": "MPRFPDQLLYIGGRYVPARGGHTLEVVNPATGEVLANVHNAGVDDLDAAVDSAKAGQQRWAALTTVERSRILLRAVALLRERNDALAQLETLNTGKPLSETRSVDVVTGADVLEYYAGVAQALQGAQVPLREGSFFYTRHEPLGVVGAIGAWNYPIQIALWKAAPALAAGNAMIFKPSEVTPLTALKLAEIFTEAGLPDGVFNVLPGDGASVGTALTEHPQIEKISFTGGTATGRKVMASASSSSLKEVTMELGGKSPLIVCADADLDVAADIAMMANFYSSGQVCTNGTRVFVPRALRHAFEARLLARVQRIHIGDPLDERTTFGPLASAAHMQRVLEHIEQGKAEGARLLCGGERLQDGALVQGYYVAPTIFSDCTDVMTIVREEIFGPVLSLLTYDDEDEAVTRANATTYGLAAGVVTPDLARAHRLIHRLEAGICWVNTWGESPAPMPVGGYKQSGVGRENGLATLQAYTRTKSVQIELERYASVF", "text": "FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MEQLQNLIRDALKAIDGATDTQALDALRVQYLGKKGVLTEQLKALGKLPPEERPAAGQAINRAKETVNEALSARLEALSAAEQEARLALESVDVTLPGRRQAVGGLHPVTRTIERITDLLGQLGFQVAEGPEVEDDYHNFEALNIPAHHPARAMHDTFYFDANRLLRTHTSPVQVRVMEQGRPPFRVIAPGRVYRCDSDLTHSPMFHQVEGLLVDEGVTFAHLRGVLDAFLQAFFEQSELKTRFRPSYFPFTEPSAEVDIQCVHCGGDGCRVCSHTGWLEVMGCGMVHPNVFAHVGIDSERYTGFAFGLGVERMAMLRYGVNDLRLFFENDVRFLRQFA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
{"protein": "MTTAARPTFEPARGGRGKGESDLSQLSKQYSSRDLPSHTKIKYRQTTQDAPEEVRSRDFRRELEERERVAVRDKNRDRPTREHTSSVSKKPRLDQIPAANLDADDPLTDEDADEDSDEDSDDDTAALLAELEKIKKERAEEQVRKELEQKAEEERIRMENILSGNPLLNLTGPAAQSQASFKVKRRWDDDVVFKNCAKGVDEMKKRQDKRFVNDTLRSEFHKKFMEKYVK", "text": "FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC15 family."}
{"protein": "MDGDGDPESVSHPEEASPEEQPEEAGAEASAEEEQLREAEEEEEAEAVEYLAELPEPLLLRVLAELPATELVQACRLVCLRWKELVDGAPLWLLKCQQEGLVPEGSADEERDHWQQFYFLSKRRRNLLRNPCGEEDLEGWSDVEHGGDGWRVEELPGDNGVEFTQDDSVKKYFASSFEWCRKAQVIDLQAEGYWEELLDTTQPAIVVKDWYSGRTDAGSLYELTVRLLSENEDVLAEFATGQVAVPEDGSWMEISHTFIDYGPGVRFVRFEHGGQDSVYWKGWFGARVTNSSVWVEP", "text": "FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Prevents formation of cytosolic aggregates of unfolded glycoproteins that have been retrotranslocated into the cytosol. Able to recognize and bind denatured glycoproteins, preferentially those of the high-mannose type. SUBCELLULAR LOCATION: Cytoplasm. Microsome membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MDKLRLEVERWLNHPNVNWELKQQIKELNESEIQELFSLEKPLFGTAGVRNKMAPGYHGMNVFSYAYLTQGYVKYIESINEPKRQLRFLVARDTRKNGGLFLETVCDVITSMGHLAYVFDDNQPVSTPLVSHVIFKYGFSGGINITASHNPKDDNGFKVYDHTGAQLLDTQTNQLLSDLPCVTSMLDLELQPNPKFVHTLDNEKVYKNYFRELKKVLVINNNNFKDIKVVFSGLNGTSVCLMQRFLKYLGYSNIISVEEQNWFDENFENAPNLNPEYKDTWILAQKYAKKNNAKLIIMADPDADRFAIAELNNNQWHYFSGNETGAITAYYKLNHKVFKSPYIVSTFVSTYLVNKIAKRYGAFVHRTNVGFKYIGQAINELSQTNELVVGFEEAIGLITSDKLNREKDAYQAAALLLEIARHCKEQNITLLDFYKRILSEFGEYFNLTISHPFKATATDWKEEIKALFNQLINANLTEVAGFKVVKVHLDKQTNILEFGFENGWVKFRFSGTEPKLKFYFDLTNGTREALEKQAKKIYKFFVNLLKLNKA", "text": "SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MIGELDFPFLGAGSTGGACGFAVANPPLYGMVSAGGPSVFNNGIGCGTCFQILCNGHPACSRRPITVTITDECPGGPCASEPAHFDLSGKAMGALARPGQGDRLRSAGVLRVYYRRVECLYRRTNIAFRMDPGANPYYISFVVEYENGDGDLAYIEIQPADGEFIPMQEMRSAVWKISSGSPLTGPFNIRLTSAESHKVVLAYNVIPANWKPNETYRSVVNFK", "text": "FUNCTION: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin B subfamily."}
{"protein": "MIHIITGSTLGGAEYVGDHLSDLLQEQGFDTKIHNQPNMSEIPAKGTWLIITSTHGAGEYPDNIQPFIQALQNTPPNTSALRYAVVAIGDSSYDTFCAAGKHAYQLLGDIGAKPLANCFTIDVQEHPVPEDAAEAWLKRVINRF", "text": "FUNCTION: Probable electron transporter required for biotin synthase activity. SIMILARITY: Belongs to the flavodoxin family. MioC subfamily."}
{"protein": "MSDEIIVVSTPYLPGHKITKTLGFTWGLIVRSRGLGRNITAGLRSLAGGEIHEYTQLLNQSRQEALDRLKEHAATMGANAVIGVSFDSSETGGVMTEVLAYGTAVVVEPETGAASPVRLG", "text": "SIMILARITY: Belongs to the UPF0145 family."}
{"protein": "MSEDYVLEMIDITKEFPGVKALDGVQLKVKRGTVHALMGENGAGKSTLMKILIGIYTPDRGKIILDGEELKVSTIKHALDRGISMIHQELSPVPNMTVAENIFLGREPSYPFAGWVKMKELVKKTRQLFERLEIDIDPNAKMADLSIANMQMVEIAKAISYHSKLIIMDEPTSAITEKEVHHLFRIIRSLKKEGVSIIYITHKMDELEQITDEVTVLRDGKYIGTKPSHQMTRDELIQMMVGRELNQIFHKPKVPIGEVALSVQGLTKKGKFHDVSFEVRKGEIVGFAGLMGSGRTEVLESVFGVTKPDAGDIYVHGKKATIRSTRDAIRYGMGLLTEDRKLTGLFLPLSVEDNMITVTVNQYTKAGFLQQRKIREDCQRLAEQLSIKTPSLQQLIKYLSGGNQQKALIARWLLHNPDILFLDEPTRGIDVGAKAEIYHLIFELAKNGKAIIVVSSEMPEILGLSDRVIVMHEGRKMGELTREEATQERIMQLATGQLIETKR", "text": "FUNCTION: Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate importer 2 (CUT2) (TC 3.A.1.2) family."}
{"protein": "MSHHWGYSKHNGPENWHKDFPIANGDRQSPVDIDTATAQHDPALQPLLISYDKAASKSIVNNGHSFNVEFDDSQDNAVLKGGPLSDSYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKIGPASQGLQKVLEALHSIKTKGKRAAFANFDPCSLLPGNLDYWTYPGSLTTPPLLECVTWIVLREPITVSSEQMSHFRTLNFNEEGDAEEAMVDNWRPAQPLKNRKIKASFK", "text": "FUNCTION: Catalyzes the reversible hydration of carbon dioxide (By similarity). Involved in the regulation of fluid secretion into the anterior chamber of the eye (By similarity). Essential for bone resorption and osteoclast differentiation (By similarity). Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption (By similarity). Stimulates the chloride-bicarbonate exchange activity of SLC26A6 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
{"protein": "MLVIFLGILGLLANQVLGLPTQAGGHLRSTDNPPEEELKYWCTYMESCKFCWECTHGLCKNKVNESMPTIIENSYLTSCEVSRWYNQCTYDEGNGHYHVMDCSDPVPHNRPHRLRMKIYKKEDL", "text": "FUNCTION: Causes the redistribution of lumenal ER protein to an enlarged ERGIC compartment. SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum-Golgi intermediate compartment. SIMILARITY: Belongs to the asfivirus MGF 110 family."}
{"protein": "MLFLLSPAKSLDYQTPTRVAATEPLYTRQAADLIEILRTKTPVEVAELMDLSDALAGLNVARYAAWQPQADRHNSKPAVLAFNGDVYDGLDARTLATPDLRWAQSHLVILSGLYGALRPLDALQPYRLEMGTRLANPQGPDLYAWWGDTVSDYLNERQSGEPHPVVVNLASQEYFKVVRRGVLKARVVDCVFEDWKGGVYKIISFHAKRARGLMARYAITQRIRRVADLQGFDLAGYAYAPAVSGPDRLVFRRHPAD", "text": "SIMILARITY: Belongs to the UPF0246 family."}
{"protein": "MAAGTSNYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSSARDGGRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGVNDKMAEYTHSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFMAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIHSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGICTILLLLYAFH", "text": "FUNCTION: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV membrane protein Note=Localizes throughout the Golgi apparatus, with lowest levels in the trans-Golgi network. Enriched on vesicular components at the terminal rims of the Golgi apparatus. SIMILARITY: Belongs to the GOSR1 family."}
{"protein": "MSSRKFFVGGNWKMNGDKKSLTELINTLNSGKISADTEVVCGAPTIYLDFARQKLDAKFAVSAQNCYKVAKGAFTGEISPAMIKDCGATWVILGHSERRHVFGESDELIGQKVAHALSENVGVIGCIGEKLDQREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPEQAQEVHKKLREWLKTNVSEDVAKSVRIIYGGSVTGGTCKELGAQPDIDGFLVGGASLKPEFIDIINAKQ", "text": "FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family."}
{"protein": "MVKIAFIGVGKIGQTIAYSVIFDGLASEAILYDIVPELPEKFEHELRHAIATRGLSTEVIGTNSLDDVTNADIILIMAGKPRKPGMSRRDLFIDNAKIQIDLAKQLPPKNPGALYIMVANPVDMMASVFMRFSKQFTISTGDAVETMRLRSYIAKKLKVPANKVTGYVAGEHGEDAVVLWSTVKVNGKPFEEVAKGLTKEEVENYVKSIPGEIIRVMGGTTWGPATIIKDIVRSVVFNEGRVMSIATPRTYQGEIIHISVPIVVGAEIGPSLEGVLPESDRQRLNKSVEDFYRVYKENLDHLLQTVKQ", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily."}
{"protein": "MKMENLISMFCFSSKGSSKRRTKGSSTWFPQPDQHITIRTFRRLKAHQMLSHTWTKTETSLTMEVSKSMADQLEEVNSLPTTLMPRHSIVDPSYRPSIY", "text": "FUNCTION: Pathogenicity determinant (By similarity). May act as a suppressor of RNA-mediated gene silencing, also known as post- transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. SIMILARITY: Belongs to the geminiviridae protein AC4/C4 family."}
{"protein": "MAKNTVSARFRKVDVDEYDENKFVDEEEAGEGQQGPDEGEVDSAIRGGNMMGALQAALKNPPINTKNQSAKDRAENLVLKVLISFKANEIEKAVQSLDKNSTDLLMKYIYKGFESPSDNSSAVLLQWHEKALAVAGVGSIVRVLTARKTV", "text": "FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:17178911). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:17178911). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (By similarity). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection Nucleus. SIMILARITY: Belongs to the ARPC5 family."}
{"protein": "MSEMEKITIENIVASTSLAEHLDLSKIALALEGSEYEPEQFPGLIYRLQEPKTAVLIFRSGKVNCTGAKNLDDVKKTIDIIIDKLKKADIEVYDNPDIIVQNIVAVYDLESNLNLTDIAMSLGLENVEYEPEQFPGLVYRVEEPKVVLLLFGSGKVVCTGAKEENEIEQAVIKVKKDLQKVGLI", "text": "FUNCTION: General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation. SIMILARITY: Belongs to the TBP family."}
{"protein": "MSRLGIMVLTLLLLVFIVTSHQDAGEKQATQRAAINFRWKRSLTRRTATEECEEYCEDEEKTCCGEEDGEPVCARFCLG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O3 superfamily."}
{"protein": "MRASCTPLKAPLRRPERLASSGRFAWVLLLAPLLLLPTSSDACDDPPRFVSMKPQGTLKPSYSPGEQIVYECHLGFQPVTPGQVLALVCQDNNTWSSLQEGCKKRRCPTLADPTNGQVILVNGSTEFGSEVHYVCNNGYYLLGTNISYCEVSSGTGVNWSDNPPTCEKILCQPPPEIQNGKYTNSHKDVFEYNEVVTYSCDPSNGPDEYSLVGESKLTCIGNGEWSSQPPQCKVVKCVYPAIEHGTIVSGFGPKYYYKATVVLKCNEGFNLYGNSVVVCGENSTWEPELPKCIKGHPPRPTDASPPNGAEGLGAGYIVLVIVAVLIGVGLLLCLYCCFCRQRKKGIYVTGESHRQDILFSL", "text": "FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. May act as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity (By similarity). In case of bovine viral diarrhea virus (BVDV) infection, involved in virus attachment to cells. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein Note=Inner acrosomal membrane of spermatozoa."}
{"protein": "MSGLLKYLFGCFILCLLLQGKTHMTSATISKPHETIDIEKQNMTGERNSTLAQQLSFPMEDPTNWNYAILALAFVVLFLAFLILAQNSRANRTRKMKALNGAGGRNETEADSTQKAMMQYVVEVDNLAETDQMLQSKPTYISLNQVAQTSSPKVLPKEGQILVEWKDGNIGFLYTDSKEDDV", "text": "FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids. May modulate slc51a glycosylation, membrane trafficking and stability activities (By similarity). Able to transport taurocholate, estrone sulfate, digoxin, and prostaglandin E(2), but not p-aminohippurate or S-dinitrophenyl glutathione. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the OST-beta family."}
{"protein": "MPIGVPKVPFRSPGEEDASWVDVYNRLYRERLLFLGQEVDSEISNQLIGLMVYLSIEDETKDLYLFINSPGGWVIPGVAIYDTMQFVRPDVHTICMGLAASMGSFILVGGEITKRLAFPHARVMIHQPASSFYEAQTGEFVLEAEELLKLRETLTRVYVQRTGKPLWVVSEDMERDVFMSATEAQAYGIVDLVAVE", "text": "FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the peptidase S14 family."}
{"protein": "MATTSRRPVLTRTKVLVPVLLVIVLAITIIAIFTRLYTDLLFYRSIDFSRVFTTVLYTRILLFVLFGVVMAIIVGTNIVLAYRLRPPLRPLSTEQQNLERYRSVIEPYMLLILLAVTTLFGLAAGLSAAGQWRTWLLWVNGESFGTPDLQFHRDISYYAFSYPFQRFLLGFLLTAVLLSLLVTLLTHYLFGGIRMQTTGERVTPAAKAHISVLLGLLALLKAWAYYLDRFGSVFSSRGVGTGASYTDVHAVLPAKLILLFISLACAVLFIYNIFQRGWTLPLLGAGILVLSSVVIGGIYPAIVQQFQVRPNEATREEPYIARNIAATRAAYGIQDVEPQDYAASTDVTAQQVAADTGTVPNIRLLDPSKLSRTFQQLQQFRGYYGFPPTLDVDRYTVTGADKKSTTQDYVVSVRELNQAGLGTQQRNWINEHLTYTHGKGFVAAPSNTVDVGRPDFDHGVSGFPQDGTFGIKENRVYFGEMSPSYSIVGTRQMEIDGPGPGETQVTTTYQGDGGVSIGSTFRRALFALRFGEKNILLSGDITKNSRILDERNPRDRVSKAAPWLTLDGDPYPAIVNGRVTWILDGYTTSDGYPYSARRTLGDVTADSVTTQSGNRTRQASNQVNYIRNSVKATVDAYNGTVTLYAWDESDPVLRTWMKAFPDTVKPKSDIPPSLRAHLRYPEDLFKVQRDLIGQYHISNPRDFYSQEDFWDVSDSPDGSGQPQPPFYVYSQLPGRKDPSYNLTSPLISARSSKLAAYMAVSSDPANYGRFTLLKLPAGNTINGPVQVQNAIEGNGDVAKQLSLWRSGGATTIEGNLLTLPLAGGLLYVEPYYVQARGSTGYPTLQGVATAFGDRIGFGASLGEALDKVFGAGAGAAAAGAGIGATTTDAGQDGTPAPRSGQGGAGVPPPGQTALQDAVGDADRAYQAGQDALRKSPPDFTAYGKAQSELADALGRLRTLSSPAATPPAATATRAGASVPASPVPASPAAKPPAPSPSATVAGGDTPGPPGARAAPAPG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0182 family."}
{"protein": "MKEKRDLKIQAIENGTVIDHITAGQALNVLRILRISSAFRATVSFVMNAPGARGKKDVVKIEGKELSVEELNRIALISPKATINIIRDFEVVQKNKVVLPSYVEGVVRCMNSNCISNSSEPIKSKFSVLRTEEEGVSLHCLYCEHVISEEIAENLL", "text": "FUNCTION: Involved in allosteric regulation of aspartate carbamoyltransferase. SIMILARITY: Belongs to the PyrI family."}
{"protein": "MAAGSTGERPFFEIITSIRYWVIHFVTLPSIFLAGFLFVSTGLAYDAFGTPRPDAYFQASESKAPVVSQRYEGKSELDVRLK", "text": "FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbE/PsbF family."}
{"protein": "MGLSDGEWQLVLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLKSEDEMKASEELKKHGVTVLTALGGILKKKGHHEAELKPLAQSHATKHKIPVKYLEFISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMAAKYKELGFQG", "text": "FUNCTION: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. SIMILARITY: Belongs to the globin family."}
{"protein": "ADDKNPLEECFCEDDDYCEG", "text": "FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18384385). Is active on L-Ile, L-Leu, L-Met, L-Phe, L- Trp, and L-Tyr (PubMed:18384385). Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
{"protein": "MAKYRIMTFDGGGTLGALSLQLLNRLARQNPKLISRTHVFSGNSIGSFTALALASGRSPRETLQYFEDEILPAFSISRPGGPVFNQQLPYSGFIKAVRNFFPADLQLIDLRKRIVVPSFKLYSQKLDRWTPVLFHNFPGSPYLNEKVSDVILRSSGAPATQRAYQNYVDGYVVATNPSTASIAFAVGKANVPLDQIAVLSIGTGEAPTRLRRDTRGWGMVSADNIRPENLKNLPPNWGVLLDRSPNEPLLPFLQMIAGGNGYYESMVSANLLGDRFFRLDPRIPNFSKTDPAVVPAVIEIANKTNLQPANQFIEKNWGSK", "text": "SUBCELLULAR LOCATION: Spore coat."}
{"protein": "MKALQFGAGNIGRGFIGKTLSESGFSVIFSDVNQNIVDAINYNREYFVKIIGSNQNKTVNIKRVSAINSNDSNIKKIISSVDLITTAVGPTALEKIALIITQGIIFKIKNQFTKPLNIIACENKIKSSSFLKQVVLKNLPIKYHDYLNKYIGFIDCSIDTIIPSINNKDDLFLTVEEFKEWIVNINQFKGAVLKIVDMKFSNNLDAFIERKLFTLNTGHAIAAYLGLIKNYKTIQDAISDKKIRVIVRSAMEESGSVLIKRYNFNKNDHLDYIEKIFLRFENPFLSDKLERIGRNPLQKLRREDRLIKPFLGAFEYNLPYSNLAKGIAAAFYYHNKNDLESIELSSSIKKQGLESTIIKICDLPVNSKEVYSIILEYNLIKKIIR", "text": "SIMILARITY: Belongs to the mannitol dehydrogenase family."}
{"protein": "MAQPAAIIRIKNLRLRTFIGIKEEEINNRQDIVINVTIHYPADKARTSEDINDALNYRTVTKNIIQHVENNRFSLLEKLTQDVLDIAREHHWVTYAEVEIDKLHALRYADSVSMTLSWQR", "text": "FUNCTION: Catalyzes the epimerization of carbon 2' of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP) (PubMed:9182560) (PubMed:9651328). Is required for tetrahydromonapterin biosynthesis, a major pterin in E.coli (PubMed:19897652). FUNCTION: Catalyzes the epimerization of carbon 2' of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP). Is required for tetrahydromonapterin biosynthesis. SIMILARITY: Belongs to the DHNA family."}
{"protein": "MPPLPQNYAQQQPSNWDKFKMGLMMGTTVGVCTGILFGGFAIATQGPGPDGVVRTLGKYIAGSAGTFGLFMSIGSIIRSDSESSPMSHPNLNLQQQARLEMWKLRAKYGIRKD", "text": "FUNCTION: Required for cell viability in cells lacking mitochondrial DNA. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MGR2 family."}
{"protein": "MFTDCSSSTTSRLIHLYNRNGVFLPRPSVSQFSLRTTASTWRCTLSIRSSSSPSAIVIDGKAEAKKIRDDIKIEVSRMKESIGVVPAEDSSEEEVLKYVSGFNDDPSVHGVLVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNIEFKGKRAVVIGRSNIVGMPAALLLQKEDATVSIIHSRTMNPEELTRQADILISAVGKPNMVRGSWIKPGAVLIDVGIKPVEDPSAAGGERLVGDICYVEASKIASAITPVPGDVGPMTIAMLLSNTLTSAKRIHNFQ", "text": "FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family."}
{"protein": "MTMAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDILTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHVEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYETSTPSLSAKELAELANRAELPLSWSVSSKLNQHAELETEEEEKNPEEQTERNGDVANLENESKV", "text": "FUNCTION: This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G- protein-coupled receptors. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ6 subfamily."}
{"protein": "MDQDYERRLLRQIIIQNENTVPCVSEMRRTLTPANSPVSSPSKHGDRFIPSRAGANWSVNFHRINENEKSPSQNRKAKDATSDNGKDGLAYSALLKNELLGAGIEKVQDPQTEDRRLQPSTPEHKGLFTYSLSSKRSSPDDGNDVSPYSLSPVSNKSQKLLRSPRKPTRKISKIPFKVLDAPELQDDFYLNLVDWSSLNVLSVGLGTCVYLWSACTSQVTRLCDLSVEGDSVTSVGWSERGNLVAVGTHKGFVQIWDAAAGKKLSMLEGHTARVGALAWNADQLSSGSRDRMILQRDIRTPPLQSERRLQGHRQEVCGLKWSTDHQLLASGGNDNKLLVWNHSSLSPVQQYTEHLAAVKAIAWSPHQHGLLASGGGTADRCIRFWNTLTGQPLQCIDTGSQVCNLAWSKHANELVSTHGYSQNQILVWKYPSLTQVAKLTGHSYRVLYLAMSPDGEAIVTGAGDETLRFWNVFSKTRSTKESVSVLNLFTRIR", "text": "FUNCTION: Substrate-specific adapter for the anaphase promoting complex/cyclosome (APC/C) E3 ubiquitin-protein ligase complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulators of the cell cycle do not accumulate prematurely. At the G1/S transition FZR1 is phosphorylated, leading to its dissociation from the APC/C. Following DNA damage, it is required for the G2 DNA damage checkpoint: its dephosphorylation and reassociation with the APC/C leads to the ubiquitination of PLK1, preventing entry into mitosis. Acts as an adapter for APC/C to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. Through the regulation of RBBP8/CtIP protein turnover, may play a role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family."}
{"protein": "MKLRIGVIGTGAIGKEHINRITNKLAGGEIVAVTDVNQEAAQQVVTDYSLNAKVYPDDDSLIAAENVDAVLVTSWGPAHESSVLKAIKANKFVFCEKPLATTAEGCMRIVNEEVKAGKRLVQVGFMRRYDSGYVQLKEAIDNRVIGEPLMIHCAHRNPVVGDNYTTDMAVVDTLVHEIDALHWLINDDYESVQVIYPKKSKNALPHLRDPQIVIIETKGGVVINAEIYVNCKYGYDIQCEIVGEDGIVKLPEPSSISLRKDGKFSTDILMDWQRRFVDAYDVEIQDFIDSIQQKGEVSGPTAWDGYIAAVTTDACVKAQESGQKEPVALQEKPEFYQTFTTVKK", "text": "FUNCTION: Involved in the oxidation of myo-inositol (MI) and D-chiro- inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D- chiro-inositol (1KDCI), respectively. SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MARKSLIQRERKRKKLEQKYHWIRRSSKTEINKVPSLSDKWEIHGKLQSPPRNSAPIRLHRRCFSTGRPRANYRDFGLSGHILREMVHACLLPGATRSSW", "text": "FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS14 family."}
{"protein": "MAALGGDGLRLLSVSRPERQPESAALSGPGSGLCCWVSVFSCFSLACSYVGSLYVWKSELPRDHPAVIKRRSTSVLVVSSLSPLCVLLWRELTGIQPGTSLLTLMGFRLEGIFPAALLPLLLTMILFLGPLMQLSMDCPCDLTDGLKVVLAPRSWARCLTDMRWLRNQVIAPLTEELVFRACMLPMLAPCTGLGPAVFTCPLFFGVAHFHHIIEQLRFRQSSVGSIFVSAAFQFSYTAVFGAYTAFLFIRTGHLIGPVLCHSFCNYMGFPAVCAALEHPQKWPLLAGYALGVGLFLLLLQPLTDPKLYGSLPLCMLLERTGASETLLCS", "text": "FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K- Ras, N-Ras, H-Ras, RAP1B and G-gamma-1 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase U48 family."}
{"protein": "MNYSNNYIEHQNKKKTIIIFFRQFKKQKPMLRMGVHLVVINKNTFNFFNRQNNYFNSGKTKKIFVIDRFLAVHQIVRKKLQLVGVTALLLACKYEEVSVPVVDDLILISDKAYSRREVLDMEKLMANTLQFNFSLPTPYVFMKRFLKAAQSDKKLEILSFFMIELCLVEYEMLEYLPSKLAASAIYTAQCTLKGFEEWSKTCEFHTGYNEEQLLACARKMVAFHHKAGTGKLTGSTTHLSSFMLQEVNQLGFCFKGGKNYNKNLI", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily."}
{"protein": "MSALAPITGTLKKRIITDIVIGFSLGGVMASYWWWGFHKNVIDRREAFYADLAEKKKAEN", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the fungal cytochrome c oxidase subunit 7a family."}
{"protein": "MTIRLVIVEPEGAYNLGFIARLVKNFLIDEFYVVNPKCDINEAIKFSAKGSEVIEKMMKITNNFDDAIRDVDLKIATSSIADIKGDLLRKSIRPIDLERLIKDKKVAFIFGRESVGLTREEIAKSDFLLFIPANPEYPVLNLSHAVGIVLYELWRNRDNKVPTVSSEPIKLIDDYSKKITDILVNKEATKSMYLVLKRVLIKGIEDNEEAMTIVRILRKIYVRLAKKENESDKLL", "text": "FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) at position 32 in tRNA. Is specific for cytidine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family."}
{"protein": "MEDYVKIEKIGEGTYGVVYKGRHKSTGQVVAMKKIRLESEEEGVPSTAVREVSLLQELKHPNVVRLLDVLMQESRLYLIFEFLSMDLKKYLDSIPSGQYMDPMLVKSYLYQILEGIYFCHRRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGVPVRVYTHEVVTLWYRAPEVLLGSPRYSTPVDVWSTGTIFAELATKKPLFHGDSEIDQLFRIFRTLGTPNNDVWPDVESLPDYKNTFPKWKEGSLSSMVKNLDKNGLDLLAKMLIYNPPKRISAREAMTHPYFDDLDKSTLPAACINGV", "text": "FUNCTION: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. May play a role in regulating the amplitude of the cyclic expression of circadian clock genes. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MIGIVSYGSYVPKFRIRVEEIARVWGEDAKKIKDGLGVHEKSVPGMDEDAATIAVEAAREAIRRAGINPEEIGAVFVGSESHPYAVKPTATIVGEALGVGNDYFAADLEFACKAGTAGMQICYSMVKAGMIKYGLAIGADTSQARPGDALEYAAAAGGAAFIIGENPIAEVEATYSFTSDTPDFWRRDLQPYPSHGGRFTGLPAYFRHVISAAKGLMEKYGYKVEDFDYAVFHMPNAKFPVRAAKMLGFSMEHISQGLVVKAIGNTYSGSSLLGLAATLDVAEPDERILLVSFGSGAGSDAFAIRVTDAIENYPREPKVWEKIERKAYVDYAIYLKHRRKIKA", "text": "SIMILARITY: Belongs to the thiolase-like superfamily. UPF0219 family."}
{"protein": "MSKLGVLLTICLLLFPLTALPLDGDQPADQAAERMQAEQHPLFDQKRRCCKFPCPDSCRYLCCG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
{"protein": "MKVRKYITLCFWWAFSTSALVSSQQIPLKDHTSRQYFAVESNETLSRLEEMHPNWKYEHDVRGLPNHYVFSKELLKLGKRSSLEELQGDNNDHILSVHDLFPRNDLFKRLPVPAPPMDSSLLPVKEAEDKLSINDPLFERQWHLVNPSFPGSDINVLDLWYNNITGAGVVAAIVDDGLDYENEDLKDNFCAEGSWDFNDNTNLPKPRLSDDYHGTRCAGEIAAKKGNNFCGVGVGYNAKISGIRILSGDITTEDEAASLIYGLDVNDIYSCSWGPADDGRHLQGPSDLVKKALVKGVTEGRDSKGAIYVFASGNGGTRGDNCNYDGYTNSIYSITIGAIDHKDLHPPYSEGCSAVMAVTYSSGSGEYIHSSDINGRCSNSHGGTSAAAPLAAGVYTLLLEANPNLTWRDVQYLSILSAVGLEKNADGDWRDSAMGKKYSHRYGFGKIDAHKLIEMSKTWENVNAQTWFYLPTLYVSQSTNSTEETLESVITISEKSLQDANFKRIEHVTVTVDIDTEIRGTTTVDLISPAGIISNLGVVRPRDVSSEGFKDWTFMSVAHWGENGVGDWKIKVKTTENGHRIDFHSWRLKLFGESIDSSKTETFVFGNDKEEVEPAATESTVSQYSASSTSISISATSTSSISIGVETSAIPQTTTASTDPDSDPNTPKKLSSPRQAMHYFLTIFLIGATFLVLYFMFFMKSRRRIRRSRAETYEFDIIDTDSEYDSTLDNGTSGITEPEEVEDFDFDLSDEDHLASLSSSENGDAEHTIDSVLTNENPFSDPIKQKFPNDANAESASNKLQELQPDVPPSSGRS", "text": "FUNCTION: Processing of precursors of alpha-factors and killer toxin. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily."}
{"protein": "MFKFGKKLMTVVLAASMSFGVFAATTGATDYWQNWTDGGGTVNAVNGSGGNYSVNWQNTGNFVVGKGWTYGTPNRVVNYNAGVFSPSGNGYLTFYGWTRNALIEYYVVDNWGTYRPTGTYKGTVNSDGGTYDIYTTMRYNQPSIDGYSTFPQYWSVRQSKRPIGVNSQITFQNHVNAWASKGMNLGSSWSYQVLATEGYQSSGSSNVTVW", "text": "FUNCTION: Involved in depolymerization of xylan, a major component of the lignocellulosic substrates. Acts as an endo-xylanase that efficiently hydrolyzes the beta-1,4 glycosidic linkages between the xylopyranosyl residues in the main chain of the polymer, leading to the degradation of xylan into short oligosaccharides. Shows high activity toward branched xylans from both softwoods (arabinoxylans) and hardwoods (glucuronoxylans), showing the highest activity on beechwood xylan. Also hydrolyzes long xylooligosaccharides (with a degree of polymerization of greater than or equal to 5), while oligomers shorter than xylotetraose are not degraded. Is not active on carboxymethyl cellulose (CMC), Avicel, starch, polygalacturonic acid, laminarin, pectin, beta-D-barley glucan, or lichenan. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MVEMSNVRKEIVAFIVLLSLLLLWTLFTQAPINTSTPVNTSTPVNTSTPVNTSTPVNTSTPVSTSTIDPESQVAGMAIQFKNGTSESEVKSTLQNYNMTQNYRITFDANHYPEYYIMVNKENITDVKGKLEKEKTWTEPIPAIEKGNYYIITISERVIHNKNFIMMLSKYNLQLEKFVWCDIRFLYSDGPLTYWISKEDAIRLKNELEQNENIFTIRFDYLYPPYDPTT", "text": "SIMILARITY: Belongs to the UPF0228 family."}
{"protein": "MLGAVVVRVTDLNLVSVATPGRVQVWATRLGSGAPVPNVQLSALAVKYDWQDGSRVVSRRTLAPVRTDAQGLATFSLRDGEQLSVRGQVTLGGQPHSAQLGRTENELWTGVAERARALIQTDKPVYRPGETLRGFAVLRRLGAGTRLPYTGPVTVRLRAGYPDATLAQLTVKPDADGLVRFSLPLPQDVKIGGYSLEVELPAAPSASNPNPEPDVSQVPVEVRAFVKPLFTLDLSGPQEVVSGTPLTLSARGELYQGGPANVQAEAFMVDGYASDELYPDYDAGDNGLRYQDLNSDEVYGENAAPGIDPKRRPDQTLTLRGGRATLPLKLQAKNGQPTRYAVALRARDEYGRDVWARRPVTVYPAAIKFVQPRVEGAERRRVSVAVQQVGSGKALAGRRVQAEVVRVFYVTQPDGKSVRREQRISQSVLTSDAAGRVTLNVTLTPGQEGGYVARLSTQDSAGRTARASLDIGSVYKSGAERQAPTLVLSPERSRYQPGDTARLTLNTDLPVGTPLLLSVNAEDRGQVKLIQVTGPTMTLTWPVTAALGPAFSVSAVAVRGGQTAQAFSGELLVPRFDQRLDVQVTAGSEVKPGAEVTFTVRTSRGGQPASALVTLAAVHESVYAVVGDPTPNPWRFLWGATTPQFEIRSSSSQADDGRGGGGGSEAVFYRSDLREVAAFQAVRTDAQGTAKVTVRMPEGLGSYRLSARAFTRTGAAGEARGEQRVGLPFAVRLIRPRVLTAGDTGSVAVSAADRTGQGGNVTLTLGANGQTQTANSPLQGGSATRLFSIKAPQDAQALTLTASAQRGANGERDGLRETVPVRPAGARQLLSGSGSVGADKAGGNASVSLKWPQEAQPESLTLDLAATPLQLALTGLDAALADPADRWVTTDALSARLSSNLDLAALAGPFGWPEVRTRALAQARRDLASLLALRGSDGWGWTEGSPASAEMTARALDALVQAKGAGLTDAVTLQVVRQQAELLLKKSPNSPVLAAGWRGLGPPLRPCDWPAPG", "text": "SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily."}
{"protein": "MGCWGRNRGRLLCMLALTFMFMVLEVVVSRVTSSLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVMGALVNAIFLTGLCFAILLEAIERFIEPHEMQQPLVVLGVGVAGLLVNVLGLCLFHHHSGFSQDSGHGHSHGGHGHGHGLPKGPRVKSTRPGSSDINVAPGEQGPDQEETNTLVANTSNSNGLKLDPADPENPRSGDTVEVQVNGNLVREPDHMELEEDRAGQLNMRGVFLHVLGDALGSVIVVVNALVFYFSWKGCSEGDFCVNPCFPDPCKAFVEIINSTHASVYEAGPCWVLYLDPTLCVVMVCILLYTTYPLLKESALILLQTVPKQIDIRNLIKELRNVEGVEEVHELHVWQLAGSRIIATAHIKCEDPTSYMEVAKTIKDVFHNHGIHATTIQPEFASVGSKSSVVPCELACRTQCALKQCCGTLPQAPSGKDAEKTPAVSISCLELSNNLEKKPRRTKAENIPAVVIEIKNMPNKQPESSL", "text": "FUNCTION: Zinc ion:proton antiporter that could function at the plasma membrane mediating zinc efflux from cells against its electrochemical gradient protecting them from intracellular zinc accumulation and toxicity (PubMed:31471319). Alternatively, could prevent the transport to the plasma membrane of CACNB2, the L-type calcium channels regulatory subunit, through a yet to be defined mechanism. By modulating the expression of these channels at the plasma membrane, could prevent calcium and zinc influx into cells. By the same mechanism, could also prevent L-type calcium channels-mediated heavy metal influx into cells (By similarity). In some cells, could also function as a zinc ion:proton antiporter mediating zinc entry into the lumen of cytoplasmic vesicles. In macrophages, can increase zinc ions concentration into the lumen of cytoplasmic vesicles containing engulfed bacteria and could help inactivate them (PubMed:32441444). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Note=Localization to the plasma membrane is regulated by cellular zinc status. Recruitment to the plasma membrane from an internal pool is stimulated by zinc while in absence of zinc the plasma membrane pool is endocytosed and degraded (PubMed:31471319). Localizes to the basolateral surface of enterocytes (By similarity). Localizes to zinc-containing intracellular vesicles in macrophages (PubMed:32441444). SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
{"protein": "MIDYEFLRFIWWVLVIVLLIGFSVTDGFDMGVTALLPVIGKKEVERRIMINTIAPHWDGNQVWLLTAGGAIFAAWPIVYAVSFSGFYIALVLVLAALFLRPLGFEYRAKIDNPTWRSVWDWGLFAGGFVPALVFGVAFGNLLQGVPFHFNELTQVTYTGSFFELLNPFALLCGVISLSMLVTHGANWLQMKTTEALRDRARTVSQIGSIVTLIAFVLAGVWLYSKDGYVVTSTIDHFAPSSPMNKEVAVETGAWFRNFNEMPILWIFPALAVVAALLNAAFSKANRCGFAFFFSALTMAGVIITAAVSMFPFVMPSSSHPEQSLLMWDSTSSELTLTLMLIFAVVFVVIALAYTIWSYSKMFGRLDANFIDKNKHSLY", "text": "FUNCTION: Probable cytochrome oxidase subunit. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2 family."}
{"protein": "MISILMQTLKIATRQSPLALWQAEHIRDRLQALYPELKVELVKFVTQGDKILDTPLAKIGGKGLFVKELEAALLDGRADLAVHSMKDVPMHLPEGLSLAVICEREDPLDAFVSNHVMSFDQLPLGARVGTSSLRRKCQILKQRPDLEIIDLRGNVGTRLAKLDDGQYDAIVLASAGLKRLGLISRIRHSINAEISLPAVGQGALGLECRANDKKILDLIAPLAHQPTSACVRAERAFNAYLEGGCQVPIAGFATLTQECLTLEGRVGSVDGKTLLKDHVEGHADQAEVLGVQLAKQLLAQGAGELLRDLYQ", "text": "FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. SIMILARITY: Belongs to the HMBS family."}
{"protein": "METLSNASGTFAIRLLKILCQDNPSHNVFCSPVSISSALAMVLLGAKGNTATQMAQALSLNTEEDIHRAFQSLLTEVNKAGTQYLLRTANRLFGEKTCQFLSTFKESCLQFYHAELKELSFIRAAEESRKHINTWVSKKTEGKIEELLPGSSIDAETRLVLVNAIYFKGKWNEPFDETYTREMPFKINQEEQRPVQMMYQEATFKLAHVGEVRAQLLELPYARKELSLLVLLPDDGVELSTVEKSLTFEKLTAWTKPDCMKSTEVEVLLPKFKLQEDYDMESVLRHLGIVDAFQQGKADLSAMSAERDLCLSKFVHKSFVEVNEEGTEAAAASSCFVVAECCMESGPRFCADHPFLFFIRHNRANSILFCGRFSSP", "text": "FUNCTION: Granzyme B inhibitor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily."}
{"protein": "MQKEIFIAGGCFWGVERYFQKVKGVLDTKACYINGGFEGVKYKEVCEGSSHVEAVRVIYDNSKITEEDLWKLYLRIINPYSLNKQGNDRGVQYRIGLYSYDKDLLKKFSDLNEAFMKSEGKKNYIEIQKVEDVTLAEEYHQNYLLKNVNGYCHINLDDIPEEYQKQ", "text": "FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family."}
{"protein": "MTAPHDPLDDIQADPWALWLSGRTRTALELPHYRRAAVLVALTREADPRVLLTVRSSELPTHKGQIAFPGGSLDAGETPTQAALREAQEEVALDPAAVTLLGELDDVFTPVGFHVTPVLGRIAPEALDTLRVTPEVAQIITPTLAELRAVPLVRERRTLPDGTEVPLYRYPWRGLDIWGMTARVLHDLLEQGPG", "text": "SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily."}
{"protein": "MSSQPSKDLETFENPQPGRDYTIRIRVPEFTCLCPKTGQPDFATLFLDYVPRARCVELKSLKLYVWAFRDQGAFHEKVTNEILNDLVAATDPNFMRLTAEFNVRGGVYTTVVAEHRHPDWQPPVPVTLP", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily."}
{"protein": "GRADYNFGYGLGRGTRKFFNGIGRWVRKTF", "text": "FUNCTION: Bacteriocin with activity against species of Lactobacillus, Lactococcus, Pediococcus, Leuconostoc and against B.subtilis and, to a lesser extent, against B.coagulans, B.cereus and species of Enterococcus, Listeria, Kocuria, Staphylococcus, Corynebacterium, Salmonella, Pseudomonas and Escherichia. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MVMKQTKQTNILAGAAVIKVLEAWGVDHLYGIPGGSINSIMDALSAERDRIHYIQVRHEEVGAMAAAADAKLTGKIGVCFGSAGPGGTHLMNGLYDAREDHVPVLALIGQFGTTGMNMDTFQEMNENPIYADVADYNVTAVNAATLPHVIDEAIRRAYAHQGVAVVQIPVDLPWQQIPAEDWYASANSYQTPLLPEPDVQAVTRLTQTLLAAERPLIYYGIGARKAGKELEQLSKTLKIPLMSTYPAKGIVADRYPAYLGSANRVAQKPANEALAQADVVLFVGNNYPFAEVSKAFKNTRYFLQIDIDPAKLGKRHKTDIAVLADAQKTLAAILAQVSERESTPWWQANLANVKNWRAYLASLEDKQEGPLQAYQVLRAVNKIAEPDAIYSIDVGDINLNANRHLKLTPSNRHITSNLFATMGVGIPGAIAAKLNYPERQVFNLAGDGGASMTMQDLATQVQYHLPVINVVFTNCQYGFIKDEQEDTNQNDFIGVEFNDIDFSKIADGVHMQAFRVNKIEQLPDVFEQAKAIAQHEPVLIDAVITGDRPLPAEKLRLDSATSSAADIEAFKQRYEAQDLQPLSTYLKQFGLDDLQHQIGQGGF", "text": "FUNCTION: Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate. SIMILARITY: Belongs to the TPP enzyme family."}
{"protein": "MTDQGENEKKQRRSNATIAVACLSFFVCMIGAAYASVPLYRIFCQVTGYGGTTQRVEQYSDTILDKTIKVRFDANIANGLPWDFKPMQREVTVRIGETTMIKYEAHNLFGEETYGRASFNVAPGRAGAYFNKVECFCFTDNTLKPGEDLELPVVFFVDPEFVNDPDLKDVKTITLSYTFFPIDKPKPVVNAKAVGSTRNGG", "text": "FUNCTION: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I. FUNCTION: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the COX11/CtaG family. SIMILARITY: Belongs to the COX11/CtaG family."}
{"protein": "MAARRANCALVLVLALALLAARDAGAAAVPKPNWLGGLSRAAFPKRFVFGTATSAYQVEGMAASGGRGPSIWDAFAHTPGNVAGNQNGDVATDQYHRYKEDVNLMKSLNFDAYRFSISWSRIFPDGEGRVNQEGVAYYNNLINYLLQKGITPYVNLYHYDLPLALEKKYGGWLNAKMADLFTEYADFCFKTFGNRVKHWFTFNEPRIVALLGYDQGTNPPKRCTKCAAGGNSATEPYIVAHNFLLSHAAAVARYRTKYQAAQQGKVGIVLDFNWYEALSNSTEDQAAAQRARDFHIGWYLDPLINGHYPQIMQDLVKDRLPKFTPEQARLVKGSADYIGINQYTASYMKGQQLMQQTPTSYSADWQVTYVFAKNGKPIGPQANSNWLYIVPWGMYGCVNYIKQKYGNPTVVITENGMDQPANLSRDQYLRDTTRVHFYRSYLTQLKKAIDEGANVAGYFAWSLLDNFEWLSGYTSKFGIVYVDFNTLERHPKASAYWFRDMLKH", "text": "FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta- D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L- arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MTTQVVNVIGAGLAGSEAAYQIAKRGVQVRLYEMRPVRQTPAHHTDKFAELVCSNSLRANTLTNAVGVIKEEMRLMDSVIIRAADECSVPAGGALAVDRHEFAAKVTEYVKNHPNVTVMNEEITEIPEGPTIIATGPLTSPDLSAQLKELTGEDYFYFYDAAAPIVEKDSIDMNKVYLKSRYDKGEAAYLNCPMTEEEFDRFYEALIAAETVPLKEFEKEIFFEGCMPVEVMASRGRQTLVFGPMKPVGLEDPKTGKTPYAVVQLRQDDAAGTLYNIVGFQTHLKWGPQKEVLQLIPGLENAEIVRYGVMHRNTFINSPNLLRPTYQYKQRDDLFFAGQMTGVEGYVESAASGLLAGINAARLVKGEEPIVLPPVTAMGSMANYITATNAKNFQPMNANFGLFAPLEKKIKKKAERNEAYATRALETIRNFVNI", "text": "FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmG family. TrmFO subfamily."}
{"protein": "MEAKAGPTAATDGAYSVSAEETEKWMEQAMQMAKDALDNTEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQALDWCRRRGRSPSEVFEHTVLYVTVEPCIMCAAALRLMRIPLVVYGCQNERFGGCGSVLDIASADLPSTGKPFQCTPGYRAEEAVEMLKTFYKQENPNAPKSKVRKKECHKS", "text": "FUNCTION: Probably participates in deamination of adenosine-34 to inosine in many tRNAs. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family. ADAT2 subfamily."}
{"protein": "MSKVLTSLPVGQRVGIAFSGGLDTSVAVAWMRDKGAIPCTYTADIGQYDEPDVSGVPARAREYGAEIARVVDCRAQLVEEGLAALACGAFHIRSGGRIYFNTTPLGRAVTGTILVRAMHEDGVDIWGDGSTFKGNDIERFYRYGLLANPQLRIYKPWLDPDFVHELGGRTEMSQWLTSHGLPYRDSQEKAYSTDANIWGATHEAKTLEHLDTSLEVVTPIMGVRFWDPAVDIATEDVTVAFEQGRPVALNGRRFDDPVELVEEANAIGGRHGLGMSDQIENRIIEAKSRGVYEAPGMALLWLTYERLMNAIHNEDTLANYQISGRRLGRLLYEGRWLDPQALMLRESIQRWVASVVTGEVTVRLRRGEDYTIVRTEGPALSYHPEKLSMERTSNSAFGPTDRIGQLTMRNLDIADSRAMLEMYAGQPLDQGQVLVENGTLFGELPSGGFDQITENPEVQAEPEEEALDAAAMEAGTD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2 subfamily."}
{"protein": "MARSLCFMAFAILAMMLFVAYEVQARECKTESNTFPGICITKPPCRKACISEKFTDGHCSKLLRRCLCTKPCVFDEKMIKTGAETLVEEAKTLAAALLEEEIMDN", "text": "FUNCTION: Involved in floral organogenesis. May play a protective role in flowers by protecting the reproductive organs from potential pathogen attack. SUBCELLULAR LOCATION: Secreted, cell wall Vacuole Note=Possibly the cell wall or vacuole. SIMILARITY: Belongs to the DEFL family."}
{"protein": "MADLIPLIATDSLPSNRARRPEWLKVRAPGGANYHDVFRLMREQNLHTVCEEAHCPNIGECWNHRTATFLLLGNICTRGCRYCAIGKGKPEPIDEHEPERVAASVAHLKLKFAVLTSVNRDDVPDGGASIFARTIELIRQKAPDCKVEVLIPDFDGNWEALETVLAAEPDVLNHNIETVPRLFRRFRPRARFEQSIELLARARAARPYLVTKSGMMVGAGETNEEVYQVIDRLRDVDVNVLTIGQYLSPGASYWPVDRYVTPAEFAEFRRYALERGFRHVESGPLVRSSYHAHLHVNAQQH", "text": "FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase family."}
{"protein": "MANIDNKEQTELDQQDMEDVEDIEEEEAGEDANSKARQLTAQMMQNPQVLAALQERLDDLVGTPTGYIESLPKVVKRRVNALKNLQVKCAQIEAKFYEEVHELERKYAALYQPLFDKRSDIINATYEPTEEECEWKVDEEEDISGDLKDKAKLEEEKKDEEKEDPKGIPEFWLTVFKNVDLLSDMVQEHDEPILKHLKDIKVKFSEAGQPMSFTLEFHFEPNDFFTNEVLTKTYKMRSEPDESDPFSFDGPEIMGCTGCLIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVPNDSFFNFFSPPEVPENGELDDDAEAILTADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADDEEGEEEADEDNDPDYEPKKDQNPAECKQQ", "text": "FUNCTION: Acts as a chaperone for the linker histone to facilitate deposition of histone B4 onto linker DNA. Required for both remodeling of sperm chromatin into nucleosomes, and linker histone binding to nucleosome core dimers. Plays a role in tissue-specific gene regulation. Required for primitive hemopoiesis, acting upstream of tal1/scl (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Cytoplasmic prior to the midblastula transition, becoming predominantly nuclear subsequently. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
{"protein": "MTANAPITQDVMTLPRKLPEGGPVNIVGLTREELLAALVAAGTPERQAKMRAGQVWQWVYHWGVRDFAQMTNLAKDYRALLAEHFAIVLPEVVTRQISADGTRKYLIRIAGGHEVETVYIPEEGRGTLCVSSQVGCTLTCSFCHTGTQKLVRNLTAAEIVGQLMLVRDDLGEWPERGAPKDETRLVSNLVLMGMGEPLYNFENVRNAMKVVMDGEGLSLSRRRITLSTSGVVPEIARTAEEIGCQLAISFHATTDEVRDILVPINKRWNIRTLLDSLRDYPRLSNSERITFEYVMLDGVNDTDADARRLVKLISGIPSKINLIPFNEWPGAPYRRSTPERIAAFADIIYKAGYASPIRTPRGEDIMAACGQLKSATERARKSRAQIAAETGL", "text": "FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family."}
{"protein": "MSLIINTFYSNKEIFLQELISNASDALDKIRYESLTDPSKLDGGKELKIDIIPNPRECILTLVNTGIGMTKADLINNLGAIAKSGTEAFMEAFQSCAEISMIGQFGVGFYSAYLVAEKVAITKHNDEEQYSWVSSAGSSFTLHVDHGEPIDRDTKVILHLKEDQTEYLEERWVKEVVKKHPQFIGCLIAVYLEKEPEKEISDDEEEKGEKEEEDKDDKEKPKTEDVGSDEEDDTDKNNKKKTKKIKEKYTDREELNQTKPIWTRNPDDITQEECGEFYKSLTSAWEDHLAVKQFPVEEQEENEQLCVHHVWIMDSFDDLMPEYVGFVREDKENNKKLDEVFSKISWLGIHEDSINWRHLSELLWSHTFQSGDEMTSLSEYVSCMKEAQKSICDIIGECKEQVANSAFVEQEWKKGFEVIYMSEPIDEYCVQQLKEFDGKSLLSVTKEGLELPEDEEEKKIMEESNVKFENLCRLMKEILDKKVERVTISSRLVSSPCRIVTSTYS", "text": "FUNCTION: Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family."}
{"protein": "YKVDEDLQGAGGIQSRGYFFFRPRN", "text": "FUNCTION: Stimulates uterine smooth muscle contraction and causes selective vasoconstriction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NmU family."}
{"protein": "MSSWLSTTGKVYLPPAQPVARVLETDEYITGTSLYFHAGTERLLTVGHPYFPVKDVQEPHKVLVPKVSGSQFRVFRFNLPDPNRFALIDNGFYDSDHERLVWKLRGIEIGRGGPLGIGTTGHPLYNKFGDTENPNGYKKQSDDNRQDVSLDPKQTQMFIIGCTPAIGEHWDKAEPCPSPAPQQGDCPPIELVNSYIQDGDMCDIGFGAFNFKALQADKSSAPLDVIATVCKWPDFLKMGKDIYGDSLFFFGRREQLYARHFFVRAGTMGDALPEPFEATSDYFIGAQNQQDQYTLGPHIYVGTPSGSLVSSESQLFNRPYWLNRAQGTNNGICWDNQLFVTLVDNTHNTNFTISVKSDGANDNYQYKASDFKQYLRHIEEFEMEFIFQLCKVPLTADVMAHLNVMNPNILDNWQLNFVPPPPSGIEDQYRFLQSRATRCPTQTPATEKEDPYKDLSFWVVDLSERFSSELSQFSLGRRFLYQSGLINGSLKRKRIISSSHAQTNTKRSAKRKRSLK", "text": "FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the papillomaviridae L1 protein family."}
{"protein": "MKTLVIAHRGDSKNVPENTIAAFKRAMELGADGIELDVQLTKDGHLVVIHDETVDRTTNGEGFVKDFTLEEIKKLDAGIKFGEKFAGERIPTLYEVFELIGDKDFLVNIEIKSGIVLYPGIEEKLIKAIKEYNFEERVIISSFNHYSLRDVKKMAPHLKIGLLYQCGLVEPWHMALRMEAYSLHPFYFNIIPELVEGCKKNGVKLFPWTVDRKEDMERMIKAGVDGIITDDPETLINLVRKGG", "text": "FUNCTION: Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol (PubMed:18214974). Can use glycerophosphocholine (PubMed:18214974). SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
{"protein": "MRRAPSLVLFFLVALCGRGNCRVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLTTLLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDRLFLWVFMFVCVLGTVGLFLPPLFQTHAASEGPYAAQRD", "text": "FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-4/CHRNB4 sub- subfamily."}
{"protein": "MAFQLTPLRVALVAGEPSGDLLGASLLGGLHARLPASSRYYGIGGPRMSAVEFDAHWPMEKLAVRGYVEALKHIPEILRIRGELKRQLLAEPPDAFVGIDAPDFNFGLEPALRGAGIPTIHFVCPSIWAWRGGRIKKIVKAVDHMLCLFPFEPELLEKAGVAATFVGHPLADEIPLEPDTHGARIALGLPGGGPVIAVLPGSRRSEIELIGPTFFDAMELMQQREPGVRFVVPAATPALRALLQPLVDAHPSLSVTLTEGRAQVAMTAADAILVKSGTVTLEAALLKKPMVISYKVPWLTGQIMRRQGYLPYVGLPNILAGRFVVPELLQHFATPDALADATLTQLRDDANRRALTDIFTDMHLALRQNTAQRAAEAVARVIDSRKPR", "text": "FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SIMILARITY: Belongs to the LpxB family."}
{"protein": "MTDFSNWSCEYHTTFDEIVRIENKFKEHLKVDKRTRRRLLECCSKDFEILKFKGLHGIPCYQIEKINVNIEIISLNGLNTNNNGRLTEKWNPDRIGNFDFASYNKREKLLIDKETKVLLSWISGLKLENEDIMEFPNPLIKINSEFNSYIIETCNFCYLTKELLVYSPKSSLDELMPNDLNKNFEKLENEKIIQCELNFNQHYSSEILPFLEFKPYRTILFLNNFLIEVNMNGISSQNIPEKTKREFINWNYENQSEINTSWDINLWSKVFDEDYNEIEFLKLKTPNEIITEDVIENFKSYNSKRFKVYWKLDKNETKKLEWNPIKSYISKNLTTKILLNEKLTKQNEYTIKKPELNFKKILYNIIDLIDIENGTFGSLNLVLNNKIENSFQDPLTKNDESSSINVEKEISESTLQINTSMIPHKRSYIDEELKSILEIKRKKKNLNDRNLKDSEDKTGSILSFINQGIITNIPRDTVLSDRQIVSDQTITESNQLPKFGLKIKFNCKEIAGKTVILNGKKIRENHKIKNILENKSQIKILEKELSYDCDFILNATTCLVRIKLDNFFQISKNGYLFYQKKLMDLTTEFKRVLVLVEYSSIIESTDKDIFWKLHLYLKNYQFYTYIIPSNIEEIARKISLLISRYSSKYNDNELDCNSSEEQILQSLNFNIFLVKDILKKFTLFDFLKGLTLNCDNRNQNILTKQQLARIKTLLTLEW", "text": "FUNCTION: Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to a meiosis specific chromosomal structure called the synaptonemal complex (SC) formed during meiotic prophase. SIMILARITY: Belongs to the ZIP2 family."}
{"protein": "MKRRLIIAASLFVFNLSSGFAAENIPFSPQPPEIHAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAWAKDNPVFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYAEKLHLKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVMGADSAKGREEEARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIDLGTEQEFWMVLPKAEIPHIKAKYTLDGKELTAPISAHQRVGEIELYDRDKQVAHWPLVTLESVGEGSMFSRLSDYFHHKA", "text": "FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein Note=N-terminal lies in the periplasmic space. SIMILARITY: Belongs to the peptidase S11 family."}
{"protein": "MADIYRFPKFSYEDNGTVEPLPLRTGSDKKAIPYIRIIKVGDPPKHGVRYLDLLLLGFFETPKQTTNLGSVSDLTEPTSYSICGSGSLPIGVAKYYGTDQELLKACTDLRITVRRTVRAGEMIVYMVDSIGAPLLPWSGRLRQGMIFNANKVALAPQCLPVDKDIRFRVVFVNGTSLGAITIAKIPKTLADLALPNSISVNLLVTLKTGISTEQKGVLPVLDDQGEKKLNFMVHLGLIRRKVGKIYSVEYCKSKIERMRLIFSLGLIGGISFHVQVTGTLSKTFMSQLAWKRAVCFPLMDVNPHMNLVIWAASVEITGVDAVFQPAIPRDFRYYPNVVAKNIGRIRKL", "text": "FUNCTION: Acts as a negative regulator for transcription and replication by sticking to the nucleocapsid. This effect might be regulated by the cytoplasmic interaction with tubulin that dissociates the M protein from the nucleocapsid (By similarity). Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane and concentrates the HN and F glycoproteins. SUBCELLULAR LOCATION: Virion Host cytoplasm Host cell membrane; Peripheral membrane protein; Cytoplasmic side Note=During bud formation, associates at the inner side of the plasma membrane of infected cells. SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus M protein family."}
{"protein": "MQNDAGEFVDLYVPRKCSASNRIIAAKDHASIQMNVAEVDRTTGRFNGQFKTYGICGAIRRMGESDDSILRLAKADGIVSKNF", "text": "FUNCTION: Component of the small ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Rough endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family."}
{"protein": "MANKEHRVKQSLGLLEVCGLALAISCADIMAKSASITLLALEKTNGSGWMVIKITGDVASVQAAITTGAHFAEQWNGLVAHKVIARPGEGILLAETPSPSVIEPEPEASEIADVVSEAPAEEAPQESELVSCNLCLDPKCPRQKGEPRTLCIHSGKRGEA", "text": "FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. FUNCTION: A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). Not required for structural integrity of BMCs nor to mitigate propionaldehyde toxicity, it might be involved in spatial organization of BMCs (PubMed:21239588). SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the bacterial microcompartments protein family."}
{"protein": "MDNDKYLKGTTTVGVVCTDGIVLASEQRATMGNFIASKTAKKVYQIDDLVAMTTAGSVGDAQQLVRLVNVESQLYKMRRNESMTIKGIATLMSNFLNSNRYYPMMVQLLIGGVDKNGPGIYSLDALGGSIEETRISATGSGSPMAYGVLEDQYREDMTVKEGLDLAIRAIHNATKRDSASGENIDVVVITKEAFRRLDPEEVKSIRASLPK", "text": "FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MDPEQNDTKPPFNPICATRQAPYSHEILENLDITGILLFAILTFMTLVSLLVFLEEAYYMYRKIPNPKNSIIIWINAGAMMIATTSCFGMWIPRSTMFTDFTASVFLAVLIHKFQLMLVNECGGRREFLSTFGDTKLKISTGPFCCCCLCLPHKDINRKTLFILKLGTFQFAFLRPVLMFLAVVLWTNGTYMIGNSSAEKATIWINIGVGITTITALWAVGIMFNLVKDNLKEKNIIGKFAVYQFTVILSQLQTSIINILGTTGVISCVPPLPGPSRASYMNQQLLIMEMFLVTVICRVLYRRRYDDKNLLENQETNDNLRNSMMHLNGKALEDGPQSV", "text": "FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for the translocation of bile acids (such as taurocholate), steroids (such as estrone sulfate), and eicosanoids (such as prostaglandin E2). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OST-alpha family."}
{"protein": "MTNRKEIIGDAEKIVIKIGTTSISREDGSLNNEFMDTIASQVSELHRAGKQIILVSSGSIGIGIEILDLGCRPKEIPVRQAAAAVGQGVLMQHWTEAFQKYGLNVAQILLTYDSFTNRLTYLNLRNSISTLLSYGVIPIINENDPICVHEIEATLGDNDKLSAMVASKMEADLLILFTDIDGLYDKNPKRHDDAVLLRTVEEITPTIESYGGNPTSMKGVGGMRTKIDAAKICNISGCYMVIANSNVDDGIRRILDGEELGTLFLTNQFVHKNRIRWIILARSSGSIVVDTGAKEALAKRMSLLPSGVLGVAGTFDRGDIVKLECDGVVFGKGITDYTSEELKAIKGKQTNEIADILGYKNYDHVVQKDNIGLFK", "text": "FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamate 5-kinase family."}
{"protein": "MGRAISKSGPVRALGAMSGTSLDGVDVAVLETDGRDILGFGETGYRAYSDAEREVLRAALGQWTGDAVAAAARVVEAAHIEVMTDHADVDLIGFHGQTVAHAPRLQGTLQVGDGGVLAEALGRPVVWDFRSDDVSMGGEGAPLAPFFHHACARYIGATEPLCFLNLGGVGNVTYVDPRKARPEDEGALLAFDTGPANAPINDFLQSRLGLAMDEGGRIASGGAVENGALELFLAEPYFARMPPKSLDRNDFPEMIGLVTELSDADATATLTAMCAAAVAQGMEHCPKAPSKVLVTGGGRHNPVLMEMLRVSLDCPVEPVETVGLDGDMLEAQAFAYLAVRVARGLPTSAPSTTGVRACVGGGTVTVPEGWTARKT", "text": "FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N- acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family."}
{"protein": "MPRGGMDDHWPSSDDQGHDPKEPEQLRKLFIGGLSFETTDDSLREHFEQWGKLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDASMSARPHKVDGRVVEPKRAVSREDSARPGAHLTVKKIFVGGIKEDTEEYHLRDYSESYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHNCEVKKALSKQEMQTASAQRGRGGGGSNFMGRGGNYGGGDGGNFGRGGGGGFGNRGGYGGGGGRGGGGYGGGGDGYNGFGGDGGNYGGGPGYGGRGYGGSPGYGNQGGGYGGGGGGYDGYNESGNFGGGNYNDFGNYGGQQQSNYGPMKGGSFSGRSSGGSGSGPYGGGYGSGGGGGGGGSYGGRRF", "text": "SUBCELLULAR LOCATION: Nucleus Note=Component of ribonucleosomes."}
{"protein": "MFRGANAVSLDAKGRLAMPSRYRDELDSRCNGQLIVTIDAVDPCLCVYPLDEWEQIEAKLRALPSLREENRRLQRLLIGNAVDLELDGSGRFLVPPRLREYAKLDKKAMLVGQLNKFQLWDEDAWNAVSAADLAAIQQPGAMPDDLRDLIL", "text": "SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the MraZ family."}
{"protein": "MDRKQKQAEKARPYGLLKPAALGKIPGRFQLHQEALPHLPVPPLQQTLDRYLLALQPIISEEELNHTQELVAEFRKPGGVGERLQKGLERRAKKTDNWLSDWWLKTAYLEYRLPVVVHSSPGVVLPKQDFQDRQGQLRFAAKLIEGILDFKTMIDNETLPVEYMGGKPLCMNQYYQILSSCRIPGPKRDSIVNYAKGKKQSRHITVVHNFQFFELDVYNSDGSPLTTDQLFIQLEKIWNTSLQTNKEPVGILTTNHRNSWAKAYNNLLKDKTNKESVRTIEKSICTICLDAPMPRVSDDIYKSPVAAQMLHGGGSRWNSGNRWFDKTLQFIIAEDGSCGLVYEHAPAEGPPIVALLDHIVEYTKKPELVRSPMIPLPMPKKLRFNITPEIKSDIEKAKQNLNIMVEDLDVIVLVFHQFGKNYPKSEKISPDAFIQLALQLAYYRMYGHSCATYESASLRMFRLGRTDTIRSTSIESHKFVQSMDSPDKSDQEKADLLRRATQAHKEYTNMAIQGNAIDRHLLGLKLQAIEDLVSIPELFMDTAYAVAMHFNLSTSQVPAKTDCVMCFGPVVPDGYGICYNPMGEHINFAISAFNSCADTNAARMAHYLEKALLDMRSLLQSAPKSKL", "text": "FUNCTION: Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta- oxidation. Responsible for the synthesis of short- and branched-chain acylcarnitines. Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates. Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates. SUBCELLULAR LOCATION: Endoplasmic reticulum Peroxisome Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family."}
{"protein": "MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMTRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKSHIL", "text": "FUNCTION: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Thiamine importer (TC 3.A.1.19.1) family."}
{"protein": "MKIIGIESSCDETGVAVYDTALSGSAALRAHSVYSQVALHAEYGGVVPELASRDHVRKLLPLLRQTLAEAKLSVEELDGVAYTAGPGLVGALLVGAGVARALAWALEVPAIGVHHMEGHLLSPLLEDDPPEVPFVALLVSGGHTQLVAVDAIGDYRLLGETLDDAAGEAFDKVAKLMGLPYPGGPQLAALAERGIPGRFCFTRPMVDRPGLDFSFSGLKTQVLLAWRNSDQSDAIRVDVARGFEDAVVDTLAIKCERALDTVACQTLVVAGGVGANKCLRARLQAMCRQRGGRACFPRPALCTDNGAMIAFAGALRLQAGQQSDVAVRVTPRWDMAALPPLVSRSCRR", "text": "FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KAE1 / TsaD family."}
{"protein": "MSNGYGDHMDDVCRDDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYLNAKDAERAINTLNGLRLQSKTIKVSVARPSSESIKDANLYISGLPRTMTQKDVEDMFLPFGRIINSRVLVDQATGLSRGVAFIRFDKRSEAEEAIASFNGHKPPGSSEPITVKFAANPNQNKNMALLSQLCHSPARRFGGPVHHQAQRFRFSPMGVDHMSSISGVNVASSASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKTLQVFFKTSKSHK", "text": "FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation (By similarity). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Acts cooperatively with cribp to stabilize AU-rich sequence (ARE)-containing mRNAs. May play a role during gastrulation. Required for the vegetal localization of vg1 mRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cell cortex Note=Enriched at the vegetal cortex in stage III and IV oocytes. Shows very weak nuclear localization. SIMILARITY: Belongs to the RRM elav family."}
{"protein": "MESYLTKQAVHNRAKEAVGKSVLELNGGESIKQSKSSVGDAFENWFGKKKDSDSKPDMAEAGVELKATPFKKLKNGKYSSKERLVLNIINYEKVANENFETSSFLSKNNTIELAFYEYIKGTPSDNWIIKEAVLYEMHKNPIDYEIIKQDWEIINQYINEGKAHELSEGLTSYLAPCTKGANASSLRNQPYSDIKAKQRAFSLKSGYMTSILRKYVLGDEKIDSIVKDPFEIKEKSIEDIVFEKFQPYINWSIDKLCEHFSINKGEKGLNYRIASAILNLKGKTTKSKPFPEVEEFEKSSIVVKTVHFNKKNVNKESMSFGAFKFEELANEEWEDSEGYPSAQWRNFLLETRFLFFVVKEDEDGVDIFKGIKFFSMPEEDINGPVKRMWDDTVKKLKEGVTLEAVPDKSTKDGWRIKNNFVDKSDDLICHVRPHTNNRDYRGGSNADKLPKKINWINRPDSDDYSDEWMTKQSFWINNDYIKKQVEDLL", "text": "FUNCTION: An E and P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GATC-3' and cleaves before G-1."}
{"protein": "MRDSTGAGNSLVHKRSPLRRNQKTPTSLTKLSLQDGHKAKKPACKFEEGQDVLARWSDGLFYLGTIKKINILKQSCFIIFEDSSKSWVLWKDIQTGATGSGEMVCTICQEEYSEAPNEMVICDKCGQGYHQLCHTPHIDSSVIDSDEKWLCRQCVFATTTKRGGALKKGPNAKALQVMKQTLPYSVADLEWDAGHKTNVQQCYCYCGGPGDWYLKMLQCCKCKQWFHEACVQCLQKPMLFGDRFYTFICSVCSSGPEYLKRLPLQWVDIAHLCLYNLSVIHKKKYFDSELELMTYINENWDRLHPGELADTPKSERYEHVLEALNDYKTMFMSGKEIKKKKHLFGLRIRVPPVPPNVAFKAEKEPEGTSHEFKIKGRKASKPISDSREVSNGIEKKGKKKSVGRPPGPYTRKMIQKTAEPLLDKESISENPTLDLPCSIGRTEGTAHSSNTSDVDFTGASSAKETTSSSISRHYGLSDSRKRTRTGRSWPAAIPHLRRRRGRLPRRALQTQNSEIVKDDEGKEDYQFDELNTEILNNLADQELQLNHLKNSITSYFGAAGRIACGEKYRVLARRVTLDGKVQYLVEWEGATAS", "text": "FUNCTION: Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity (PubMed:23142980, PubMed:23228662, PubMed:31959557). Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation (By similarity). Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells (By similarity). Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex (By similarity). In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally (By similarity). Binds to the metal- regulating-element (MRE) of MT1A gene promoter (By similarity). FUNCTION: Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity (By similarity). Regulates the transcriptional networks during embryonic stem cell self- renewal and differentiation. Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells. Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex. In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally. Binds to the metal-regulating-element (MRE) of MT1A gene promoter (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Localizes to chromatin as part of the PRC2 complex. SUBCELLULAR LOCATION: Nucleus Note=Localizes to chromatin as part of the PRC2 complex. SIMILARITY: Belongs to the Polycomblike family."}
{"protein": "MDFFIDATDNNARACTIKTSHSTIKTPVFMPVGTAASVKSLDTVDLRDILQTQIILANTYHLYLRPGDNVVKKLGGLHGFTGYNRSFLTDSGGFQAFSLSDISKANERGIEFQSHIDGSKHFFTPQKVLDIQYNLGSDIMMILDDLVALPATKERLALSVDRTTRWAQESIKYHKKMQAQGIGTNQNIFAIIQGGTDYEFRKKSAMELTALDFDGFAIGGLSVGEENSVMYNTVEFTTPFMPKNKPRYLMGVGTPEDLVECIDRGVDMFDCVMPTRNARNGTIFTSFGRLNIKAAKYKLDQNPIDEACSCYTCQNYTRAYLNHLYRAKELTYYRLASIHNLHYYLTLMKEAREAIEKGEYKAFKKAFYARRQS", "text": "FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- yl)amino)methyl)-7-deazaguanosine). SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family."}
{"protein": "MRQRTIVCPLIQNDGCYLLCKMADNRGVFPGQWALSGGGVEPGERIEEALRREIREELGEQLILSDITPWTFRDDIRVKTYADGRQEEIYMIYLIFDCVSANRDICINDEFQDYAWVKPEELALYDLNVATRHTLALKGLL", "text": "FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP). SIMILARITY: Belongs to the Nudix hydrolase family. NudI subfamily."}
{"protein": "MASRAPLELLPLNRSQLSPPNATTCDDAPEAWDLLHRVLPSVIIIICVCGLLGNLLVLAVLLRPRRRLNVAEMYLANLAASDLVFVLGLPFWAANISNQFRWPFGGLLCRLVNGVIKANLFISIFLVVAISRDRYRALVHPMATRRRRQARATCVLIWVAGSLLSVPTFLFRSIEAVPELNNDSACVLLHPPGAWHVARMVELNVLGFLLPLAAIVFFNCHILASLRGRPEVRGARCGGPPDGRTTALILTFVAAFLVCWTPYHFFAFLEFLTQVQVVRGCFWENFKDLGLQYASFFAFINSCLNPVIYVFVGRLFRTRVWDLFKQCAPRRPPAVSWSHRKRVLQLFWQN", "text": "FUNCTION: This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily."}
{"protein": "MLKRQSAPLGTWLMSASASTAEALGYAGFDWLLVDMEHVPIEFRDLWHILQAIQCTGAQPIVRVAANDPVLLKRALDLGSTNVMVPFVENAEQARAAVSAVKYPPMGTRGFAAVHRASRYGTWKGYGQQANDSVSCILQIETATALANLEEIAAVPGVDALFLGPGDLSSVCGHIGNPAHPDIQAMISDAIVRCKAIGMPIGIVGGTPELVGSYLEQGYAFAAVASDMAMMMSKANELLVALKGRQAPEAVATAY", "text": "FUNCTION: Catalyzes the retro-aldol cleavage of 2-dehydro-3,6-dideoxy- 6-sulfo-D-gluconate to (2S)-3-sulfolactaldehyde and pyruvate. Is involved in a degradation pathway of sulfoquinovose (SQ) that allows P.putida SQ1 to use SQ as the sole carbon and energy source for growth. SIMILARITY: Belongs to the HpcH/HpaI aldolase family."}
{"protein": "MKGRLLQRLRQLSISNSLRGAFLTGALLTLIVSMVSLYSWHEQSSQVRYSLDEYFPRIHSAFLIEGNLNLAVDQLNEFLLAPNTTVRLQLRTQIIQHLDKIERLSQGLQLAERRQLAVILQDSRTLLAELDNALYNMFLVREKVSELSARIDWLHDDFTTELNSLVQDFTWQQGTLLDQIEANQGDAAQYLQRSREVQNEQQQVYTLARIENQIVDDLRDRLNELKSGNNDGMLVETHIRYLENLKKTADENIRALDDWPSTITLRQTIDELLEIGMVKNKMPDTMRDYVAAQKALLDASRAREATLGRFRTLLEAQLGSSHQQMQTFNQRLEQIVRVSGGLILVATLLALLLAWGLNHYFIRSRLVKRFTALNQAVVQIGLGRTDSTIPVYGRDELGRIARLLRHTLGQLNMQRRQLEQEVAERKEIEADLRAMQDELIQTAKLAVVGQTMTTLAHEINQPLNALSMYLFTAGRAIEQGQSGQARNTLTKAEGLINRIDAIIRSLRQFTRRAELETPLYPVDLRQTFVAAWELLAMRHQSRQGALSLPTDTVWVSGDEVRIQQVLVNVLANALDACSHDAVIAVTWQTQGEALEVYIADNGPGWPVALLPSLLKPFTTSKAVGLGIGLSISVSLMAQMKGDLRLASTLTRNACVVLQFSVTDVDDVE", "text": "FUNCTION: Member of the two-component regulatory system PgtB/PgtA that regulates the inducible phosphoglycerate transport system. Activates PgtA by phosphorylation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MAKRSGSGLQSSAGLMRYYEADKNAVHIQPKTVLIVGALAGIAVLFLSAVNGFWP", "text": "FUNCTION: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SEC61-beta family."}
{"protein": "MVNSSPVPGALAIFGTASDVGKSIVATALCRMFSNAGIDVAPYKAQNMSNNSGVTPDGCEIGRAQIAQAEAARVVPTADMNPVLLKPNSDTGAQIVLQGKVCSTETAKGYFLDTSLWAEAARKSLDQLMQRHELVVIEGAGSCAEMNLYDRDFVNFRTARISGAPVILVADIDRGGVFAQVVGTLAVLPPEDRALVKGVIINRFRGDIDLFRDGVKLIETLAGIPVLGVIPYFRGFRIDAEDAVPLSSKVDPSGAPEKGRIAVAAIYFPHISNFTDLSPLELDPKVELHYLHFPRSLRGYQALILPGTKNVRGDLDWLTSLGWAEKIREFRRDGGLIMGICGGYQMLGATIADPSGVEGEPGESAGLGMLPVHTVLEEEKCLSNAIGNIQGESIAVSGYEIHMGRTTSNGDCSSFLRVTARNNRPADDVDGVITPDGKVIGTYFHGIIDEPEVRCWFLRQIDPAYTPDAEERGRQESYDLLADHFSGYLDIPKLYEIIQRPCPNP", "text": "FUNCTION: Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily."}
{"protein": "MEKQAEKQLEKQLESFILHLKRKTVVGSYQVSRASAELLRQWVHKGKWGNAKSLIDQIKIIGKKLMNAQPLEFCIGNIVRRVLFIIREEYLTFFRNKKNGLNNDDYDDDDFETTTSNNNNNNNNNNINSSSNINKNNKYSNVMLQDDPIDDQEDIDFTETFPRLKAAIMDSINELIDELEGLHRNVAEQAIEHIHSNETIMTLGCSRTVEEFLKEAARKRSFKVIVVETAPSLEGQKTAISLSKASIDTTLITDSAVFAMMSRVNKVIIGTHAVMANGGLIATSGTHTLAVAAKYHSVPIVVCTGLYKLCPLYAYDQDTFNNFGSPGEYLKFEEAEFLENVHSYNPTFDYVAPDLVSLFITNIGGHNPSYIYRLLQEYYDARDILEDE", "text": "FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2- bound GDP for GTP. SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family."}
{"protein": "MQDDILESEMSKAPQLQQESQEGQDKQTLSPPGHQEPPGIISELDNALPEENQLEKGTMENANGKETLRLESPVLSGFDYQETTGIGTLAQSSSSSSSSLTGFSSWSTAMPPNPSTLIEEVGFFNQAATTNNAPPPLLFQSFSHHTSTGFGGNFSHQIGPLSQHHPSPHPHFQHPHNQHRRSSASPHPPPFSHRSAAFNQLPHLGNNLSKPPSPWGSYQSPSSTPSSTSWSPGGGYGGWGSSQGREYRRGGVNPLNSISPLKKSFPNNQTQTQKYPRNNSGFNTKPWVEDTINRNESIFPFQERSRSFDGFSMHSLENSLIDIMRAEQDSLKGHSSLFPMEDERSYGEDERSDQSLSGLGSPHSFPHQNGERIERYSRKVFVGGLPPDIDEDEITASFRRFGHLFVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACMEEDGKLYLCVSSPTIKDKPVQIRPWNLNDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN", "text": "FUNCTION: Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism. SUBCELLULAR LOCATION: Cytoplasm Cell projection, dendrite Cell projection, dendritic spine Postsynaptic density Cell projection, axon Cell projection, growth cone Endoplasmic reticulum Cytoplasm, perinuclear region. SIMILARITY: Belongs to the RRM CPEB family."}
{"protein": "MAAPCVSCGRVLSLWFTPAVRASLCQRPGYWTASAVGWQTGTRFQLSKLIHTTVVTTKKNVQASRQESYTEDFIKKQIEEFNIGKRHLANMMGEDPETFAEEDIDRAIAYLFPSGLFEKRARPMMKHPEHIFPKQRATQWGEDGRPFHFLFYTGKQSYYSLMHDVYGKVMQLEKHRGPLSASAESRDLIGSRWLIKEELEEMLVEKLSDEDYAQFIRLLEKLLTLPCGPAEEEFVQRFRRSVTIQSKKQLIEPVQYDEQGMAFSTSEGRRKSATAQAVVYEHGSGKIHVNGVDYLIYFPITQDREQLMFPFHFLDRLERHDVTCTVSGGGRSAQAGAIRLAMARALCSFVTEDEVEWMRQAGLLTPDPRIRERKKPGQEGARRKFTWKKR", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MSEGEGQAKNRLFLGIDLGTSHTAVMSSRGKKFLLKSVVGYPKDVIGLKLLGRPYVVGDEAFEMRSYLDIRYPLQDGVLSEISDRDIEVARHLLTHVVKSAEPGPNDEICAVIGVPARASAANKALLLKMAQEVVHTALVVSEPFMVGYGLDKLINTIIVDIGAGTTDICALKGTVPGPEDQVTLTKAGNYVDERLQNAILERHPELQMNVNVACAVKEQFSFVGTPTEVASFEFRAAGKPVRADVTEPVKIACEALMPDIIESIETLLRSFQPEYQATVLQNIVFAGGGSRIRGLAAYVKEKLRPFGDANVTCVKDPTFDGCRGALRLAEELPPQYWRQLGDVSGS", "text": "FUNCTION: Protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that organize magnetosomes into long chains running parallel to the long axis of the cell (Probable) (PubMed:21883528, PubMed:28790202, PubMed:23204522, PubMed:24957623). Turnover of MamK filaments is probably promoted by MamK-like, which provides a monomer pool (PubMed:24957623). Forms twisted filaments in the presence of ATP or GTP (PubMed:20161777, PubMed:23204522, PubMed:27391173). Serves to close gaps between magnetosomes in the chain (PubMed:26884433). Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation (PubMed:20471399). Expression in E.coli yields a filament in the cell's longitudinal axis; the protein nucleates at several sites and one extremity of the filament is located at the cell pole (PubMed:17085581, PubMed:20161777). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Magnetosome membrane; Peripheral membrane protein Note=Tagged protein forms straight lines extending along most of the cell associated with its inner curvature, in the correct position to be filaments that are seen associated with magnetosomes (PubMed:17085581, PubMed:16373532, PubMed:20471399, PubMed:27481925, PubMed:21883528). Colocalizes in filaments with paralog MamK-like (PubMed:24957623). SIMILARITY: Belongs to the FtsA/MreB family. MamK subfamily."}
{"protein": "MRLLLLLILIITINFSYGVLTPKNLAGEASEFGSFNIPNPMDVAQSSDSSLFGISMTQSQLKNSFEWSGVVPVDSEEEFTLTFFSSFPLSEFKVEASPKTSLSSSKSESEHKSKFYKVIKSIYQTPTVTNGSFGIDGATTPSFSLTWDKPVVGDWNVVITASSSLRKNEKFQKMVEDSTPQLLMLVQNPSDTHIYSYVSSYNNLFTGQKVSVLAMLHKKSEFIKKSSANRPLNWKPSPILLSDVSAEMILGLPDGSKETIPMFDDGLHDDEQANDGLFGGYINVSELGNYDLQVVYKGSQNGNGVIRSNQHLIPITSQYLELTGEVQSVQDGDANLNIYFIVNSPNQTTVDQTPVHVYSEVYGTDDDGKKVAIAWVAGVTSAQPIQGSTTTFALSAVLNERWIAKVGATAPFFVKNVQVSDLDTFIPLSNTTSTSNVKMVGEYKDVRTIVHSPPLHEITKEMRDGKMPKELADRIGKSTGNGKLILTHGYCSEGVWPIEDFENSVEFQDFNQNRGNDEFAQILANFGSQYTDGFSLVAHSQGGNAALHLVTFYFSGLDLSQKLEGRVIQSMGTPYQGTALAGTWASIGSAVGVGCSANDDLTVDGAALWLKSIPADKRALVYYTTTQYSTGSLINYCNLASNAVLEWPNDGVVDNEHTPLEGGVYLNNFKDWCHSDGMHSPQQTTNTEYNKEMSSNSVW", "text": "FUNCTION: Involved in cell density sensing and might synchronize the onset of development by triggering aggregation when a majority of the cells in a given area have starved."}
{"protein": "MSGYQNGGPRGLADDSDVEEEALVADYREQVQYEEGMDDPDMGLAQQTDDIQSRLVAAAQPLDFSAPLEVKFQSYDQYCSLFHFILNSDGPVDLEPPSYYWAWDVIDEFIYQFNSFSSYRMRIARQANNEEEAQILRENPNTWGCYSVLNVLYSLIQRSQILEQLQAMKRNEDPMAVAGDYGSRSLYRMLGYFSIIGLLRVHCLLGDFSLALRTLDDIELNKKAMFARVMAAHFTTYYYVGFSYMMVRRYADAIRMFSHILVYVSRTKNFQKNAQYDSITKKNDQMLALIAICVAFHPTRLDDTIHTALREKFGDQLLKLQRGGPESLPVYEELFRTACPKFISPVPPDFDNPEANVDPIEHHLSVFMDEVKTNMWSPTVKSYLRLYTTMDLKKLAGFLSVKPEELRSWLLVNKQRTKQLRWADHGLLDGELVNVSDLDYAMQGDLIHISEAKVGRKLVDWYLRNLSRTYV", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit L family."}
{"protein": "MERQQIIESLRRIIPTESTEYNERLISLGESFLEWSKYKHNLKATEELCRPYMAAHLACELLSNDLNLEINLLATPIPKKKYYKLFTYFQEILSPLTKSLAAKDDLMETITYLCTKLGGSTAIPYVKQLVKAVVTNDMRIEHKRGIIIAAYLLVSAKAFGKDELHINHTERRKAQSVLQDTSSALQIQYWMHVLSESWQYKEIPLNGIEGYESQKQRIKPWSGIASMIQIDYEKRLQNYPIWKACIEERIQYYKSQLEKDGTAS", "text": "FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. ORC binds to multiple sites within the ars1 origin of DNA replication in an ATP-independent manner. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC6 family."}
{"protein": "MYVSMLFGFSYVFWLIGVSSNISVYYGVVSLVCTAGTGCVVLAWKGGSFLALVLFLIYLGGMLVIFAYSITLVMEPFPEVMGDWVGVMHAGKYVVLAVVFVLVGWGWWGVGECGDGVVDAGGLSIVRVDSSGLSLLYAIGGGALMMAMFGLFLTFFIVLVLVQGLFRVACPTI", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 6 family."}
{"protein": "EFLFARTMIGVFKNIEYMCNRTSSKTWGKEAWKKIVVCIVSDRRAKINPRTRAVLAGLGVYQDGIAKQQVNGKDVTAHIYEYTTQVGLELKGTQVSLKPRSATPVQLLFCLKEKNQKKINSHRWFFQAFGRVLDPNICVLIDAGTKPGKDSIYQLWKAFDLEPMCGGACGEIKVMLDHGKKLYNPLIAT", "text": "FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chitin synthase family. Class I subfamily."}
{"protein": "MTHTPSFDLSDIKSTLSTNVLHADDAYALENDVAPPIHISTTYTYPGTPDTLQPFTKLAEEDFPYYARISGNNVDRAEASLSSVLGAPSVVYSSGLAAIYGLLSYLNPKHIAVHKPGFGGYSGTIQIIARINRLTGLETSFIDGKCDAIGEGDVIWLETPLNPLGIAFDIPFYKELAKKKGAILVVDSTFAPPPIQDALVLGADYVVHSATKYLAGHSDVLAGVTASKDRSKILDLKADRAYLGTILHPQQAFLLLRSLRTFPLRIAKHSENGFLVAQHLNKLATDEQFATSLGIDSSLILEVYHNSLQTKEFVAKNLTGGHASCFSVLLKSDTVAKHLCCELKYFHHATSLGSVESLIEWRRMTDSKIDPRLVRLSIGIEDAADLIADLNRVFASLS", "text": "SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
{"protein": "MIREKFAYRETITTILADDTSHVEAAKGGMIAARTGVEEYLLTDPFFQMSYSPVSAPADAPESVRCMAAASFEADVGPMAAVAATIGWAGVKAMQNRGAAFGLIDNGGDIVLFSNRELRVGIYAGPAPSSGKFAFLITPQTEILGICTSSATVGPSVSFGIADSVTCFSHDPAKADAWATGLCNILTPENFDKVMKKVEESSVFAVYAVIGDWIGRWGDLPEIVPAHVSYDLITKG", "text": "SIMILARITY: Belongs to the UPF0280 family."}
{"protein": "MTVSKYNGVASTFNGVARRFDFAPLEADKLNWYPRSALPPEIPAIDLNKVNTEEELAQFLVDIRKSGLFYIVDHGIPEEISIGCYNAFREFCNLPEEAREKYNTDESFKSGGYVPFKGTSIGGGNLFERQKDFVVKFFWRGPSVVNRSPNDRFAEFHDEHHRKTAELAEKIITTILKALKTRFPEFHPDELKDNINVRNMFFSNRIYPEAPPDDGEKADYRLVPHRDLSFITLANQVPANNGFKGLFILTGDGEKIPVPPIRNSYLVFIGQGLSYLTNKYLPAALHGVDFPDNTNFEGSERASLISFYEPNDYMMPSKNINPLPEEIFEKSCTFYDDVGVGRAGTTYNYVRYKFHEGYYL", "text": "FUNCTION: Iron/ascorbate-dependent oxidoreductase: part of the gene cluster that mediates the biosynthesis of kainic acid (KA) and derivatives, natural products with neurochemical activity acting as ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins (PubMed:30995339). Catalyzes the conversion of prekainic acid to kainic acid and kainic acid lactone (PubMed:30995339). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MDRVVLLLSVLSLGVSSQPITDSQHLFSIAVSRIQNLHLLAQRLFSNFESTLQTEDQRQLNKIFLQDFCNSDYIISPIDKHETQRSSVLKLLSISYRLVESWEFSSRFLSGGSALRNQISPRLSELKTGIQLLITANQDGAEMFSDVSALQLAPYGNFYQSLGGEELLRRNYELLACFKKDMHKVETYLTVAKCRLSPEANCTL", "text": "FUNCTION: Growth hormone plays an important role in growth control and is involved in the regulation of several anabolic processes. Implicated as an osmoregulatory substance important for seawater adaptation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MSGRSVRAETRSRAKDDIKKVMAAIERVRRWEKKWVTVGDTSLRIFKWVPVTETKQIYKPKGAGPAVRELKGFPTDVVLENARSVLLDFQDDNSNQSFLSDAYQSNTKVDSSSNSSPQHVSEAVSPSHPPYYRTEDSQPPTLGQESMEAEREASTTSSEVTDEPPTLIKEDVLSLSTQEEEEAIGAPPLKRVCTEHNSTVS", "text": "SIMILARITY: Belongs to the BCL7 family."}
{"protein": "MPLRALVAVIVTTAVMLVPRAWAQTAWERYKARFMMPDARIIDTANGNVSHTEGQGFAMLLAVANNDRPAFDKLWQWTDSTLRDKSNGLFYWRYNPVAPDPIADKNNATDGDTLIAWALLRAQKQWQDKRYATASDAITASLLKYTVVTFAGRQVMLPGVKGFNRNDHLNLNPSYFIFPAWRAFAERTHLTAWRTLQSDGQALLGQMGWGKSHLPSDWVALRADGKMLPAKEWPPRMSFDAIRIPLYISWVDPHSALLAPWKAWMQSYPRLQTPAWINVSTNEVAPWNMAGGLLAVRDLTLGEPLERRRLTTRMIITPPASSCWSGWRNRISASAVMALQVSQPVCLRAERKEQERLTM", "text": "FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family."}
{"protein": "MIEKLTFGLFKKEDARSFMRLMAYVRPYKIRIVAALIAIFGVAATESYLAAFIAPLINHGFSAPAAPPELSAAAGIISTLQNWREQFTYMVWGTENKIWTVPLFLIILVVIRGICRFTSTYLMTWVSVMTISKIRKDMFAKMLTLSSRYHQETPSGTVLMNMLNLTEQSVSNASDIFTVLTRDTMIVTGLTIVLLYLNWQLSLIVVLMFPLLSLLSRYYRDRLKHVISDSQKSIGTMNNVIAETHQGHRVVKLFNGQAQAANRFDAVNRTIVRLSKKITQATAAHSPFSELIASIALAVVIFIALWQSQNGYTTIGEFMAFIVAMLQMYAPIKSLANISIPMQTMFLAADGVCAFLDTPPEQDKGTLAPQRVEGRISFRNVDVEYRSDGIKALDNFNLDIRQGERVALVGRSGSGKSTVVNLLPRFVEPSAGNICIDGIDIADIKLDCLRAQFALVSQDVFLFDDTLFENVRYSRPDAGEAEVLFALQTANLQSLIDSSPLGLHQPIGSNGSNLSGGQRQRVAIARAILKDAPILLLDEATSALDNESERLVQQALERLMENRTGIIVAHRLTTIEGADRIIVMDDGKIIEQGTHEQLMSQNGYYTMLRNISNKDAAVRTA", "text": "FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Lipid exporter (TC 3.A.1.106) family."}
{"protein": "MANSDKRLFEKVAIITGGARGIGAATARLFTENGAYVIVADILENEGILVAESIGGCYVHCDVSKEADVEAAVELAMRRKGRLDVMFNNAGMSLNEGSIMGMDVDMVNKLVSVNVNGVLHGIKHAAKAMIKGGRGGSIICTSSSSGLMGGLGGHAYTLSKGAINGVVRTTACELGSHGIRVNSISPHGVPTDILVNAYRKFLNHDKLNVAEVTDIIAEKGSLLTGRAGTVEDVAQAALFLASQESSGFITGHNLVVDGGYTSATSTMRFIYN", "text": "FUNCTION: May play a role in tapetum development. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MDLVTFLVLTLSSLILLSLWRQSSRRRKLPPGPTPLPIIGNFLQIDVKNISQSLTKFSKTYGPVFTLYLGSQPTVILHGYEAIKEALIDNGEKFSGRGSYPMNENVTKGFGIVFSNGNRWKEMRRFTIMNFRNLGIGKRNIEDRVQEEAQCLVEELRKTKGSPCDPSLILNCAPCNVICSITFQNHFDYKDKEMLTFMEKVNENLKIMSSPWMQVCNSFPSLIDYFPGTHHKIAKNINYMKSYLLKKIEEHQESLDVTNPRDFVDYYLIKQKQANNIEQSEYSHENLTCSIMDLIGAGTETMSTTLRYALLLLMKYPHVTAKVQEEIDRVIGRHRSPCMQDRKHMPYTDAMIHEVQRFINFVPTNLPHAVTCDIKFRNYLIPKGTKVLTSLTSVLHDSKEFPNPEMFDPGHFLDENGNFKKSDYFLPFSAGKRACVGEGLARMQLFLFLTTILQNFNLKSLVHPKDIDTMPVLNGFASLPPTYQLCFIPS", "text": "FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MNFSYSSLSTWTTLMTLGCLLLHSSISSAQLTPTFYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAAPNANSARGFPVIDRMKAAVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFFALANTNLPAPFFTLPQLKASFQNVGLDRPSDLVALSGGHTFGKNQCQFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKELKGLIQTDQELFSSPNATDTIPLVREYADGTQKFFNAFVEAMNRMGNITPLTGTQGQIRQNCRVVNSNSLLHDVVEIVDFVSSM", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. FUNCTION: Exhibits a Ca(2+)-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall. SUBCELLULAR LOCATION: Secreted Vacuole Note=Carboxy-terminal extension appears to target the protein to vacuoles. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MDHTSSVGLRKTGRRKCAVAQVRIIEGTGQLTINQRPGVPYLQYNPAYLLAAQGALDVTELTNRYDTIVKTKGGGLTGQAEAIKLGLARALCSLHIKHRKALKPQGYLTRNPLRKERKKYGLKKARKAPQFSKR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MFGKGGMGNLMKQAQQMQERMQKMQEQLAQMEVVGEAGAGMVKVTMAGSHSVRRIEIDPSLMEDDKEMLEDLVAAAVNDAVRRVEEQNKSKMGELTGGMQLPPGFKMPF", "text": "FUNCTION: Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the YbaB/EbfC family."}
{"protein": "MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA", "text": "FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MDALKSAGRALIRSPSLAKQSWGGGGRHRKLPENWTDTRETLLEGMLFSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAFEFWQVSKEEKEKRDKASQEGGDVLGARQDCTPSLKSLVATGNLLDLEETAKAPLSTVSANTTNMDEVPRPQALSGSSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDMHYAQCLSPVDWDKPDSSGTEQDDLFSF", "text": "FUNCTION: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non- polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytosis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSSQRWLWRNQHSVQTNIGSREKDLKITKTKKIKKKHERAYELLAEAAYSDPFAALGPFIDDGEGSLRVWMPGANKVELLVNGEPRVALERDGDSGFILKEQRDLHLTHYRLAVDWNGVEQIIDDPYQYHNIYQEYEHLHTPKDMYHYMGAHFVTLERGGENISGVRFLVYAPHASAVSLVGCFNQWDGRRHPMQRLDYGIWGLFIPGLEEGVQYKFELKGPNGEGLPHKQDPWGFYSEQYPSFASITYDHKRYQWQDAKWQNRAVTQKRDEALSFYELHAGSWKRDGKGDFLNYRELAEQLVPYLVDMGYTHVELMPVSEHPFYGSWGYQPVGLFAPTSRYGSPDDFKFFVDACHQAGIGVVLDWVPAHFPSDDHGLANFDGTPLFHDPDPRRGWHQDWNSYIYDLGREHVRRFLVSNALYWFEQFHIDGIRVDAVASMLYLDYSRSHDQWVPNVDGGNENYDAIATLKWMNEEVYKHFPNAMTIAEESTAFPGVSAPTFMGGLGFGFKWNMGWMHDSLSYVKEDPVHRKYHHNTITFPLVYAHSENYVLSLSHDEVVYGKGSIHNKMPGDEWQQTANLRAYYGYMYGQPGKKLNFMGAEIGQTAEWNHDDQLQWFLLEYERHQGVQKLMRDLNHLYRNEAAMHDQDCVPAGFEWRLQDEADASILAHERISKEGERILIITNFTPVPHERFRLGVPNVGQYELLLNTDDSKYGGSDFKVLTSVKTEKVESESLPQSLELRLPPLSTVFYKLHK", "text": "FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB subfamily."}
{"protein": "MLDDVAFIKTPAAKKQPPASNECGVWTTDSPAIHNAPLPADGPGSTSFSNTILFSILALVPGYITYKLGLGFKTWVFFFLILAIPILMAYWSIMSTFSPRINEKVKYPNRPISYYLEFHTPELKAKYETSNGGKGSKIPIETFQELYFDGKVSFKGDCLDVLEYKHDWASFRFTLGLFRFFLLGMIPEVIFHSQSQDEEQVRDHYDRGDDFYTWFLGPRMIYTSGVISDITREETLEELQDNKLTVMADKIDLKKGDHVLDIGCGWGTWTTFASSKYGANVTGITLGRNQTKWGNTLLKEYGIPSDQSRIVCCDYRDAPKSSKPSGKYDKITSVEMAEHVGIRRLTAYLEQCRDALEDDGLLFLQYSGLRKNWQYEDLEWGLFMNKYIFPGADASTPLSFFASCMESVGFEIVSVDNIGVHYSATLWRWYRNWIGNKDKVVNKYGVKWYRIWEFFLGSSVVASRNGTATCYQFICRKNINSYRRIDYVPQQKGLQGPVQEGTKWAKEFTNFYD", "text": "FUNCTION: Catalyzes methylation of the sphingoid base component of glucosylceramides (GluCers) at the C9-position. Sphingolipid C9- methylation requires 4,8-desaturated ceramides as substrates. Glucosylceramides play important roles in growth, differentiation and pathogenicity. The methyl group at the C9-position distinguishes fungal glucosylceramides from those of plants and animals, and may thus play a role in host-pathogen interactions enabling the host to recognize the fungal attack and initiate specific defense responses. Not necessary for vegetative growth at low temperatures, but plays a role in hyphal formation on solid medium. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the CFA/CMAS family."}
{"protein": "MTTQLEQAWEIAKQRYAAVGVDVEEALRQLDRLPVSMHCWQGDDVAGFENPAGSLTGGIQATGNYPGKARNAEELRADLEQALSLIPGPKRLNLHAIYLESDAPVARNEIKPEHFKNWVTWAKANKLGLDFNPSCFSHPLSADGFTLSHANDEIRQFWIDHCKASRRVSAYFGEQLGTPSVMNIWVPDGMKDITVDRFAPRQRLLNALDEVISEKLDPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYIPRLLLHVSRPVRWDSDHVVLLDDETQAIASEIIRHNLFDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALLEPTAQLRQLENDGDYTARLALLEEQKSLPWQAIWEMYCQRHDTPAGSQWLDNVRAYENAVLSQRG", "text": "FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose isomerase family."}
{"protein": "MEFIRIDGSYGEGGGSLLRYAIALSSVTMKPVEIYNIRVKRANPGLRPQHLNAVRALARITEATVEGDEVGSTALRFIPRKRAGGSFEIDIGTAGSISLIIQAILPACISSEEEISLRIRGGTDVPLAPPIDYMAEVFLRNMAPLGVRAELKLLRRGHYPRGGGIVELHASPSKLFPIDKVRGEKFDRVLGRCHAVKLPRSVVERISSSAIDTLRKEGLRVEIEEEWSEDGHLGPGAGIVLWTDSNPRIGADELGEKGKPSEVVGKNAASKLLDEIKAGMAFDSHMGDMIIPYLALARGRSRVGISKLTLHAESNIWLVERFLPVKFIVQGGVGSPTVIEVEGAGLEL", "text": "FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily."}
{"protein": "MLTEEELIQIRRHLHQIPELALQEFDTHQYLVETIAGFNQAFLEVRTFKELPTALMVLVHGKNPQRTIGYRTDIDALPVEEQTGLPYSSTHPGVMHACGHDIHMTVALGVLNYFSEHQPQDNILFFFQPAEESENGGKRAYELGLFSGKWKPDEFYGLHDNPDLPAGAIGCRMGTLFAGTTEVNIDLNGKGGHAAYPQNANDTVVAAASLILQVQTVISRSIDPIQSGVITLGKIDGGTIRNVIAGHTRIEGTIRGLTQTMIETIDNRLKDVCEGIGCSFNMDVSLELNQGGYWPVENNPELTKRFIHYMEETPTVNFIETEPAMTGEDFGYLLAKFPGTMFWLGVEDDSQLHSATLTPNEKAIKRGVDAITGFLEYRMQN", "text": "FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate. SIMILARITY: Belongs to the peptidase M20A family. N- acetyldiaminopimelate deacetylase subfamily."}
{"protein": "MKEARKRMVKRAVQEIKDGMNVNLGIGMPTLVANEIPDGVHVMLQSENGLLGIGPYPLEGTEDADLINAGKETITEVTGASYFDSAESFAMIRGGHIDLAILGGMEVSEQGDLANWMIPGKMVKGMGGAMDLVNGAKRIVVIMEHVNKHGESKVKKTCSLPLTGQKVVHRLITDLAVFDFVNGRMTLTELQDGVTIEEVYEKTEADFAVSQSVLNS", "text": "SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B family."}
{"protein": "MAIDAQKLVVVIVIVVVPLLFKFIIGPKTKPVLDPKRNDFQSFPLVEKTILTHNTSMYKFGLPHADDVLGLPIGQHIVIKANINGKDITRSYTPTSLDGDTKGNFELLVKSYPTGNVSKMIGELKIGDSIQIKGPRGNYHYERNCRSHLGMIAGGTGIAPMYQIMKAIAMDSHDTTKVSLVFGNVHEEDILLKKELEALVAMKPSQFKIVYYLDSPDREDWAGGVGYITKDVIKEHLPAATVDNVQILICGPPAMVASVRRSTVDLGFRRSKPLSKMEDQVFVF", "text": "FUNCTION: NADH-dependent reductase for KTI11/DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post- translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH- dependent reductase, predominantly CBR1. By reducing KTI11/DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
{"protein": "MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLDIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF", "text": "FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. FabH family."}
{"protein": "MIDPNLLRNNLAEVAEKLKVKRNFMLDTEKLTALEDQRKNLQVTTENLQAERNARSKAIGAAKVRGEDIAPLLAEMDDMGNQLTEAKAQLDAVLAEINQIALSIPNLPADEVPLGKDDTENKEILRWGTPHTFDFEVKDHITLGEEANGLDFAAGAKLAGARFAVMKGQIAKMHRALAQFMLDLHTEQHGYLETYVPYLVNHATLYGTGQLPKFGEDLFHTLALEGEQPYALIPTAEVPVTNLVRDVIIDEAELPIKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQIVDPDKSMEALEELTGHAEKVLQLLNLPYRKVLLCTGDMGFGSCKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCKAKGDKKTRLVHTLNGSGLAVGRTLVAVLENYQNADGSITVPEELRPYMGGLDVIGK", "text": "FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily."}
{"protein": "MGNCLQRTTRWQLDMQETPWNLRLSAKGRTCRYFRGWSCCHSVEGCSCLPWKNIRTFKARQESPKQNEGMTSAPVQDNANETYTEELCYILVDHEAVRGRPSVNPAEGFYENISNKAERHKESSRGTETEYSVLRFPSPPQPLPSTDDEYELLMPSRFSSHAFQQPRPLTTPYETHFSYPQ", "text": "FUNCTION: Involved in the negative regulation of lymphocyte motility. It mediates the migration-inhibitory effects of IL6. Serves as a positive regulator of the RhoA signaling pathway. Enhancement of RhoA activation results in inhibition of lymphocyte and lymphoma cell motility by activation of its downstream effector ROCK. Is a regulator of B-cell receptor signaling, that acts through SYK kinase activation. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=It relocalizes from the cytoplasm to podosome-like structures upon cell treatment with IL6."}
{"protein": "MDFYSVKSQPFVRSPLVDQNPSIQNINEEVKRDIQNPLSYKTETSDKELCQTAACATSCSDWYPQQQTHMPHQNAFDSAKATAKMALPPTAFSNYCVKPSLTRNKDIPRTSIRVSKLRYWQRDYRLAFPNFIFYFDNVDEEIKRRVTQKINNLGAKVATLFTFEVTHFITTRTTDPEMCQPNDVLYLSKTANMKIWLLDKLLNRILFTLLNSDSLVNTSASCLQSLLDGEKVYGTSDKDFYVPSKNVEYFREYFLCIRDLSQYYKPIAVREWEKTLDSGEILWPSLAITAQGRCPFNTGRRRELKITKHNHPAHEIRKQLLSCTNQTNQNNVVKNSASVLVRQIMGDYNITESAVDGAKQMPTEFPKPENLLPVEKRAAMSPLNLLEPRLINKQNTLANQSPRQPPNAFDADPLAHKKVKIETKSGYCENCCERYKDLERHLGGKHHRRFAEKDENFQGLDDLFLLIRRPIRTN", "text": "FUNCTION: May act as a kinase regulator. Essential for progression of meiosis II and sporulation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MEKRIVCLAGDGVGPEVMESAKEVLHMVERLYGHHFHLQDEYFGGSAIDLNGQPLPQRTLAACLASDAVLLGAVGGPRWDSAKERPEKGLLALRKGLGVFANVRPVTVESATAHLSPLKKADEIDFVVVRELTGGIYFSYPKERTDEVATDTLTYHRHEIERIVSYAFQLASKRKKKVTSIDKANVLESSKLWRTVTEEVALRYPDVELEHILVDAAAMELIRNPGRFDVIVTENLFGDILSDEASVLAGSLGMLPSASHAEKGPSLYEPIHGSAPDIAGKNKANPIAMMRSVAMMLGQSFGLTREGCAIEEAISAVLKLGKCTADIGGTETTTSFTKAVMQEMEEQALVGRGR", "text": "FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily."}
{"protein": "MSTKNKKAAGGNGGAPKQTRQQSHDSQDYSSFKTVLFYCMLIVFLPVLTFFVLKGFVLDQFLDISEVKVNIASAVGAVVALHVALGLYIYRAYFGAPGSKASKTD", "text": "FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the VMA21 family."}
{"protein": "MYTKIALLGLVGSAAAFNAPMMTVRRDAIATGAAAAVVAPMLRPAGAAMKKDSKAPCVEVFDERDGCKAAGTQKASGDDGFCVKVSMKAIGFNAAEAASVTKNYGIKRFGAKSV", "text": "FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore- protein from the phycobiliprotein complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the phycoerythrin family."}
{"protein": "MKENIKRVLPFLLVLLFAFAPLALASAPVDAPAPADAPADALPSAKVISAPADAGVIEAVELEHATVTGAHDVAVAHVADSLSHEKLMDLFWRVLNFAVLMAILIKFGAKPIANALSGRQQRVKSEVEDLEARRIVAEKEFRQFEAKLANVEKDIDSIVDKAVAQAEIEKAKILERAEQAAADIQKSAEQAIQNEIANAKRSLKNDAADQAAVMAEELIVKHLTADDQVKIVEDYLAKVGAV", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MTQAAPVTFSTVRENYFGPPAEMQALRHKAPVTRTAFADGRPGWLVTGYSAARAVLSDSRFTARGEREHPAVPRAATLEDERCRRLIAGQFTARRMRQLTGRTERIVREHLDAMEHMGSPADLVEHFALPVPSLVIAELLGVPPPDREHFQHDTLRWGGFGRSTEEVTEAFVSLGGQLQRLVRLKRTEPGDDLLSGLIAADPALTDEELASIAFLLLVAGHGTTAHQIALGAFLLLEHPDQLAALRADPALTESAVEELLRHLSVVHHGPTRAALQDADIEGTPVKAGEVVVVSLGAANRDPARFERPDAVDVTREDTGHLAFGHGMHQCLGRQLARIELRVALTALLERFPHLRLACPAAEIPLRHDMQVYGADRLPVAW", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSQQKQQSWKPPNVPKCSPPQRSNPCLAPYSTPCGAPHSEGCHSSSQRPEVQKPRRARQKLRCLSRGTTYHCKEEECEGD", "text": "FUNCTION: Precursors of the cornified envelope of the stratum corneum. SIMILARITY: Belongs to the LCE family."}
{"protein": "MHFIDEVKIYIKGGNGGNGCVSFHREKFIDRGGPDGGDGGRGGSVIFRSNHHLNTLVNYRYKQHFTAENGENGKDSNRSGKSGKSLVLDVPIGTQIFSEDGNILFYDFTVDDQSFEIIKGGSGGLGNSHFKSSVNQAPRKRTEGEIAEEMWIHLSLKLLSDVGLVGLPNAGKSTFLSVVTAAKPKIADYPFTTLVPNLGVVYVDDEEFVIADIPGLIEGAHQGHGLGDKFLKHIERCNVLIHLIDGSSNDVVADYNTVRLELELYSDYLKNKIETICLNKCDVLTDEEIQEKINKLQKATNKEIFPISTCTNAGVNKIVKLALETIKNQK", "text": "FUNCTION: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family."}
{"protein": "MKLTPKELDKLMLHYAGELAKKRKEKGIKLNYVEAVALISAHIMEEARAGKKTAAELMQEGRTLLKPDDVMDGVASMIHEVGIEAMFPDGTKLVTVHTPIEANGKLVPGELFLKNEDITINEGKKAVSVKVKNVGDRPVQIGSHFHFFEVNRCLDFDREKTFGKRLDIASGTAVRFEPGEEKSVELIDIGGNRRIFGFNALVDRQADNESKKIALHRAKERGFHGAKSDDNYVKTIKE", "text": "FUNCTION: Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Note=Also associates with the outer membrane upon autolysis of neighboring bacteria. SIMILARITY: In the C-terminal section; belongs to the urease beta subunit family. SIMILARITY: In the N-terminal section; belongs to the urease gamma subunit family."}
{"protein": "MKVDYYEILGVTRECDDKKLKSAFRKLAMQYHPDRNAGDKEAERKFKEIGEAYEVLKDPQKRAAYDRFGHAAFENNNNGGGSPFSGFSAGGFADIFEDFFGEIMGGGHRKRSDGRERGADLSYNMEVTLEEAFSGKTAQINIPSSVVCDACEGSGAKKGSKPQTCGTCHGAGRVRAAQGFFSIERTCPVCHGRGETIKDPCPKCQGTRRVEKNRSLSVNIPAGIEDSTRIRLSGEGDAGIRGGPSGDLYIFLSVKPHEFFQREGADLHCRVPISMVTAALGGEFEVSDLDGIKARVKIPEGTQNGRQFRLKGKGMPMLRRQQVRGDLYIHITIETPQKLTQEQRELLQKFEKLSNHENSPQSHGFFSRMKEFFENISGKNE", "text": "FUNCTION: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaJ family."}
{"protein": "MGHQQLYWSHPRKFGQGSRSCRVCSNRHGLIRKYGLNMCRQCFRQYAKDIGFVKLD", "text": "FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Rough endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uS14 family."}
{"protein": "MKFSIIALALAVAFVCVAESRSEEEGYDVSEEIQAEELEEAARGGINRKLMEMVNKLRKVQGREDSEDAGRAGINRKLMEMVNKLRKVQGREDTEEAGRGGINRKLMEMVNKLRKVQGREDSEEAGRGGINRKLMEMVNKLRKVQGREDTEEARSLKDKVKSMGEKLKQYIQTWKAKFG", "text": "FUNCTION: [Repetitive polypeptide element type 1c]: Shows no antimicrobial activity against Gram-positive bacterium B.subtilis B-501 or Gram-negative bacterium E.coli DH5-alpha at concentration up to 20 uM. FUNCTION: M-zodatoxin-Lt4b: Has antimicrobial activity against Gram- positive bacteria (A.globiformis VKM Ac-1112 (MIC=0.3 uM), and B.subtilis VKM B-501 (MIC=1.1 uM)), Gram-negative bacteria (E.coli DH5- alpha (MIC=4.4 uM), E.coli MH1 (MIC=4.4 uM), and P.aeruginosa PAO1 (MIC=>35 uM)), and yeasts (P.pastoris GS115 (MIC=>35 uM), and S.cerevisiae Y190 (MIC=35 uM)). Does not have hemolytic activity against rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (M.domestica) larvae. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 03 (latarcin) family. 04 subfamily."}
{"protein": "MSSEARMFTISDTTMKEIDRFRLRLKKSVMYAFILKVDKATKEIVPDGEIMDLQSIEEVADELSETNPRFILVSYPTKTTDGRLSTPLFMIYWRPSATPNDLSMIYASAKVWFQDVSQVHKVFEARDSEDITSEAVDEFLH", "text": "FUNCTION: Actin depolymerizing factor involved in the control of the disassembly of actin patches. Binds and suppresses the arp2/3 complex functions such as the promotion of actin polymerisation and branching filaments. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, actin patch. SIMILARITY: Belongs to the actin-binding proteins ADF family. GMF subfamily."}
{"protein": "MDYNKRSSVSTVPNAAPIRVGFVGLNAAKGWAIKTHYPAILQLSSQFQITALYSPKIETSIATIQRLKLSNATAFPTLESFASSSTIDMIVIAIQVASHYEVVMPLLEFSKNNPNLKYLFVEWALACSLDQAESIYKAAAERGVQTIISLQGRKSPYILRAKELISQGYIGDINSIEIAGNGGWYGYERPVKSPKYIYEIGNGVDLVTTTFGHTIDILQYMTSSYFSRINAMVFNNIPEQELIDERGNRLGQRVPKTVPDHLLFQGTLLNGNVPVSCSFKGGKPTKKFTKNLVIDIHGTKGDLKLEGDAGFAEISNLVLYYSGTRANDFPLANGQQAPLDPGYDAGKEIMEVYHLRNYNAIVGNIHRLYQSISDFHFNTKKIPELPSQFVMQGFDFEGFPTLMDALILHRLIESVYKSNMMGSTLNVSNISHYSL", "text": "FUNCTION: This protein is a negative regulator for the gene expression of the lactose/galactose metabolic genes. It binds to GAL4 and so blocks transcriptional activation by it, in the absence of an inducing sugar. SIMILARITY: To K.lactis GAL80."}
{"protein": "MQIYLVGGAVRDSLLNIDVKDKDWVVVGSTPTHMNSLGYQSVGQDFPVFLHPRTKEEYALARTERKSGQGYKGFTCYAEADVTLEEDLLRRDLTINAIAQSDKGLLIDPYHGQEDLKNRLLRHVSNAFVEDPLRVLRVARFAARFHYLGFTIAPETMQLMKTLVSSGELSHLTPERVWQEWEKSLSSKHPNIFLSVLKECGALAVVLPEIDALFGVPQPEQWHPEIDTGMHTLMVSQQASLLSTSLPIRFAAQVHDLGKGITPESEWPSHKMHCHTGIKVIKNLCKRVRVPNEYKELALLVCEHHTNVHRASELRAQTFIKIFDKMDLWRKPERLESILLCCQADHAGRLGLELNPYPQKERMESAFNAAQHVEVKEVVAAGFKGPEIRDELTKRRIEAVKVALLIN", "text": "FUNCTION: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily."}
{"protein": "MGFITKAIPLALAAASVINGAEIMETRAGVQTLADKYIVVMNDGMTDKDFDSHRSWVNRTHRRRLIRRGAKAMGGMKHTYRFPTGLKGYSGHFDEQMINEISKRADVKYIERDARVQINAIEQQDNVPSWGLARVGSKEPGGTTYYYDGTAGEGSTAYVIDTGTDIQHEEFEGRATWGANFVDDMDMDCNGHGTHVSGTIGGKTFGVAKKSNVVAVKVLDCNGSGSNSGVIMGMEWATKDAQQKGADKAVANMSLGGAFSQASNDAAAAIAKGGVFLAVAAGNDNVDAADSSPASEPSICTVAASTEQDSKADFSNFGQVVDVYAPGDSITSAKPGGGSQVLSGTSMATPHVAGLGAYLIGLGKGGGPGLCDTIKQTAIDVIQNPGASTTSKLINNGSGIGFLSFPLNIYEEQWSKLFDL", "text": "FUNCTION: Secreted subtilisin-like serine protease with keratinolytic activity that contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MTQENIPVQPGTLDGERGLPTVNENGSGRTRKVLLFLFVVGFIVVLLLLLVFHMRGNAENNPHSYKTMVQTSTVPMRTFKLPPPPPPAPPEPPAPPPAPAMPIAEPAAAALSLPPLPDDTPAKDDVLDKSASALMVVTKSSGDTVVQTTNARIQALLDSQKNTKQDAGSLGTLLHGTQTDARMASLLRNRDFLLAKGSIINCALQTRLDSTVPGMAACVVTRNMYSDNGKVLLIERGSTISGEYDANVKQGMARIYVLWTRVKTPNGVVIDLDSPGADPLGGAGLPGYIDSHFWKRFGGALMLSTIETLGRYATQKVGGGGSNQINLNTGGGESTSNLASTALKDTINIPPTLYKNQGEEIGIYIARDLDFSSVYDVKPK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TrbI/VirB10 family."}
{"protein": "MVLATTLPDTTWTPSVGLVVILSNLFAIALGRYAIQSRGKGPGLPIALPALFEGFGLPELLATTSFGHLLAAGVVSVGLQYAGAL", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the PsaG/PsaK family."}
{"protein": "MDIIPPRLKEPAYRIYEMRLRHELVRSKAQLPRHIAVLCDGNRRWARDAGYDDVSIGYRKGAAKIAEMLRWCQAAGIEMATIYLLSTENLQRDPDELTALIEIITDVVEEICAPYNKWSVRTVGDLELLGDEPARRLREAVESTTTKGANFHVNVAVAYGGRQEIVDAVRSLLSKELANGATAEQLIEAVTVDGISENLYTSGQPDPDLVIRTSGEQRLSGFLLWQSAYSEMWFTEAYWPAFRRVDFLRALRDYTARHRRFGK", "text": "FUNCTION: Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the UPP synthase family. Z-FPP synthase subfamily."}
{"protein": "MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHGDLEEVFPISFKGDSNI", "text": "FUNCTION: Expression of the eut operon allows this bacteria to use ethanolamine as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration- dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136). FUNCTION: Probably a major component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation (PubMed:22428024, PubMed:27063436). Each homohexamer has a central pore with an opening of up to 8.6 Angstroms. A positively-charged funnel leads to the pore from each side of the hexamer. The pore probably allows metabolite passage into and out of the BMC (By similarity). Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC. Expression alone leads to thick filaments that interfere with cell separation (PubMed:22428024, PubMed:27063436). Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo. May play a role in BMC shell biogenesis (PubMed:27063436). Can replace homolog pduA in the pdu operon, cells grow better than wild-type on 1,2-propanediol and vitamin B12. Protein is incorporated into the pdu BMC microcompartment (PubMed:28585808). FUNCTION: The ethanolamine (EA) catabolic bacterial microcompartment (BMC) probably concentrates low levels of ethanolamine catabolic enzymes, concentrates volatile reaction intermediates, keeps the level of toxic acetaldehyde low, generates enough acetyl-CoA to support cell growth, and maintains a pool of free coenzyme A (CoA) and NAD (Probable) (PubMed:16585748). Deletion of BMC genes (eutK, eutL, eutM) restores growth of eutD deletions, suggesting there are dedicated pools of coenzyme A (CoA) and NAD in the BMC (PubMed:23585538). SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the bacterial microcompartments protein family."}
{"protein": "MQAERGARGGRGRRPGRGRPGGDRHSERPGAAAAVARGGGGGGGGDGGGRRGRGRGRGFRGARGGRGGGGAPRGSRREPGGWGAGASAPVEDDSDAETYGEENDEQGNYSKRKIVSNWDRYQDIEKEVNNESGESQRGTDFSVLLSSAGDSFSQFRFAEEKEWDSEASCPKQNSAFYVDSELLVRALQELPLCLRLNVAAELVQGTVPLEVPQVKPKRTDDGKGLGMQLKGPLGPGGRGPIFELKSVAAGCPVLLGKDNPSPGPSRDSQKPTSPLQSAGDHLEEELDLLLNLDAPIKEGDNILPDQTSQDLKSKEDGEVVQEEEVCAKPSVTEEKNMEPEQPSTSKNVTEEELEDWLDSMIS", "text": "FUNCTION: Protects against apoptosis mediated by Apaf-1. SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Note=Associated with intracellular membranes."}
{"protein": "MLTAERIKFTQKRGFRRVLNQRVDAYFAEHGLTQRDNPSMYLKTLIIVLWLFSAWAFVLFAPVIFPVRLLGCMVLAIALAAFSFNVGHDANHNAYSSNPHINRVLGMTYDFVGLSSFLWRYRHNYLHHTYTNILGHDVEIHGDGAVRMSPEQEHVGIYRFQQFYIWGLYLFIPFYWFLYDVYLVLNKGKYHDHKIPPFQPLELASLLGIKLLWLGYVFGLPLALGFSIPEVLIGASVTYMTYGIVVCTIFMLAHVLESTEFLTPDGESGAIDDEWAICQIRTTANFATNNPFWNWFCGGLNHQVTHHLFPNICHIHYPQLENIIKDVCQEFGVEYKVYPTFKAAIASNYRWLEAMGKAS", "text": "SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
{"protein": "MTTWSCMNLQDSASPIMEQLIFFHDHTLMIVTMILVSVLYFMTSMTINKNENRYMLEGQTIELIWTIAPAVILVFITTPSLRLLYLMDEIHNPTMTIKTIGHQWYWSYEYSDFIKVEFDSYMTPYEEDNKKMFRLLETDNHVTLPMNSFIRIIVTAADVLHSWTIPSLGIKADATPGRLNQSSFMINRPGLLYGQCSEICGANHSFMPIVIESVSTKKFIEWIKNLSE", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
{"protein": "MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK", "text": "FUNCTION: [Isoform Cytoplasmic]: Catalyzes the dehydration of L-malate to fumarate (By similarity). Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by- product of the urea cycle and amino-acid catabolism (By similarity). Also plays a role in DNA repair by promoting non-homologous end-joining (NHEJ) (PubMed:20231875, PubMed:26237645). In response to DNA damage and phosphorylation by PRKDC, translocates to the nucleus and accumulates at DNA double-strand breaks (DSBs): acts by catalyzing formation of fumarate, an inhibitor of KDM2B histone demethylase activity, resulting in enhanced dimethylation of histone H3 'Lys-36' (H3K36me2) (PubMed:26237645). FUNCTION: [Isoform Mitochondrial]: Catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH. FUNCTION: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:30761759). Experiments in other species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable). SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol Nucleus Chromosome Note=Translocates to the nucleus in response to DNA damage: localizes to DNA double-strand breaks (DSBs) following phosphorylation by PRKDC. SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase subfamily."}
{"protein": "MGAMIVREVYEIAEKIKSMEIRGAGKIARSVAQALMIQAEKSTAKSPEELWTELKEAAKILYKTRPTAVSLPNALRYVMHRAKIAYSSGADLETLRFTVINSAKEFIHNSEKAIERIGEIGAKRIEDGDVIMTHCHSKAAISVMKTAFDQGKDIKVIVTETRPRWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGADSITANGAVINKIGTSLIALTAKEHRVWVMIAAETYKFHPETMLGQLVEIEMRDPTEVIPEEELKTWPKNIEVWNPAFDVTPPEYIDVIITEKGIIPPYAAIDILKEEFGWALKYREPWED", "text": "FUNCTION: Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO. SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family. R15P isomerase subfamily."}
{"protein": "MFNYSGLNEECGVFGIWNHPEAAQLTYMGLHSLQHRGQEGAGIVVSDQNELKGERGLGLLTEAIKDDQMERLKGYQHAIGHVRYATSGNKGIENIQPLLYHFYDMSVGICHNGNLINAKSLRQNLEKQGAIFHSSSDTEVIMHLIRRSKAPTFEEALKESLRKIKGGFTFAILTKDALYGAVDPNAIRPLVVGKMKDGTYILASETCAIDVLGAEFVQDIHAGEYVVINDKGITVKSYTHHTTTAISAMEYIYFARPDSTIAGKNVHAVRKASGKMLAQESPVKADMVIGVPNSSLSAASGYAEEIGLPYEMGLVKNQYVARTFIQPTQELREQGVRVKLSAVKDIVDGKNIILVDDSIVRGTTIRRIVKMLKDSGANKVHVRIASPEFMFPSFYGIDVSTTAELISASKSPEEIKDYIGADSLAYLSVDGLIESIGLDYDAPYSGLCVESFTGDYPAGLYDYEANYKAHLSHRQKQYISKNKHYFDSEGNLNV", "text": "FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MSKTYHFIGIKGSGMSALALMLYQMGHKVQGSDVEKYYFTQRGLEQAGITILPFDEKNLDGDMEIIAGNAFRPDNNVEIAYADQNGISYKRYHEFLGSFMRDFVSMGVAGAHGKTSTTGMLSHVLSHITDTSFLIGDGTGRGSANAKYFVFESDEYERHFMPYHPEYSIITNIDFDHPDYFTSLEDVFNAFNDYAKQITKGLFVYGEDAELRKITSDAPIYYYGFEAEGNDFVASDLLRSTTGSTFTVHFRGQNLGQFHIPTFGRHNIMNATAVIGLLYTAGFDLNLVREHLKTFSGVKRRFTEKIVNDTVIIDDFAHHPTEIIATLDAARQKYPSKEIVAVFQPHTFTRTIALLDDFAHALNQADAVYLAQIYGSAREVDHGDVKVEDLANKINKKHQVITVENVSPLLDHDNAVYVFMGAGDIQTYEYSFERLLSNLTSNVQ", "text": "FUNCTION: Cell wall formation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family."}
{"protein": "MDNQFPSRKGPCFCSFRYVLALFMHFCNIVIIAQRMCLSLTMVAMVNNTNLHGSPNTSAEKRLDNTKNPVYNWSPDVQGIIFSSIFYGAFLIQIPVGYISGIYSIKKLIGFALFLSSLVSIFIPQAAAVGETWIIVCRVVQGITQGTVTTAQHEIWVKWAPPLERGRLTSMSLSGFLLGPFIVLLVTGIICESLGWPMVFYIFGACGCAVCLLWFVLYYDDPKDHPCVSLHEKEYITSSLIQQGSSTRQSLPIKAMIKSLPLWAISFCCFAYLWTYSRLIVYTPTLINSMLHVDIRENGLLSSLPYLFAWICGVIAGHTADFLMSRNMLSLTAIRKLFTAIGLLLPIVFSMCLLYLSSGFYSTITFLILANASSSFCLGGALINALDLAPRYYVFIKGVTTLIGMTGGMTSSTVAGLFLSQDPESSWFKIFLLMSIINVISVIFYLIFAKAEIQDWAKEKQHTRL", "text": "FUNCTION: Important for the resorption of phosphate by the kidney. May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Plays a role in urate transport in the kidney. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family."}
{"protein": "MWQLLLPTALLLLVSAGMRAEDLPKAVVFLEPQWYRVLEKDRVTLKCQGAYSPEDNSTRWFHNESLISSQTSSYFIAAARVNNSGEYRCQTSLSTLSDPVQLEVHIGWLLLQAPRWVFKEEESIHLRCHSWKNTLLHKVTYLQNGKGRKYFHQNSDFYIPKATLKDSGSYFCRGLIGSKNVSSETVNITITQDLAVSSISSFFPPGYQVSFCLVMVLLFAVDTGLYFSMKKSIPSSTRDWEDHKFKWSKDPQDK", "text": "FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory- like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (By similarity). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (By similarity). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Secreted Note=Exists also as a soluble receptor."}
{"protein": "MAGKMKLFSVTSERPLATKIADYLDIPLCEVELQKFSDGEVKINIEESIRGTNAYVVQSMNSNVNERLMELLIMVDALKRASVHSINIIMPYYGYARQDRKARSREPITAKLMANLIQRAGADRLITVDLHAAQIQGFFNIPIDHLSAIPLIGDYLIENYGEKDVVVVAPDHSGVVRARRIADRLNAPIAILNRKPRPHEDEIMSVIGDVKGKVAIVVDDIIDTGVRATTSADILLEKGAVEVIACATHSVMAGNATERLQNSNIKEVITSDSIDLPEDKQFDKLTTISIGRILGRAIEGVQENRSLHPLF", "text": "FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily."}
{"protein": "MKVLILVLLAVVILQAAPIRKLEDLLPTRYPPDHELVYWCTYANQCDFCWECVHGICRNRIQADWPVIHQNDWIINCTVSRWNGICSYYEGPRNHTDHQMDCANPTSHTYPHREYMKIYERDDL", "text": "FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. SIMILARITY: Belongs to the asfivirus MGF 110 family."}
{"protein": "MALKFAPFASEIELPFYTALSQLKIDHDKLDDSARPVLGLYEPRATQSPDQSSRMRVLGNALSSTEVPLGHIRAEGIIKNVNTIEDFKNTDKQAMLQTSAKQIWDAINDGTIYSIPSLLSSFTILSFANLKKYTFTYWFAFPALHSEPAWKKVEQPPKFSAEETTALTEELAKRVYPSLEQPQDPENESNSDLPFKWVIGSLREFEDGFFNGVDAKDQYVSFVDPSTYLENPGWMLRNLLVLIRRRYKLDKVQILCYRDNHAKRHVPQSLILVLESIYDPEYQSTGPDETPKVTGWERNSLGKLTAKVTNLAQYMDPAQLADQAVDLNLKLMKWRIAPELDLDAIKNTKCLLLGAGTLGTYVSRLLMGWGVRKITFIDNASVSFSNPVRQPLFDFKDCIDGGAKKAYRAAEALQEIYPGVDSTGHVMSVPMLGHPITDEAATKMDFELLQKLVEDHDAIFLLMDTRESRWLPTVMGKAAGKIVMNAALGFDTYVVMRHGVTPEDGGPAALGCYFCNDVVAPSDSVKDQTLDQQCTVTRPGVAPEASSKLVELLASVLQHPLRGAAPAPKLSANQQSGQMEFDRDPPNHPLGLVPHQIRGFLSAYKTMLISGPSYDCCSACSPKIVNAYKEDGWEFIKRALTEKDYITELSGLAEVQRKAEEAANDVEWDSEEEGVEDEEAELL", "text": "FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates atg12 for its conjugation with atg5 and atg8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the atg8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Preautophagosomal structure. SIMILARITY: Belongs to the ATG7 family."}
{"protein": "MAVCARLCGVGPARGCRRRQQRRGPAETAAADSEADTDPEEERIEAGPARCSLLELPPELLVEIFASLPGTDLPSLAQVCSRFRRILHTDTIWRRRCREEYGVCENLRKLEITGVSCRDVYAKLLHRYRHILGLWQPDIGPYGGLLNVVVDGLFIIGWMYLPPHDPHVGDPMRFKPLFRIHLMERKSATVECMYGHKGPHNGHIQIVKRDEFSTKCNQTDHHRMSGGRQEEFRTWLREEWGRTLEDIFHEHMQELILMKFIYTSQYDNCLTYRRIYLPPSHPDDLIKPGLFKGTYGSHGLEIVMLSFHGSRARGTKITGDPNIPAGQQTVEIDLQRRIQLPDVENLRNFNELSRIVLEVREQVRQEQEAGEGAAPPREPSAKAADGPPAKDGKEPGGGAEAAEQSASSGQGQPFVLPVGVSSRNEDYPRTCRLCFYGTGLIAGHGFTSPERTPGVFVLFDEDRFGFLWLELKSFSLYSRVQATFQNAAAPSPQAFDEMLRNIQSLTS", "text": "FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest (By similarity). SIMILARITY: Belongs to the FBXO31 family."}
{"protein": "MLDTNMKTQLRAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSDKVTFKEDNTLPVRKPSFLITNPGSQQGPRFAGSPLGHEFTSLVLALLWTGGHPSKEAQSLLEQIRDIDGDFEFETYYSLSCHNCPDVVQALNLMAVLNPRIKHTAIDGGTFQNEITERNVMGVPAVFVNGKEFGQGRMTLTEIVAKVDTGAEKRAAEALNKRDAYDVLIVGSGPAGAAAAVYSARKGIRTGLMGERFGGQVLDTVDIENYISVPKTEGQKLAGALKAHVSDYDVDVIDSQSASKLVPAATEGGLHQIETASGAVLKARSIIIATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQVLQDKVRSLKNVDIILNAQTTEVKGDGSKVVGLEYRDRVSGDIHSVALAGIFVQIGLLPNTHWLEGALERNRMGEIIIDAKCETSVKGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYLIRTKIA", "text": "FUNCTION: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MTVVSVPQREPLVLGGRLAPLGFSSRGYFGALPMVTTAPPPLPRIPDPRALPPTLFLPHFLGGDGPCLTPQPRAPAALPNRSLAVAGGTPRAAPKKRRKKKVRASPAGQLPSRFHQYQQHRPSLEGGRSPATGPSGAQEVPGPAAALAPSPAAAAGTEGASPDLAPLRPAAPGQTPLRKEVLKSKMGKSEKIALPHGQLVHGIHLYEQPKINRQKSKYNLPLTKITSAKRNENNFWQDSVSSDRIQKQEKKPFKNTENIKNSHLKKSAFLTEVSQKENYAGAKFSDPPSPSVLPKPPSHWMGSTVENSNQNRELMAVHLKTLLKVQT", "text": "FUNCTION: Nuclear receptor coactivator. May play a role in signal transduction. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PNRC family. PNRC1 subfamily."}
{"protein": "MNHCLVVSHKKLQTFRTFAASKFSSFTKSAQKSIKYSFQFIYQNNPLFVHVAYFALISFAGYGSLKVLKPRDKSNTLKDLDVLFTSVSASTVSSMATVEMEDFSSAQLWVLTILMLIGGEVFTSMLGIHFMRAEFGTKESVSTRDHSPCIDIESITSTKFGPSTQGTKVTVSFSELRMENGGHVEPKTIKFLGFVVMGYLLITNLGGSLLIYLYLNLVPSAHKILKRKGIGIIVFSVFTAISSVGNCGFTPVNENMIIFQKNSILLLLILPQILAGNTLFAPCLRLMVWSLEKITGKKDCRYILEYPKAIGYKHLMSTRESVYLTLTVVSLIILQTVLFLSLEWSSVALDGMSNYQKIVSALFQSVNARHAGESVTDLSNLSSAILVLYTIMMYLPGYTSFLPRHDGEDSKTEKINKRKGLLENWIFSHMSYLAIFVMLICITERDSMATDPLNFNVFSILFEVVSAYGNVGFSVGYSCKRLLNHDARCKDASYGFAGKWSDNGKAILIIVMLFGRLKTFNMKGGRAWKLR", "text": "FUNCTION: Functions as a highly-selective sodium transporter (PubMed:19482918, PubMed:25750424). Does not seem to function as sodium-potassium cotransporter (PubMed:19482918, PubMed:25750424). May be involved in turgor changes for rolling and unrolling of leaves in response to environmental variations (PubMed:19482918). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TrkH potassium transport family. HKT (TC 2.A.38.3) subfamily."}
{"protein": "MAAEVKTVIKPLGDRVVVKRIEEEPKTKGGIVLPDTAKEKPQKGKVIAVGTGRVLENGQRVPLEVKEGDIVVFAKYGGTEIEIDGEEYVILSERDLLAVLQ", "text": "FUNCTION: Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GroES chaperonin family."}
{"protein": "MAGKLGVLLLALVLSLAQPASARRKLLVFLLDGFRADYISDEALESLPGFKEIVSRGVKVDYLTPDFPTLSYPNYYSLMTGRHCEVHQMTGNYMWDPDTNKSFDLGINRDSRLPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYCLEYKSVPTDINFVNAVSGALDVFKSGQADLAAIYYERVDVEGHHYGPSSPQRKDAVKAVDTVMAYMTKWIQERDLQDDLNVIIFSDHGMTDISWTDKVIKLDNYINLRDLQQLKGRGPVVSLWPAPGKHSEIYNKVRRVEHMTVYAKEDIPSRFYYKKGKFVSPLTLVADEGWFITENRESLPFWMNSTVTRKPEGWQWGWHGYDNELRAMRGIFLAFGPDFKSDFRAAPIRVVDIYNLMCKVTGVTPLPNNGSWSRVMCMLKDPASSAPGAPPCACALVTVLLVLLAILA", "text": "FUNCTION: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells (PubMed:23161088). Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet- activating factor (PAF) and lysoPAF, but not other lysophospholipids (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase family."}
{"protein": "ADKIFEETKKIINAFIQRITYVEFLPEILNAETLKNNELNEGIYGYEEFTDPRISNVFSTAAFQFIHSLTPSSIEFDGTETPLMDLFNNQNFLFLDTEKVAVYMMSSAGEPMDRFFSKQLTDHYFQSGNISFDLVAQIIQRGRDHGLPSYNTFRRHCGLPRLPHFYAMEAANVLKAVYHNIDDVDVFVGGMVEIPLPGSLLGPTFSCLIARQFRDTKFGDSHWYESADPKKGFNEGQLKSIKAMSAAKILCDGFGLSLIPENPFRVTSPSNPMVVCADLPGLDFQPWFLLGNQI", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family."}
{"protein": "MLHKSVLGLVLAAGMGTRMRSNQSKALQMIGGKPMIAHLLASMQETNLLTHQAIVYGYRGEALQAALKADFPNVFWVKQEQQLGTGDAVKSATALIEQHDLTLIAFADIPLIRPHTLQQLLHSAAQHGFAILTAQMENPFGYGRIIHDETGGVCAIVEEKDANREQKNIREINVGVMAVKQEWLLTYLPRLENHNAQGEFYLSDLVELIARDGHFIESFCLESADEAMGANDRAQLAALEAVYRQRKVQELFAQGVTLIDPNRIDIHGTVIAGADVVIEPNVFLKGTVVIGDGVTIESGCCLKDCEIGRNTIIRSHSVIDTATIGAQADIGPFARIRPQTVIADGGKIGNFVEIKAAKIGQESKVNHLSYIGDAHIGAKVNVGAGTITCNYDGAAKHPTFIGDHVFIGSNTALVAPVTIKNGATIGAGSVITRDVAADTLALTRPKLTQIEHWRRPQKKKEHKNDA", "text": "FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the N- acetylglucosamine-1-phosphate uridyltransferase family. SIMILARITY: In the C-terminal section; belongs to the transferase hexapeptide repeat family."}
{"protein": "MTSSIVLKFFLIATLLVIANSLPACHNGQFLKINKGPNCDDAKYENPDYVIVGGGAAGSVLLDKCISYGYKCTLIERGIDYEDEQVVSQPSGSGLVQSSNAVLLTTTYPNSNIFNKTLVITEPNIIGGSTSINGEISVFTDIENFFEEISIPGWSYLDVLPYYLNVTNSVNRPSHQGAVDVTNTLVTDPKYVAFKAAIQQVFPNIHEKLPDMNTASLNGGFPGYGPPETSVKTSFIPIGDTQVPVSGFRESAYRAYIHPIRNHPNVRIMLRSRVDKVAFDKCGETAKKVFVTYQNYQGSDSQCELKAKKGIILSAGALRTPQILMQSGVGPADHLNELGIPVVSDMPDVGQHLDDHPTVVRTFLGIIPDSSISANIDGHAYWNHLDDPNKVPNWSIQISGFYGPNFKNILNVYMDQMSRGWIKLRSTDPADTPIFNLGHFSDLEDVGPASLGFNKTNQVISNLQYIPIPGLTDVVCPSFIPNCQSNLTEYYMAAYYQFGYSGYHYTGTCAFEKVVDPNTGLVYGFDNLYVVDASVFPKAPRGNTQIGTYAISAKLADIIFGCQ", "text": "SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "GVGFKAGVKDYRLTHYTPDYETKDTDILAAFRMTPQPGVPAAEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYEIEPVPGEENQFIAYVAYPPDLSEEGSVTNMFTSIVGNVFGFKALRALRLEDSRIPPAYSKTFMGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEALFKSQAETGEIKGHYSNATAGTCEEMLKRAVFARELGVPIVMHDYLTGGFTANTSLAFYCWDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSSGDHIHSGTVVGKLEGERDITLGFVDLLRDDYIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVAPEACVQARNEGRDLAREGNETIREAAKWSP", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
{"protein": "MIKDNIKLKLTIIGDWNVGKSSLLYRFFNDVFYEQTKLSMGEHFFYKTVLIRGESIDLQITDTSGMEKFRSLNNSFYSNLDGILIVYDISDQETFENTKLWLNEANKLAPKDCIKIIVASKFDLENKVVDSNIVKSYADNLNLKFFETSSKNSINVEETFITLVEDILLKKNYQFNNITKNKNNQDEDFNKKKGCSIN", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MTVSFRPTADLVDDIGPDVRSCDLQFRQLGGRTEFAGPISTVRCFQDNALLKSVLSEPGGGGVLVVDGGGSLHTALVGDVIAELARANGWAGLIVNGAVRDSAALRGMDIGVKALGTNPRKSTKTGAGERDVDITLGGVTFTPGDIAYSDDDGIVVAVGD", "text": "FUNCTION: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions (By similarity). SIMILARITY: Belongs to the class II aldolase/RraA-like family."}
{"protein": "MNIHAATPEHSPLGKTVSYQDQYDPSLLFPIARQTKRDEIGVDEAALPFAGVDIWTGFELSWLNARGKPQIGIATFRIPAGSPRLIESKSFKLYLNSYNQTRMDGIDALAAQLARDLSAAAGAEVAVSIALPQAFAAERIAELAGECIDELDIAVDNYAPCPEILSADSTAIVSETLCSNLLKSNCLVTGQPDWGSVSIRYTGPKIDREALLRYLIGFRRHNEFHEQCVERIFVDVLRACAPTKLTVYARYTRRGGLDINPWRSNCDAAPTDNVRTARQ", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 2 subfamily."}
{"protein": "MRTNPTTSSPVVSTLEEKNLGRIAQIIGPVLDVVFPPGKMPNIYNALVVEGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRVLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTSQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEVESKLKK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MAANVPPSAETLLSGAAAHPPKTAEEIANQYNLLPKLIPYLDRHLVFPLLEFSSGQDDEKEVVRAKYELLKHTNMTDYVANLWKEINNSDDIPDEFVKKREEVLAKLQQYEEESAKITQLLQDESVVANLRSDKVANLKFLEEQHGVTIEMVNSLYDYGRFQYSCGSYGNAAELLYQFRVLSTDNDKVASATWGKFASEILTTSWEAAMEEVQKVKDSIETRLFNNPLGQLQNRSWLIHWSLFPFFNHDPARDVLTDLFFSPAYINTIQTNCPWILRYLAAAVITNRNRAHKSSSVYQKQLKDLIRVVRQEGYEYNDPITDFVKALYVDFDFEEAQKKLGEAEDVLRSDFFLVSTTDAFVEAARHLISESYCKIHQRIDIKDLSTRLGLNQDEGEKWIVNLIRDTRVDAKIDYKEGTVIMNHPPQSVYQQVIEKTKGAFFRTQVLRFVRLLYPHD", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit E family."}
{"protein": "MAGIQQQQLVNDTLPASLNGSSNRIASVNVEGQPQPWADDLDLQDPNHQKPGWRKFLSYVGPGFLVSLAYLDPGNLETDLQAGANHRYELLWVILIGLIFALIIQSLAANLGVSTGKHLSELCKTEYPKYVKYCLWLLAEISVIAADIPEVIGTAFALNILFHIPVWVGVLCTGCSTLVLLGLQKYGVRKLELLIAVLVFVMAACFFGEMSYVKPSATDVLKGMFIPKLSGQGATGDAIALLGALIMPHNLFLHSALVLSRKMPNSVRGINDACHYFLIESGFALFIAFLINLAVISVSGTVCSAQNLSSENADRCGDLTLNSASFLLQNVLGKSSSKIYAIALLASGQSSTITGTYAGQYIMQGFLELKMRKWIRNLVTRCIAIAPSLVVSIIGGSSGAGRLIIIASMILSFELPFALIPLLKFSSSTTKMGPHKNSIYIIVISWILGLGIIGINIYYLSTGFVGWLIDNNLPKVGNVFIAIIVFPLMAIYILAVIYLTFRKDSVVTFLGPNKNDPQQQANMENGLTKSTEGPEMERVPYRGDLADIPLPE", "text": "FUNCTION: Probable divalent metal transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family."}
{"protein": "MISGLFKLSNKQSVLQNATKLVLQRRTFFNIVPNPSVGLTEDQKQFQSMALDFAQEKMKPFAEKWDKEEYFPRDVMREAAELGFGGIYVREDVGGSGLSRLDASIIIEALASADVSTTAFISIHNMCAGLIDIYGTEEQRKKFLPSLVSMEKIASYCLTEPGSGSDAGSLSTKATKDGDHYILNGSKAFISGGGDSEVYLVMVRTGAEKGPKGISCLLVEKDTPGLSFGKKEEKLGWNTQPTRALIFEDCRVPVGNLIGKEGQGFSIAMNALNGGRINIGACSLGGAQSCLVAARDHVKVRKQFNQPLEHFQAVQFKMADMATKLHASRIMIRNAAAMLDAKDPSAHVYIAMAKLFACDECFKVTDDSLQLFGGYGYLKDYPVERYLRDLRVHRILEGSDAVMRLIISRELSKDDH", "text": "FUNCTION: Isobutyryl-CoA dehydrogenase which catalyzes one of the steps of the valine catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MSETVGNGENFPAVAARDDRLVWVDLEMTGLDLERHVIVEVAALVTDANLNILGEGVDLVVHATDEELARMDDFVTRMHDSSGLTPLIRASTVSLKDAEDAVLALIEEHCDPAHPAPLAGNSIATDRAFIREQMPRLDAALHYRMVDVSSVKELARRWCPRVYYKQPTKGLAHRALADIVESIRELDYYRRSFFVADPGPTSAQCEADAETSVARFAHYLE", "text": "FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the oligoribonuclease family."}
{"protein": "MAGKRQSQDPVNAIKVVASTMLNSFLEDLKEKNVLNKQELQTMGQTVNVITKKTENLVGDLTEKTQVVGKIFKDHFLNSGSLLSLKSHAENEDECSESSSAVLQEIQASQVKVRKLCPCDHSHEPKITNVHEIYPVMEKEGRTRLALIICNSEFDYLSKRQGSEIDILGMQDLLENLGYSVVVKENLSALEMKTELKNFAARQEHKFSDSTFLVFMSHGTLDGICGTKHRNEEPDILHDDTIFQIFNNRNCRSLKDKPKVIIMQACRGRGDGAVWVTDVGEASAWTCDQPLQCYIFNDAIEKTHVEKDFIAFKSSTPHNVSWRLNTDGSLFISHLIHYFREFSCCHHLEEIFRKVQNSFETPNTMIQMPTIERVSMTRYFYLFPGN", "text": "FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. SIMILARITY: Belongs to the peptidase C14A family."}
{"protein": "MNTATGVIALLVLATVIGCIQAEDTMADLQGGFESYDGEAAKRIFRRSPVCIPSGQPCPYNEHCCSGSCTYKENENGNTVQRCD", "text": "FUNCTION: Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 01 (omega toxin) subfamily."}
{"protein": "MESRMEGDVYSGFGERYQMDGKLLQNFQKSFVQVQDILDQNRLLINEINQNHESKQADHLGRNVGLIRELNNNIRTVASLYGDLSHSFARSVDASSEGESTGTLKSDGKANNQKRFRSG", "text": "FUNCTION: Component of the central CCA1/LHY-TOC1 feedback loop in the circadian clock that promotes clock accuracy and is required for sustained rhythms in the absence of daily light/dark cycles. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EARLY FLOWERING 4 family."}
{"protein": "DEPKPDQFVGLM", "text": "FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the tachykinin family."}
{"protein": "MLMITSFANPRVAQAFVDYMATQGVILTIQQHNQSDIWLADESQAERVRVELARFIENPGDPRYLAASWQSGQTNSGLRYRRFPFLATLRERAGPVTWIVMIACVLVYIAMSLIGDQTVMVWLAWPFDPVLKFEVWRYFTHIFMHFSLMHILFNLLWWWYLGGAVEKRLGSGKLIVITVVSALLSGYVQQKFSGPWFGGLSGVVYALMGYVWLRGERDPQSGIYLQRGLIIFALLWIVAGWFDWFGMSMANGAHIAGLIVGLAMAFVDTLNARKRT", "text": "FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane proteolysis. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase S54 family."}
{"protein": "APSEPHHPGDQATPDQLAQYYSDLYQYITFITRPRF", "text": "FUNCTION: Hormone secreted by pancreatic cells that acts as a regulator of pancreatic and gastrointestinal functions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
{"protein": "MENAKQSFHDVLEFVRLFRRKNKLQREIHDNEKKIRDNQKRVLLLDNLSEYIKPGMSIEAIQEIIASMRSDYEDRVDEYIIKVADLSKERRDLSKKLKTLGEVKG", "text": "SIMILARITY: Belongs to the UPF0265 family."}
{"protein": "MEPAGPCGFCPTGEAQPARYTCPRCNVPYCSLRCYRAHGSCAEEFYRDQVLGELRGRSASPSRLATALRRLRQQRETEDEPGDAGLRPGPAPGGLSGLWERLAPAEKVAFERLLSRGEAGRLLPPWRPWWWGRGAGPRLLEELGDAPSGDAEELEPSPARMPPEPVRDEPAAVEQVLGDLPGACPPAVPTRIPALASLSRGRTSPLVRFQLPNVLFAYAHTLALYHGGDEALLSDFCATLLGVSGALGAQQVFASAEEALQAAAHVLEAGEHPPGPLGTRGAMREAARILLGEGPANQKSYTLAALGDLAQTLGRARKQAVAPEERDRLYRARKKCQFLLSWTNENEDALTPLALDCATAHRAHTVAAEDVAALTGELEQLWGGPLPPARRTLIEELPG", "text": "FUNCTION: May act as a bridging factor mediating the interaction between the R2TP/Prefoldin-like (R2TP/PFDL) complex and U5 small nuclear ribonucleoprotein (U5 snRNP) (By similarity). Required for the interaction of R2TP complex subunit RPAP3 and prefoldin-like subunit URI1 with U5 snRNP proteins EFTUD2 and PRPF8 (By similarity). May play a role in regulating the composition of the U5 snRNP complex (By similarity)."}
{"protein": "MSAKSKGNPSSSSAAEGPPAASKTKVKEQIKIIVEDLELVLGDLKDVAKELKEVVDQIDTLTSDLQLEDEMTDSSKTDTLNSSSSGTTASSIEKIKEQANAPLIKPPAHPSAILTVLRKPNPPPPPPRLTPVRCEEPQRVVPTANPVKTNGTLLRNGGLAGRPNKIPNGDICCIPNSNLDKAPLQSLMHRPEKDRSPQAGPRERVRFNEKVQYHGYCPDCESRYNIKNREVHLHSEPVHPPGKIPHQGPLLHPPPHLPNFPLENGGLGISHSNSFPPPTPATVPPPAAPKPQKTILRKSTTTTV", "text": "FUNCTION: Regulator of cell size that promotes cell size increase independently of mTOR and Hippo signaling pathways. Acts by stimulating the translation of specific mRNAs, including those encoding proteins affecting mitochondrial functions. Increases mitochondrial mass and respiration (Probable)."}
{"protein": "MTRFVLFICCFFLIGMVVECKDGYLVGNDGCKYSCFTRPGTYCANECSRVKGKDGYCYAWMACYCYSMPNWVKTWDRATNRCGRGK", "text": "FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. Strongly affects skeletal muscle channels Nav1.4/SCN4A, poorly affects the neuronal channels Nav1.6/SCN8A and Nav1.2/SCN2A. Induces spastic paralysis of rear limbs, increased salivation, apnea, tachycardia and increased perspiration. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MSASESAPSAPPVKGMRKNGKNWHDSKKPFRPTAGMTSYAKRLEARKHQEAVKEHERELKEEKEAERQAHIQRIKDRRAAKEEKERYDKMAEKMHRKRVERLKRREKRNKLLNS", "text": "FUNCTION: Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the CGR1 family."}
{"protein": "MMTGTTLILEPVMDSKDELVKQHAKVAEDAVAGWEKAENEVVELKQKLEDAADKNIVLEDRVSHLDGALKECVRQLRQFRDEQEKNIQAAVTESTKELHSANTGLEKRVLELQKEAEAAKSENMMLRREFLTQREDLEIVMIERDLSTQAAETASKQHLDIIKKLAKLEAECRKLRILAKTSSSLSSNQSVDSHSDGGRERVEGSCSDSWASSAFISELDQIKNEKGGNRSLQGTTSSTEIDLMDDFLEMERLVALPTETQAKNSKDGYELSLMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAMKRELKLANESKTQAESRVTRMEAEVRKERIVSDGLKEKCETFEEELRREIEEKTMIKREKVEPKIKQEDIATAAGKFADCQKTIASLGKQLQSLATLEEFLIDTASIPGSARSVHNKEALLGKDPHECIKTINGRSLEFLAIQNSNNKTSPPCSSSSDSTTVSLIMSSNRGSSEKNRNGFATVFTRSRNSVNLGI", "text": "FUNCTION: Ensures, when in complex with FPP3/VETH1 and COG2, the correct secondary cell wall (SCW) deposition pattern by recruiting exocyst components to cortical microtubules in xylem cells during secondary cell wall deposition by recruiting EXO70A1. SUBCELLULAR LOCATION: Vesicle Note=Present in vesicle-like small compartments which exhibit microtubule plus-end-directed and end-tracking dynamics. SIMILARITY: Belongs to the FPP family."}
{"protein": "MTKKLTAQEKLNRKPIPTACVFCHEKHLQCDLGRPCQNCSKRGIGDTCRDKERKPRKRGPRKVKKEREVSASTKSEISNTINQQLIPVINTATAVSNRQNSSKIIKAKQTGVSTKKTRISKLAMDSLPLQMPVINSPSDMFGKQKKVMSPELPKIPSLTQLFNPTAEPIISDALLPSNQNSAANLPSLADKTPLEEFKNKPLSERAPQQGPQQPAQQLLPIPEKLNSDHTSSNSSTGEFGSVWTTEEYTKLNDMLSTPNLSRNNSKTYLNSNIAWSPSNMMKMDPITESQRPINTQELLNLTSNGLKRTHSRPHISLDQMASESKRHSANDTSPESQGGETVENLSPYRFRLLVKTPEDLYKHQALIQPHNYKSAYLELLRFLRWRFINSDKPSSGKSQRDGPEQLQNIAHSIKTHYAPIFVTLTNSLIAQDLKLQEIILQRALLEYESMAKLVNCTPMCIWRRSGEICFASNEFISLTGFNKKEILNKRKFIMEFMDNESIVDYYDIFHEYLAFGSTQSGPFNSSTGTSDGQAIFSECNLLLKNGCYLRCACIWTVKRDAFNIPMLIMGQFLPIFDIE", "text": "FUNCTION: Transcription factor which regulates nonfermentable carbon utilization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ERT1/acuK family."}
{"protein": "MKNQLNFNIVSDEELSEANGGKLTFIQSTAAGDLYYNTNTHKYVYQQTQNAFGAAANTIVNGWMGGAAGGFGLHH", "text": "FUNCTION: Kills Lactococci. SUBCELLULAR LOCATION: Secreted. Host cell membrane; Single-pass membrane protein."}
{"protein": "MDKMFCYQCQETAKGTGCTSIGVCGKTSETSGLQDLLLYTEKGVAAYSTVFRKNGKAKELLEGKVNRYLINSLFITITNANFDDNAILDEIKAGLKLREELKALATDEEKKEAEKYGADLVNWYYESNEDLIKFSENQSVVGVLRTENEDVRSLRELIMYGLKGMAAYAEHAFNLGKTSEEIFAFVEEALLGTMDDSLNAEQLVALTIKTGEYGVKVMALLDEANTSALGTPEITKVKIGAGKRPGILISGHDLWDLKQLLEQSKDSGIDIYTHSEMLPGHGYPELKKYSHFYGNYGNAWWDQRKDFTNFNGPIIFTTNCIVPPVKNATYKDRVFTTNAAGYPGWKRIKVNADGTKDFSEVIELAKICQAPVEVESGEITVGFAHNQVLSLADKVVENIKSGAIKRFVVMSGCDGRMSQRHYYTEFAENLPKDTIILTSGCAKYKYNKLNLGDINGIPRVLDAGQCNDSYSWAVVALKLKEVFGLNDINELPIVFNIAWYEQKAVIVLLALLYLGIKNIHVGPTLPGFLSPNVAKVLVENFGIAGITTVEEDLKKFGLYEGSGLDN", "text": "FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HCP family."}
{"protein": "MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRINAFGYLECSAKTKEGVREVFEMATRAGLQVRKNKKRRGCPLL", "text": "FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cleavage furrow Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDATGHIDYADLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKGKVLDICARYPVYA", "text": "FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules (PubMed:3891721, PubMed:1517215, PubMed:7925461, PubMed:10858298, PubMed:19883126). Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine (PubMed:3891721, PubMed:1517215, PubMed:10858298, PubMed:19883126). Also catalyzes the irreversible conversion of 5,10-methenyltetrahydrofolate to 5- formyltetrahydrofolate (PubMed:2201683, PubMed:10858298). FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family. SIMILARITY: Belongs to the SHMT family."}
{"protein": "MAANGSTQLSQKEADIKMMCAAEVHLGTKNCNYQMERYVFKRRNDGIYIFNLGKTWEKLMMAARVIVAIENPQDIIVQSARPYGQRAVLKFAQYTGANAIAGRHTPGTFTNQMQTSFSEPRLLILTDPRTDHQPIKEGALGNIPIIAFCDTDSPMRFVDIGIPANNKGKHSIGCLFWLLARMVLQMRGTIRPAQKWDVMVDLFFYREPEETKPEDEDEVAPQAEFGLPAPEYGGGDQWTTAAIPDAAWPGEAQAPISAAPAAGSWNDSAAPAAAEGGWDAAVPPTTAVTNWE", "text": "FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MSGRGKAVSKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAHRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKSRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSGGVSTSGKKSSQQSQEY", "text": "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post- translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H2A family."}
{"protein": "MGVYLAVLFSLLVIEMAILFILVLPLPQRMRRWLYIRYSIISTNKKFRTYMVGIMIFVGLLFIDSWKRSQIRVSTYRNQKNPYIINSVTPVDALASRAYNQRNVYISGFIIYFYICILTVMSILRRIVEWNDKMKAGDDILKEKLRRKQKYLEELQKKKF", "text": "FUNCTION: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BCAP29/BCAP31 family."}
{"protein": "MFLPRPDFRIALSICFMAVSFVISRFGSEVRPTLLLALPLVLGHVSTGLIGFVLNVIAGHHSTVTLAASTIGTALLWLPMLVPMGTLISLTVLVSQLHGAERERDIGPLFRQALWLAMLLGLVMFTFLSVVPALLPLFGIVPDIVPGAAKFLHVVRWGSLAFPLYFCMRYFCEGMHCTFPTMLLGFGGLLVLVPLSYALTYGRFGFAEYGVEGLGIATVTVMWLQAVVFALYLWRSRRFAHLQLFAHLELPCWARIRDLLNIGLPIGISILMEGGLFIVTTLLIGRFGTDEIAAHQIALSVAQLCFMIPMGVAEATTVRIGHAVGRCDLLVMRRVAWAGYAIVIGTQTLSASVLLLGYDVIVAAYTDDLVVASLASKLLLFAAIFQFPDGLQMLSSGVLRGMKDTRVPMLLAMISYWGLGMPLGLGLGFALEWNSRGMWIGLIIGLTAAALLLGWRFRVVSERMFAGIP", "text": "FUNCTION: Multidrug efflux pump. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MSMACTKVWRSTMYTPRRLKRTTPASRVSSTAMAAANGDASHGANGGIQIQSKEMKTAIHSNDSPKTLLKSESLHEYMLNTMVYPRENEFMRELRLITSEHTYGFMSSPPEEGQLLSLLLNLTGAKNTIEVGVFTGCSVLATALAIPDDGKVVAIDVSREYFDLGLPVIKKAGVAHKVDFREGAAMPILDNLLANEENEGKFDFAFVDADKGNYGEYHERLLRLVRAGGVLAYDNTLWGGSVALEDDSVLEEFDQDIRRSIVAFNAKIAGDPRVEAVQLPVSDGITLCRRLV", "text": "FUNCTION: Catalyzes the stepwise methylation of tricetin to its 3'- mono- and 3',5'-dimethyl ethers. No 3',4',5'-trimethylated ester derivatives are produced. Can use caffeoyl CoA, 5-hydroxyferulic acid, luteolin, tricetin, quercetin, myrcetin and 7,8-dihydroxyflavone as substrates, but not naringenin, apigenin or kaempferol. The 2,3-double bond and the O-dihydroxyl group of the substrate are both required for catalytic activity of the enzyme. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily."}
{"protein": "MYRRDFLKSVTAAWVAFGLPNPLGGAFATNRVIPLRRLGQSQRFDYEWLKERARALAATPYHSRKRVLPTPLERLSWDQYQSIRYRQDHALWADSDAHFQVKFFHLGLYFHSPVRMYEVVDGMAQELAYDPAAFDYGSSGLNGKGLPKDLGFAGFRLNTRKDIDRDFAAFLGASYFRAVGQEGQYGQSARGLAVNTGSSGPEEFPDFIAYYLEQPTADADTVVMYGLLDSPSIAGAYRFSITHADVLRMDIDSALYPRETIERLGIAPCTSMYQVGENDRRMGWDWRPEIHDTDGLFLWTGNGEWIWRPLCNPLHLRFNMFLDNNPRGFGLLQRDRDFDHYQDDGVFYEKRPCLWVEPKHGWGEGSVQLVEIPTFDETFDNIVAFWNPRNKPHPGQELLFGYRLYWGAFPPVSSSLAYCVATRTGLGGVVGQKRKYFSWRFAVDFVGGKLAALARVHDVSVEPVLHMTRGRPEIVSARPLHEIRGYRVMFDVVPLEDSAQQIDIRLYLRDTNGEPLTETWLYQWVPPILEERKY", "text": "FUNCTION: Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the OpgD/OpgG family."}
{"protein": "MTIAVGRAPAGRGWFDVLDDWLKRDRFVFVGWSGLLLFPCAYMALGGWLTGTTFVTSWYTHGIASSYLEGCNFLTAAVSTPADSMGHSLLLLWGPEAQGDFVRWCQLGGLWAFVALHGAFGLIGFMLRQFEIARLVGIRPYNAIAFSGPIAVFVSVFLMYPLGQSSWFFAPSFGVAAIFRFLLFLQGFHNWTLNPFHMMGVAGILGGALLCAIHGATVENTLFEDGDGANTFKAFEPTQEEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVMGLWTSSIGIIGLALNLRAYDFVSQELRAAEDPEFETFYTKNILLNEGLRAWMAPADQPHENFIFPEEVLPRGNAL", "text": "FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family."}
{"protein": "MAHPHLLAERISRLSSALEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQRARAFEYLMTRFSTPEEVFGPLSIQALKDEGRYERLTTGYLPEAEIVFLDEIWKAGPAILNTLLTAINERHFRNGAFEEKIPMRLLVAASNELPEADSSLEALYDRMLIRLWLDKVQDKANFRSMLVSQQDESDNPVPASLQVSDEEYQQWQKDIGAISLPDPVFELIFTLRQQLDNLPNAPYVSDRRWKKAIRLLQASAFFSGRDAVAPIDLILLKDCLWYDAQSLNLMQQQLEILMTGHAWQQQAMLTRLGGIVQRRLQLQQQQSDKTAFTVIKEGGMFSRRPHYTLPPEASASTLTLLLQKPLKLHDMEVIHITFDRSALELWLTKGGEIRGKLNGIGFAQTLNMEVDNAQHLVVRDISLQGTRLALPGTAEDSMPAEIKQQLETLENDWRQQHTRFSEQQHCLFIHSDWLGRIEASLQDVGEQIRQAKQC", "text": "FUNCTION: Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RavA family."}
{"protein": "KHHLEYHLRNHFGSKPFKCEKCSYSCVNKSMLNSHLKSHSNVYQYRCANCTYATKYCHSLKLHLRKYSH", "text": "FUNCTION: Gap class segmentation protein that controls development of head structures. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein family."}
{"protein": "MLCSLSLVLCGLLAGTRADPGGLLRLGMDIMNHEVQSAMEESHILEKMAAEASNPQPGGKAIKGLSNMKVKDVLEPVITLNFVPGVGISQCVSTGMTITGKSFTGGNMEINVVLNITATDRLLQDEEAGTPVFRSEGCEVILVSVKTNLPNNKAINKFVDSTLRKVLPGLMCPAIDAVLEYVNKKWAKLTDPMPVDKMGTVKYALTSPPATTASHIQVDFSPVVQLQEGQLIQLATDGSLPEFPEGSAKDSQLLLSATFLTAELALLQKSLEVKLKDKRVGKLPQNTRTLAGFIPQVAKTYHKPKPLLIKVKINKPPKVTMKAGKSLMHLHGSLEMFAARRHGKHPKSLFRLETHIGLEIHYSVQDNRLQMVTSMDSLLSLARESSSVGDFHEAELTGFITDYLQKAYIPVVNDVLHVGLPLPDLLAINYNLAELDIVEDALVLGLKTE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family."}
{"protein": "MVVKTVRVLNRAGVHARPAALIVQAASRFDSKIMLVRDTIRVNAKSIMGVMAMAAGCGSELELVVEGPDEVAALSAIERLFQNKFEEE", "text": "FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HPr family."}
{"protein": "MIKHRPHGIEHPYAVSPDQRVPVLPLAGEPVLLGVVAPEADRVVCEWGTLELPLSATSAAAADAAALAGGEGHLSEAQAKSLGADGAWSVQTPPLAEPVKYRFHAHRGGAAESTEWFEVSPAVWTADGVGEVRGGGERVRGVEWLVSSQGVHRGRFRLQLQDGDRLVGFGERYDALDQRGRELDAVVFEQYKAQGVHGRTYLPMPFAHVVGADGNGWGFHVRTSRRTWYSSAGNELTVEVALGDEPVVDLAIYEGDPATVLTGFLDEVGRAEELPGWVFRLWASGNEWNTQQLVTARMDTHRDLAIPVGAVVIEAWSDEQGITIWRDAVYAVTEDGSAHRAEDFSYRPDGAWPDPKAMIDELHARGIKVILWQIPLQKTEFSTGQVAADAAAMVRDGHAVLEADGTAYRNRGWWFPQALMPDLSVQRTRDWWTEKRRYLVEHFDVDGFKTDGGEHAWGHDLVYADGRKGDEGNNLYPVHYARAFGDLLRSAGKAPVTFSRAGFTGSQAHGIFWAGDEDSTWQAFRSSVTAGLTAASCGIVYWGWDLAGFSGPVPDAELYLRAAAASAFMPIMQYHSEFNHHQLPLRDRTPWHVAETTGDDRVVPLFRRFATLRESLVPYLTEQAARTIATDRPLMRPLFFDHENDPEIWNHPYQYLLGDELLINPVLEPGATTWTTYLPAGEWIDVWTGDRVPSGLVTRDVPLEVVPVYCRASRWSELQPVFS", "text": "FUNCTION: Involved in the intracellular degradation of the cyclic tetrasaccharide cyclobis-(1-6)-alpha-nigerosyl (CNN) formed extracellularly from starch. Catalyzes the hydrolysis of the alpha-1,3- glucosidic linkage of cyclobis-(1-6)-alpha-nigerosyl (CNN) to yield isomaltose via a possible linear tetrasaccharide. It has a strong preference for the alpha-(1-3)-isomaltosyl moiety. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 31 family."}
{"protein": "MLRVRCLRGGSRGAEAVHYIGSMLRKSFVGWVQRSFQSTQAAAVSEKPCAADEKVRDTAAQECPVCSYNEWDPLEEVIVGRPENANVPPFSVEVKANTYEKYWPFYQKHGGQSFPVDHVKKAIEEIEEMCKVLKHEGVIVQRPEVIDWSVKYKTPDFESTGMYAAMPRDILLVVGNEIIEAPMAWRARFFEYRAYRPLIKDYFRRGAKWTTAPKPTMADELYDQDYPIRTVEDRHKLAAMGKFVTTEFEPCFDAADFMRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYKVHIISFKDPNPMHIDATFNIIGPGLVLSNPDRPCHQIELFKKAGWTVVTPPTPLIPDNHPLWMSSKWLSMNVLMLDEKRVMVDANETSIHKMFEKLGISTIKVNIRHANSLGGGFHCWTCDIRRRGTLQSYFR", "text": "FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane. SIMILARITY: Belongs to the amidinotransferase family."}
{"protein": "MDGIIEQKSMLVHSKISDAGKRNGLINTRNLMAESRDGLVSVYPAPQYQSHRVGASTVPASLDSSRSEPVQQLLDPNTLQQSVESRYRPNIILYSEGVLRSWGDGVTTDCCETTFIEDRSPTKDSLEYPDGKFIDLSADDIKIHTLSYDVEEEEEFQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDLHQASTSSRRALFLAVLSITIGTGVYVGVAVALIAYLSKNNHL", "text": "FUNCTION: May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Early endosome membrane; Single-pass type II membrane protein Postsynaptic density membrane Synapse Cell projection, dendrite Cell projection, dendritic spine Note=Shuttles between the cell surface and early endosome membrane. SIMILARITY: Belongs to the CD225/Dispanin family."}
{"protein": "MFAKAFRVKSNTAIKGSDRRKLRADVTVAFPTLGTDQVSELIPGKEELNVVKLYAHKGDAVTVYTSGGNPILFELEKNLYPTVYTLWSHPDLLPAFITWPLVLEKLVGGADLMLPGVVVPPTGLPQVQQGDLCAIALVGNRAPVAVGVAAMSTAQMLASGLKGKGISVLHTYQDHLWRSGDKSSPPAIAPLDPTDSCEEKADLGLHGNLRSLSLEGEEENGQVPNPEASDDPNSRALSQDSVDGKPLQEQMDELLEQCFLHALKSRVKKADLPLLTSTLLGSHMFSCCPEGQQLDIKKSSYKKLSKFLQHMQQEQIVQVKELSKGVESIVAVDWRHPRITSFIVPEPSLASQTVQEGSREKPYLPPDIKSLYCVPANMTQLFLESGHKKGSTLEGSEVRRIITDYAKRNNLVDADNRNLVKLDPILCDCILEKNEQHLVMKLPWDSLLTRCLKNLQPAYQVTFPGQEPIIKKGKLCPIDITLVLKTYNKKVTVVRNLETYGLDPCSVAAILQQRCQASTIVSPAPGAKDSLQVQVQGNQIHHLGQLLLEEYRLPGKYIQGLEKAPKPGKK", "text": "FUNCTION: Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF2D family."}
{"protein": "MKTNVKTDNKKGIVIAPINDRTFSLSEITASPALDYVGIGFDENYNCYLPPVNRHALAKLPHQNAQHGGILHSRANMVSATYEGGKALSKMEMRALCLNLIQFGDVGLLKVRNGFGQVVRLVPLSSLYLRVHKDGGYSYLMKKSLYDTAQEIYRYDAKDIIFIKLYDPMQQVYGSPDYVGGIQSALLNSDATVFRRRYFSNGAHMGFILYSTDPDLTEEMEEEIARKISESKGVGNFRSMFVNIAGGHPDGLKVIPIGDTGTKDEFANIKNISAQDVLTAHRFPAGLSGIIPTNTGGLGDPLKYREVYHYDEVMPLQEIIAETINQDPEIKNLLKIKFREQNFAK", "text": "FUNCTION: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the terminase subunits to form the packaging machine. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the phage portal family. PBSX subfamily."}
{"protein": "MSNTSLPSSFDSHPEFFQETKWQKFTRRIKEEPLIPIGYAATSYALWRAYKSMKAGDSIELNRMFRARIYGHAFTLFAIVAGGIYYGNERRQRKEFEKALQEKSNQQKRDSWLRELEIRDKEDKDWRQRHAAIEAAAKEAEKKG", "text": "FUNCTION: Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RCF1 family."}
{"protein": "MTLTASPTAARTPAEEKARFEGNKLAKRLARETTRAIADYNMIEAGDKVMVCLSGGKDSYALLDILLSLQKRAPFAFEIIAVNLDQKQPGFPPEILPDYLRALGVPFHIETQDTYSIVTRVIPEGKTMCSLCSRLRRGILYRVASELGATKIALGHHRDDILGTFFLNLFYGGKAKGMPPKLVSDDGRHTVIRPLAYVPESDLIAYAQFKQFPIIPCNLCGSQENLKRKEVGRMIQEWDRKHPGRSWNVFNALSRVVPSHLMDRDLFDFVGLKPTGVADAGGDTAFDQIDPEPDTAGPGCASDAPAGQADGMAEQRVVFR", "text": "FUNCTION: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TtcA family."}
{"protein": "MADATSPFNVSILDNSTKLSEMVESGWNVLASTSVQAFNEAMDVLEESYPLCKKMLDHNNLFPERDPNDTRIWCNATYDTVLCWPPTPANSSVTLQCPHMKGLDPNKNITKDCHVSGVWSGRNAGEMGPTLPGWTNFTMCYTDEVIYIMQNLNNESLTIAQEVARNARKLEFVGLGLSLVSLILAISIFSYFRRLRVFRNLLHLHLMIAMLMVVILRLVLYIDLIFTGENGPHTNSAEGKTINTMPIVCEGMFFFLEYFKTVTFCWMFLEGIYLNNQIVFGFFNSEPKLLPYFIAGYGIPLVHTMLWLLVVLIKKDFKVERCLGSYYLEPEFWILDGPRMAELVINLFFICNVIRVLYSKVRESNNTSEAGLKKSVKAAMMLLPLLGVPNIMQTIPFAPTRDNIMVFAVWTYTASFTYMYQGLMVASIYCFTNKEVNHVLKTFYARYRLLHKSQNELRRGSRSVASHYAAKNGTANASAPQTNNADEFGKLSPFPSRSKKGSDDSTTKLMKDAVMEEEKNANNNGYGSAGEMTPLREGSNRSTKSP", "text": "FUNCTION: [Isoform a]: G-protein coupled receptor which is activated by neuropeptides PDF-1 and PDF-2 (PubMed:18390545). Probably acts through the G-alpha(s) type of G proteins to elevate cAMP levels (PubMed:18390545). FUNCTION: G-protein coupled receptor for PDF neuropeptides (PubMed:18390545). Plays a role in responses to environmental signals, including chemicals and touch, and in modulating locomotory behaviors (PubMed:30024377, PubMed:18390545, PubMed:14551910, PubMed:22579613, PubMed:23143519, PubMed:23972393, PubMed:26113231). Capable of transducing signals via an adenylate cyclase acy-1 cAMP-dependent pathway (PubMed:23972393, PubMed:30024377). Required to regulate the sex-specific expression of TGFbeta-like daf-7 in the ASJ chemosensory neurons, perhaps acting via acy-1 (PubMed:30024377). Involved in modulating mate searching behavior independent of nutritional status (PubMed:18390545, PubMed:22579613, PubMed:23143519, PubMed:14551910). In the presence of food, plays a role in initiating and extending exploratory roaming behavior, perhaps acting in AIY, RIM, RIA, and other neurons, in opposition to 5-hydroxytryptamine (serotonin) signaling (PubMed:23972393). Involved in mediating arousal from the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity (PubMed:18390545, PubMed:23764289). May play a role in circadian rhythms of locomotor activity (PubMed:26113231). FUNCTION: [Isoform b]: G-protein coupled receptor which is activated by neuropeptides PDF-1 and PDF-2 (PubMed:18390545). Probably acts through the G-alpha(s) type of G proteins to elevate cAMP levels (PubMed:18390545). FUNCTION: [Isoform c]: G-protein coupled receptor which is activated by neuropeptides PDF-1 and PDF-2; however, activation is lower compared to isoforms a and b (PubMed:18390545). Probably inhibits cAMP levels through the G-alpha(i/o) type of G proteins (PubMed:18390545). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family."}
{"protein": "MDAREIIEMIAKAKKKTPIVAYIKGDLAGIDFSSFKFFGDEKFGILFGEYEDFKKLLEEHKEKIEDYHLEVKARNSALPLADITKYKARIEPGAIIRDMVEIGEGAVIMMGAVINVGAVIGEGTMIDMNAVIGGRAIIGKKCHIGAGAVIAGVIEPPSAKPVVIEDEVVVGANAVILEGVTVGKGAVVAAGAVVTKDVPPYTVVAGVPARVIKQIDERTKEKTKIVDELRNLE", "text": "FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate. SIMILARITY: Belongs to the transferase hexapeptide repeat family. DapH subfamily."}
{"protein": "MAGMKEIRGKIKSVQNTRKITKAMEMVAASKMRRAQERMRAARPYAEKVRAIAAHMSRANPEYRHPFMVANEGVKTAGMILVTTDKGLCGGLNTNVLRASLQKFKELEEKGQKVEATAIGGKGLGFLNRFGAKVISQVVHLGDTPHLDKLIGAVKTQLDLYSEGRLSAVYLAYTRFVNTMKQETVIEQLLPLSSEHFDANDGTPATSWDYIYEPDAQAVVDELLVRYVEALVYQAVAENMASEQSARMVAMKAASDNAKTVISELQLSYNKSRQAAITKELSEIVGGAAAV", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family."}
{"protein": "MEAVIKAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDTNCSTVGTDRLVLSASITGGPDNSTTLTYRKVSCLLLKLNVSMWDEPPELQLLGSQSLPNVTNITQVSGVAGGCVYFAPRATGLFLGWSKQGLSRFLLRHPFTSTSNSTEPFTVVTADRHNLFMGSEYCGAYGYRFWEIYNCSQTRNTYRCGDVGGTGLPETWCRGKGGIWVNQSKEINETEPFSFTANCTGSNLGNVSGCCGEPITILPLGAWIDSTQGSFTKPKALPPAIFLICGDRAWQGIPSRPVGGPCYLGKLTMLAPNHTDILKILANSSRTGIRRKRSVSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDVAGMCCFNLSDHSESIQKKFQLMKKHVNKIGVDSDPIGSWLRGIFGGIGEWAVHLLKGLLLGLVVILLLLVCLPCLLQFVSSSIRKMINSSINYHTEYRKMQGGAV", "text": "FUNCTION: [Surface protein]: The surface protein (SU) attaches the virus to the host cell entry receptor TVC (PubMed:16051833). This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate its fusogenic potential. Fusion occurs at the host cell plasma membrane (By similarity). FUNCTION: [Transmembrane protein]: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre- hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N- terminus of Gag (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the Alpharetroviruses envelope glycoprotein family."}
{"protein": "MAAAPPAVAVNGGGMAAAKVASQAYLESKAVKDTRVLIADLCKQFYTLGWVSGTGGSITIKAHDDSIPKRQQLILMSPSGVQKERMEPEDMYVLATNGSILSSPSPKPYPYKPPKCSDCAPLFLKAYDMRNAGAVIHSHGMESCLVTMINPLSKEFRITHMEMIKGIQGHGYYDELVVPIIENTAYENELTDSLAKAIEAYPKTTAVLVRNHGIYIWGDSWISAKTQAECYHYLFDAAIKLHQIGLDWSTPNHGPIQNVKVKAGMNNSNNRIEPLPRCIVLDIEGTTTPITFVADVLFPYARDNVGRHLSATYDTAETKDDINLLRTQVEDDLAQGVDGAIPIPTDDAGKEEVIAALVANVEAMIKADRKITALKQLQGHIWRTGYENNELEGVVYDDVPEALEKWHALGIKVYIYSSGSRLAQRLIFGKTNYGDLRKYLSGFFDTTVGNKKETRSYIEISESLGVDKPSDILFVTDVFQEAFAAKGAGLDVMISIRPGNAPLPENHGFKTITSFAEI", "text": "SIMILARITY: In the C-terminal section; belongs to the HAD-like hydrolase superfamily. MasA/MtnC family. SIMILARITY: In the N-terminal section; belongs to the aldolase class II family. MtnB subfamily."}
{"protein": "MRSFLRYFSSVKEATQFRFESCRVENKSYIRLLGPDSIKFLNGLVTSKLQPNFVKKNLTTISTKEQEKNNTLSSLNFSKYNWGIYKECTRLEDHISRFGTYTGFLNMKGKLLTDSIIYPYPFTLKSIQDKKFPEYLMEFDSHIAQKMERTLDNHKLLSKVKFKHVQNEELRTWDAYITMPEEYQLLENLLNPMQEMKDGEQALHFANFFASMFFQGNEHKLKAVYFDTRLIDDMYEGKIKPMFRIVTDNSVSDINDIFNCTAFGENPFEKANISATEIQKERFKFGLFDGNHEYIPETLLALEANFDYFEDSINSDKGCYVGQELTARTFATGVLKKRCVGITIDEPQKLADWDHSKYLSIFSKLELQVQNQDTQAAINPFGSLSKPVKKRTRPAGQLINYNGNIGVAVVRKDYIYHALKHHHDIDAYVELPNKETVACSIKLEWLDRFLEETEAEEVEQEQ", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvT family. CAF17 subfamily."}
{"protein": "MSTTTAGILFALSLALALAAVHVPLGDYMYRVYASEKHWRAERVAYRIIGADPAAEQGWGSYARSVLAFSAVSILFLFGLQLLQGRLPLHLNDPATEMTPALAWNTAVSFVTNTNWQAYSGESTQGHLVQMAGLSVQNFVSAAVGMAVAMAFVRGLARRDTGELGNFWVDLIRGSLRILLPLSIIGAIILVSGGVIQNFALHDTVVSTLSGAQQTIPGGPVASQEAIKELGTNGGGFFNANSAHPFENPTTWTNWVEIFLLSCIAFSLPRTFGRMVGSRKQGAAILAVMAVIATLSLSLMMLFQSQTHGTVPTAVGSATEGVEQRFGVADSAVFADLTTLTSTGAVDSFHDSYTSLGGLMTLFNMQLGEVAPGGVGSGLYSMLVLAVITVFVAGLMVGRTPEYLGKKITPREIKLAATYFLVTPLIVLIGTAVAMALPGQRDGMLNTGPHGLSEVLYAFTSAGNNNGSAFAGLSVNTEWYNTALGLAMVFGRFLPIILVLALAGSFARQGRTPESVGTLPTHRPQFVGMVTGVTLILVALTFLPVLALGPLAEGLH", "text": "FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KdpA family."}
{"protein": "MAIAGVLFLLFLARQASAAGYGGWQSAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGAACGSCYELRCDNAGSSCLPGSITVTATNFCPPNYGLPSDDGGWCNPPRPHFDMAEPAFLHIAQYRAGIVPVSFRRVPCVKKGGVRFTVNGHSYFNLVLVTNVAGAGDVRSVSIKGSRTGWQPMSRNWGQNWQSNAFLDGQSLSFQVTASDGRTVTSNNVAHPGWQFGQTFEGGQF", "text": "FUNCTION: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. Required for normal plant growth. May be required for rapid internodal elongation in deepwater rice during submergence. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily."}
{"protein": "MAKDMDSVVQLAKHRGFVFPGSEIYGGLSNTWDYGPLGVELKNNIKQAWWKKFISQSPYNVGLDAAILMNPRTWEASGHLGNFNDPMIDNKDSKIRYRADKLIEDYMQNEKGDENFIADGLSFDEMKRIIDEEGIKDPVSGTSNWTDIRQFNLMFKTFQGVTEDSTNEIFLRPETAQGIFVNYKNVQRSMRKKLPFGIGQIGKSFRNEITPGNFIFRTREFEQMELEFFCKPGEEIEWQNYWKTFAEKWLLDLGIKNDSIRLRDHDEDELSHYSNATTDIEYKFPFGWGELWGIASRTDYDLKQHSEFSGDDFKYHDPETNEKYIPYCIEPSLGADRVTLAFLCDAYDREGVEGSKDERTVLHFHPAIAPYKAAVLPLSKKLSEEAIKVYEQLSENFTVDFDESQSIGKRYRRQDEIGTPYCITFDFDSLEDQQVTVRDRDSMEQVRMPISELNDFISEKVRF", "text": "FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MARLSEPSPYVEFDRAQWRALRMSTPLKLTEDELVRLRGIGEKIDLLEVEEVYLPLARLIHLQVAARQALFATTADFLGEPQQNPDRPVPFVIGVAGSVAVGKSTTARVLQALLARWEHHPRVDLVTTDGFLYSNSELSRRNLMHRKGFPESYDRRGLMRFVTTVKSGSDVACAPVYSHLLYDIVPGEKQIIEHPDILILEGLNVLQTGPALMVSDLFDFSVYVDARIEDIENWYISRFLKMREGAFADPASHFHHYSTLTDEQAVFAARDIWHSINRPNLIENILPTRPRATLVLRKDSDHSINRLRLRKL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic pantothenate kinase family."}
{"protein": "MLFHSLSGPEVHGVIDEMDRRAKSEAPAISSAIDRGDTETTMPSISSDRAALCAGCGGKISDRYYLLAVDKQWHMRCLKCCECKLNLESELTCFSKDGSIYCKEDYYRRFSVQRCARCHLGISASEMVMRARDLVYHLNCFTCTTCNKMLTTGDHFGMKDSLVYCRLHFEALLQGEYPAHFNHADVAAAAAAAAAAKSAGLGAAGANPLGLPYYNGVGTVQKGRPRKRKSPGPGADLAAYNAALSCNENDAEHLDRDQPYPSSQKTKRMRTSFKHHQLRTMKSYFAINHNPDAKDLKQLAQKTGLTKRVLQVWFQNARAKFRRNLLRQENTGVDKSTDAALQTGTPSGPASELSNASLSPSSTPTTLTDLTSPTLPTVTSVLTSVPGNLEGHEPHSPSQTTLTNLF", "text": "FUNCTION: Acts as a transcriptional activator. Stimulates the promoter of the alpha-glycoprotein gene. Transcriptional regulatory protein involved in the control of cell differentiation in developing lymphoid and neural cell types (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKNLKGIFSALLVSFNEDGSINEKGLREIVRYNIDKMKIDGLYVGGSTGENFMLSTAEKKEIFRIAKEEAKDQVALIAQVGSVNLHEAVELGKYATELGYDSLSAVTPFYYKFSFAEIKHYYETIIAETGNNMIVYSIPFLTGVNMGVEQFGELYANPKVLGVKFTAGDFYLLERLKKAYPNHLVWAGFDEMMLPAVSLGVDGAIGSTFNVNGLRARQIFELAKAGKVAEALEIQHVTNDLIEGILANGLYLTIKEILKLQGVNAGYCREPMTAKATEKQLAVAKELKEKFL", "text": "FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family. NanA subfamily."}
{"protein": "INGDAKGTVFFEQETSEAPVKVTGEGLGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPRNKEHGAPTDENRHLGDLGNIQAAGDSPTAVSITDSKITLFGADSIIGRTVVVHADA", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MAGVSVESKVSSLVCNLSSTSGLIRRTANPHPNVWGYDFVHSLKSPYTDSSYRERADALVVEIKAMLNAAIAGDGESTITPSAYDTAWVARVPAIDGSARPQFPQTVDWILKNQLKDGSWGIESHFLLSDRLLATLSCVIALFKWNVGDLQVKQGIEFIKSNLELVKDESDQDSLVTDFEIIFPSLLREAQSLSLELPYDLPYIHLLQTKRQERLAKVSREEIYTVPSPLLYSLEGIQDIVEWDRIMDVQGQDGSFLSSPASTACVFIDVKCLEFLNNVMMKLGNFVPCLYPVDLLERLLIVDNIERLGIYRHFEKEINEALDYVYRHWNERGIGWGTRNPIADLETTALGFLLLRLHRYNVSPAVFDNFKDSNGQFFCSTGQLNKDVASMLSLYRASQLAFPGEDILDEAKSFTTKYLREALEKSETSSAWNNKQNLSQEIKYALKTSWHASVARVEAKRYCQVYRPDYARLAKSVYRLPYVNNEKFLELGKLDFNIIQAIHQEEMKTVTSWFRDSGLPLFTFARERPLEFYFLVATGTYEPQYAKCRFLFTKVACLQTVLDDMYDTYGTLDELKLFTEAVRRWDLSFTENLPDYMKLCYKIYYDIVHEVAWEAEKEQGRELVSFFRKGWEDYLLGYYEEAEWLASEYVPSLDEYIKNGITSIGQRILLLSGVLIMDGQLLSQEALEKVDYPGRRVLTELNSLISRLADDTKTYKAEKARGELASSIECYMKDHPECTEEEALAHIYSILEPAVKELTREFLKPDDVPFACKKMLFEETRVTMVIFKDGDGFGVSKLEVKDHIKESLIDPLPL", "text": "FUNCTION: Converts farnesyl diphosphate to alpha-bisabolene (PubMed:28096378). Involved in defensive oleoresin formation in conifers in response to insect attack or other injury (By similarity). Involved in sesquiterpene (C15) olefins biosynthesis (By similarity). SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
{"protein": "MSRILMSQLTHPQRVRLLYKTILRLHRGLPAELRALGDNYVRDEFRRHLKCNPMEAQLFMTEWARYASTITQQLGIRGKPKGELGEEIDPKTVEMLKDDQVVQLYELMLAAKGVEDAQGK", "text": "FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SdhB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily."}
{"protein": "MSATIEREFEELDAQCRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTRAVVMLNRTVEKESVKCAQYWPTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQILLSMRKYRMGLIQTPDQLRFSYMAIIEGAKYTKGDSNIQKRWKELSKEDLSPVCRHSQNRTMTEKYNGKRIGSEDEKLTGLSSKVPDTVEESSESILRKRIREDRKATTAQKVQQMRQRLNETERKRKRWLYWQPILTKMGFVSVILVGALVGWTLLFQLNVLPRLTDT", "text": "FUNCTION: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T- cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Also plays an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. May also bind DNA (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum Nucleus membrane. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus Cytoplasm Cell membrane Note=Predominantly localizes to chromatin. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors. Recruited by activated ITGA1 at the plasma membrane (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum-Golgi intermediate compartment Note=Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class 1 subfamily."}
{"protein": "MAYCRQEGKDRIIFVTKEDHETPSNAELVADDPNDPYEEHGLILPNGDINWNCPCLGGMASGPCGEQFKAAFSCFHYSKEDVKGSDCVDQFRAMQECMQKYPDLYPQEEEEEEEQPADPLPEAASEASATKEAAASS", "text": "FUNCTION: Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes. Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17, COX19, MICU1 and COA7. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Required for the import of COA7 in the IMS. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system. Mediates formation of disulfide bond in MICU1 in the IMS, promoting formation of the MICU1- MICU2 heterodimer that regulates mitochondrial calcium uptake. SUBCELLULAR LOCATION: Mitochondrion intermembrane space."}
{"protein": "MDLEFGRGMRSPQRDSWKTTLLLAYQSLGVVYGDLSISPLYVFKSTFAEDIQHSETNEEIFGVLSFVFWTLTLIPLIKYVSIVLRADDNGEGGTFALYSLICRHANVSLLPNRQIADEELSTYKLECSSERTDKSCIKVWLEKHKKLHTALLIMVLIGTCMVIGDGVLTPAISVFSAVSGLEFSLSKDHREYAVIPITCVILAFLFALQHYGTHRVGFLFAPIVLAWLICMSALGLYNIIHWNPHVYQALNPCYMFKFLKKTRKYGWMSLGGILLCMTGSEAMFADLGHFSYSAIQLAFTSLVYPALILAYMGQAAYLSKHHDFYSNSQVGFYIAVPDKVRWPVLVLAILASVVGSQAIISGTFSIINQSQSLSCFPRVKVVHTSDKIHGQIYIPEINWLLMILCIAVTVGFRDTKHMGNASGLAVITVMLVTTCLTSLVIMLCWRRPPVLALCFLLFFGSVEALYFSASLIKFLEGAWLPILLALFLMAVMLVWHYTTIKKYEFDLHNKVTLEWLLALGDKLGMVRVPGIGLVYTDLTSGVPANFSRFVTNLPAFHQVLVFVCVKSVPVPYVFPAERYLIGRVGPPGHRSYRCIVRYGYRDVHQDVDSFETELVESLATFIKLDASYRCSDASGGGGDHEPEEERGTRLAVIGSSHASYDIQDSVQHSSAASVETTTTRRRSGGGDDDGSPGGGGGRAKQVRFFIDSHVASPEAADNKQVAEELEALAAARDAGTAFILGHSHVQCKPGSSLLKRLAVDVGYNFLRRNCRGPDVALRVPPASLLEVGMVYVL", "text": "FUNCTION: High-affinity potassium transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72.3) family."}
{"protein": "MGRMHAPGKGLSQSALPFRRSVPTWLKLTSDDVKEQIFKLAKKGLTPSQIGVILRDSHGVAQVRFVTGNKILRILKSKGLAPDLPEDLYHLIKKAVAVRKHLERNRKDKDAKFRLILVESRIHRLARYYKTKRVLAPNWKYESSTASALVA", "text": "FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MARGGGAAGVSMAHHLGIALVVLVFAAMAQVARGGGGGHDYGMALSKSILYFEAQRSGVLPGSQRIAWRANSGLADGKANGVDLVGGYYDAGDNVKFGLPMAFTVTMMAWSVIEYGEEMAAAGELGHAVEAIKWGTDYFAKAHPEPNVLYAEVGDGDSDHNCWQRPEDMTTSRQAYRLDPQNPGSDLAGETAAAMAAASLVFRSSNPGYADQLLQHSKQLFDFADKYRGRYDNSITVARNYYGSFSGYGDELLWASAWLYQASDDRRYLDYLANNADALGGTGWSINQFGWDVKYPGVQILAAKFLLQGKAGEHAGVLQGYRRKADFFACSCLGKDAADNVGRTPGGMLYHQRWNNIQFVTSASFLLAVYSDHLAGGAVRCSGGGGAVAGAAELLAFAKSQVDYILGSNPRGTSYMVGYGAVYPRQAHHRGSSIASIRASPSFVSCREGYASWYGRRGGNPNLLDGAVVGGPDEHDDFADERNNYEQTEAATYNNAPLMGILARLAAGHGARARGRLGQSLQHGIAANHTSLPHGANHQHASPVEIEQKATASWEKDGRTYHRYAVTVSNRSPAGGKTVEELHIGIGKLYGPVWGLEKAARYGYVLPSWTPSLPAGESAAFVYVHAAPPADVWVTGYKLV", "text": "FUNCTION: Hydrolyzes 1,4-beta-glycosyl linkages of 1,4-beta-glucans and 1,3-1,4-beta-glucans. Possesses broad substrate specificity for hemicelluloses of type II cell walls. Substrate preference is carboxymethyl-cellulose > 1,3-1,4-beta-glucan > lichenan > arabinoxylan > phospho-swollen cellulose > xylan > glucomannan. May participate in lateral root development. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family."}
{"protein": "MQDYKIKIENVVASTQIGENIDLNKISREIKDSEYKPKQFPGLVLRTKEPKAAALVFRSGKVVCTGSKSVEDARRAVKQIVKMLKEIGISVIDEPEVKVQNIVASADLGVDLNLNAIAIGLGLENIEYEPEQFPGLVYRLDNPRVVVLIFGSGKMVVTGGKSPEDARKAVERISEELRTLGLM", "text": "FUNCTION: General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity). SIMILARITY: Belongs to the TBP family."}
{"protein": "MKINGQSVSRETQERLEHFVELFKKWNKTTNLVAPSTLTELWSRHVADSAQIFQLSPQPKKWIDLGSGGGFPGVITAIFLAELGDGWVDLVESNNKKAAFLRIALKETGARGAVHPVRIETASEIITTCNAVSARALADLDLLFGYIHPWAQNNPNLKAYFNKGRDYDSEVQKAHGRWQFDLIKHRSAIEADSVVLEISNLVLRR", "text": "FUNCTION: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family."}
{"protein": "MSKKSGKWWESDDKFAKAVYQQFVEFYEKVTGTDLELIQILKDHYNISLDNPLENPSSLFDLVARIKNNLKNSPDLYSHHFQSHGQLSDHPHALSSSSSHAEPRGENAVLSSEDLHKPGQVSVQLPGTNYVGPGNELQAGPPQSAVDSAARIHDFRYSQLAKLGINPYTHWTVADEELLKNIKNETGFQAQVVKDYFTLKGAAAPVAHFQGSLPEVPAYNASEKYPSMTSVNSAEASTGAGGGGSNSVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPAASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALTVTISEIAVKDVTDKTGGGVQVTDSTTGRLCMLVDHEYKYPYVLGQGQDTLAPELPIWVYFPPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTASMSYKFPPVPPENLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTKEGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVTGINAISHGQTTYGNAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTYFPNKGTQQYTDQIERPLMVGSVWNRRALHYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQYAVGIMTVTMTFKLGPRKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEKPEELWTAKSRVHPL", "text": "FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. The additional N- terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus. SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP1]: Virion Host nucleus Host cytoplasm. SUBCELLULAR LOCATION: [Isoform Major capsid protein VP2]: Virion Host nucleus Host cytoplasm. SIMILARITY: Belongs to the parvoviridae capsid protein family."}
{"protein": "MEKMTVSSNYTIALWATFTAISFAVGYQLGTSNASSTKKSSATLLRSKEMKEGKLHNDTDEEESESEDESDEDEDIESTSLNDIPGEVRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNPARASYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGVNAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY", "text": "FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PTH2 family."}
{"protein": "MTDFPSIFVPLVGLVFPAIAMASLSLHVENNKIV", "text": "FUNCTION: May help in the organization of the PsaL subunit. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaI family."}
{"protein": "MSASRFIKCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLISKASYENVSKKWIPELRHYAPGVPIILVGTKLDLRDDKQFFVDHPGAVPISTAQGEELRKLIGAAAYIECSSKTQQNIKAVFDAAIKVVLQPPKQKKKKKKAQKGCAIL", "text": "FUNCTION: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Note=Associated with the membrane when activated. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MPRKAREYPEEGEFVVATVKNIHPYGAFLILDEYPGKEGFMHISEVAPTWVKNIRDYVKEGQKVVVKVIRVDPEKGHIDLSLKRVNQQQRKAKLQEYKRAQKAENLLKMAAEKIGKDFETAWREVWVPLEEEYGEVYAAFEDAAQNGIEVLKGLIPDEWLDALKPIIEAYVEIPTVTIDAEFEITVPKPNGIEIIKEALIRARDRANEEKDIDVKFTYQGAPRYRIDITAPDYYKAEEVLESIAEEILRVIKEAGGEATLIRKEKRIRKIKRR", "text": "FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. SIMILARITY: Belongs to the eIF-2-alpha family."}
{"protein": "MSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG", "text": "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF- regulatory region of its mRNA (By similarity). FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endosulfine family."}
{"protein": "MYKPKISCLLLGLLSGLVFAPTFLLPALLTLSYLCCLVQKSKDWQEAAKLGYIFGFGHFLSGIYWISIGVSVYISDFWWAIPFALFGLPIILAFFVSASCVFSFFVRNNKYYHFIFCLYWVLFEWVRSWIFTGLPWNLIGYAFSFSDILIQSLNIIGIYGLSFIVIYISTSFYPFFTKQFDQLKVLLLTSSITLAVIITYGSVRLHNHPTNFTDIKVRLVQPSIPQTEKWSEEEFWHNLMLHINLSENSQPIDLVIWSEAALVVPYDIPVVKSELLGLLNSVDATLITGGISDNKKRGEDFELYTAMYALEKNGNKLFEYHKSHLVPFGEYMPFKKILPFKKLTHGFVDYTEGNGGLVYLDKYNLKIKPLICYESIFPDFVRTNNETADVIINVTNDAWYGKSSGPYQHFHISRSRAVENGLPMVRVANNGISAIIDPLGRVIKKLDLNEINYIDGLIPKKLDSPTIFSKFGNITILLIVFFIFLVNYLLDKKLINSRD", "text": "FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N- acyltransferase subfamily."}
{"protein": "MVWPRLVLAACLLAMPPAAAECLSQCSLCAVRTQDGPKPINPLICSLECQETLLPSEEWERCQGILSFFPSALRLRDQSGLDSRAALEEVYGELAKRARPFLQELEKSRFLPSTPAEDKFRGLLGGLGEGLGSEAMGAPQLNSGAVEAAALDFDEDPKEQVKRYGGFLRKYPKRSSEVAREGDRDGDNAGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQEDPNAYSEEFFDV", "text": "FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity). FUNCTION: Leumorphin has a typical opiod activity and may have anti- apoptotic effect. FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the opioid neuropeptide precursor family."}
{"protein": "MVHLRRSLAPYWWPIPRKAGGVWVVKPSPGPHSFAYSLPLAIVIRDVLRYAKTLREARYIVSRGYIKVDGVVRKDYRFPVGLMDVIEIVPTGEVYRVVPDQDRYYNLLPIPSSEASLKLLRVEGKTTVNGGRLQLHFHDGRNLITSPDMGAKIKTFDTILYDLENKTIKTHIPMKLGVVAVVTHGSNVGFSGKLYEIVWTLKRRQSVVGLKKGEEVRRTILDYIMAVGEESPVIKITP", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family."}
{"protein": "MTIEVLDRGFVKLLDHMGDDFSAVKAARISHGRDLIDEERDRKLIEYLLRSGHESPFEHIVFTFHIKCPIFVARQWMRHRIASYNELSGRYTELAEEFYLPDLYKRYGERLNENDLQKASKLIEESYKKSHEAYKCLIDMKIPKELARVVLPFATYTQFIWSVNARSLMNFLSLRADSHSQWEMQQFALAVAQVFKSICPWTYESFIRYRYEGDLLKGVNP", "text": "FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant. SIMILARITY: Belongs to the thymidylate synthase ThyX family."}
{"protein": "MLRLLRSSWARGLGSGVATWRPSAGLFRPGCPGIRQASGASDTPHHQSPSSESPVQPVGVGVCSMMRLPLQSSPEGLDAAFIGVPLDTGTSNRPGARFGPCRIREESLMLGAVNPSTGALPFQSLRVADLGNVNVNLYNLQDSCLLIREAYQNVLAAGCIPLTLGGDQTITYPILQAVAKEHGPVGLVHVGAHTNTTDKPREEKVYHRTPFRRSVDEGLLDSKRVVQIGIRGSSRTLDPYRYSRSQGFRVVLAEDCWMKSLVPLMAEVRQQMGGKPLYISFAIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVVGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV", "text": "FUNCTION: Hydrolyzes linear guanidino acids to form urea and the corresponding amines. Displays specificity for substrates having a negatively charged head group and short chains including taurocyamine, guanidino propanoic and butanoic acids. May protect cells by detoxifying potentially harmful amounts of guanidino acids. Metabolizes L-arginine with low efficiency. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the arginase family. Agmatinase subfamily."}
{"protein": "MISYYFQGFALGAAMILPLGPQNAFVMNQGIRRQYHLMIALLCALSDLVLISAGIFGGSALLMQSPWLLALVTWGGVAFLLWYGLGALKTAMSSNLELASAEVMKQGRWKIIATMLAVTWLNPHVYLDTFVVLGSLGGQLAMEPKRWFALGTISASFLWFFGLALLAAWLAPRLRTAKAQRIINILVGVVMWLIAFQLAREGVAHMHALFN", "text": "FUNCTION: Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LysE/ArgO transporter (TC 2.A.75) family."}
{"protein": "MARIAGINIPPQQHAEIGLTAIFGVGRTRARKICEAAGVPVTKKVKDLTDAELERIREHLGVFTVEGDLRREVQLSIKRLIDLGTYRGMRHKRGLPVRGQRTRTNARTRKGPRRAAASLKK", "text": "FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. SIMILARITY: Belongs to the universal ribosomal protein uS13 family."}
{"protein": "MNKNQKPVLTGQRFKTRKRDEKEKFEPTVFRDTIVQGLNEAGSDLEAIAKFLDSAGSRLDYRRYADTLFDILVAGSMLAPGGTRIDDNDKTKMTRHCVFFAEEDHDAIRNYAQVFNKLIRRYKYLEKAFEDEIKKLLLFLKAFSETEQTKLAMLSGILLANGTLPATILTSLFTDNIVKEGIAASFAVKLFKAWMAEKDANSVTSALRKANLDKRLLELFPANRQNVDHFAKYFTEAGLKELSDFLRVQQSLGTRKELQKELQERLSQECPIKEMVLYVKEEMKRNELPEPAVIGLLWTCVMNAVEWNKKEELVAEQALKHLKQYAPLLAVFSTQGQSELILLQKVQEYCYDNIHFMKAFQKIVVLFYKADVLSEEAILKWYKEAHVAKGKSVFLDQMKKFVEWLQNAEEEFRI", "text": "FUNCTION: Translation initiation regulator which may repress non-AUG initiated translation and repeat-associated non-AUG (RAN) initiated translation by acting as a competitive inhibitor of eukaryotic translation initiation factor 5 (EIF5) function. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the BZW family."}
{"protein": "MSNKKADSKPQAKYPVNLLDTPFPMRGDLPKREPQWVKEWEERGIYEKIRAASKGRPKFILHDGPPYANGDIHLGHAVNKILKDIVVKSRNMAGFDAPYVPGWDCHGMPIEIQIEKQFGKSLPAAEVMSKARAYATEQIEKQKVGFKRLGVLGDWANPYKTMNFVNEAEEIRALGKIIEKGYVYRGLKPVNWCFDCGSALAEAEVEYKDRTDPTIDVMFAFAEPEKTAQAFGLPALPRADGGIVIWTTTPWTIPANQALNLHPEIVYALVDTERGLLIIAEERVEACMADFKLTGRIVATAPGVKLANLRFHHPLASAHPGYKRTAPVYLGDYVTTDTGTGVVHSSPAYGIEDFVSCKSHGMTDSDIINPVMGDGRYIESLPLFGGLSIWDANPKVVEALRAAGSLLRSEKYTHSYMHCWRHKTPIIYRATSQWFAGMDVTPHAGGKTLRETALEGIDATAFYPSWGKQRLFSMIANRPDWTLSRQRQWGVPMAFFVHKETGELHPRTLELLEEVAKRVEQSGIEAWQSLDPRELIGDDANLYEKNRDTLDVWFDSGTTHWHVLRGSHKDQLQFPADLYLEGSDQHRGWFHSSLLTASMIDGRAPYKGLLTHGFTVDGEGRKMSKSLGNGIDPHEVANRLGAEIIRLWIASTDYSGELAISEEILKRVTEGYRRIRNTLRFLLANLSDFDFAQHAVPVDEWLEIDRYAVAFSAQLQTELLGHYEKYEFHPVVAKLQTYCSEDLGGFYLDVLKDRLYTSAADSRARRSAQTALYHLTQGLLRVLAPFLSFTAEEAWKVFQPASDTVFTETYYAYPEVAGAAALIEKWALLRDVRGNVTKALEEARTANRIGSSLQAEVAVHASGARYDALTSLGDDLKFVLITSAASVVKVDDEAHESVDVAASKYQKCERCWHYREDVGAHAEHPTLCGRCFSNLFENGEIRSAA", "text": "FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily."}
{"protein": "MLRYAIVFFIIALIAALFGFTGIAAGAVEIAKIMFFIFVLLALVSLVMGFTRRK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0391 family."}
{"protein": "MAKAPVCARKRVRKQVSDGVAHIHASFNNTIVTITDRQGNALGWATAGGSGFRGSRKSTPFAAQVAAERCADAVKEYGIKNLEVMVKGPGPGRESTIRALNAAGFRITNITDVTPIPHNGCRPPKKRRV", "text": "FUNCTION: Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "MPELLKQRVETCYQQAETFFKRPFPRPQVSFKLRGQKAGVAHLHENLLRFNLQLYRENQDDFLRQTVAHEVAHLVAHQLFGDKIQAHGEEWQLIMRGVYELPPNRCHNYEVQRRVATRYIYRCPCPESDFPFTAQRHKLVRQGRRYLCRRCREILVYSGETRVE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SprT family."}
{"protein": "MAQPGKILKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNLVSGEDAGNNFFLQKSSIGKNRAQAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTIVVATQLLESTLLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHLQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYNETNGRIPKSYKEKEDFRDLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPTFWILARALKEFVAKEGQGNLPVRGTIPDMIADSNKYIKLQNVYREKAKKDAAAVGNHVAKLLQSVGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGLDTVNKDEIISSMDNPDNEIVLYLMLRAVDRFHKQHGRYPGVSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL", "text": "FUNCTION: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation (By similarity). The covalent attachment of NEDD8 to target proteins is known as 'neddylation' and the process is involved in the regulation of cell growth, viability and development. SUBCELLULAR LOCATION: Cell membrane Note=Colocalizes with APP in lipid rafts. SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1 subfamily."}
{"protein": "MKTAWLGTFAASALLVAGYAQADADLAKKNNCIACHQVETKVVGPALKDIAAKYADKDDAATYLAGKIKGGSSGVWGQIPMPPNVNVSDADAKALADWILTLK", "text": "FUNCTION: Monoheme c-type cytochrome. Probable electron donor to membrane cytochrome oxidase and to periplasmic nitrite reductase. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MYRALYAFRSAEPNALAFAAGETFLVLERSSAHWWLAARARSGETGYVPPAYLRRLQGLEQDVLQAIDRAIEAVHNTAMRDGGKYSLEQRGVLQKLIHHRKETLSRRGPSASSVAVMTSSTSDHHLDAAAARQPNGVCRAGFERQHSLPSSEHLGADGGLYQIPLPSSQIPPQPRRAAPTTPPPPVKRRDREALMASGSGGHNTMPSGGNSVSSGSSVSSTSLDTLYTSSSPSEPGSSCSPTPPPVPRRGTHTTVSQVQPPPSKASAPEPPAEEEVATGTTSASDDLEALGTLSLGTTEEKAAAEAAVPRTIGAELMELVRRNTGLSHELCRVAIGIIVGHIQASVPASSPVMEQVLLSLVEGKDLSMALPSGQVCHDQQRLEVIFADLARRKDDAQQRSWALYEDEGVIRCYLEELLHILTDADPEVCKKMCKRNEFESVLALVAYYQMEHRASLRLLLLKCFGAMCSLDAAIISTLVSSVLPVELARDMQTDTQDHQKLCYSALILAMVFSMGEAVPYAHYEHLGTPFAQFLLNIVEDGLPLDTTEQLPDLCVNLLLALNLHLPAADQNVIMAALSKHANVKIFSEKLLLLLNRGDDPVRIFKHEPQPPHSVLKFLQDVFGSPATAAIFYHTDMMALIDITVRHIADLSPGDKLRMEYLSLMHAIVRTTPYLQHRHRLPDLQAILRRILNEEETSPQCQMDRMIVREMCKEFLVLGEAPS", "text": "FUNCTION: Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis. SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes."}
{"protein": "MNFETIIGLEVHVELNTNSKIFSPSSAHFGEDPNANTNVIDWSFPGVLPVMNKGVIDAGIKAALALNMDIHKEMHFDRKNYFYPDNPKAYQISQFDEPIGYNGWIEIKLEDGSTKKIRIERAHLEEDAGKNTHGTDGYSYVDLNRQGVPLIEIVSEADMRSPEEAYAYLTALKEIIQYTGISDVKMEEGSMRVDANISLRPYGQEQFGTKTELKNLNSFSNVRKGLEFEVERQAKLLRSGGVIRQETRRYDEANKGTILMRVKEGAADYRYFPEPDLPLYEIDDAWIDEMRAQLPQFPAQRRAKYEEELGLSAYDASQLTATKALSDFFETAVSLGGDAKQVSNWLQGEVAQFLNAEGKTIEEIRLTPDNLVEMIAIIADGTISSKMAKKVFVHLAKNGGSARAYVEKAGLVQISDPAVLVPIIHQVFADNEAAVADFKSGKRNADKAFTGFLMKATKGQANPQVAQQLLAQELQKLRD", "text": "FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln). SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily."}
{"protein": "MAEHDAPPESGAARSPPAKKRGGDARSPQQDAQPLSSRDRVRERDEDKDRERHRRHGEDRERYRDRESVRERGEGSRDRERHRREHREESRDRERHHREHREGSRDRERHHREHREGSRDRERHHREHREGSRDRERHHRDHREGSRDRERHHRDHRERSERREHRDRSDDRDYRRSCDRDAERRDRDRDGHRRHRSRSPLRSESQSKRMSGFDQRPSEAIPILAPDATPSQLPELPAANPGMFPNMLPNLVNVPALGQPLAMTQQATRHARRVYVGGLPPIANEQTVAVFFNQVMAAIGGNTFALGHAVVNVYINHDKKFAFVEMRSVEEASNAMALDGIMFEGAPVKVRRPTDYNPSQAAALGPSQPNPNLNLAAVGLTPGAGGGLEGPDRIFVGGLPYYFTEAQVRELLETFGPLRGFDIVKDKETGNSKGYAFCLYKDGTVTDIACAALNGIQLGDRTLTVRRANQGAEPRPEQENILLQAQQEAQMKRLVYEVGRTLTTKVVCLTQVVSADDLRDDEEYNDILEDMTLEGHKYVPHSTIAESFIIRPHAKFAIRPKLTEDTNLFHLDLTNHMFSSLPFCHVHVCSY", "text": "FUNCTION: Necessary for the splicing of pre-mRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family."}
{"protein": "MNPSSLVLNGLTSYFENGRARVVPPVGRNILGVVNYASVCEYPTLDHGYPELEINMVAPTAEPFAEVWVTDAESEHGERDGITYAHDGEYFFCAGRVPPTGRYTEATRAAYVTMFELLEEFGYSSVFRMWNFIGDINRDNAEGMEVYRDFCRGRAEAFEQCRLEFDQFPAATGIGSRGGGIAFYLLACRSGGHVHIENPRQVPAYHYPKRYGPRAPRFARATYLPSRAADGVGGQVFVSGTASVLGHETAHEGDLVKQCRLALENIELVISGGNLAAHGISAGHGLTALRNIKVYVRRSEDVPAVREICREAFSPDADIVYLTVDVCRSDLLVEIEGVVM", "text": "FUNCTION: Involved in the biosynthesis of BC325, a rapamycin analog containing a 3-hydroxybenzoate starter unit. Catalyzes the hydrolysis of chorismate via an intramolecular mechanism to yield 3- hydroxybenzoate (3HBA). SIMILARITY: Belongs to the FkbO/Hyg5 family."}
{"protein": "MDIKYNELVNQFAPGAKQITIKKIRKKGNGIFSLNRYTSGTVLLEVPLENIICRKTVEQFRNSCDKFASIATLEEWNDMSFRTQAMLFLCYLWLGIQPRTNKWDKFLTVLPLSINTPAQWPEKEVYSLQGTSIFNPVCVKRKILQQEWLSLNQRYSDSWPSKITLPKWVHADALFHSRCLESPFKDPVLAPVIDLCNHSSKSNAKWSFSEDAMQLYLDKDIDENEEVTINYGSEKGSAEFLFSYGFLPEPEGDRITNVMKLLIPEDSNDSLDLAKRRSCKTPPMIEFVSDSSGELWWHAPFLFFSVLNVEDFTNFKMVCDESKAQTVDWEFEGQKCSVEDLPKLVQLSPKRDLYILRVFCLAEQLADAALNTNIENMYNPTERRSESVELLKRESFLLKKVLLYLRDVISKLLKSKVVVEFIHSQTIES", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
{"protein": "MNATDTGMQADPTDLIQRIASLTRMLRDSMRELGLDQAIKDAAEAIPDARDRLRYVAQMTEQAANRVLNATEAAGPIQDGMARGAQALDERWQQWYDQPLELPQARALVQDTRAFLAAVPQHTQQTQAKLMEIVMAQDFQDLTGQVIMRMMDVVGAIERELLQVLLDNVPQERRDEANSLLNGPQVNPGGKADVVTSQDQVDDLLASLGF", "text": "FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CheZ family."}
{"protein": "MPPNLQRIFPALCLLGVLFLLHCTPVLCGCDNPPVVAHGHHTQIIGLFGMKKDEVVYKCDEGYTLVGEDRLSCRSSRWSPAAPQCKALCPKPQIDRGKLSVDQDEYIESENVIVQCGSGYGLVGPKIITCTEDGTWHPRVPKCEWEYPEDCEQVHEGKKLMQCLPNLEEIKLALELYKLSLETKLLELQIDKEKKAKAKYSI", "text": "FUNCTION: May be a lipoprotein-borne regulator of either the coagulation or the complement cascades. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MPTVFPHDSVGLVTPQTAHFSEPLALACGRSLPAYDLIYETYGQLNAARSNAVLICHALSGHHHAAGFHSADDRKPGWWDSCIGPGKPIDTNTFFVVSLNNLGGCNGSTGPSSIDPDTGKPLGANFPVVTVEDWVNSQARLADLLGIDTWAAVIGGSLGGMQALQWTISYPDRVRHCLAIASAPKLSAQNIAFNEVARQAILTDPEFHGGSFQERGVIPKRGLMLARMVGHITYLSDDSMGEKFGRGLKSEKLNYDFHSVEFQVESYLRYQGEEFSGRFDANTYLLMTKALDYFDPAANFNDDLAKTFANATAKFCVMSFTTDWRFSPARSRELVDALMAARKDVCYLEIDAPQGHDAFLIPIPRYLQAFGNYMNRISL", "text": "FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family."}
{"protein": "MIERCLGAYRCRRIQRALRQLKVTILCLLLTVVVLRSTIGAGKFGTPEQDLDEIRQHFHARKRGEPHRVLEEIQTGGDSSSGDGGGNSGGSNNYETFDINKIFVDEGEEEKPDPNKPYTLGPKISDWDEQRSDWLAKNPSFPNFIGPNKPRVLLVTGSAPKPCENPVGDHYLLKSIKNKIDYCRLHGIEIFYNMALLDAEMAGFWAKLPLIRKLLLSHPEIEFLWWMDSDAMFTDMAFELPWERYKDYNLVMHGWNEMVYDQKNWIGLNTGSFLLRNNQWALDLLDTWAPMGPKGKIREEAGKVLTRELKDRPVFEADDQSAMVYLLATQRDAWGNKVYLESGYYLHGYWGILVDRYEEMIENYHPGLGDHRWPLVTHFVGCKPCGKFGDYPVERCLKQMDRAFNFGDNQILQIYGFTHKSLASRKVKRVRNETSNPLEMKDELGLLHPAFKAVKVQTNQV", "text": "FUNCTION: Xylosyltransferase specific to UDP-D-xylose that accepts both cellopentaose and cellohexaose as substrates, with a better use of cellohexaose, to produce xyloglucan. Adds preferentially the first xylosyl residue to the fourth glucosyl residue from the reducing end of both acceptors. Transfer one xylose mainly to the second glucose residue from the non-reducing end. The acceptor should have a minimum of four glucose residues (PubMed:16982611, PubMed:18544630). Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan synthesis in the Golgi (PubMed:25392066). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 34 family."}
{"protein": "MAIRWSELCIVLFALSYAICVLAGKSYYDVLQVPKGASDEQIKRAYRKLALKYHPDKNQGNEEATRKFAEINNAYEVLSDEEKREIYNKYGEEGLKQFSANGGRGGGGGGMNMQDIFSSFFGGGSMEEEEKVVKGDDVIVELEATLEDLYMGGSMKVWREKNVIKPAPGKRKCNCRNEVYHRQIGPGMFQQMTEQVCDKCPNVKYEREGYFVTVDIEKGMKDGEEVSFYEDGEPILDGDPGDLKFRIRTAPHARFRRDGNDLHMNVNITLVEALVGFEKSFKHLDDHEVDISSKGITKPKEVKKFKGEGMPLHYSTKKGNLFVTFEVLFPSSLTDDQKKKIKEVFA", "text": "FUNCTION: Regulates protein folding in the endoplasmic reticulum (ER) lumen. Forms a complex in the ER with SDF2 and MED37A/BIP1 which is required for the proper accumulation and function of the surface- exposed leucine-rich repeat receptor kinases EFR involved in pathogen- associated molecular pattern (PAMP) triggered immunity. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "MDSPEKLEKNNLVGTNKSRLGVCGWILFFLSFLLMLVTFPISVWMCLKIIKEYERAVVFRLGRIQADKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLKSASMVLAESPVALQLRYLQTLTTVATEKNSTIVFPLPMNILEGIGGISYGNNKKVTAKA", "text": "FUNCTION: Required for the function of many mechanoreceptors. Modulate mechanotransduction channels and acid-sensing ion channels (ASIC) proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their sensitivity to mechanical stimulations. SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein Note=Detected in lipid rafts, in apical dendrites and in olfactory cilia. SIMILARITY: Belongs to the band 7/mec-2 family."}
{"protein": "MSNFEMAGTGSSRNNEEDNQQNTNWVWYKHTNNNLSTSHNNQIWQQPSLDLYPGQIDVCDMTTSSRSLTISCQECGNQAKKGCTHGRCRTCCKSNGLHCPTHVRSTWIPIAKRRERQQQLQTPTSNPTGGSGRVGKYRDINQHATLDSSGLEMGETRFPDEVSSDALFRCVRMSGTDDGEGQYAYQTTVGIAGHLFKGILYNQGPENKSMRSTQFYENPPRS", "text": "FUNCTION: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influences vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SHI protein family."}
{"protein": "MDFQQLADVAEKWCSNTPFELIATEETERRMDFYADPGVSFYVLCPDNGCGDNFHVWSESEDCLPFLQLAQDYISSCGKKTLHEVLEKVFKSFRPLLGLPDADDDAFEEYSADVEEEEPEADHPQMGVSQQ", "text": "FUNCTION: Promotes megakaryocyte differentiation by enhancing ERK and JNK signaling as well as up-regulating RUNX1 and FLI1 expression (PubMed:24681962). Represses NF-kappa-B transcriptional activity by inhibiting phosphorylation of RELA at 'Ser-536' (PubMed:24681962). May be involved in early neuronal development (By similarity). FUNCTION: Promotes megakaryocyte differentiation by enhancing ERK and JNK signaling as well as up-regulating RUNX1 and FLI1 expression (By similarity). Represses NF-kappa-B transcriptional activity by inhibiting phosphorylation of RELA at 'Ser- 536' (By similarity). May be involved in early neuronal development (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MTURN family."}
{"protein": "MSKVLVLKTTAQADEVSNSVALTNRFLEEYKKFNPDDEIIIVDLNKDEVGTSILTSETSSTFYQQEVTKKYINLLKSVDKLVIACPMYNFSTPVTLKSFIDHVSVANETFSYKYSKKGDVIGLITNLKAQILGVQGAPLGWYPWGQHTQYVEGAMRFLGIDFNKTVLLAGVKVAPLLQLTPEQRVETIIDEVIEAARTF", "text": "FUNCTION: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. SIMILARITY: Belongs to the azoreductase type 1 family."}
{"protein": "MSRIALYPGSFDPVTNGHLDVVRHAVALCDRLVVAIGIHPGKKPLFTTEERLMMVKSVFEPVANAAGCTFDCTTYDNLTVTSAQQVGATLMIRGLRDGTDLDYEMQIAGMNETMAPGIHTVFVPASVGVRPITATLVRQIAAMGGDVSAFVPPDVAASLKSKFAG", "text": "FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the bacterial CoaD family."}
{"protein": "MSDLHNESIFITGGGSGLGLALVERFIEEGAQVATLELSAAKVASLRQRFGEHILAVEGNVTCYADYQRAVDQILTRSGKLDCFIGNAGIWDHNASLVNTPAETLETGFHELFNVNVLGYLLGAKACAPALIASEGSMIFTLSNAAWYPGGGGPLYTASKHAATGLIRQLAYELAPKVRVNGVGPCGMASDLRGPQALGQSETSIMQSLTPEKIAAILPLQFFPQPADFTGPYVMLASRRNNRALSGVMINADAGLAIRGIRHVAAGLDL", "text": "FUNCTION: Converts 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol) into 3-(2,3- dihydroxylphenyl)propanoic acid (DHPP) and 2,3-dihydroxicinnamic acid (DHCI), respectively. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSLMDPLANALNHLTNCERVGKKVFYIKPASKLIGRVLKVMQDHGYIGEFEFIEDGRAGIFKVELIGKINKCGAIKPRYAVKKHEFEKFEKRYLPARDFGLLIVSTSQGIMTHYEAKEKGIGGRLISYVY", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS8 family."}
{"protein": "MLQSVVFFALLTFASSVSAIYSNNTVSTTTTLAPSYSLVPQETTISYADDTTTFFVTSTVYSTSWFTSTSATITNAASSSLSTSSASGSVTPESTHEITSTSTITSTLLLTLHDSTTLSPSSTAASVSDEDSNNKDAKVKSFEQASTSNGCVPITKFVTVTNEPVTQYVTVTPNTTTQYVTVTGAPSVTTTSPGNVQWYNTTSITNSTSW", "text": "FUNCTION: Required to stabilize the cell wall in the absence of multiple GPI-anchored mannoproteins. SUBCELLULAR LOCATION: Secreted, cell wall. Cell surface."}
{"protein": "MSQLDLGTQSLELERFPPQENSNTLQAWEAADEYLLQNIDLSQIDGRPVLVFNDQFGTLACALHAYRPFSSSDSYMSQLATAHNLRLNHLDESAVTLLSSVDDLPEAPKLVVIKIPKALALLEHQLRALRRVVAPDTVIIAGAKSRDVHNSTLQLFEKILGPTKTTLAWKKARLIHCEVADIPLADAPETIDWPLPNTDYIIHNHANVFSRNNLDIGARFFMEILPYDVTGKIADLGCGNGVVGLIALEQNPLAEMLFVDESYMAVASSELNITVNRPQDLSRCEFMVSHGLAGVERESLQLVLCNPPFHQQHAVSDHVAWQMFCDAKRCLKAGGELMIVGNRHLDYFHKLKRLFGNCETLDSNQKFMVLKSVKQASSRSEGGGSGSLDMSYSDF", "text": "FUNCTION: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family."}
{"protein": "MERITVTLGERSYPITIAAGLFNDPASFLPLKAGDQAMLVTNETLAPLYLDKIRHLLEQAGVNVDSVILPDGEQYKSLAVLETVFTALLQKPHGRDTTLLALGGGVVGDLTGFAAASYQRGVRFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLNTLPQRELASGLAEVIKYGIILDGEFFSWLEDNMDALLNLDGKALAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFKQEETQRIITLLERAGLPVTGPREMSSHAYLPHMMRDKKVLAGEMRLVLPLAIGKSEVRGGVPHDVVLGAIADCQQA", "text": "FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family."}
{"protein": "MQYQLLINGVLVDGEGERQSVYNPATGEVILEIAEASPAQVDAAVLAADSAFAEWGQTTPKARAECLLKLADSIEQNALEFARLESQNCGKPLHCVINDEIPAIVDVFRFFAGAARCLSGLAAGEYLEGHTSMIRRDPIGVVASIAPWNYPLMMAAWKLAPALAAGNCVVIKPSEITPLTALKLAALAKDIFPPGVLNVLFGRGQTVGDVLTGHEKVRMVSLTGSIATGEHILRHTAPAIKRTHMELGGKAPVIVFDDADLDAAAQGVRTFGFYNAGQDCTAACRIYAQRGIYDALVEKLGNAVSSLKMGAPEDESTELGPLSSLAHLKRVTAAVEEAKALSHIRVITGGSQTEGKGYYFAPTLLADAKQEDAIVQREVFGPVVSITVFDDEDQVLRWANDSRYGLASSVWTQDVGRAHRLSARLQYGCTWINTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTLVRHIMVKH", "text": "FUNCTION: Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4- aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma- aminobutyraldehyde dehydrogenase subfamily."}
{"protein": "MGRFIFVSFGLLVVFLSLSGTGADQDCLPDWSSHERHCYKVINEYKTWEEAEQYCTEEANGGHLVSFHNRQEVAFVVKLGYTILKADVVWIGLRDFWRECQWEWSNGAKLNYKGWSDEPNCFIAYTVGNRWVRRKCSSTHPFVCKSPA", "text": "FUNCTION: Interferes with one step of hemostasis (modulation of platelet aggregation, or coagulation cascade, for example). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
{"protein": "MEAIIVYTTFPDWESARKVTRELLERKLIVCANLREHEAMYWWEGKIEEGKEVGAIYKTEVSKWKELRETIKELHPYDVPMIARIDLDKLNREYSEWMARVLFG", "text": "FUNCTION: Involved in resistance toward heavy metals. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutA family."}
{"protein": "MSGSRRKATPASRTRVGNYEMGRTLGEGSFAKVKYAKNTVTGDQAAIKILDREKVFRHKMVEQLKREISTMKLIKHPNVVEIIEVMASKTKIYIVLELVNGGELFDKIAQQGRLKEDEARRYFQQLINAVDYCHSRGVYHRDLKPENLILDANGVLKVSDFGLSAFSRQVREDGLLHTACGTPNYVAPEVLSDKGYDGAAADVWSCGVILFVLMAGYLPFDEPNLMTLYKRICKAEFSCPPWFSQGAKRVIKRILEPNPITRISIAELLEDEWFKKGYKPPSFDQDDEDITIDDVDAAFSNSKECLVTEKKEKPVSMNAFELISSSSEFSLENLFEKQAQLVKKETRFTSQRSASEIMSKMEETAKPLGFNVRKDNYKIKMKGDKSGRKGQLSVATEVFEVAPSLHVVELRKTGGDTLEFHKFYKNFSSGLKDVVWNTDAAAEEQKQ", "text": "FUNCTION: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Involved in K(+) homeostasis under low-K(+) stress. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Targeted to the tonoplast when interacting with CBL2 or CBL3. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily."}
{"protein": "MKISERQKDLLKEIGNIGAGNAATAISYMINKKVEISVPNVEIVPISKVIFIAKDPEEIVVGVKMPVTGDIEGSVLLIMGTTVVKKILEILTGRAPDNLLNLDEFSASALREIGNIMCGTYVSALADFLGFKIDTLPPQLVIDMISAIFAEASIEELEDNSEDQIVFVETLLKVEEEEEPLTSYMMMIPKPGYLVKIFERMGIQE", "text": "FUNCTION: Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a structural motif that mimics a CheD substrate recognition site to bait and inactivate it. SIMILARITY: Belongs to the CheC family."}
{"protein": "MRLILLSGLLLLGIFLANGDEVDREGKVVNSLIDALMHLQREFAKLKGSFLIVHKARSFGSGSERMYVTNKEIKNFEALRQICEQADGHIPSPQLENQNKAFANVLERHGKEAYLVVGDSANFTNWAAGEPNKAAGACVKADTHGSWHSASCDDNLLVVCEFYFIL", "text": "FUNCTION: This phospholipase A2 inhibitor binds directly phospholipase A2 in the presence or absence of calcium. SUBCELLULAR LOCATION: Secreted Note=Secreted in plasma. SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor family."}
{"protein": "MSRKATIERVTKETQIKLSLEIDGTGEAKICTSVPFLDHMLDLFARHGLFNLQVDATGDIDIDFHHTVEDIGIVLGQALKEALGDKKGIRRYGQATVPMDETLASVAVDISGRPYLVYHVSLPKVKIGEFDVELVREFFQAVVNNLGANIHVNVMYGDNVHHIVEACFKAFARAVDQATQVDSRIQGVMSTKGKL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family."}
{"protein": "MKRNHDFSSSDSELDENIEVEKESADENAGANSPLGSMSPSTTSQVQARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHAAGGKGYFDAHALAMDYRGLGFRECLAETARYLSIIEGLDNTDPLRIRLVSHLNSYASQREAHSGLGHLAWGSAFGTPPSHLAHHLLLQQQQQQGAPLARSTSSPPSSNSSSPSSSSPSAPSTEPRLSGTVISEAGQTGPLRVPPSTSLPPGLTPPTASKLSPPLLTSLSSLSAFPFPLSAFPLLSPSSLGPATPSSSLGKPYRPWSMEIGAF", "text": "FUNCTION: Transcriptional repressor which functions as a downstream effector of Notch signaling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HEY family."}
{"protein": "MKHTLQVIITEKELDIRVRELGQEITKKYRNSRNKMILIALLRGSFIFISDLCRRIHIEHEIDFMTTSSYGRGMLSSGDVKIIKDLDEDIYNKNVLIVEDIIDSGKTLSKVLDILKLRNPKSLSICTLLDKPECREVNINVDFIGFSILENFFIVGYGIDYAQSYRYLPNIGKVVFKK", "text": "FUNCTION: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MNYEAIVIGVSAGGINAMKTILPTLPTQFGIPIVIVQHIGARSDGEWFRILEKLCNIKIKEAEEKEEIKSGMVYVAPPNYHLLIEKDKTFSFSIGERVNFSRPSIDVLFETASEVYEDKLIGVILTGANSDGAQGLKKIKENGGLAVVQDPLTAEIALMPRSAIEATSVDYVLSLEKIAELFIRLDQNNLEQR", "text": "FUNCTION: May be involved in chemotaxis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CheB family."}
{"protein": "MYLLIVFLSMLSSSVAGFFGRFLGSESVSRFNLIIFLILLVFSICLFRSLKQYLGKRMTQWCYLALVCQISLFLVLLRSHILAGFGTFSADVFTVFMGTFSVTGSSGGIVNHQDGASSEWFTYTSDMVEDSASSGRTSSSVNQPIPEEQAWEREARAQEHDRISAEVETITSACENLEAAMVRKAQILLHQRGVTLGDPEDVKRALQLALHDDWEHAIDDRKRHFTVLRRNFGTARCERWNPFIDELRGLGNHQVNARHYVD", "text": "SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein."}
{"protein": "MSSYQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDREALLQYLEQQALEVKERDDLVPFTGEKKGKPYIQPKREIPAEEQITLEPELEEALAHATDAEMCDIAAILDMYTLMSNKQYYDALCSGEICNTEGISSVVQPDKYKPVPDEPPNPTNIEEILKRVRSNDKELEEVNLNNIQDIPIPMLSELCEAMKANTYVRSFSLVATRSGDPIANAVADMLRENRSLQSLNIESNFISSTGLMAVLKAVRENATLTELRVDNQRQWPGDAVEMEMATVLEQCPSIVRFGYHFTQQGPRARAAQAMTRNNELRRQQKKR", "text": "FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments (PubMed:25250574). SIMILARITY: Belongs to the tropomodulin family."}
{"protein": "MATDDSIIVLDDDDEDEAAAQPGPSNPASNPVSPGPEASGPSESHGDGGSSNSGSRKCYKLENEKLFEEFLELCKMQTSDHPEVVPFLHKLQQRAQSAFLASAEFRNILSRVLSRSRNRPAKLYVYINELCTVLKAHSIKKKLNLAPAASAESSGDNPPTDPPSDLTNTETTASEASRTRGSRRQIQRLEQLLALYVAEIQRLQEKELDLSELDDPDSSYLQEARLKRKLIRLFGRLCDLKDCSSLTGKVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTDDYRPGVDPALTDPTLARRLRENRTLAMSRLDEVISKYAMMQDKSEEGERQKRRARLLATSQSSDLPKASSDSGEGPSGVASQEDPTTPKAETEDEEDDEESDDEEEEEEEEEEEATEDEDEDLEQLQEDQDDEEEEEGDNEDDKSPASPSPIFRRKEFSNPQKGSGPQEEQQERGLTGTPASPLEASPGLPSTDAESSGEQLQERLLAGESPVSQLSELDMEALPEETIPSPEERGISSSRRKSDSSLPTILENGAAMVTSTSFNGRVSSHPCRDASPPSKRFRKEKKQLGPGPLGNSYVKKQTMAQQDSGWKISVLSTPSSPLASVGPVADSSTRVDSPSHELVTSSLCNPSPSLILQTPQSQSPRPCIYKTSVATQCDPEEIIVLSDSD", "text": "FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Nucleus, PML body Nucleus, nucleolus Chromosome, centromere Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. SIMILARITY: Belongs to the DAXX family."}
{"protein": "MTHTAAGAPRDAKTAIHAPSSRMALMLGALGVVYGDIGTSPLYTLRACLNTIDDLQPAHVLGVLSILFWLLMIVVSLKYVTLVLRADNRGEGGTLALLELAVRGREGRARWLLIVLGIFGAALFYGDSMITPAISVLSALEGISIVSHTLEPWVVPVALVVLVALFAIQSHGTGAVGKLFGPIMALWFATLAVLGGYQIWLTPEVLAALNPVWALRFIAEFPVMSFLLLGAVVLALTGAEALYADMGHFGRPAIRRAWFAMVLPALTLCYFGQGALLLRDPAAIRNPFFLMAPEWGLAALVGLATVATVVASQAVISGAFSVTRQAVQLGFWPRMQILHTSAVEKGQIYLPQVNALLLCAVLVLVLLFRNSENLAAAYGFAVTGTMLTTSVLAFAVLPRDSTGGKRVLWMVLLGALLVIDILLFGANIFKIHEGGWLPLLVGVVVFTLMMTWRRGRRLLADMQARDRQPLREFMTQLEAFPPARVQGTAIFMTMNAGNVPPALLHNLKHNKVLHDHVLFLSIRVADVPYVSEDERFEMHKISASSWQASINYGFKEDPDVPDALRQVAEAYPEIDLEPMRTSFYLSRQTVVAARRPAMARWRRALFAFMARNSTRSTRFFKIPPNRVVEMGMQVEL", "text": "FUNCTION: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family."}
{"protein": "MGLRYSREVKQRYGEKELEGRIPITLDMPQTLYGRYNCKSCWFANKGLIKCSNHYLCLKCLTAMLSRSDYCGICGGILPKKLVFETTPSAPPYTP", "text": "FUNCTION: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. SUBCELLULAR LOCATION: Virion Host cytoplasm, host perinuclear region Host cell membrane; Lipid-anchor; Cytoplasmic side Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. SIMILARITY: Belongs to the arenaviridae Z protein family."}
{"protein": "MSENSNHHCIIVGIAGASASGKSLIASTIYNELRAKVGDHQIGVITEDSYYKDQSHLTMEERVKTNYDHPNALDHRLLSEHLEQLMRGEAVNIPTYSYTEHTRTSDVEVMTPKKVIILEGILLLTDPRLRNLMHASVFMDTPLDICLLRRAKRDVEERGRSMESVFEQYQKTVRPMFMQFIDPSKQHADIIVPRGGKNRIAIDVLKAHISRLLKA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uridine kinase family."}
{"protein": "MSAQPVDLQIFGRSLRVNCPPEQRDALNQAAEDLNQRLQDLKERTRVTNTEQLVFIAALNISYELTQEKAKTRDYASSMEQRIRMLQQTIEQALLEQGRISEKPGSKFE", "text": "FUNCTION: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at mid-cell. SIMILARITY: Belongs to the ZapA family. Type 1 subfamily."}
{"protein": "MANILSLETLLISWLSSFILMFFILKWVSFYSKTKKNLPPSPQKLPIIGNFHQLGPNPHRSLQALSEKHGPIMLLHLGSVPMLVASNSEVAQEIMKTHDVSFASRPNSPILNILLYGCKDIAFAPSGEYWRQLKSIIVSNLLSSTQVKSFKNVREKEIGHMIGVIGESYGSSVDMSALLVSLAENVICTVALGRKFDGLKLTSLLRRYLSMFNLFSVGSYIPWLSWVDQLSGLTGRATKVVKEFDEFLEVIIEDHANAKINGGKDFIDMLLNAQQDQTTGFAFQRDTIKAVIFDIFGGGIDSVSTSIDWVMSELVKHPNVMKKLQKEVTEISQGRSMVAEEDLEKMQYLKAVIKESWRLHPPVPLLIPRKSTNDVKLMGYDIQAGTQVMVNVWQIGRDPTLWDEPNEFRPERFSKGSVNYSGLNFEWLPFGVGRRACPGTQFGAAVIELAIANIVYKFDLALPNGVKHEDLDMSEKYGITVHRKNPLLVTASPRF", "text": "FUNCTION: Probably involved in the biosynthesis of germacrene-derived sesquiterpene lactones. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSESKDTTEVNQEVNEKASSQSTKKQINFKRSHFIIILIVTILVTAMIAVFATIGISHWTSGLNSDQRDEMKKVEQVYQTLDDEYYKDTSSEELGTAAIDGMVKKLDDPYSDYMTKKETKSFNEDVSGDFVGIGAEMQKKGNQIQITSPMKQSPAEKAGIQPKDVVTKVNGKSIKGQPLEAIVKKVRGKQGTKVTLTIERGGQAHDITIKRDKIHVKSVEYQKHGDVGVFTINKFQNSTSGELKSAIIKAHKDGIRKIVLDLRNNPGGLLDEAVKMANIFIDKNETVVQLEKGKHKEAIKASNDASKEAKDMDVSILVNKGSASASEVFTGAMKDYNKAKVYGSKTFGKGIVQTTREFEDGSLLKFTNMKWLTPKSHYIHGKGITPDKKIEEPAYQSLNVIPSNKTYQLGDDDKNVKTMKVGLNVLGYHINNHSTEFDSELEDALKSFQKKNNLDVNGTFNKSTNEKFTQQLVEKANKEDTVLNELLKKLN", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S41A family."}
{"protein": "MQITVREALRDAMQEEMIRDDKVFVMGEEVAEYQGAYKVTQGLLEQFGPKRVIDTPITEYGFAGLAVGAAFAGLRPIVEFMTFNFAMQAMDHIVNSAAKTHYMSGGQVRCPIVFRGPNGAASRVAAQHSQNYAACYSYIPGLKVVAPYSAEDHKGLMITAIRDDNPVIFLENEILYGHSFDISENVEPIPFGKAKVLKEGDSVTIVTFSIQVKLALDAANILQSDNINCEVIDLRTIKPLDIDTIIESVKKTGRLVVIEEGWFFAGIGATIAAIVMKEAFDYLDAPVEIVSGKDVPLPYAVNLEKLALPSEYDVINAVKKVCYIK", "text": "FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity)."}
{"protein": "MTNTKSNVTKKSLHPRNKHTGNYDFPALIKACAELKPFVETNQYGNESINFSDPQAVKALNKALLAHFYNVPFWDIPQGYLCPPIPGRADYIHNIADLLAITNEGTIPTGKKVKGLDVGVGANCVYLIIGNREYQWSFVGSDIDPQSIKMASFIANNNPSLKGIECRLQKNEENIFKGIIKPTEFFDFTMCNPPFHASEAEATAGTERKQKNLAANKAKKGHAFQEMQNAKALNFGGQKAELWCEGGELAFILKMAQQSREFSLQVQWFTTLISKKENVAELYKELEKIGVKTIKTIEMAQGQKISRFVAWTYQANVNL", "text": "FUNCTION: Specifically methylates the adenine in position 1618 of 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. METTL16/RlmF family."}
{"protein": "MAWPLCTLLLLLATQAVALAWSPQEEDRIIEGGIYDADLNDERVQRALHFVISEYNKATEDEYYRRLLRVLRAREQIVGGVNYFFDIEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFQIYEVPWEDRMSLVNSRCQEA", "text": "FUNCTION: Thiol protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cystatin family."}
{"protein": "MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV", "text": "FUNCTION: Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21961565, PubMed:21502315, PubMed:23106432, PubMed:22123821, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716). SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase family."}
{"protein": "MKSALCSRFFILLPWILIVIIMLDVDPRRPAPQLTSRPYFSPHAVGCGGSRVPLRRSSPGRDAAEKRNESRPQLQPEPRLPTIYAITPTYSRPVQKAELTRLANTFRQVAQLHWILVEDRATRSELVSSFLARAGLPNTHLHVPTPRRYKRPWLPRATEQRNAGLAWLRQRHQHQSAQPGVLFFADDDNTYSLELFQEMRTTRKVSVWPVGLVGGRRYERPLVKNGKVVGWYTGWREDRPFAIDMAGFAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVEELEPKASNCTKVLVWHTRTEKVNLANEPKYHLDTVNIEV", "text": "FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 43 family."}
{"protein": "MDFPQHSQRVLEQLNQQRQLGLLCDCTFVVDGVDFKAHKAVLAACSEYFKMLFVDQKDVVHLDISNAAGLGQVLEFMYTAKLSLSPENVDDVLAVASFLQMQDIVTACHTLKSLAEPSSTTGESADASAVEGGDKRAKDEKAAATMLSRLDQARGSSSTGPGRELKEERGGQAESASSGAEQTEKADAPREPPPVELKPDPTSSMAAAEAEALSESSEQEMEVEPASKGEDGQEEEGAGPATVKEEGMHLDNGEPPEENEESAGTDSGQELGMEGQNLRSGTYGDRTESKAYGSIIHKCEDCGKEFTHTGNFKRHIRIHTGEKPFSCRECSKAFSDPAACKAHEKTHSPLKPYGCEECGKSYRLISLLNLHKKRHSGEARYRCGDCGKLFTTSGNLKRHQLVHSGQKPYQCDYCGRSFSDPTSKMRHLETHDTDKEHKCPHCDKKFNQVGNLKAHLKIHIADGPLKCRECGKQFTTSGNLKRHLRIHSGEKPYVCTHCQRQFADPGALQRHVRIHTGEKPCQCVICGKAFTQASSLIAHVRQHTGEKPYVCERCGKRFVQSSQLANHIRHHDNIRPHKCSVCSKAFVNVGDLSKHIIIHTGEKPYLCDKCGRGFNRVDNLRSHVKTVHQGKAGIKILEPEEGGEVSVVTVDDMVTLATEALAATAVTQLTVVPVGAAVTADETEVLKAEISKAVKQVQEEDPNTHILYACDSCGDKFLDANSLAQHVRIHTAQALVMFQTDADFYQQYGPGSTWPAGQMLQAGELVFRPRDGTEGQPTLAESPPTAPDCLPPAE", "text": "FUNCTION: Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation. Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment. Represses RB1 transcription; this repression can be blocked by interaction with ZBTB49 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MKVTQEKLPDSQVGLEIEIPATASKKVYENVVKKLTRTVNIPGFRRGKVPRAIVIQRLGQSYIKATAIEELIDDSIKAAVKQEELPIIGNFSLRSDMENLIQIFDPEAPLTIKVAADVFPEAEYEPESYKKITAQAEEIEYSADAVDQWLKGEQEKRATLVPVEDRPAALGDLAIVDYAAFQVAEDGQAGEAIAEVKGSDFEVTLEDGRFVAGIVDGIVGMAVDETKLIPVTFPEDYPLEAVAGEDVLFEIKLKEIKFRELPELDDDFAEDVSEFETMAELKADLEKQFQEQAKQRTDDNIKAAIKKKLGELFTGDLPETMIKQECDRLVAQTAMELERMGLDVSQLFRQGDDMLQTLKDNSRPEAIANLKTDLMIGAIAKEEKIQPTEAEVKERCDELRQEFKGEKIDESRLVNFVESSLTESKVLDLLKEWADVELLPEGSLSQTEEDTPDDDAEEEAIVDVEATSDEE", "text": "FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily."}
{"protein": "MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETEKSPEESAALVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVAPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPENVLLKELELVQNAFFTDPNDQSAWFYHRWLLGRAEPHDVLCCVHVSREEACLSVCFSRPLTVGSRMGTLLLMVDEAPLSVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTGSDSQKECVLLKDRPECWCRDSATDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFSTLKAVDPMRAAYLDDLRSKFLLENSVLKMEYADVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNALENVDGVANLPRLQELLLCNNRLQQSAAIQPLVSCPRLVLLNLQGNSLCQEEGIQERLAEMLPSVSSILT", "text": "FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. SIMILARITY: Belongs to the protein prenyltransferase subunit alpha family."}
{"protein": "MKVAVLGAAGGIGQALSLLLKTQLPAGTELALYDVAPVVPGVAVDLSHIPTDVKVEGFGKDDLAKALTGSDIVLIPAGVPRKPGMDRSDLFNINAGIVRNLVDSVADNCPEACLCIITNPVNTTVAIAAEALKAKGVYNKNKLFGVTTLDVIRAETFVGNLRDLNPANVHVPVIGGHSGTTILPLLSQVEGVEFTDEEVASLTTRIQNAGTEVVEAKAGGGSATLSMGQAAARFCLSLVSAMRGENVVEYTYVETNSDDAQFFSHPVRLGKNGVEEILPYGELSDFEQKAKESMLEGLRGDIKLGVEFVNN", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family."}
{"protein": "MASRGVNKVILVGNLGQDPEVRYMPNGNAVANITVATSESWKDQQGQQQERTEWHRVVLFGKLAEITGEYLRKGSQVYLEGKLQTRKWKDQSGQDRYSTEVVIDQSGSMQMLGSRNQGGQGAPMGGMPQNGGYQSAPQQAAPAQNQYAPAPQAAPAYQAPAPQPQSGYNQPPAQQSYGQQQAQPHVQPHAQPQQGGYAPKPAAPAYQAPAAPAQRPAPQPQQNFTPDLDDGWDDDIPF", "text": "FUNCTION: Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism."}
{"protein": "MGTIVLKMTAEQISVLQKDLASYATATKNPYAFFSAKVDGTSVIAYTSGKVTFQGAKPEILASRFGYQAEPKQSPDGQNLALIGSDEVGNGSYFGGLAVVASLVTPADHAFLKSLGVDDSKNLNDSKIRQIAPLLEEKIPHKALLLSPRKYNEVVGDGKAHNAVSVKVALHNQAIFLLLQSGAKPDKIVIDAFISEKNYQKYLKNERNHFEFPITLEEKAEGKYLAVAVSSIIARNLFLKNLDKLSQEVGYTLPSGAGAKSDQVAAKLLQAYGDQALQTTAKYHFANTKKAYQRLK", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family. RnhC subfamily."}
{"protein": "MATTKSFLILFFMILATTSSTCATLGEMVTVLSIDGGGIKGIIPAIILEFLEGQLQEVDNNKDARLADYFDVIGGTSTGGLLTAMITTPNENNRPFAAAKDIVPFYFEHGPHIFNYSGSIFGPRYDGKYLLQVLQEKLGETRVHQALTEVAISSFDIKTNKPVIFTKSNLAESPQLDAKMYDICYSTAAAPIYFPPHHFVTHTSNGATYEFNLVDGAVATVGDPALLSLSVATRLAQDDPAFSSIKSLDYKQMLLLSLGTGTNSEFDKTYTAEEAAKWGPLRWMLAIQQMTNAASSYMTDYYISTVFQARHSQNNYLRVQENALTGTTTEMDDASEANMELLVQVGETLLKKPVSKDSPETYEEALKRFAKLLSDRKKLRANKASH", "text": "FUNCTION: Probable lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the patatin family."}
{"protein": "MDGTSTDTSAQQAEGRTVDIAGIMRAIPHRYPFLLIDRVVELVPNVSAIGVKNVSVNESFFQGHFPGHPVMPGVLIIESMAQTAAVLVVETLGPEEAGKVVYFMSVEGAKFRRPVVPGDVLRIHVAKERNRGNVWKFNAVARVDGVAVAEATYAAMIMDKKAGEG", "text": "FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioester dehydratase family. FabZ subfamily."}
{"protein": "MPSRAGPKMDGSGGRVRLKAHYSGDIFITSVDAATTFEELCEEVRDMCGLHQHHPLTLKWVDSEGDPRTVSSQMELGEAFRLAGQHRDDGLILHVFPSTPEQPGMPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRRHMDSVMPSQEPPVADKSDDADLPSQETDGIAFISTRKQDSGQEDAEDLKPVIDGVDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNGQVYAMKVVKKELVHDDEDIDWVQTEKHVFEQASGNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNSDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEESV", "text": "FUNCTION: Calcium- and diacylglycerol-independent serine/threonine- protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5- MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF- kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Phosphorylates VAMP2 in vitro (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endosome Cell junction Membrane; Peripheral membrane protein Note=In the retina, localizes in the terminals of the rod bipolar cells (By similarity). Associated with endosomes (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (By similarity). Colocalizes with VAMP2 and WDFY2 in intracellular vesicles (By similarity). Transiently translocates to the membrane of CA1 hippocampal cells in response to the induction of long term potentiation (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily."}
{"protein": "MSLNKAVLEIRQRIKVKPSPTNEPAASWTGTDLVNGVQTKTLTVIFKSAGCRWGKAGGCTMCGYVYDCASEPPSLEDYMAQLEKAMRKAEKFPEFMVKIFTSGSFLDEQEVLPEARDAILKNLTEDPRVTKVLVETRPNYVTEENVQACLSILKNKPFELAFGLETSSDKIRRDSINKGFTFQDFVHAAETAKKYGVTVKVYLMLKPLFLSERQAMEDIIRSIDDAAPYADTISINLCNVQKGTLVEALWEKGQYRPPWLWSIIEILRQAKAAHPELPLMSDPVGAGSKRGPHNCKICSSEVADSLRTFSLTQNPADLSTADCECKELWKKVLEIEDFTYGTPILD", "text": "FUNCTION: Radical SAM enzyme involved in the synthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the cleavage of the C(epsilon)-N bond of the lysine moiety of q0kN15-tRNA, leading to the formation of archaeosine at position 15 in tRNAs. SIMILARITY: Belongs to the radical SAM superfamily. RaSEA family."}
{"protein": "MNDQLTEVYASIDALIDYALAHLDLDPRNADWTRNQIFALFRLDSYPGPKTTTSAASVSDVVQDIVGSRSQAPYGEKTPDPLLAAFRAAATTAGLFKPEEGPAYADTIMGILSANPADLDDRFLLVEHRDGGMAAMQWFYDYCVANNYVKRAQLDRNPRFDSHGLTVTINLAKPEFKNMKKAAAGNAVAGGYPKCTICHENEGFAGRDKRTLRTLPVTLGGESWFWQFSPYGYFDQHGICVNTDHTPMHVDRDTFGHLLDFVDRFPGYFLGCNAALPRIGGSVLAHDHYQGGGELLPMHKAATWAAFTLADYPDAVVEILDWPGTAVRVVSKSRQSIIDVSDIIREAWVGYDDAANGIASHDADGNRQSALSPSAIITERGYEMSLIFRNNAISDEYPEGIFHAHPEYWPVKQEPIGLIEAQGLFILPGRLVDQLGIVEEALAEGRDLPDEVSEFSLEWGELAETLAGNHDREAIRQAVHDELGSVCYRILGNTAVFKQKATTQTFLESLGFAAR", "text": "FUNCTION: Transfers the UMP unit from UDP-glucose (UDP-Glc) to Gal1P. Can also transfer the UMP unit to GlcNAc1P and GalNAc1P. Involved in the general galactose metabolism, and also involved in the lacto-N- biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 2 family."}
{"protein": "MPSITVRRLYQENQQKLNLTWVAGTGGSDNVIGNDDQRPTLALVGHLNFIHPNRVQVLGLAEVDYLNKLEQSAAKTALDQLFHKSMSVVMVANGQPVPRLLRDYCHSHNVPLMCSTLESPYLMDVLRIYLARALAVSTVLHGVFLDVFEIGVLIMGDSAMGKSELALELISRGHGMVADDAVELYRIGPDTLEGRCPPLLRDFLEVRGLGILNIRTIFGETAVRPKKVLKLIIHLVKANDQAMQALDRLNIQSETQDIIGVTVRKVVLPVAAGRNLAVLVEAAVRNYILQLRGIDSTREFIERHTNFLRDQENAPDID", "text": "FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). SIMILARITY: Belongs to the HPrK/P family."}
{"protein": "MKLSKIALAAALVFGINSVATAENETPAPKVSSTKGEIQLKGEIVNSACGLAASSSPVIVDFSEIPTSALANLQKAGNIKKDIELQDCDTTVAKTATVSYTPSVVNAVNKDLASFVSGNASGAGIGLMDAGSKAVKWNTATTPVQLINGVSKIPFVAYVQAESADAKVTPGEFQAVINFQVDYQ", "text": "FUNCTION: Major structural component of PMF fimbriae. SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the fimbrial protein family."}
{"protein": "MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFSMASALASFDILTAVHKHYSVEEWQAFINNSSADVLKHVMVSTGTSDADFEKTKQILDLNPALNFVCIDVANGYSEHFVQFVAKAREAWPTKTICAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGMIVSDGGCTTPGDVAKAFGGGADFVMLGGMLAGHEESGGRIVEENGEKFMLFYGMSSESAMKRHVGCVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRIFNNL", "text": "FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily."}
{"protein": "MDIWLLCWVTLCLLAAGHSEPGVSQTPRHKVTNMGQEVILRCDPSSGHMFVHWYRQNLRQEMKLLISFQYQNIAVDSGMPKERFTAERPNGTSSTLKIHPAEPRDSAVYLYSSG", "text": "FUNCTION: Probable non-functional open reading frame (ORF) of V region of the variable domain of T cell receptor (TR) beta chain (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive T cell receptor (TR) chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). SUBCELLULAR LOCATION: Cell membrane."}
{"protein": "MWRLVPPKLGRLSRSLKLAALGSLLVLMVLHSPSLLASWQRNELTDRRFLQLNKCPACFGTSWCRRFLNGQVVFEAWGRLRLLDFLNVKNVYFAQYGEPREGGRRRVVLKRLGSQRELAQLDQSICKRATGRPRCDLLQAMPRTEFARLNGDVRLLTPEAVEGWSDLVHCPSQRLLDRLVRRYAETKDSGSFLLRNLKDSERMQLLLTLAFNPEPLVLQSFPSDEGWPFAKYLGACGRMVAVNYVGEELWSYFNAPWEKRVDLAWQLMEIAEQLTNNDFEFALYLLDVSFDNFAVGPRDGKVIIVDAENVLVADKRLIRQNKPENWDVWYESKFDDCDKEACLSFSKEILCARATVDHNYYAVCQNLLSRHATWRGTSGGLLHDPPSEIAKDGRLEALLDECANPKKRYGRFQAAKELREYLAQLSNNVR", "text": "FUNCTION: May play a role in cardiomyocyte proliferation through paracrine signaling and activation of the PPI3K-AKT-CDK7 signaling cascade. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle. Golgi apparatus. Secreted. SIMILARITY: Belongs to the DIPK family."}
{"protein": "MRLHYRRRFNFLRRILFILCITSLYLSRDSLKLHAKNVLMDHNVAEYHGGMIDDIQILRCYHWYRQCSSLYAPKLHPSNTAKKIKDKNSILWTRVSKNITVETLYSLQSGPFYNSYLYVHLKDFQSNPKNTIKELAIARDSALIPLQVLRDINKLVKSSDSSVFHNHVYLREKPTSSWWKLLFGISVDTDNIAVFGEEWVYKGSGIWCKYILNDDDNDAPITNLEIYLGSSFIESRPSWKEVIHEFHRNNIPSLPISITRKLETKNHHHKFSNGLLGSLRTPSKDINIQVDADYKITSPHIQFSRGQRSFKILQITDFHFKCTDNSMTVINEIKTVNFIDRVLASENPDLVVITGDLLDSHNTIDYQTCIMKVVQPMISNKIPYAISLGVSDESNLATSAQIRDFIRNLPYTFNNVASEEGHMAIEVSFKKKLTKNTLLERDIDTEDETNPSEALFFVFDSFAPVNNFLQDYNDLIGKIDFGLAFQYFPLSEYRPHGLFPIIGQYNERSTLTVDTPRSRGQVSMTINGKHYKSFLDILSLWNIKGVSCGHEHNNDCCLQSKNEMWLCYGGSAGIGLPRIQGIYPTVRLFNLDDILDEITSWKRNSNLVDEVYDYQYIYKGKQ", "text": "FUNCTION: Involved in the activation of the plasma membrane proton- ATPase (PMA1) by glucose."}
{"protein": "MKYYLYLFLLFTFANLLYSCPTYPLPIKIDQNDPLLLKAYNDIDLLIQSKMKADGVKSFVATIVYMDKVVFSKAYGKLNYLDINSPNLTLDHNFRISSVTKVFTSLMMFKLRDQGIINSLDDDIRDYFPKFKIKSIFKKKEEKFITFRQLASHQSGLSRETPCHRNEFGTSNCTEKIILAKLSKQFLISKPTTLSHYSNLGYSLLGRTLGESLRMKRMKEQEPYEYWVTNNIFKPLGMNNTTFNYEDIINNTAPGLVNNNGKYSIPSMTKSGWNSPGGGVFSTARDMGKLLIHLLGMNNNSLDIRSPSYLKESTLNELFSPSNLLNDGSASYGMPFLHSYSTNNSLWILSKNGDLQGYVSNIAFVKPYKLGLFFSSLTSVSSSDVYTNAAIDILIPVYKKLLEQAAIDSVINSTTTSSNSTTTTTTTTTTTTTTTNNTMESIFISKIPHSLLIGIYTNDYGNKFLILNQTTYGDYLNRLLVSYNGASLVLNKFELDNEYPYIKRISFYNESIPTCRTIASGSNDELIYFTFKDINGTIIDFNNNNNNQNIDINNLFVYSVQIMGSLLFK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-lactamase family."}
{"protein": "MTRPVVASIDLLALRQNLQIVRRAAPGSRLWAVDKDNAYGHGVARVWSALSAADGFALLNLEEAILLREQGWKGPILLLEGFFHADELAVLDQYRLPTSVHSNWQIKALQQAKLRAPLDIYLKVNSGMNRLGFMPERVHTVWQQLRAISNVGEMTLMSHFAEAENPQGIVEPMRRIEQAAEGLDCPRSLANSAATLWHPEAHFDWVRPGIVLYGASPSGQWQDIANTGLKPVMTLRSEIIGVQNLRPGEAIGYGGLYRTTQEQRIGIVACGYADGYPRVAPSGTPVLVDGVRTTTVGRVSMDMLAVDLTPCPQAGIGAPVELWGKEIKIDDVAASSGTVGYELMCALAPRVPVVTL", "text": "FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. SIMILARITY: Belongs to the alanine racemase family."}
{"protein": "MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNSCAFLESSAKSKINVNEIFYDLVRQINRKTPVTGKPRKKSTCQLL", "text": "FUNCTION: Probable GTP-binding protein that possesses GTPase activity. May play a role in endothelial cell polarity and endothelial barrier function (By similarity). SUBCELLULAR LOCATION: Cell membrane Cytoplasm, cytosol Cell junction Note=May shuttle between plasma membrane and cytosol. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
{"protein": "MSLGLLGNKIGMTQIFDESGNIIPVTILKVGPCVITQVKTDLNDGYNAIQIGYGTVSNKSLTQPELGHLQKSNIQPLKYLKEFRVNNPEEFKVGQVVNVESLSTGQFIDVTGKSSGKGFSGLQKRHNFTRGPMTHGSKNHRAPGSIGMGTTPGRVLPGKKMAGQLGNKVTKTKKLKIIQVNGNENILVVKGSVPGKPGNLVTIHVSN", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL3 family."}
{"protein": "MHLKMLKSKIHRATVTGANLDYEGSITIDGELLEAAGILVFEQVQVANLNNGVRFETYVIPGARGSGVINLNGAAARLAVPGDQVIIMAYSWCSESEVREWAPVVVLVDARNRVAKVLAAEGLPPLNMTGPEK", "text": "FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanD family."}
{"protein": "MSKQQIGVIGLAVMGKNLALNIESRGFSVSVYNRSSSKTEEFLQEAKGKNVVGTYSIEEFVQSLETPRKILLMVKAGTATDATIQSLLPHLEKDDILIDGGNTYYKDTQRRNKELAESGIHFIGTGVSGGEEGALKGPSIMPGGQKEAHELVKPILEAISAKVDGEPCTTYIGPDGAGHYVKMVHNGIEYGDMQLISESYFILKQVLGLSADELHEVFAEWNKGELDSYLIEITADIFTKKDEETGKPLVDVILDKAGQKGTGKWTSQSALDLGVPLPIITESVFARFISAMKEERVKASGLLSGPEVKPVTENKEELIEAVRKALFMSKICSYAQGFAQMKAASEEYNWDLKYGEIAMIFRGGCIIRAAFLQKIKEAYDREPELDNLLLDSYFKNIVESYQGALRQVISLAVAQGVPVPSFSSALAYYDSYRTAVLPANLIQAQRDYFGAHTYERTDKEGIFHTEWMK", "text": "FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate. SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family."}
{"protein": "MSAEGQEELLDYSDSEEIAVPSNAPEAGADGADKDADKKGSYVGIHATGFRDFLLKPELLRAIGDCGFEHPSEVQQVCIPQSILGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEITTLVICHTRELAYQIRNEYARFSKYMPDVKTEVFYGGIPIAKDIEKLKNKDTCPHIVVATPGRLHALVEEKAIRLNNVKSFVIDECDKVLEAIDMRRDVQDIFRNTPHQKQVMMFSATLSQEIRPVCKKFMQNPLEIYVDDEAKLTLHGLQQYYLKLDEKEKNRKLADLLDSLEFNQVIIFVKSTSRANELNKLLVASNFPSIAVHSAMPQEERIARYKSFKEFNKRICVSTDVFGRGIDIERINLAINYDLPNEADQYLHRVGRAGRFGTKGLAISFVGSKEDEEVLEKIQSRFDVKITEFPEEGVDSSTYMNT", "text": "FUNCTION: ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily."}
{"protein": "MSDQIKFIMDSLNKEPFRKNYNLITFDSLEPMQLLQVLSDVLAEIDPKQLVDIREEMPEQTAKRMLSLLGILKYKPSGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRTNELKKRAYLARFLIKLEVPSEFLQDETVADTNKQYEELMEAFKTLHKEYEQLKISGFSTAEIRKDISAMEEEKDQLIKRVEHLKKRVETAQNHQWMLKIARQLRVEKEREEYLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRQAAADAKPESLMKRLEEEIKFNLYMVTEKFPKELENKKKELHFLQKVVSEPAMGHSDLLELESKINEINTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQEAKEKLASLEREASVKRNQTREFDGTEVLKGDEFKRYVNKLRSKSTVFKKKHQIIAELKAEFGLLQRTEELLKQRHENIQQQLQTMEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLYSLVSEKKSALASVIKELRQLRQKYQELTQECDEKKSQYDSCAAGLESNRSKLEQEVRRLREECLQEESRYHYTNCMIKNLEVQLRRATDEMKAYISSDQQEKRKAIREQYTKNTAEQENLGKKLREKQKVIRESHGPNMKQAKMWRDLEQLMECKKQCFLKQQSQTSIGQVIQEGGEDRLIL", "text": "FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region (PubMed:23990561). Required for ciliogenesis (PubMed:27666822, PubMed:23990561). Required for proper regulation of SHH signaling (PubMed:27666822). Plays an important role during spermatogenesis by modulating the assembly and elongation of the sperm flagella (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm. SIMILARITY: Belongs to the IFT81 family."}
{"protein": "GLTDQKSAPPGL", "text": "FUNCTION: Serine protease. SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITWDQAFDVMEDKFKTALKEKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRITNRRLSNQNVTVAVLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFFSKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEYTLEKTAEMTGVPKDQLEQLAQLYADPNKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNEKHRDICEKKWNIPSGTIPAKIGLHAVAQDRALKDGKLNVYWTMCTNNMQAGPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEELLAKKPELRGKTLYEVLYATPEVSKFPVSELAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPVVNGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEKV", "text": "FUNCTION: Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily."}
{"protein": "MGGWSSPSHWLIILLIVVLLFGAKKIPELAKGLGKGIKTFKDEMNNDDEVAKNTQKIEENKNTTNNTNADASIDETKKA", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatA/E family."}
{"protein": "AKVANSTDSSSLAEVIDRILDKGIVIDAWVKVSLVGIELLAIEARVVVASVETYLKYAEAIGLTIP", "text": "FUNCTION: Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell. SUBCELLULAR LOCATION: Gas vesicle shell. SIMILARITY: Belongs to the gas vesicle protein type A family."}
{"protein": "MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVMVGGEVTTSAWVDIEELTRKTVREIGYTHSDMGFDADSCAVLNAIGKQSPDINQGVDRADPKEQGAGDQGLMFGYASNETDVLMPAPITYAHALVKRQSEVRKDNTLPWLRPDAKSQVTFAYEDNKIVGIDAVVLSTQHCDSVSQSDLIEGVMETIIKPVLPAQWLNKETKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSISVETFGTGKVSEEVLIGLVRQHFDLRPYGLTEMLDLARPIYKATAAYGHFGRNEFPWERTDKAEALRADAKL", "text": "FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AdoMet synthase family."}
{"protein": "MPLIMEDGINVDDLFGEPGSLELGLSPSTPSPRGLAQRLDEMRLIGCCQKIAWSKLGCIAYISQDGLRVNVRHLQCRPSDGKWVLSEETPLLPVTDAHGGHTLVHLCWNEPGAELAVADSSGRVSIYSISIALNSIAGHRQAAFDPDDDGAQIVGMMWLNTQRTVHSFYQAAKVQGRWAYSPFRRRPIGPFHPVNKAGLVCVTRSGIIRLLYQNPDSRWAEISAELKNTGYSDRLLTHAALVSTQGGILVATHSACQKICLYRVHIAWTPTQYDPGQQKPPAPWPVPSFRFLHCKVESQCDVPGTNRNAGDNAQGLPSFTNSFYCLTGLDIVLPALDNPAGSTANPWVVAIYSAPLHVTQDHPQQQGPASVIVRWQLDTGPLTLHPKFDDVPSKKNNAQVKPKLELRRLDDVYSDKYAISIDQIEYGNVLAITYDDGSVVFYDPKTMAVFNGVDDANTVTSLAQAGFHHPPEPSGLHISFSPNACAAVMLDGEGQTHLRLTEHSYGAEGGLHDENKYSAAIAALTLAFCRGCGSDVNTDDILLILVRQLTPEAQATFINEAYRALPINCNFTVEQDKLMNHPYIPRCLSIQAALGFKNKYTPRSFASSIPWAVLQLRHASVLYAFFFQYNKGGATEPHDPDVLRMVLGNTKWALDFSFYVLNELFDLADDFESLSGDQEAFTQKLKSTSSLPLIILLSSMSRAFLRFICRGLRGIYAGYATAAPLSGDARVYYAEIYQTLESAPIRIDAYEKFLAGVDSAVRHAYHGAGFGDAERPGPEKELLVNARVPPVLVPAVSTILRQTVPALKTEIDRITIYMGDYSWLGLSNDRRTEMYRRNRDVDIIKKIPCRPAASALPETNANANANQNGKSSTQVQQRRRRCVRCCEVSSDTHPPRSLLSFRMIAKLGLLRACVCGGMWTLEPSVYSSAQSSGAPVGQATGRTPALMAAGLAGSS", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 16 family."}
{"protein": "MKSLGRHIIAEFYDCDKEMLDNIDAIEFHMKQAAYETGATIVNSSFHRFLPYGVSGVVVISESHLTIHTWPEYGYAAVDLFTCGDHVDPWKAFSYLKKIFKSQRAHVVEHLRGKYDEVGIPENAPHKAVEAEMAEIF", "text": "FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily."}
{"protein": "MTGCGSCGKIIKNIEKKYYNQLKEKDIVLVGGAVNLDDEEEVKKIMEIRKNSKVLIAVGSCAVSGGFQRMLIGLENGFPQRFVRIGDVVKVDYAIIGCPPDEEEVERIVKAVIEKDKEIVDSYLILKPYEVIAGKPIIDAYMKVNDVLLTSNKELCLGCDDKPINDEFCTGCGTCVAKCPANALTIDEKPKVNISKCIKCGTCFFNCIRVKEALLP", "text": "SIMILARITY: Belongs to the FrhG family."}
{"protein": "MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLFEQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTFIYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRITGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRLGYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLLNQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQSLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT", "text": "FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2- acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG). SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane Secreted Note=May associate with lipid draft. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane Secreted Note=May associate with lipid draft. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MAISIKSPKEIKALRKAGELTAQALALLEREVRPGVSLLELDKMAEDFIKSSHARPAFKGLYGFPNSVCMSLNEVVIHGIPTDYVLQEGDIIGLDLGVEVDGYYGDSALTLPIGAISPQDEKLLACSKESLMHAISSIRVGMHFKELSQILEGAITERGFVPLKGFCGHGIGKKPHEEPEIPNYLEKGVKANSGPKIKEGMVFCLEPMVCQKQGEPKILADKWSVVSVDGLNTSHHEHTIAIVGNKAVILTER", "text": "FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily."}
{"protein": "MFPMVTEFMNYGQQTVRAARYIGQGFMITLSHANRLPVTIQYPYEKLITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLETDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPMSIIDDYTIRTILNLPEIKN", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family."}
{"protein": "MSNTAYIDTCYGPVADDVIQRAANIRLLICDVDGVMSDGLIYMGNQGEELKAFNVRDGYGIRCLITSDIDVAIITGRRAKLLEDRANTLGITHLYQGQSDKLVAYHELLATLQCQPEQVAYIGDDLIDWPVMAQVGLSVAVADAHPLLLPKAHYVTRIKGGRGAVREVCDLILLAQDKLEGATGLSI", "text": "FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8- phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. SIMILARITY: Belongs to the KdsC family."}
{"protein": "MATIPIRLQALATDQTVLKLPHPYKTEFAVRKASKASTKLPVYNLVPKPFPTRPLPFELHNDHLVFTDAIHLKSSELPPDSNNGAWARARRAPCVTLYWDGVEVPTLKQAWLVVYAFFTMRPGMDSFRLELDGNSAANLARQIKDVLLGIDHPIKARQQQEPCAKTKENTLLILRSTFWQGAGCPFGPRPVWCPQESPSSLLPSTCLSSFPLAPFHRTSTISLAGDPEDFDRCQQSWHPIRPAKPAPGSIIYSRWIPYLGEMFSMVALDPEDSEHVRLFHEWQSDPRVLQGWTETKTLDQHRRYLEALHKDPHQLTVLAKWDDSPFAYFELYWAKENRLGGYIDAGDFDRGRHSFVGDVRFRGPLRVSAWWSSLMHYLFLDDPRTMHIVGEPRDTHSTVLMYDFIHGFGLDRFIDLPSKRSAFMRCSRDRFFQSFPLEDSEKVIGGTSIRVVQKL", "text": "FUNCTION: Putative O-acetyltransferase; part of the satratoxin SC2 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings (PubMed:25015739). Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton (PubMed:25015739). SC1 encodes 10 proteins, SAT1 to SAT10 (PubMed:25015739). The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding (PubMed:25015739). The putative short-chain reductase SAT3 may assist the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity (PubMed:25015739). The probable transcription factor SAT9 may regulate the expression of the SC1 cluster (PubMed:25015739). SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases (PubMed:25015739). The SC2 cluster may be regulated by the transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites (PubMed:25015739). The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression (PubMed:25015739). SIMILARITY: Belongs to the lysine N-acyltransferase MbtK family."}
{"protein": "MFDIGVNLTSTQFAKDRDKVVKRAREAGISGMLITGTNALESQQALSLARQHANYCWSTAGVHPHHASEWSAETAATLRRLAESPLVVAIGECGLDFNRNFSQPEQQVYAFNAQLALAAELSLPVFLHCREAHERFITILKPWLPSLKAAVLHCFTGARAELESCLAEGLSIGITGWICDERRGQELRELVPLIPADRLLLETDAPWLLPRDMRPRPPSRRNEPCFLPHIVQQVALLRGDDVDELAAQTALNARALFGL", "text": "FUNCTION: 3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family. TatD subfamily."}
{"protein": "MTRYIFVTGGVVSSLGKGIASASLAAILEARGLKVTMLKLDPYINVDPGTMSPFQHGEVFVTHDGAETDLDLGHYERFIRTTMTQNNNFTTGRIYEHVLRKERRGDYLGATIQVIPHITDEIKRRIIKGAGDADVALVEIGGTVGDIESQPFLEAIRQLRVEVGSKRAMLMHLTLVPYIATAGETKTKPTQHSVKELRSIGLQPDVLICRSDHPVDASSRRKIALFTNVEERAVISLEDVDTIYKIPGVLHAQGLDDFVVERFGLQCNGADLSEWDKVVDAKLNPEHEVTIAMVGKYMELLDAYKSLIEAMSHAGITNRTKVNLRYIDSEDIENQGTSLLEGADAILVPGGFGLRGVEGKITAVQYARENKVPYLGICLGMQVAVIEFARNVMGWKDANSTEFDRNSGHPVVGLITEWADATGAVETRDEASDLGGTMRLGAQDCQLAAGSKVHDCYGKDVITERHRHRYEVNNNLLPQLVEAGLVVSGRSEDGALVEVVESKDHPWFVACQFHPEFTSTPRDGHPLFSGFVKAALAQKNKA", "text": "FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. SIMILARITY: Belongs to the CTP synthase family."}
{"protein": "QSSTVTPNVVVAADGSGDYKTVSEAVAAAPEDSKTRYVIRIKAGVYRENVDVPKKKKNIMFLGDGRTSTIITASKNVQDGSTTFNSATVAAVGAGFLARDITFQNTAGAAKHQAVALRVGSDLSAFYRCDILAYQDSLYVHSNRQFFINCFIAGTVDFIFGNAAVVLQDCDIHARRPGSGQKNMVTAQGRTDPNQNTGIVIQKSRIGATSDLQPVQSSFPTYLGRPWKEYSRTVVMQSSITNVINPAGWFPWDGNFALDTLYYGEYQNTGAGAATSGRVTWKGFKVITSSTEAQGFTPGSFIAGGSWLKATTFPFSLGL", "text": "FUNCTION: Catalyzes the deesterification of methyl-esterified D- galactosiduronic acid units in pectic compounds. It participates in modulating cell wall during fruit ripening, cell wall extension during pollen germination, and in defense mechanisms against pathogens. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the pectinesterase family."}
{"protein": "MAVAMDNAILENILRQVRPLIGQGKVADYIPALATVDGSRLGIAICTVDGQLFQAGDAQERFSIQSISKVLSLVVAMRHYSEEEIWQRVGKDPSGSPFNSLVQLEMEQGIPRNPFINAGALVVCDMLQGRLSAPRQRMLEVVRGLSGVSDISYDTVVARSEFEHSARNAAIAWLMKSFGNFHHDVTTVLQNYFHYCALKMSCVELARTFVFLANQGKAIHIDEPVVTPMQARQINALMATSGMYQNAGEFAWRVGLPAKSGVGGGIVAIVPHEMAIAVWSPELDDAGNSLAGIAVLEQLTKQLGRSVY", "text": "SIMILARITY: Belongs to the glutaminase family."}
{"protein": "MERWSINDSAKIYNLNNWGADLFSINKKGNVCVHPSSNSKHSIDLRALVDDLIKRKIKPPILLRFMDVLQGRIASINRVFKNAIQENNYPAKYQTFYPIKVNQQRQVVEAIANFGKRYNIGLEVGSKPELVAGISFATGNNLPIICNGYKDTEYIEMVLSATKIGYDITLVVEKLFELEKIIELVKKTGVQPKLGIRVKLSSKGIGKWATSGGEDAKFGLRMSEIIAAIEMLEKHDLIKCVKLLHFHIGSQITKIDKIKTALIEGARIYAEMRKLGVGIEYLDIGGGLGVDYDGSKSSNFSSVNYSIEEYANDVIYQIKNICEDAGVECPNIISESGRATVAHYSVLVTNVLNTNTQNIMPDFEATLNEAEKLAPTVKKLEDIYKSIDRYSLREDYHDTLQLIQEAVSLFNLGYLTLNDRAMAEWLYGKIIRKINSIVEKIKPIPEELQNFQLSLRQTYFANFSLFQSVPDSWAIDQLFPIVPIQRLNQKPDVIASIADITCDSDGEITSFVGENGRTKFLPLHKIRKDEAYYIGFFLIGAYQEILGDMHNLFGDTNAVHITFNKKTGYIIDTVINGDATWESLKYVQYKGPEILKRVRDNLEKDVALRKISIEESSHFLELLDRTLLGYTYLGE", "text": "FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily."}
{"protein": "MGSQHLPLAALYLLELLVTSCLGGLKVEVQGLTMRLSGSGSRCQGRLEVSNGTEWYAVHSQSWGQLSLYQVAPRQFLKLCQELQCRDPLLLSSSRYFKEVQFQKLIICHGQLGSFSNCSLNRGRQVDSLALICLEPPRTTAPPTTSPPTTTPEPTAPPRFQLVAEPGGLRCAGVVEFYSGGLGGTIGIEPQNDIKDLGQLICAALQCGSFLKPLPETEEAQTQKPEGQRPLPIRWEIQNPKCTSLEQCFRKVQPWVGGQALGLICSDFQPKVQSRLVGGSDVCEGSVEVRSGKGQKWDTLCDDSWAKGTARWEEVCREQQCGNVSSYRGLDPSEKTLGGFYCPPGILSRCHKLEEKKSHCKRVFVTCQNSSRAGLGAGAVMSIILALLLLAVLLVVCGPLAYKKVVKKFRQKKQRQWIGPTGMNQNMSFHRNHTVTVRSQVENATASHVENEYSQPPRNSQISAYPALEGALHRISTQPDNSSDSDYELHGAQRL", "text": "FUNCTION: May act as a receptor in regulating T-cell proliferation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MGKVGNIEHIEERAETELMPPSMYKVILNNDDYTPMDFVIEVLQLFFNKNEQEATDIMLAIHHQGKGICGVFPFGIAETKVAQVNQFARQNQHPLLCSLEKA", "text": "FUNCTION: Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation. SIMILARITY: Belongs to the ClpS family."}
{"protein": "MMVIRPVERRDVSALMQLASKTGGGLTSLPADEATLTSRIERALKTWRGELPKSEQGYVFVLEDSDTGSVAGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNEKVVAEMRGVIDEHGYSPFWESLGERFFSMEFSRADYLCGTGQKAFIAELMPKHPIYTHFLSEEAQAVIGEVHPQTAPARTVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLLDVVEGQPAPGEFPACLVANENYHHFRAMLIRTDPDTQRLVLTAAQLDALKCHAGDRVRLVRLCAEEKTA", "text": "FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. SIMILARITY: Belongs to the arginine N-succinyltransferase family."}
{"protein": "MGLLFVELLPRHGDGGGPASAVLKCRRCRVDAASADAILSRDFRGRFGRAYLFDHVVNISLGPNEDRYLMTGLHTVKDIYCSCCQQILGWRYEKAYEESEKYKEGKFILEKARMWKEAR", "text": "SIMILARITY: Belongs to the yippee family."}
{"protein": "MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITGAIAGGVAAGAALLFAVPAIALAWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQKEEMFRQDFNYPTHHPAVSGWIIGDSTSQIENEYPSGPR", "text": "FUNCTION: Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1- BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen- associated molecular pattern (PAMP)-triggered immunity (PTI) via its interactions with FLS2 and EFR, and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR- independent cell-death pathway (PubMed:17583510, PubMed:17600708, PubMed:18667726, PubMed:18694562, PubMed:19124768, PubMed:20018402, PubMed:20404519, PubMed:21693696). Phosphorylates BIR2 and thus promotes interaction with BIR2 (PubMed:24388849, PubMed:24556575). This interaction prevents interaction with FLS2 in the absence of pathogen- associated molecular patterns (PAMP) (PubMed:24388849, PubMed:24556575). Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity (PubMed:27251392). Required for PSK promotion of seedling growth and protoplast expansion (PubMed:26071421). CNGC17 and AHAs form a functional cation- translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421). Required during SCOOP small peptides (e.g. RGF1, SCOOP10 and SCOOP12) perception and signaling; associates with MIK2 as a coreceptor upon MIK2 perception of SCOOP peptides, and relays the signaling through the activation of receptor- like cytosolic kinases (RLCKs) BIK1 and PBL1 (Probable) (PubMed:30715439, PubMed:34535661). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endosome membrane; Single- pass type I membrane protein Note=Endocytosis enhanced upon interaction with MSBP1. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MATAWGLRWGLSRTGTLLLAPPARCARRALHRQVDGTTFQSIYSLDKLYPESKGADTAWKVPEHAKQASSYIPLDRLSISYCRSSGPGGQNVNKVNSKAEVRFHLASADWIEEPVRQKIALTHKNKINKAGELVLTSESSRYQFRNLAECLQKIRDMIAEASQVPKEPSKEDARLQRLRIEKMNRERLRQKRLNSALKTSRRMTMD", "text": "FUNCTION: Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit (PubMed:20869366). Acts as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion, possibly in case of abortive elongation. May be involved in the hydrolysis of peptidyl-tRNAs that have been prematurely terminated and thus in the recycling of stalled mitochondrial ribosomes (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family. Mitochondrion-specific ribosomal protein mL62 subfamily."}
{"protein": "MESLSRAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVLEEETRRSQQAARDKQSPNQANGCSDHRPIDILEMLSRAKDEYERNQMGDSNISSPGLQPSTQISNLGSTETLEETPSGLQDKSALSGHKHLTVEELFGTSLPKEQPTVVGLESEEVEKLPGDASQKEPSSFLPFSFEPSGGGPQSENMGIRPAAHHSVQPEVTTPVLITPASITQSSEKQAPSYAIPLHPVLSPTLPAEASTAQAPPSLPRSTTMMQAVKTTPRQRSPLSSQPVPELSQASLAASQSPFRAPLNVTNTASTSLPSVDLLQKLRLTQQHDQIQTQSLGKGAVAPSFSPAAGQLATPESFIEPPPKTAAARASASLSNMVLAPLQSMQQNQDPEVFAQPKVLSSAIPVAGPALVTATTSAVSSVLLSPSVFQQTVTRSSDLERKASSPSPLTVGTSENQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHNL", "text": "FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). Essential for embryonic development (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body Nucleus Note=Co-localizes with NANOS3 in the processing bodies (By similarity). Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4 (By similarity). SIMILARITY: Belongs to the DCP1 family."}
{"protein": "MMNRLLVFLMLGAAFMLVVSAIDQDANEDINKRGIPCLCDSDGPSVRGNTLSGIIWLAGCPSGWHNCKKHGPTIGWCCKQ", "text": "FUNCTION: Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation during signal transduction (PubMed:19609479). Has a strong effect on crustaceans and insects and a weaker effect on mammals (By similarity). It strongly inhibits D.melanogaster sodium channel (DmNav1) (PubMed:19609479). It strongly affects the heart sodium channels (Nav1.5/SCN5A) and weakly inhibits the brain sodium channel Nav1.2/SCN2A (By similarity). In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours (PubMed:22048953). Its effect on zebrafish (D.rerio) larvae is much faster, since it induces paralysis or strong convulsion and impaired swimming, within 10 minutes (PubMed:22048953). SUBCELLULAR LOCATION: Secreted Nematocyst Note=In nematocyst, is associated with the tubule prior to discharge. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type I subfamily."}
{"protein": "MGTQKALNEQSLTSETDTGRREEKLFLIKGGIFLGMVATAGMFAGFGTTLSLAKKRSPNWFNKGVAATATLPESGSSLALRALGWGSLYAWCGVGLISFAVWKALGVHSLKDFREKMQTIFPTVSKDPEHQPTSEFSFEDLLKSK", "text": "FUNCTION: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC3. Participates in the incorporation of the c-ring into vestigial complexes. Additionally influences the incorporation of subunits MT-ATP6, MT-ATP8, ATP5MJ, and ATP5MK in the ATP synthase. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM242 family."}
{"protein": "MNFSNDSEEKVFNEIFDQLPTLIKDKCSDYDELYGYKLNYNDSKEKLVEQYYDEDIAKALIFKICKAYQFDKTKIITSIVDILNWRKSFNPLSAAYKETHNEALQTVGLLTSYPDDEPNKRVVTWNLYGQIVKKKELFKDSSKFIRYRIGLMERGLRLLDFNNDANNYMTQVHDYKGVSMFRLDSEIKACTKQVIAIFQKYYPELLYAKYFVNVPSILSWMYDLMKSFIDEQTRKKFVVLNDGNKLGNYLKSCPSENYGGTDKKNNLQKQDVDTPRPTPYALYILESQANEDID", "text": "FUNCTION: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SFH5 family."}
{"protein": "MASNFTQFVLVNDGGTGNVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQNRKYTIKVEVPKVATQTVGGVELPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY", "text": "FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein. FUNCTION: Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. SUBCELLULAR LOCATION: Virion Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. SIMILARITY: Belongs to the Leviviricetes capsid protein family."}
{"protein": "MAFQQGEAAPVSTQSSLSFTQGFLLGQLSVVLLIGAFIKFFIFGEAPPPPSRGLRASTHRRSNSIFSQDAPPPRSLREKPSTSNVLRPVPSSATNTRSILRKTYYSAIPPNPSSKHRIHHSSHQPESLDWFNVLIAQTIAQYRQTAYLLKDSPTSSILHSLTAALNNPEKKPSFIDKITVTDISLGEEFPIFSNCRIIAVDDPMSDGGRLQALLDVDMSDDNLSIAVETSLVLNYPKPCSAILPVALSISVVRFSGTLCISLVPASTPPLHTPSPMPSPPTAGAQPAAGAQPTDGGDIPPKSSSKSNIAFSFLPDYRLDLSVRSLIGSRSRLQDVPKVAQLVEARVHAWFEERVVEPRVQVVGLPDLWPRMGRTGVRTGDESETGSNTASRPAMSVDMSSPGHLQGDGGNHEEELRFRGLGPRPPLPFDAVSRTSSYQVETGAPRSPSLTRERSLGDDFHMPGSMPEAPGAQ", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta- barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MMM1 family."}
{"protein": "MQAIILGSAAGGGVPQWNCRCPICAMAWAGDRRVLPRTQSSLAVSPDGERWLLVNASPDIRQQLLATPALHPRHGLRHTPIEAVLLTNGDVDHVAGLLTLRESQPFRLHATRNILESVSANRVFDVLAADLVARREVGLNETFEPVSGLAVTLFPVPGKVPLWLEEGTPEIGAETETTVGAMIEAGGRRLAYVPGCARVTEDLRHRLAGVDALLFDGTVLADDDMIRAGVGTKTGWRMGHVPMTGQGGSIAALAEVPIGRRIFVHINNTNPVLVENSEARRAVEAAGWDVGHDGMALRL", "text": "FUNCTION: May be involved in the transport of PQQ or its precursor to the periplasm. SIMILARITY: Belongs to the PqqB family."}
{"protein": "MNANTVLPPGLLLVLSAPSGAGKTTLAHRLLKETPDAVFSISVTTRRPRGKEREGVDYNFVDVATFQSKIERGEFVEWAEVYGHFYGSPQSVVDEARARKSAAIFDIDVQGGQAIKRKHPDAVTIFVLPPSMEELERRLRDRQTDSDETIRRRMLAARSEIERGIASYDYVVVNDDFERAFSDLRSVVVAERCRRERVDVSKLGLGIGG", "text": "FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family."}
{"protein": "MAKGKDVRIRVILQCVSCVRKGANEESAGISRYSTQKNRHNTPGQLELRKFCRYCRKHTIHAEIKK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MNKSFLPQFTSDQAVTFLKEWNFSLGVILLFITIILQFGYTSRSMFVYLIKMIILWLMWPLTITLTIFNCFYALNNAFLAFSIVFTIISIVIWILYFVNSIRLFIRTGSWWSFNPETNNLMCIDMKGKMFVRPVIEDYHTLTATVIRGHLYIQGVKLGTGYTLSDLPVYVTVAKVQVLCTYKRAFLDKLDVNSGFAVFVKSKVGNYRLPSSKPSGMDTALLRA", "text": "FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Host Golgi apparatus membrane; Multi-pass membrane protein Note=Largely embedded in the lipid bilayer. SIMILARITY: Belongs to the betacoronaviruses M protein family."}
{"protein": "MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN", "text": "FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity, and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. FUNCTION: The uncleaved form of allele alpha-2 (2-2), known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MGKYNFTALRVRQTALRQHAAGKIRAPPKWLDVVADIPPAQVLVRNQAPQHQLVRQRVKTLPGTSKPQVVFEVQEKRIKPKKASRMFLPTEIKYEEDQLRQEFFRDHPWELARPRVLVESTGKDSEHYDWSRLQQPGKRLDGESVVQRQLWLLNNVPDMTKSAAYDIARREFYRLRLQEDIERRVAAEEAEATGATFGPSLLEVGMELENQEYERWKAWAKMEAQLLDQKTAAFTGAPEIAAADDAVEELEEKVPVPV", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS23 family."}
{"protein": "MADFKPRIEISFLETFICSAFAACFAELCTIPLDTAKVRLQLQRKIPTGDGENLPKYRGSIGTLATIAREEGISGLWKGVIAGLHRQCIYGGLRIGLYEPVKTLLVGSDFIGDIPLYQKILAALLTGAIAIIVANPTDLVKVRLQSEGKLPAGVPRRYAGAVDAYFTIVKLEGVSALWTGLGPNIARNAIVNAAELASYDQIKETIMKIPFFRDSVLTHLLAGLAAGFFAVCIGSPIDVVKSRMMGDSTYRNTVDCFIKTMKTEGIMAFYKGFLPNFTRLGTWNAIMFLTLEQVKKVFLREVLYD", "text": "FUNCTION: PUMPS are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. This leads to a decrease in the efficiency of oxidative phosphorylation and an increase in heat production. May be involved in protecting plant cells against oxidative stress damage (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MRKKRLLSRISFSSLFLLCGTLLSACTGIQADLRNLIKETTGKDIDLSKAIKTKEGKKNIIASLKKSYEVNPRDTTKLLLDAWKQSFEEGKLGIPDFDLTM", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the MG439/MG440 family."}
{"protein": "MTLLLKNTLYLALIISVISSFPTSLFAQNCGCAPNLCCSNFGFCGTGTPYCGVGNCQSGPCEGGTPTTPTTPTTPTTPGTGGGGSSVSDIVSQAFFDGIIGQAAASCPGKNFYTRAAFLSAVDPKFGNEGSSDDNKREIAAFFAHISHETTNLCHIEERDGDVGDAYCDQDKAAQYPCAAGKKYYGRGPLQLSWNYNYALAGQAIGFDGLGNPEKVATDVNTSFKAAMWFWMTNVHSVMNQGFGATTKAINGALECNGQNQDQANDRIQFYKKYCADFGVAPGDNLTC", "text": "FUNCTION: Defense against chitin-containing fungal pathogens. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily."}
{"protein": "MKQAFNQRISSALNQRKQAGLNRSRRVVSQGNQATLVVDGKSYLNFSGNDYLGLASSKELMEAWQEGLSLYGSGSGASPLVTGYSKPHANLESQLAEWLGLDCAILFNSGFSANQAVLFSLLEKGDTLLQDKLNHASLMEAGMLSPAVMKRFKHNDVDHLKSLLKRSSDEPTLVVTEGVFSMDGDLSPLADIAKLTKENDAWLMVDDAHGCGVLGTNGKGCCDVYSITPDILIVTFGKGFGLSGAAVLCNQECGDYLSQFARHHVYSTAMPPAQAHALSHALLMIQQQEWRRDKLKELNQQFESELMNFLGAEKTPTPIKPIIIGEATDAMILADSLKERGLWTTAIRPPTVPVGSARIRVTLSANHSSADISALTQAINELG", "text": "FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily."}
{"protein": "MNRDNAIAWSVEDLCVNYDHSDVLCHITFSLPAGAMAAIIGPNGAGKSTLLKASLGLIRASSGQSLFFGQRFSKVHHRIAYMPQRASVDWDFPMTVLDLVLMGCYGYKGIWNRISTDDRQEAMRILERVGLEAFANRQIGKLSGGQQQRAFLARSLMQKADLYLMDELFSAIDMASYQMVVDVLQELKSEGKTIVVIHHDLSNVRKLFDHVILLNKHLVCSGSVEECLTKEAIFQAYGCELELLDYTLKLSRGKYQGSC", "text": "FUNCTION: Part of an ATP-driven transport system CT_067/CT_068/CT_069/CT_070 for a metal. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MNRLLSVFALGGAVLLAGCVAPTPKPNDPYYAPVLPRTPLPAAANNGSIYQAGFEQNLYSDRKAFRVGDIITITLNERTSASKNAGSQIAKTSKTDIGLTSLFGSTPNTNNPFGGGDLSLEAGYSGDRATKGDSKATQGNTLTGSITVTVAEVLPNGIIAVRGEKWLTLNTGEELVRIAGMVRADDIATDNTVPSTRVADARITYSGTGSFADASQPGWLDRFFISPLWPF", "text": "FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family."}
{"protein": "MAVLSSVSSLIPFSYGATRLTSKASLASRTSGFNLSSRWNSTRNSPMLYLSRAVTNNSGTTEISDNETAPRTYSWPDNKRPRVCILGGGFGGLYTALRLESLVWPEDKKPQVVLVDQSERFVFKPMLYELLSGEVDVWEIAPRFSDLLTNTGIQFLRDRVKTLLPCDHLGVNGSEISVTGGTVLLESGFKIEYDWLVLALGAESKLDVVPGAMELAFPFYTLEDAIRVNEKLSKLERKNFKDGSAIKVAVVGCGYAGVELAATISERLQDRGIVQSINVSKNILTSAPDGNREAAMKVLTSRKVQLLLGYLVQSIKRASNLEEDEGYFLELQPAERGLESQIIEADIVLWTVGAKPLLTKLEPSGPNVLPLNARGQAETDETLRVKGHPRIFALGDSSSLRDSNGKILPTTAQVAFQEADFTGWNIWAAINNRPLLPFRFQNLGEMMTLGRYDAAISPSFIEGLTLEGPIGHAARKLAYLIRLPTDEHRFKVGISWFAKSAVDSIALLQSNLTKVLSGS", "text": "FUNCTION: Bifunctional oxidoreductase ables to act both on prenyl naphthoquinones and on prenyl benzoquinones (PubMed:21844348, PubMed:26023160). May serve a respiratory function (PubMed:12972666). Involved in an electron flow toward the plastoglobule plastoquinone pool (PubMed:21844348, PubMed:25018761). Required for plastochromanol-8 accumulation and for phylloquinone (vitamin K1) production (PubMed:21844348, PubMed:25018761). Probably not directly involved in cyclic or chlororespiratory electron flows under standard growth conditions, but participates in the redox metabolism of plastoquinone-9 and the tocophrol recycling-intermediate alpha-tocopherol quinone (PubMed:21844348, PubMed:25018761). Catalyzes the penultimate step in the biosynthesis of vitamin K1 (PubMed:26023160). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Plastid, chloroplast Plastid, chloroplast, plastoglobule. SIMILARITY: Belongs to the NADH dehydrogenase family."}
{"protein": "MADKITDEYAVGIDPEIYANNPAYSSLFNPYIHKQTIIADHVSVQCHIDLNGIDAVGSKFGNLNAHAGNFTSLCAPNCLPERFALVAYTVEYAFLHDALNQSGMTSVSTRVSDKAQRKSEVQAKIAAEYLRLDPVFGEWFLNKWQTFTACVKDVRSLEFPSLDDYLEFRIVDAAADWTLYNFRWGSGITLTPEEEKIADPMSYVAYAELCLVNDLFSWDKEYASHIKSNGDVPLVNAVHIVAVTQGLTHCAAKAVVQAEVRAHEERFCQLKEQYEATDKPSHEVLRWLRLLEHSMAGNWVWSLCVPRYCKVDRNPYKDHLEKYGSDAVRVLTPLDRLCWPKQEIKDMKQSELKDPSSSTYKSHFSPLEPNPGPEQMRLTISQTQQQRPVLNPYTYINSLPSKNVRQTLIAALNSWYKVPVKSLLIIEGAVNFLHNSSLLLDDIQDGSFLRRGRPVAHQIFGVGQTINTATYLMNEALYLIQMLSPSAVSVYTEIDEMRNLQLGQGRDLYWSYHTHVPTPAQYISMVDGKTGGLFRLISRLMRSEATKNSDLDISQFATLLGRHFQIRDDYQNLQSEDYTKNKGFCDDLDEGKLSFPIILSMQSPGFSNTALSSVFKGSQKGQTLSLEMKQYMLEEITARGAFSETKAVLRKLHTELLRLLIETEKKAGGVENWALRLLIMKLDIAEEKKVAPPKSDSHWGVNQRRAWKGCQKNGRPIDKACFLRAMEETLQK", "text": "FUNCTION: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of conidiogenone, a diterpene known to induce the conidiation (PubMed:30343633). The bifunctional terpene synthase PchDS converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into deoxyconidiogenol (PubMed:30343633). The C- terminal prenyltransferase (PT) domain of PchDS catalyzes formation of GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GGPP into deoxyconidiogenol (PubMed:30343633). The cytochrome P450 monooxygenase PchP450 then catalyzes two rounds of oxidation to furnish conidiogenone (PubMed:30343633). SIMILARITY: In the N-terminal section; belongs to the terpene synthase family. SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase family."}
{"protein": "MMLEYVLFLSAYLFSIGIYGLITSRNMVRALMCLELILNAVNINLVTFSDLFDSRQLKGDIFSIFVIAIAAAEAAIGPAIVSSIYRNRKSIRINQSNLLNK", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
{"protein": "MRQMKYQFKFNPLAAAIFTLLCGGSMQSSYADANDSASSVDNKKLKESIQKAYPGQEFFEQYYVEKSSPEAQVRDTRSLSSAFCTGTWITPISPTTQAVPADQATSVVTADYAHYNPNGDSELEGNVLIDQQGRSIRANKVTIDRTQTYANAEGNVQLAQAGLLAQSDQINYNLKTQQGDLKNSFYISEQQHAHGHAEQIQRTSPTEIILRNATYTTCPPEQKPTWRLEAKEIKLNQDTGRGTTKNTKLYVKDVPILAVPYFNFPIDNRRTTGILNPNIGFSNDGGLELTVPVYLNLAPNYDATLTPRYISDRGVMLQSEFRYLTENFGQGKIWGGYLPDDKKYNNEDRKDFNLLHKWKINDYWSTDVEYHYASDKDYVTDLDTNPDSKTDLNLRRAWTLKYKNQIPGLTAQLKVEDFQTLDKTVSDVDKPYARLPQFLLNYVTGNPLGLQYEFNNDTAYFKKNIDDAANYSTQPSGTRIYNQFATRYNFRTPWAFAIPEVSIRSINTFYDQNTVENLGLNSDNKSKSVVVPQFSLDTGLIFQRDGDYLQTITPRAFYAYAPYKNQTGYPNFDTTSASINYDQLFSPYRFYGHDRLEDNNFLSLGVSYSLFDPQGLERLRAGVGQSFYFADRRVTLNNTDDTIDTSKNSGPIVSISSQLTNKFTVAANSAWMSNGDNAQHDFQTYYTGDHGNLYNLGYFNRKNIPDRQLAYDAAVASFVQPIMNNWRIMGHVQFDFRNNVAREYLLGVNYESCCYAISVYGRSYYNDLDDPKDPNVNVKRAVMAEITFKGLGGLNNKLASLLENRVLGFKEINQSWTQR", "text": "FUNCTION: Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the LptD family."}
{"protein": "MTWKDIIENEQQKPYYGKLKEEIDKRYENSIVFPEKQNIFKAFSLTKFEDLKVVILGQDPYHGIGQAQGLSFSTPSNIKNPPSMVNILKEINDDLGKKSVCEDGDLTPWAKQGIMLLNTILTVEQGLAKSHHNLGWEIFTDNIIKYISDNKENVIFLLWGSPAISKTKLIDKNKHFILTAPHPSPLSVYRGFYGCKHFSKTNEILKKLNKEEIIW", "text": "FUNCTION: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family."}
{"protein": "MASMAFTLVGAFKGMSLSSPCHSSSSASFLRADRVSLSVGGGVGMGVPMTMPVRRLTIQMAHKKGAGSTKNGRDSPGQRLGVKIYGDQVAKPGAIIIRQRGTRVYPGNNVGMGKDHTLFSLIDGLVKFEKYGPDKKKVSVYPYEKQPENPNSYRARKREYFRMQRERKKARAEGIVEVQLVLAAADESPEVNADC", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
{"protein": "MFENNRVRIAMQKTGRLSKDSIRLLTSCGVKINLKQQKLIAFAENMPIDVMLVRDDDIPGLVMDGVVDLGIVGENVLEEELLKRKSQKSECSYITLRRLDFGVCRLSLALPVNTIYTNITCLKNIRIATSYPHLLKKYLDEKNISFKSCMLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVQVVYHSHACLICKTGNINSIKKEFINKLMTRIKGVIKARESKYIMLHAPIKQLEAVISLLHGAERPTILKLAGDDNRVAMHMVSSETLFWETMEKLKLLGASSILVLPIEKMME", "text": "FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily."}
{"protein": "MAAQSDKDVKYYTLEEIKKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTFIIGELHPDDRSKLSKPMETLITTVDSNSSWWTNWVIPAISALIVALMYRLYMADD", "text": "FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Microsome membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the cytochrome b5 family."}
{"protein": "MFACLRIGRFIRLGNVTVKSTNLVLRCVFIRNFATHADHLFDELPQRDLSSLNSQLSSHLRSGNPNDTLALFLQIHRASPDLSSHTFTPVLGACSLLSYPETGRQVHALMIKQGAETGTISKTALIDMYSKYGHLVDSVRVFESVEEKDLVSWNALLSGFLRNGKGKEALGVFAAMYRERVEISEFTLSSVVKTCASLKILQQGKQVHAMVVVTGRDLVVLGTAMISFYSSVGLINEAMKVYNSLNVHTDEVMLNSLISGCIRNRNYKEAFLLMSRQRPNVRVLSSSLAGCSDNSDLWIGKQIHCVALRNGFVSDSKLCNGLMDMYGKCGQIVQARTIFRAIPSKSVVSWTSMIDAYAVNGDGVKALEIFREMCEEGSGVLPNSVTFLVVISACAHAGLVKEGKECFGMMKEKYRLVPGTEHYVCFIDILSKAGETEEIWRLVERMMENDNQSIPCAIWVAVLSACSLNMDLTRGEYVARRLMEETGPENASIYVLVSNFYAAMGKWDVVEELRGKLKNKGLVKTAGHSLFI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PPR family. PCMP-E subfamily."}
{"protein": "MTSPNILLTRIDNRLVHGQVGVTWTSTIGANLLVVVDDVVANDDIQQKLMGITAETYGFGIRFFTIEKTINVIGKAAPHQKIFLICRTPQTVRKLVEGGIDLKDVNVGNMHFSEGKKQISSKVYVDDQDLTDLRFIKQRGVNVFIQDVPGDQKEQIPD", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MQSVDTTKYIIYADITADGIVERPDVVGAIFGQTEGLLGSDLDLRDLQKTGRLGRIDVQISSSGGKSMGTISIPSSFDKVETAILAAALETIDRVGPCMARIHVTKIEDVRAAKRKYIIDRAKRILVEMFDENLLETEQITEEIKQSVRVEEITYIGKDNLPAGPNVLDSDAILVVEGRADVLNLLKYGIKNAVAVGGTNIPPTITELCSKKIATAFTDGDRGGELIVKELLQVADIDYVARAPEGKCVEELTQKEIIRALRQKIPVEQVMDMYKIKPFTRKKREIVTKRKSLIRERPVSVRTVAQVVPIAHHAEIAPPHEIQTRVHQKEVHEHYEEPEIEGQEPEEWFKHHVEELDGTLTARLFDRNNNPIRDVAVRDLARELKESNGSVHGVIFDGVITQRLLDIAAEKGLDYLIGAKMGSIAKTPVGIKVITSGQ", "text": "FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome. SIMILARITY: Belongs to the archaeal DnaG primase family."}
{"protein": "MDKFLIKMPIKHKNNETPEQKPIVKKETPKAAAKQSNKNTPIQAKEKENAQNDTPKQGRAGRSAKPAAKRKNLDTLEVNTEKNTAESENPPKRRSGRLTRSTRSMAEEGTPSPEKVKPEKLPFIKYRGAIKYFTENQDIAASADDVMQWVDKQTDVDVVPMAFDMEWPFSFQTGPGKSSVIQICVDEKCCYVYQLTNLKKLPAALVALINHPKVRLHGVNIKADFRKLQRDFPEVSADALIEKCVDLGVWCNEICETGGRWSLERLANFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRDLEQREKQKLINELQFKEQNGEAAFKAVKGLGETFLSKINEITL", "text": "FUNCTION: Has exonuclease activity on both single-stranded and duplex templates bearing overhangs, but not blunt ended duplex DNA, and cleaves in a 3'-5' direction. Essential for the formation of DNA replication focal centers. Has an important role in maintaining genome stability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRNexo family."}
{"protein": "MASNLTFEDKIGILDPKGLRPNPLNNEPYSDDYKKLAMVWSTYPAYSAADRVLSALENYQLVFVTSSTGSGKSVLIPKLALHYTNYNGRVVMTLPKRIITLSAAIFSAKVSDVKLGESIGYAYKGSDKSMYNDQNKIIYVTDGIFVMEYVRDPLLSKFNVVIIDEAHERRIQIDLILLFLRTLLQSGNRPDLKVIIMSATIDTDKYQKYFNSVDSTVIDIAGQPNHPIETHFMDKPVTSYMKEGLELIEDLIHQQIKKDMLFFITTSNEALQLCRSIRPQYPRVYCVEVYSDMDKNLKQYAESRDKYLELGNYDQKLVMATNVAESSLTIDGLVYVIDSGYELSSRFDPECYGQILEKKFVSKAQALQRRGRVGRTEPGVCYHLLTKQQFDGLADYPTPDILRQDITMDLIKIIQVSPNKTYAEGINMMNQLMDPPLRSHINATRNLFDLYNVVDDNGILTQVGIVATQFSSLPLNRILFLIYAFELQCAREASIIVAMTEFLNGRVTNLFYKSDTICESNCEKQAANLLLEKLIQKRGDHFTYLKIYQEFSKSTDQKSWARKYGVRLDTINNIERTANQYFYRILNLLRKPRLPNNKNTLIDTSIDTPMDIQSRISSTDTKTNLLNALKKSHQHLTASKLKPTYSKENITGKISRDSVLNQIYKKNEISKKKIIYDELSNINGKWEFRTVTIIS", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily."}
{"protein": "MMRFVPLFLACISLPAFQATEFTKCEVSHAIEDMDGYQGISLLEWTCVLFHTSGYDSQAIVKNNGSTEYGLFQISNRNWCKSSEFPESENICDISCDKFLDDELADDIVCAKKIVAIKGIDYWKAHKPMCSEKLEQWRCEKPGAPALVVPALNSETPVP", "text": "FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N- acetylglucosamine of the oligosaccharide chains in glycoproteins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 22 family."}
{"protein": "MVASIAGEEEPAAEKSQQSPDHFQPYRPYYYPPYRGYPITYPYPYPHGYPKPYHNFQTIAKPNEGPTDQPEANSANSIEEGGVSKRLFIEPIFNLFRPRPRDPIVVNQAPPPPPVIYQAPPPPPPPPIFQQAPPTIYQQPSPTIIQQAPQPSVTKLVYSQPEPSHSVIYQTQPKTELVYLNQ", "text": "FUNCTION: Structural protein of a layer within the wall of the spermatophore produced probably by cell type 4 of the bean-shaped gland (BAG). Fixation in the spermatophore seems to require covalent cross- linking of spermatophorins. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTMLNFTYYNPVRLIYGKGSLDEIEKQHLIPEDARIMMTYGGGSIKKNGVYEEVLKHIKPIVEFGGIEPNPSHETCIKAIKIAKENKINFLVAVGGGSIIDATKYIALGMEHTYSDDPYDICLKGGKFKVNPAQAKIGVVLTIPATGSETNCWGVISRHADKLKLPFNNESVFPTWSIVDPCFTMSLPDNQIRNGLVDSFVHCIEQYIGNYHLNPVVEAETEGVMRTIIGVSHKTLENHQDYQARITFCYAATVALNMSLLCGVTLCGGAHAVGHELTSYYGLAHGETLAITTPGVMRFNKEKNAKKLIQMGEQVFGIKNSTPEAAIEATEKWFKSIGMKTRLSEWGKGKEEFETIARKFEGNPAGAHKDIDYKGCLQILNDIY", "text": "FUNCTION: Has NADP-dependent alcohol dehydrogenase activity. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family."}
{"protein": "MGDKRGLVLDETATYGTVDRLTGWFRNVCIQLPEGTLLVLCCCAVEQRIGVTTFSIGLSYDLLTGLDPSNPDTVQSPWILTLQVDQKEEYPKGLLLRIPTKQTLKDYWIHQLKEACVSRDGNANRVMSLSNANSQKMWDSLVSHDFKTFWSIMTTILPREKDSGAIRSLPIKVYLPMSNQCIAAIVKPETDDGKLTTIGQSLHSHLPTFFPSETKPVVARAVVHGVEVPLNAVLANLYYMAMYPDGFLHISLVMIN", "text": "FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1- like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG5 family."}
{"protein": "MEPGFWHEKWYKQQIGFHQQDINPFLVQYWQRLALPAGAKVFVPLCGKSLDMCFLAEQGHQVIGCELNELAVQQFFSDNQLEMTQTVEGEHQHYQTEQVSLYQGDIFTLPKRITQDVTAFYDRAALIAWPEEMRTQYAKQLANLLPSGSLGLLVTLDYPQETLNGPPFAVSPNWIEAHLTDDFEIQVLACQDVLADNPRFVKKEVPWLNEAAYLLKRK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TPMT family."}
{"protein": "MACEIMPLQSSQEDERPMSPFYLSSAHVSQVSSVSSTGELLERTIRSAVEQHLFDVNSSGGQSSEDSESGASSSSSTSTKQRRRQAKEQDESRHSRDVGRLNKENIPSGFSNLDECMLNACEVEKLYENTSGYIGERGKPKRQKSSSRLSELNENQDGLVNMENLNPTPSHERTGSDHVELISDGSKENEKDGRQSQHLENPTMKIQEHPSLPDSKLQRTPDADDQQESFVSEVPELDLTALCDQKSWEEPIPAFSSWQQESVDADEARLSPQAGRLIRQLLEEDSDPMLSPRFYAYGQSRQYLDDTEMPPSPPNSHPFMRRRSSSLGSYEDEQEDLTPAQLTRRIQSLKKKIRKFEDRFEEERKYRPSHSDKAANPEVLKWTNDLAKFRKQLKESKLKISEEDLPPRMRQRSNTLPKSFGSQLEKEDEKKQELVDKAIKPSVEATLESIQRKLQEKRAETSRPEDIKDMTKDQIANEKVALQKALLYYESIHGRPVSKNERQVMKPLYDRYRLVKQILSRASTIPIIGSPSSKRRSPLLQPIIEGETASFFKEIKEEEEGSEDDNYTKPDFMVTLKTDFSARCFLDQFEDDADGFISPMDDKIPSKCSQDTGLSNLHAASIPELLEHLQEMREEKKRIRKKLRDFEDNFFRQNGRNVQKEDRTPMAEEYNEYKHIKAKLRLLEVLISKRDTDSKSM", "text": "SIMILARITY: Belongs to the FAM13 family."}
{"protein": "MKIEVKDSTMIKPSAETPGGSLWLSNLDLLSPANYHTLSVHFYSHDGSDNFFDAAGLKESLSRALVEFYPYAGRLKLNGNRLEIDCNNEGLLLVEAECDGALDELGDFAPRPELNLIPKVDYSRGISTYPLMVFQLTRFKCGGVALGVANEHHLSDGVAALHFINTWAHLSRGAPAPTPLPHFDRSSLSARNPPQPQFSHAEYQPPPTLENPLPHTDIAHSRFKLTRDQLNSLKSKFKTAPADGGAGKSYSTFEVLAGHIWRSVCIARGLPEGQETKLHIPFDGRGRLQLPPGFFGNAIFFATPIATCGEIESNSLNYAVRRVSDGVSRLDEDYLRSSIDFLELQEDISKLAQGAHSFRCPNLWVISWVWLPIYEPDFGWGKAVYMGPWAAPFEGKSYLLPNPEKDGSLFVSITLHKQHMERFEKLFYEI", "text": "FUNCTION: Involved in the biosynthesis of rosmarinic acid, a compound with antiviral, antimicrobial and anti-inflammatory activities. Can use 4-coumaroyl- and caffeoyl-CoA as hydroxycinnamoyl donors and 4- Hydroxyphenyllactate and 3.4-Dihydroxyphenyllactate, but not shikimate or quinate, as hydroxycinnamoyl acceptors. Can also putatively catalyze amide formation with D-amino acids as acceptors. SIMILARITY: Belongs to the plant acyltransferase family."}
{"protein": "MARYRHSRSRSRSRYRRRRRRRSRYRSRRRRYRGSRRRRSRRRGRRRGYSRRRYSRRRRRRY", "text": "FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the protamine P1 family."}
{"protein": "MLIVNRNPKSLVRGYCKKDIVLRNLDGWLFDMITISTIFKLYNQICSLSSTDRKKTSISNKLQQEFCIMDINKVGRNFISLGKIRSSKRRNAILSYQTIISSFPHNHVQKLFQRTQSTNMIYTKLEYFGHSLFFYFTAFTLSFKDRKILMQADVFFRLKLVFKIAFFFTQTTFLNKKENREL", "text": "SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MSSGEPTTMTPSPSERTPLLSNGSGGAADDGGTTVTISKPNDGVRRIADSLPLSVWLISTIELCERFAYFGTIAPMQNYIQNPRNDPLRPGGIGKTASTMIYPAV", "text": "FUNCTION: Part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination (PubMed:29182847). ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors (PubMed:29182847). N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline (PubMed:29182847). Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation (PubMed:29182847). The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH (PubMed:29182847). Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins (PubMed:29182847)."}
{"protein": "MRILQNKTMKEQDNQLKIPEPLRADWFMVLVTIQADLIYNALVVLSSPFFLLYRSYRRAVVTVSAAEKAVKRAPAQIAGGAGRVVRRTWFGILGACHVSMVMVLALILAVVIGVGIVSLYVEKPVVVRDRLFFDYTEENPSAVFSFDKKKRSFSVPVGHSVHVSLVLWMPESEINRRIGVFQLKVELLSLKGETIARSSQPCMLRFRSKPIRLARTFVMSVPLIAGIANEAQTMRIDALKHQEKMPRTKAVRATLIPRAQTRTLPQLYEAEIVINSKPPWIKRMAYNWKWTLCVWTSMYLYVAILTALLWCFRPVLFPYTSSRTISESENLEIEVVEEEQEQVMERRRRERRNQPRRRNFATTQKSYT", "text": "FUNCTION: Involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. Facilitates the formation of large-sized LDs and modulates triacylglycerol accumulation. Induces probably a reorganization of the endoplasmic reticulum into LD-forming domains. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localized to the lipid droplet-forming sites. SIMILARITY: Belongs to the seipin family."}
{"protein": "MLDREGFRPNVGIILLNARNEVFWGKRLREHSWQFPQGGIKYGETPMQAMYRELHEETGLHPEHVKIIGRTRDWLRYEVPDKFIKREVRGHYRGQKQIWFLLRMVGRDCDICLRATDHPEFDAWRWNEYWVPLDAVIEFKRDVYQLALTELSRFLRRPAQRAEKPRGPRPLRYPRIGGAPAQQTLTIVDTSVVCSEIEVEARTLDEMPPRVIIGK", "text": "FUNCTION: Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily."}
{"protein": "MDALTDRQLEVLRFIARQIEDNGYPPTIREIGEALDIRSTNGVNDHLKALERKGFLTRDPVKSRALIPTPQAREVLGGGARASNVVPFTRTPAVGLKPAGRLVEIPILGRVAAGQPILAQERVEDTVQVDSFLLGTNKKVYGLRVQGDSMIGDGILPGDYIFVKKQLHAEDGDIVVAMIDEEATVKRVYFEGDRVRFQPSNPRMAPIYVRGSDFRTTMILGVVVGVYRKLG", "text": "FUNCTION: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. SIMILARITY: Belongs to the peptidase S24 family."}
{"protein": "MGCRQSSEEKEAARRSRRIDRHLRSESQRQRREIKLLLLGTSNSGKSTIVKQMKIIHSGGFNLDACKEYKPLIIYNAIDSLTRIIRALAALKIDFHNPDRAYDAVQLFALTGPAESKGEITPELLGVMRRLWADPGAQACFGRSSEYHLEDNAAYYLNDLERIAAPDYIPTVEDILRSRDMTTGIVENKFTFKELTFKMVDVGGQRSERKKWIHCFEGVTAIIFCVELSGYDLKLYEDNQTSRMAESLRLFDSICNNNWFINTSLILFLNKKDLLAEKIRRIPLSVCFPEYKGQNTYEEAAVYIQRQFEDLNRNKETKEIYSHFTCATDTSNIQFVFDAVTDVIIQNNLKYIGLC", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily."}
{"protein": "MTQMLEAMRGNITEAMKTVAADEKLDPEYIRKMVAKGYIAIPDNNQRETVAVGIGENLRTKVNATIGTSTDINDLDMELEKAKIAEEAGADTLMELSIGGDLDNIRRTVLKNTKKPVGSVPIYQTAVEAIEKDGSAINMDPDDMLKNIEKQAKDGIDFMAIHCSVNRETLKRLKRQGRNGGLVSRGGSFISSWMVHNDCENPLYENYDQVLDIVEEYDVCLSMANAMRAGALTDSTDRAQIQELIVLGELVDRARERGVQTIVEGPGHIPINEIETNINIQKKMCKNAPFYMLGPIVTDIAPAYDHIVSAIGAAQCARYGANFICYVTPAEHLALPGPEDVREGVIATRIGAHAGDLAIDLERFGEDDIAMAHARKSLNWTEQYEHAMWPADAKAIRDKRPPEADDTCTMCGNYCAIKIVNQWLDKADKDAFDN", "text": "FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. SIMILARITY: Belongs to the ThiC family."}
{"protein": "MDLFVFFALIWPPYVANGSAVLASRLKWRHPVDFGHNFVDGRRLFGDGKTYEGLAIGVVLGTVVGYLPNLLHPTLTLLDALILSVAALLGDLLGAFIKRRLCMPRGHPAFPLDQLDFILMAMLVRSLYADVPVEYIIAASVVTPIIHRATNIAAYILRLKKEPW", "text": "FUNCTION: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn- glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1- phosphate (DGGGP) and CTP. This reaction is the third ether-bond- formation step in the biosynthesis of archaeal membrane lipids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-archaeol synthase family."}
{"protein": "MQVLSSLKTAKQRHRDCQIVRRRGKVYVICKSNPRFKSRQR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
{"protein": "MVTGVFAALGFVVKELVFLVSYVKNNAFPQPLSSSEEKKYLELMAKGDEHARNMLIEHNLRLVAHIVKKFENTGEDAEDLISIGTIGLIKGIESYSAGKGTKLATYAARCIENEIVITKGGCIHPSLIRFNIYGVRIHNGNFFHDKVNNCFFIFKSMPPLFVMNNEILMHLRALKKTKKDVSLHDPIGQDKEGNEISLIDVLKSENEDVIDTIQLNMELEKVKQYIDILDDREKEVIVGRFGLDLKKEKTQREIAKELGISRSYVSRIEKRALMKMFHEFYRAEKEKRKKAKGK", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes in the mother cell. SIMILARITY: Belongs to the sigma-70 factor family."}
{"protein": "MALRDLSSSLSSSSSPELHVLAVDDSFVDRKVIERLLKISACKVTTVESGTRALQYLGLDGDNGSSGLKDLKVNLIVTDYSMPGLTGYELLKKIKESSALREIPVVIMSSENIQPRIEQCMIEGAEEFLLKPVKLADVKRLKELIMRGGEAEEGKTKKLSPKRILQNDIDSSPSSSSTSSSSSSHDVSSLDDDTPSSKRIKLESRG", "text": "FUNCTION: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARR family. Type-A subfamily."}
{"protein": "MNKNGGPPVANITTSSTTITSTTTTQAKSQLPSSLSVNNLHTTQGSTDQPTILGVTEPISTAPPSSIDFKLSTELENTLISFNLFESPEESRKREEILGKLNQIVREWAKQVSLKKGYPEQTASEVVAKIFTFGSYRLGVHGPGSDIDTLCVGPKHIMRSDFFDDLSDILKVHPEITEFTTVKDAFVPVITMVFSGIPIDLIYAKLALTAIPEELNDLIDESFLKNIDEKSILSLNGCRVTDQILKLVPNIPNFRMALRCIKLWAIRRGIYSNILGFLGGVSWALLTARICQLYPNSAPSTIIHRFFKVYEIWKWPAPILLCHIQEGGILGPKVWNPKRDKAHLMPIITPAYPSMNSTYNVSKSTLQLMKSEFVRGAEITRKIETGECTWKNLLEKCDFFTRYSFYIEIDCYSMNEEDSRKWEGWIESKLRFLISNLESTPKMKFAVPYPKGFTNNLHKANNPDQICTSFFMGLSFNFSNTPGADKSVDLTKAVTEFTGIIKDWLRTQPNPDTMDIKVQYIKKKQLPAFVKDEGPEEPVKTTKKRSSTGEPSATRKKLKSENSDNKLNSPKSPITTNINSTPTTSTPTTTANTTTNTTTATTTTTTTTVPITSTPTSNISSPTMNSTELTTPTSTSTTTSNDSITTPPTTTTINSVQPPSAQPTENGSSTSNSPTSTSINNTALPPNPTTNSESTIETTITLPTTLESQTSTLKDSNEISTNGTAVATEPTITSPSVNINESSTSTSTTTTTTVTEQQIQTAPTTATPINKTIVNTMEVNELSFISSSSETSQSKPPPKKPTISIIRGN", "text": "FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the poly(A) polymerase family."}
{"protein": "MEASFVQTTMALGLSSKKASSRNVAVERKNLITVCRFSVKTLLEKYTAEPIDDSSEEFVNFAAILEQILSHRFKACAPAGPVSWFSSDGQRGFWDYIRLACSKVPNNCVSSIENMENISTARAKGRAWIRVALMEKRMSEYITTALRDTRTTRRFYDSGAIMLRDEATILTGMLIGLSAIDFSFCLKGEVLDGKTPVVIDYTPYLKFTQSYDYLTDEEERHSAESSTSEDNSPEHPYLPLVTDEDSWYSKWHKMEQKFRIVYAQKGYLEELVRLRESQLKDLEAENRRLQLQLEEAAAQNQREKRELEGVILELQEQLTGLIPSDHAPLAQGSKELTTPLVNQWPSLGTLNGAEGASNSKLYRRHSFMSTEPLSAEASLSSDSQRLGEGTRDEEPWGPIGKDPTPSMLGLCGSLASIPSCKSLASFKSNECLVSDSPEGSPALSPS", "text": "FUNCTION: May act as an effector of RAP2A in neuronal cells. SIMILARITY: Belongs to the RUNDC3 family."}
{"protein": "MDGLLNPRESSKFIAENSRDVFIDSGGVRRVAELLLAKAAGPELRVEGWKALHELNPRAADEAAVNWVFVTDTLNFSFWSEQDEHKCVVRYRGKTYSGYWSLCAAVNRALDEGIPITSASYYATVTLDQVRNILRSDTDVSMPLVEERHRILNETGKILLEKFGGSFLNCVRESENSAQKLMHLVVESFPSYRDVTLFEGKRVSFYKRAQILVADTWSVLEGKGDGCFKDISSITMFADYRLPQVLAHLGALKYSDDLLKKLLKGEMLSYGDRQEVEIRGCSLWCVELIRDCLLELIEQKGEKPNGEINSILLDYYLWDYAHDHREDMKGIPFHRIRCIYY", "text": "FUNCTION: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly. In vitro, can also catalyze the release of the q base directly from Q as substrate; however, it was shown that Q is not the biologically relevant substrate. Shows a very low activity on queuosine 3',5'-diphosphate, and cannot release q from queuosine 3'-phosphate and from the 5'-nucleotides AMP, UMP, CMP or GMP, indicating specificity for the queuine base (PubMed:36610787). Can complement the yeast mutant SPAC589.05c, restoring Q incorporation into tRNA (PubMed:24911101). SIMILARITY: Belongs to the QNG1 protein family."}
{"protein": "MGKYHSFVNVVALSLSLSGRVFGAIGPVTDLTISNADVTPDGITRAAVLAGGVFPGPLITGNKGDEFQINVIDNLTNETMLKSTTIHWHGIFQAGTNWADGAAFVNQCPIATGNSFLYDFTVPDQAGTFWYHSHLSTQYCDGLRGPLVVYDPDDPNASLYDVDDDTTVITLADWYHTAAKLGPAFPAGPDSVLINGLGRFSGDGGGATNLTVITVTQGKRYRFRLVSISCDPNFTFSIDGHNMTIIEVDGVNHEALDVDSIQIFAGQRYSFILNANQSIDNYWIRAIPNTGTTDTTGGVNSAILRYDTAEDIEPTTNATTSVIPLTETDLVPLDNPAAPGDPQVGGVDLAMSLDFSFNGSNFFINNETFVPPTVPVLLQILSGAQDAASLLPNGSVYTLPSNSTIEISFPIITTDGVLNAPGAPHPFHLHGHTFSVVRSAGSSTFNYANPVRRDTVSTGNSGDNVTIRFTTDNPGPWFLHCHIDFHLEAGFAIVWGEDTADTASANPVPTAWSDLCPTYDALDSSDL", "text": "FUNCTION: Lignin degradation and detoxification of lignin-derived products. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MPAKLGYWKLRGLAQPVRLFLEYLGEEYEEHLYGRDDREKWMSEKFNMGLDLPNLPYYIDDKCKLTQSVAIMRYIADKHGMLGTTPEERARISMIEGAAMDLRIGFGRVCYNPKFEEVKEEYVKELPKTLKMWSDFLGDRHYLTGSSVSHVDFMLYETLDSIRYLAPHCLDEFPKLKEFKSRIEALPKIKAYMESKRFIKWPLNGWAASFGAGDAPPS", "text": "FUNCTION: GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Mu family."}
{"protein": "MAAGLRKRGQPASVGQPAGIWKQWLQRAWQERYLLLREPRYTLLVASCLCIAEVGITFWVIHRVAYTEIDWKAYMAQVEGFINGTYDYTQLQGDTGPLVYPAGFLYIFTGLFYATDRGTDIPMAQNIFAVLYLVTLVLVFLIYHQTSKVPPFVFFFMCCASYRVHSIFVLRLFNDPVAMALLFLSINLFLAQCWSWGCCCFSLAVSVKMNVLLFAPGLLFLLLTQFGFRGALPKLAICAALQVVLGLPFLLENPIGYLSRSFDLGRQFLFQWTVNWRFLPETIFLHRAFHLALLAAHLSLLLLFALCRWHRTGESILALLKDPSKRKVPPQALTPNQIVSILFTSNFIGICFSRSLHYQFYVWYFHTLPYLLWAMPARWLTHLLRLLVLGLIELSWNTYPSTSFSSAALHLCHAVVLLQLWLSPESFPKSIQPSRKTH", "text": "FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 58 family."}
{"protein": "MARSLKKNPFVANHLLRKIKNLNIKKEKKIIVTWSRASVIVPAMIGHTIAVHNGREHLPIYVTDRMVDHKLGEFAPTLLFQGHARNDKKSRR", "text": "FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS19 family."}
{"protein": "MKEQKWIHEGLITESLPNGMFRVRLDNEDLILGYVSGRIRRSFIRILPGDRVKIEVSRYDSTRGRIIYRLRNKDSND", "text": "FUNCTION: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the IF-1 family."}
{"protein": "MAMSELGIQKTSDGTVSRLLNVVESELQAGREKGDPTEKQLQIILEDAPLWQRFKEVTNEMIVTKNGRRMFPVLKISVSGLDPNAMYSLLLDFVPTDSHRWKYVNGEWVPAGKPEVSSHSCVYIHPDSPNFGAHWMKAPISFSKVKLTNKLNGGGQIMLNSLHKYEPQVHIVRVGGAHRMVMNCSFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERNHLKDIPEAVSESQHVAYSHLGGWIFSNPDGVCAAGNANYQYATPLPLSAPHTHHGCEPYPGLRGHRQAPYPSAYMHRNHSPSVNLIESSSNNLQVFSGPDSWTSLSSTPHTSILSVPHTSGPINPGPSPYPCLWTISNSGGGPAGPGPDVHASSPGAFLLGGPAVTSPLSAQAPTSAGVEVLGEPSLTSIAVSTWTAVASHPFSGWGGPGGGGHHSPSSLDS", "text": "FUNCTION: Transcriptional regulator involved in developmental processes. Can activate POMC gene expression and repress the alpha glycoprotein subunit and thyroid-stimulating hormone beta promoters (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKFAAVVVLAAAAAAVSAETNAQRMARGLPPKAPIRRHGTPADTEKRSHPSSTGGGQCNTGPIQCCNTVATSGSQSGVDELLTLLGLSVPVGTQVGASCSPISAVGTGSGAQCSGQTVCCEQNEWNGLVNIGCMPINLNA", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the fungal hydrophobin family."}
{"protein": "MAGKSAEEEHPIKAYGWAVKDRTTGILSPFKFSRRATGDDDVRIKILYCGICHTDLASIKNEYEFLSYPLVPGMEIVGIATEVGKDVTKVKVGEKVALSAYLGCCGKCYSCVNELENYCPEVIIGYGTPYHDGTICYGGLSNETVANQSFVLRFPERLSPAGGAPLLSAGITSFSAMRNSGIDKPGLHVGVVGLGGLGHLAVKFAKAFGLKVTVISTTPSKKDDAINGLGADGFLLSRDDEQMKAAIGTLDAIIDTLAVVHPIAPLLDLLRSQGKFLLLGAPSQSLELPPIPLLSGGKSIIGSAAGNVKQTQEMLDFAAEHDITANVEIIPIEYINTAMERLDKGDVRYRFVVDIENTLTPPSEL", "text": "FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts precondylocarpine acetate to dihydroprecondylocarpine acetate. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MKPEIHPIYREVVFHDVTSNFKFLTRSTMGTKETTLWEDGLEYPLVKVEISSASHPFYTGKHKLVDTSGRIDKFKKRYAR", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily."}
{"protein": "MWWPMLWAFPVLLCLCSSQALGQESGACPDVKIVGLGAQDKVAVIQSCPSFPGPPGPKGEPGSPAGRGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQKELGDALCRRGPRSCKDLLTRGIFLTGWYTIYLPDCRPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYLHLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFLEGTAGDSLTKHNNMAFSTHDQDNDTNGGKNCAALFHGAWWYHDCHQSNLNGRYLPGSHESYADGINWLSGRGHRYSYKVAEMKIRAS", "text": "FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen- associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage (By similarity). SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein; Extracellular side Note=Found on the monocyte and granulocyte surface. SIMILARITY: Belongs to the ficolin lectin family."}
{"protein": "MVSDFFFPQPGGIESHIFQLSQRLIDLGHKVIVITHAYKDRVGVRYLTNGLTVYYVPLHTVYRETTFPSFFSFFPIFRNIVIRENIEIVHGHGSLSFLCHDAILHARTMGLKTCFTDHSLFGFADAGSIVTNKLLKFTMSDVNHVICVSHTCRENTVLRAVLNPKRVSVIPNALVAENFQPDPSKASKDFLTIVVISRLYYNKGIDLLIAVIPRICAQHPKVRFVIAGDGPKSIDLEQMREKYMLQDRVEMLGSVRHDQVRDVMVRGHIYLHPSLTEAFGTVLVEAASCGLYVISTKVGGVPEVLPSHMTRFARPEEDDLADTLSSVITDYLDHKIKTETFHEEVKQMYSWIDVAERTEKVYDSICSENNLRLIDRLKLYYGCGQWAGKLFCLLIAIDYLVMVLLEWIWPASDIDPAVDRVSSTFKISKQNFDESLVLTDPKKKTKIKTACLKDAQ", "text": "FUNCTION: Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MATPFLPSGATTGDSGGELSSGDDSGDMESFQTPEAEGTRSLAELFEKAAAHVQGLVQVASREQLLYLYARFKQVKVGNCNTPKPNFFDFEGKQKWEAWKALGDSSPSQAMQEYIAAVKKLDPGWNPQVSEKKGKEGSSGFGGPVVSSLYHEETIREEDKNIFDYCRENNIDHIAKAIKSKAADVNMTDEEGRALLHWACDRGHKELVKVLLQYEAGINCQDNEGQTALHYAAACEFLDIVELLLQSGADPTLRDQDGCLPEEVTGCKAVSLLLQRHRASKA", "text": "FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not bind fatty acids (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MEKIFLNGEFVSPSEAKVSYNDRGYVFGDGIYEYIRVYNGKLFTVTEHYERFLRSANEIGLDLNYSVEELIELSRKLVDMNQIETGAIYIQATRGVAERNHSFPTPEVEPAIVAYTKSYDRPYDHLENGVNGVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNAVEAIQHRGETVTEGSSSNAYAIKDGVIYTHPINNYILNGITRIVIKKIAEDYNIPFKEETFTVDFLKNADEVIVSSTSAEVTPVIKLDGEPINDGKVGPITRQLQEGFEKYIESHSI", "text": "FUNCTION: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity). SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MERNQRKTLYGRVVSDKMDKTITVVVETKRNHPVYGKRINYSKKYKAHDENNVAKEGDIVRIMETRPLSATKRFRLVEVVEKAVII", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. SIMILARITY: Belongs to the universal ribosomal protein uS17 family."}
{"protein": "MVKSHMGSWILVLFVVTWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGAHGQWNKPSKPKTSMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYKPVDQYSNQNSFVHDCVNITVKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYQREYQASYGRGASVIFSSPPVILLISFLIFLIVG", "text": "FUNCTION: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Golgi apparatus Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. SIMILARITY: Belongs to the prion family."}
{"protein": "MSAPEGPSKCTWTPNTTENTPHTTRRTPKKLIMDNILDNIGGTPLVRVNKVSSDLECELVAKCEFFNAGGSVKDRIGHRMIVDAEESGRIKKGDTLIEPTSGNTGIGLALTAAIKGYKMIITLPEKMSQEKVDVLKALGAEIIRTPTEAAFDAPESHIGVAKKLNSEIPNSHILDQYGNPSNPLAHYDGTAEELLEQCEGKIDMIVCTAGTGGTITGIARKIKERLPNCIVVGVDPHGSILAQPESLNNTNKSYKIEGIGYDFIPNVLERKLVDQWIKTDDKESFIMARRLIKEEGLLCGGSSGSAMVGALLAAKQLKKGQRCVVLLADSIRNYMTKHLNDDWLVDNGFVDPEYKTKDQQEEEKYHGATVKDLTLPKPITISATTTCAAAVQLLQQYGFDQLPVVSESKKVLGQLTLGNLLSHIASKKAVPTDAVSKVMFRFTKNEKYIPITQSTSLATLSKFFENHSSAIVTENDEIISIVTKIDLLTYLMKSQQKN", "text": "SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family."}
{"protein": "MEANVTIPIWQNKPHGAARSVVRRIGTNLPLKPCPRASFETLPNISDLCLRDVPPVPTLADIAWIAADEEETYARVRSDTRPLRHTWKPSPLIVMQRNASVPNLRGSEERLLALKKPALPALSRTTELQDELSHLRSQIAKIVAADAASASLTPDFLSPGSSNVSSPLPCFGSSFHSTTSFVISDITEETEIEVPELPSVPLLCSASPECCKPEHKATCSSSEEDDCVSLSKASSFADMMGILKDFHRMKQSQDLSRSSLKEEDPAVLISEVLRRKFALKEEDISRKGN", "text": "SIMILARITY: Belongs to the MTFR1 family."}
{"protein": "MSNDQGSQFLRAPIVVVLGHVDAGKTTLLDKIRGTAVAKREPGTMTQHIGASFLPWKALEAVCGSLVSQIRAEVVIPGFLVIDTPGHEAFSNLRRRGGSIADIAILVVDVLRGLEQQTFESIDILRERKVPFIVAVNKIDKIPGWKSFPNTPFVESVKRQSEAAQLKLEELLSYIIQQFASLGFRSDRYDRIRDFTRVLALVPVSAVTGEGIPDLLLVLAGLAQRYLKGRLLASIAPGKGVILELKEEAGLGMTATLILYDGVIRRGDIVVTGGIEGAFSTRVRALLMPKPLDEMRSPEDRFLEVERIVAAAGVKLVAEGLEKAVPGAPLFVAVSEEEVGRLKQLVEEEISGVKFERDVVGVVVKADTLGTLEALVGYLKKQGIPIRVADIGPVVKRDVVQASMVKEKDPLYAAILAFNVKILPEAQDEAARHGIPVFQERIMYKLVENYQKWLQETRDAEVRKAFEKITPPAVVQILPGYVFRRRDPIIVGVRVVCGRIRSGVPLITKDGREIGEIMQIKEHDKVLDVVSEGAEVAISIRSKAIVGRQVKEGDYLYSNLSIEEINRLLEKYEKYLAENEKSYLRKLMRFKMGLSKEIEYP", "text": "FUNCTION: Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily."}
{"protein": "MLSSGDLTSASWELVVRVDHANGEQQTEITLRVSGDLHIGGVMLKLVEQMNIAQDWSDYALWWEQKRCWLLKTHWTLDKCGVQADANLLFTPQHKMLRLRLPNAKTVRLRVSFSAVVFKAVADICKVLNIRRPEELSLLKPSSDYCKKKKKKEKNSKEPVIEDILNLESSSTSSGSPVSPGLYSKTMTPTYDPINGTPALSTMTWFGDSPLTEQNCSVLAFSQPPPSPDVLADMFQPRSLVDKAKMNAGWLDSSRSLMEQSIQEDEQLQLRFKYYTFFDLNPKYDAVRINQLYEQARWAVLLEEIDCTEEEMLIFAALQYHISKLSQCAEIQDFATKSEVDEVEAALSSLEVTLEGGKADNTLEDITDIPKLADYLKLFRPKKLMLKACKQYWFVFKDTSIAYFKNKELEQGEPIEKLNLRGCEIVPDVNVSGRKFGIKLLIPVADGMNEVYLRCDHEDQYARWMAACILASKGKTMADSSYQPEVISILSFLKMKNRNSSPLVASSLENMDMNPECLVSPCCAKKHKSKQLAARILEAHHNVAQMPLVEAKLQFIQAWQSLPEFGLTYYLVRFKGSKKDDILGVAYNRLIRIDAVTGIPVTTWRFANMKQWNVNWEIRQVAIEFDQNVSIAFTCLSADCKIVHEYIGGYIFLSTRSKDQNETLDEDLFHKLTGGQD", "text": "FUNCTION: Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell junction, focal adhesion Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Note=Colocalizes with filamentous actin. Constituent of focal adhesions (By similarity). Localized at the basal aspect of skin keratinocytes, close to the cell membrane (By similarity). Upon TGFB1 treatment, it localizes to membrane ruffles (By similarity). SIMILARITY: Belongs to the kindlin family."}
{"protein": "MKRRRRWRGWLLFPALCFCLLCEAVETNATTVTSTTAAAATTNTTVATTGTTTTSPNVTSTTSNTVTTPTTVSSVSNLTSSTTSIPISTSTVSGTRNTGNNNTTTIGTNATSPSPSVSILTTVTPAATSTISVDGVVTASDYTPTFDDLENITTTRAPTRPPAQDLCSHNLSIILYEEESQSSVDIAVDEEEPELEDDDEYDELWFPLYFEAECNRNYTLHVNHSCDYSVRQSSVSFPPWRDIDSVTFVPRNLSNCSAHGLAVIVAGNQTWYVNPFSLAHLLDAIYNVLGIEDLSANFRRQLAPYRHTLIVPQT", "text": "FUNCTION: Chaperone protein that cooperates with UL148 to regulate the abundance of gH complexes in virion (PubMed:33889136, PubMed:26937030). First interactor of gH in the host endoplasmic reticulum, regulates the early folding steps of virion assembly. Then, UL148 is recruited and favors the binding of gL (PubMed:34011552). SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum Note=First localizes to the cellular site of virus assembly and then inserts into the virion envelope. SIMILARITY: Belongs to the HHV-5 UL116 protein family."}
{"protein": "MKYLAAYLLLTVGGKQSPSASDIESVLSTVGIEAEAERVESLISELNGKNIEELIAAGNEKLSTVPSAGAVATPAAGGAAGAEATSAAEEAKEEEAAEESDEDMGFGLFD", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family."}
{"protein": "MKLLMLCREPRLYSCQRLKESAEDNGHQIDILDPNRCLLKLSKNAPHFELYYQVNSKSEPYLLPDYDAIIPRFGSTSTRMGCAVLRHFRTKNIFCLNDDVAFLKARDKWLSLQLLTEQGIAVPNSALSGAEFSATQAILQIQSPTILKTLHGSQGIGVILAENRKSAVSIMETLTQADVPLLMQDFIQEAQGTDIRCFVIGDKVVATMQRIGQEDEFRANFHRGGSAEKIQLTEQEKVLALKATKCLGLDVAGVDLIRSKQGLLVLEVNASPGLEMIEKTSGIDIALQMIVHIEKQFKR", "text": "SIMILARITY: Belongs to the RimK family."}
{"protein": "MSFVSKSPPIVNSASPTGQVNPMEVEKANKLLEINRLILWKCLELQHIKTAQNSTLEQRALSTELFNSYIQRLKANLAFVVSIASPRQMQVLTPPLSCPESLPQLEPLYKELRQYFQIAQTSTLSYPPSNGDSSSYANGTDLHGNTGTMQQEEKANPSLTRSDSVSSGSYITMQGANSLKAQQDLLNSFTGAPSNNSHNIPDPNLSQTFSATSMGPPNNNYSKFRTDNYLARSSNRSGTPNIQNEQSRFFDSQQAQVQARALMQRYQQGMEFNK", "text": "FUNCTION: Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MEEAPRRRPGGSREAEGIFRYYEDWECWDHVSQRVPNEVLQRWLAMLTNNQLRRKVIREAQIWMWKNANAPIRRNCGCRLCNPGWGSQVRDVEL", "text": "FUNCTION: Seems to function as a Vpr-like protein, since it mediates host cell cycle arrest in G2 phase. Cell cycle arrest creates a favorable environment for maximizing viral expression and production (By similarity). SUBCELLULAR LOCATION: Virion Host nucleus."}
{"protein": "MGGWSSKHRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPNKDHWPEANQVGAGAFGPGFTPPHGGFLGWSPQAQGILTTVPAAPPPASTNRQSGRQPTPISPPLRDTHPQAMQWNSTAFHQALQDPRVRGLYFPAGGSSSGTVNPVPNTVSHISSIFTKTGDPASNMESTTSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGAPGCIGQNSQSQTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPGSTTTSTGPCRTCTITAQGTSMFPSCCCTKPSDGNCTCIPIPSSWGFAKFLWEWASVRFSWLSLLVPFVQWFAGLSPTVWLSVIWMIWYWGPSLYNILSPFLPLLPIFLCLWVYI", "text": "FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. SUBCELLULAR LOCATION: Virion membrane. SIMILARITY: Belongs to the orthohepadnavirus major surface antigen family."}
{"protein": "MDPFSQLSQLQQNLQAMTKTVAGLENDMLEVLKENTELKVENQLLREKISKLDANKEPAENKSQAGLKSLRNIYDSGYHICNMYYGSHRESGEDCMFCLDILDNFVNHGQKNRG", "text": "FUNCTION: Involved in initiation control of chromosome replication. SIMILARITY: Belongs to the YabA family."}
{"protein": "MDPRECVCMSGGICMCGDNCKCTTCNCKTYWKSCCPCCPPGCAKCARGCICKGGSDKCSCCP", "text": "FUNCTION: Seems to bind zinc and copper. Could play a special role in regulating zinc metabolism during the differentiation of stratified epithelia. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family."}
{"protein": "MLFLGAGELGKEVAIELMRLGAWVCAADSYAGAPAQQVAHEYRALDMANAAELQALFDEIKPDIIVPEVEAIATDVLAGTAAAGAQVVPSAEIAAICMDRERLRVLAHEELGLPTTPYRFAGSLEELRAGASEVGYPCVVKPVMSSSGHGQSVVRSADAIDAAWTEAQEGRRAADEGDVSRVIVEALAPLERELTVLTVSSSAGIVTCAPIGQRQESGDYRESWQPATEPDGEAERARDIARTAVEGLVAKAQAAGETGWGVFGVELFVLTDGSILFNEVSPRPHDTGMVTMASQRLSEFALHARAILGLPITPEHVSLTIPAGSVAASHAIVVAGDGEVEFTDVAAALAEPGTDLRIFAKPEVHGHRRMAVALAVGESEADARAKAGLVADALTITVE", "text": "FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. SIMILARITY: Belongs to the PurK/PurT family."}
{"protein": "MAVLCGVCGIKEFKYKCPRCLVQTCSLECSKKHKTRDNCSGQTHDPKEYISSEALKQADDDKHERNAYVQRDYNYLTQLKRMVHVQKMDARMKNKRVLGPVGGHNSNFKKRRYDIDEDDRDSTECQRIIRRGVNCLMLPKGMQRSSQNRSKWDKTMDLFVWSVEWILCPMQEKGEKKELFKHVSHRIKETDFLVQGMGKNVFQKCCEFYRLAGTSSCIEGEDGSETKEERTQILQKSGLKFYTKTFPYNTTHIMDSKKLVELAIHEKCIGELLKNTTVIEFPTIFVAMTEADLPEGYEVLHQEPRPLEHTSTLNKFIDNAREEEDAEEDSQPTEEPVQKETQDASDSDSDSDDDYNPGLSMDFLTA", "text": "FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BCD1 family."}
{"protein": "MVTIANAHDELIHDAVLDYYGKRLATCSSDKTIKIFEVEGTENYQLTETLVGHEGPVWQVAWAHPKFGSILASCSYDGKVLVWKESPDRSWSIISEHKVHQASVNSVSWAPHELGAVLLCTSSDGRVSVVDFNDDGTSTHIIFEAHKIGVNSASWAPVDTKSPVRRFVTGGSDNLAKVWSLDASKSTYVEEAKLEGHTDWVRDVCWSPSALVRSYIATASQDRTVLIWHQDGEGKWQKQKLTEELFPDVCWRCSWSFSGNILAVSGGDNKVSLWKENLQGKWESAGEVDQ", "text": "FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Nucleus, nuclear pore complex. SIMILARITY: Belongs to the WD repeat SEC13 family."}
{"protein": "MCLSLGQRCGRHSNCCGYLCCFYDKCVVTAIGCGHY", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin I1 superfamily."}
{"protein": "MVFLKRFRAYGFKSYADEITINFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEVELTFDNSQKLLHDPRPEISVMRRIYRGSGQSEYYINGELVTLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRKIFEDASGIGRYTKRKEEVTNQLARTVQNLKQVSIVLNELKKDLKKLTIQADKAQRFVKLKEELKELELSVLVADYLKSQGELDRFNHQIGYIEQDFKLHEPQLQLLEDQLNIFNQRFRDADEQSIKLQQELQAVYQTINELEQRKAVIDVQLKNELSKKDEKHKIQALKKLIRVDQAQLESLQAQVLKTTSEITLLTNELSTVQTELDTTKLNLNQNSAALVYQQAQQEFLKAQNEEWVKTNPAHVLVKNVKALTGLLNTLNTFLKFEKQYEKALLKALGKSIGYLVVNNNLAALKAIDFLLTNQIGQVTFLPIDDIAFDTKIAPEHMEILQQLDGFLGVGSDHVSCDESLQPIVNALLGQVIIASDLQAALKLSSYTYKLYRVVTLNGETVYAGGIIQGGYVKDNLSLYNLQEKLASSEANITQLEHNEKQLRTNLTSLETKLNELNKKLKYEEILLEKFNERVNHTNKAILSYKIEYEQLTNESFDGTPHSFDETRLVESLNRAWAERDELNSQLKLNQELKETLAKSIKLAEAKTADLRALLDEQRSQLVLAREGKIRFENTIHNITDKINGGYKLTMEFAIANYNKPIKLSTMQAQNKIARMQSQLDEMGPINLESIAEIADKQKRFDDINGEYESLQTAIKDLQTAIGEIDELACKEFDELIQKVNAELPKTFNYLFGGGSCQIRYTDTDNVLLSGIEVFANPPGKNVANLMLLSGGEKTLVALSVLFSILRVSAFPLVILDEAESALDPANVERFANIIGNSSNNTQFLIITHRQGTMMKCDMLLGAAMQTKGVTKTFAVSLEKAEQYISKDKQN", "text": "FUNCTION: Required for chromosome condensation and partitioning. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SMC family."}
{"protein": "MAQKHPGERGLYGAHHSGGASLRTLGPSVDPEIPSFSGLRDSAGTAPNGTRCLTEHSGPKHTQHPNPAHWLDPSHGPPGGPGPPRDAEDPDQSETSSEEESGVDQELSKENETGNQKDGNSFLSIPSACNCQGTPGIPEGPYSEGGNGSSSNFCHHCTSPALGEDELEEEYDDEESLKFPSDFSRVSSGKKPPSRRQRHRFPTKEDTREGGRRDPRSPGRHRLGRKRSQADKRKGLGLWGAEELCQLGQAGFWWLIELLVLVGEYVETCGHLIYACRQLKSSDLDLFRVWMGVWTGRLGGWAQVMFQFLSQGFYCGVGLFTRFLKLLGALLLLALALFLGFLQLGWRFLVGLGDRLGWRDKATWLFSWLDSPALQRCLTLLRDSRPWQRLVRIVQWGWLELPWVKQNINRQGNAPVASGRYCQPEEEVARLLTMAGVPEDELNPFHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYEMKRMAENELSRSVNEFLSKLQDDLKEAMNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQRVGISPDTHRVPYHISFGSRIPGTRGRQRATPDAPPADLQDFLSRIFQVPPGQMPNGNFFAAPQPAPGAAAASKPNSTVPKGEAKPKRRKKVRRPFQR", "text": "FUNCTION: Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
{"protein": "MLEYLLLLISTVLVNNFVLVKFLGLCPFMGVSKKIEPAVGMGLATTFVLTLTSAFAYLVQHYLLVPLAAESLSTLAFILVIAVVVQFTEMVIHKSAPDLYRILGIYLPLITTNCIVLGLALLNITMQHNFMQSVVYGFGGGLGFMLVLILFASLRERLAAADVPAPFQGIAIGMVTAGLMSLAFLGFTGLIKL", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrDE/RnfAE family."}
{"protein": "MGSSKDSASVTNISVEEHFSVSQSSPGGQFVGPTEEISTAAEALIGRSTTLTEALKAASMNVGHKPVETTDVAAIKEVETRAIGGDIESEGGVTAVASKAVARNQKIGKDNEKTNLGDVIAEIDVKVTRDREVTSEDAEAVIRAELNHSPFNNIIPGGVAESVAAAYKLNHDPSSL", "text": "FUNCTION: LEA proteins are late embryonic proteins abundant in higher plant seed embryos. The function of those proteins is not known. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the LEA type SMP family."}
{"protein": "MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ", "text": "FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MEVVKDIAESYGAERIYTVGDVVTQNFFKHGLIPTSAAVDEKTRRGVRIEQLAVFKRVIKVNNPPGYITEEAWSAVEEAVRGGVIIKVEGEEDMLSLAFIKLAPPKSIVAYGHYLGALIALPVDWYKEYVLKLFDYLEKC", "text": "FUNCTION: Catalyzes the GTP-dependent phosphorylation of the 3'- hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). SIMILARITY: Belongs to the GTP-dependent DPCK family."}
{"protein": "MASRGKSETIKLRQNLEEQLDRLMQQLQDLEECREELDGDEYEETKKETLEQLSEFNDSLKKIMSGNMTLIDELGGMQLAIQAAISQAFKTPEVIRMFAKKQPGQLRTRLAELDRDLMVGKLGRDLYTQQKGEILIALQKLGEKLSPEDEAFLSENAGAVFNQFQKVSEGLGSGDKVLALASIEVENTRK", "text": "SIMILARITY: Belongs to the CTNNBIP1 family."}
{"protein": "NCCPIDEESCCS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin T superfamily."}
{"protein": "MRIVIYSMLVLLIAIQYPLWLGKGGWLKVYEMEKQVELQEAKNSLLALRNAKLEGDVKDLKDGTRAIEERARVEHGLIKEGEFFVQILPADQSSADTAKASTVKQ", "text": "FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the FtsB family."}
{"protein": "GFGSLFKFLAKKVAKTVAKQAAKQGAKYIANKQME", "text": "FUNCTION: Has antimicrobial activity against E.coli, E.faecalis, P.aeruginosa, and S.aureus. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane function with its amphipathic structure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 01 subfamily."}
{"protein": "MSLVSGARDMGFDDNNNNKNNKDGDDENSSSRTRADDDALSRQMSESSLCATEEEEDDDSKLQLGPQYTIKEHLEKDKDDESLRKWKEQLLGSVDVTNIGETLDPEVRIDSLAIISPGRPDIVLLVPENGNPKGMWFTLKEGSKYNLKFTFHVNNNIVSGLRYTNTVWKTGVKVDRAKEMLGTFSPQLEPYNHVMPEETTPSGMFARGSYSARTKFLDDDNKCYLEINYSFDIRKEWPAL", "text": "FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rho GDI family."}
{"protein": "MPQSPRPVPSWALLLRLLALLRPPGLGEACSCAPAHPQQHVCHSALAIRAKISSEKVVPASTDPADPQKMIRYEIKQIKMFKGFEKVNDIQYIYTPFDSSLCGVKLEANSQKRYLLTGQILSDGKVFVHLCNYIEPWENLSFLQRESLNHHYHLNCGCQITTCYAVPCTISAPNECLWTDWLLERKLYGYQAQHYVCMKHVDGSCSWYQGRLPLRKEFVDIIQP", "text": "FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family."}
{"protein": "MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHGESGLDGPALPEPAFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWTPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKWGFVGAPLHDPCTIAWLLKPELFTTVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLKFYA", "text": "FUNCTION: Hydrolyzes with equal efficiency cytidine or uridine to ribose and cytosine or uracil, respectively. SIMILARITY: Belongs to the IUNH family. RihA subfamily."}
{"protein": "MNAPHPASAALTQTLAARPTLAELEARDAFAERHIGPSPDEQAAMLATLGYASRAALIDAVIPPAIRRQDGMPLGEFTQPLTEEAALAKLRGIAGQNRVVRSLIGQGYYGTHTPGVILRNILENPAWYTAYTPYQPEISQGRLEAMLNFQQMVMDLTAMDIANASMLDEATAAAEAMTLLQRVGKHPSNVFFVADDVLPQTLDVVRTRAEPIGVQVVTGPAADAAKHNAFGVLLQYPGTGGALLGGLSTYQALTDAVHAAGGLVVAAADLLALTLLAAPGEWGADVVIGNTQRFGVPFGFGGPHAGYMAVRDAFKRSMPGRLVGVTVDAQGNPAYRLALQTREQHIRREKATSNICTAQVLLGVMASMYAVYHGPQGLKRIAQRVHRLTATLAAGLRQIGYTLEAGAFFDTLTVATGPRTANLHIAAQAHGFNLRQIDDGRLGVSLDETVTRAEVVALWEIFAHAAHAGAPDFDQVEAGIADAFPASLARQSAYLTHPVFNAHHSEHEMLRYLRSLADKDLALDRTMIPLGSCTMKLNATAEMLPVTWPEFANIHPFAPADQTVGYREMIDQLEQMLCAATGYAAVSLQPNAGSQGEYAGLLIIHAYHASRGESHRDVCLIPSSAHGTNPASAQMAGMKVVVVACDERGNVDLADLEKKAAEHSANLAAIMITYPSTHGVFEEGVKRVCEIVHSHGGQVYVDGANMNAMVGTAAPGHFGGDVSHLNLHKTFCIPHGGGGPGVGPVAVGAHLAPFLPGRAASGEDASQNIGAVSAAPFGSASILPISWMYIAMMGAAGLTAATEAAILSANYVARRLSPYYPVLYTGAHGLVAHECILDIRPLQKESGISNEDIAKRLMDFGFHAPTMSFPVPGTLMIEPTESEPKVELDRFIDAMIAIRGEVDQVISGAFDREDNPLKHAPHTAQVVMADDWSHRYTREQAAYPVASLRTRKYWPPVGRADNVYGDRNLFCACVPMSEYAQD", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. SIMILARITY: Belongs to the GcvP family."}
{"protein": "MTRVVLAAAYRTPIGVFGGAFKDVPAYDLGATLIEHIIKETGLNPSEINEVIIGNVLQAGQGQNPARIAAMKGGLPETVPAFTVNKVCGSGLKSIQLAYQSIVTGENDIVLAGGMENMSQSPMLVNNSRFGFKMGHQSMVDSMVYDGLTDVFNQYHMGITAENLVEQYGISREEQDTFAVNSQQKAVRAQQNGEFDSEIVPVSIPQRKGEPIVVTKDEGVRENVSVEKLSRLRPAFKKDGTVTAGNASGINDGAAMMLVMSEDKAKELNIEPLAVLDGFGSHGVDPAIMGIAPVDAVEKALKRSKKELSDIDVFELNEAFAAQSLAVDRELKLPPEKVNVKGGAIALGHPIGASGARVLVTLLHQLNDEVETGLTSLCIGGGQAIAAVVSKYK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MNTEATHDQNEALTTGARLRNAREQLGLSQQAVAERLCLKVSTVRDIEEDKAPADLASTFLRGYIRSYARLVHIPEEELQPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMTFTWLVLFVVIGLSGAWWWQDHKAQQEEITTMADQSSAELNNNQSQSVPLDTSTTTDQAMATTPTSPVDTTATNTQTPAVTAPAPAVDPQQNAVVPPSQANVDTAATPAPAATTTPDGAAPLPTDQAGVTTPAVDPNALVMNFTADCWLEVTDATGKKLFSGMQRKDGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAEQSPAQ", "text": "FUNCTION: Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Forms helical filaments along the long axis of the cell. SIMILARITY: Belongs to the RodZ family."}
{"protein": "MMSMASTTASPFCPSPMPRGRKCTVRVQAGAAGADASDKSLEIMRKFSEQYARRSNTFFCSEKSVTAVVIKGLADHKDQLGAPLCPCRHYDDKAAEVAQGFWNCPCVPMRERKECHCMLFLTPDNDFAGQDQAITLEEIKDATSKI", "text": "FUNCTION: Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta subunit family."}
{"protein": "MSSKLRVGVAGPVGSGKTALLETLCLSLKKNYEIAVVTNDIYTKEDANFLINKKVLEEGRIIGVETGGCPHTAIREDCSLNKNAVLDLENKYNPLDFVFVESGGDNLASSFSPELVDLSIYVIDVSAGDKIPRKGGPGITRSDLLLINKIDLADMVGADLNIMKSDTEFMRKGKPWFFTNLSIGKGVKEISQFLESHLPNNQN", "text": "FUNCTION: Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG subfamily."}
{"protein": "MVKLAFPRELRLLTPSQFTFVFQQPQRAGTPQITILGRLNSLGHPRIGLTVAKKNVRRAHERNRIKRLTRESFRLRQHELPAMDFVVVAKKGVADLDNRALSEALEKLWRRHCRLARGS", "text": "FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. SIMILARITY: Belongs to the RnpA family."}
{"protein": "MTAISSPINLFEYEQLAKTHLSQMAFDYYISGAGDEITLQENRAVFERIKLRPRMLVDVSQINLTTSVLGQPLQLPLLIAPMAFQCLAHTEGELATAMAAASAGTGMVLSTLSTKSLEEVAEVGSKFSPSLQWFQLYIHKDRGLTRALVERAYAAGYKALCLTVDAPVLGQRERDRRNEFVLPPGLHLANLTTISGLNIPHAPGESGLFTYFAQQLNPALTWDDLEWLQSLSPLPLVLKGILRGDDAARAVEYGAKAIVVSNHGGRQLDGAIASLDALPEIVAAVNGKAEVLLDGGIRRGTDIIKALAIGAQAVLIGRPVLWGLAVGGQAGVSHVISLLQKELNVAMALIGCSQLQDIDTSFLHL", "text": "FUNCTION: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. In extant N2-fixing cyanobacteria such as Nostoc, this enzyme primarily serves as an O2- scavenging enzyme, protecting nitrogenase that is extremely sensitive to O2, and is therefore an essential partner in N2 fixation. Also shows clear oxidase activity with glyoxylate in vitro, and low activity with glycerate, hydroxypyruvate and glycolate. The very low glycolate oxidase activity indicates that this enzyme is unlikely to be involved in photorespiratory glycolate metabolism, a pathway that seems to exist in this cyanobacterium, but in which the oxidation of glycolate is taken over by glycolate dehydrogenase (GlcD). Is not able to use D- lactate as substrate and does not show any dehydrogenase activity with NAD(+) or NADP(+). SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
{"protein": "MRPLTHEETKTFFEKLAQYIGKNITHLIDRPDDPHCFRLQKDRVYYVSERAMKMATSVARQNLMSLGICFGKFTKTNKFRLHITALDYIAQYARYKIWVKSNGEMPFLYGNHVLKAHVGRITDDTPQHQGVVIYSMNDTPLGFGVTARSTLELRRLEPTAIVAFHQADVGEYLRDEDTLF", "text": "FUNCTION: Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the NIP7 family."}
{"protein": "MSPIEKSSKLENVCYDIRGPVLKEAKRLEEEGNKVLKLNIGNPAPFGFDAPDEILVDVIRNLPTAQGYCDSKGLYSARKAIMQHYQARGMRDVTVEDIYIGNGVSELIVQAMQALLNSGDEMLVPAPDYPLWTAAVSLSSGKAVHYLCDESSDWFPDLDDIRAKITPRTRGIVIINPNNPTGAVYSKELLMEIVEIARQHNLIIFADEIYDKILYDDAEHHSIAPLAPDLLTITFNGLSKTYRVAGFRQGWMVLNGPKKHAKGYIEGLEMLASMRLCANVPAQHAIQTALGGYQSISEFITPGGRLYEQRNRAWELINDIPGVSCVKPRGALYMFPKIDAKRFNIHDDQKMVLDFLLQEKVLLVQGTAFNWPWPDHFRIVTLPRVDDIELSLSKFARFLSGYHQL", "text": "FUNCTION: Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L- alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction. FUNCTION: Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L- alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWIRAIQMVANSLKQRGPGEDAMDYKCGSPSDSSTSEMMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGDLFFHLSRERVFTEDRARFYGAEIVSALEYLHSTDVVYRDIKLENLMLDKDGHIKITDFGLSKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLGPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGSLELDQRTHFPQFSYSASIRE", "text": "FUNCTION: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E- BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF- kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P- 5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet- derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. FUNCTION: One of the few specific substrates of AKT2 identified so far is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Phosphorylates CLK2 on 'Thr-343'. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane; Peripheral membrane protein Early endosome Note=Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N- terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3. Colocalizes with WDFY2 in early endosomes. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily."}
{"protein": "MFMTKDLFFVYIFTTMIKLVVLDVDGTLTDKSRMISVNAVNAIRNLKTKVALVSGNVLPVLYGLKIYIGFDGYIFAENGGIALINNNIEKFFEKDGPESFLNDISGYTSARGILTNRWRETSMAFTANHDEMDIIDREAASRDLYIVDSGFTLHILNKGQDKGFAVKKMIDIMNIDYNNVLVIGDSQNDESMFSLGTLSACPGNASEKIKEMSNYVSGKCYGDELFDVFRHFDLIH", "text": "FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate. SIMILARITY: Belongs to the archaeal SPP-like hydrolase family."}
{"protein": "MSTEGGGRRCQAQVSRRISFSASHRLYSKFLSDEENLKLFGKCNNPNGHGHNYKVVVTVHGEIDPATGMVMNLADLKKYMEEAIMQPLDHKNLDMDVPYFADVVSTTENVAVYIWDNLQKVLPVGVLYKVKVYETDNNIVVYKGE", "text": "FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. SIMILARITY: Belongs to the PTPS family."}
{"protein": "MKVEIFCDGACSGNPGVGGWGSILRYGDTVKELSGADGDTTNNRMEMTAAIEALASLKRPCEVVLTTDSQYLVKGMTEWMSGWIRKGWVNSKKEPVLNRELWERLLALSKIHKIRWAWVRGHNGHPENERCDELARAAIEVFKGRKP", "text": "FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase H family."}
{"protein": "MAFAVWFLSTFVIVAAQRHMALEHEGTYNIGGVLTNSDSEEHFRTTIAHLNFDQQYVPRKVTYYEKTIRMDKNPIKTVFNVCNKLIEKRVYAVVVSHEQTSGDLSPAAVSYTSGFYSIPVIGISSRDAAFSDKNIHVSFLRTVPPYYHQADVWLEMLSHFSYTKVIIIHSSDTDGRAILGRFQTTSQTYYDDVDVRATVEMIVEFEPKLTSFSEHLTYMKTAQSRVYLMYASTEDAQIIFRDARDHNMTQEGHVWIVTEQALFANNTPEGVLGLQLEHAHSDKGHIRDSVYVLASAIKEMISNETIAEAPKDCGDSAVNWESGKRLFQYLKTRNITGETGQVAFDDNGDRIYAGYDVINIRENQKQHVVGKFSYDNMRAKMRMKINDSEIIWAGKQKRKPEGIMIPTHLKLLTIEEKPFVYVRRMGDDEFHCEPNERPCPLFNTTDATANEFCCSGYCIDLLIELAKRINFTYDLALSPDGQFGHYILRNNTGATLRKEWTGLIGQLVNERADMIVAPLTINPERAEYIEFSKPFKYQGITILEKKPSRSSTLVSFLQPFSNTLWILVMVSVHVVALVLYLLDRFSPFGRFKLSHSDSNEEKALNLSSAVWFAWGVLLNSGIGEGTPRSFSARVLGMVWAGFAMIIVASYTANLAAFLVLERPKTKLSGINDARLRNTMENLTCATVKGSSVDMYFRRQVELSNMYRTMEANNYATAEHAIQDVKKGKLMAFIWDSSRLEYEASKDCELVTAGELFGRSGYGIGLQKGSPWTDAVTLAILEFHESGFMEKLDKQWIFHGHVQQNCELFEKTPNTLGLKNMAGVFILVGVGIAGGVGLIIIEVIYKKHQVKKQKRLDIARHAADKWRGTIEKRKTIRASLAMQRQYNVGLNSRAPGTISLAVDKKRYPRLSQRMGPERAWPGDAAEVLRMRRPYEIGKPGQSPKVIGGPPHPMLGKTRPQAQQNLLPPRYSPGYTSDVSHLVV", "text": "FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors. Plays a role in associative learning and in long-term memory consolidation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane Postsynaptic density. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family."}
{"protein": "MARFTLHDLAATVDARAASGGESSYTKKLLDKGPEHCAKKFGEEAVEMVIAAVENDRGHLISETADVLFHMLVLLKSRGVKLEEVEAALAQRTSMSGLEEKASRKRD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family."}
{"protein": "MIKDNDNSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLNRTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICRNPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKGGRIIWISSLMSNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFFKFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCALGNESQSVKVCSVSNRTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP", "text": "FUNCTION: Responsible for the reduction of the keto group on the C-3 of sterols. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily."}
{"protein": "MELLLPHPSNSTPLTVLGFLDRAASVYGDCPSILHTANTVHTWSETHNRCLRIASALTSSSIGIKQGQVVSVVGPNVPSVYELQFAVPMSGAILNNINPRLDAHALSVLLRHSESRLVFVDHRSISLVLEAVSLFTQHEKPHLVLLDDDQENDSSSASDFLDTYEEIMERGNSRFKWIRPQTEWQPMVLNYTSGTTSSPKGVVLSHRAIFMLTVSSLLDWSVPNRPVYLWTLPMFHANGWGYTWGTAAVGATNICTRRVDAPTIYNLIDKHNVTHMCAAPMVLNMLINYPLSTPLKNPVQVMTSGAPPPATIISRAESLGFNVSHSYGLTETSGPVVSCAWKPKWDHLDPLERARLKSRQGVRTLGFTEVDVRDRKTGKSVKHDGVSVGEIVFRGSSVMLGYYKDPQGTAACMREDGWFYSGDIGVIHKDGYLEIKDRSKDVIICGGENISSAEIETVLYTNPVVKEAAVVAKPDKMWGETPCAFVSLKCDNNGDGSVPVTEREIREFCKTKLPKYMVPRKVIFQEELPKTSTGKIQKFLLRQMAKTLS", "text": "FUNCTION: May act as an acid--thiol ligase that activates carboxylic acids by forming acyl-CoAs. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MQTIRKSLGLVLIMFVLCGFIFPLTVTALGQVLFPEQANGSLVKQDGKVIGSKLIGQQWTEPKYFHGRISAVNYNMNANEVKESGGPASGGSNYGNSNPELKKRVQETIKQEGQKLSSDAVTTSGSGLDPDITVDNAKQQVKCIAKERNIDASKINHLIDENKQASPMADDYVNVLKLNITLDKL", "text": "FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the KdpC family."}
{"protein": "MASNIRIIFYGTGGSWPTPLRAMPGVGVKIDDVLNLFDCGEGTQKQIMKSSTSFMDIDNIFITHFHGDHFLGLLGLVQSMSFNNRTKQLNIFGPHGAIKILSNALNVGYYTLHFPLKIYELEPDRTYDLGKFLIRTMLNDHPVPALSYSIEERDLVRIDPEKAREKNIPSRIIEKIRENGSYVYKGNEYRIDDIAGGVRKGRRIVYTGDTRPMDRMIEFARNADVLIHDTTTDSSFEPMVNEFGHSSSRQAARIARQARVGRLYLYHYSPRITDTSVLLEDARKEFQETYESKDLMEYEVKVRRDVD", "text": "FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. SIMILARITY: Belongs to the RNase Z family."}
{"protein": "MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYPDFPFPEDYPNYVPNSHFLEYLRMYANQFNLLKCIQFKTKVCSVTKHEDFNTTGQWDVVTLCEGKQESAVFDAVMVCTGFLTNPYLPLDSFPGINTFKGQYFHSRQYKHPDIFKDKSVLVVGMGNSGTDIAVEASHLAKKVFLSTTGGAWVISRVFDSGYPWDMVFMTRFQNMFRNSLPTPIVNWLIAKKMNSWFNHANYGLIPEDRIQLREPVLNDELPGRIITGKVLIKPSIKEVKENSVVFNSSPEEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAVIGLIKPLGSLLPTGDTQARWAVRVLKGVNKLPPSSVMIQEVNTRKENKPSGFGLCYCKALQSDYIAYIDELLTYIDAKPNMFSLLLTDPHLALTIFFGPCTPYQFRLTGPGKWEGARNAIMTQWDRTFKVTKTRIVKESPSPFASLLKLFSFLALLVAIFQIFL", "text": "FUNCTION: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics (PubMed:7758472). Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes (By similarity). In vitro, catalyzes the N- oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L- carnitine (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FMO family."}
{"protein": "MKSLILLAILAALAVVTLCYESHESMESYELNPFINRRNANTFISPQQRWRAKVQERIRERSKPVHELNREACDDYRLCERYAMVYGYNAAYNRYFRKRRGTK", "text": "FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family."}
{"protein": "MKPSKSHHKEKTARRREEKLEESDNPKYRDRAKERRENQNPDYDPSELSSFHAVAPPGAVDIRAADALKISIENSKYLGGDVEHTHLVKGLDYALLNKVRSEIVKKPDGEDGDGGKTSAPKEDQRVTFRTIAAKSVYQWIVKPQTIIKSNEMFLPGRMTFVYDMEGGYTHDIPTTLYRSKADCPVPEEFVTVNVDGSVLDRIAKIMSYLRLGSSGKVLKKKKKEKDGKGKMSTIANDYDEDDNKSKIENGSSVNISDREVLPPPPPLPPGINHLDLSTKQEEPPVARTDDDDIFVGEGVDYTVPGKDVTQSPISEDMEESPRDKEKVSYFDEPAYGPVQEKVPYFAEPAYGPVQPSAGQEWQDMSAYGAMQTQGLAPGYPGEWQEYQYAEQTGYQEQYLQPGMEGYEVQPETDVLLDPQLMSQEEKDRGLGSVFKRDDQRLQQLRESDAREKDPTFVSESYSECYPGYQEYNHEIVGSDEEPDLSKMDMGGKAKGGLHRWDFETEEEWEKYNEQKEAMPKAAFQFGVKMQDGRKTRKQNRDRDQKLNNELHQINKILTRKKMEKEGGDVASLDAAEAQTPKRSKH", "text": "FUNCTION: Auxiliary spliceosomal protein involved in splicing of specific pre-mRNAs that affect multiple aspects of development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RED family."}
{"protein": "MAQDDEDVGLALGLSLGSGGHRRQRESRDEAPSSAAASLLTLRLPAESGGQPQVVVKREVVRAEEEEYEYEYERALYSSSAAAADDDEGCNSRKKLRLSKEQSALLEDRFKEHSTLNPKQKVALAKQLNLRPRQVEVWFQNRRARTKLKQTEVDCELLKRCCETLTEENRRLHRELQQLRALTHSTAAGFFMATTLPVPAATLSICPSCERLATAAAAGASPTAAADRTNKPTAPHLFSPFAKSAAC", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class II subfamily."}
{"protein": "MPEQGPRMNGFSLGELCWLFCCPPCPSRIAAKLAFLPPEPTYTVREMEAPASTAQQPPREEGSGEPAACSLHLSERADWQYSQRELDAVEVFRWRTERGSFLGCMFVRCSPGSRYTLLFSHGNAVDLGQMCSFYIGLGTRINCNIFSYDYSGYGVSSGKPSEKNLYADIEAAWHALRTRYGVTPENIILYGQSIGTVPTVDLASRYECAAVILHSPLMSGLRVAFPDTRKTYCFDAFPSIDKISKVTSPVLIIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDIELYAQYLERLKQFISHELPNS", "text": "FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS. SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Cell projection, dendritic spine Postsynaptic density membrane. SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family."}
{"protein": "MSNQHSPQPFCLDTKLVKLLEELQEGKQFNNKNIFPEKALYLKLALDYSFFRKNLLEFCVHLDKIKGVIRPNYDTIYILCLLEVDLLNLVFTDNILEICLPRFVSREDLRVFNNTFYTYHDNRLRILQEDFSQLFKKIKTKASVLCFTVEEIFLTNQEILPQNSTVAELQKSTNKVQTNGPQRHDFIVTLEIKLNKTQITFLIGAKGTRIESLREKSGASIKIIPISDKMTAHERNHPESVQQTILISGDLYSIALAVTSIESALITLDL", "text": "FUNCTION: Required for chromosome pairing and genetic recombination. MER1 may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product."}
{"protein": "MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK", "text": "FUNCTION: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys. FUNCTION: Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (PubMed:15546957, PubMed:16709924, PubMed:19380772). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival (By similarity). In humans, the immunological role in the monocytic/macrophage/dendritic cell (DC) lineage is unsure. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic granule Note=Localized in azurophil granules of neutrophils (PubMed:15546957). SIMILARITY: Belongs to the arginase family."}
{"protein": "MSTLADLRKNYSLGSLDISDVDPNPFGQFDRWFKQAIDAQLPEPNTMTLATADARGRPSARIVLIKGVDERGFVFFTNYESRKGQELAQNPHASLLFYWIELERQVRIEGTVVKTSPEESDAYFASRPVGSRIGAWASEQSKVIESRAALEAREREFSAQYGENPPRPPHWGGYRLIPDAIEFWQGRPSRLHDRLLYTHSGGAGWTITRLSP", "text": "FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family."}
{"protein": "MKMINLDSKKLASFYVACELFKQIQQYPHTKLGLATGGTMTDVYHYLVNLLTKNKADVSQVETFNLDEYVGLKASHQQSYHTYMNKVLFEQYPHFAKNHIHIPDGYSENLEAEAERYNKLLDERGPIDIQILGIGENGHIGFNEPGTDFNSETHVVNLTESTIKANSRYFDNEADVPRQAVSMGLASILKAKRIILLAFGPKKKEAISKLLNEQVTEDVPATILHTHPNVEVYVDDDAAPDCL", "text": "FUNCTION: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily."}
{"protein": "MATRGGGGGGGGKEAKGKVMGPLFPRLHVNDAAKGGGPRAPPRNKMALYEQFTVPSHRFSGGGGGGGVGGSPAHSTSAASQSQSQSQVYGRDSSLFQPFNVPSNRPGHSTEKINSDKINKKISGSRKELGMLSSQTKGMDIYASRSTAEAPQRRAENTIKSSSGKRLADDDEFMVPSVFNSRFPQYSTQENAGVQDQSTPLVAANPHKSPSTVSKSSTKCYNTVSKKLERIHVSDVKSRTPLKDKEMEAAQTSKNVEVEKSSSFHASKDMFESRHAKVYPKMDKTGIINDSDEPHGGNSGHQATSRNGGSMKFQNPPMRRNEISSNPSSENTDRHYNLPQGGIEETGTKRKRLLEQHDAEKSDDVSRLLEQHDAENIDDVSDSSVECITGWEISPDKIVGAIGTKHFWKARRAIMNQQRVFAVQVFELHKLVKVQKLIAASPHVLIESDPCLGNALLGSKNKLVEENLKAQPLLVATIDDVEPSLQQPEVSKENTEDSPPSPHDTGLGSGQRDQAATNGVSKSNRRATPVASDNKQNNWGVQLQPPQNQWLVPVMSPLEGLVYKPYSGPCPPAGSILAPFYANCTPLSLPSTAGDFMNSAYGVPMPHQPQHMGAPGPPSMPMNYFPPFSIPVMNPTAPAPVVEQGRHPSMPQPYGNFEQQSWISCNMSHPSGIWRFHASRDSEAQASSASSPFDRFQCSGSGPVSAFPTVSAQNNQPQPSYSSRDNQTNVIKVVPHNSRTASESAARIFRSIQMERQRDD", "text": "FUNCTION: Involved in the regulation of flowering time under short day (SD) and long day (LD) conditions. Functions as floral promoter by negatively regulating GHD7, a repressor of the photoperiodic control of flowering (PubMed:22399582, PubMed:22422935, PubMed:22912900). Acts as floral activator in the LD photoperiodic pathway (PubMed:22888152). Involved in blue light-induced activation of EHD1 expression to promote flowering under SD conditions (PubMed:22912900). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISSGRDDLSPSSSLNGYSANESCDAKKSKKGPAPRVQEELCLVCGDRASGYHYNALTCEGCKGFFRRSVTKSAVYCCKFGRACEMDMYMRRKCQECRLKKCLAVGMRPECVVPENQCAMKRREKKAQKEKDKMTTSPSSQHGGNGSLASGGGQDFVKKEILDLMTCEPPQHATIPLLPDEILAKCQARNIPSLTYNQLAVIYKLIWYQDGYEQPSEEDLRRIMSQPDENESQTDVSFRHITEITILTVQLIVEFAKGLPAFTKIPQEDQITLLKACSSEVMMLRMARRYDHSSDSIFFANNRSYTRDSYKMAGMADNIEDLLHFCRQMFSMKVDNVEYALLTAIVIFSDRPGLEKAQLVEAIQSYYIDTLRIYILNRHCGDSMSLVFYAKLLSILTELRTLGNQNAEMCFSLKLKNRKLPKFLEEIWDVHAIPPSVQSHLQITQEENERLERAERMRASVGGAITAGIDCDSASTSAAAAAAQHQPQPQPQPQPSSLTQNDSQHQTQPQLQPQLPPQLQGQLQPQLQPQLQTQLQPQIQPQPQLLPVSAPVPASVTAPGSLSAVSTSSEYMGGSAAIGPITPATTSSITAAVTASSTTSAVPMGNGVGVGVGVGGNVSMYANAQTAMALMGVALHSHQEQLIGGVAVKSEHSTTA", "text": "FUNCTION: Receptor for ecdysone (PubMed:1913820, PubMed:30293839). Binds to ecdysone response elements (ECRES) following ecdysone-binding, and recruitment of a complex containing the histone methyltransferase trr, leads to activate transcription of target genes (PubMed:1913820, PubMed:30293839). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MPGLTLGDVVPDLELDTTHGKIRLHDFVGDAYAIIFSHPADFTPVCTTELSEMAGYAGEFDKRGVKLLGFSCDDVESHKDWIKDIEAYKPGRRVGFPIVADPDREAIRQLNMIDADEKDTAGGELPNRALHIVGPDKKVKLSFLFPACTGRNMAEVLRATDALLTAARHRVATPVNWKPGERVVIPPGVSDEEAKARFPAGFETAQLPSNKCYLRFTQVD", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily."}
{"protein": "MSDMSDQTRLSSPPSLPLHKQPQSRYAWLVRSIQLMKPVTWFAPTWAFMCGAIASGALGWNESIGRLLLGMFMAGPILCGLSQVVNDYADREVDAINEPHRLIPSGQVSLRHVYILTAVLTWIGASIALFLGRQVAFFVALGLVFALAYSLRPIRGKRNGWIGNALVAISYEGLAWMAGHAAFAPLTGESVTIALLYSLGAHGIMTVNDFKSIRGDTIMGIRSIPVQYGKVMAARMVVTTMGVAQIAVIGLLFHWGHPVAATVVAILLAAQSIPNARFIRDPENNEVFFNATAIMLYVWGMLAAAIGLAA", "text": "FUNCTION: Catalyzes the esterification of bacteriochlorophyllide a by geranylgeraniol-PPi. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MKAKGFVHKYGDNVDTDVIIPARYLNTANHKELAAHCMEDIDKDFVKKVKTGDIMVGGDNFGCGSSREHAPIAIKESGISCVIASSFARIFYRNSINIGLAILECDEASKKISDNDEVEVDFDNGLIKNITKNETYKAEPFPEFIKKIINSNGLLNSIKNSKG", "text": "FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily."}
{"protein": "MCFGLPNINREGYSFIVVSFIVTCIAFSISWGFGVTCLFPTLLCTYFFRDPARAVPNNKNLILSPADGVISKIEEVNYPLSAENGEEKKFTLVSIFLSVLNVHVNRIPISGTIKEMSYKKGKFVSAMSNRSSNENEKQVIVIEYEKGKEIIVEQIAGLIARRIVCNLGISQNVKAGERFGIIRFGSRVNIYVPADTEVRVSEGQTVIGGETIIANLNKENVQEKLTFDVI", "text": "FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily."}
{"protein": "MSMGILDELDWRGLIAQSTDRETLANDLANGPMTVYSGFDPTAPSLHAGHLVPLLTLRRFQRAGHRPIVLAGGATGMIGDPRDTGERTLNTADTVADWAGRIRGQLERFVEFDDTPTGAIVENNLNWTGRLSAIEFLRDLGKYFSVNVMLDRETVRRRLEGDGISYTEFSYMLLQANDFVELHQRYGCALQIGGSDQWGNIVAGARLVRQKLGATVHAMTTPLVTDSEGKKFGKSTGGGNLWLDPEMTSPYAWYQYFVNTADADVIGYLRWFTFLSADEIAELEDATQNRAHERAAQKRLARELTTLVHGEGATTAVELASQALFGRAELADLDESTLGAALREASNGQVAELKPGGPDSIVDLLVETGLAASKGAARRNVAEGGVYVNNIRIESDEWIPQHSDFLHERWLVLRRGKRHIAGVERVGA", "text": "FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily."}
{"protein": "MRLALLCGLLLAGITATQGGLLNLNKMVTHMTGKKAFFSYWPYGCHCGLGGKGQPKDATDWCCQKHDCCYAHLKIDGCKSLTDNYKYSISQGTIQCSDNGSWCERQLCACDKEVALCLKQNLDSYNKRLRYYWRPRCKGKTPAC", "text": "FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular lipids, exerting anti-inflammatory and immunosuppressive functions (PubMed:10531313, PubMed:23690440, PubMed:26392224, PubMed:10455175). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). In draining lymph nodes, selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are precursors of the anti-inflammatory lipid mediators, resolvins (PubMed:23690440). During the resolution phase of acute inflammation drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses dendritic cell activation and T-helper 1 immune response (PubMed:23690440, PubMed:27226632). May act in an autocrine and paracrine manner. Via a mechanism independent of its catalytic activity, promotes differentiation of regulatory T cells (Tregs) and participates in the maintenance of immune tolerance (PubMed:19564598). May contribute to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (PubMed:11694541). SUBCELLULAR LOCATION: [Isoform 1]: Secreted Cell membrane Note=Localizes to cell membrane likely through binding to heparan sulfate proteoglycans. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MTEAMKITLSTQPADARWGDKATYSINNDGITLHLNGKDDLGLIQRAARKIDGLGIKQVALTGEGWDIERCWAFWAGYKGPKGVRTVMWPDLDDAQRQELDNRLTIIDWVRDTINAPAEELGPEQLAQRAVDLLCSVACDSVTYRITKGEDLREQNYMGLHTVGRGSERPPVLLALDYNPTGDKDAPVYACLVGKGITFDSGGYSIKQSAFMDSMKSDMGGAATVTGALAFAITRGLNKRVKLFLCCADNLISGNAFKLGDIIRYRNGKNVEVMNTDAEGRLVLADGLIDASAQHPELIIDMATLTGAAKTALGNDYHALFSFDDTLAGRLLTSAAQENEPFWRLPLAEFHRNQLPSNFAELNNTGSAAYPAGASTAAGFLSHFVENYREGWLHIDCSATYRKAPVEQWAAGATGLGVRTIANLLTA", "text": "FUNCTION: Probably plays an important role in intracellular peptide degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M17 family."}
{"protein": "MKIYFATGNPNKIKEANIILKDLKDVEIEQIKISYPEIQGTLEEVAEFGAKWVYNILKKPVIVEDSGFFVEALNGFPGTYSKFVQETIGNEGILKLLEGKDNRNAYFKTVIGYCDENGVRLFKGIVKGRVSEEIRSKGYGFAYDSIFIPEEEERTFAEMTTEEKSQISHRKKAFEEFKKFLLDRI", "text": "FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP (PubMed:10404228, PubMed:11452035). Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions (PubMed:11452035). Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than XTP, and has nearly no activity toward the canonical nucleotides ATP, CTP, and TTP, and toward 6-N-hydroxylaminopurine deoxynucleoside triphosphate (dHAPTP) (PubMed:10404228, PubMed:11452035). Displays neither endonuclease nor 3'-exonuclease activities (PubMed:11452035). SIMILARITY: Belongs to the HAM1 NTPase family."}
{"protein": "MGIALMFLLALYQMQSAIHSEIIDTPNYAGNSLQDADSEVSPSQDNDLVDALLGNDQTERAELEFRHPISVIGIDYSKNAVVLHFQKHGRKPRYKYDPELEAKRRSVQDNFMHFGKRQAEQLPPEGSYAGSDELEGMAKRAAMDRYGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRTPAEDFMRFGRTPAEDFMRFGRSDNFMRFGRSPHEELRSPKQDFMRFGRPDNFMRFGRSAPQDFVRSGKMDSNFIRFGKSLKPAAPESKPVKSNQGNPGERSPVDKAMTELFKKQELQDQQVKNGAQATTTQDGSVEQDQFFGQ", "text": "FUNCTION: In insects, FMRFamide and related peptides have modulatory actions at skeletal neuromuscular junctions, and peptides that are immunologically related to FMRFamide are released into the circulation from neurohemal organs. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
{"protein": "MVGGLKRKHSDLEEEEERWEWSPAGLQSYQQALLRISLDKVQRSLGPRAPSLRRHVLIHNTLQQLQAALRLAPAPALPPEPLFLGEEDFSLSATIGSILRELDTSMDGTEPPQNPVTPLGLQNEVPPQPDPVFLEALSSRYLGDSGLDDFFLDIDTSAVEKEPARAPPEPPHNLFCAPGSWEWNELDHIMEIILGS", "text": "FUNCTION: Antiviral interferon-stimulated protein that plays a role in innate immunity and in the suppression of viruses through different mechanisms (PubMed:33147462, PubMed:36594413). Plays a role in the late phase response of TLR-induced immune effector expression (By similarity). During influenza infection, interacts with PB2, PB1, and PA to disrupt the formation of the viral RdRp complex (PubMed:33147462). Inhibits zika virus by interacting with the capsid protein in the nucleolus and reducing its abundance through proteasomal degradation (PubMed:36594413). Strong transcriptional coactivator (PubMed:10982866). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELFCKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDFGLC", "text": "FUNCTION: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). SIMILARITY: Belongs to the GST superfamily. Omega family."}
{"protein": "MNHSSNEKEPETIEPLRYLSKTEVATVETELLRDYRFGQQQLIEIWGHACAIAITKAFPLSSLSKKQPTLLVVCGPEQNGSIGLVCARHLRMFEYEPTIFYPKRSTLGLHQDFTVQCEKMDIPFLSYLPTEVQLLNDAYNLVIDAILGPETDHKDVKEPYAGMLVTLKQVKIPIVSVDVPSGWDADEPAKDGINPEVLISLTAPKKCATGFSGKHFLAGRFLPYDIQKKYELNLPEFPGTECIIEL", "text": "FUNCTION: Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (PubMed:23719382). Orchestrates hematopoietic stem and progenitor cell emergence from the hemogenic endothelium, a type of specialized endothelium manifesting hematopoietic potential. YJEFN3-mediated cholesterol efflux activates endothelial SREBF2, the master transcription factor for cholesterol biosynthesis, which in turn transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence (PubMed:30705153)."}
{"protein": "MTLASIRRGYHVIKTLLQYGLDDVLPPKMTPWYFKLARNSLFWIRNKHKNKPGGERLKLAMQELGPVYIKLGQMLSTRRDLLSDEWASELAMLQDKVPPFDGALARQAIEAELKAPIESLFDDFNEIPLASASISQVHTATLKSNGKDVVLKVLRPNVETKIQADLQLMSQTAKLIEYLLGEGNRLRPAEVIEDYRVTILGELNLKLEALNAVKLRNNFLDSDALYVPYVYEEFCYPRLMVMERIYGISVSDIAALKAQGTNFKLLAERGVELFFTQVFRDNFFHADMHPGNIFISRDHPENPYYIGLDCGIMGTLSEVDKRYLAENFLAFFNRDYHRIAQLYIESGWVSEKTDLQAFEQAIKVVCEPMFNKPLDEISFGHVLLELFRTARHFDIVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMADQVGPKAMFKKVSTKLPYWADKLPEFPELIYDNLKLGRKLLSSQQQMLDKYLKYQQQAHKSNYLLITSAVLLICGTLLINRDATLWTPYVCLVSGIILWFVGWRSRPKNRKF", "text": "FUNCTION: Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC1 family. UbiB subfamily."}
{"protein": "MSLFLKDDSIQIREVWNDNLQEEMDLIRDVVDDFPYVAMDTEFPGIVVRPVGTFKSNADYHYETLKTNVNILKMIQLGLTFSNEQGNLPTCGTDKYCIWQFNFREFDLDSDIFALDSIELLKQSGIDLAKNTLDGIDSKRFAELLMSSGIVLNENVHWVTFHSGYDFGYLLKLLTCQNLPDSQTDFFKLINVYFPTVYDIKHLMKFCNSLHGGLNKLAELLEVERVGICHQAGSDSLLTSCTFRKLKENFFVGPLHKYSGVLYGLGVENGQVAI", "text": "FUNCTION: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CAF1 family."}
{"protein": "MASPCLTKSDSGINGVDFTEKFRLEDSTLLANGQVVLTDVPVNVTLTSSPYLVDKDGVPLDVSAGSFIGFNLDGEPKSHHVASIGKLKNIRFMSIFRFKVWWTTHWVGSNGRDIENETQIIILDQSGSDSGPGSGSGRPYVLLLPLLEGSFRSSFQSGEDDDVAVCVESGSTEVTGSEFRQIVYVHAGDDPFKLVKDAMKVIRVHMNTFKLLEEKSPPGIVDKFGWCTWDAFYLTVNPDGVHKGVKCLVDGGCPPGLVLIDDGWQSIGHDSDGIDVEGMNITVAGEQMPCRLLKFEENHKFKDYVSPKDQNDVGMKAFVRDLKDEFSTVDYIYVWHALCGYWGGLRPEAPALPPSTIIRPELSPGLKLTMEDLAVDKIIETGIGFASPDLAKEFYEGLHSHLQNAGIDGVKVDVIHILEMLCQKYGGRVDLAKAYFKALTSSVNKHFNGNGVIASMEHCNDFMFLGTEAISLGRVGDDFWCTDPSGDPNGTFWLQGCHMVHCAYNSLWMGNFIQPDWDMFQSTHPCAEFHAASRAISGGPIYISDCVGKHDFDLLKRLVLPNGSILRCEYYALPTRDRLFEDPLHDGKTMLKIWNLNKYTGVIGAFNCQGGGWCRETRRNQCFSECVNTLTATTSPKDVEWNSGSSPISIANVEEFALFLSQSKKLLLSGLNDDLELTLEPFKFELITVSPVVTIEGNSVRFAPIGLVNMLNTSGAIRSLVYNDESVEVGVFGAGEFRVYASKKPVSCLIDGEVVEFGYEDSMVMVQVPWSGPDGLSSIQYLF", "text": "FUNCTION: Transglycosidase operating by a ping-pong reaction mechanism. Involved in the synthesis of raffinose, a major soluble carbohydrate in seeds, roots and tubers (By similarity). SIMILARITY: Belongs to the glycosyl hydrolases 36 family."}
{"protein": "MITSFYAFLDYLKNMKASSLHTLRNYCMDLSSLKCFLEKKSDLSPTPPLSLHDNTYDYPPLSFSLFTKDNIRLYLLEQIQTHHSKRTVRRRLSAIKSFARFCVKNQLIPENPAEMIRGPRLPQELPSPLTYEQVLALMAAPELDKVTGFRDRCLLELFYSSGLRISEITALNRADIDFQSHLLHIRGKGKKERIVPMTKVAVQWLQDYLNHPDRASVEQDHQACFLNRFGKRLSTRSIDRKFQQYLLKTGLSGSITPHTIRHTIATHWLERGMDLKTIQLLLGHTSLETTTIYTHVSMKLKKQIHDETHPHNLEE", "text": "FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily."}
{"protein": "MWTIMIGSKNRAKVHALQEVVIRDKIIVRSEAVPSDVASQPFSDQETIQGAINRANHCLSFDGVDYGVGLEGGVVRSEYGLFLCNWGALVSQTGDQWVAGGARVPLPQEVAHELEGGKELGDIMESLTKNPDVRMTDGAIGYLTDGEISRKAMFQHVVHLLIGQARRDGHLLRTVTH", "text": "FUNCTION: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. SIMILARITY: Belongs to the YjjX NTPase family."}
{"protein": "MPSQRHYSPADRLLMQADAALRTLLPFSGQPSRPSPALLKTEAELSESEARHVAGLMRINHTGEVCAQALYQGQALTARLPQVRQAMEQAADEEIDHLAWCEQRIRQLGSHTSVLNPIFYGLSFGIGASAGLISDRISLGFVAATEDQVCKHLDDHLGQLPAGDEKSRAILEQMREDEAQHSTAAIEAGGLRFPAPVKFGMSLVSKVMTKATYRI", "text": "FUNCTION: Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6- methoxy-1,4-benzoquinol during ubiquinone biosynthesis. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the COQ7 family."}
{"protein": "MVILTKEASMVRQALLANGLEPFLRGEERLGIEARKRRIAAHMKKIMTLLNLDLADDSLAKTPYRIAYMYIEEIFPGLDYANFPQITLISNKMKADEMVTVRNITLTSTCEHHFLMIDGKATVSYIPKSNVIGLSKINRIVRFFAQRPQVQERLTQQILLALQTILGTNNVAVSIYAVHYCVKARGICDSTSTTTTTSLGGIFKSSQNTRQEFLRTINQT", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I family."}
{"protein": "MKLLSITFLFGLLALASANPLSPGNVIINGDCKVCNIRGD", "text": "FUNCTION: Secreted immune-induced peptide induced by Toll signaling. Has a role in resistance to bacterial and fungal infections (PubMed:25915418, PubMed:29920489). The strength of antimicrobial activity appears to correlate with the overall level of expression (PubMed:29920489). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bomanin family."}
{"protein": "MKTTATSFVTGERVVVFVVVSRILLSLPLSLISHGFSLFLLSLSAFLVEIRVETSPFLLSHFSSRRGASSGILLGAVTLPSVMISKLVQLSRAISIHEAEQDELAHVTMQYWAASASCCAILIYLSVIMSQVRKDESLSSSSIWLTRVSLTGTVLYGVACFVSLSMISHTGLNTSLKMLWMLFHGLAAVKLIRHLLCTFPSCASIGEALLVTSGLVLYFGDFLACTIAKIFEKLIPVDLVSISYGIKRTETGIIVQGLLLGLLLFPMVFRFVLHIYESSLRKRDARQRNCSDAAKSVLFFVSLLFFMVVAVPSWMQFVHDFNQHPFLWVLTFVFSEPLKRLSLCIYWILLIVVSVSRFYNISRSSKVERILLRKYYHLMAVLMFLPALVLQPKFLDLAFGAALAVFVALEIIRIWRIQPLGEPLHQFMNAFTDHRDSEHLIVSHFSLLLGCALPIWMSSGFNDRALSPFAGILSLGIGDTMASMVGHKYGVLRWSKTGKKTVEGTAAGITSMMAVCFVLVPILASMGYILSQGWWSLLVAVTATGMLEAYTAQLDNAFIPLVFYSLLCL", "text": "FUNCTION: Essential for pollen development. Involved in protein N- glycosylation in the endoplasmic reticulum (ER), especially in the female gametophyte. Mediates pollen tube (PT) reception in synergids through protein glycosylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the polyprenol kinase family."}
{"protein": "YPPKPENPGEDAPPEELAKYYSALRHYINLITRQRY", "text": "FUNCTION: Elicits an increase in arterial blood pressure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
{"protein": "MFSHCEGYRIEGGVTDGETNWNNNFNQNNNNNDNNKVMASIYKQQFYGKPHKTFMSLSSPNGPILVCIKKVGNSSDDFYLLVCTEKGFEEVRANKDSLQKSKTTRSFLKMRPTSLNVITSVRPELTKVPLCKVTDKSIQEELVKVCEPEFNKVIKSALLYCKESQRDDNDMLKNISSNVSQEYNDFLNFLGEKVELKDFSKFNGGLDIKNNSHGTHSIYSQINDVEVMYHVATMLPFFPSDPKQSERRKLISLDRVVIIFNDGSKPMSPNCIKSKSTQIIILIQPIKNFVGNSKTTIGISNDENRVVGEQPSPSLTTTTTTTTTTSPTINSNSPTPSNKIKYRVSISNRDEVPNYGPPLPDPPIFEKDDSFRNFLYQKMVGGAASLRNTPAFTSKNSEKASALINVISKYSTKGMEQI", "text": "FUNCTION: Mediates the deactivation of rap1 during multicellular development and is required for normal morphogenesis. Also required for the correct patterning of specific subtypes of prestalk cells."}
{"protein": "MSPPAATFDIPVANTGNGLSLKKDLAVKPAASGVAKSLAEIEHNWEKFTFAPIRESQVSRAMTRRYFNDLDTYAESDVVIIGAGSCGLSAAYTLASKRPDLKIAMVEAGVAPGGGAWLGGQLFSAMVMRKPAELFLNEIGVPYEDEGDFVVVKHAALFTSTLMSKVLNFPNVKLFNATAVEDLITRPAPTSNDPNAVRIAGVVTNWTLVSMHHDDQSCMDPNTINAPLIISTTGHDGPFGAFSVKRLVSMQQLPQLGGMRGLDMRTAEDAIVKRTREVVPGLIVGGMELSEVDGANRMGPTFGAMVLSGVKAAEEAIGVWDERKAQNDE", "text": "FUNCTION: Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the THI4 family."}
{"protein": "MAAQNEQRPERIKTTPYLEGDVLSSDSGPLLSVFALQEIMQKVRQVQADYMTATREVDFTVPDVQKILDDIKTLAAEQVYKIVKVPSISFRHIVMQSRDRVLRVDTYYEEMSQVGDVITEDEPEKFYSTIIKKVRFIRGKGSFILHDIPTRDHRGMEVAEPEVLGVEFKNVLPVLTAEHRAMIQNALDGSIIENGNVATRDVDVFIGACSEPIYRIYNRLQGYIEAVQLQELRNSIGWLERLGQRKRITYSQEVLTDFRRQDTIWVLALQLPVNPQVVWDVPRSSIANLIMNIATCLPTGEYIAPNPRISSITLTQRITTTGPFAILTGSTPTAQQLNDVRKIYLALMFPGQIVLDLKIDPGERMDPAVRMVAGVVGHLLFTAGGRFTNLTQNMARQLDIALNDYLLYMYNTRVQVNYGPTGEPLDFQIGRNQYDCNVFRADFATGTGYNGWATIDVEYRDPAPYVHAQRYIRYCGIDSRELINPTTYGIGMTYHCYNEMLRMLVAAGRDSEAAYFRSMLPFHMVRFARINQIINEDLHSVFSLPDDMFNALLPDLIAGAHQNADPVVLDVSWISLWFAFNRSFEPTHRNEMLEIAPLIESVYASELSVMKVDMRHLSLMQRRFPDVLIQARPSHFWKAVLNDSPEAVKAVMNLSHSHNFINIRDMMRWVLLPSLQPSLKLVLEEEAWAAANDFEDLMLTDQVYMHRDMLPEPRLDDIERFRQEGFYYTNMLEAPPEIDRVVQYTYEIARLQANMGQFRAALRRIMDDDDWVRFGGVLRTVRVKFFDARPPDDILQGLPFSYDTNEKGGLSYATIKYATETTIFYLIYNVEFSNTPDSLVLINPTYTMTKVFINKRIVERVRVGQILAVLNRRFVAYKGKMRIMDITQSLKMGTKLAAPTV", "text": "FUNCTION: The VP3 protein is one of the five proteins (with VP1, VP4, VP6 and VP7) which form the inner capsid of the virus. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the orbivirus VP3 family."}
{"protein": "MAPTTTNPMNETIPGSIDIETLIPNLMIIIFGLVGLTGNVILFWLLGFHLHRNAFLVYILNLALADFLFLLCHIINSTMLLLKVHLPNNILNHCFDIIMTVLYITGLSMLSAISTERCLSVLCPIWYRCRRPEHTSTVLCAVIWFLPLLICILNGYFCHFFGPKYVIDSVCLATNFFIRTYPMFLFIVLCLSTLALLARLFCGAGKTKFTRLFVTIMLTVLVFLLCGLPLGFFWFLVPWINRDFSVLDYILFQTSLVLTSVNSCANPIIYFFVGSFRHRLKHKTLKMVLQSALQDTPETPENMVEMSRSKAEP", "text": "FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily."}
{"protein": "MSQDSNALEMIQNEGPKWDDGFDHDDVTKIYLVGGKTGIDFIKIDYVKSGKPKNGPFHGYSGGGFLQMFEIDNLKNEYLESVEGYYTNRSGEFIGAIQFKTNLRVSEIIGYSYWGLKKFKLAKHGNKIIGFQGSAEYRLKDLDAYFTPITPTRMEAQGGNGGTKWDDGGDHDSVTKIQVRINKEGIQYIKFNYVDKDGDPEKEQLHGSETGRGYTLEPFEINHSDKEYLLSIDGCYDEDSGVIQSLQLKTNIKTSEVMGDDEKGTKFTLGCNGHEIIGFHGSAQDNLNALGAYITTLTLTKLEYIGEGSDIWDDGTFEGVKKVSFYHNDGIVRCIEFDYVKDGKIETRVQGGKRGTGDFTKEEFTVDYPNEFLTSVEGTYRDNPGGTLITSLTFKTSNNRTSPILGKASNKTFLLESKGCALVGFHGASSDFFLYALGAYSFPMTSLAEAGRGAIHTSW", "text": "SIMILARITY: Belongs to the jacalin lectin family."}
{"protein": "MTVMSIQDNLTINEKKVLLALEELRSAVPDKLEEKSGLQIDAAMQAAFMLQEKELASVSEKVLERYSLTKEGEEYKKTGLPERQIIDALKNPVSLEELRSCFSPQTVGIATGWLVKKGWAKVENGIMVPSGEASEGKDEKALSAFAGKAKTLEELGADEGTVKDLLKRKLVVKHEEKFRTVSITDAGSELASQGLVLEEEIAQLTPELLKSGAWKEKKFRPYRLDITPKPLYGTKIHPYRRLIEQMRQIFLEMGFTEIKGGIIQSSFWNFDALFQPQDHPARDMQDTFHLGSTCQIPAEYSGKVAAMHENGGDIDSCGWGGIWDRELAGRNVLRTHTTSVTIKYLADNPEPPVKAFCIDRAYRRETIDPTHTPEFEQLEGVVMDKDMSFADLLGLLAEFYHRMGFEEVRFRPGYFPYTEPSVEPEVYVDGLGWVELGGAGVFRKEVTEPLGIKAPVLAWGLGVSRLAMLKLGLKDLRLLYQSDIDWLRKSEVCKI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily."}
{"protein": "MEINKNDNNNNINNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNQNNNQKNNYRNYKPIKTGTLIQHQILQQTLSNFQTKNKVFQLGSDKLILIFKENETIYFHGTIQARSIIGSVEVYGYTITPQSTTYYPIYSPFCSPTLSITSNNSNNKLYTLKEIIENQLIKIPELVKNKLKENEKQIEIDEPTLAISSIIVLKILDDHCENPKMFTKKKIEIIDSFKLLKGFYPLYQPDFNTQLLTIPNEWLNLINTQFLYNDHCNNNGLSILTCGERNVGKSTFNRILINKLLKKYTHIIFIETDTGQTEFTPSGIMSIDIINSPLLGPPFTHCKNNPLKSYFFGDTSPKNNPEYFLNLSFQLIDCCNLIKQQYPNIPIILNTNGWLKSLGLHLTQEIIKYFKPTSIVQLINNNNNNNNNNNNNNNNNNNNNNNNNNLNDNLNNFINRFDSTVTFSQDCINQLFEDCDDDNDDNKNLKTTIITKLYSINSINNFSQSIYKPIFNLGSSEIRNLMFKSYFKLESKGSLSHQSPYQVSWKELKVKILTNNVPPSQTMYALNASLVGICIDEDPEKNYKYISYKVGNNLPTIINQSPLISQCIGLGLIRSIDMVNGYYYIITPIDPSLLEISNTILKGSIEIPQTLTISVSSKGKILVPYLQLDVLSSYGTGSDVMNRPSFFDD", "text": "FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily."}
{"protein": "MLPSTMFLVHLPLSTNRLHCLRNTSLESYLCSFVHLNHPLHISDRVILISLHEAVRFSFAFSFPRGTLSIAYCLMSSVSTSSEAIMSTELLANYCHSSLHVCICISSFPNETGNHDSFPGAVVSISDQPTDQCKLAAKELPLRNLLECRFFDCMGEEDLINLGVIGTER", "text": "SIMILARITY: Belongs to the FAM106 family."}
{"protein": "MSFHHRVFKLSALSLALFSHLSFASTDSELNLDFLQGMSAIPSVLKSGSDFPAGQYYVDVIVNQENVGKARLSITPQEESANALCLSPEWLKAAGVPVRLEGYASTLNAAGQCYVLSRNPYTRVDFSYGSQSLVFSIPQSFLVGKTDPSRWDYGVPAARLKYSANASQTSGQSTSAYANADLMVNLGRWVLASNMSASRYADGSGEFTARDITLSTAISQVQGDLLLGKSQTRSALFSDFGFYGAALRSNSNMLPWEARGYAPLITGVANSTSRVTISQNGYAVYSKVVPPGPYQLDDVRSVGNGDLVVTVEDASGHKTTTVYPVTTLPTLLRPGEVEYNVAVGRKSSNYKLKKPFADGENGMFWMGSVGYGFDSTTLNAASILHGKYQAGGVSVTQALGGFGAVSAGMNLSQAKYDNGDNKRGHSVSAKYAKSFSDSSDLQLLAYRYQSKGYVEFADFYSTDRYTRYNTKSRYEMRFSQRLGNSNLNLAGWQEDYWWMKGKAIGGDVSLSTTILDGVSVFLNGSYSKRPYLDKPDYSTSLSFSIPFTLGGVRHYSSTGLSYSSSGRMGMNSGVSASPTDRLSYGLNTNLSDKGDRSLSGNLSYGFDAIQTNMMLSQGRDNTTVSGSVSGTILGTADSGLMMTKETGNTLGVARIPGVKGVRINGSAPTNSKGYTVVNLSDYSLNRVSVDMENVPDDLELQTTSFNVVPTEKAVVYREFGAEHVLRYILRVKERDGRILNGGSAQTEQGLDAGFIAGNGVLLMNMLSAPSRVSVERGDGSVCHFSVKGIVPNTGKVQEVYCE", "text": "FUNCTION: Involved in the export and assembly of FimA fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
{"protein": "MQNQGNKVLSAAMLDSADRYWLRLCDVWPEAKTALTAMQQQELTAVFGLSDYMGEQLCRHPEWIVQLFDGLLDDVVRSEFDAQLHSLIADLTQEELVKSALRRYRNLQMVRLAWRDFLNYTPVEESLLDLSALAEALVIAGRDWLYQEMCQQYGTPTSAEGNPQPLLILGMGKLGGRELNFSSDIDLIFTFPEHGETVGGRRTQANQQFFIRMGQRLVNLLDQVTVDGFVFRVDMRLRPYGESGPLVVSFSGLEDYYQEQGRDWERYAMVKARVLGPWSGYCDELHDLLRPFVYRRYIDFSAIESLRKMKQLIAQEVRRRQLTDNIKLGAGGIREVEFVVQSFQLIRGGREPALRQQSLFGAIDTLYSLGQLEYLAVDELKHSYIILRRVENLLQAIDDKQTQTLPNNELDWQRLCYPLDMADEVELRQKINQAMVTIHGHFNATVGGTDSHEHNDHWTALFWNVQQDEHANALLQEQQVDDAELWQLLSEWRQTVSKRSIGPRGRETLDKLMPKLLEELVTQTKPSQAFKPVAKVLDKILTRTTYLELLCENPGARQQLVSLCCASPWIARELANFPMLLDELIDPSQLYDITSIDDYPSELRQYLLRVPEDDMEQQMEALRQFKLSQQLKIAAADVTGVLPVMQVSDHLTFLAEAIIEQVVLQAWHQVASRHGIPAETSPSNMGFAVIGYGKLGGIELGYGSDLDLVFLHGHTGSGTTDGKRPIDNGHFYLKLAQRIVHLFATRTTSGELYEVDMRLRPSGASGLLVSEIEHFGAYLQQEAWTWEHQALVRSRFVFGDYSLAGRFSDLRAQVLKIERDKQVLAKAVKDMRIKMREHLLQVEPGQFDLKQSAGGIADIEFIAQYLVLANAHQYHELTIWSDNVRIFEVLAELELLPIMQAQHLTQTYCWLRDENHELTLQQLPGKLPIQSVLQKTDSVIEIYNEILAI", "text": "FUNCTION: Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell. SIMILARITY: Belongs to the GlnE family."}
{"protein": "MLTKRIIPCLDIKDGRVVKGTKFLNLRDAGDPVELAQYYDDEGADELVFLDITASAEKRDIIIDVVERTAEKVFIPLTVGGGIKSIEDFRRILRAGADKVSINTAAVKNPNLIKEASEIFGSQCVVVAIDAKRHYVNEDEIDKINKNVVKVEDGYCWFEVYIYGGRKETGIDAINWAKKVEELGAGEILLTSIDKDGTKSGYDLILTKEISKSVKLPVIASGGCGKPEHVYEAFVYGKADAALMAGILHYREYTIEEIKKYCADRGIPMRLL", "text": "FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MKREILLERIDKLKQLMPWYVLEYYQSKLAVPYSFTTLYEYLKEYDRFFSWVLESGISNADKISDIPLSVLENMSKKDMESFILYLRERPLLNANTTKQGVSQTTINRTLSALSSLYKYLTEEVENDQGEPYFYRNVMKKVSTKKKKETLAARAENIKQKLFLGDETAGFLTYIDQEHPQQLSNRALSSFNKNKERDLAIIALLLASGVRLSEAVNLDLRDLNLKMMVIDVTRKGGKRDSVNVAAFAKPYLENYLAIRNQRYKTEKTDTALFLTLYRGVPNRIDASSVEKMVAKYSEDFKVRVTPHKLRHTLATRLYDATKSQVLVSHQLGHASTQVTDLYTHIVNDEQKNALDSL", "text": "FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerS subfamily."}
{"protein": "MKCIILLAVLGTAFAQRNGFCRLPADEGICKALIPRFYFNTETGKCTMFSYGGCGGNENNFETIEECQKACGAPERVNDFESADFKTGCEPAADSGSCAGQLERWFYNVQSGECETFVYGGCGGNDNNYESEEECELVCKNM", "text": "FUNCTION: Midgut thrombin inhibitor that plays a major role in keeping the midgut microenvironment at low hemostatic and inflammatory tonus (PubMed:18286181) (By similarity). Also inhibits FXIa (F11), kallikrein (KLK1), neutrophil elastase (ELANE) and cathepsin G (CTSG), which play a role in the contact pathway of the coagulation cascade (PubMed:18286181) (By similarity). Also abrogates platelet aggregation by cathepsin G and plasmin, and attenuates tissue factor (F3) pathway inhibitor cleavage by elastase (PubMed:18286181) (By similarity). In vivo, inhibits thrombosis and promotes bleeding in mice (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MLVYQDKLSGDELLSDSFPYRELENGVLWEVDGHWVVQGAVDVDIGANPSAEGGGDDEGVDDQAVKVVDIVDTFRLQEQPAFDKKQFISHMKRYIKNLSAKLEGDDLDVFKKNVESATKYLLSKLKDLQFFVGESMHDDGGVVFAYYKEGAADPTFLYFAHGLKEVKC", "text": "FUNCTION: Involved in calcium binding and microtubule stabilization. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCTP family."}
{"protein": "MSHDTNTVDSRTHEGQLNKLGFWIFLTAEFSLFGTLFATLLTLQHGGDYAGKMTTELFELPLVLIMTFALLISSYTCGISIYYMRKEKQNLMMFWMILTVLLGLVFVGFEIYEFAHYVSEGVTPQIGSYWSSFFILLGTHGAHVSLGIGWIICLLIQVATRGLNKYNAPKLFIVSLYWHFLDVVWIFIFTAVYMIGMVYSG", "text": "FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family."}
{"protein": "MGWIRASIRWIWGRVTWFWRVISRPSSFLSIGFLTLGGFICGVIFWGGFNTALEITNTEKFCTSCHEMRDNVYQELMPTVHFSNRSGVRASCPDCHVPHEWTDKIARKMQASKEVWGKIFGTISTREKFLEKRLELAKHEWARLKANDSLECRNCHAAVAMDFTKQTRRAPQIHERYLISGEKTCIDCHKGIAHQLPDMTGIEPGWLEPPELRGEEQAWLGGGAEAVHRYLATVETR", "text": "FUNCTION: Mediates electron flow from quinones to the NapAB complex. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the NapC/NirT/NrfH family."}
{"protein": "MIALDQHLTEHKKDITQQWLEVCTSNGSWLYSAKDQQKLEQKLKDQHELLVTIVAKSLRKEDVEDELNRWSLQCARDRAVHEVTVTQSVGQFNTFRHIMFEWIHKFSEASSQDISIQEFYEWSRILNQNIDEIIEVFTEEYHQVTMIQLNAQKEMINELSAPIMPITDGIGILPLVGEIDTHRARTILESVLEQCSALKLSYLFLDISGVPIVDTMVAYQIFKVIDSTKLLGIETIISGIRPEIAQTVVKLGLDFSNVKTEQSLAKALANKGFKIKEC", "text": "FUNCTION: One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. FUNCTION: Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU."}
{"protein": "MNEETQTSELTNTDQGPQIEPGPISKWLNQKGLIHKLLEPDEIGIENLGVDPQQLFKIVSELKMNGFNYLQCQGGYDEGPGLSLVCFYHLMEMKDFNEGDKPREVRLKVFLDRNGSLRVPSLYKLFRGCDWQERETYDMFGINFDGHPHPKRLLMPEDWRGWPLRKDYIQPDFYEMQDAY", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 30 kDa subunit family."}
{"protein": "MQIEKVYEPQRFEPHWAQWWIDSNIFRANPESPGRVFSLVIPPPNVTGVLHIGHMLEHTEIDVSTRWHRMLGDNTLWLPGTDHAGIATQMVVARQLKEEGINYRDLGREKFEERVWQWKAQSGDTIKRQMVRLGASCDWSRERFTLDPGLSRAVREVFVSLYERGLLYRGEYMTNWCPSCNTAISDLEVAHADVAGHLWHIRYPVNGMPGRFVTVATTRPETMLGDTAIAVNAKDPRYQDLHGKTVQLPLMDREIPIILDDLADPQFGTGVVKVTPAHDPNDFEAGKRHNLAKIQVIDNNARMTAAAGPYAGLDRFDARKRVVSALEEIGALVKVEDYPLSLGKCDRCKTPVEPLISTQWFVKTKPLAEKAIAVVESGEIGFVPQNWTKTYYEWMYNIRDWCVSRQLWWGHRIPAWHCGECKEIIVAREAPKACPRCASENLTQDTDVLDTWFSSGLWPFSTLGWPDQTADLAKYYPTTLLITGFDILFFWVARMVMFGLEFMGEVPFKQVYIHGLVRDADRQKMSKTKGNVIDPLVVTEKYGTDAVRMALLQGAAPGTDIVLTEERMESSRAFANKIWNAARFLFMNADQSAAAPAEPTIEDRWIVSRLNAAAETANRAIEQYRYHELAQELWKFFWHEFCDWYLELKKVSATGWGNAVAAFETALRLLHPAMPFLTEELWQRLERKEGDPKSIALAQYPQYRAELADSEAEKEVAIIQEIVTLARTLRTESKLDPKQQLKGALYCRTASLAIAQRHADAIQKIARTTLEFKAEAPPKADVIRSTVEFDLVLDVPKVEEDPARKQKEREQLEKNIANSKRQLGDEVFLSKAPAKVVDSIRAKLVDYEAQLAKML", "text": "FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily."}
{"protein": "MRVFKVTACVPSQTRIRTQRELQNTYFTKLVPYDNWFREQQRIMKMGGKIVKVELATGKPGTNTGLL", "text": "FUNCTION: Rod linker protein, associated with allophycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=This protein occurs in the rod, it is associated with allophycocyanin. SIMILARITY: Belongs to the phycobilisome linker protein family."}
{"protein": "MVRTKNQSSSSSASSSSTKSPIKSSSGAGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHSYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELNREGDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRLSLKEKQKEEARSKPQKTREPMLAGMTNEPMKLRVRSSGYGPKATTSAQPTASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI", "text": "FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton Chromosome Lipid droplet Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily."}
{"protein": "MTKSHVIFSASIALFLLLSISHFPGALSQSNKDCQSKSNYSCIDKNKALDLKLLSIFSILITSLIGVCLPFFARSIPAFQPEKSHFLIVKSFASGIILSTGFMHVLPDSFEMLSSPCLNDNPWHKFPFAGFVAMMSAVFTLMVDSITTSVFTKSGRKDLRADVASVETPDQEIGHVQVHGHVHSHTLPHNLHGENDKELGSYLQLLRYRILAIVLELGIVVQSIVIGLSVGDTNNTCTIKGLVAALCFHQMFEGMGLGGCILQAEYGWVKKAVMAFFFAVTTPFGVVLGMALSKTYKENSPESLITVGLLNASSAGLLIYMALVDLLAADFMGQKMQRSIKLQLKSYAAVLLGAGGMSVMAKWA", "text": "FUNCTION: Probably mediates zinc uptake from the rhizosphere. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MINMRDNPTMHVLQASKFLFLALILIQLLSTQLFAQRSKSPWQTLTGDAPLVIARGGFSGLLPDSSLDAYSFVSQTSVPGAVLWCDVQLTKDAIGLCFPDVKMMNASNIQDVYPKRKTSYLLNGVPTQDWFTIDFNFKDLTKVILKQGILSRSAAFDGNSYGISTVKDISTQLKPEGFWLNVQHDAFYAQHNLSMSSFLLSISKTVIIDYLSSPEVNFFRNIGRRFGRNGPKFVFRFLEKDDVEVSTNQTYGSLAGNLTFLKTFASGVLVPKSYIWPIESQYLLPRTSFVQDAHKAGLEVYASGFGNDFDLAYNYSFDPLAEYLSFMDNGDFSVDGLLSDFPLTASSAVDCFSHLGSNASSQVDFLVISKNGASGDYPGCTDLAYTKAIKDGADVIDCSLQMSSDGIPFCLSSINLGESTNVVQSPFRNRSTTVPEIGSLPGIYSFSLAWSEIQTLRPAIENPYSREFTMFRNPRERSSGKFVSLSDFLNLAKNSSSLTGVLISVENATYLREKQGLDAVKAVLDTLTEAGYSNKTTTTRVMIQSTNSSVLIDFKKQSRYETVYKVEETIRDILDTAIEDIKKFADAVVISKKSVFPTSESFTTGQTKLVERLQKFQLPVYVEVFRNEFVSQPWDFFADATVEINSHVTGAGINGTITEFPLTAARYKRNSCLTRKDVPPYMIPVQPAGLLTIVSPASLPPAEAPSPVFTDADVTEPPLPPVSARAPTTTPGPQSTGEKSPNGQTRVALSLLLSAFATVFASLLLL", "text": "FUNCTION: Involved in primary cell wall organization. Required for the accumulation of crystalline cellulose. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
{"protein": "MDKSKIRNFSIIAHIDHGKSTLADRILELTNTVAARDLEEQFLDQMDLERERGITIKLNAVQIKYKDYTFHLIDTPGHVDFTYEVSRSLAASEGALLLVDATQGIEAQTLANVYLALENNLEIIPIINKIDLPSANVEKTKEEIENVIGIPADNAVCVSAKTGLNCEKVLDAIVDYVPAPKDADDNKPLKALIFDSYFDEYRGVIMLIRVFQGKLKVGDDFKFMSNNANYHVIELGVRNPKETKKEYLEAGEVGYVAATIRDAKEVHVGDTITLVENPALEPLPGYKRKKPVLFTGFYPIDTRDYAELKKSLDKISLSDSSLTWEQETSKALGFGFRVGFLGMLHMDVIQERLSREYKVGIIATSPSVEYKVVKTNGTFEMISNPSLMPDRTYIDHIEEPYIEATIILPNEYIGNIMDLCQNKRGIYKSLDYIDDSRSRLIYEMPLGEIVFDFFDKMKSLSKGYASFEYDLIGYKTSDLVKVDILLNGDKIDAFSIITHKDSAYEKSRDLTKRLKDAIPRQNFEVPVQATIGGKIIARETIKAFRKDVTHKLHASDISRYKKLLEKQKAGKKKMKMLGSVEVPQEAFLDILKTNVDK", "text": "FUNCTION: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily."}
{"protein": "MASICTSNFHFLCRKNNSSPISHHLLLSPSSLSFSRCGGLRLCRCAAVKTGSEGGGIRSDNAELLRKPVISTELETTSESEELVKEESDDEVGKKSGDGEGWVDWEDQILEDTVPLVGFVRMILHSGKYAIGDRLSPDHQRTILQRLLPYHPECDKKIGPGVDYITVGYHPDFENSRCLFIVRKDGETVDFSYWKCIKGLIRKNYPLYADSFILRHFRKRRRND", "text": "FUNCTION: Has a function in the early stage of chloroplast development and palisade cell morphogenesis (PubMed:8861949). Required for correct plastid ribosome assembly. Required for processing and maturation of 4.5S rRNA (PubMed:15010617). SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MVCLKLPGGSYMAKLTVTLMVLSSPLALAGDTRPRFLQQDKYECHFFNGTERVRFLHRDIYNQEEDLRFDSDVGEYRAVTELGRPDAEYWNSQKDFLEDRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPARTQTLQHHNLLVCSVNGFYPGSIEVRWFRNSQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRAQSESAQSKMLSGVGGFVLGLLFLGAGLFIYFKNQKGHSGLHPTGLVS", "text": "FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Golgi apparatus, trans- Golgi network membrane; Single-pass type I membrane protein Endosome membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Late endosome membrane; Single-pass type I membrane protein Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation. SIMILARITY: Belongs to the MHC class II family."}
{"protein": "MSDIEQRVKKIVSEQLGANEADVKNESSFVDDLGADSLDTVELVMALEEEFDCEIPDEEAEKITTVQQAIDYVNANLK", "text": "FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acyl carrier protein (ACP) family."}
{"protein": "MNIGIGVLIFVIGALLGAVAGFFGARAYMKKYFEENPPVNEDMLKAMMMQMGQKPSEKKLNQMMSSMKAQQKRSKK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0154 family."}
{"protein": "MTNEGIGINRDTSTICLREYVFIHFFPVKLISALTNKTNTMVKLTSIAAGVAAIAAGVAAAPATTTLSPSDERVNLVELGVYVSDIRAHLAQYYLFQAAHPTETYPVEIAEAVFNYGDFTTMLTGIPAEQVTRVITGVPWYSTRLRPAISSALSKDGIYTAIPK", "text": "SIMILARITY: Belongs to the SRP1/TIP1 family. Seripauperin subfamily."}
{"protein": "MAASGTSATFRASVSSAPSSSSQLTHLKSPFKAVKYTPLPSSRSKSSSFSVSCTIAKDPPVLMAAGSDPALWQRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRRENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLDV", "text": "FUNCTION: The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TrpB family."}
{"protein": "MDKKAANGGKEKGPLEACWDEWSRCTGWSSAGTGVLWKSCDDQCKKLGKSGGECVLTPSTCPFTRTDKAYQCQCKK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the macin family."}
{"protein": "MEFAFYFAAGVAVLATLRVITNSNPVHALLYLIISLLAISMTFFSLGAPFAGALEIIVYAGAIMVLFVFVVMMLNLGPAVVEQERKWLTPGIWVGPSALALVLLVELLVVLARTPSGAGIGHTTVDAKAVGISLYGPYLLVVELASMLLLAALVAAYHLGRQDAKQ", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 6 family."}
{"protein": "MKYATGTDNAMTSGISGQTNNSNSASTEMQPTTSTPTAVHKEATPTATTTATYANGNPNPNANPSQSQPSNALFCEQVTTVTNLFEKWNDCERTVVMYALLKRLRYPSLKFLQYSIDSNLTQNLGTSQTNLSSVVIDINANNPVYLQNLLNAYKTFQPCDLLDAMSSSSSDKDSMPCYGSDFQITTSAQCDERKLYARKEDILHEVLNMLPLLKPGNEEAKLIYLTLIPVAVKDTMQQIVPTELVQQIFSYLLIHPAITSEDRRALNIWLRHLEDHIQAAAAGLTNRSYFLQPSPQLVAGGSSTGSGSCSSSATSSSTASCSSVASSSLCPASGSRSSRTNDWQTIAPPSKQLQNKLAGDWRGSGGGSSSGSINPLCDNLNGITLNELASSQNSLGLSLEGSSSLVNGVVAGAGSMLGIGGGDDHDTSFSKNGTEILDFDPVTADMGEACSLASSSLCGRNGGNPVEDRSQPPPNLQQQMLQPPPYASILMGNVGDQFGEINRWSLDSKIAALKTRRSNSLTTQTISSCSSSSNSSVITVNDNCSNSTENLAQFANKPRSFSLSIEHQRGALINSGSDTRLDEFKPNYIKFHTRNVGMSGIGLWLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGVTKGASHKLALCIEKLKERANILNRVEQELLTGQMELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYAAQDDETLGVLMWILDRSIHNEAFMNHASQLKDLKFKLSKMKISMVPKMHHVKPAGVGPNNGNINKPRWNGKTRKCDPKNGSNDRINNRKNSNDMLNFSLNCLPHPLPHHSQQPPPPLPQFDYNGYGGGPSHQPQYKSSSYPSFMGNPQQQPPPPPPTKSHHHAQQMQQMLQQHNHFPALPQQTPPQSHRRSLNNLILVAGGPQQPQQLIFKPGQGVLTNNGSSDNLGLERNQQPQQQQRKLSGGVTSAEQQPKKTMAAVVMENLAKFDQHFTLF", "text": "FUNCTION: Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevent their translation. Prevents translation of unlocalized nos in the bulk cytoplasm via the recruitment of cup (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SMAUG family."}
{"protein": "MEVKDTNCTSLGYGKPPWIFKGSALYQLHLVKAENARAFIPKECKLVEAFGYTLGGFFLASYDDSPAGIFDELVVIAGLVWNPPTSCAWAARVLVGSDEACLHGRKVVGLPSQVARFSKKITALPQKPESKSSSFLRRIGLRTSSNYKNHMDVEVTEIKKQTAMSICNINVNATASQQDSKGWMGPLIKMSLPNFSGRTKYNSDLLKYSCQIECRVRAVQPAKVSGPSESDADKENSSEDQSSNVESVSRVPRGTKRNFSISVMLSKPILALEFNHLKMRVEAPTTVTACSHDTT", "text": "FUNCTION: Required for neoxanthin biosynthesis. Probably not involved directly in the enzymatic conversion of violaxanthin to neoxanthin. Is necessary but not sufficient for neoxanthin synthesis. Seems not required for abscisic acid (ABA) biosynthesis in response to drought stress."}
{"protein": "MVAQYIGRFSPSPTGPLHAGSLVAALASWLDARAHAGQWLVRIEDVDTPRCVAGMDRVILQQLAACGLHADQPPVWQSQRTGLYQQALDQLVVQGLAYPCACSRKDIETALSRLGQARARHGELVYPGTCRTGLHGRVGRAWRLRTDLFKQNKPLATVEYTQEATNLIACNIIHWTDRRLGAQQQDVPAQVGDFVLKRFDGCFTYQLAVVVDDAAQGITDVVRGEDLADNTARQILLQQYLGLPTPRYLHTPLVLGAHGEKLSKQNGAQALDTTEPLAALNHAARVLGLPACSGSVAGALEAWVEAWDA", "text": "FUNCTION: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily."}
{"protein": "MIINHNMSAINANRVLGBTNADITKDL", "text": "FUNCTION: Component of the core of the flagella. SUBCELLULAR LOCATION: Periplasmic flagellum. Periplasm. SIMILARITY: Belongs to the bacterial flagellin family."}
{"protein": "MIMKTYFSGVSTLGVHSLATEDYGFFPLSVDQKTMERMKNVLDIPATQLNISNSSLIGSLCVGNSNGLLVPDITTEKEVELIKMFLKENSLDVNLERLKAKNTAFGNLILTNNKGCIISEELSRFRKTIEDVLDVESGVGNYAELATVGSNGVATDKGCLVHPLTDELELEWIQNILRVDYVERGTANRGVTSVGACILANSKGAVVGGDTSGPEILKIEEALDLID", "text": "FUNCTION: Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex. SIMILARITY: Belongs to the eIF-6 family."}
{"protein": "MDVLVPLLQLLVLLLTLPLHLLALLGCWQPICKTYFPYLMATLTARSYKKMESKKRELFSQIKDLKGTSNEVTLLELGCGTGANFQFYPPGCKVTCVDPNPNFEKFLTKSMAENRHLQYERFIVAYGENMKQLADSSMDVVVCTLVLCSVQSPRKVLQEVQRVLKPGGLLFFWEHVSEPQGSQALLWQRVLEPTWKHIGDGCHLTRETWKDIEKAQFSEVQLEWQPPPFKWLPVGPHIMGKAVK", "text": "FUNCTION: Thiol S-methyltransferase that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine to hydrogen sulfide and other thiol compounds including dithiothreitol, 7alpha-thiospironolactone, L- penicillamine, and captopril. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Lipid droplet Note=Highly concentrated in the perinuclear area of the endoplasmic reticulum (ER) and surrounding lipid droplets. May be associated with the specific regions of the LR that form lipid droplets and targeted to the initial deposits of lipids where the lipid droplets form. SIMILARITY: Belongs to the methyltransferase superfamily."}
{"protein": "MSFLKEFREFAMRGNVVDLAVGVIIGAAFGKIVSSLVADIIMPPLGLLIGGIDFKQFAVTLRDAQGDVPAVVMHYGVFIQNVFDFIIVAFAIFMAIKLMNKLNRKKEEAPAAPPAPSKEEVLLSEIRDLLKEQNNRS", "text": "FUNCTION: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscL family."}
{"protein": "MSDDAGDTLATGDKAEVTEMPNSDSLPEDAEVHCDSAAVSHEPTPADPRGEGHENAAVQGAGAAAIGPPVQPQDANALEPPLNGDVTEDTLAECIDSVSLEAEPRSEIPLQEQNYLAVDSPPSGGGWAGWGSWGKSLLSSASATVGHGLTAVKEKAGATLRIHGVNSGSSEGAQPNTENGVPEITDAATDQGPAESPPTSPSSASRGMLSAITNVVQNTGKSVLTGGLDALEFIGKKTMNVLAESDPGFKRTKTLMERTVSLSQMLREAKEKEKQRLAQQLTMERTAHYGMLFDEYQGLSHLEALEILSNESESKVQSFLASLDGEKLELLKNDLISIKDIFAAKELENEENQEEQGLEEKGEEFARMLTELLFELHVAATPDKLNKAMKRAHDWVEEDQTVVSVDVAKVSEEETKKEEKEEKSQDPQEDKKEEKKTKTIEEVYMSSIESLAEVTARCIEQLHKVAELILHGQEEEKPAQDQAKVLIKLTTAMCNEVASLSKKFTNSLTTVGSNKKAEVLNPMISSVLLEGCNSTTYIQDAFQLLLPVLQVSHIQTSCLKAQP", "text": "FUNCTION: May play a role in neuronal cell development. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAM114 family."}
{"protein": "MAAFTLDLMAQLPEAYQAYAPAVDVLPLIPIFFFLLVFVWQASVGFR", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbK family."}
{"protein": "MGFASASREEKLKMLKTNKTRKTTKHLNRLAKRKKLSREIRDGMADIKSRKSADLRQRAVNIEDDFIADRQAHYENSDEDLPLDMMDADIDWENSAFANAKRRLEKKRSGVESDSDDEDDVEKKKRKFAGLLEEGHEELLPIKLKDGTLIRPTREKEVKEDEEEKSGDEEEEGEEDEPHREDFSHLSASELIAKRRELMQEFKDTIASHANMLLSNPQVNIVRLRDLYNLCNGEKIHSLVRESVQKLAIASTLQVLLDILPGYAIREQTAEEKAQKQKKETRNLVNYEESLLRYHLKYLQLCEKLSNKLVGKDRHNDESTFTFKMGILSVKALARIVVSAPHFNYSTNIVSSLVRLSLAKNETVIREVCEAIRTVFKEDIHLKITLFTARSISTLVTKRKGRVPPELLRTLLSMNITEVKDEDKKSGKDALIAKKYQIKKEKASKTAKKYKKQLARLEADLLEVEAEESMSKKLKNATEAMKFAFQSYFSILKRMPNSALLEPVLEGLSKFAHLLSIEFYEDIVSTMENMVQNENLKSLDQLHCINTVFVILSGDGQLLNIDPSKFYRLAYRVLNHLPFEKRPEQRKNQIIMAAKTLETMLVIRRKAVPLSRVAAFVKRLLSIATVLDDFPALCIVSLVRSLFIAHPKLSSMIEDEEGGAPGIYRPDIDDPDVANALASDVRDELSMLARRRNTELSRFANNILYGVPSTGIFKLNPQLSSLKPWILMGQLMDNAKDAYDKVESKYLDDLEKAAKKRNQSVTPKNINFHISNWLAASK", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the CBF/MAK21 family."}
{"protein": "MGSEQALSEVVESAKERFGRLRHLVQKFLDDDDVPQECLPLLQECAEIWSSYVDACQDITMQAPKEDANRLSKGFLRLNETAFLYYMIVYTLLEDTLPRLKEFSSNKDQNVRNLYGERIQLLHNDPNIERIRNVIENYPKFIQLQTIEPGKLSSMLHFHGDALLLIDVRPRSEFVRAHIKCKNIICIDPASFKDSFTDQQIESVSLITSPHSDITFFSNRDKFKFIILYTDTQLHNNFQQRQTRILAKILSQNSVIKPLSGTKILILENGFSNWVKLGGAYQSSVSETAHLTSSSSTPAFGSPQVPTGLFNQKSLSPNKDKSMPMVSMNTQPLLTTVQRPQLPLYYSDLPIIPQPSPNRNSPTVQKFSPHPPTTLSKLNTPSTIQNKANTVERISPDIRAAQAHAYLPPASNVFSPRIPPLPQQNLSSSRQTILNNSQVLDLDLIVGLENIGNCCYMNCILQCLVGTHDLVRMFLDNTYLNFINFDSSRGSKGLLAKNFAILVNNMHRHGAFTPPNVRTIPVQTIQFKKICGHINPMYSDSMQQDCQEFCQFLLDGLHEDLNQNGSKKHLKQLSDEEERMREKMSIRKASALEWERFLLTDFSAIIDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKTCNILDCFREFTKCERLGVDEQWSCPKCLKKQPSTKQLKITRLPKKLIINLKRFDNQMNKNNVFVQYPYSLDLTPYWARDFNHEAIVNEDIPTRGQVPPFRYRLYGVACHSGSLYGGHYTSYVYKGPKKGWYFFDDSLYRPITFSTEFITPSAYVLFYERIF", "text": "SIMILARITY: Belongs to the peptidase C19 family."}
{"protein": "MKKTLLAVAIGGAMFATSAAAVDFHGYARSGIGWTSGGGEQTALKVNGGGSKYRLGNETETYAEFKLGQELFKDGNKSIYLDSNIAYSIDQQVDWEATDPAFREINVQFKNFAEDLLPGATLWAGKRFYQRHDVHMNDFYYWDISGPGAGVENIDLGFGKLSLAVTRNTEGGGTATYGQDKVYYIDNNGQIQYRYEDRKADVYNDVFDIRLAELNVNPNGKLEIGFDYGNAHTKNGYHLEPGASKNGYMITLEHTQGEFFGGFNKFVAQYATDSMTSWNTGHSQGGSVNNNGDMLRLIDHGVVQFSPKVEMMYALIYEKTDLDNNQGKTWYSAGIRPMYKWNKTMSTLLEVGYDRIKEQSSGKKNDLAKVTLAQQWQAGDSIWARPAIRVFGTYGHWNDKFNITDRTNAGYKAKDAEFVAGVQFEAWW", "text": "FUNCTION: Involved in the transport of maltose and maltodextrins. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family."}
{"protein": "MHAALVPTWSSPCPIYTEIPDPGPPPPEQLQLKVLAVGIPRVVRLRARGIHPTAKSASLPYDPSIDGVGIDEQTGIMYYILPLSASCLAEKVNVDRDNLVPLQPGAPKPQPRNGPENGYGIALGDAADHRAETLDPIAIAGLVNPVSSSWMALRTRVDGEITGKTVLVLGATSKSGRAAVLVARFLGANKVIGVARREEGLRSVEGLDGWVTSGDMLPGETGVRFALPDWVGPVHIVLDYVGGSVAAGVLGSAEIEEGRELQYVQVGNLALELGTGEKHMFETLPGHLISRKPICIRGSGMGSFSRRDLVREMPGLVAFLARMKAPFGIASAPMCEVASVWQDEDTKGSRVVIVP", "text": "FUNCTION: Probable NADPH-dependent quinone reductase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L- tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MTTVTVTTEIPPRDKMEDNSALYESTSAHIIEETEYVKKIRTTLQKIRTQMFKDEIRHDSTNHKLDAKHCGNLQQGSDSEMDPSCCSLDLLMKKIKGKDLQLLEMNKENEVLKIKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVALSSETPRTKVSKAVSTSELKTEGVSPYLMLIRLRK", "text": "FUNCTION: Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC120, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localizes to the subdistal appendages of centrioles (PubMed:28422092)."}
{"protein": "MAMAMRLPAISRAVTEVASAPVGLRRLFCSNASRFSFLSPQAESQTPARPQAEPSTNLFVSGLSKRTTSEGLRTAFAQFGEVADAKVVTDRVSGYSKGFGFVRYATLEDSAKGIAGMDGKFLDGWVIFAEYARPREQSQSYQPQNNMSRPPYYGNR", "text": "FUNCTION: Involved in C-to-U editing of mitochondrial RNA. Functions as minor mitochondrial editing factor. Controls 6 percent of the mitochondrial editing sites. SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MDTFLYTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCSKTNMVMVFGEITTKANVDYEKIVHKTCRDIGFVSDDVGLDADNCKVLVQIEQQSPDIAQGVHGHLTKRPEDIGAGDQGHMFGYATDETPELMPLSHVLATKLGAKLTEVRKNGTCPWLRPDGKTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPIIPAKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVASGLARRCIVQVSYAIGVPEPLSVFVDSYGTGKIPDREILQIVKETFDFRPGMISINLDLKRGGNGRFLKTAAYGHFGTGKIPDREILKIVKETFDFRPGMISINLDLKRGGNGRFLKTAAYGHFGRDDPDFTWEVVKPLKWEKPQA", "text": "FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AdoMet synthase family."}
{"protein": "MVDTHGQPLKLGYKASAEQFAPGKLADFAVQAEEQGLDSVWISDHFQPWRHVDGHAPSALVWLPWVAAKTSRVQLGTSVLTPTLRYNPAVIAQAFATLGCLAPGRAILGIGTGEALNETAVGVTFPETRERFARLREAVRLIKQLWSEERVTFEGEYYNLHDATVYDRPEQPVPIYVAAGGPGVTKYAGRAGDGYICTSGKGMDLYSETLLPALREGLEASGRTEGQIDRTIEIKLSFDEDPAQALENTRFWAPLSLTAEQKSSVHDPIEMARLADELPIEQVAKRWIVSSDPTEVAAAVQGYVDAGFTHLVFHAPGQDQSRFLTQFSADVVPLLRP", "text": "FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. SIMILARITY: Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family."}
{"protein": "MAVSTIFSQDSNSKRLLIAFAITTLFMVTEAIGGWLSGSLALLADAGHMLTDSAALFIALMAVHFSQRKPDPRHTFGYLRLTTLAAFVNAAALLLIVILIVWEAVHRFFSPHEVMGTPMLIIAIAGLLANIFCFWILHKGEEEKNINVRAAALHVLSDLLGSVGAMIAAIVILTTGWTPIDPILSVLVSVLILRSAWRLLKESFHELLEGAPQEIDINKLRKDLCTNIYEVRNIHHVHLWQVGEQRLMTLHAQVIPPLDHDALLQRIQDYLLHHYRISHATVQMEYQHCGTPDCGINQAAPADGHHRHHHHE", "text": "FUNCTION: Involved in zinc efflux across the cytoplasmic membrane, thus reducing zinc accumulation in the cytoplasm and rendering bacteria more resistant to zinc. It may contribute to zinc homeostasis at low concentrations of zinc. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
{"protein": "MEKKVICQDIFWSCDGTSFVSVHNDFGIRQYLVPEESNTDKLNRNLLLPFTRFFRNQSIVSCAIDPFYTLYNENSDRLAGDRIVVGGKNFPLQLYSLMDGQCILSYDTMNKINGEYETVYSVKIDVESRVYTGSCRNKVAIYDKSRRDAVWMNQSTKKASKGRQSIISCFEEQPMGGQALSRGSLLCGSYANEMFQVDCRHQRLERLNYTRTVAGGIVQILTSDNGRYVYVVRRNSDAISIYDRRNLQHELNVLRLPFRIHHNSAKLKAYIDTAYGLSMGTPQGTILNWGRDLVEFGGVPSHNSVEDPLITSIPPESEWRTNLDSTIPATVVKNCPGDPELFALSHGGTISLCRFGG", "text": "FUNCTION: Involved in mRNA splicing. Helps to stabilize the U1 snRNP-5' splice site interaction (By similarity). FUNCTION: Involved in mRNA splicing. Helps to stabilize the U1 snRNP-5' splice site interaction. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SWT21 family."}
{"protein": "MQRSSGINNLHIPTSPMSFSSNGINLPGSMVLDGSPSMQHLPQQQQRQLLEQQAGQGSVPMRENSYSHVDKKLRLEVKQEDLLQQQILQQLIQRQDPTGRNPQMQALLQQQRVRQHQQMLQSMSPSQRLQLQKQQQLRQQLQQQGTQQISPNVRPYEVGVCARKLMMYLYHLQQRPAENCITYWRKFVAEYFSPRAKQRLCLSQYESVGHHALGMFPQAAPDMWQCDLCGTKSGKGFEATFDVLARLIEIKFASGIIDELLYLDHPRENRFPNGLMMLEYRKAVQETVHEQFRVVREGHLRIIFSPDLKILSWEFCARRHEELLLRRLIAPQVNQLLQVAQKCQSTISESGSQGVSQQDIQSNSNMVLGAGRQLAKFMELQSLNDLGYPKRYIRTLQISEVVKSMKDLMNFTGEHKVGPLEGLKQLLEQTATVKLQRQKMQEMEQFGNSGAMSGPAQAQMTLSSGTMSGSTANNNSNNHHQIVGRGAMNGSPQATAALTNYQSMLIRQNAMNNQNSNTGNQEGFSSQNPTLNSNQSPSSSSQQRENLATSGFPSSPQMQQQQHILNGTPNMLPQNHPHQLQSPHSHGNTQEQQMLHQLLQEMTENGASVEQQQAFPGQSGSNNNTERNTTASTSNISGGGRVPSRINSFKASSNNNLPFSEDISVTDHDFSEDGFFNNSDIYGGL", "text": "FUNCTION: Probable transcription regulator that functions in the development of the carpel margin meristem similarly to SEUSS (SEU). In association with SEU, supports organ development from meristematic regions by facilitating auxin response and thus organ initiation, and by sustaining meristematic potential through the maintenance of PHABULOSA expression (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the adn1/SEU family."}
{"protein": "MPSGTSQCEDGSAGCPQDLEVQPEKGQLEKGASGDKERVWISPDTPSRCTWQLGRPMADSPHYHTVPTKSPKILPDILRKIGNTPMVRINRISKNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYMSKFLSDKWMLQKGFMKEELSVKRPWWWHLRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIHLTDTLGMLSHILEMDHFALVVHEQIQSRDQAWSGVVGGPTDRNNGVSSKQLMVFGVVTAIDLLNFVAAREQTRK", "text": "FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (By similarity). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (PubMed:20149843, PubMed:8558235). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family."}
{"protein": "MERRQSICPQGRLPLYSAVVRSTSDIQASVRFASRHNLRLVIKNTGHDSAGRSSAPHSFQIHTSLLQNISLHKNFIARGSTTGRGPAVTLGAGVMQWQAYVHGAKNGYTILGGECPTVGAVGGFLQGGGVSSIHSFTRGLAVDQVLEYQVVSANGDLITANEDNNQDLFWALKGGGGGTFGVVTEATVRVFSDDPVTVTSTKIEAAAANVLFWKEGVHELLRLLQRFNNLHVAGQLVISAPTKDSLQAGLELHFANLTDETQAIQLLRSEARALETHGISASTSVRVQRKASSELRMKPDVYPPHYGILEASVLISAATFHANDGPALIASKLSGLTLKPNDILFTSNLGGRVSENTAIEIALHPAWREAAQLVTLVRVVEPSIEGKLSALNNLTARDVPILYSIDPAAKISYRNLGDPQEKEFQTRYWGADNYARLAATKAAWDPSHLFMTSLGVGSEVWDAEGICRKRRGFRAKASSLIGM", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L- methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non- enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate- dependent dioxygenase easH which introduces a hydroxyl group into N-(D- lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MSKTVKKFETEVQQLLDLVIHSLYSNKDIFLRELISNASDAIDKVLFESHQNAAVIEGEPEGKIKLIPDKDAGTLTIRDNGVGMTLEEVEKNIGTIAHSGTKAFLANLKEQNVADHPELIGQFGVGFYASFMVADRVTLVTRRAGHDKAAGVRWESTGDGTYTVEECAKETRGTEITLHLKEEMKEYLDEWKIRSIVRKYSDYVQYPIVMDVTRTEVPKGVNGEEIEGAGTIEKTEEETLNSMKAIWTRSKSEVTEEEYEEFYKHVSHDFEKPLKTIHYSAEGTSEFKALLYLPAHKPFDLFMPERKKGVQLYVRRVFITDSCEQLLPDYLRFVKGVVDSSDLPLNVSREILQEDVQIKRIQKSLVSKILSTLSEMREKEADSYLDFYKEFGPVLKEGVHFDYANRDKLQDLLLFESTATDAGSFVSLKEYVERMPEGQEEIYFITGTSRAALEQSPHLEIFRKKGYEVLFLTDPVDEWVVQGLPEYGGKKLKAVDRGDVIPATEEEKKEQEAKREEAAKQYGDLLSFVKEKLAERVKEVRLSNRLTDSACCLVADEHGLNANMERILRAMNQTVPESKRILELNPDHPIMQVMATLFGKDKTNPRLADYCDLLYDQALLTEGSPIADPLRFTRLVAELMVADGKAAAGE", "text": "FUNCTION: Molecular chaperone. Has ATPase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family."}
{"protein": "MNIAIRNPVATRPAERREEGSLQVALDPDLRIDTAKVFAVYGKGGIGKSTTSSNLSVAFSKLGKRVLQIGCDPKHDSTFTLTKRLAPTVIDALEAVKFHAEELRVEDFVVEGYNGVMCVEAGGPPAGTGCGGYVVGQTVKLLKEHHLLEETDVVVFDVLGDVVCGGFASPLQHADRALIVTANDFDSIFAMNRIVAAIHAKAKNYGVRLGGVIANRSAATDEIDRFNAAVGLRRLAHFQDLDVVRRSRLRKATLFEMESSPELDAVLAEYLALAEALWAGVEPLEAEPMRDRDLFEFLGFD", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. SIMILARITY: Belongs to the NifH/BchL/ChlL family."}
{"protein": "MRAELNQGLIDFLKASPTPFHATASLARRLEAAGYRRLDERDAWHTETGGRYYVTRNDSSLIAIRLGRRSPLESGFRLVGAHTDSPCLRVKPNPEIARNGFLQLGVEVYGGALFAPWFDRDLSLAGRVTFRANGKLESRLVDFRKAIAVIPNLAIHLNRAANEGWPINAQNELPPIIAQLAPGEAADFRLLLDEQLLREHGITADVVLDYELSFYDTQSAAVVGLNDEFIAGARLDNLLSCHAGLEALLNAEGDENCILVCTDHEEVGSCSHCGADGPFLEQVLRRLLPEGDAFSRAIQRSLLVSADNAHGVHPNYADRHDANHGPALNGGPVIKINSNQRYATNSETAGFFRHLCQDSEVPVQSFVTRSDMGCGSTIGPITASQVGVRTVDIGLPTFAMHSIRELAGSHDLAHLVKVLGAFYASSELP", "text": "SIMILARITY: Belongs to the peptidase M18 family. SIMILARITY: Belongs to the peptidase M18 family."}
{"protein": "MQPSYKDLHCACQSNSQTNQSSVYSMSDDIWEDDDEDEEQEEYDRGDNSNDYNKDGVGSRQQNKQTQSLAMNEIARRHRKQGYVDGLAKHQEENLQKGFDFAYSIGADLGIKVGRLLARACIADGANNDLKDKSGGSGNDLGSLKECMNALNISKVLDLKYFDDHLNLKDGKHGLIEEWQNKSN", "text": "FUNCTION: The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the YAE1 family."}
{"protein": "MATLQCRIVSAREELYSGEISMLIASGTEGEIGILPGHTPLITLLKPGAMRVQTSNGEEEVIYVSGGVLEVQPKMVTVLADTAMRAHNLDESKIVEARKKAEQMLVNQSDTVQINAALASLAESVAQLQTIRKYKNRA", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family."}
{"protein": "MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKESKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPVAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDLDLHNQASVPLEPRPLRRESEI", "text": "FUNCTION: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Blocked by external barium or cesium (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane; Lipid-anchor. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ2 subfamily."}
{"protein": "MTHLHFDNRLRQQLPGDPEEGARRREVGAAWSSVLPTPVAAPYLIAHSAEMAQVLGLEAAEIASAQFAQVFGGNALYPGMQPWAVNYGGHQFGHWAGQLGDGRAISLGEAIGTDGGRYELQLKGAGPTPYSRGADGRAVLRSSIREFLCSEAMHHLGVPTTRALSLVGTGEAVVRDMFYDGHPQREPGAIVCRVAPSFIRFGNFELPSARGDIALLKQWVDFTIARDFPALAGAGEALYADWFAQVCERTAVMVAHWMRVGFVHGVMNTDNMSILGLTIDYGPYGWVDDYDPDWTPNTTDAQGRRYRFGTQPQVAYWNLGRLAQALAPLFADQALLQYGLDRFRDTYLACDRRDTAAKLGLAECRDEDLQLIDALRALMRESEMDMTLTFRGLIDLSPEHPDPAQLRDAFYDEDKRLVDAPQLQQWLQRYAARLQQDPLSPEERRARMRLANPRYVLRNYLAQQAIDRAEQGDPSGVQELLEVMRRPYDDQHGRDAFAARRPDWARDRAGCSMLSCSS", "text": "FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation). SIMILARITY: Belongs to the SELO family."}
{"protein": "MSDNQVKIKKQTIDPTLTLEDVKKQLIDKGKKEGHLSHEEIAEKLQNFEMDSDQMDDFFDQLNDNDITLVNEKDSSDTDDKINPNDLSAPPGVKINDPVRMYLKEIGRVNLLSAQEEIELAKRIEQGDEIAKSRLAEANLRLVVSIAKRYVGRGMLFLDLIQEGNMGLIKAVEKFDFSKGFKFSTYATWWIRQAITRAIADQARTIRIPVHMVETINKLIRVQRQLLQDLGRDPAPEEIGEEMDLPPEKVREILKIAQEPVSLETPIGEEDDSHLGDFIEDQEAQSPSDHAAYELLKEQLEDVLDTLTDREENVLRLRFGLDDGRTRTLEEVGKVFGVTRERIRQIEAKALRKLRHPSRSKRLKDFMD", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily."}
{"protein": "MTESAMTSRAGRGRGADLVAAVVQGHAAASDAAGDLSFPDGFIWGAATAAYQIEGAWREDGRGLWDVFSHTPGKVASGHTGDIACDHYHRYADDVRLMAGLGDRVYRFSVAWPRIVPDGSGPVNPAGLDFYDRLVDELLGHGITPYPTLYHWDLPQTLEDRGGWAARDTAYRFAEYALAVHRRLGDRVRCWITLNEPWVAAFLATHRGAPGAADVPRFRAVHHLLLGHGLGLRLRSAGAGQLGLTLSLSPVIEARPGVRGGGRRVDALANRQFLDPALRGRYPEEVLKIMAGHARLGHPGRDLETIHQPVDLLGVNYYSHVRLAAEGEPANRLPGSEGIRFERPTAVTAWPGDRPDGLRTLLLRLSRDYPGVGLIITENGAAFDDRADGDRVHDPERIRYLTATLRAVHDAIMAGADLRGYFVWSVLDNFEWAYGYHKRGIVYVDYTTMRRIPRESALWYRDVVRRNGLRNGE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MSWRGRSTYYWPRPRRYVQPPEVIGPMRPEQFSDEVEPATPEEGEPATQRQDPAAAQEGEDEGASAGQGPKPEADSQEQGHPQTGCECEDGPDGQEVDPPNPEEVKTPEEGEKQSQC", "text": "SIMILARITY: Belongs to the GAGE family."}
{"protein": "MSNKESNVALQTLRVTKDMKDFLSHRIVGEPPANIKIEYQKIHRYRTCVCPSTGHISELCPSGDLILSLGAHRNVIAAATVYDVVKNKIKSTTSKAGTSSTLSSLGLSGFQKPKIGSKNKKTMFSKQNNSTNESDESGGEEGSSLNDLPKSDLINAIMELASQGRNNSKGKGKRGGKR", "text": "FUNCTION: Constituent of viral factories. Binds to ssRNA and dsRNA (By similarity). SUBCELLULAR LOCATION: Host cytoplasm Note=Constituent of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the phytoreovirus RNA-binding protein family."}
{"protein": "MAAIPSSGSLVATHDYYRRRLGSSSSNSSGGSAEYPGDAVPHSPGLPKADSGHWWASFFFGKSTLPFMAAVLESPEHSAESPQASRSPISCGLAPETMKKQPVMHPSQTNSRAPS", "text": "FUNCTION: Probable regulator of exocrine pancreas development. SIMILARITY: Belongs to the PPDPF family."}
{"protein": "MNHDYGRLVSRAALAATLVATLLLIIKIFAWWYTGSVSILAALVDSLVDIAASLTNLLVVRYSLQPADEEHTFGHGKAESLAALAQSMFISGSALFLFLTGIQHLITPEPMRAPLVGIVVTVAALVTTLMLVTFQRWVVRKTRSQAVRADMLHYQSDVMMNGAILVALALSWYGLHRADALFALGIGVWILYSALRMGYEAIQSLLDRALPDDERQAIVDIVAAWPGVRGAHDLRTRQSGPTRFIQLHLEMEDNLPLVQAHLIAEQVEQAILSRFPGSDVIIHQDPCSVVPRFQQGQFEH", "text": "FUNCTION: Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. FieF subfamily."}
{"protein": "MMEPPLSKRNPPALRLADLATAQAQQLQNMTGFPVLVGPPAHSQRRAVAMHLHPRDLGTDPGVASTALGPEHMAQASGQGPCPPSQGLPGLFQVPAPAARSVASGTHPGARTHPDGGGSSGAQASAPPPPAPPLPPSQSSSPPPPPPPPPALSGYTATNSGGGSSSGKGHSRDFVLRRDLSATAPAAAMHGAPLGGEQRSGSSSPQHPTPPPHPAGMFISASGTYAGRDGGGSALFPALHDSPGAPGGHPLNGQMRLGLAAAAAAAAELYGRAEPPFAPRSGDAHYGAVAAAAAAALHGYGAVNLNLNLAAAAAAAAAAGPGPHLQHHAPPPAPPPAPAPHPHHPHLPGAAGAFLRYMRQPIKRELICKWLDPEELAGPPASADSGVKPCSKTFGTMHELVNHVTVEHVGGPEQSSHVCFWEDCPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFDGCDRKFANSSDRKKHSHVHTSDKPYYCKIRGCDKSYTHPSSLRKHMKIHCKSPPPSPGALGYSSVGTPVGDPLSPVLDPTRSRSSTLSPQVTNLNEWYVCQASGAPSHLHTPSSNGTTSESEDEEMYGNPEVMRTIH", "text": "FUNCTION: Essential for neural crest development, converting cells from an epidermal fate to a neural crest cell fate. Binds to DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
{"protein": "MAVPKKKMSKSRRNSRKSNWKKKVLKKVLFALSLGKSFEANTNVNFSFGDKLPQ", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
{"protein": "MGLCVNGAVPSEATKKDENLKRGNWGNQIEFVLTSVGYAVGLGNVWRFPYLCYRNGGGAFMFPYFIMLIFCGIPLFFMELSFGQFASQGCLGVWRVSPIFKGVGYGMMVVSTYIGIYYNVVICIAFYYFFASMNRVLPWTYCNNLWNTNNCAGVLSPNSSASFNLSSQQNLLNLTLGLNQTLKRTSPSEEYWRRHVLKISEDIGDFGEVQLPLLGCLGVSWLVVFLCLIRGVKSSGKVVYFTATFPYVVLTILFIRGITLEGAINGILYYLTPQWDKILHAMVWGDAASQIFYSLGCAWGGLITMASYNKFHNNCYRDSIIISITNCATSVYAGFVIFSILGFMATHLGVDVSEVADHGPGLAFVAYPEALTLLPISPLWSILFFFMLILLGLGTQFCLLETLVTAVVDEIGNDWIIRWKTLVTLGVAIIGFLLGIPLTTQAGIYWLLLMDNYAASFSLVIISCIMCIAVMYIYGHRKYFKDIEMMLGFPPPLFFQICWRFISPGIIFFILIFTVIQYRPIQYNDYLYPDWAITIGFLMALSSVICIPLYAIFKIWCSEGDTFLQRLKNAVKPSKDWGPALQEHRTGRYAQMSSTRSESNPEAQPLNPEKMKEDLSLTIQGSNGQAHTQDSKV", "text": "FUNCTION: Sodium- and chloride-dependent glycine transporter which is essential for regulating glycine concentrations at inhibitory glycinergic synapses. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A9 subfamily."}
{"protein": "MSGKGKSAGADKASTSRSAKAGLTFPVGRIHRLLRKGNYAQRVGSGAPVYLTSVLEYLTAEILELAGNAARDNKKSRIIPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNIHQNLLPKKSGKGDKASQEL", "text": "FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H2A family."}
{"protein": "MRAKLLGIVLTTPIAISSFASTETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKVSQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRGGNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIKGWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGFRDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELGGTFKYSGWVEASDNDEHYDPGKRITYRSKVKDQNYYSVSVNAGYYVTPNAKVYVEGTWNRVTNKKGNTSLYDHNDNTSDYSKNGAGIENYNFITTAGLKYTF", "text": "FUNCTION: Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A26 family."}
{"protein": "MDYSYLNSYDSCVAAMEASAYGDFGACSQPGGFQYSPLRPAFPAAGPPCPALGSSNCALGALRDHQPAPYSAVPYKFFPEPSGLHEKRKQRRIRTTFTSAQLKELERVFAETHYPDIYTREELALKIDLTEARVQVWFQNRRAKFRKQERAASAKGAAGATGAKKGEARCSSEDDDSKESTCSPTPDSTASLPPPPAPSLASPRLSPSPLPAALGSGPGPQPLKGALWAGVAGGGGGGPGTGAAELLKAWQPAEPGPGPFSGVLSSFHRKPGPALKTNLF", "text": "FUNCTION: May be involved in regulating the specificity of expression of the catecholamine biosynthetic genes. Acts as a transcription activator/factor. Could maintain the noradrenergic phenotype (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family."}
{"protein": "MDNNNDFWKFSDQLRLESGLANLSLNDYSIWSNSYSSKRPDQRRNFDVKGSDFNNNNNSSKAFDDDFNDGWKITNSNGPLFSMPHNNNNNTLEVGGFNKGGGIYSNTNTTISSYHPNNLNNNAFGGFNKGIYSNTTSSPYLNNNHHHLDDNNNLNRNNLKGYKTYFKGEDQFHTPKSAKKKNTTNNTNNKKHGDNTNNNDGTKTGAEKKFKTLPPSESLPKNETIGGYIFVCNNDTMAENLQRQLFGLPPRYRDSVRTITPGLPIFLYNYSTHQLHGIFEAASFGGSNIDPTAWEDKKCPGESRFPAQVQVITRKVCEPLEEDSFRPILHHYDGPKFRLELSVPEALSLLDIFANQNSFDDIFKAIPA", "text": "FUNCTION: Involved in stress signaling pathway that mediates cell death in response to endoplasmic reticulum (ER) stress and osmotic stress. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MLMPRRMKYRKQQRGRLKGATKGGDYVAFGDYGLVALEPAWITAQQIEAARVAMVRHFRRGGKIFIRIFPDKPYTKKPLEVRMGKGKGNVEGYVAVVKPGRVMFEVAGVTEEQAMEALRIAGHKLPIKTKIVRRDAYDEAQ", "text": "FUNCTION: This protein binds directly to 23S rRNA. Interacts with the A site tRNA. SIMILARITY: Belongs to the universal ribosomal protein uL16 family."}
{"protein": "MSSLKVSQQDKKWVNSGSVAILAYCASSILMTITNKVVMSDRTFNMNFLLLFIQSLVCVITLLVLKVLGSVNFRSFNKTDARNWFPISICLVLMIFTSSKSLQYLSVPVYTIFKNLTIIVIAYGEVLFFGSSVGNMELGSFALMIVSSLIAAHGDYLHSVERLKKMLGPNVSFSFIVNIGYFWIAANCFASALFVLLMRKRIQVTNFKDFDTMFYNNVLSLPLLLLGSYLFEDWSQENLLPHVDIDNLSTMIISGLASVAISYCSGWCVRVTSSTTYSMVGALNKLPIALTGFLFNDAARNLSSAASILLGFASGIIYAVAKQKKLQNSEKI", "text": "FUNCTION: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily."}
{"protein": "MQSYGNPDVTYEWWAGNSVVTSRSGRFIASHIGHTGLIAFAAGGSTLWELARYNPEIPMGHQSSLFLGHLAAFGVGFDEAGAWTGVGVAAVAIVHLVLSMVYGGGALLHAVYFEADVADSEVPRARKFKLEWNNPDNQTFILGHHLFFFGMACIAFVEWARIHGIYDPAIGSVRQVNYNLDLTMIWNRQFDFIGIDSLEDVMGGHAFLAFAELTGATIHMVAGSTQWENKRLGEWSKYKGAELLSAEAVLSWSLAGIGWMAIVAAFWAATNTTVYPIEWFGEPLKLQFSVAPYWIDTADSTGITAFFGHTTRAALVNVHYYFGFFFLQGHFWHALRALGFDFKKVSEAIGNTEGATVRVEGAGFNGRAPR", "text": "FUNCTION: The antenna complex functions as a light receptor, it captures and delivers excitation energy to photosystems II and I. The Prochlorales pcb genes are not related to higher plant LHCs. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. IsiA/Pcb subfamily."}
{"protein": "MANASEPGGGGGGAEAAALGLRLATLSLLLCVSLAGNVLFALLIVRERSLHRAPYYLLLDLCLADGLRALACLPAVMLAARRAAAAAGTPPGALGCKLLAFLAALFCFHAAFLLLGVGVTRYLAIAHHRFYAERLAGWPCAAMLVCAAWALALAAAFPPVLDGGGADDEDAPCALEQRPDGAPGALGFLLLLAAVVGATHLVYLRLLFFIHDRRKMRPARLVPAVSHDWTFHGPGATGQAAANWTAGFGRGPTPPALVGIRPAGPGRGARRLLVLEEFKTEKRLCKMFYAITLLFLLLWGPYVVASYLRVLVRPGAVPQAYLTASVWLTFAQAGINPVVCFLFNRELRDCFRAQFPCCQSPQATQATLPCDLKGIGL", "text": "FUNCTION: Orphan receptor. Possible candidate for amine-like G-protein coupled receptor (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRFEDYPAEPFRIKSVETVKMIDKAAREEVIKKAGYNTFLINSEDVYIDLLTDSGTNAMSDKQWGGLMQGDEAYAGSRNFFHLEETVKEIFGFKHIVPTHQGRGAENILSQIAIKPGQYVPGNMYFTTTRYHQERNGGIFKDIIRDEAHDATLNVPFKGDIDLNKLQKLIDEVGAENIAYVCLAVTVNLAGGQPVSMKNMKAVRELTKKHGIKVFYDATRCVENAYFIKEQEEGYQDKTIKEIVHEMFSYADGCTMSGKKDCLVNIGGFLCMNDEDLFLAAKEIVVVYEGMPSYGGLAGRDMEAMAIGLRESLQYEYIRHRILQVRYLGEKLKEAGVPILEPVGGHAVFLDARRFCPHIPQEEFPAQALAAAIYVECGVRTMERGIISAGRDVKTGENHKPKLETVRVTIPRRVYTYKHMDVVAEGIIKLYKHKEDIKPLEFVYEPKQLRFFTARFGIKK", "text": "SIMILARITY: Belongs to the beta-eliminating lyase family."}
{"protein": "MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGCDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGNAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSVVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRIEIQPKHIFWSGSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQHPLVTPNEERNVMEEAKGFQPSRSTAQQELDGKPASPTPVIVASHTANKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD", "text": "FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). FUNCTION: This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP- dependent manner (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. SIMILARITY: Belongs to the WD repeat COPB2 family."}
{"protein": "MSTDNKQSLPAITLAAIGVVYGDIGTSPLYTLRECLSGQFGFGVERDAVFGFLSLIFWLLIFVVSIKYLTFVMRADNAGEGGILTLMSLAGRNTSARTTSMLVIMGLIGGSFFYGEVVITPAISVMSAIEGLEIVAPQLDTWIVPLSIIVLTLLFMIQKHGTAMVGKLFAPIMLTWFLILAGLGLRSIIANQEVLYALNPMWAVHFFLEYKTVSFIALGAVVLSITGVEALYADMGHFGKFPIRLAWFTVVLPSLTLNYFGQGALLLKNPEAIKNPFFLLAPDWALIPLLIIAALATVIASQAVISGVFSLTRQAVRLGYLSPMRIIHTSEMESGQIYIPFVNWMLYVAVVIVIVSFEHSSNLAAAYGIAVTGTMVLTSILSTTVARQNWHWNKYFVALILIAFLCVDIPLFTANLDKLLSGGWLPLSLGTVMFIVMTTWKSERFRLLRRMHEHGNSLEAMIASLEKSPPVRVPGTAVYMSRAINVIPFALMHNLKHNKVLHERVILLTLRTEDAPYVHNVRRVQIEQLSPTFWRVVASYGWRETPNVEEVFHRCGLEGLSCRMMETSFFMSHESLILGKRPWYLRLRGKLYLLLQRNALRAPDQFEIPPNRVIELGTQVEI", "text": "FUNCTION: Responsible for the low-affinity transport of potassium into the cell. Likely operates as a K(+):H(+) symporter. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family."}
{"protein": "MVLITVLANLLILQLSYAQKSSKLVFGGDECNINEHRSLVVLFNSSGFLCAGTLINKEWVLTAAHCDSENFQMQLGVHSKKVPNKDEETRDPKEKFICPNRKKNDEKDKDIMLIRLNRPVSNSEHIALLSLPSSPPSVGSVCRIMGWGTISPTKEIYPDVPHCADINILDHAVCRAAYSGWLATSTTLCAGILEGGKDSCHGDSGGPLICNGQFQGIVSLGRHPCGHPDEPGVYTKVFDYTDWIQSIIAGNTDAACPP", "text": "FUNCTION: Snake venom serine protease that activates plasminogen. Weakly hydrolyzes the alpha chain of human fibrinogen without releasing fibrinopeptide A. Does not hydrolyze plasma kallikrein or factor Xa. Does not clot fibrinogen. Does not affect platelet function. Induces hypotensive effects on rats. Shows a preferential cleavage at Lys-|-Xaa over Arg-|-Xaa bonds. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MASSSGLRSCSAVGVPSLLAPSSRSGRSGLPFCAYATTSGRVTMSAEWFPGQPRPAHLDGSSPGDFGFDPLGLATVPENFERFKESEIYHCRWAMLCVPGVLVPEALGLGNWVKAQEWAALPDGQATYLGNPVPWGNLPTILAIEFLAIAFAEQQRTMEKDPEKKKYPGGAFDPLGFSKDPAKFEELKLKEIKNGRLAMLAFVGFCVQQSAYPGTGPLENLATHLADPWHNNIGDIVIPRNIYGP", "text": "FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family."}
{"protein": "MSAYRHAVERIDSSDLACGVVLHSAPGYPAFPVRLATEIFQRALARLPGDGPVTLWDPCCGSGYLLTVLGLLHRRSLRQVIASDVDPAPLELAAKNLALLSPAGLTARELERREQSERFGKPSYLEAAQAARRLRERLTAEGGALPCAIRTADVFDPRALSAVLAGSAPDVVLTDLPYGERTHWEGQVPAQPVAGLLRSLASALPAHAVIAVTDRSRKIPVAPVKALERLKIGTRSAVLVRAADVLEAGP", "text": "FUNCTION: Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic."}
{"protein": "LVNQHLCGSHLVEALYLVCGERGFFYTPKAGIVEQCCNSICSLYQLETYCN", "text": "FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
{"protein": "MNWITNFVRPRINSVFGRRAIPENLWVKCPETGAMVYHKDLKENQWVISSSDFHMKIPAKERLKFLFDNAKYCLLDQPQVCQDPLKFRDNKKYIDRLKENRSKTGLIDSIVSAVGNVRDFKLVAVVHEFSFIGGSIGIAAGEAIVKSCERAIAEKCPLVMFTASGGARMQEGILSLMQLPRTTIAINMLKDAGLPYIVVLTNPTTGGVTASYAMLGDIHLAEPGAEIGFAGRRVIEQTVREKLPDGFQRSEYLVEHGMIDRIVHRHDIPEVVSSLCKILTKSVQ", "text": "FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AccD/PCCB family."}
{"protein": "MLDTGLLLVVILASLSVMFLVSLWQQKIRERLPPGPTPLPFIGNYLQLNMKDVYSSITQLSERYGPVFTIHLGPRRIVVLYGYDAVKEALVDQAEEFSGRGELPTFNILFKGYGFSLSNVEQAKRIRRFTIATLRDFGVGKRDVQECILEEAGYLIKTLQGTCGAPIDPSIYLSKTVSNVINSIVFGNRFDYEDKEFLSLLEMIDEMNIFAASATGQLYDMFHSVMKYLPGPQQQIIKVTQKLEDFMIEKVRQNHSTLDPNSPRNFIDSFLIRMQEEKYVNSEFHMNNLVMSSLGLLFAGTGSVSSTLYHGFLLLMKHPDVEAKVHEEIERVIGRNRQPQYEDHMKMPYTQAVINEIQRFSNLAPLGIPRRIIKNTTFRGFFLPKGTDVFPIIGSLMTEPKFFPNHKDFNPQHFLDDKGQLKKNAAFLPFSIGKRFCLGDSLAKMELFLLLTTILQNFRFKFPMNLEDINEYPSPIGFTRIIPNYTMSFMPI", "text": "FUNCTION: Highly active in the 15-alpha-hydroxylation of testosterone. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MAVCLPDTQDDTPSIPIKLTRVGVTGVKKLLQLERNNKRPIILVPTFDAFVDLPNDQKGVHMSRNPEAISEVLDEVANDSSVEVETLCAKIVSKMMSKHEYAKRVEISMTTDYMFMKESPVTKNKTQEMAKLKAKAVGYREDGEIKIRKSIGAEVIGMTVCPCAQESVKESDKNKLLEFLDEETTQKVLDTVTFASHNQRGVGTLLIEVPEDREVKGEDIIEIIEESMSSPVCELLKRPDENATVLNAHKKPVFVEDCVRNMMEKIAKKYADFPEDTIITSRQENHESIHRHNAFAEKVTTMGELKEELRI", "text": "FUNCTION: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin. SIMILARITY: Belongs to the GTP cyclohydrolase IV family."}
{"protein": "MVGASRTILSLSLSSSLFTFSKIPHVFPFLRLHKPRFHHAFRPLYSAAATTSSPTTETNVTDPDQLKHTILLERLRLRHLKESAKPPQQRPSSVVGVEEESSIRKKSKKLVENFQELGLSEEVMGALQELNIEVPTEIQCIGIPAVMERKSVVLGSHTGSGKTLAYLLPIVQLMREDEANLGKKTKPRRPRTVVLCPTRELSEQVYRVAKSISHHARFRSILVSGGSRIRPQEDSLNNAIDMVVGTPGRILQHIEEGNMVYGDIAYLVLDEADTMFDRGFGPEIRKFLAPLNQRALKTNDQGFQTVLVTATMTMAVQKLVDEEFQGIEHLRTSTLHKKIANARHDFIKLSGGEDKLEALLQVLEPSLAKGSKVMVFCNTLNSSRAVDHYLSENQISTVNYHGEVPAEQRVENLKKFKDEEGDCPTLVCTDLAARGLDLDVDHVVMFDFPKNSIDYLHRTGRTARMGAKGKVTSLVSRKDQMLAARIEEAMRNNESLESLTTDNVRRDAARTHITQEKGRSVKQIREVSKQRNSRDKPSSSSPPARSTGGKTPVRKSSSSSFSKPRKASSPPEKSSKPKRKILKTVGSRSIAARGKTGSDRRPGKKLSVVGFRGKSSSARAS", "text": "SIMILARITY: Belongs to the DEAD box helicase family."}
{"protein": "MSIPTMQWAQVAEKVGGPLVYKQIPVPKPGPDQILVKIRYSGVCHTDLHAMMGHWPIPVKMPLVGGHEGAGIVVAKGELVHEFEIGDQAGIKWLNGSCGECEFCRQSDDPLCARAQLSGYTVDGTFQQYALGKASHASKIPAGVPLDAAAPVLCAGITVYKGLKEAGVRPGQTVAIVGAGGGLGSLAQQYAKAMGIRVVAVDGGDEKRAMCESLGTETYVDFTKSKDLVADVKAATPDGLGAHAVILLAVSEKPFQQATEYVRSRGTIVAIGLPPDAYLKAPVINTVVRMITIKGSYVGNRQDGVEALDFFARGLIKAPFKTAPLKDLPKIYELMEQGRIAGRYVLEMPE", "text": "SUBCELLULAR LOCATION: Cytoplasm Secreted. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MQMESQRRDVFYVSDGTAITCETLGHVVLGQFAVQPNEKTFPFVESDEKLSELLKQIQRSYQLHGVKPLVFFSMVIPEMRTRLLQAPAHFYDVLESIVQRVSLDIEMEPAPKLQRSRSVGKDSDTYFDRIAAIEYTLAHDDGVSLKDLDRADIILLGVSRSGKTPTSLYMAMQFGLRVVNYPFIAEDMHAMRLLPEFEFHRHKLFGLTINAERLTEIRENRLAGSEYASNQQCQQELATVEALFRREAISYINTSSLSVEEISTRILERTGLKRRLF", "text": "FUNCTION: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation. SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PSRP subfamily."}
{"protein": "MTITPPALSVFETLESEVRSYCRGWPAVFDRAQGARLTDEDGHSYLDFFAGAGSLNYGHNNPVLKRALIDYIERDGITHGLDMATTAKRAFLETFQNVILRPRDLPYKVMFPGPTGTNAVESALKLARKVKGRESVVSFTNAFHGMSLGSLAVTGNAFKRAGAGIPLVHGTPMPFDNYFDGTVPDFLWFERLLEDQGSGLNKPAAVIVETVQGEGGINVARAEWLRALQELCLRQVMLLIVDDIQMGCGRTGGFFSFEEAGIVPDIVTLSKSISGYGLPMSLCLFKPELDIWEPGEHNGTFRGNNPAFVTAAAVLDAYWADGQMEKQTLARGEQVEQTLLAICAEEPTAQFRGRGLVWGMEFEDKARASAVCARAFELGLLLETSGPQSEVVKLLPPLTITPEELDEGLRTLARCVRETA", "text": "FUNCTION: Catalyzes reversively the conversion of L-aspartate beta- semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination with L-glutamate. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MPVGLSVGGALGDPSPSRPFRPSRYVPVSAATAFLVGATTLFLCFTCPWLSEKFSSFIPLYNVVVFLFTLANFCMATFMDPGVFPRAEEDEDKEDDFRAPLYKTVEVRGIQVRMKWCSTCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTVHIMDVFGFSLLYILHHTKQLDLVQSGVTMAVMCVAGLFFVPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTHGCFKNIAHVLCSSQAPRYLGRLRKPQSVQVQPPFLRPPLSEAQLAAKVLDNGIQQSKSSLEIMESQSTDADPPPPPKPEHRYPGLPHTQNEECSLLTEAPPTPSLYKYRPAYSSPGKNHTASTHSSKMSRGNSMTESPSVPVTTGQPSYRSDPSLSSRGAAGCRGGAEGGRSGSGGLGGASAFGGRSYPSFTDTLLQSAAASCSSSLRSAHTAHNALGPLISEGTTSTSYKSLANQTRNGSLSYESLLTPSESPEFESAAHELSPPRPHPPHSLSTAAGAAPILGYTSPFLSAQQREGSLQACPAPLRPSPNRAFLRPISSPPSRAPPLSPRARSLGSPPPGPAPGHTPLGKSMSYGGGAELQHRPSSSGGGTSMPNSTIKQNVANHNTHSHKPARGVKKVSGVGGTTYEISV", "text": "FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily."}
{"protein": "MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDYYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPRPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA", "text": "FUNCTION: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane protein Note=Localizes to the Z ring in an FtsZ-dependent manner. SIMILARITY: Belongs to the ZipA family."}
{"protein": "MDKIKIITDSTCDLSKEIIEKYDIDVMPMLINFGEESYLDGVEIKVDSMMERIEREDTLPTTAQIVPTRFIEKYKGYLEEGYKVISIHISSNMSGTYQSACLAKTELESDDIVVIDSRNVTVGLGLIILKAARLIESGITLEDLEKEILEYRNHIKSTIAFESLDNLVRGGRLSKGKALFVSALGIKLMLNVLDGEMNVQGKIRGTKKMVKAMIEQFDSIPKKEGEPIILVELENEDIYLPIKEYLENNNIEYLKLPLGCSVAIHSGPKVCALFYVEEY", "text": "FUNCTION: May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism."}
{"protein": "CNMALADIVRLPPASEAPFAPLGAPRDLSGPPSKLAVRPWGGADLPGPGLQLLHGTTTLAFKFAHGVVVAVDSRATAGSYIASQTVQKVIEINPSLLGTMAGGAADCSFWERLLARQCRVYELRNKEPISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGTRIPGEAFAVGSGSSYAYGVLDGGRRPDMATDEALELARRAIFQAARRDAYSGGSVTVYHVGPRGWRRVSSHDVAGLHDGYGG", "text": "FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP- dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin- independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MPRPPICRRVEFLPGVTYFKPAAVPLRELEEVVLAVEELEAIRLKDKEGLEQEDCAARMGVSRPTFVRILNSARDKVADALVNGKAIRVEGGYYHLVGPKVRCRRCGHEWEPEQGGKEACPRCGSEELAGRGPGRGRCHRHGRFGEGEH", "text": "SIMILARITY: Belongs to the UPF0251 family."}
{"protein": "MRSSTVLYVLGAAILAVNGVTTALISDGVDKGSQEQTRWLRSNAMEHETDDEERVLEFKLPSSISTWRAERFERLESLEKQKEMERQAVLELVDKYAPLLLTDRMFAGFTKLDQEGIPLPSMIALLREHGKDITSEMEAYLINSYKTTHKIPLELNTAR", "text": "FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus Host cytoplasm. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MNFDTIIIGGGMAGLSCALRCLEAGLKTAVIASGQSALHFSSGSIDVLAKTPSGEPVSNPMTCIDTFAKEYPNHPYATLGKETVERAIDWYRNTLSTIGVPLTSQNNGLNHYRLTPLGAMKSTWLSQPFVHQFPMDLEKNKTQKMVLITIDGFRDFQPKLAQDNLKQITQLSDLEITTANISLSAFNDIQRNHCELRSIDLSRLLSKRANRQELAYALQQHAQPGDLVVIPSIFGNGTGLTYLKEIEQLTKLTLCEVPTMPPSLLGIRLEESMKHAFIELGGTMLNGDHVVQGEFSYVDKSDPEHSHYRLNRIFTKNHGDFPLQAKQFVLATGSFFSQGLKANVDSMIEPIFGLDIAQSDKRTDWYSHDFFSTQSHPFLSMGIKTTANFQAIKSGHVIDNLYCAGAILSGYNPILEGSGSGVAISSGFHAAESIIEQLQPNDFFQNNNIKAEVAL", "text": "FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B family."}
{"protein": "MKKWMAGLFLAAAVLLCLMVPQQIQGASSYDKVLYFPLSRYPETGSHIRDAIAEGHPDICTIDRDGADKRREESLKGIPTKPGYDRDEWPMAVCEEGGAGADVRYVTPSDNRGAGSWVGNQMSSYPDGTRVLFIVQ", "text": "FUNCTION: Degrades both double-stranded linear and covalently closed circular DNA. Likely to play a scavenging role in order to supply nutrients under starvation conditions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: To B.subtilis NucA/ComI."}
{"protein": "MAATSTAAVDQLAADLGNTSLDNKAAAPAPIDTSAVPEAQAEGAEAAPTPTAAPHPQASASLYVGELDPSVTEAMLFELFSQIGSVASIRVCRDAVTRRSLGYAYVNYNTTADGEKALEELNYTLIKGRPCRIMWSQRDPALRKTGAGNIFIKNLDAAIDNKALHDTFAAFGNILSCKVAQDEHGNSKGYGFVHYETDEAASQAIKHVNGMLLNEKKVYVGHHIPKKDRQSKFEEMKANFTNVYVKNINNEVTDEEFRELFAKFGEVTSSSLARDQEGKSRGFGFVNFTTHEAAAQAVDELNGKDFRGQDLYVGRAQKKHEREEELRKSYEAARLEKANKYQGVNLYIKNLGDDVDDDKLRAMFSEYGPITSAKVMRDSLIEGSEEKDEKDKENKKEGETKEEEQNEGSEKKTEKKGDRKLGKSKGFGFVCFSNPDDATKAVTEMNQRMVDGKPLYVALAQRKDVRKSQLEASIQARNQLRMQQAAAQAGMPQQYMQAPVYYAGQQPGFMPAPGGRGVPFPQGGIVPGVQGGRPGQYPYQQGGRGGVPPQQMPPMGYPINQFGPGAFPPNTPQYMAAMGQVGALGGGRGGPAGRGPQGIPAGIPQGLQGGPAVPGYPPAGRPQNGGGRGTPRGNANFMAAGRGASPIPGAPADLSAGSFLQAQLATTQDPQAQKQIIGENLFPKIQAIQPALAGKITGMLLEMDNAELINLFEDDNALNVKVQEALAVYDEYLKTQGQQPTQQPAEANGEQPKAEEQKPEEQKA", "text": "FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, involved in both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. In the cytoplasm, stimulates translation initiation and regulates mRNA decay through translation termination- coupled poly(A) shortening, probably mediated by PAN (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family."}
{"protein": "MTGKITTLLFDLDGTLINTNELIIKTFQVTLQEFLPDRVFTREDILPFIGPSLMETFREINPAHADEMRAFYREYNLKHHDDLILEYDGVYEAIRALYEEDYKLGIVSTKMYDTIMRGLKVTGLDKFFQVVIGLDQVSNAKPDPEGIEMALSLLNATKEEAIMIGDNYHDIEAGKNAETLTAGVAWAIKGPEHLAQFQPDFMLEKMSDLLAIVRDEE", "text": "FUNCTION: Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PpaX family."}
{"protein": "MTILNHTLGFPRVGLRRELKKAQESYWAGNSTREELLAVGRELRARHWEQQKQAGIDLLPVGDFAWYDHVLTTSLLLGNVPARHQNNDGSVDIDTLFRIGRGRAPTGEPAAAAEMTKWFNTNYHYMVPEFVKGQQFKLTWTQLLEEVDEALALGHKVKPVLLGPVTYLWLGKVKGEQFDRLSLLNDILPVYQQVLAELAKRGIEWVQIDEPALVLELPQAWLDAYKPAYDALQGQVKLLLTTYFEGVTPNLDTITALPVQGLHVDLVHGKDDVAELHKRLPSDWLLSAGLINGRNVWRADLTEKYAQIKDIVGKRDLWVASSCSLLHSPIDLSVETRLDAEVKSWFAFALQKCHELALLRDALNSGDTAALAAWSAPIQARRHSTRVHNPAVEKRLAAITAQDSQRANVYEVRAEAQRARFKLPAWPTTTIGSFPQTTEIRTLRLDFKKGNLDANNYRTGIAEHIKQAIVEQERLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPIVIGDVSRPAPITVEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEAAGIGIIQIDEPALREGLPLRRSDWDAYLQWGVEAFRINAAVAKDDTQIHTHMCYCEFNDIMDSIAALDADVITIETSRSDMELLESFEEFDYPNEIGPGVYDIHSPNVPSVEWIEALLKKAAKRIPAERLWVNPDCGLKTRGWPETRAALANMVQAAQNLRRG", "text": "FUNCTION: Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation. SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase family."}
{"protein": "MGEEVVQALVVDNGSGNVKAGVAGDDAPRSVFPSIVGRPKNPGIMVGMEEKDAFVGDEAQTKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRERMTQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRLDLAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEKSYELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIVLSGGTTMYEGTGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWITKEEYDESGPSIVHRKCF", "text": "FUNCTION: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm. Polymerizes into shorter and less stable actin filaments compared to ACT2/actin-2; this is thought to facilitate gliding motility and host cell invasion. Has ATPase activity. ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi. ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP- Pi-bound actin. Plays an essential role during the asexual blood stage. At the segmented schizont stage, required for apicoplast migration and segregation into individual daughter merozoites. Also, required for the separation of daughter merozoites in the final stages of cytokinesis. Essential for merozoite invasion of, but not adhesion to or reorientation towards, host erythrocytes. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton Note=During host erythrocyte invasion, filamentous actin localizes close to the junction between merozoites and the host cell. In schizonts, filamentous actin appears to connect apicoplasts (By similarity). Prior to gametocyte activation in the mosquito midgut, localizes to both the cytoplasm and the nucleus. Following gametocyte activation, relocalizes completely to the cytoplasm, in an ACT2-dependent manner (By similarity). SIMILARITY: Belongs to the actin family."}
{"protein": "MADGDKAAIQFFRGTDEPVVPDIRLTRSRDGRTGQATFIFEQPEALAPETLGNIAGMWMVDEEGELVTREVNGKFVNGKPSALEATYTWKTEQDFERFMRFAERYAETKGLGYSNNSGNNEGADEASEG", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the Psb28 family."}
{"protein": "MTSLPDRGVSSSSSDPLCEGNIAPCSSSSEQKEDCSLKQSKTSILSCVFNSPFNIFEAHQDSSANKSPKSSSGSYDWSRVLRRIVCSGSMWRFLGTSKVLTSSDVWFLGKCYKLSSEESSSDSDSESGHATFLEDFSSRIWITYRRGFDAISDSKYTSDVNWGCMVRSSQMLVAQALIFHHLGRSWRRPLEKPYNPEYIGILHMFGDSEACAFSIHNLLQAGNSYGLAAGSWVGPYAMCRAWQTLVRTNREQHEVVDGNESFPMALYVVSGDEDGERGGAPVVCIDVAAQLCCDFNKGQSTWSPILLLVPLVLGLDKINPRYIPLLKETFTFPQSLGILGGKPGTSTYIAGVQDDRALYLDPHEVQMAVDIAADNIEADTSSYHCSTVRDLALDLIDPSLAIGFYCRDKDDFDDFCSRATELVDKANGAPLFTVVQSVQPSKQMYNQDDVLGISGDGNINVEDLDASGETGEEEWQIL", "text": "FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. In addition to the protease activity, also mediates delipidation of PE-conjugated ATG8 proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C54 family."}
{"protein": "MRYWGKLLGLVLGVMYAPGVVGALLGLLVGHMVDRALGAKRRGFFADQQTRQSLFFRTTFQVMGHLTKAKGRVTEVDIQLASQLMDRMQLHGAARTAAQQAFREGKESHFPLRKTLQEFRRVCFGRFDLIRIFLEIQLQAAFADGSLHPNERQVLYVIAEELGISRGQFDQFLRMFDGGRQFGGHGGWQGQQGGYSQSGYQRAPQGPTLEDACKVLGVNSSDDSVAIKRAYRKLMGEHHPDKLVAKGLPPEMMEMAKQKAQEIQAAYDLIKREKGFK", "text": "FUNCTION: Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type III membrane protein."}
{"protein": "MSSSTDDAGTTTHSLQEFKLFETQSNFYMIGWDGSGVYRVLKIDRLDPSELNISQDSTHYTKKECYELLKRIHEGNKATGGLKLVTLCYGIIGFVKFLGPYYMLLITERRHIGDLFGHSVYAVSKSEIVALHNSTVQCNFANSRDENRYKRLLCMVDLTKDFFFSYSYNVMRSYQKNVCNYETGHNLYEKMFVWNEFLTRGIRHHLRNTLWTVALVYGFFKQASLSESGKDFKITLIARRSRHNAGTRYLKRGVNRNGDVANDVETEQIVSEDVPEDHPMQISSVVQNRGSIPLFWSQETSRLNLKPDIVLSKKEPNYEATRLHFDNLVERYGNPIIILNLIKTKERRPRESILREEFVNAIDFINKDLPEENRLRFLHWDLHKHFRSKTKNVLALLCKVATCALMLTDLFYYQVTPAMTIEDSMSLSSSSDADTGDISPHTSSDDDNGDHDSLEKKSSRSKNIAYGKCDVKPPRLQSGVLRTNCIDCLDRTNVAQYAYGWAALGQQLHVLGIRDVPAIELDDPLAISLMGLYERMGDTLAHQYGGSAAHNKVFSERRGQWRAATQSQEFLRTLQRYYNNAYMDADKQDAINIFLGTFQPEQGMPAIWELRSNSLSNGRNGEMNIGKDERFLVKRCLSDGDFLHESCTPLSAMSSNHESMPQKGFSAPLQHVSHILSESSSDIPVSNDVALSRCTPSMPRKQLFGDVQKVHRFGSDQVYFGGEEDMSSVSNFVDIEWLSSENPCENALFDRSSELTRNLTAETSSTENSVNGVGQSAPTISESGSSSSKGKEPMGTKIREDFPDSFKEWVAYGEALCH", "text": "FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein."}
{"protein": "MSTDDGRRPIRRALISVYDKTGLVDLAQGLSAAGVEIISTGSTAKTIADTGIPVTPVEQLTGFPEVLDGRVKTLHPRVHAGLLADLRKSEHAAALEQLGIEAFELVVVNLYPFSQTVESGASVDDCVEQIDIGGPAMVRAAAKNHPSAAVVTDPLGYHGVLAALRAGGFTLAERKRLASLAFQHIAEYDIAVASWMQQTLAPEHPVAAFPQWFGRSWRRVAMLRYGENPHQQAALYGDPTAWPGLAQAEQLHGKDMSYNNFTDADAAWRAAFDHEQTCVAIIKHANPCGIAISSVSVADAHRKAHECDPLSAYGGVIAANTEVSVEMAEYVSTIFTEVIVAPGYAPGALDVLARKKNIRVLVAAEPLAGGSELRPISGGLLIQQSDQLDAHGDNPANWTLATGSPADPATLTDLVFAWRACRAVKSNAIVIAADGATVGVGMGQVNRVDAARLAVERGGERVRGAVAASDAFFPFPDGLETLAAAGVTAVVHPGGSVRDEEVTEAAAKAGVTLYLTGARHFAH", "text": "SIMILARITY: Belongs to the PurH family. SIMILARITY: Belongs to the PurH family."}
{"protein": "MSLEVRGIEVWRGRGRTLGPMDLTLEPGEVLAVVGPNGAGKSTLLSAMSGELRCSTGEVLLDGTPLLQWKPRERAMRLGVLPQESSLGFGFTALEVALLGRSPHSSRAEGSADLAAAVAALDATDTRHLASRSYLTLSGGERQRVQLSRVLAQLSEPLASGHRYLLLDEPTASLDLAHQHLVLEAAARFAQAGGAVLAVLHDLNLAARYAHRMAVLAEGRVVELGAPAQVLSQELVARVFGLRVQVVEWPGSPGPLVIPEGRAPLTP", "text": "FUNCTION: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Heme (hemin) importer (TC 3.A.1.14.5) family."}
{"protein": "MCSRVPLLLPLLLLLALGPGVQGCPSGCQCSQPQTVFCTARQGTTVPRDVPPDTVGLYVFENGITMLDAGSFAGLPGLQLLDLSQNQIASLPSGVFQPLANLSNLDLTANRLHEITNETFRGLRRLERLYLGKNRIRHIQPGAFDTLDRLLELKLQDNELRALPPLRLPRLLLLDLSHNSLLALEPGILDTANVEALRLAGLGLQQLDEGLFSRLRNLHDLDVSDNQLERVPPVIRGLRGLTRLRLAGNTRIAQLRPEDLAGLAALQELDVSNLSLQALPGDLSGLFPRLRLLAAARNPFNCVCPLSWFGPWVRESHVTLASPEETRCHFPPKNAGRLLLELDYADFGCPATTTTATVPTTRPVVREPTALSSSLAPTWLSPTEPATEAPSPPSTAPPTVGPVPQPQDCPPSTCLNGGTCHLGTRHHLACLCPEGFTGLYCESQMGQGTRPSPTPVTPRPPRSLTLGIEPVSPTSLRVGLQRYLQGSSVQLRSLRLTYRNLSGPDKRLVTLRLPASLAEYTVTQLRPNATYSVCVMPLGPGRVPEGEEACGEAHTPPAVHSNHAPVTQAREGNLPLLIAPALAAVLLAALAAVGAAYCVRRGRAMAAAAQDKGQVGPGAGPLELEGVKVPLEPGPKATEGGGEALPSGSECEVPLMGFPGPGLQSPLHAKPYI", "text": "FUNCTION: May act as an inhibitor of TGF-beta signaling. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein Secreted."}
{"protein": "MDWKDVLRRRLASPNSDPKRKKSEQELKDEEMDLFTKYYSEWKGGRKNTNEFYKTIPRFYYRLPAEDEVLLQKLREESRAVFLQRKSRELLDNEELQNLWFLLDKHQIPPMIGEEAMINYENFLKVGEKAGPKCKQFFTAKVFAKLLHTDSYGRVSIMQFFNYVMRKVWLHQTRIGLSLYDVAGQGYLRESDLENYILELIPTLPQLDGLEKSFYSFYVCTAVRKFFFFLDPLRTGKIKIQDILACSFLDDLLELRDEELSKESQETNWFSAPSALRVYGQYLNLDKDHNGMLSKEELSRYGTATMTNVFLDRVFQECLTYDGEMDYKTYLDFVLALENRKEPAALQYIFKLLDIENKGYLNVFSLNYFFRAIQELMKIHGQDPVSFQDVKDEIFDMVKPKDPLKISLQDLINSNQGDTVTTILIDLNGFWTYENREALVANDNENSADLDDT", "text": "FUNCTION: May regulate MCM3AP phosphorylation through phosphatase recruitment. May act as a negative regulator of ABCB1 expression and function through the dephosphorylation of ABCB1 by TFPI2/PPP2R3C complex. May play a role in the activation-induced cell death of B- cells. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Excluded from the nucleoli. Localization is cell cycle-dependent. Localizes to the cytoplasm during cytokinesis."}
{"protein": "MSTSTAKRPFDNKRAGSPDDGTDSDSGGNNSGSSPASKRRERKPGRKPLETEAKDKRTAQNRAAQRAFRERRERKMKELEDKVSQLESLNKQSELETKFLRNQVTNLLSELKRYNPELPKKRDSILLDYLAKQRKASIDSNPDFSAAANKAANSKDSSTAISSSNFQFEFPWKMDPSKIPSPSSDSTSPSASTSILDNANNKSVSSTNLNHSRSSISNSSSSPSNVNGLSSRKHSNTLNLYQTQSNVTSEFDFDSQFDESVSSFCSKLSMACGTKSNPIPKASPVSTPSSSDLLKPKSNSNVNITNHNNNKINSKDLSSSAPLHDSASASALNNHDSVNAVSNQFSVDKQYNDSSHSQATPNGLDNDSSVSAWQQPSFGQLGFRTDQLFDLDLDSASPITKQKDNNYSTTTNNTNSPAKADGMYWNFNTPLSNMVSRNMQNPEIPFIDTGLAFPDYDDPLLDILKEEQENEQVEGDSDPIQALINEEPSMPLCHDPAANAGASVSETDKLSNQEEIVQDIIPSNDGKLLKCSEVWDRITAHPRYSDLDIDGLCLELRTKAKCSEKGVVVNAEDVQKALISHMQ", "text": "FUNCTION: Transcription activator involved in oxidative stress response and cadmium resistance (PubMed:9439570). Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Activation by alkyl hydroperoxides or cadmium induces nuclear accumulation and as a result YAP1 transcriptional activity (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Oxidized YAP1 is found predominantly in the nucleus, while reduced YAP1 is continuously exported to the cytoplasm by CRM1/exportin 1. SIMILARITY: Belongs to the bZIP family. YAP subfamily."}
{"protein": "MAISLSAPRTTELKPRIVVFGVGGAGGNAVNNMIEAGLEGVEFVVANTDAQQLQFAKTDRRIQLGVQITQGLGAGAHPEVGMSAAEESFPEIGEHLDGAHMVFITAGMGGGTGTGAAPIIAKCARERGILTVGVVTKPFHFEGRHRMRLADSGIQELQRYVDTLIVIPNQNLFRVANERTTFAEAFGMADQVLHSGVRSITDLMVLPGLINLDFADVRTVMTEMGKAMMGTGEGTGEDRALMAAQNAIANPLLDEVSLKGAKAVLVNVTGGMDMTLLEVDEAANAISDQVDPEANIIFGAAFDPSLEGVIRVSVVATGMDGASIAQIEPKPVSRNISAAPLIAETSRPAPQPEPARPTARYEAARPAERPVAFAPEPAPEPEIVMSAPQPEPEAELYYDEPTVAEEPRVSAAPARSVNRIVDPLVDDVAEEPLFPENNYYEERRPQKQGGFFSMFGGGRQRYEQQASAPQAQARSAQSARPQLQPIETPQADDAEDLEIPSFLRRLAN", "text": "FUNCTION: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. SUBCELLULAR LOCATION: Cytoplasm Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. SIMILARITY: Belongs to the FtsZ family."}
{"protein": "MRTIAILAAILLVALQAQAESLQERADEATTQKQSGEDNQDLAISFAGNGLSALRTSGSQARATCYCRIGHCTILESLSGVCEISGRLYRLCCR", "text": "FUNCTION: Host-defense peptide that maintains sterility in the urogenital system (By similarity). Has antimicrobial activity against a wide range of bacteria, including Gram-negative E.coli, P.aeruginosa and S.typhimurium, and Gram-positive E.aerogenes, S.aureus, B.cereus, E.faecium and L.monocytogenes (By similarity). Confers resistance to intestinal infection by S.typhimurium (By similarity). Exhibits antimicrobial activity against enteric commensal bacteria such as B.adolescentis, L.acidophilus, B.breve, L.fermentum, B.longum and S.thermophilus (By similarity). Binds to bacterial membranes and causes membrane disintegration (By similarity). Induces the secretion of the chemokine IL-8 by intestinal epithelial cells (By similarity). Binds to B.antracis lef/lethal factor, a major virulence factor from B.anthracis, and neutralizes its enzymatic activity (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasmic vesicle, secretory vesicle Note=Stored as propeptide HD5(20-94) in secretory granules of small intestinal Paneth cells and found in the ileum lumen as processed mature peptides, predominantly in the HD5(63-94) form. Peptides HD5(20- 94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94) being the predominant intracellular form. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the most abundant form (By similarity). Secreted into the female genital tract lumen (By similarity). SIMILARITY: Belongs to the alpha-defensin family."}
{"protein": "MNLLIMGLPGAGKGTQAAKIVEKFNVAHISTGDMFRAAMANQTEMGILAKSYIDKGDLVPDEVTNGIVKERLVQDDIKEKGFLLDGYPRTIEQAHALDENLADLGIELQGVINIEIDPSKLVERLSGRIIHKETGETFHKVFNPPVGDYKEEDFYQREDDKPESVKRRLEVNIAQGQPIIDHYRAKGLVHDIEGDQDIDLVFQAIDTVLSKLQ", "text": "FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylate kinase family."}
{"protein": "MKGSRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQKNLKVPSGQNADVQKTDN", "text": "FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:22311970, PubMed:21900231, PubMed:27484799). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929). Autoacetylates in vivo (PubMed:19744929). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929). Component of N-alpha- acetyltransferase complexes containing NAA10 and NAA15, which has N- alpha-acetyltransferase activity (PubMed:16507339, PubMed:29754825, PubMed:27484799, PubMed:32042062). Does not influence the acetyltransferase activity of NAA10 (PubMed:16507339, PubMed:27484799). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (PubMed:32042062). The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821). FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (By similarity). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (By similarity). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (By similarity). Autoacetylates in vivo (By similarity). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (By similarity). Component of N-alpha-acetyltransferase complexes containing NAA10 and NAA15, which has N-alpha-acetyltransferase activity (By similarity). Does not influence the acetyltransferase activity of NAA10 (By similarity). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (By similarity). The multiprotein complexes probably constitute the major contributor for N- terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (By similarity). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes to the cytoplasm in interphase cells (PubMed:17502424). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes to the cytoplasm in interphase cells. SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily."}
{"protein": "MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGATLLSLGLIFLLYTMFVWWRDVLRESTLEGHHTKAVQLGPRYGSILFIVSEVMFLFAFFWASSHSSLAPTVEIGGIWPPKGIGVLDPWEIPLLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVSLALVSTGFQGMEYYQAPSTISDSIYGSTFFLATGFHGFHVIIGTLFLIVCGIRQYLGLMTKKHHVGFEAAAWYWHFVDVVRLFPFVSIYWWGGI", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family."}
{"protein": "MVAEHPTPPQPHQPPPMDSTAGSGIAAPAAAAVCDLRMEPKIPEPFVWPNGDARPASAAELDMPVVDVGVLRDGDAEGLRRAAAQVAAACATHGFFQVSEHGVDAALARAALDGASDFFRLPLAEKRRARRVPGTVSGYTSAHADRFASKLPWKETLSFGFHDRAAAPVVADYFSSTLGPDFAPMGRVYQKYCEEMKELSLTIMELLELSLGVERGYYREFFADSSSIMRCNYYPPCPEPERTLGTGPHCDPTALTILLQDDVGGLEVLVDGEWRPVSPVPGAMVINIGDTFMALSNGRYKSCLHRAVVNQRRERRSLAFFLCPREDRVVRPPPSAATPQHYPDFTWADLMRFTQRHYRADTRTLDAFTRWLAPPAADAAATAQVEAAS", "text": "FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA53 to GA20 via a three-step oxidation at C-20 of the GA skeleton (PubMed:12077303, PubMed:11961544, PubMed:30002253). Catalyzes the conversion of GA12 to GA9 via a three- step oxidation at C-20 of the GA skeleton (PubMed:30002253). Contributes to the promotion of internode elongation in response to submergence via ethylene and gibberellin signalings (PubMed:30002253). FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA53 to GA20 via a three-step oxidation at C-20 of the GA skeleton. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family. GA20OX subfamily."}
{"protein": "MIGLVGKKVGMTRIFTEDGVSIPVTVIEIEANRVTQVKSLENDGYRAVQVTTGAKKANRVTKPEAGHFAKAGVEAGRGLWEFRLPEGQEFTAGQEISVEIFADVKKVDVTGTSKGKGFAGTVKRWNFRTQDATHGNSLSHRVPGSIGQNQTPGKVFKGKKMAGHMGDERVTVQSLDVVRVDAERNLLLVKGAVPGATGGNLIVKPAVKA", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SIMILARITY: Belongs to the universal ribosomal protein uL3 family."}
{"protein": "MLKFIQNNREITALLAVLLLFVLPGFLDRQYLSVQTLTMVYSSAQILILLAMGATLVMLTRNIDVSVGSITGMCAVLLGMLLNAGYSLPVACVATLLLGLLAGFFNGVLVAWLKIPAIVATLGTLGLYRGIMLLWTGGKWIEGLPAELKQLSAPLLLGVSAIGWLTIILVAFMAWLLAKTAFGRSFYATGDNLQGARQLGVRTEAIRIVAFSLNGCMAALAGIVFASQIGFIPNQTGTGLEMKAIAACVLGGISLLGGSGAIIGAVLGAWFLTQIDSVLVLLRIPAWWNDFIAGLVLLAVLVFDGRLRCALELNLRRQKYARFMTPPPSVKPASSGKKREAA", "text": "FUNCTION: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. AraH/RbsC subfamily."}
{"protein": "MKYQQLENLESGWKWKYLVKKHREGELITRYIEASAAQAAVDDLLTIENEPVLVHAWIEQHMNPALMNRMKQTIRARRKRHFNAEHQHTRKKSIDLEFVVWQRLAGLAQRRGKTLSETIVQLIEDAEHKEKYASKMSSLKHDLQELLGKE", "text": "FUNCTION: Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MatP family."}
{"protein": "MPRMEQRFDYIKISIASPERVMAWGQRTLPNGQVVGEVTKPETINYRTLKPEMDGLFCERIFGPSKDWECYCGKYKRVRHRGIVCERCGVEVTESKVRRHRMGYIKLAAPVTHVWYLKGIPSYISTLLDMPLRDVEQVVYFNAYVVLNPGNAENLYYKQLLTEDQYIEVEDQIFAEDSSLELPEGWAKMGAEAIHELLAAIEMESEAERLRADLGESKGQKRTKLIKRLRVLDNFIATGSRPEWMVLTAIPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLARLQEILAPEIIVRNEKRMLQEAVDALIDNGRRGRTVVGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIVVGPKLKLHQCGLPKEMAIELFQPFVIHKLIQRGLVNNIKAAKKMIQRNDARIWSVLDEVITGHPVLLNRAPTLHRLGIQAFEPILVSGRAIQLHPLVCTAFNADFDGDQMAVHVPLSLESQAEARLLMLASNNVLSPATGRPIITPTQDMVLGCYYLTVDNPDATKGSGKYFGSSEDAVIAYNQGMIDLHAKIWLRFEGEVETDNPEDLRVRRDEQGNALSQFVRTTVGRIIFNQVIQETLVAS", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily."}
{"protein": "MSGPASSTGFHIHAEGLHGRNVQPSKPTSDGGVAPTALGEKARVEEDERTDSEKKTFGRTPDGTIFTVPPTRDMVSQLLSPSEPKNLSDIFVLAIISCHIFLLRFLPSSSRVAAFAIIFLFWRAAYNIGIGWLLHMQSNGRTLVCWAKKSNIFVNPSTGQNPHPVLYNLLKWELETKIPEQYSFEDAPTEYNTWLVFRRVVDLILMCDFTSYCLFAIACGGRPAGEGFIMLALRWITGMSLVLFNLWVKLDAHRVVKDFAWYWGDFFYLIDQDLTFDGVFEMAPHPMYSVGYAGYYGISLMAASYKLLFISILAHAAQFAFLVLVENPHIEKTYNAPPPRKRVAVDTDNVKPQDDDVSQDSSVINDNVYSGQAVATLEPSSMHNLLGPHNIDLYRITDSSVLLIQILFSALAILTPSTPVYQFFFVLNAALWRVWYSVGIGYILNRQSHCKMWTRHFVKYGESNQEAWQQWKGTYHLSMTMTYASFIAATWKMYSFPQDWGYGLVLLRHILGASLIALQIWTSASIYESLGEFGWFFGDFFFDQSPKLTYSGIYRYLNNPERVLGLAGVWGAVLITSTKSVIFLALLSHTLTIAFIQLVERPHMQKLYGQSLRRDAGLVRSLKRSLPPSLKQFHGSVDKILDDSIEFIEEFIEAARPKLAAGVKTFVKDTSALFQKYPARITISRLEPDLAGYDQKDYSISLEGTQSSEPAQFERASGKEGEKARSMPDRRGDKKNLMFEYGAPIKVKWTAPLNHSKKDWIGLYMVTDNTSREITRISSQGRWIGTNKASFDSLTCEQGLISSDIVINKFREDGEPKDVASGEMVFSGDKLWWTQGVFEFRYHHNGKHSVMAVSRPFEIRIGRFDDDAIYGDRYGLVRAAIESALLPVVQNCFDRDPEIAPQTVEEQYGSLVDRNGKYSRRVVFAVHQMFGIEFAPEVVRADGNVRNLAWRICNAKKVLAPYSMSRTNGATTPTAEHEG", "text": "FUNCTION: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family."}
{"protein": "MAFKKLLAVLTAALSLRAAQGAAVEKRATCSNGKVVPAASCCTWFNVLSDIQENLFNGGQCGAEAHESIRLVFHDAIAISPAMEPQASSVRGADGSIMIFDEIETNFHPNIGLDEIVRLQKPFVQKHGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPFHSVDQIIDRVFDAGEFDELELVWMLSAHSVAAANDIDPNIQGLPFDSTPGIFDSQFFVETQLAGTGFTGGSNNQGEVSSPLPGEMRLQSDFLIARDARTACEWQSFVNNQSKLVSDFQFIFLALTQLGQDPDAMTDCSAVIPISKPAPNNTPGFSFFPPGMTMDDVEQACAETPFPTLSTLPGPATSVARIPPPPGA", "text": "FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin. SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily."}
{"protein": "MDPRSEVLLRQPELFQGSLLLVGLPADDLLGKLPNARGWCWHAGDQAALDARFEGRVDFGVEAPEATFEAAVLFLPKARDLTDYLLNALASRLAGRELFLVGEKRGGIEAAAKQLSPFGRARKLDSARHCQLWQVTVENAPQAVTLESLARPYQIELQDGPLTVISLPGVFSHGRLDRGSALLLENIDKLPSGNLLDFGCGAGVLGAAVKRRYPHNDVVMLDVDAFATASSRLTLAANGLEAQVVTGDGIDAAPMGLNTILSNPPFHVGVHTDYMATENLLKKARQHLKSGGELRLVANNFLRYQPLIEEHVGYCHVKAQGNGFKIYSAKRS", "text": "FUNCTION: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family."}
{"protein": "MTATSSPTTRFTDRVVLITGGGSGLGRATAVRLAAEGAKLSLVDVSSEGLEASKAAVLETAPDAEVLTTVADVSDEAQVEAYVTATTERFGRIDGFFNNAGIEGKQNPTESFTAAEFDKVVSINLRGVFLGLEKVLKIMREQGSGMVVNTASVGGIRGIGNQSGYAAAKHGVVGLTRNSAVEYGRYGIRINAIAPGAIWTPMVENSMKQLDPENPRKAAEEFIQVNPSKRYGEAPEIAAVVAFLLSDDASYVNATVVPIDGGQSAAY", "text": "FUNCTION: Catalyzes the regio- and stereoselective reversible NAD- dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MKTVARALSGSARAMARKPMRFTDLRTVQLRPPIVPTHRNFEVSPDHPLWAFFPDGNNSQTCYREASDLDIQSRAWTTAELRRKSFEDLHQLWYLVLKERNVLAREVRLADAINERNTHVHDQVDEKLLLTQKRIKQVLLERQTAFERVQTFTQQQQEYLEEFRQRYLDADASQIASYNEKLIRLQYAFFGIQPQLEDYNWETDINERFVDGLNYVSHIKLARYFAQNPDVEEEIGYPLKGVVEELPFLLRDPSEAVEEVRALRQSGAQVKLDKIDVLPFLRSALQAALEQEGRM", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MTMDRTSPIFTVRWLAVHGLAVPTVFFLGSISAMQFIQR", "text": "FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbE/PsbF family."}
{"protein": "MVQLDVEKTIEELTLGEKVALTAGIDFWHTAAVPRLNIPSLRLSDGPNGVRGTRFFNGVPAACFPCATALGATWDTKLLHEVGRLMGEESIAKGTHVVLGPTINIQRSPLGGRGFESFAEDGVLSGILAGHYCKGLQETGVAATLKHFVCNDQEHERLAVDSIVTMRAMREIYLLPFQLAMRICKTACVMTAYNKINGTHVSENKQIITDILRKEWGWDGLVMSDWFGTYSTSDAINAGLDLEMPGPTRWRGTALAHAVSSNKAFEFVVDERVRNILNLHNFVEPLGIPENAPEKALNRPEDQALLRRAAAESVVLMKNQDNILPLKKEKPILVIGPNAKTAAYCGGGSASLDAYYTVTPFEGVSAQSQGEVKFSQGVYSYKELPLLGPLLKTDDGKKGFKFRVYNEPPSEPNRQLIDELHLESSSGFLMDYKHPKIKTFTFYVDMEGYFTPEEDGIYDFGVTVVGTGKLFVDDELVVDNSKNQRQGTAMFGNATVEEKGSKELKAGQTYKVVLQFGTAPTSDLDMRGVVIFGPGGFRFGAARRVSQEELISKAAELASQASQVVIFAGLTSEWETEGHDRDHMDLPPGSDEMISRVLDANPNAVVVIQSGTPVTMPWAHKAKALLQAWFGGNECGNGIADVLYGAVNPAAKLPLSFPVRLQDNPSYLNFRSERGRVLYGEDVYVGYRYYEKVDLAPLFPFGHGLSYTTFSRSDLSLATTPEKPQLEDGEPITATVSVTNTGSVAGAEIVQLWVAPPPTGVNRPVRELKGFAKVFLQPGETKKVEIVVEKKLATSWWDEQREKWASEKGTYEVLVTGTGDEVLKTSFEVGKTRYWLGL", "text": "FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 3 family."}
{"protein": "MDGPAIITQVTNPKEDEGRLPGAGEKASQCNVSLKKQRSRSILSSFFCCFRDYNVEAPPPSSPSVLPPLVEENGGLQKGDQRQVIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSREDDVYSMLHRLCNR", "text": "FUNCTION: Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSEPIKLHDLRPAKGANKPKTRVGRGEASKGKTAGRGTKGTKARKQVSAAFEGGQMPLHMRLPKLKGFKNPAKVYYQVVNVSDLEKAFPQGGEIAVADIVAKGLVRPKQPVKVLGNGEISVKLNVTATKFSKSAVEKIEAAGGSVTEA", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MASLKDLEGKWRLVESHGFEDYMKELGVGLALRKMGAMAKPDCIITLDGNNLTVKTESTVKTTVFSCTLGEKFDETTADGRKTETVCTFTDGALVQHQKWEGKESTITRKLKDGKMVVECVMNNAICTRVYEKVQ", "text": "FUNCTION: Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (By similarity). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF- kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Synapse Postsynaptic density Secreted Note=Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into nucleus (By similarity). Secreted by astrocytes, but not by neurons (By similarity). SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MSEHSRNSDQEELLDEEINEDEILANLSAEELKELQSEMEVMAPDPSLPVGMIQKDQTDKPPTGNFNHKSLVDYMYWEKASRRMLEEERVPVTFVKSEEKTQEEHEEIEKRNKNMAQYLKEKLNNEIVANKRESKGSSNIQETDEEDEEEEDDDDDDEGEDDGEESEETNREEEGKAKEQIRNCENNCQQVTDKAFKEQRDRPEAQEQSEKKISKLDPKKLALDTSFLKVSTRPSGNQTDLDGSLRRVRKNDPDMKELNLNNIENIPKEMLLDFVNAMKKNKHIKTFSLANVGADENVAFALANMLRENRSITTLNIESNFITGKGIVAIMRCLQFNETLTELRFHNQRHMLGHHAEMEIARLLKANNTLLKMGYHFELPGPRMVVTNLLTRNQDKQRQKRQEEQKQQQLKEQKKLIAMLENGLGLPPGMWELLGGPKPDSRMQEFFQPPPPRPPNPQNVPFSQRSEMMKKPSQAPKYRTDPDSFRVVKLKRIQRKSRMPEAREPPEKTNLKDVIKTLKPVPRNRPPPLVEITPRDQLLNDIRHSSVAYLKPVQLPKELA", "text": "FUNCTION: Essential for the organization of sarcomeric actin thin filaments in skeletal muscle (PubMed:25250574). Increases the rate of actin polymerization (PubMed:25250574). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, myofibril, sarcomere, M line Cytoplasm, myofibril, sarcomere, A band Cytoplasm, cytoskeleton Note=Highly expressed in nonstriated areas of developing myotubes, where it shows a granular cytoplasmic pattern. In sarcomeres, highly expressed in the M band region and, at lower levels, along actin thin filaments. Not detected in Z-disks. In sarcomeres, may be located near, but not at, actin thin filament pointed end. SIMILARITY: Belongs to the tropomodulin family."}
{"protein": "MERIKELRDLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRIMEMIPKRNEQGQTLWSNTNDAGSDRVMVSPLAVTWWNRNGPTTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKIAPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVEREEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEPIDNVMGMIGILPDMTPSTEMSLRGIRVSKMGVDEYSSTERVVVSIDRFLRVRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQDPTMLYNKMEFEPFQSLIPKAARGQYSGFVRTLFQQMRDVLGTFDTVQIIKLLPFAAAPPEQSRMQFSSLTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGALTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN", "text": "FUNCTION: Plays an essential role in transcription initiation and cap- stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7- methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the influenza viruses PB2 family."}
{"protein": "MSVPAELKYTESHEWVRLEADGSVTVGITQHAQELLGDMVFVQLPDVGRALAQREDCAVVESVKAASDIYAPLGGEVIAVNSEVETSPEKINEDCYAAWLFKLKPANAGEVDGLLDAGGYQKLLDSEAH", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. SIMILARITY: Belongs to the GcvH family."}
{"protein": "MKTVTVRDLVVGEGAPKIIVSLMGKTITDVKSEALAYREADFDILEWRVDHFANVTTAESVLEAAGAIQEIITDKPLLFTFRSAKEGGEQALTTGQYIALNRAAVDSGLVDMIDLELFTGDDEVKATVGYAHQHNVAVIMSNHDFHKTPAAEEIVQRLRKMQELGADIPKIAVMPQTKADVLTLLTATVEMQERYADRPIITMSMSKTGVISRLAGEVFGSAATFGAVKKASAPGQISVADLRTVLTILHQA", "text": "FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. SIMILARITY: Belongs to the type-I 3-dehydroquinase family."}
{"protein": "MSHPALTQLRALRYFKEIPALDPQLLDWLLLEDSMTKRFEQQGKTVSVTMIREGFVEQNEIPEELPLLPKESRYWLREILLCADGEPWLAGRTVVPVSTLSGPELALQKLGKTPLGRYLFTSSTLTRDFIEIGRDAGLWGRRSRLRLSGKPLLLTELFLPASPLY", "text": "FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UbiC family."}
{"protein": "MRLSRFFLPILKENPKEAEIVSHRLMLRAGMLRQEAAGIYAWLPLGHRVLKKIEQIVREEQNRAGAIELLMPTLQLADLWRESGRYDAYGPEMLRIADRHKRELLYGPTNEEMITEIFRAYIKSYKSLPLNLYHIQWKFRDEQRPRFGVMRGREFLMKDAYSFDVDEAGARKSYNKMFVAYLRTFARMGLKAIPMRAETGPIGGDLSHEFIVLAETGESGVYIDRDVLNLPVPDENVDYDGDLTPIIKQWTSVYAATEDVHEPARYESEVPEANRLNTRGIEVGQIFYFGTKYSDSMKANVTGPDGTDAPIHGGSYGVGVSRLLGAIIEACHDDNGIIWPEAVAPFRVTILNLKQGDAATDAACDQLYRELSAKGVDVLYDDTDQRAGAKFATADLIGIPWQIHVGPRGLAEGKVELKRRSDGSRENLALADVVARLT", "text": "FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily."}
{"protein": "MIFLKRFIVWTFLFIVTLIQLLLYLPDFSCISKNGGLPICTSQFNFAIVDSSHITHDFITSIRELLRLLSYLTIDMGWSSGLPAPDAYNDENLVDTFHLNNIYKVNYFGYCKKNGKQKEYCTSNHSSGMDILALLVRDVGIQLGKLSSAYENNTEILGESLVFTYELSLSSLHTFIKGDRQRGNILPKIVTNQGNEQTDLEYSSSKAYDKGVSLAYGLMLFNEIMYFIHIFEITISVHCFLNVILFGFALVWGKKQILLPTLLKITSSLLLVFASISFSGNLLYLLLLKMLEPDPTGITTTGWEMLEVKAGSGFIITCIRVGIQWIFLPVAFITSNHYIQPKKQQTKIDELKSDDESTVKQV", "text": "FUNCTION: Involved in spore and ascus formation. Required for the efficient assembly of the precursors of the prospore membrane to a continuous prospore membrane (By similarity). SUBCELLULAR LOCATION: Prospore membrane; Multi-pass membrane protein Note=Localizes to prospore membrane. SIMILARITY: Belongs to the SMA2 family."}
{"protein": "MVHFHPFGNVNFYEMDWSLKGDLWAHDPVIAKEGSRWYVFHTGSGIQIKTSEDGVHWENMGRVFPSLPDWCKQYVPEKDEDHLWAPDICFYNGIYYLYYSVSTFGKNTSVIGLATNRTLDPRDPDYEWKDMGPVIHSTASDNYNAIDPNVVFDQEGQPWLSFGSFWSGIQLIQLDTETMKPAAQAELLTIASRGEEPNAIEAPFIVCRNGYYYLFVSFDFCCRGIESTYKIAVGRSKDITGPYVDKNGVSMMQGGGTILDAGNDRWIGPGHCAVYFSGVSAILVNHAYDALKNGEPTLQIRPLYWDDEGWPYL", "text": "FUNCTION: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of endo alpha-(1->5)-L-arabinofuranosyl residues in debranched arabinan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 43 family."}
{"protein": "MEINKFICSQGPKKNSCEDFWRMVLEQESCIIVSLTETDDEDQVCYEYWVKEEDYELAFGRYVVKTLEIIEESSFTRTRLRLTDVSSDTSREIHHFWYPHWSDYGNPTNPAEILNLISKVNQKRKEMKKTADSQPGPIVVHCSAGIGRTGTFCTIDNALSQLRKEQTVCLPQTVLKIQKSKI", "text": "SIMILARITY: Belongs to the protein-tyrosine phosphatase family."}
{"protein": "MPKELKELKDYLSVLKRPDARSVVVYKKKSKGGLLSTKFKVRCSRYLYTFSVPNQVKAAKVEATIPSHLEKKVITNKKN", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL38 family."}
{"protein": "MELILGSQSSARANLLKEHGIKFEQKALYFDEESLKTTDPREFVYLACKGKLEKAKKLLTNHCVIVVADSVVSVDNRMQRKAKNKQEALEFLKRQNGNEIEVLTCSALISPVLEWLDLSVFRARLKAFDSSEIEKYLESGLWQESAGCVRLEDFHRPYIKSSSKNLSVGLGLNVEGLLGALKLGAKLSLL", "text": "FUNCTION: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Maf family."}
{"protein": "MELLRTITYQPAAGTKMCEQALGKACGGDSKKKRPQQPSEDGQSQAQVTPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYNDTHNKVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPPTTFAKSGTSAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICNQNEEYLLTYINEDRISTTFRLTTLLMSGCSLELKHRMEYALNMLLQRCN", "text": "FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cell projection, dendrite Note=Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
{"protein": "MSITASEARQNLFPLIEQVNEDHAPVHITSRKGNAVLMSEEDFTAWTETVHLLRSPRNARRLLDSIAEAEAGDATEHDLIDPDAERA", "text": "FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. A probable antitoxin for the putative mRNA interferase YeoB (By similarity). SIMILARITY: Belongs to the phD/YefM antitoxin family."}
{"protein": "MIQAEKNPXL", "text": "FUNCTION: Converts (3-methyl-)-quinoline to (3-methyl-)2-oxo-1,2- dihydroquinoline."}
{"protein": "MYPAKYQVVPSGINYSDTPVGTFEQYQPQKAGESSEHFFSKVVVALIVILFAVGIVYLAYTLFLKDLILLLKAKKQKTTTEIGFGNTPLRRPGEGNPNGGPV", "text": "FUNCTION: Involved in the viral transport within, and between cells. SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the mastrevirus movement protein family."}
{"protein": "MNNFSIISGYKPAGDQPKAIDEIITGLNSKKRSQMLLGITGSGKTFTMANIIERTNRPTLIMAHNKTLAAQIYLEMKSIFPKNAVEYFVSYYDYYQPESYIVRTDTFIEKDSSINEQIDLMRHSATRSLLERRDVIVISSVSCIYGLGAPDLYYQMTVHLEPGQNYPRDKLLNDLINLQYKRNDIGFERGCFRVKGDNMDIFPSHYSDKAWRLSFFGDELEYIHEFDPLTGEKLTQLDKAMIFGNSHFVMPRERINHAISSIEVELQKRLEFLKSQDKLIEAKRLNQRTLYDLEMLTETGSCKGIENYSRFFTGRNAGQPPPTLFEYLPEDALLFIDESHVSVPQIRAMYNSDRARKEVLVEHGFRLPSALDNRPLKFEEWEKFRPQTVFVSATPGQFELEETGGTVVELIIRPTGLLDPECIIKPATNQVEDLISEIQTTINTGLRILVTTLTKKMAEDLTSYLQDLQYKTYYLHSNIHTLERIEILRNLRQGTIDILVGINLLREGIDIPECGLVAILDADKEGFLRSETSLIQTIGRAARNSRGKVILYADKMTKSIDKAVSETLRRRQIQQEYNKKHGIIPKTINRAIHALESLEEIHDNKLDKKQANALLNNPAKLKAHMDKLKKEMFKAASNLEFEQAAKLRNQLKALEEAALKLS", "text": "FUNCTION: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UvrB family."}
{"protein": "MHIKMKDIFKAFGQNQVLSGVSFELQEGEVHALMGENGAGKSTLMNLLTGLHKLDSGTIEIDGKETYFSDPKEAEQNGIAFIHQELNIWPEMTVLENLFIGRELSSKLGFLNNKKMKALAKEQLERLGVSISLEKEAGDCSVGQQQMIEIAKALMTDAKVIIMDEPTAALTEREIEKLFGVIRALKKNGVSIVYISHRMEEIFTICDRITVMRDGKTVDTKRIPDTDFHEVVKKMVGRELTERYPERQPNPGRVVLEVKQASKKGVFQNISFSVRSGEIVGISGLMGAGRTELMRAVFGLDPLDSGDIFIEGKKAALKKPSDAVQKGIGFITENRKDEGLVLDTSIRENIALPNLASFSPKGWIDKKSEQEFVDLLIKRLTIKTESPETHARNLSGGNQQKVVIAKWIGIGPKVLILDEPTRGVDVGAKREIYQLMNELTDRGVAIVMVSSELPEILGMSDRVLVIHEGTLSGELSRNDATQERIMTLATGGR", "text": "FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Ribose importer (TC 3.A.1.2.1) family."}
{"protein": "MKLIIFTGLALLLIVSLIDVEAQNEGACLPRGSVCTTNHASCCSKLSCDCYRRFEKGVEKGQKCWRIPTGLRYSKEKE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 07 (U7-Lctx) subfamily."}
{"protein": "MRRSLAPSQRGPLRPESRHSFTPPLLKKNKRSCQQELEREQELDRRRLGALRDASNTSELPLPIRFTANSEYELAIAKVLARKFKVPMDNYVPDYGGKRVLGVRRCISRRPLHDPMACNALVLFHPPAYTEHERMGMDPTKVLVHVVVDPLLSNILRPHQREGVRFMYECVEGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCIIRRTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDQVRRSLADCNEKASLTALADITTLKKICSHPDLIYEKLTAREKGFENSQNVLPSNYKPKDLNPELSGKFMLLDFMLAAIRAEGNDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLVASGSIEEKILQRQTHKKSLSSTIIDNNESAEKHFTRDDLKDLFTFDANILSDTHDKLKCKRCVQNIQMKPPPEDTDCTSHLSQWYHCSNNRGLPDNILAQAWMDCKCVSFVFHHRSQAQEIVPSAEEEATDQPEEKPESRKRSSTPASDDSADEDFRGF", "text": "FUNCTION: Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNF2/RAD54 helicase family."}
{"protein": "MIGLSTYRNLPTLLTTTTVISTALRSKQLLRFTTTTSTKSRSSTSTAATTVGNSNPKSPIDEDNLEKPGTIPTKHKPFNIQTEVYNKAGIEANDDDKFLTKPTYRHEDFTEAGVYRVHVTHRPPRTIGDKISCYGTLFFRKCFDLVTGYAVPDPDKPDQYKGTRWEMTEEKWMTRCIFLESIAGVPGSVAGFVRHLHSLRMLTRDKAWIETLHDEAYNERMHLLTFIKIGKPSWFTRSIIYIGQGVFTNIFFLVYLMNPRYCHRFVGYLEEEAVRTYTHLIDELDDPNKLPDFQKLPIPNIAVQYWPELTPESSFKDLILRIRADEAKHREINHTFANLEQWQDRNPFALKIKDSDKPQPNYNLDVTRPQGWERKDLYL", "text": "FUNCTION: Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side Note=Possibly in the inner surface of the inner mitochondrial membrane. SIMILARITY: Belongs to the alternative oxidase family."}
{"protein": "MSEKFEVTNLNMKSGMSLKIKGKIHNDVNSFTINLGQGKETLNLHFNPRFNESTIVCNTLDGSSWGQEQRENHSCFSPGSEVKLTLTFQDKDFKVTLPDGHSLTFPNRLGHNHLRYLSMDGLQISSFKLE", "text": "FUNCTION: This protein binds beta-galactoside. Its physiological function is not yet known."}
{"protein": "MTDPWRYATHGVMVAVRVTPRGGRDAVDGIEMLANGKSVVKVRVRVAAEGGEANRAVTELFAGLLRVPKSKVKVASGVTSRIKQIAIEGDPKQLGEALKAATSIES", "text": "SIMILARITY: Belongs to the UPF0235 family."}
{"protein": "MEAARALRLLLVVCGCLALPPLAEPVCPERCDCQHPQHLLCTNRGLRVVPKTSSLPSPHDVLTYSLGGNFITNITAFDFHRLGQLRRLDLQYNQIRSLHPKTFEKLSRLEELYLGNNLLQALAPGTLAPLRKLRILYANGNEISRLSRGSFEGLESLVKLRLDGNALGALPDAVFAPLGNLLYLHLESNRIRFLGKNAFAQLGKLRFLNLSANELQPSLRHAATFAPLRSLSSLILSANNLQHLGPRIFQHLPRLGLLSLRGNQLTHLAPEAFWGLEALRELRLEGNRLSQLPTALLEPLHSLEALDLSGNELSALHPATFGHLGRLRELSLRNNALSALSGDIFAASPALYRLDLDGNGWTCDCRLRGLKRWMGDWHSQGRLLTVFVQCRHPPALRGKYLDYLDDQQLQNGSCADPSPSASLTADRRRQPLPTAAGEEMTPPAGLAEELPPQPQLQQQGRFLAGVAWDGAARELVGNRSALRLSRRGPGLQQPSPSVAAAAGPAPQSLDLHKKPQRGRPTRADPALAEPTPTASPGSAPSPAGDPWQRATKHRLGTEHQERAAQSDGGAGLPPLVSDPCDFNKFILCNLTVEAVGADSASVRWAVREHRSPRPLGGARFRLLFDRFGQQPKFHRFVYLPESSDSATLRELRGDTPYLVCVEGVLGGRVCPVAPRDHCAGLVTLPEAGSRGGVDYQLLTLALLTVNALLVLLALAAWASRWLRRKLRARRKGGAPVHVRHMYSTRRPLRSMGTGVSADFSGFQSHRPRTTVCALSEADLIEFPCDRFMDSAGGGAGGSLRREDRLLQRFAD", "text": "FUNCTION: Component of the TLR4 signaling complex. Mediates the innate immune response to bacterial lipopolysaccharide (LPS) leading to cytokine secretion. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MENIFDAKAFLSRVTSQPGVYRMYDASGTVIYVGKAKDLKKRLSSYFRAQVNSRKTEALVKCIANIDVTVTHTETEALLLEHSYIQRYQPRYNVLLRDDKSYPYIYLSADKHPRLASYRGAKHAKGEYFGPFPNSLAVRETLALMQKLFPIRQCEDSVYRNRSRPCLQYQIGRCLAPCVKGYVSDEEYAQQVNYVRLFLSGDDSQVIEGLIKRMEEASQALRFEEAARIRDQIHAVRQVTEKQFVANIGDDLDVISVAFNGAIACVYVLFFRQGKVLGSRSYFPKVPANTSLDEVVQTFIGQFYLQGSAIRTLPTEILLDFNLEDKTILAESISSIAGRKIHIQTKPRGDRARYLKLARTNAATALATKQVEQSTISQRYNSLMSLLEMKEIKRMECFDISHTMGEQTVASCVVFDMNGPLKSEYRRYNISGITPGDDYAAMNQVLTRRYGKSLEESKIPDIIFIDGGKGQLAQAIDVFQSLDVDWDKSHPKLIGVAKGSDRKAGLETLFFKPEGEGVALPSDSPALHLIQHIRDESHRHAITGHRQRRAKVKNTSSLESIEGVGPKRRQMLLKYMGGLQALRDASVEEIAKVPTISTALAEKIFNALKH", "text": "FUNCTION: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UvrC family."}
{"protein": "MQTIYTRITDIKGNLITVEAEGASLGELVQIERADGRSSYASVLRFDAKKVTLQVFGGTSGLSTGDKVVFLGRPMEVVYGDSLLGRRFNGTGKPIDNEEICFGEPIPITTPSFNPVCRIVPREMVRTNIPMIDMFNCLVKSQKIPIFSSSGENHNALLMRIAAQTDADIVIIGGMGLTFVDYSFFVEESQRLGFADKCVMFIHKAVDAPVECVLIPDMALACAERFALEQKKNVLVLLTDMTAFADALKEIAITMDQIPANRGYPGSLYSDLAVRYEKAVDIAQGGSITLISVTTMPGDDITHPVPDNTGFITEGQFYLKDNRIDPFGSLSRLKQLVIGKRTREDHGDLANALIRLYADSRKSAERMSMGFKLSNWDKKLLAFAELFETRLMSLEVNIPLEEALDIGWKILAQSFHSEEVGIKEQLIQKYWPKACLHK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGAKWNKVHELKEHNGQVTGIDWAPESNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNENKFAVGSGSRVISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRIFSAYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHGVCFSASGSRVAWVSHDSTVCLVDADKKMAVATLASETLPLLAVTFITENSLVAAGHDCFPVLFTYDNAAVTLSFGGRLDVPKQSSQRGMTARERFQNLDKKASSEGGAATGAGLDSLHKNSVSQISVLSGGKAKCSQFCTTGMDGGMSIWDVKSLESALKDLKIK", "text": "FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus. SIMILARITY: Belongs to the WD repeat ARPC1 family."}
{"protein": "MNNHIEALSYYLGAFVDELARLNVCDVVISPGSRSTPLALLMEQHEQIKTYLHVDERSAAFFALGMAKAKKQPVAILCTSGTAAANYYPAVCEAYHARVPLLVLTADRPHELRDVGAPQAMNQFNLYGSFVKQFMEMALPEAREPMYQYVRMAAGRAVASASFAPMGPVHMNFPLREPLIPDFSLDGLWEQGCGEYTNRVQQGSMTLTSEYIRSLIKRLSRLEKGLIVCGDDSHLELVEVIAEFAEKTGYPVLADPLSNLRTGSHNQTMIIDCYDTFLRNELLKDTWKPDIIIRFGGMPVSKALTQYIKKQESAVHIIVDESGKWRDPALMTTEVVSASDVAFCKAMTEHMQKREQNDWFKKWKHINDKTKETLREVEAYDTAFEGKVITDIVRILPEGATLFVSNSMPIRDADTFLFTNEKKIHVMANRGVNGIDGIISTALGASTVCEPLVLVIGDLSFYHDLNGLLAAKLHDLNITIVVVNNDGGGIFSFLPQYESKEHFESLFGTPLGLDYEHVVKMYGGSFVRVSGWEAFREEVQKGIIERGLHVVEICTNREENVQLHRKLWAKSVIEIKDMLQGDTE", "text": "FUNCTION: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2- succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily."}
{"protein": "MGSLFRSETMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEINRADIPLPEGEASPPAPPLKQVLEMQEQLQKLEVELREVTKNKEKLRKNLLELIEYTHMLRVTKTFVKRNVEFEPTYEEFPSLESDSLLDYSCMQRLGAKLGFVSGLINQGKVEAFEKMLWRVCKGYTIVSYAELDESLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHVYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVYSRVIQVKKMKAIYHMLNMCSFDVTNKCLIAEVWCPEADLQDLRRALEEGSRESGATIPSFMNIIPTKETPPTRIRTNKFTEGFQNIVDAYGVGSYREVNPALFTIITFPFLFAVMFGDFGHGFVMFLFALLLVLNENHPRLNQSQEIMRMFFNGRYILLLMGLFSVYTGLIYNDCFSKSVNLFGSGWNVSAMYSSSHPPAEHKKMVLWNDSVVRHNSILQLDPSIPGVFRGPYPLGIDPIWNLATNRLTFLNSFKMKMSVILGIIHMTFGVILGIFNHLHFRKKFNIYLVSIPELLFMLCIFGYLIFMIFYKWLVFSAETSRVAPSILIEFINMFLFPASKTSGLYTGQEYVQRVLLVVTALSVPVLFLGKPLFLLWLHNGRSCFGVNRSGYTLIRKDSEEEVSLLGSQDIEEGNHQVEDGCREMACEEFNFGEILMTQVIHSIEYCLGCISNTASYLRLWALSLAHAQLSDVLWAMLMRVGLRVDTTYGVLLLLPVIALFAVLTIFILLIMEGLSAFLHAIRLHWVEFQNKFYVGAGTKFVPFSFSLLSSKFNNDDSVA", "text": "FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery (PubMed:16415858). May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (PubMed:18157129). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endosome membrane. Note=In kidney proximal tubules, also detected in subapical vesicles. SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family."}
{"protein": "MAPENFTRVTEFILTGVSSCPELQIPLFLVFLVLYVLTMAGNLGIITLTSVDSRLQNPMYFFLRHLAIINLGNSTVIAPKMLMNFLVKKKTTSFYECATQLGGFLFFIVSEVMMLAVMAYDRYVAICNPLLYMVVVSRRLCLLLVSLTYLYGFSTAIVVSPCIFSVSYCSSNIINHFYCDIAPLLALSCSDTYIPETIVFISAATNLVFSMITVLVSYFNIVLSILRIRSPEGRKKAFSTCASHMIAVTVFYGTMLFMYLQPQTNHSLDTDKMASVFYTLVIPMLNPLIYSLRNNDVNVALKKFMENPCYSFKSM", "text": "FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MGLLDGNPANETSLVLLLFADFSSMLGCMAVLIGFWRLKLLRNHVTKVIACFCATSFCKDFPSTILTLTNTAVNGGFPCYLYAIVITYGSFACWLWTLCLAISIYMLIVKREPEPERFEKYYYLLCWGLPLISTIVMLAKNTVQFVGNWCWIGVSFTGYRFGLFYGPFLFIWAISAVLVGLTSRYTYVVIHNGVSDNKEKHLTYQFKLINYIIVFLVCWVFAVVNRIVNGLNMFPPALNILHTYLSVSHGFWASVTFIYNNPLMWRYFGAKILTVFTFFGYFTDVQKKLEKNKNNNNPSPYSSSRGTSGKTMGGHPTGDDVQCSSDMEQCSLERHPNMVNNQQNLNNNYGLQQNYNDEGSSSSSLSSSDEEKQTVEMQNIQISTSTNGQGNN", "text": "FUNCTION: Receptor for cAMP. Coordinates the aggregation of individual cells into a multicellular organism and regulates the expression of a large number of developmentally regulated genes. The activity of this receptor is mediated by G proteins. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 5 family."}
{"protein": "MHSLTRIKVLQRRCTVFHSQCESILLRYQDEDRGLQAEEEAILEQIAGLKLLLDTLRAENRQLSREEIYTLLRKQSIVRRQIKDLELQIIQIQEKRSELEKKREEFQKKSKYWLRKEGNYQRWIIRQKRFYIQREIQQEEAESEEII", "text": "FUNCTION: Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. SIMILARITY: Belongs to the SpaM family."}
{"protein": "MAYRLITQVVVVGSRVLGRAFAEAYKQAAASSQYQRAQQKNGNAATGRASLTSGMTLDEACKILNVNKPADGTAANMEEVMERFKRLFDANDPEKGGSFYLQSKVVRARERLEAEIKPKMEEKQAEEEVKEGWNPKIYKDR", "text": "FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (hsp70-5) via its interaction with tim14/pam18. May act by positioning tim14/pam18 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TIM16/PAM16 family."}
{"protein": "MISKSSPLIFERSKKDRYAYSLPQNDIENISIASLLDDKYIRKHKAEFPEVSELDLVRHYTELSNKNFGVDTGFYPLGSCTMKYNPKINEKVARISGFSESHPLQEEEHVQGSLEIIYSLQEELKEITGMDEVTLQPAAGAHGEWTALMIFKAYHEKNGQSHRDEVIVPDSAHGTNPASASFAGFKSVTVKSNQRGEVDIEDLKRVVNDNTAAIMLTNPNTLGIFEQDIIEIGKIVHEAGGLLYYDGANLNAILDKVRPGDMGFDAVHLNLHKTFTGPHGGGGPGSGPVGVVEKLASYLPKPMVIKDNDRYKYDNDIPNSIGRVKPFYGNFGIYLRAYTYIRSMGANGLKEVSEAAVLNANYIKSRLKNHFEIPFNQYCKHEFVLSGTLQKQYGVRTLDMAKRLLDFGVHPPTIYFPLNVEEGMMIEPTETESKETLDYFIDAMIQIADETKNDPDKVLEAPHTTIIDRLDETTAARKPILKFEELKDEKYKEHTNIDSEDN", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily."}
{"protein": "MIQVLLVTICLAALPYQGSSIILESGNVNDYEIVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLYLEKNKQLFSKDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLSNSEAHAVYKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEHQKYNPFRFVELVLVVDKAMVTKNNDDLDKIKTRMYELANTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSPINLVVAVIMAHEMGHNLGIHHDSGYCSCGDYACIMRPEISPEPSTFFSNCSYFDCWDFIMNQNPECIVNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTKCADGKVCSNGHCVDVATAY", "text": "FUNCTION: This protein is a zinc metalloprotease from snake venom that possesses hemorrhagic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily."}
{"protein": "MLYLSEENKSVSTPCPPDKIIFDAERGEYICSETGEVLEDKIIDQGPEWRAFTPEEKEKRSRVGGPLNNTIHDRGLSTLIDWKDKDAMGRTLDPKRRLEALRWRKWQIRARIQSSIDRNLAQAMNELERIGNLLNLPKSVKDEAALIYRKAVEKGLVRGRSIESVVAAAIYAACRRMKLARTLDEIAQYTKANRKEVARCYRLLLRELDVSVPVSDPKDYVTRIANLLGLSGRVMKTAAEIIDKAKGSGLTAGKDPAGLAAAAIYIASLLHDERRTQKEIAQVAGVTEVTVRNRYKELTQELKISIPTQ", "text": "FUNCTION: Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). SIMILARITY: Belongs to the TFIIB family."}
{"protein": "MAKKKASIPFLSLTSIVFLPWCISFTCKKGMEYWVTNWWNTKQSEIFLNIIQEKSILKKFMELEELFFLDELLKEYSETRLQILRTGIHKETIQLIKTHNEDRIYTILHFSTNIIYFIILSGYSILGNQELIILNSWVQEFLYNLSDTIKAFSILLVTDLCIGFHSTHGWELLIGSVYKDFGFIQNDQIISGLVSTFPVILDTILKYWIFRYLNRVSPSLVVIYHSMND", "text": "FUNCTION: May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Cema family."}
{"protein": "MSLAEAKKLDKKFPTFKNEFAIPTFGSLGIKNNKYESSTESIYLCGNSLGLMPKNTKKAINDELNAWVERGVESHFNHPDKSLTPWVDIDLPLLPLIAPIVGAKENEVAVMGSLTANLNALLIHFYKPEGKRTKILFEKQAFPSDYYAFLNIVKLFGYDEKHLIQLEVQPGETYIKTERIIKAIDENSDELALVCFPGIQYYTGQFFKIEEITKYAKEKSQQIKVGWDLAHAVGNVPLNLHDWGVDFAAWCSYKYLNSGPGAIGGIFVHEKYTIENKKSSFVPRLAGWWGNNSQERFKMLEEFDPINSALSYRQSNPSVLDVVAVKSSLEVYAKVGGVSKLREKSVALTQFLQDLLTNSKYYIPQSSTSNSKFGFKILTPLNPAERGCQLSIMFQPHFDEKDKNVMERVNAYLHDHAIICDERRPDVIRLAPLPLYNTFEETFIAVQRLFEALDNISKEYM", "text": "FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the kynureninase family."}
{"protein": "MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKTLDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQQQEEARRRRQEQSPWNPRAGLDPRE", "text": "FUNCTION: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates. SUBCELLULAR LOCATION: Host cell membrane. Host nucleus envelope. Host nucleus lamina. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. SIMILARITY: Belongs to the adenoviridae E1B 19 kDa protein family."}
{"protein": "MYPVDLHMHTVASTHAYSTLSDYIAQAKRKGIKLFSITDHGPDMADAPHHWHFINMRIWPRIVDGVGILRGIEANIKNTEGEIDCFGQMYDSLDLIIAGFHEPVFAPHDKATNTQAMIATIASGNVHIISHPGNPKYPIDIMAVAEAAAKHQVALEINNSSFIHSRKGSEDNCRAVAAAVRDAGGWIALGSDSHTAYTLGEFDEALKIIEAVDFPEDRILNVSPARMLGFLESRGMTPIAEFAEL", "text": "SIMILARITY: Belongs to the PHP family."}
{"protein": "MYPEYQNIFTQVQVRGTPEMGMDDAGNNMMEERVGKPFFSTLAGLFGNGQIGPYYFGWTSIVAFGTGIAWFVIVGFNMLAQVGWSIPQFIRQLFWLALEPPSPEYGLSMPPLNDGGWYIIASFFLLVSVMTWLLRAYLLAEQHKMGKHIFWGFAAAVWLFLVLGLFRPILMGSWSEAVPYGIFPHLDWTTAFSIRYGNLYYNPFHCLSIVFLYGSVLLFCMHGGTILAVTRYGGDRELEQIYDRGTATERAALFWRWTMGFNATMEGIHRWAWWFAVLTPITGGIGILLTGTVVDNWFIWAQEHHFAPMYDGSYGYEDYGSYEAFIGKEN", "text": "FUNCTION: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. SUBCELLULAR LOCATION: Cellular chromatophore membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family."}
{"protein": "MNDNREQLTQQIIDAGRFLYGRGWSPATSSNYSARLDEQRALLTVSGKHKGQLGFDDVLATDLAGNSLEPGKKPSAETLLHTQLYAWNPAIGAVLHTHSVNATVLSRLVRGDRLVLQDYELQKAFAGVTTHEGQVEVPIFDNDQDIARLASRVQPWLEAHPHCPGYLIRGHGLYTWGARMSDALRQVEAFEFLFECELKVLSLSR", "text": "FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily."}
{"protein": "MSPVFPMLTVLTMFYYMCLRRRARTATRGEIMNSHRTVESNSRTSPLNAEVVQYAKEVVDFSSHYGSENSMSYTMWNLAGVPNVFPSSGDFTQTAVFRTYGTWWDQCPSAPVPFKRTPANFQSQDYVELAFEQQVYPTAVHVLETYHPGAVIRILACSANPYSPGPPAEVRWETLWSEKPTKVNASQARQFKPCIKQINFPTNLIRLEINSSLLDYYTELDAVVLHGMKDKPMLSLKTSLIDMNDLDEDDYEEKDDCEIDNLNKKFSSTALREGPSNGYFDKLPYELIQLILNHLTLPDLCRLAQTCKLLNQHCCDPLQYIHLNLQPYWAKLNDTSLEFLQARCTLVQWLNLSWTGNRGFISVAGFSRFLKVCGSELVRLELSCSHFLNETCLEIISEMCPNLQDLNLSSCDKLPPQAFSHIAKLCGLKRLVLYRTKVEQTALLSILNFCSDLQHLSLGSCVMIEDYDVTASMIGAKCKKLRTLDLWRCKNITESGIAELASGCPLLEELDLGWCPTLQSSTGCFARLARQLPNLQKLFLTANRSVCDTDIEELASNCTRLRQLDILGTRMVSPASLRKLLESCKDLSLLDVSFCSQIDNRAVLELSASFPKVFIKKSFTQ", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion."}
{"protein": "MSAHLIDGKAIAAEIDARAGEVGAKLASSLGRPPCLAVVLVGEDPASDVYVRNKVRRTEAAGLTSIEIRKSAEATEAEIIAIVERLNADDGVDGILVQMPLPGHIDTNRVIGRIDPDKDVDGLTEVSAGRLVLGKPGLRPCTPAGCVLLAERALGDLSGKSVVVIGRSILVGKPAALLFLEKNATVTIAHSRTADLPSLCRTADILVPAVGRPEMVRGDWVKPGACVLDVGINRIDAPERGAGKTRLVGDAAFDEIVGHAGWITPVPGGIGPMTIAMLLKNTVIAAALRAKQPALADF", "text": "FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family."}
{"protein": "MRPLARLRGRRVVPQRSAGELDAMAAAGAVVAAALRAIRAAAAPGTSSLSLDEIAESVIRESGATPSFLGYHGYPASICASINDRVVHGIPSTAEVLAPGDLVSIDCGAVLDGWHGDAAITFGVGALSDADEALSEATRESLQAGIAAMVVGNRLTDVAHAIETGTRAAELRYGRSFGIVAGYGGHGIGRQMHMDPFLPNEGAPGRGPLLAAGSVLAIEPMLTLGTTKTVVLDDKWTVTTADGSRAAHWEHTVAVTDDGPRILTLG", "text": "FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily."}
{"protein": "MRDIVIIGHKAKTSGDFSLNDLPGSAGRMDILCRCVSSALFLSFGMRRDVNVHLLLLGEPEPGKIIRFEGLHLRYLNPDERSSGSLIQKALQKTVTEKDIRSTPGVWVRNGDLNTLLASFEGRTLFYLREDGEDIRGLDREIRDPVFILGDHMGVTEEEEKQLLEAGAKIISVGPISLHSNHCITLLHNELDRAEAERGEIPGGEKLRAGE", "text": "FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family."}
{"protein": "MATDMSQGELIHPKALPLIVGAQLIHADKLGEKADDSTMPIRRAVNSTRETPPKSKLAEGEEEKPEPDGSSEESISTVEEPENETPPAPSREAEQPKGEPESGEKEESKSAEETKKEEKDQSKEKEKKVKKTIPAWATLSASQLARAQKQTPMASSPRPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLDLERRGYLLKQALKRELNRGVIKQVKGKGASGSFVVVQKSKTPQKSKNRKKGSAVDPEPQVKLEDVLPLAFTRLCEPKEASYSLIRKYVSQYYPKLRVDIRPQLLKNALQRAVERGQLEQITGKGASGTFQLKKSGEKPLLGGSLMEYAILSAIAAMNEPKTCSTTALKKYVLENHPGTNSNYQMHLLKKTLQKCEKNGWLEQISGKGFSGTFQLCFPYYPSPGVLFPKKVSDGSEDEDEEEDEEESSEDSEDEEPPPKRSLQKKTPAKPQGKTASMKQRGAKPARKVPAAQRGKVRPLPKKAPPKAKTPARKGRPAPSAVKKPSGSTSKKPVANARKEAKLPGKGKSAMKKKSFKTKK", "text": "FUNCTION: Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity. May play a role in hypoxia-induced oncogenesis. SUBCELLULAR LOCATION: Nucleus Chromosome Note=localized in nuclei but not in nucleoli in interphase. Colocalized with chromosomes in mitosis, with a gradually increased during G1 progression and a maximum level during late G1 phase (G1/S)."}
{"protein": "MGSRPFTKNPAPMMLTIRVALVLSCICPANSIDGRPFAAAGIVVTGDKAVNIYTSSQTGSIIVKLLPNLPKDKEACAKAPLDAYNRTLTTLLTPLGDSIRRIQESVTTSGGGRQGRLIGAIIGGVALGVATAAQITAAAALIQAKQNAANILRLKESIAATNEAVHEVTDGLSQLAVAVGKMQQFVNDQFNKTAQELDCIKIAQQVGVELNLYLTELTTVFGPQITSPALNKLTIQALYNLAGGNMDYLLTKLGIGNNQLSSLIGSGLITGNPILYDSQTQLLGIQVTLPSVGNLNNMRATYLETLSVSTTRGFASALVPKVVTQVGSVIEELDTSYCIETDLDLYCTRIVTFPMSPGIYSCLSGNTSACMYSKTEGALTTPYMTIKGSVIANCKMTTCRCVNPPGIISQNYGEAVSLIDKQSCNVLSLGGITLRLSGEFDVTYQKNISIQDSQVIITGNLDISTELGNVNNSISNALNKLEESNRKLDKVNVKLTSTSALITYIVLTIISLVFGILSLILACYLMYKQKAQQKTLLWLGNNTLDQMRATTKM", "text": "FUNCTION: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family."}
{"protein": "MTIISDSQIVVALISALVTGILALRLGRELYR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaM family."}
{"protein": "MTAEGPSPPARWHRRLPGLWAAALLLLGLPRLSVRADGKFFVLESQNGSQGLQLEAARLSCKSRGAHLASADELRRVVQDCSFAVCTTGWLADGTLGTTVCSKGSGEQQIMRAVDVRIESNPVPGGTYSALCIKDEEKPCGDPPSFPHTILQGRTGLEMGDELLYVCAPGHIMGHRETAFTLLCNSCGEWYGLVQACGKDEAEAHIDYEDNFPDDRSVSFRELMEDSRTEADEDRGQGDSSEEAPKQDRLVSISVGRENIARDKVFVPTTGLPGAGSSVPADSPGSRLLQKHLFWFPAEAFHKPGLEKEVDDDTKKQFSAGDNHSGVKLVPGEPETKVIYGNTDGPSGPFVGKNDSKAGDPVVSSSDESWLDGYPVTEGAWRKTEAEEEEDGDRGDGSVGLDENVLVTPDQPILVEVKKPKSSTLTPSEGMTHSSVLPSQMLDVEALALRPVNASETEGIGDGDLTKYQSTLPWRFITEESPMATLSYELTSSTLEILTVNTVKQTPNHIPSTIMATTQPPVETTVPEIQDSFPYLLSEDFFGQEGPGPGASEELHPTLESCVGDGCPGLSRGPVIATIVTVLCLLLLLAGVGMVWGYRKCQHKSSVYKLNVGQRQARHYHQQIEMEKV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MFDIGFWELVLISVIGLVVLGPERLPHAIRSVMHWITTAKNMANSVKTEVTQELKLHEINENMIKASKQGLSDLDPELQKSIDEMKETAEQLSRPYKKDIDDIKTSLDKNPSGTTQQENSILDSSKTTPPRQDKNE", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatB family."}
{"protein": "MAHFGVVVGLMMILVFLVFLSSIHKVEEGHLAVYYRGGALLGGPGDPGYHIMFPFITYFRSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNMLTPSAVYDVVRNYTADYDKTLIFNKIHHELNQFCSSHTLQEVYIELFDQIDENLKLSLQMELNVMAPGLTIQAVRVTKPKIPEAIRRNFELMESEKTKLLIAEQRQKVVEKEAETERKKAVIEAEKVAQVAKIQYRQKVMEKETEKFISEIEDSAYLAREKAKADAEYYTAQKSADANKLKLTPQYLELIKYQAVSANNKIYFGSNIPTMFFDSSSRSRIEGKSA", "text": "FUNCTION: Mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. Binds cholesterol and may promote ER retention of the SCAP-SREBF complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane. SIMILARITY: Belongs to the band 7/mec-2 family."}
{"protein": "MKKAVVLLSGGMDSAAVIALAQEQGFAVYALSVRYGQRHTSELDAAARVAAAQGVVAHKVVDVDLRSIGGSALTDDIDVPDAGGDGIPVTYVPARNTIMLSLALGWAEVVGANDLFCGVNAVDYSGYPDCRPEFVRAFEVLANLATKAGVEGAGLRVHAPLQFLSKADIVREGVRLGVDFGLTVSCYRADADGRACGHCDACRLRAAGFADAGVPDPTHYAILS", "text": "FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). SIMILARITY: Belongs to the QueC family."}
{"protein": "MLTKNLLLCFAAAKAALAVPHDSVAQRSDALHMLSERSTPSSTGENNGFYYSFWTDGGGDVTYTNGDAGAYTVEWSNVGNFVGGKGWNPGSAQDITYSGTFTPSGNGYLSVYGWTTDPLIEYYIVESYGDYNPGSGGTYKGTVTSDGSVYDIYTATRTNAASIQGTATFTQYWSVRQNKRVGGTVTTSNHFNAWAKLGMNLGTHNYQIVATEGYQSSGSSSITVQ", "text": "FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MNQLLCPGLYCPFPSQTNKYVDVLEEYSLEWVLRFNLLANESAYKRFCKSKFFFLAASAYPDSKFEELKITHDWLSWVFIWDDQCDLSELKKQPEVLNNFHQRYLEILNGAELTSQDTLFSHALIDLRKRTLQRASIKWFNYFISYLEDYFYGCVQEATNRAKGIVPDLDTYIMIRRSSVGVYAVLALSEFCNQFIIPDVLRNHHLVKKLELITTDIIAWSNDIFSASREIASGDVHNLIFVLHYHKKISLEKAIEQVVKIHNEEVHSLIKVESSLSFFSEELDVEITKYISGMHSWIRGNLDWCYESYRYHNLERLELTEFK", "text": "FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to the sesquiterpene germacrene A. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MSQMLHIEIPNFGNTVLGCLNEQRLLGLYCDVSIVVKGQAFKAHRAVLAASSLYFRDLFSGNSKSAFELPGSVPPACFQQILSFCYTGRLTMTASEQLVVMYTAGFLQIQHIVERGTDLMFKVSSPHCDSQTAVIEDAGSEPQSPCNQLQPAAAAAAPYVVSPSVPIPLLTRVKHEAMELPPAGPGLAPKRPLETGPRDGVAVAAGAAVAAGTAPLKLPRVSYYGVPSLATLIPGIQQMPYPQGERTSPGASSLPTTDSPTSYHNEEDEEDDEAYDTMVEEQYGQMYIKASGSYAVQEKPEPVPLESRSCVLIRRDLVALPASLISQIGYRCHPKLYSEGDPGEKLELVAGSGVYITRGQLMNCHLCAGVKHKVLLRRLLATFFDRNTLANSCGTGIRSSTSDPSRKPLDSRVLNAVKLYCQNFAPSFKESEMNVIAADMCTNARRVRKRWLPKIKSMLPEGVEMYRTVMGSAAASVPLDPEFPPAAAQVFEQRIYAERRGDAATIVALRTDAVNVDLSAAANPAFDAGEEVDGAGSVIQEVAAPEPLPADGQSPPQPFEQGGGGPSRPQTPAAAARRPEGTYAGTL", "text": "FUNCTION: Functions as a transcriptional repressor through its association with the NuRD complex. Recruits the NuRD complex to the promoter of MDM2, leading to the repression of MDM2 transcription and subsequent stability of p53/TP53. SUBCELLULAR LOCATION: Nucleus Note=Predominantly associated with chromatin."}
{"protein": "MDTTHDRRTSLSCDECRRRKLKCDRVRPQCGTCALSESECVFPGDSRKRGPKKGQLQALRARIRTLEQQLAAKDATWNMTYDFQDSTAAEPDEFSQCIQPNVNVFEPESMETLIFGIASSTSWPKNGMTPLDPALGAESHDSHISSTLSSLSLSALVQADLEQLFFDRVYQSAPIIHKARYITLMEQEDPLPACVCLRLAIRTSAAAFSARYHDIGERLYLETLQSLESLESNEHTLPWGAKNIQIEHIQSWLLLAVYEHMRMDKSQASSATSRALRLVQRCRLGDLDASDCLIQVGSHTTTATEEDFAVMEEKRRTFWLAFCFDRLLNTRDDLNWALPEEMVGFQHGHSLFSPGHFQGASLMYDLQIRMRVPASEASFQHSQDTNMPLLSEVMGEGNDDSLSPFATCVALMALYGCCATHRRLVSIAGGSGNESTKFWMRHNWLMSAIEKQRRLLQAPESTPNIFGDDPMLAFTHFFVPTLILHLVETADLWQWHSAEQEELRSVYKQQAYIAAKDRTRVAESLLCFSGFKVHPFLPTVLVRFFDFSGKRRIEMSDPDATSESRRNIRAMTKVLSLLRDIHRSAKEIPDDVLDGLETTLL", "text": "FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAKEPVRVLVTGAAGNQEPILVKEESVVGIPTPLLKLKSWQWWVLVSVNIFFLIGGQAASVLLGRFYYDEGGNSKWMATLVQTAAFPILYIPLLLLPSSASVESSESSCSLKYIVLIYVLLGVIIAGDNMLYSVGLLYLSASTYSLICATQLAFNAVFSYFINAQKFTALILNSVVLLSFSAALIALNDDADTPSGVSRSKYIVGFVCTLAASALYSLLLSLMQFSFEKILKRETFSVVLEMQIYTSLVATCVSVIGLFASGEWRTLHGEMEGYHKGQASYVLTLVWTAVTWQVCSVGVVGLIFLVTSLFSNVISTLSLAVTPLAALVVFRDKMSGVKIMAMLIAIWGFASYVYQNHIDDLKVRQARQQAQAGRVEPPC", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the purine permeases (TC 2.A.7.14) family."}
{"protein": "MENYPQFLLFFILASVVGIVSIAVALSWVLHYREGLGWDGGAAEFNWHPLLMVIGFIFLQGIAIVVYRLPWTWRCSKQMMKLIHAGLHILAFILAVISVVAVFVFHNAKNIPNMYSLHSWVGLAAVVLYPSQIVLGIAVYLIPVTPVRVRAALMPLHIYSGLFIFISVIAAALMGITEKLIFSLKSPAYKDSPPEAVLVNVLGLLIAAFGALVVWIATRSAWKRPREETAQTLSNNTTSPEEIKVGTDMTTTS", "text": "FUNCTION: Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe(3+) into Fe(2+). It is also able to reduce extracellular monodehydro-L-ascorbate and may be involved in extracellular ascorbate regeneration (By similarity). May also function as a cupric transmembrane reductase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein."}
{"protein": "MSESGSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKVTTAPGRKPRGRPKKLEKEEEEGISQESSEEEQ", "text": "FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the HMGA family."}
{"protein": "MEKRRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESARQAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTFGDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGTNGTLVLSRVFD", "text": "FUNCTION: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition. SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family."}
{"protein": "MTSTPDSRSVLTVIILGASGDLAKKKTYPALFGLYLRDLLPSNTIIYGYARSHIEIGDFKARISKGLKGDEEKKKQFLNLLHYHSGKYDEKASYDEFEKLILAEEKKQQGVDKFNRLFYMAIPPSIFIEVSIGIHGSLISKNGWSRVIVEKPFGRDLASSRELVSELGKLFKEKDLFRIDHYLGKEMVQNLMVLRFANAVFEPLWSKSHISSITITFKEDIGTEGRGGYFDQFGIIRDVMQNHLLQVLSLVAMEPPVSLNADDITNEKVKLLRCIQPIKMSEVVLGQYTSDPEGKIPAYLDDEGVPKDSTTPTYAAAVFHINNPRWRGMPFILKCGKALDERKTEVRIQFKRPDNFLFSDDDISRNELVMRIQPGEAVYLKLLSKKPGLENKIEQTELDLSYRHRFENLDLPDAYERLILDSIKGDHNLFVRDDELDVAWQIFTPLLDQIEKEKIKPEPYSFGSRGPKSADELSKKFGFIRSLGYNWPGNSPQGSKK", "text": "FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family."}
{"protein": "MTRVKRGYVARKRHNRILKLTAGSKRAHSRLVRPAQQQAMKTLAYSHRDRNRRKRDFRHLWIARINATVRQYDVSYSQAISLIQKSKMLLNRKMLAQIAVLDNSSFNSILTAAIYST", "text": "FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
{"protein": "MESMLTLAMEQPVKRNTLKKYKIACIVLLALLVIVSLGLGLGLGLRKPEKQGSCRKKCFDASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNQFRCGETRLEASLCSCSDDCLQRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLHTWDTLMPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVMGLYPESHGIIDNNMYDVNLNKNFSLSSKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEAAINGSFPSIYMPYNGSVPFEERISTLLKWLDLPKAERPRFYTMYFEEPDFSGHAGGPVSARVIKALQIVDHAFGMLMEGLKQRNLHNCVNIILLADHGMEQTYCNKMEYMTDYFPRINFYMYEGPAPRIRAHSIPHDFFSFNSEEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDRQWLAVRSKSNTNCGGGNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLNHLLKVPFYEPSHAEEVSKFSVCGFANPLPAESDCLCPHLQNSIQLEQVNQMLNLTQEEITATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPTVPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEEFTKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHYFVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNMESCPEGKPEALWVEERFTAHIARVRDVELLTGLDFYQEKVQPVSEILQLKTYLPTFETTI", "text": "FUNCTION: Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (By similarity). Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells (By similarity). Has also alkaline phosphodiesterase activity (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Apical cell membrane; Single-pass type II membrane protein Secreted Note=Detected at the cell surface of basophils. Detected at the apical plasma membrane of bile duct cells. Located to the apical surface in intestinal and kidney epithelial cells. Secreted in serum, and in lumen of epithelial cells."}
{"protein": "MKIEAVIFDWAGTTVDYGCFAPLEVFMKIFHKRGVEITAEEARKPMGLLKIDHVRALTEMPRIADEWKRVFGQLPTEADIHEMYEEFAEILFSILPSYATPIDGVKEVIASLRERGIKIGSTTGYTREMMEIVVKEAVLQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGVILGSSELGLTEEEVESMDSVELREKIEIVRNRFVENGAHFTIETMQELENVMEHIEKQELIIS", "text": "FUNCTION: Involved in phosphonate degradation. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family."}
{"protein": "MMDLDNIPDTQTEAEELEEVVMGLIINSGQARSLAYAALKQAKQGDFAAAKAMMDQSRMALNEAHLVQTKLIEGDAGEGKMKVSLVLVHAQDHLMTSMLARELITELIELHEKLKA", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ChbABC PTS system is involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2) (PubMed:10913118, PubMed:10913117). Also able to use N,N',N''-triacetyl chitotriose (GlcNAc3) (PubMed:10913117). FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ChbABC PTS system is involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MTRVLEPAEPILSNDGTPYSPRYDDVYHSARGGLAQAHHVFLGGNGLPEGWAGREQFVIVETGFGQGLNFLATWQAWRSDPQRCRRLHFVSIEKHPFTREGLARLHAHAGLGDLLPLSDQLQQQWPDALPGLHRLSFEDGAVTLTLALGDVETMLPKLVLGADAFYLDGFSPSRNAEMWSDTVFRGLARLARIGATLATYTAAGFVRRGLTAAGFEAHKAPGFGGKRDMTVARFAPVWKNRRHAPPEAAQWAERHAIVIGAGLAGCAVTERLAARGWRVTLLDAHDGPARQTSCHRAAAMHAHVSADDSFLSRLSRAGNLHALRAWGALEAAGYPVGWHGTGVLQIGEDDAENAAQQAALAELRFPESFVRWMSPQEATEQHGATVPRGGLWFPKGGWVAPPDICRAQLAKAGAAVDALFNCRVAAIRRIGDAWQALADDGGVLAAAPVLVLANAYEADRLTSGQFLALRRVRGQLTDLAPAQAEALGGWPDCVVTGGGYLLPRDAAGGARMGSSYEADEGPLVERPEVHAANLDRLASMLPDRASQIAQIDPATLQGYVGVRTVTYNRLPLVGRIADDAQALSRAAALRGAHLRDLPRLPGLYAALAYASRGLTWAALCAELIASQIEGEPLPLEADLADAIDPARLLLRALRHGHAQAPESAGPGVDAAG", "text": "FUNCTION: Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the DAO family. SIMILARITY: In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family."}
{"protein": "MALSSALDSLWHQLDQLLSLINRNIITGIIVLPVLYVLLKVIYNLYLSPLAGYPGPKLWAVSRLPWNRANMKGRISWKIRELHDKYGPVVRIAPDELSYTTSGAWKKIYGQRNPEFVKALDGRGIAPASIGGQRSLMTEHQDKHLRLRRAIDPAFSQRALREQESYFQDHSDNLVQKLKQRCKDGPLDMTTWYNLVAFDIVSDLAFGEPSGCVNNPDQPWIQAILARAKAIVWFQLAVQYGFMGLLNWMTPKYVTESRKKHIAMTEAKLKARVEAKNPGKDFMSYILENDEKLNHLELVMLSSNFIVAGSGTSAGGMSGLTYLLLRNPDKLEKLKQEIRGLFKSRADMTLQAVTSCKYLRACLNEGMRLYPPTPGSLPRFVPGKGEMIEGKWVPGGYAVGVNQLAAGHSERNFKKAREFHPERWLDEPDSEFKDDDRSAVQPFSYGQRGCIGRSMAYAEMSLTMAKLVWYFDWELDEPDNDWWNQQGTYLVWEKLPLQVKLTPVSDVVE", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of alternapyrone derivatives (PubMed:16356847). Alternapyrone is a decaketide with octa-methylation from methionine on every C2 unit except the third unit (PubMed:16356847). All the domains in the polyketide synthase alt5 are apparently involved in alternapyrone synthesis, that is, the 8 CMeT, 7 KR, 7 DH, and 4 ER reactions in the 9 KS-mediated condensation steps required for alternapyrone synthesis (PubMed:16356847). the alternapyrone produced by alt5 might be intensively modified by cytochrome P450 monooxygenases alt1, alt2 and alt3 and FAD-dependent oxidoreductase alt4 present in the alt gene cluster (PubMed:16356847). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MDIGKKHVIPKSQYRRKRREFFHNEDREENLNQHQDKQNIDNTTSKKADKQIHKDSIDKHERFKNSLSSHLEQRNRDVNENKAEESKSNQDSKSAYNRDHYLTDDVSKKQNSLDSVDQDTEKSKYYEQNSEATLSTKSTDKVESTDMRKLSSDKNKVGHEEQHVLSKPSEHDKETRIDFESSRTDSDSSMQTEKIKKDSSDGNKSSNLKSEVISDKSNTVPKLSESDDEVNNQKPLTLPEEQKLKRQQSQNEQTKTYTYGDSEQNDKSNYENDLSHHMPSISDDKDNVMRENHIVDDNPDNDINTPSLSKTDDDRKLDEKIHVEDKHKQNADSSETVGYQSQSSASHRITEKRNNAINDHDKLNGQKPNAKTSANNNQKKATSKLNKGRATNNNYSDILKKFWMMYWPKLVILMGIIILIVILNAIFNNVNKNDRMNDNNDADAQKYTTTMKNANNTVKSVVTVENETSKDSSLPKDKASQDEVGSGVVYKKSGDTLYIVTNAHVVGDKENQKITFSNNKSVVGKVLGKDKWSDLAVVKATSSDSSVKEIAIGDSNNLVLGEPILVVGNPLGVDFKGTVTEGIISGLNRNVPIDFDKDNKYDMLMKAFQIDASVNPGNSGGAVVNREGKLIGVVAAKISMPNVENMSFAIPVNEVQKIVKDLETKGKIDYPDVGVKMKNIASLNSFERQAVKLPGKVKNGVVVDQVDNNGLADQSGLKKGDVITELDGKLLEDDLRFRQIIFSHKDDLKSITAKIYRDGKEKEINIKLK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S1C family."}
{"protein": "MLTYETWEEDSMSFSERDETKGALAVLEWAYKQYNDEIVYACSFGVEGMVLLHLINEVNPFAQVVFLDTNVHFCETYALIERVRQRFPKLNIIEKQPGLTLEEQEDKYGKDLWEHNPNLCCKLRKILPLEELLANKNAWISGLRREQSETRKHTKFINQDHRFQSIKICPLIHWTWKEVWRYVYKHNLPYNPLHDVGYPSIGCEKCTLPVGKYGSSRDGRWAGSVKTECGLHDQ", "text": "FUNCTION: Catalyzes the formation of sulfite from adenosine 5'- phosphosulfate (APS) using thioredoxin as an electron donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily."}
{"protein": "MKRVLSNVLKAWIFTIVAFHNFSTSVTADAPVNAAEYNALCRLYNIARAGEGLKEEDWLPCAGKAACEKTAASIEDVFMKLNFSEPSAVVTTLDGTRVELQNSASTRIKRAKLAKVLAAAETIKAQQLKYHESSKSLLESAKANFTKAIVGGWGNPTTPDESGLPTTFKTNRADDCKLAGGNGGKSLVFDIACLCTTSDSASGSKYTCGPKSGDNGSGWLDNNGDNQGKPAAKEAWKNLRADCRRQSAGVRVTPELISQSLVIFEGLIGTRAASGHDNARYIFGTVATAQSCGHSTATNKGSIDYKASNAQQRGDIEWEKNLRMAEGDLRGLLTAKQLVAALQARAEHLEDAAFTIFNESVLETQIAWESSRPPSTDANTSQKGPLQRPEKSGESSHLPSGSSHGTKAIRSILHVALLM", "text": "FUNCTION: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Note=A soluble form is released from ruptured cells by the action of a PI-PLC."}
{"protein": "MDFVAGAIGGVCGVAVGYPLDTVKVRIQTEPKYTGIWHCVRDTYHRERVWGFYRGLSLPVCTVSLVSSVSFGTYRHCLAHICRLRYGNPDAKPTKADITLSGCASGLVRVFLTSPTEVAKVRLQTQTQAQKQQRRLSASGPLAVPPMCPVPPACPEPKYRGPLHCLATVAREEGLCGLYKGSSALVLRDGHSFATYFLSYAVLCEWLSPAGHSRPDVPGVLVAGGCAGVLAWAVATPMDVIKSRLQADGQGQRRYRGLLHCMVTSVREEGPRVLFKGLVLNCCRAFPVNMVVFVAYEAVLRLARGLLT", "text": "FUNCTION: Uncoupling protein which may catalyze the physiological 'proton leak' in liver. Overexpression induces the dissipation of mitochondrial membrane potential. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MVHMHITAWALGLILFFVAYSLYSAGRKGKGVHMGLRLMYIIIIVTGVWLYLDQTIVDKSYHMWYGLKMLAGILVIAGMEMVLVKMSKNKATGAFWGLFIIALVAVFYLGLKLPIGWQVF", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0344 family."}
{"protein": "MSLPPFTCRLLAAAAALYLIGLLCVGADTKDVTAPKIPGCSNEFQMVKVENWVNGENGETFTAMTAQFGTMLPSDKDKAVKLPVALTTPLDSCSNLTSKLSWSIALSVRGECAFTVKAQVAQAGGAAALVLINDKEELDEMVCGEKDTSLNVSIPILMITTSSGDALKKSIMQNKKVELLLYAPKSPIVDYAVVFLWLMSVGTVFVASVWSHVTSPKKNDEQYDELSPKKSSNVDATKGGAEEETLDISAMGAVIFVISASTFLVLLFFFMSSWFILILTIFFVIGGMQGMHNINVTLITRRCSKCGQKNLKLPLLGNTSILSLVVLLFCFVVAILWFMNRKTSHAWAGQDIFGICMMINVLQVARLPNIRVATILLCCAFFYDIFWVFISPLIFKQSVMIAVARGSKDTGESIPMLLRIPRLSDPWGGYNMIGFGDILFPGLLICFIFRFDKENNKGVSNGYFPWLMFGYGLGLFLTYLGLYVMNGHGQPALLYLVPCTLGITVILGLVRKELRDLWNYGTQQPSAADVNPSPEA", "text": "FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A22B family."}
{"protein": "MKDNSLLKMDHEDTHLGKVEIAPEVIEVIAGIAASEVDGVAEMRGNFATGVVERFGKVNHGKGVKVDLADDGITIDVYCVVTFGVSIPKVAASVQENIRQTLLNMTSLSINEINIHIVGIQFDTKAQEVQIDEEM", "text": "SIMILARITY: Belongs to the asp23 family."}
{"protein": "MTSPSTIKQKFIAKGHQLGVVAVGFSDGQPNQGVDPSGLIEAGLLDQLRDDLEYDIRHDGQVHTYAEFVPEHDPNHRGMKKPRTVSAATQQLSRQVYEHAREGRLVLTLGGDHSIAIGTISGTAKAIRERLGREMAVIWVDAHADINRPEDSDSGNIHGMPLAFLTGLAKDDNEDMFGWLQPDNLISPRKLVYIGLRDVDRAEKRLLREHGIKAFSMHDIDKYGIGRVVEMALAHIGQDTPIHLSFDVDALDPQWAPSTGTPVRGGLTLREGDFIAESIHETGSLVAMDLVEVNPTLETLGASETIRAGCSLVRSALGDTLL", "text": "SIMILARITY: Belongs to the arginase family."}
{"protein": "MPNWGGGKKCGVCQKTVYFAEEVQCEGNSFHKSCFLCMVCKKNLDSTTVAVHGEEIYCKSCYGKKYGPKGYGYGQGAGTLSTDKGESLGIKHEEAPGHRPTTNPNASKFAQKIGGSERCPRCSQAVYAAEKVIGAGKSWHKACFRCAKCGKGLESTTLADKDGEIYCKGCYAKNFGPKGFGFGQGAGALVHSE", "text": "FUNCTION: Could play a role in neuronal development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MATKINDDILSTPGKKTSVGDILKPLNSEYGKVAPGWGTTVLMGVFMALFAVFLVIILEIYNASVLLDGIPVSWNSLS", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbH family."}
{"protein": "MKTIILILLILGLGIDAKSLEESKADEEKFLRFIGSVIHGIGHLVHHIGVALGDDQQDNGKFYGYYAEDNGKHWYDTGDQ", "text": "FUNCTION: Exhibits broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria. Has potent hemolytic activity. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MARTKQTARKSTGGKAPRKQLATKVARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLMREIAQDFKTDLRFQSSAVMALQEACESYLVGLFEDTNLCVIHAKRVTIMPKDIQLARRIRGERA", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H3 family."}
{"protein": "MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNILTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDADLLHKHIEVANGPASHYETRPQTYVDHMDGSYSLSALPFSQMSELLTRAEERVLVRPHEPPPPPPMHGAGDAKPTPTCISSATGLIENRPQSPAAGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPATALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVAVAALAHPPSGLHPAPSTAPGPHAPLMPPSPPSQVLPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE", "text": "FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). Also involved in the regulation of mitochondrial dynamics (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Synapse Cell junction, focal adhesion Note=Dot- like pattern in the cytoplasm. Concentrated in Rac-regulated membrane- ruffling areas. Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2. In neurons, colocalizes with activated NTRK2 after BDNF addition in endocytic sites through the association with TMEM108 (PubMed:27605705). SIMILARITY: Belongs to the SCAR/WAVE family."}
{"protein": "MGLNKDRGLSSLISDMDTVYSKELGFDKNQSTMIEIDQISPNPFQPRKNFDQEALDELANSIKEFGLIQPIIVFKKNNKFILIAGERRLRAVKALGKKEILAFIADIDENKLRELALIENIQRENLNPIELANSYKDLMQVHKITQENLAELIHKSRTQITNTLRLLNLDIRTQELIASGKISQGHAKVLVGLDQKDEKMLVDSIIGQKLNVRDTEKIVKKIKNNESLPNQEFEDEIKKLKQILNRFGFDCKNKNNDFVIHLENIDKIKKLIKMLEKL", "text": "FUNCTION: Involved in chromosome partition. Localize to both poles of the predivisional cell following completion of DNA replication. Binds to the DNA origin of replication (By similarity). SIMILARITY: Belongs to the ParB family."}
{"protein": "MTKLQQTLYQFFGFTSFKKGQQDIIESILSGKDTIAMLPTGGGKSLCYQLPGYMLDGMVLIVSPLLSLMEDQVQQLKARGEKRAAALNSMLNRQERQFVLEHIHRYKFLYLSPEALQSPYVLEKLKSVPISLFVIDEAHCISEWGHDFRPDYSKLGQLRKKLGHPPVLALTATATKETLQDVMNLLELQHAVRHLNSVNRPNIALRVENAADTAEKIDRVIQLVENLQGPGIVYCPTRKWAKELAGEIKSKTSSRADFYHGGLESGDRILIQQQFIHNQLDVICCTNAFGMGVDKPDIRYVIHFHLPQTAEAFMQEIGRAGRDGKPSVSILLRAPGDFELQEQIIQMESVTAEEIADVIRVLEKTEERDERRLRDVLLQYGVGETQARMMIHLFMQGKTSVELMKKEISYRMELKLEKMHRVSFLLQRDGCLRQALLTYFDESYEPDDGNLPCCSHCGFDLSLYEQKGERSKMAPLDSWSSELHRIFSLQTVGELN", "text": "FUNCTION: Probable DNA helicase. Required in synaptic and/or post- synaptic stages of recombination. Probably has overlapping function with RecQ (AC O34748). It probably acts to help generate ss-DNA from ds-DNA breaks. SIMILARITY: Belongs to the helicase family. RecQ subfamily."}
{"protein": "MNLFRFLGDLSHLLAIILLLLKIWKSRSCAGISGKSQVLFAVVFTARYLDLFTNYISLYNTCMKVVYIACSFTTVWMIYSKFKATYDGNHDTFRVEFLVVPTAILAFLVNHDFTPLEILWTFSIYLESVAILPQLFMVSKTGEAETITSHYLFALGVYRTLYLFNWIWRYHFEGFFDLIAIVAGLVQTVLYCDFFYLYITKVLKGKKLSLPA", "text": "FUNCTION: Receptor for the C-terminal sequence motif K-D-E-L that is present on endoplasmic reticulum resident proteins and that mediates their recycling from the Golgi back to the endoplasmic reticulum. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPI-coated vesicle membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Note=Localized in the Golgi in the absence of bound proteins with the sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum together with cargo proteins containing the sequence motif K-D-E-L. SIMILARITY: Belongs to the ERD2 family."}
{"protein": "MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGVAVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGAPGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDRFDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFLGSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRSRIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIHLMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSLWRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAVQGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPVPQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCAPEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPEHCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAEQHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL", "text": "FUNCTION: Part of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGQ family."}
{"protein": "MQGRLSAWLVKHGLIHRSLGFDYQGIETLQIKPEDWHSIAVIFYVYGYNYLRSQCAYDVAPGGLLASVYHLTRIEDGVDQPEEVCIKVFASRRNPRIPSVFWVWKSVDFQERESYDMLGISYDNHPRLKRILMPESWIGWPLRKDYIAPNFYEIQDAH", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the complex I 30 kDa subunit family."}
{"protein": "MNNTLKYWKEAATLIVAARTSHGHFPYIQPQVQFPNQQNNTSDYEVLLLKRSQKSGFMPNAFVFPGGNIESSDFSSDWIKVFSRYEQKPNFGLGLVKQLDNRSPMFTADSSKFGSLIPGEVATRICAIRETFEESGILLVVPENFNSEDNQHLVEVTDQDKEKLSKWREEVQRNPSQFIQMCKEMRCMPNIWALKEWSNWLTPVISQGVKSRRFDTAFFICCLNAKPAVSDDNKEVTSFKWWTPTEALEDYKSHKIWIPPPQFYELSRLCHFAPINELHKFIVNRSLEGCERWMPVIAQCEDGIVHTLPGDDLYPEDPDLTGEKQTVVCSNETIENLIQKGGRFHRLVLIDGKPTLLVNIKPKYKHINPLTIESESKNKL", "text": "FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'- bisphosphate (By similarity). Mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters and at low substrate concentrations medium and long-chain fatty- acyl-CoA esters are the primary substrates (By similarity). Highest activity seen with medium-chain acyl-CoA esters and higher rates of activity seen with the unsaturated acyl-CoA esters compared with the saturated esters (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MSCSLRSGLVIVFCFILLLLSSNVGCASAARRLRSHKHHHHKVASLDVFNGGERRRALGGVETGEEVVVMDYPQPHRKPPIHNEKS", "text": "FUNCTION: [GLV1p]: Signaling peptide (root growth factor) that regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells (PubMed:22307643, PubMed:23370719). Also involved in the regulation of hypocotyl bending and root gravitropism in a PIN2-traffic dependent manner, thus influencing the formation of auxin gradients (PubMed:22421050). Maintains the postembryonic root stem cell niche (PubMed:20798316). SUBCELLULAR LOCATION: Endoplasmic reticulum Note=The precursor is detected in the endoplasmic reticulum probably during its processing. SUBCELLULAR LOCATION: [GLV1p]: Secreted. SIMILARITY: Belongs to the RGF family."}
{"protein": "MTEHVQVGGLQVAKVLFDFVNNEAIPGTGLTADKFWEGADKVIHDLAPKNKALLAKRDDFQARIDGWHQSRAGQPHDAVAYKAFLQEIGYLLPEAADFQATTQNVDDEIARTAGPQLVVPVMNARFALNASNARWGSLYDALYGTDAISEAGGAEKGKGYNKVRGDKVIAFARAFLDEAAPLATGSHVDSTGYKIADGKLVVTLKGGSTSGLRNDAQLIGFQGDANAPIAILLKNNGLHFEIQIDASTPVGQTDAAGVKDILMEAALTTIMDCEDSVAAVDADDKVVIYRNWLGLMKGDLAESVSKGGQTFTRTMNPDRTYTKVDGSELTLHGRSLLFVRNVGHLMTIDAILDKHGNEVPEGILDGLVTCLAAMHNLSGNTSRKNTRTGSVYIVKPKMHGPEEAAFTNELFGRIEDVLGLKRNTLKVGIMDEERRTTVNLKACIQAASERVVFINTGFLDRTGDEIHTSMEAGPMVRKADMKAEKWIGAYENWNVDIGLSTGLQGRAQIGKGMWAMPDLMAAMLEQKIAHPLAGANTAWVPSPTAAALHALHYHKVDVFARQAELAKRARASVDDILTIPLAVNPNWTPEQIKNELDNNAQGILGYVVRWIDQGVGCSKVPDINDVGLMEDRATLRISSQHIANWLRHGVVTEAQVMESLKRMAPVVDRQNANDPLYRPLAPNFDSNIAFQAAVELVIEGTKQPNGYTEPVLHRRRREFKAANGL", "text": "FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the malate synthase family. GlcB subfamily."}
{"protein": "MALRFPRFSQGLAQDPTTRRIWFGIATAHDFESHDDITEERLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFEAWVQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGALGPVNIAYSGVYQWWYTIGLRTNEDLYTGALFLLFLSAISLIAGWLHLQPKWKPSVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPGSRGEYVRWNNFLDVLPHPEGLGPLFTGQWNLYAQNPDSNSHLFGTSQGSGTAILTLLGGFHPQTQSLWLTDIAHHHLAIAFIFLVAGHMYRTNFGIGHSIKDLLEAHTPPGGRLGRGHKGLYDTINNSIHFQLGLALASLGVITSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFFIRDYNPEQNEDNVLARMLDHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPIFAQWIQSAHGKTSYGFDVLLSSTNSPAFNAGQSIWLPGWLNAINENSNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVSQFNESSTYLMGWLRDYLWVNSSQLINGYNPFGMNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWRDKPVALSIVQARLVGLAHFSVGYIFTYAAFLIASTSGKFG", "text": "FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family."}
{"protein": "MRILKPYLRSTSIQCYLCLLLNSHFLTEAGIHVFILGCISAGLPKTEANWQSVIHDLKTIEHLIQSMHMDATLYTESDAHPNCKVTALQCFLLELRVILHESKNAAIYEIIENLTMLADRNLSSIENKTELGCKECEELEKKSIKEFLKSFVHIVQMFINTS", "text": "FUNCTION: Cytokine that plays a major role in the development of inflammatory and protective immune responses to microbial invaders and parasites by modulating immune cells of both the innate and adaptive immune systems. Stimulates the proliferation of natural killer cells, T-cells and B-cells and promotes the secretion of several cytokines. In monocytes, induces the production of IL8 and monocyte chemotactic protein 1/CCL2, two chemokines that attract neutrophils and monocytes respectively to sites of infection. Unlike most cytokines, which are secreted in soluble form, IL15 is expressed in association with its high affinity IL15RA on the surface of IL15-producing cells and delivers signals to target cells that express IL2RB and IL2RG receptor subunits. Binding to its receptor triggers the phosphorylation of JAK1 and JAK3 and the recruitment and subsequent phosphorylation of signal transducer and activator of transcription-3/STAT3 and STAT5 (By similarity). In mast cells, induces the rapid tyrosine phosphorylation of STAT6 and thereby controls mast cell survival and release of cytokines such as IL4 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-15/IL-21 family."}
{"protein": "MPIGVPKVPFRSPGEEDAVWVDVYNRLYRERLLFLGQEVDSEISNQLIGLMVYLSIEDETKDLYLFINSPGGWVIPGVAIYDTMQFVPPDVHTICMGLAASMGSFILVGGEITKRLAFPHARVMIHQPASSFYEAQTGEFVLEAEELLKLRETLTRVYVQRTGNPLWVVSEDMERDVFMSATEAQAHGIVDLVAVENTGDLV", "text": "FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the peptidase S14 family."}
{"protein": "MMETQEKVLVLVGALFINTFNLNYKSIVLTHDSEQAYGFKDKWEAQKVAANVGGQVVIRTTSFKIV", "text": "SIMILARITY: Belongs to the phi29likevirus GP5.5 family."}
{"protein": "MPTLFISDLHLEIEKPDLTRFFFNFLDKVAPNAEALYILGDFFEVWVGDDEQSPLQVEVAQRLHKLAEAGTHIHLMHGNRDFLIGETYAKQCGATLLAEPHALDLYGVPSLLMHGDSLCTLDAAYQKARATFRNPAFQSQFLSRPLDQRQLTARQMRQISMAKNQGKAEVIMDVAPDEVINTFNTYGIELLIHGHTHRPDTHRYNLPQGEVKRIVLGDWGEETWYGRADADGFQLLNLKAEDIA", "text": "FUNCTION: Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the LpxH family."}
{"protein": "MVNLVIVSHSARLGEGVGELARQMLMNDGCKLAIAAGIDDPASPIGTDPIKVMEAIESVADADHILVMMDIGSALLSAETALDLLDPAIAAKVRLCAAPLVEGTLAATVSAAAGAGIDKVIEDAMNALEAKRVQLGLPSQPQHASLTAAPVDDRDARSVSVVIQNHNGLHVRPASKLVAALAGFNADLVLEKGGKCVTPDSLNQIALLQVRRNDTLRLLARGPDADAALAAFQALAAENFGEPTEAAPARRPASADRVEGKVVLYPQPQDRISRETSAAIGQQQLRLKRAIDRTLEDLSALTTLAEATFSADIAAIFSGHHTLLDDPDLYAAACDIIRDEQCSAAWAWQQVLSDLSQQYRHLDDAYLQARYIDIEDILHRTLRHLNERNEALPQFSAPSILVADDIFPSTVLQLNAEQVKGICLQAGSELSHGAIIARQAGIAMLCQQSDALTLQDGENVILDIPGKRVIRG", "text": "FUNCTION: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. SIMILARITY: Belongs to the PEP-utilizing enzyme family."}
{"protein": "MSNVRYISNLTRETYALILAGGRGSRLHELTDWRAKPALYFGGKFRIIDFPLSNCINSGIRRVGVVTQYKSHSLIRHVMRGWGHFKKELGESVEILPASQRYSENWYQGTADAVFQNIDIIRHELPKYVMVLSGDHVYRMDYAGLLAAHAESGADMTVSCLEVPVAEAAGAFGVMEVDDEMRILGFEEKPKHPKHSPGNPEKCLASMGNYVFNTEFLFDQLKKDAQNANSDRDFGKDIIPSIIEKHKVFAYPFKSAFPNEQAYWRDVGTLDSFWQANMELLSPTPALNLYDAKWPIWTYQEQLPPAKFVFDDDDRRGMAVDSIISGGCIISGATVRRSVLFNEVRVCSYSVVEDSVVLPDVVVLRHCKIKNAIIDRGCIIPEGTVIGYNHDHDRAKGFRVSEKGITLVTRDMLGLPVGYE", "text": "FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc. SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family."}
{"protein": "MEKDILIELKNVSKKYGENYVIKNLNLFVRRNEFLTFLGPSGCGKTTTLNMIAGFETPDEGNIIFEDSSINIVPPHKRQINTVFQKYALFSHMNVYENVAFGLRIKKLPEKQIREEVEKMLSLVDLKGFEKRSTDSLSGGQQQRVAIARALVNKPKLLLLDEPLGALDLKLRKEMQLELKNIQQKLGITFIFVTHDQEEALTMSDTIVVLNKGTVQQIGTPEDIYNEPKNKFVANFIGVSNILNGVMLHDYKVKFDDETFDCVDTGFNENEDVDVVVRPEDIKIVSKENGKLFGKVISAVFRGVHYEIKVEVKNTTWIIHNTKHVRVGDSIGLDILPDDIHIMRKEKIDEEA", "text": "FUNCTION: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Spermidine/putrescine importer (TC 3.A.1.11.1) family."}
{"protein": "MAAHSIFTTTSTTNSFLYPISSSSSSPNINSSFLGVSLNVNAKFGQSLTLYAVTTPKPLTVFAATKKAVAVLKGNSNVEGVVTLSQDDDGPTTVNVRITGLAPGLHGFHLHEYGDTTNGCMSTGAHFNPNKLTHGAPGDEIRHAGDLGNIVANADGVAEVTLVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSLTTGNAGGRLACGVVGLTPI", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MSGNREFYFRRLHSLLGVIPVGIFLIQHLVVNQFAARGAEAFNSAAHFMDSLPFRYALEIFIIFLPLIYHAVYGVYIAFTAKNNAGQYSYMRNWLFVLQRVTGIITLIFVSWHVWETRIAAQMGAEVNFDMMANILSSPAMLGFYIVGVLSTIFHFSNGLWSFAVTWGITVTPRSQRISTYVTLIIFVALSYVGLKAIFAFV", "text": "FUNCTION: Di-heme cytochrome of the succinate dehydrogenase complex. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b558 family."}
{"protein": "MDKERILTPAVVFSVALLHLAMVALLWQAHKLPVIESGNVIEFVDLGDFGGGDGAPEGAGAPAAPEPQPVPEPPKPVEPPKPVLKPVVTKKADADIQQPKEEPKPEEKPKPEEKPKPEPKPEAKPVPKPAEKPVEKPSEKPAEHPGNASAKADSEQGNGEDKGTGTKGDGTGRGEGSGKGSGGVKGEHGEGAGSSKGNPLRANGSIPRPAYPTLSMENDEQGTVVLSVLVSPGGHVESVKIVKSSGFSRLDNAARKAAQNGHFQANAWTEFKVPVKFELN", "text": "FUNCTION: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Required for heme utilization and virulence. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein; Periplasmic side. SIMILARITY: Belongs to the TonB family."}
{"protein": "MAAYLQWRRFVFFDKELVKEPLSNDGAAPGATPASGSAASKFLCLPPGITVCDSGRGSLVFGDMEGQIWFLPRSLQLTGFQAYKLRVTHLYQLKQHNILASVGEDEEGINPLVKIWNLEKRDGGNPLCTRIFPAIPGTEPTVVSCLTVHENLNFMAIGFTDGSVTLNKGDITRDRHSKTQILHKGNYPVTGLAFRQAGKTTHLFVVTTENVQSYIVSGKDYPRVELDTHGCGLRCSALSDPSQDLQFIVAGDECVYLYQPDERGPCFAFEGHKLIAHWFRGYLIIVSRDRKVSPKSEFTSRDSQSSDKQILNIYDLCNKFIAYSTVFEDVVDVLAEWGSLYVLTRDGRVHALQEKDTQTKLEMLFKKNLFEMAINLAKSQHLDSDGLAQIFMQYGDHLYSKGNHDGAVQQYIRTIGKLEPSYVIRKFLDAQRIHNLTAYLQTLHRQSLANADHTTLLLNCYTKLKDSSKLEEFIKKKSESEVHFDVETAIKVLRQAGYYSHALYLAENHAHHEWYLKIQLEDIKNYQEALRYIGKLPFEQAESNMKRYGKILMHHIPEQTTQLLKGLCTDYRPSLEGRSDREAPGCRANSEEFIPIFANNPRELKAFLEHMSEVQPDSPQGIYDTLLELRLQNWAHEKDPQVKEKLHAEAISLLKSGRFCDVFDKALVLCQMHDFQDGVLYLYEQGKLFQQIMHYHMQHEQYRQVISVCERHGEQDPSLWEQALSYFARKEEDCKEYVAAVLKHIENKNLMPPLLVVQTLAHNSTATLSVIRDYLVQKLQKQSQQIAQDELRVRRYREETTRIRQEIQELKASPKIFQKTKCSICNSALELPSVHFLCGHSFHQHCFESYSESDADCPTCLPENRKVMDMIRAQEQKRDLHDQFQHQLRCSNDSFSVIADYFGRGVFNKLTLLTDPPTARLTSSLEAGLQRDLLMHSRRGT", "text": "FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes (PubMed:21148287). Involved in the retrograde Shiga toxin transport (PubMed:23593995). SUBCELLULAR LOCATION: Endosome Late endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Early endosome Cytoplasmic vesicle Cytoplasmic vesicle, autophagosome Cytoplasmic vesicle, clathrin-coated vesicle. SIMILARITY: Belongs to the VPS11 family."}
{"protein": "MVSAMWDTSALKLRNIFEEEFGGYLEKRLRESIQLNRPTKRYLKLATRSDIDLKFHKVGKKESNGSSLVKYIIEFDTTAILVKGYIRPWNNPEWKCKAPYNSNQNVDTRSLYKEKIIVRDNVKDLFSAALTKLDLSVRLNKFDQNVHAKYRLNEDFLQPLGRTLRHSCEFPVMHSRLVQRESELYEEFLSYDLPKRQMTTMDIQFKTVKVQSFQQYKIQYIQTLTREKTSQEYTSSARLPHWQSNQIQNSSIKFLKLCCEDEDFHPLELYKLENPKADQFQRKAVYRSKPIKPKWRISDEIIKRLNWNPFKELNLPKNSELLESLRDVQVRCTSYALVFKRIPSSKIDLMVSKIPVSFRSVNAISYDQFDPKSKENVQESSQCIDSLANEETTDVDEVTNKRIMTSGKRSFINADLVSIIAAKRSKLKRLSISNGDVNPVATLNETVEQSTMSNVTFQLSDKSFHNAEEKVIIFNAEYIAKNYKLINFLHQNNFCVLEMDLGDHSDILLDASTCLILRNITSVYQKQVDSFPLLRAIQELKCKYKRVVIFLSYSERSLALDSNLAYKTQLLLNCLGGTTTHLVEETQLKLTATWISLYCGTNTPNEQQIYRMSLSKEVLQHFDINPIAIESILSLTSLEEFLSISYGKRALLYGKFLTEYQLAHIDDFVTMSWSE", "text": "FUNCTION: Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=localizes to a meiosis specific chromosomal structure called the synaptonemal complex (SC) formed during meiotic prophase. SIMILARITY: Belongs to the ZIP2 family."}
{"protein": "MAIKINEKGRGKFKPAPTYEKEEVRQLLMEKINEEMEAVATATSDISNDEIQYKSDKFNVLSLFCGAGGLDLGFELAGLEQSLGTDKALEAFKDRDVYNAIRHESVFHTVYANDIFSEALQTYEKNMPNHVFIHEKDIRKIKEFPSANLVIGGFPCPGFSEAGPRLVDDERNFLYIHFIRCLMQVQPEIFVAENVKGMMTLGGGEVFRQIVEDFGAAGYRVEARLLNARDYGVPQIRERVIIVGVRNDIDFNYEYPEITHGNEEGLKPYVTLEEAIGDLSLDPGPYFTGSYSTIFMSRNRKKKWTDQSFTIQASGRQAPIHPGGLPMEKVDKNKWIFPDGEENHRRLSVKEIKRIQTFPDWYEFSDGGNMKVSVNNRLDKQYKQIGNAVPVFLARAVAKSIAQFAADYLKDNHPHEAPQMKLFI", "text": "FUNCTION: A methylase, recognizes the double-stranded sequence 5'-GGCC- 3', methylates C-3 on both strands, and protects the DNA from cleavage by the BspRI endonuclease. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
{"protein": "MTGRDDISEAKSKGKILAPSVGNEKSGRLHGPAMRSKGFAITDLLGLEAELQPPSISLPNCEGPGVSLGGVSLTNGSLPLGLGFLCGFASQQPPGTTCLLPTHIPFLQPRPDHHYLHTSDKHKENISDDDSILGDKNDLKASSAQSKRKKRRHRTVFTAHQLDELEKSFNEAHYPDVYAREMLALKTELPEDRIQVWFQNRRAKWRKREKCWGRSSVMAEYGLYGAMVRHSIPLPESIINSAKNGLVGSCAPWLLGMHKKSVDITSKVDADDLVTERSRGESQVRDFTNPHSESHRSPRHHSHSMDISEERAIDLSSTAKQENQSSGRHNSIRDSQSDFTDSDH", "text": "FUNCTION: Involved in the differentiation of bipolar cells, the last neurons of the retina to form. Together with other retinal homeobox proteins, acts as an effector of a cellular clock which, depending on cell cycle progression, establishes the generation of distinct retinal neuronal cell types. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family."}
{"protein": "MTVYFIGAGPGDPDLITVKGQRLIRQCPVILYAGSLVPQALLEGHQAGQVVNTAELDLEQIVELLAQAHRRGLDVARVHSGDPSLYGAIGEQIRHLRELGIPYEIVPGVTATAACAALLGCELTLPEVSQTLILTRYAARTKMPEGESLGDLARHRATLAIHLGVAHLAKIVEELLPHYGADCPVAVIHRASWPDQEQVRGTLGDILPKVAARNFRRTALILVGEVLAAEGFADSSLYRAEHRHLYRPGE", "text": "FUNCTION: Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5. SIMILARITY: Belongs to the precorrin methyltransferase family."}
{"protein": "MDSSRTIGLYFDSALPSSNLLAFPIVLQDIGDGKKQIAPQYRIQRLDSWTDSKEDSVFITTYGFIFQVGNEEVTVGMISDNPKHELLSAAMLCLGSVPNVGDLVELARACLTMVVTCKKSATDTERMVFSVVQAPQVLQSCRVVANKYSSVNAVKHVKAPEKIPGSGTLEYKVNFVSLTVVPRKDVYKIPTAALKVSGSSLYNLALNVTIDVEVDPKSPLVKSLSKSDSGYYANLFLHIGLMSTVDKKGKKVTFDKLERKIRRLDLSVGLSDVLGPSVLVKARGARTRLLAPFFSSSGTACYPISNASPQVAKILWSQTARLRSVKVIIQAGTQRAVAVTADHEVTSTKIEKRHTIAKYNPFKK", "text": "FUNCTION: The M protein has a crucial role in virus assembly and interacts with the RNP complex as well as with the viral membrane. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the morbillivirus/respirovirus/rubulavirus M protein family."}
{"protein": "MEFPDIHAYNSTKYLEDGDTTILGDTIQFQFIYENIDNKEHISLPKIKIFKYFRDKISFETLDRIIKNDYINPSYFQLKDKKFCAHNRDFYHLSTGGYGIIFRMEKYVVKFVFEDGSKKYKPMEVTSEFTIPRFLYNNLKGDERKFIVCAIAMGINFKIDFLRTIYYNTMSLMSALFNIMEGEPLENKYSHRKVLRYFAKYKQSNDFVKLISQFYPYVVNSNINVINNFNYLINFFERSRRSNGYFNRGNIIIFPLAKCSAEKITPDNYAQYGFSSIVEYTKFMFLQIALLYIKIYELPCSNFVHLDLKPDNILIFDSKEPINIYVGDMHYVFKEPIRCTLNDFDFSQISEIIPNKKAVTAINKEQNWYYDFHFFSHVLFKVYPEISKDEDFTSLLNEFTICDKYICENFRLQVNKLPSISFLINIVSRDIFSKWIDGKSTSHQ", "text": "FUNCTION: Essential serine-protein kinase involved in the early stage of virion morphogenesis. SUBCELLULAR LOCATION: Host endoplasmic reticulum Host endoplasmic reticulum-Golgi intermediate compartment. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Poxviruses subfamily."}
{"protein": "MEINGVEIEDTFAEAFGIKVSRVLVTAATKKLAKIAATEATGYGTSVIGCPAEAGIDCYVPPEETPDGRPGYIIMICNPSKKSLDHELLERIGMGILTAPTTAVFDALDDEDEKLNIGFKLKFFGDGYEKELEIDGRKIHSIPIMSGDFLIESEFGIKDGVAGGNFFIMGDSQASALLAAQAAVDAIAAVEGTVTPFPGGVVASGSKVGSNKYKFLNASTNEKMCVTLKDEVEDTQIPENVNGVYEIVIDGVDEEAVREAMKEGIKAACTVPGIIKISAGNYGGNLGAYKIKLHDLF", "text": "FUNCTION: Catalyzes the reversible transfer of a formyl group from formylmethanofuran (formyl-MFR) to tetrahydromethanopterin (H(4)MPT) to produce 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) and methanofuran (MFR). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FTR family."}
{"protein": "MNVPNLLSLSRLILSPLILYFVLEENYLSSLVLVLFLALMDFLDGFFARKLNQSTRMGKILDPLADKVFTFFSLLSYTFFSKERLNPLIFFLLLGRDITLIIGGIFLIKRKFTPEPSIYGKFTTLFVSLSLLSVGILNVYDVNFLRILTNVLEIVSLILILVSWVDYTLKGFKMIFKE", "text": "FUNCTION: This protein catalyzes the committed step to the synthesis of the acidic phospholipids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family."}
{"protein": "ADDRNPLEECFRETDYEEFLEIARNGLSDTDNPKEGWYANLGPMRLNEFSQENENAWYFIKDPGVLDYPVKPSEVGKHDDIFAYEKRFDEIVGGMDKEVTVTYQTSEKFEPPLPPK", "text": "FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:28495622) (By similarity). Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His (PubMed:28495622, PubMed:30534149). Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation (By similarity). Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation (By similarity). These different effects are probably due to different experimental conditions (By similarity). In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL) (PubMed:28495622). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress (PubMed:30654040). It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets (PubMed:29222016). It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function (PubMed:29222016). In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes (PubMed:29222016). Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line) (PubMed:28495622). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
{"protein": "MIRVACVGITVMDRIYYVEGLPTESGKYVARNYTEVGGGPAATAAVAAARLGAQVDFIGRVGDDDTGNSLLAELESWGVNTRYTKRYNQAKSSQSAIMVDTKGERIIINYPSPDLLPDAEWLEEIDFSQWDVVLADVRWHDGAKKAFTLARQAGVMTVLDGDITPQDISELVALSDHAAFSEPGLARLTGVKEMASALKQAQTLTNGHVYVTQGSAGCDWLENGGRQHQPAFKVDVVDTTGAGDVFHGALAVALATSGDLAESVRFASGVAALKCTRPGGRAGIPDCDQTRSFLSLFV", "text": "FUNCTION: Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6- sulfo-D-fructose 1-phosphate (SFP). SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
{"protein": "MTELKNDRYLRALLRQPVDVTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELACEVTLQPLRRFPLDAAILFSDILTIPDAMGLGLYFETGEGPRFTSPIKSKADIDKLPIPDPEGELGYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGGSSKAFTVIKKMMYAEPMALHALLDKLAKSVTLYLNAQIKAGAQSVMIFDTWGGVLTGRDYQQFSLYYMHKIIDGLLRENEGRRVPVTLFTKGGGQWLEAMAATGCDALGLDWTTDIADARRRVGDTVALQGNMDPSMLYAQPARIEEEVASILAGFGQGEGHVFNLGHGIHQDVPPEHAGAFVEAVHRHSAQYHL", "text": "FUNCTION: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family."}
{"protein": "MLLHFSPAKPLISPPNLRRNSPTFLISPPRSLRIRAIDAAQIFDYETQLKSEYRKSSALKIAVLGFGNFGQFLSKTLIRHGHDLITHSRSDYSDAANSIGARFFDNPHDLCEQHPDVVLLCTSILSTESVLRSFPFQRLRRSTLFVDVLSVKEFPKALFIKYLPKEFDILCTHPMFGPESGKHSWSGLPFVYDKVRIGDAASRQERCEKFLRIFENEGCKMVEMSCEKHDYYAAGSQFVTHTMGRVLEKYGVESSPINTKGYETLLDLVENTSSDSFELFYGLFMYNPNALEQLERLDMAFESVKKELFGRLHQQYRKQMFGGEVQSPKKTEQKLLNDGGVVPMNDISSSSSSSSSSS", "text": "FUNCTION: Involved in the biosynthesis of tyrosine. Has a weak prephenate dehydrogenase activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family."}
{"protein": "MPNNLQHQEGSYSLRSSNDVSPADDWTQTNDPKEKKRIQNRVAQRTYRNRIRARLEELENKIRCHEKASKQDGNENEDRASEKAMAQDFLITDQALQSLTLPRRVSSAGLSQEPATPPDLLLPSFFHQQQVKIPSAADELNQPKPPSSPPAWAEGQLNVAPRAAQARSIAPTSTGMHQISPSYGPPVFLPTEDLSIDIISSRGLSSSWKTAADLTVQGTHPLPAFPSCSLANIESPSPASSQATDPMDMTFHTATEANTAILPGHRSSLDERLEYVLERAEQVGFDNFDSLVTAYYSETFHGSSRLASEQRLSRNRRLPRVIAEIFRAASHWSAWERGGMNQEVIKSAECLLISEGTAARNALEGSLSLLVDGGNGSGDASSVERLVQNEIPNLWALMTSLASGTHSPRQQDRSGTALAAIMLLYFSGSMPKEQLLRLLIICLPDPVSPQKNN", "text": "FUNCTION: Transcription factor that positively regulates the expression of the gene clusters that mediate the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:19101477). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MFTLKKSLLLLFFLGTISLSLCEQERSAEDEGEVIEEEVKRGFMDTAKNVAKNVAVTLLDKLKCKITGGC", "text": "FUNCTION: Has antimicrobial activity against Gram-negative bacterium E.coli ATCC 8739 (MIC=100 ug), against Gram positive bacteria S.aureus ATCC 6538 (MIC=25 ug), methicillin-resistant S.aureus ATCC 43300 (MIC=100 ug), B.subtilis ATCC 6633 (MIC=12.5 ug) and against fungus C.albicans ATCC 90028 (MIC=100 ug). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MAVNPDRTTPFLGVNDPKVAQTGDSMFEGYLEPEQAQDYFAEAEKISIVQQFAQKIPMGTTGQKIPHWTGDVSASWIGEGDMKPITKGNMTSQTIAPHKIATIFVASAETVRANPANYLGTMRTKVATAFAMAFDNAAINGTDSPFPTFLAQTTKEVSLVDPDGTGSNADLTVYDAVAVNALSLLVNAGKKWTHTLLDDITEPILNGAKDKSGRPLFIESTYTEENSPFRLGRIVARPTILSDHVASGTVVGYQGDFRQLVWGQVGGLSFDVTDQATLNLGTPQAPNFVSLWQHNLVAVRVEAEYAFHCNDKDAFVKLTNVDATEA", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the L5likevirus major capsid protein gp17 family."}
{"protein": "MIIKPKIRGFICTTTHPVGCEANVKEQIAYTKAQGPIKNAPKRVLVVGASSGYGLSSRIAAAFGGGAATIGVFFEKEGSEKKPGTAGFYNAAAFEKLAREEGLYAKSLNGDAFSNEAKQKTIDLIKEDLGQVDMVVYSLASPVRKLPETGELIRSALKPIGQTYTSTAVDTNKDIIIEASVEPATEQEIQDTVTVMGGEDWELWINALAEAGVLAEGCKTVAYSYIGTELTWPIYWDGALGKAKMDLDRAASALNDKLSATGGSANVAVLKSVVTQASSAIPVMPLYIAMVFKKMREEGVHEGCMEQIYRMFSQRLYKEDGSAAEVDEKNRLRLDDWELRDDIQEHCRNLWPQITTENLKELTDYVEYKEEFLKLFGFGIDGVDYEADVNPDVATDFIAI", "text": "FUNCTION: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). SIMILARITY: Belongs to the TER reductase family."}
{"protein": "MAGVACLGKTADADEWCDSGLGSLGPDAAAPGGPGLGAELGPELSWAPLVFGYVTEDGDTALHLAVIHQHEPFLDFLLGFSAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLACRVRAHTCACVLLQPRPSHPRDASDTYLTQSQDCTPDTSHAPAAVDSQPNPENEEEPRDEDWRLQLEAENYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKPEPTCGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPNPILARLLRAHGAPEPEDEDDKLSPCSSSGSDSDSDNRDEGDEYDDIVVHSGRSQNRQPPSPASKPLPDDPNPA", "text": "FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the NF-kappa-B inhibitor family."}
{"protein": "MAIHEWPEGERPREKLLALGASALSDAELLAIFLRVGVKGRSAVDLARDLLLAFGGLRPLLEADLARFCAEHGLGEAKYVQLQASLELSRRHLGSLLERGAALTSPTLVRRFLTSQLRHLPHEAFAALFLDTQHRVIRFETLSKGTLDSASVYPREVSRRALALNAGALIFAHNHPSGVAEPSDADRRITQRLSDALGLFDIRVLDHFVVGDGEVVSFAERGWL", "text": "SIMILARITY: Belongs to the UPF0758 family."}
{"protein": "MRIPEDVRKDIPLTQEVIYFDNTATSLTPKPVIEAMDEYYLRYRANVHRGVHRLSQMATQKYEESRKVVADFINAEFDEIAFTKNTSESLNLVALGLEHLFKKGDKIVTTPYEHHSNLLPWQRLAKKKGLKLEFIEGDDEGNLDLADAEKKIKGAKLVAVQHVSNALGVIHEVEELGKMVKEEGAIFVVDAAQSVGHMEVDVKKLKADFLAFSGHKGPMGPTGIGVLYINKEFFDVFEPPLIGGGTIEDVELCCYKLTEPPERFEAGTPNIGGAIGLAAGIKYIEKIGIDKIEKQERKLVKRTTEGLDELEIPWYGPRNLDKHAGVVSFNVPPLHPHDVASVLDEHKIMVRSGHHCALPVMKRLKINGTVRASFHVYNSLEEVETFLGVLEELVKSLRSSQ", "text": "SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily."}
{"protein": "MSSWNEAWDRGKQMVGEPLAKMTAAAASATGAAPPQQMQEEGNENPMQMHSNKVLQVMEQTWIGKCRKRWLLAILANMGFMISFGIRCNFGAAKTHMYKNYTDPYGKVHMHEFNWTIDELSVMESSYFYGYLVTQIPAGFLAAKFPPNKLFGFGIGVGAFLNILLPYGFKVKSDYLVAFIQITQGLVQGVCYPAMHGVWRYWAPPMERSKLATTAFTGSYAGAVLGLPLSAFLVSYVSWAAPFYLYGVCGVIWAILWFCVTFEKPAFHPTISQEEKIFIEDAIGHVSNTHPTIRSIPWKAIVTSKPVWAIIVANFARSWTFYLLLQNQLTYMKEALGMKIADSGLLAAIPHLVMGCVVLMGGQLADYLRSNKILSTTAVRKIFNCGGFGGEAAFMLIVAYTTSDTTAIMALIAAVGMSGFAISGFNVNHLDIAPRYAAILMGFSNGIGTLAGLTCPFVTEAFTAHSKHGWTSVFLLASLIHFTGVTFYAVYASGELQEWAEPKEEEEWSNKELVNKTGINGTGYGAAETTFTQLPAGVDSSYQAQAAPAPGTNPFASAWDEHGSSGVVENPHYQQW", "text": "FUNCTION: Required for glutamatergic synaptic transmission (PubMed:10818169, PubMed:14762140, PubMed:14981253, PubMed:15371514, PubMed:9526004, PubMed:9870947). In AWB and AWC sensory neurons, required for the detection of preferred food sources, probably via glutamatergic neurotransmission from sensory neurons (PubMed:25009271). Negatively regulates the turning step of male mating behavior (PubMed:17611271). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Synapse. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily."}
{"protein": "MGRGWGLLVGLLGVVWLLRSGQGEEQQQETAAQRCFCQVSGYLDDCTCDVETIDKFNNYRLFPRLQKLLESDYFRYYKVNLRKPCPFWNDINQCGRRDCAVKPCHSDEVPDGIKSASYKYSKEANLLEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDSFCEVDDIQSPDAEYVDLLLNPERYTGYKGPDAWRIWSVIYEENCFKPQTIQRPLASGQGKHKENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDNWLEKKWGHNVTEFQQRFDGVLTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKVQDVENKELLLEILHEVKSFPLHFDENSFFAGDKNEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFQLTRQEIVSLFNAFGRISTSVRELENFRHLLQNVH", "text": "FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side Golgi apparatus lumen Secreted Cell projection, dendrite Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (By similarity). In neurons, it localizes to dendrites (PubMed:12694393). SIMILARITY: Belongs to the EROs family."}
{"protein": "MLAKRIIPCLDVKEGRVVKGVNFIGLQDVGDPVEIAALYNDAGADEIVFLDITATHEGRKTIIDVVEKTASKVFIPLTVGGGISSVKDMYNLLRAGADKVSINSAAVRNPKLIEEGAQHFGSQCIVVAIDARKVAEGKWNVYVNGGRVDTGMDAIEWAKRVVMLGAGEILLTSMDADGTKNGYDLRLTEEISKSVSVPVIASGGCGHADHIIEVFQKTTVDAALAASIFHYGEVTIGDVKRKLRNANVEVRL", "text": "FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MNTVKTVRELRAAVARARGEGKRIGFVPTMGNLHSGHAALVTKAAQRADFVVASIFVNPLQFGANEDLDKYPRTLAADQERLLQAGCNLLFAPAVEEMYPDGMSVQTRVSVPQLSEGLCGASRPGHFEGVATVVSKLFNMVQPDLAVFGEKDFQQLAVIRAMVRDLNMPIQIIGEPTVRADDGLALSSRNGYLTPEQRTAAPALYRTLQHIAAGIGRGQRDFAALVAEGQAQLSAAGFRPDYLEVRHAVSLRPALIDDRDLVVIAAAYLGNTRLIDNLYLHLEEKTA", "text": "FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the pantothenate synthetase family."}
{"protein": "MSRAQALPDPAAVGYPSFKLILVGDGGTGKTTFVKRHITGEFEKRYEPTIGVEVRPLDFHTSRGKVRFCCWDTAGQEKFGGLRDGYYIHGHCAIIMFDVTSRLTYKNVPTWHKDICRVCDNIPIVLCGNKVDMKNRQVKAKMVTFHRKKNLQYYEISAKSNYNFEKPFLYLARKLTGDMNLRFVEELALLPADVTIDLIAQQKIETEIAAAAAMPLPDEDEDGLMD", "text": "FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. Ran family."}
{"protein": "MVEDILAPGLRVVFCGINPGLSSAGTGFPFAHPANRFWKVIYQAGFTDRQLKPQEAQHLLDYRCGVTKLVDRPTVQANEVSKQELHAGGRKLIEKIEDYQPQALAILGKQAYEQGFSQRGAQWGKQTLTIGSTQIWVLPNPSGLSRVSLEKLVEAYRELDQALVVRGL", "text": "FUNCTION: Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family."}
{"protein": "MAGRVGQMKNQDEVHQNQILRELFLKELRAQKLYTQYHVNPLRKVHTITRKPMSWHDNLEEPEDAKFLNLIHHAAQGPKKKYSETQTEAQEIGWDPNPLINPDRQDHRLNHFRVYHDITLYKAKLWSLGEDDHQK", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. SIMILARITY: Belongs to the CFAP144 family."}
{"protein": "MNKLALYCRAGFEKELAGEITDKAAQLGVFGFVNLTEQSGYVIFECYQANEADHLAREIKFEQLIFARQMIVVGELLEDLPTADRISPIIAQYKTLQPKHSSALFVETPDTNEAKALLTFCRKFTVPLRNSLKQEGWLTSSDNVKDSISLHILFIRPGCCYVGYAYNHNKSPFFMGIPRLKFPSDAPSRSTLKLEEAILTFIPINQEKKRFNEQMKGVDLGACPGGWTYQLVKRGLFVYAVDHGKIAATLHETGRIEHCVEDGFKFQPPKLKQMDWLVCDMVERPMRISQLIGKWLMNGWCRETIFNLKLPMKKRYHEVQLCLSLFRQLTKQGLCFKLQAKHLYHDREEITVHIVIMGKK", "text": "FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. RlmM subfamily."}
{"protein": "MNDFITETWLRANHTLSEGSEIHLPADARLTPSARELLESRRLRIKFLDPQGRLFVDDDEQQPQPVHGLTSSDTHPQACCELCRQPVVKKPDTLTHLTADKMVAKSDPRLGFRAALDSAIALTVWLQIELAEPWQPWLFDIRSRLGNIMRADAIDEPLAAQSIVGLNEDELHRLSHQPLRYLDHDHLVPEASHGRDAALLNLLRTKVRETETLAAQVFITRSFEVLRPDILQALNRLSSTVYVMMILSVAKHPLTVAQIQQRLGEKP", "text": "FUNCTION: Converts cyanocobalamin (CN-B12) to adenosylcobalamin (AdoCbl), the inducer of the eut operon (PubMed:15516577, PubMed:16636051, PubMed:24336938). Is not active on cobinamide nor other intermediates in the adenosylcobalamin synthetic pathway. Allows full induction of the eut operon (PubMed:15516577). Can use ADP, CTP and dATP in place of ATP, and cobinamide in place of cobalamin, none are as efficiently used as ATP and cobalamin (PubMed:16636051). FUNCTION: Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration- dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136). SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family. EutT subfamily."}
{"protein": "GVDKPGCRYMFGGCVQDDDCCPHLGCKRKGLYCAWDAS", "text": "FUNCTION: Paralytic toxin on insects that inhibits voltage-gated sodium (Nav) and calcium (Cav) channels in P.americana (American cockroach) dorsal unpaired median (DUM) neurons, and also inhibits the B.germanica (German cockroach) Nav channel (BgNaV1) (PubMed:28475112). May act as a gating-modifier toxin on Nav and as a pore blocker on Cav (PubMed:28475112). In vivo, reversibly paralyzes both L.cuprina (Australian sheep blowfly) and M.domestica (housefly), but does not affect larvae of H.armigera (cotton bollworms) (PubMed:28475112). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 28 (Jztx-11) subfamily."}
{"protein": "MIRITSRSVKGAAGIRSVSSSTVRLNIAPKVVSPPVPPPVKPQGSEIPPPPPPPPPPPKAKRFSLFGFLFKTTLLATVVYGGTLYAATKNDKVMDFVIDKQLPFHEELIDLIENGSTEDLQEAWEQLKNKFTDVKLPTKDDIDELTQKLEHRGEDIIKETKKKIASTHIGHKSGTDLTPTEQLQRGVEIESVKKDVAHLPLIELNSDLGKSVDETVKQTITSFNNFIQSIDASSLATKDDKLITSINTSVNQLASRLNSLTKDFDNELQNKLKVSQTELFSSFTKKELELTENLLHQFSTEKQQLEAKLNQKLSQEIQAARAAISQAASNAVAMVRIEQTKNFEKLVSEKLNEERNGRLANLEKLNDRIVELEKFAEGFETQIVSNHKKAIIHQAVSKLKSLLLAPAAGDKPQPIKPYIDELTKIATDDEVLALAIKDLSPLITNESTHSILTNAQLLSRWEQLAPELRSASLLPPNAGLLGHLASIVFSKLLLPVKGVKEDGKDIESVIGRVESSLARGELDIAVEEAANLKGWSRKLANDWVVEGRKRLEIEFLLGLIESESKII", "text": "FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MICOS complex subunit Mic60 family."}
{"protein": "MLGVALLSGAVHAAVQPLDRVVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGVPPTSALEQQVLERLIVENLQLQIGERSGIRITDEELNQAIGTIAQRNGMSLDQFRAALARDGLSFDDAREQVKREMIISRVRQRRVAERIQVSEQEVKNFLASDLGKMQMSEEYRLANILIPTPEAANSDDIQKAARKVGDVYQQLRQGADFGQMAIANSASENALEGGEMGWRKAGQLPPDFAKMLSSMPVGEITQPIRIPNGFIILKLEEKRGGSENVLRDEVHVRHILIKPSEIRSEAATEQLAERLYDRIKNGEDFGELAKSFSEDPGSALNGGDLNWVDPNSLVPEFREQMANAQQGVVTKPFKTQYGWHVLEVLGRRATDSTEQAREQQALSVLRNRKYDEELQTWLRQIRDEAYVEIKLPGADQAAQ", "text": "FUNCTION: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. SUBCELLULAR LOCATION: Periplasm Note=Is capable of associating with the outer membrane."}
{"protein": "MKETLSGVVTRVTGASYIVETGDGLKVRCRTVPGTVSENEGSNLVAVGDRVEFRPKASETDMAEGVITRVEERRTALVRRREVRRNRSKEKEQVIVANIDQLVLITSFDDPPFNSRLVDRYLVFAESEKLPLLIVVNKIDLDEEGMVEEDLEVYRQLDCNICLVSAEDGRGIEELRELLRDRVSAFSGHSGVGKSTLINLLVGCEELRTAETSGKTGKGVHTTTSSAMFQLPGGGYVIDTPGIREFNLAGITRENLRFYYTEFLRYMPECTFSSCSHTVEPGCAVIAAVESGSIARERYESYLALLDSLAE", "text": "FUNCTION: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily."}
{"protein": "MLGVQKKRSTRKTAARKTVVRKPAAKKTAAKKASVRKVAAKKTVARKTVAKKAVAARKPAAKKTAAKKAPVRKVAAKKTVARKTVAKKAVAARKTVAKKSVAARKTAAKKAPVRKVAAKKTVARKTVAKKAVAARKPAAKRTVSTKKTAVAAKAGVCMKKHKHTAACGRVAASGVKVCASSAKRRTHHNRSRTAHSWRQQLMKLVAK", "text": "FUNCTION: Might have a role in establishing the nucleoid structure of elementary bodies. SIMILARITY: Belongs to the histone H1/H5 family. HCT subfamily."}
{"protein": "MPSISMMSDAITPETLKKEKKMKSETLDSDDTVVKKEKSSSKKKEKSSSSGKKDKEEKEKKKKRKAVDLDDSSDKSDNSSELVQADDLKPKKAKVMEEAVVEAEDPNSLSNFRISKPLKDVLISKGIKALFPIQAMTFDNVIDGCDLVGRARTGQGKTLAFVLPIVESLVNGRTKDLRRSGHGRLPSVLVLLPTRELATQVLADFQVYGGAVGLTACSVYGGAPFHSQISSLTRGVDIVVGTPGRVKDLLEKGVLKLGSLLFRVLDEADEMLKMGFVDDVELILGKVDHVSKVQTLLFSATLPSWVKQISTRFLKSAKKTVDLVSDQKMKASISVRHIVIPCSASARPDLIPDIIRCYGSGGRSIIFTETKESASQLAGLLTGARPLHGDIQQTQREVTLKGFRTGKFMTLVATNVAARGLDINDVQLIIQCEPPRDVEDYIHRSGRTGRAGNTGVAVMLYDPKRSSVTKIERESGVKFEHLSAPQPVDVAKAVGIEAAAAILQISDSVIPAFKDAAEELLSTSGLSAVDILSKALAKAAGYSDIKERSLLTGMEGYVTLLLDAGRPFYGQSFAYTVLKRFLPATKADSIMGVALTADKSGAVFDVPVDDLETFLVGAENAAGVNLDVVKALPPLEEKVQISRRFGGGGRGGRGGGYGGRGGGYGGGGYGGGGGYGGRGGGYGRR", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily."}
{"protein": "MNAGILGVGKYVPEKIVTNFDLEKIMDTSDEWIRTRTGIEERRIARDDEYTHDLAYEAAKVAIKNAGLTPDDIDLFIVATVTQEATFPSVANIIQDRLGAKNAAGMDVEAACAGFTFGVVTAAQFIKTGAYKNIVVVGADKLSKITNWDDRTTAVLFGDGAGAVVMGPVSDDHGLLSFDLGSDGSGGKYLNLDENKKIYMNGREVFRFAVRQMGEASLRVLERAGLEKEDLDLLIPHQANIRIMEASRERLNLPEEKLMKTVHKYGNTSSSSIALALVDAVEEGRIKDNDNVLLVGFGGGLTWGALIIRWGK", "text": "FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities (PubMed:19863661). Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature (PubMed:19863661). Shows weak activity with acetyl-CoA (PubMed:19863661). FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. FabH family."}
{"protein": "MPAASLTSVRSFVAAPVPTRPAISVEGRRAFAFKGVEKRFGDKIVLDGIDLDVPAGQFVAVIGKSGCGKSTLLRLLAGLDRPTSGSLTLGAEEEGHSRTRFMFQEPRLLPWASVVKNVEIGLTGIAAGQDARQRALDILGEVGLADRADEWPSVLSGGQKQRVALARALVGHPQILALDEPLGALDALTRIEMQQLLERIWLAQKFTAVLVTHDVAEAVTLADRVVVISAGRIALDLEVPVARPRRRGSAELARLEGTILDRLFG", "text": "FUNCTION: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Aliphatic sulfonates importer (TC 3.A.1.17.2) family."}
{"protein": "MKHGIRVLGIDDGPFIKNSDKRTVITGVILKSNLYIEGISIKYIDVDGSDAEDVIISMIKGRFKNEISAVMTDGITFGGFNIVDIKNINEATGVPVISITRREPNIQRIISAVSRYFPEKVDRALKALSNGPVRLDNIYINSAGISLTEAGILIRRFTFMGRLPEPVRLAHIISTAIIRGESHGRA", "text": "SIMILARITY: Belongs to the UPF0215 family."}
{"protein": "MANAPHGGVLKDLLVRDAALHDSLLQEARSLNDIFLTERQLCDLELILNGGFSPLEGFMNERDYTSVVETLRLAPYNGQKHGDVFPIPITLDVSQEDINTLGLKQGGRVALRDPRDDAALAILTVSDIYRPNKAIEAEKVMGADDIAHPSVAYLRNNVKEFYVGGKVQAIQAPTHFDYVPLRFTPAELRAHFHKLAWRKVVAFQTRNPMHRAHRELTVRAARQRRANVLIHPVVGLTKPGDVDHYTRVRAYQALMPSYPEGMAHLALLPLAMRMAGPREAVWHAVIRKNFGATHFIVGRDHAGPGKNSQGQDFYGPYDAQELVTQFKDELQIEMVPFQAMTYLPGSDEYQPVDEVPKGTPTADISGTELRKRLRTGASIPDWFSYTGVVKVLRESYPPRPQQGFTILLTGLHNSGKDTIARALQVTLQQQGSRSVSLLLGEELRSDLDPQIGRAITPEQKHINLERIGFVAGELTKAGAAVIAAPTAPYERSRQAFKKQVVGSGGGNYFLVHVATPLEWCEKVDRRGLYKAARAGEIKNLTGVDDVYEAPEDADLVCDLRNDTVPEIVHSIIMILESQNLV", "text": "FUNCTION: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the sulfate adenylyltransferase family. SIMILARITY: In the C-terminal section; belongs to the APS kinase family."}
{"protein": "MSSDKVKNGNEPEESEESCGDESASYTTNSTTSRSKSPSSSTRSKRRGRRSTKSKPKSRAAYKYDTHVKENHGANIFGVAFNTLLGKDEPQVFATAGSNRVTVYECPRQGGMQLLHCYADPDPDEVFYTCAWSYDLKTSSPLLAAAGYRGVIRVIDVEQNEAVGNYIGHGQAINELKFHPHKLQLLLSGSKDHAIRLWNIQSHVCIAILGGVEGHRDEVLSIDFNMRGDRIVSSGMDHSLKLWCLNTPEFHHKIELSNTFSQEKSTLPFPTVTKHFPDFSTRDIHRNYVDCVQWFGNFVLSKSCENAIVCWKPGQLHQSFEQVKPSDSSCTIIAEFEYDECEIWFVRFGFNPWQKVIALGNQQGKVYVWELDPSDPEGAHMTTLHNSRSVATVRQIAFSRDASVLVYVCDDATVWRWNRRQTTSI", "text": "FUNCTION: Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat ESC family."}
{"protein": "MGAGVLALGASEPCNLSSAAPVPDGAATAARLLVPASPPASLLTSASEGPPLPSQQWTAGMGLLMAFIVLLIVVGNVLVLVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARALVCTVWAISALVSFLPIFMQWWGDKDAKASRCYNDPECCDFIINEGYAITSSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLSGPARLPSPAPSPGPPLPAATVANGRANKRRPPRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRDLVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAACGSHAAAGDPPRALGCLAVARPSPSPGAASDDDDDDDEDDVGAAPPVRLLEPWAGYNGGAAANSDSSPDEPSRAGCASESKV", "text": "FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling (By similarity). Involved in the regulation of sleep/wake behaviors (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome Note=Colocalizes with RAPGEF2 at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily."}
{"protein": "MTGKTQTSNVTNKNDPKSINSRVFIGNLNTAIVKKVDIEAIFSKYGKIVGCSVHKGYAFVQYMSERHARAAVAGENARIIAGQPLDINMAGEPKPYRPKPGNKRPISALYRLESKEPFLSVGGYVFDYDYYRDDFYNRLFDYHGRVPPPPRAVIPLKRPRAAVTTTRRGKGVFSMKGGSRSAVSGSSSSGSKLKSDELQTIKKELTQIKTKIDSLLGRLEKIEKQQKAEAEAQKKQLEASLELIQDECVSENADHSAEEPAEGAPDADGEELTDGVEEDFDEDGAHELFLQIK", "text": "SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily."}
{"protein": "MTEVEPKSVLYCGVCSFPPEFCEFGGSFKRCKEWLEQNDKELYEKLYSEDALANATSTLSIDKEQKIAKELEKKQAKEEAKQERELKKQLASKVTIKRIERNKRKHVIAISGLEVFDIDMKKLSKTFASKFATGASVTKNAEKKDEIIVQGDVSDEARAYIEKLLEEKGLNEVKVEQIDDKKKKKAAEAAEAAAAATGNKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DENR family."}
{"protein": "MLKREGKVQPYTKTLDGGWGWMIVIHFFLVNVFVMGMTKTFAIFFVVFQEEFEGTSEQIGWIGSIMSSLRFCAGPLVAIICDILGEKTTSILGAFVVTGGYLISSWATSIPFLCVTMGLLPGLGSAFLYQVAAVVTTKYFKKRLALSTAIARSGMGLTFLLAPFTKFLIDLYDWTGALILFGAIALNLVPSSMLLRPIHIKSENNSGIKDKGSSLSAHGPEAHATETHCHETEESTIKDSTTQKAGLPSKNLTVSQNQSEEFYNGPNRNRLLLKSDEESDKVISWSCKQLFDISLFRNPFFYIFTWSFLLSQLAYFIPTFHLVARAKTLGIDIMDASYLVSVAGILETVSQIISGWVADQNWIKKYHYHKSYLILCGITNLLAPLATTFPLLMTYTICFAIFAGGYLALILPVLVDLCRNSTVNRFLGLASFFAGMAVLSGPPIAGWLYDYTQTYNGSFYFSGICYLLSSVSFFFVPLAERWKNSLT", "text": "FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
{"protein": "MTAVADAPQADIEGVASPQAVVVGVMAGEGVQIGVLLDANAPVSVMTDPLLKVVNSRLRELGEAPLEATGRGRWALCLVDGAPLRATQSLTEQDVYDGDRLWIRFIADTERRSQVIEHISTAVASDLSKRFARIDPIVAVQVGASMVATGVVLATGVLGWWRWHHNTWLTTIYTAVIGVLVLAVAMLLLMRAKTDADRRVADIMLMSAIMPVTVAAAAAPPGPVGSPQAVLGFGVLTVAAALALRFTGRRLGIYTTIVIIGALTMLAALARMVAATSAVTLLSSLLLICVVAYHAAPALSRRLAGIRLPVFPSATSRWVFEARPDLPTTVVVSGGSAPVLEGPSSVRDVLLQAERARSFLSGLLTGLGVMVVVCMTSLCDPHTGQRWLPLILAGFTSGFLLLRGRSYVDRWQSITLAGTAVIIAAAVCVRYALELSSPLAVSIVAAILVLLPAAGMAAAAHVPHTIYSPLFRKFVEWIEYLCLMPIFPLALWLMNVYAAIRYR", "text": "FUNCTION: Part of the ESX-5 specialized secretion system, which is responsible for the secretion of EsxN and a number of PE_PGRS and PPE proteins, including PPE41. FUNCTION: Part of the ESX-5 specialized secretion system, which is responsible for the secretion of EsxN and a number of PE_PGRS and PPE proteins, including PPE41. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EccD/Snm4 family."}
{"protein": "MDPALSAVRLTVQEAIHILSSSEDAGHILSTLGTLKRYLGGTEDPVLPEEKEEFATVHFSAVLRCLVSKLSPGWLELSPGGQLERLWESFFLDGPPDQAFLVLMEAIESTAGPSFRLMKMAQLLDTFLSTGRVAALMEEQCRPQTKPSFPLFQETLLSKVVGLPDLLGNCLQRDNLTQFFPQNYFPLLGQEVVQALKAVVNFLQDGLDCSVSFVSRVLGKVCIQGRKREILSVLVPQLTVLTQDSCLWQRVCWRLVEQVPDRAVEAVLTGLVEAAPRPEVLSRLLGNLVVKNKKARFVVTRKLLLLQYQHTTPMVQSLLGYLALDSQRRPLLIQVLKELLETWGCSSAVRHTPLEQQCYISKAILVCLAHLGEPELQDIRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVISSRIHPEGPLLKFQYEDDEMSRELLALATPEPAGDCSSVSRGPSPAPVDTESPVEMPEKAVESDVPPTQPQGSDSELDSDDEFIPYDMSGDRELKSSKEPLYIRDCVEALTTSEDMERWEASLKGLEGLVYRSPTATREVSVELAKVLLHLEEKTCVAEFEQLRQSALVAVTVTDPEQVAKYLTSQFYGLNYSLRQRMDILDVLVLAAQALSRPKSLQRRSQHGPPVPGTMCSPALAVSQTGNVAAPDWQVVVEERIRSKTRRFSKGCPQRELSGVPNEFSSVAGYFFFPLLQHFDRPLVTFDLLGDDQLVLGRLTHTLASLMYLAVNTTVAVPMGKALLEFVWALRFHVDIYVRRGLLSAVSSVLLSVPTERLLGDLPDELLEARSWLADVAEKDVDEDCRELAVRALLLLERLKDKLLSSSSPQP", "text": "FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane Nucleus Chromosome, telomere. SIMILARITY: Belongs to the TEL2 family."}
{"protein": "MPAKTPELEMMDEDRLIEEVLDKFVNCHEQTYEEFLRTFTHLSKDNVTKREAFGTNSSENNFTSIKFTQRNEPNDCRLSNKAIFLHTSSQCSEEEQIMIGDGQKAGSSFQGDLNRAGKVKVDNFLDIEDLDLDEEINPQLSKDVLLLPGQVEQEVSLSVPSYIPSVAIQPVTPGTKPRPTVKAADKQSKEIVGDEVQPFSLDEEFDYDAVVLTPKFTPAEMNAIKELSKQKTKSADLEDPHD", "text": "FUNCTION: Seems to play a role in ciliary BBSome localization, maybe through interaction with IFT-A complex."}
{"protein": "VCRDWFKETACRHAKSLGNCRTSQKYRANCAKTCELC", "text": "FUNCTION: Inhibits voltage-dependent potassium channels of the Kv1 family (Kv1.1/KCNA1 (Kd=6 nM), Kv1.2/KCNA2 (Kd=15 nM), Kv1.3/KCNA3 (Kd=10-39 nM), Kv1.6/KCNA6, and KCa3.1/KCNN4 (Kd=172 nM)). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin family. Type 1b subfamily."}
{"protein": "MESQQLSQHSPISHGSACASVTSKEVQTTQDPLDISASKTEECEKVFTQANSQQPTTPPSAAVPENHHHASPQAAQVPLPQNGPYPQQRMMTPQQANISGWPVYGHPSLMPYPPYQMSPMYAPPGAQSQFTQYPQYVGTHLNTPSPESGNSFPDSSSAKSNMTSTNQHVRPPPILTSPNDFLNWVKIYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFALSQFLPTWVKDILSVDYTDIMKILSKSINKMQSDTQEVNDITTLANLHYNGSTPADAFEAEVTNILDRLKNNGIPINNKVACQFIMRGLSGEYKFLRYARHRYIHMTVADLFSDIHSMYEEQQESKRNKSTYRRSPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTSNNFPGPDNDLIRGSTTEPIQLKNKHDLHLRPGTY", "text": "FUNCTION: Capsid protein (CA) is the structural component of the virus- like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid- like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MEFPDLGKHCSEPTCKQLDFLPITCDACKQDFCKDHFSYVGHKCPFAFKKDVQVPVCPLCNAPIPVKRGEIPDVVVGEHMDRDCTFHPGRNRNKVFTHRCSKEGCRKKEMLQLACAQCHGNFCIQHRHPLDHNCQAGSSSASRGRTSTSRAAEQKPSGVSWLAQRLRRTVK", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MKLHQGLVCLSVLILLPTCILGDRKFEVYWNIPTFMCPDQNKTIMDLNKKHGVIQNTEDLFRGDKISLLYHPGAFPAITRNKTTNTLIYENGGVPQAGNLSLHLKLLEKDINEQITDKNFSGLAVIDFELWRPIFRQNGGSLSDYQNLSLKLEKDLHPEFNEDQLRKEAERRIEKFGRSFIKQTLIKAKKLRPKAQWGYYAFPYCFNGRRRYVDTCIPSAKIDNDRILYMFENSDVIYPAVYLQTDLAQKNQTGLVKGRVDEAVRMAKMVKKPAKPPVLVYHRYVFTDTLEYISKENTTAVFKAMKDNGADGVIIWGSSFDLNSKEKCAKFLDYLREVLWPVIDEVKRS", "text": "FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 56 family."}
{"protein": "SETAAEKFERQHMDSYSSSSSNSNYCNQMMKRREMTDGWCKPVNTFIHESLEDVQAVCSQKSVTCKNGQTNCHQSSTTMHITDCRETGSSKYPNCAYKASNLKKHIIIACEGNPYVPVHFDASV", "text": "FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double- stranded RNA (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pancreatic ribonuclease family."}
{"protein": "MNPQFRNMVDGMDPHKFSYNFKNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYFELKNHPEMRFFHWFSKWRKLHRDQECEVTWYMSWSPCTKCTRNVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQERDGPRANMKIMNYDEFQHCWNKFVYSQRELFEPWNNLPKYYIVLHIILGEILRHSMDPLTFTSNFNNEPCVEGRHETYLCYKVERLHNDTWVLLNQRRGFLCNQAPAIHGFPEGRHAELCFLDVIPFWKLDGKQRYRVTCFTSWSPCFRCAQEMAKFISNNQHVSLCIFAARIYDDQGRCKEGLRTLDEAEAKISIMTYDEFQHCWDTFVDHQGRPFLPWIRLHEHSEALSGRLRAILLNQGN", "text": "FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, P-body Note=Mainly cytoplasmic, small amount are found in the nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MYVVSTKQMLNNAQRGGYAVPAFNIHNLETMQVVVETAASMHAPVIIAGTPGTFTHVGTENLMALVSAMAKQYHHPLAIHLDHHTKFDDIAQKVRSGVRSVMIDASHLPFAQNISRVKEVVDFCHRFDVSVEAELGQLGGQEDDVQVNEADAFYTNPVQAREFAEATGIDSLAVAIGTAHGMYARAPALDFSRLENIRQWVNLPLVLHGASGLSTKDIQQTIKLGICKINVATELKNAFSQALKNYLTEHPEATDPRDYLQSAKSAMRDVVSKVIADCGCEGRA", "text": "FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol. SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase family. TagBP aldolase GatY subfamily."}
{"protein": "MRPVIKVGLSTASVYPLRAEAAFEYAAKLGYDGVELMVWGESVSQDIDAVKGLSRRYRVPVLSVHAPCLLISQRVWGANPVPKLERSVRAAEQLGAQTVVVHPPFRWQRRYAEGFSDQVAELEAASDVMIAVENMFPFRADRFFGADQSRERMRKRGGGPGPAISVFAPSFDPLAGNHAHYTLDLSHTATAGSDSLEMVRRMGSGLVHLHLCDGSGLPADEHLVPGRGTQPTAAVCQLLAGADFAGHVVLEVSTSSVRSATERETMLTESLQFARTYLLR", "text": "SIMILARITY: To M.tuberculosis Rv0498 and S.coelicolor SCO3347."}
{"protein": "MAKAKEVKAKPIKGEEAEKLVYEYLRKTNRPYSATDVSANLKNVVSKQVAQKALEQLRDTGLIHGKLYGKQSVFVCLQDDLAAATPEELAEMEKQIQELKDEVSVVKTLYKEKCIELQALNNSLSPAEIREKIQSIDKEIEETSSKLESLRNGTVKQISKEAMQKTDKNYDFAKKGFSNRKKMFYDLWHLITDSLENPKQLWEKLGFETEGPIDLN", "text": "FUNCTION: Required for proper homologous pairing and efficient cross- over and intragenic recombination during meiosis. Acts indirectly in a process facilitating homologous recombination. Acts during mid- to late-horse-tail period. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HOP2 family."}
{"protein": "MALSYKEKLIECIDNELQNGGTLLLLTNNNVVSEISYYGNGYKYFTFNTNHDLISQEELKGATSNNIARMIYNWIMKNPQNNKIWNGEPQTRIYFENNVYHTNYNHECIKDFWEVSTKVGPCIFNDRSIWCTKCTTFYPFSNILSPNMLE", "text": "FUNCTION: May participate in a redox cascade for the formation of disulfide bonds in viral proteins. SIMILARITY: Belongs to the asfivirus A151R family."}
{"protein": "MDCKYLLELLDSYSFIRSSRSFSSPIIIHGVAGCGKSTIIQKIALAFPELLIGSFTPALLDSNSGRKQLAVTSDPLDILDEYLGGPNPVVRLAKFCDPLQYSCEQPEVPHFTSLLTWRFCVRTTALLNGIFGCQIKSRREDLCHLTHENPYTTDPKGVVVAHEQEVINLLLQHGCPVTPTQHLWGLTIPVVSVYITSIASLSTVDRANLFLSLTRDSKALHIFEFDAWSHATC", "text": "FUNCTION: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Increases plasmodesma size exclusion limit. Acts as a suppressor of RNA-mediated gene silencing, also known as post- transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (By similarity). SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the Tymovirales TGBp1 protein family."}
{"protein": "MSERVSEEPGLDKGDGAEECELDDPELKAIRMRVREMEEEAERLKGLSGQDKSIGVSPRPCMKLIHSKMTAGEYTEGPPRPLSAEEKKEIDKRSVYVGNVDYGGTAQDLEAHFSSCGSINRITILCDKFSGHPKGYAYIEFAERNSVDAAVTMDETVFRGRTIKVLPKRTNMPGISSTDRGGFRGRPRGNRGNYQRGQRPRGRPFRGCGRPGPLNHPY", "text": "FUNCTION: Binds the poly(A) tail of mRNA. Unable to interact with the cap-binding complex and is therefore unlikely to be involved in translation initiation. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSRWLMQMLMLPLLLLPLGQAAPKDGVARLDPEAQQQLTTNPFQPGPEQLRRLRDYLKGLEKMEEDPEQMNREQVLLYLFALHDFDQNGQLDGLELLSMLTAALAPGAAHFPINPVILVVDMVLETQDLDGDGLMTPAELINFPGEAPKRAESLPPALQEPQPAGSQPLLANSPLQSETQQSLGTKEEITSQVEAKRALEPEQEAGHHIETKVDALSPEGEARGQAESEGDAPGPREDAERQVESKDNEGEAKDLPAETLETQNTPNVVEAHSIQLENDEI", "text": "FUNCTION: Mediates cell-cell adhesion in a calcium-dependent manner. Able to inhibit growth in several cell lines. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKIIFNLLILFSLVNFINSQSTTQATTLKLEGTIYDQYPYYDNNFEPIAGSLTTRLVQNAINTTTRTPTLNTLLPFTTTNVMGRMVTPSLFQYFYQPNKNAPLTNNSGANFPIPMTVNLTLNPSTGTYVYDNQFFFPIDYQGFDTNPFYRNYTDGTDYHNFHFCLKINTRFTYTGNEVFYFVGDDDVWVFINDQLVIDLGGLHEAAGKNIDLTTLGLTKNKDYTFDFFYCERHTTKSTIRIETSIQAYCPFYDYCGVCYGDGSTCCDPVVNCNDGDLCTIDSCPPRDTIIPAGFSISDLCQHAPVSCPSIDMCTNNTCDSKSGQCTPTSIKCDDKSSQCLTLKPCDPSSGCLYTSSCTSAHNPCNTGACSNGQCQTKSNSTCAAELGNDPCKVYYCDINSGCVSQPLCKQGPDSCEQNVCNAGVCTIKKLDPSVCSCGCVLNKCQKNNCVTASNGTSVCSPLPLDEIDDGNPCTDDHCDETTGLITHNITTKCTGCMKCNTTTGSCSPTNNECQDGNECTDNICVAAATNINQGECSNKTVSCPTTDKCLVYTCDTNKGCVSKPVVCPNSGNCQVGVCDSVKGCTLVPRVCNSTAFCLVSQCDEAIGCITFEKRCSPDNSKCQSGVCVNATATEPGKCKSVDYDPKPFICQTGAIVSTAVVASVVVVGAVVLGAAIFAGKKGYDHWKANQGQVFASSNANPLYQQSNNGGENALFEAPQ", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the prespore-cell-inducing factor family."}
{"protein": "KCNTATCATQRLANFLVHSNNNLGPVLSPTNVGSNTY", "text": "FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calcitonin family."}
{"protein": "FDAFTTGF", "text": "FUNCTION: Myotropic peptide, enhances both the frequency and amplitude of spontaneous hindgut contractions. It is synthesized by abdominal ganglionic neurons. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MASLQLLRGPFLCVLLWAFCVPGARAQEHGAGVHHGSVGLDKSTVHDQEHIMEHLEGVINQPEAEMSPQELQLHYFKMHDYDGNSLLDGLELSTAITHVHKEEGSEQVPPMSEDELISIIDGVLRDDDKNNDGYIDYAEFAKSLQ", "text": "FUNCTION: The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment Endoplasmic reticulum Golgi apparatus."}
{"protein": "MASQGTKRSYEQMETGGERQNTTEIRASVGRMIGGIGRFYIQMCTELKLSDYEGRLIQNSITIERMVLSAFDERRNKYLEEHPSAGKDPKRTGGPIYRRIDGKWIRELILYDKEEISRIWRQANNGEDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGLAVASGHDFEREGYSLVGIDPFRLLQNSQVFSLIRPNENPAHKSQLVWMACHSAAFEDLRVSSFIRGKRVVPRGQLSTRGVQIASNENMETMDSSTLELRSRYWAIRTRSGGNTNQQRASAGQISVQPTFSVQRNLPFERATVMAAFTGNTEGRTSDMRTEIIRIMESARPEDVSFQGRGVFELSDEKATSPIVPSFDMSNEGSYFFGDNAEEYDN", "text": "FUNCTION: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the influenza viruses nucleoprotein family."}
{"protein": "MFVFILLSLAAVLQQSFGNVDFNSESPRIKAKQREIVDKHNAFRRSVRPTASNMLRMEWYSEAASNAERWAYRCVLDHSPETSRILNGIQCGENIYMSSIPRTWIDIIKLWHDEYKNFIYGVGANPPGSIIGHYTQIVWYKSYRIGCAASYCPSSSYDYFYVCQYCPTGNFGGLTATPYKSGPTCGDCPSACDNGLCTNPCSREDVFTNCKSLVAKSNCQDDYIRKNCLATCFCPNK", "text": "FUNCTION: Weakly blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffeine- stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MKVEEREYIKKYWVGLMDGVGSIEVNHYRMKNLQYRLVLNVNDSSENMAMLLKIQQVIGGYLIKRKEKALIAWTINNKMQIEDVIKIFEDYNLVTVRKRNQLQFLKENLKRNDVNWYLSERKNKYKKSLIVSNIEEISYFNEWFSGFVEATGSFCIRAQKEKYFRIAHRYDMPLLLNLIIKFNITTKLREQKNEQYAIEIYKKTLLEVLITHFEKYPLLGDKKNSLETFKTR", "text": "FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the LAGLIDADG endonuclease family."}
{"protein": "MLENIRIVLIETSHSGNIGSAARAMKTMGLTQLCLVSPKSVDEQSYALSAGAENIVKNARVVDSFDEAVDDCSLVIGTSARLRHLQNTLIEPRECAEKVVAYKGKIAIVFGRERIGLTNEELLKCHYHLNIPANPDYSSLNLAMAVQLVSYELRMAFLVQNNKKNSLSLIEKNYPTTDQLAYFFDYTERIYQSLGFIQNQGVMRKLKRLYYRAKLEKNELNILNGMLSAVEKRIDLTKEDN", "text": "SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family."}
{"protein": "MLYNIPILTHLYEIRLRIIYLLYSIFLTCFCSYQYKEEIFYLLFIPLSKNFIYTDLIEAFITYIKLSIIVGIYLSYPIFLYQIWSFLIPGFFLYEKKLFRLLCLTSIFLYFLGSCIGYYLLFPIAFTFFLGFQKLGKDQLFTIELQAKIHEYLILNTKLIFSLSICFQLPVLILFLFKIYPKTYLWLIHKRRFIYLFFFILAAILSPPDILSQFILVIPLILFFEISLFCIKLIQKYNSFMEPIGFEPTASCLQSTRSTI", "text": "SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family."}
{"protein": "MATKFPKFSQDLAQDPTTRRIWYGIATAHDFETHDGMTEENLYQKIFASHFGHIAIIFLWTSGTLFHVAWQGNFEQWIKDPLNIRPIAHAIWDPHFGEGAVNAFTQAGASNPVNIAYSGVYHWFYTIGMTTNQELYSGAVFLLVLASLFLFAGWLHLQPKFRPSLAWFKNAESRLNHHLAGLFGVSSLAWAGHLVHVAIPEARGQHVGWDNFLSTPPHPAGLMPFFTGNWGVYAADPDTAGHIFGTSEGAGTAILTFLGGFHPQTESLWLTDIAHHHLAIAVIFIIAGHMYRTNWGIGHSIKEILNAHKGPLTGAGHTNLYDTINNSLHFQLGLALASLGVITSLVAQHMYSLPSYAFIAQDHTTQAALYTHHQYIAGFLMVGAFAHGAIFFVRDYDPVANKDNVLARMLEHKEALISHLSWVSLFLGFHTLGLYVHNDVVVAFGTPEKQILIEPVFAQWIQATSGKALYGFDVLLSNPDSIASTTGAAWLPGWLDAINSGTNSLFLTIGPGDFLVHHAIALGLHTTALILIKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAMFWMLNTLGWLTFYWHWKHLGVWSGNVAQFNENSTYLMGWFRDYLWANSAQLINGYNPYGVNNLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETIVWAHERTPLANLVRWKDKPVALSIVQARLVGLAHFTVGYVLTYAAFLIASTAGKFG", "text": "FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family."}
{"protein": "MKAFSCLLSVIATAASLFQHVDARSHARDKLNNISRVERPVIHTPSRRVHAHSHFDLTFDLYPRSSRIKLQLEPNHDVLSHDARVTFLDTEGNVDRTERIERRDHSVFKGWAWTQAKSGAWERVGWARIILHRDGEDPLFEGVFTVMHDHHQVIAKSKYVRKRHQQDPPLDNTPGEYMLLFRGSDIAQTQSTGNVERSIMSSPSCDADTLAYDSNSNFMFPPLPEENNTSIWNYFMTSIGKRQMTDTGGVVPGSRDLKETIGSTSGCPNTRKVALIGVVADCTYTNTFASEMDARADIISVVNAASVVYEHSFNISLTLGEINILPKNCPATASSATPFNQQCDDRAGGGSFTLADRLNTFSAWRGKKTDDFAFWTLMTDCTTENQVGLAWAAQLCVKGVQGNPDSRNSSSQAVAGANVVSKTDNTWQVFAHEAGHIFGAVHDCDSMLCQNPANPDNSRCCPATASTCDARGRFMMNPTSGSQITDFSPCSIGQICSRMARRTILTSCLTTNRGVDTISGQQCGNGIVEDGEDCDCGDEESCKGNTCCDPKTCKYTSGSQCDDANEECCKGCKFASSSTICRTSSGPCDPEEKCSGNSGDCPHDIHSKDGETCGTDLQCASGQCTSRDLQCQMHLGNQVAGSRTVAFDSYGCEVACKDPDRPNVRYEGSLTFLDGTPCGGGGTCKNGQCSGSTFGNEVSDWVSRHKPIVIGVAVGAGCLLLLAIASCICGRSRRQRPRNRKMPPINMRPMAPVYNGWNGAPPNAQQSSPGGHPPYNNIPPPINAPPPAYPGHLPSTRYA", "text": "FUNCTION: Probable zinc protease. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MIPDVSQALSWLESHPNALDGIRRGIERETLRVTPEGHLATTPHPAVLGKALTHPWITTDFAESLLEFITPVDGSIDHMLTFLSDIHRYVARNLGDERMWPLSMPCFIGSEQDIILAQYGSSNLGRFKTLYREGLKNRYGALMQTISGVHYNFSLPLSFWQARAGVQDADSGKAAISDGYFRLIRNYYRFGWVIPYLFGASPAICSSFLNGRESALPFERRGGTLFLPYATSLRLSDLGYTNKSQSNLGITFNHLNQYVEGLKRAIHTPSAEFARLGVEESGHYHQLNANILQIENELYAPIRPKRVTRDGESPSDALLRGGVEYIEVRSLDINPFTPIGVDADQARFLDLFLIWCVLADAPEMSSDELLCTRQNWNRVILEGRKPGQTIGIGCHDARQPLAYVGQSLFADLHRVAEVLDGINGDARYQQVCARLVAAFEDVSLTYSARVVAQMGERGIGGYGLTLAQHYRDRLCSEPLALLDETTLAVQAQRSVTRQAALESQSCESFASYLRQHAGG", "text": "SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily."}
{"protein": "MGVVAEVWRSSVRLLTNSPQLNGGSHKSALWKWRFFSAQPKRTVMWTWVCGFMLFSLGVISLFTGHVVSHLEWYSQQLSKRSLLDMSRREPIDVWKSKYSKFFYGCSERGRNFLPAVQEQSSNGYLLIAASGGLNQQRTGITDAVVVARILNATLVVPELDHHSYWKDDSDFSDIFDVNWFISSLAKDVTIVKRVPDRVMRAMEKPPYTTRVPRKSTLEYYLDQVLPILTRRHVLQLTKFDYRLANDLDEDMQKLRCRVNYHALRFTKRIQSVGMKVVKRMRKMAKRFIAVHLRFEPDMLAFSGCDFGGGEKERAELAEIRKRWDTLPDLDPLEERKRGKCPLTPHEVGLMLRALGFTNDTYIYVASGEIYGGEKTLKPLRELFPNFYTKEMLANDELKPLLPYSSRLAAIDYIVSDESDVFITNNNGNMAKILAGRRRYMGHKRTIRPNAKKLSALFMDREKMEWQTFAKKVKSCQRGFMGDPDEFKPGRGEFHEYPQSCICQRPFSYDKTSTDDEEEDMSEENHNSTSPGHVHLSSADNERDEVFPD", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase GT106 family."}
{"protein": "MSGGGGKDRIAVFPSRMAQTLMKTRLKGAQKGHSLLKKKADALNLRFRDILKKIVENKVLMGEVMKEAAFSLAEAKFTAGDFSHTVIQNVSQAQYRVRMKKENVVGVLLPVFDAYQDGPDAYDLTGLGKGGANIARLKKNYNKAIELLVELATLQTCFITLDEAIKVTNRRVNAIEHVIIPRIENTLTYIVTELDEMEREEFFRMKKIQANKKKLKEQEAAQRALEGPPKEEAGGTHSENQPPRNLLAVEEDNLPVLFN", "text": "FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. SIMILARITY: Belongs to the V-ATPase D subunit family."}
{"protein": "MSAQDDIDTGASNQPRSVVETDQQRAAVVGPRPPRHGEAECTDAIPARDSYQRYDTEVVDVPSMRPPVLPPSRANTLSKQQPRGDLSQSSASSHLPGLRQFTRLAPANMQGKDRSGLLSDRPSGLLLSDHTPNSQHAHRSAPQRDDNGRQSAASNRLSDTNSSAPSPGSTENERVRMHDQRTAPSAPPPLLSDLPRHSTDNKTYRLIIRQQPKQGRLCGLGSKDKRPLDPLPILQLRIIRPDGTEDEDAENSSNLVLQVSLCKEDPITGGYTDAVLVETNDPSYPWTRMLEGRIVASANLARDLDGSRACFFVFTDLSIRQEGQFRLAFKLLALSPPGQVPASAGGHVLTEALTEPFTIYSPRRFPGMTESTDLAKCLARQGIQVPVRNDIRKKQEHLDSLTASTDDMNGLE", "text": "FUNCTION: Velvet-domain-containing protein not required for disease or sexual development on seedlings (PubMed:24064149). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the velvet family. VelC subfamily."}
{"protein": "MSNPEQYDMGFYQSNYIIDNQEPSCNDSNAYGNVYGYREPQATEQPSSPAPPEMFLPSDYGGQLFQPASNLDYYSQSPSVDTFDEEPPLLEELGINFDHIWQKTLTVLNPMKPADGSIMNETDLTGPILFCVALGATLLMAGKAQFGYVYGMSAIGCLGIHALLNLMSNSGVSYGCVASVLGYCLLPMVLLSSCAVFFSLQGTIGTMSALLIITWCSLSASKIFISALAMEGQQLLVAYPCALLYGLFALLTVF", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus, cis-Golgi network membrane Golgi apparatus, trans-Golgi network membrane. SIMILARITY: Belongs to the YIP1 family."}
{"protein": "MAEENKATEQIYTIPLREVKDYPVWKRSNKAIKVIREYLSKHMKIEEEKIKISSELNEAVWEHGIEKPPSAVRVKAVRSEEGVTAQVVGAE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family."}
{"protein": "MQAGRQLFLVDCWLGVLQRASAGPTHTPAVCQRCCSTHLHGDRISDLGDLLITHWVTTFALDPPPLPIIGSPDTAETVEAKLKASGHDIEYQITHHTYLNTPPLIEVYEYTKGFVGAPPDGVSIRGSTNHGPVTPTIGFRIESGPTSVVLTGGTVPCASLDELAAEADALVHTIIRKNIVIRVHQQADQGHLQPPLVNRASDSNRGARGHRHPGHNVLCP", "text": "FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (By similarity). SIMILARITY: Belongs to the RNase Z family."}
{"protein": "MKKEKNFFHLYMVSDATGETLISAGKAVASQYPTIQPIEHIYPMIRNKTQLQRVLDEIQREPGIVLYTIIDQEIKQLLSRECTKIGVPCAAVLDPVLNVFQSYLGTPKNLRVSAQHDLNTDYFRRIEALDFTIEHDDGQSSDDLFNADVILVGISRTSKTPTSIYLANRGIKTANVPLIPGIDLPKALLEEKNSLIIGLIASAERISHVRQNRELGKDVSIERYTDRVNIAEELTYAKRICERFGWPIIDVTRRSIEETAAAVFELLSRFREEKLREIL", "text": "FUNCTION: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation. SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PDRP subfamily."}
{"protein": "MDTKAFKRSLHSSNQYHRKGFGHEAEVTEMLRFEYQSSLIQQIRENGNRFQRGEVTIQLAEAFGFCWGVERAVALAYETRQHFPTERIWITNEIIHNPSVNQNLREMQVEFIPVDEQGQKDFSVVAGEDVVILPAFGASVQEMQLLNDKGCKIMDTTCPWVSKVWNSVEKHKKGSYTSIIHGKYQHEETIATSSYAATYLIVLDLKEAEYVCNYILNGGDREEFLHKFRHAYSPDFDPDRDLVRVGIANQTTMLKGETEQIGKLFERTLMRKYGPDQINQHFLSFNTICDATQERQDAMFKLVEYPLDLMVVIGGFNSSNTTHLQEISIEREIPSYHIDSADRIGPGNRVEHKPLHRPLEIKENWLPEGPIVVGITSGASTPDKVVSDVLEKIFALKSTSPALIP", "text": "FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. SIMILARITY: Belongs to the IspH family."}
{"protein": "MAAPTMKERQACWGARDEYWKCLDENTEDASKCKKLRSSFESSCPQQWIKYFDKRRDYLKFKEKFEAGDFQPSKMTAKS", "text": "FUNCTION: Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family."}
{"protein": "MSEQAVENTVLDRFECRSCGYVYEPEKGDSKHDIAPETPFAELPINWRCPVCTAKKAAFSNIGPAGTASGFRENLGYGLGVNKLTPAQKNILIFGALALGFLFFISLYGLQ", "text": "FUNCTION: Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Could be involved in hydrogenase-linked redox processes (By similarity). SIMILARITY: Belongs to the rubredoxin family."}
{"protein": "MAYDDSVKKEDCFDGDHTFEDIGLAAGRSQREKKRSYKDFLREEEEIAAQVRNSSKKKLKDSELYFLGTDTHKKKRKHSSDDYYYGDISSLESSQKKKKKSSPQSTDTAMDLLKAITSPLAAGSKPSKKTGEKSSGSSSHSESKKEHHRKKVSGSSGELPLEDGGSHKSKKMKPLYVNTETLTLREPDGLKMKLILSPKEKGSSSVDEESFQYPSQQATVKKSSKKSARDEQGALLLGHELQSFLKTARKKHKSSSDAHSSPGPEGCGSDASQFAESHSANLDLSGLEPILVESDSSSGGELEAGELVIDDSYREIKKKKKSKKSKKKKDKEKHKEKRHSKSKRSLGLSAVPVGEVTVTSGPPPSIPYAGAAAPPLPLPGLHTDGHSEKKKKKEEKDKERERGEKPKKKNMSAYQVFCKEYRVTIVADHPGIDFGELSKKLAEVWKQLPEKDKLIWKQKAQYLQHKQNKAEATTVKRKASSSEGSMKVKASSVGVLSPQKKSPPTTMLLPASPAKAPETEPIDVAAHLQLLGESLSLIGHRLQETEGMVAVSGSLSVLLDSIICALGPLACLTTQLPELNGCPKQVLSNTLDNIAYIMPGL", "text": "FUNCTION: Negatively regulates Wnt/beta-catenin signaling during development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPFSLGQRWISDTESELGLGTVVGVEGRMVTVLFPATGENRLFSRTEAPLTRVIYNPGDTIESHEEWSLVVTEVEEKDSLIIYHGTHSETGEQVSLRETLLNHNIRFNKPQDRLFAGQIDRLDRFNVRYQCQLLRNKLATSDLLGLQGPRVGLIPHQQWIAHEVGQRFAPRVLLADEVGLGKTIEAGLIIHQQLLTGRAERILVIVPDTLRHQWLVEMLRRFNLRFSVFDEDRCVEAYADNDNPFYTEQLVICSLDLLRKKRRLDQALDADWDLMVVDEAHHLEWSEEAPSRAYQIVEALSEEIPGVLLLTATPDQLGHQSHFARLRLLDPDRFYDYQAFLKEEDSYKDVATAADALASGESLSDESIAGLTQLLSEKDISASIALIQDDSADTDTRLQARDELLQDLLDRHGTGRVLYRNSRASVKGFPQRNLHVHPQKMPEQYVTAYRVSAMMNKHLDTNAKVRQVLSPEKIYQDFDSGSASWWKFDPRVDWLIDFLKTNRSKKVLIIASQAETALSLEEALRTREGIQATVFHEGMSIIERDKAGAYFAQETGGAQALICSEIGSEGRNFQFASNLVLFDLPLNPDLLEQRIGRLDRIGQKNDVEIHLPYLANTAQERLTEWYHQGLNAFECTCPSGHILFNEFSGELLETLLNNDETSLETLLDNTKARYQELKLAMEQGRDKLLEINSHGGERANKLVQSLADKDGDTQLIGSVIRLWDIIGVEQEDSGENAIVLHPSEHMMFPTYPGLPEDGITVTFDREMALSRDDIALITQEHPLVQTGLDLITSSETGTTSVAVLKNKALPAGTIFLELIYLADASAPKSSQLYRYLPPTPVRVLLDKNGNNLSDNVTYESFNKQLSAVNRHIASKLVNASQAILHPLFAKAETFANAELQTLTACAREKMTSQLSGELERLKALKAVNPNIRDEELSHLSEQMSELNRYLDSSKLQLDAVRLVLVSHA", "text": "FUNCTION: Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair. SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA subfamily."}
{"protein": "MAGRATATATAAGKDRSSFAVTCSLLSQFLKEKKGGGGGLQGLGLGLRPAPAAPPAAGAGGAFRPPPTTMNLLSGLDAPAVEVEPNTAETAADELPLIKAPADQQSDESASEAAGEKAQQLTIFYGGKVVVFENFPSTKVKDLLQIVSTGDGVDKNTGTAATQSLPRPAHNSLPDLPIARRNSLHRFLEKRKGRMNANAPYQANCTAAPSKQANGDKSWLGFGQEMTIKQEI", "text": "FUNCTION: Repressor of jasmonate (JA) responses. Acts as a repressor of JA-induced resistance to the bacterial blight pathogen Xanthomonas oryzae pv. oryzae (Xoo) (PubMed:23104764). Regulates JA-induced accumulation of linalool at the transcriptional level of linalool synthase gene LIS. Linalool is important for resistance to bacterial blight pathogen Xoo (PubMed:23889289). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Mainly localized in the nucleus. SIMILARITY: Belongs to the TIFY/JAZ family."}
{"protein": "MANAKGKVTQVIGAVVDVQFEDTLPEILNALNTENNGKKLVLEVAQHLGENTVRTIAMDATEGLVRGAEVTDTGGPITIPVGNATLGRIMNVIGEPIDEKGPVEASESRAIHQPAPEFSEQSTGSEILVTGIKVIDLLAPYSKGGKIGLFGGAGVGKTVLIMELINNIAKVHSGYSVFAGVGERTREGNDLYHEMIESNVIKPDNLSESQVALVYGQMNEPPGARARVALTGLTLAEQFRDQSGTDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGQMQERITSTKGGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRAISELGIYPAVDPLDSSSRILDPGIVGEEHYQVARDVQGILQRYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFDVAKVFTGSDGVQVPIEDTISSFKAVVAGEYDHLPEGAFYMVGGIDEVIAKAERMAADAA", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MTTARYRPTWDLALDPLVSCKLCLGEFPLEQMTTITQCQCVFCTMCLKQYVELLIKEGFETAISCPDSACPKRGHLQENEIECMVATEIMQRYRKLQFEKEVLLDPSRTWCPSSTCQAVCQLKESDTVLPQLVRCSVCTLEFCSACKASWHPDQDCQENVPITSFLPGESSSFFKADDDDAPIKRCPKCKVYIERDEGCAQMMCKNCKHAFCWYCLESLDDDFLLIHYDKGPCRNKLGHSRASVIWHRTQVVGIFAGFGLLLLVASPFLLLATPFVLCCKCKCSKGDDDPLPT", "text": "FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes ube2l3 and ube2l6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RBR family. RNF144 subfamily."}
{"protein": "MKLVYLVLGAVALLLLGGPDSVLSSSSGNLHTFVGCAVREFTFMAKKPGCRGLRITTDACWGRCETWEKPILEPPYIEAYHRVCTYNETRQVTVKLPNCAPGVDPFYTYPMAVRCDCGACSTATTECETI", "text": "FUNCTION: Functions as a heterodimeric glycoprotein hormone with GPHA2 able to bind and activate the thyroid-stimulating hormone receptor (TSHR), leading to increased cAMP production. Plays a central role in controlling thyroid cell metabolism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
{"protein": "MEITKEIFSLIAAVMLLLGSFIALISAIGIVKFQDVFLRSHAATKSSTLSVLLTLIGVLIYFIVNTGFFSVRLLLSLVFINLTSPVGMHLVARAAYRNGAYMYRKNDDHTHASILLSSNEQNSTEALQLRAKKREEHRKKWYQND", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit G family."}
{"protein": "MRVSKVLTLASFISVCSYSEAKSNETDPNGYIVFCPCMGRFGNQVDQFLGVLAFAKALDRTLVLPNFIEFKHPETKMIPFEFLFQVGTVAKYTRVVTMQEFTKKIMPTVWPPEKRKAFCWTPRQAIYDKSAEPGCHSKEGNPFGPYWDQIDVSFVGDEYFGDIPGGFDLNQMGSRKKWLEKFPSEEYPVLAFSSAPAPFPSKGKVWSIQKYLRWSSRITEQAKKFISANLAKPFVAVHLRNDADWVRVCEHIDTTTNRPLFASEQCLGEGHHLGTLTKEICSPSKQQILEQIVEKVGSIGAKSVFVASDKDHMIDEINEALKPYEIEAHRQEPDDMYTSLAIMGRADLFVGNCVSTFSHIVKRERDHAGQSPRPSAFFGIRAVKRHIDL", "text": "FUNCTION: Catalyzes the reaction that attaches fucose through an O- glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines (PubMed:21966509). Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 65 family."}
{"protein": "MDIFREIASSMKGENVFISPPSISSVLTILYYGANGSTAEQLSKYVEKEADKNKDDISFKSMNKVYGRYSAVFKDSFLRKIGDNFQTVDFTDCRTVDAINKCVDIFTEGKINPLLDEPLSPDTCLLAISAVYFKAKWLMPFEKEFTSDYPFYVSPTEMVDVSMMSMYGEAFNHASVKESFGNFSIIELPYVGDTSMVVILPDNIDGLESIEQNLTDTNFKKWCDSMDAMFIDVHIPKFKVTGSYNLVDALVKLGLTEVFGSTGDYSNMCNSDVSVDAMIHKTYIDVNEEYTEAAAATCALVADCASTVTNEFCADHPFIYVIRHVDGKILFVGRYCSPTTN", "text": "FUNCTION: Viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes (PubMed:10975564). Major anti-apoptotic protein which inhibits both intrinsic and extrinsic pathways and strongly cleaves host CASP1 and CASP8 but is a rather poor inhibitor of host CASP3 (PubMed:10903953). Prevents the proteolytic activity of host interleukin-1-beta converting enzyme (ICE) and ICE-like enzymes. Can also block apoptosis through host tumor necrosis factor (TNF) receptor. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the serpin family. Poxviruses subfamily."}
{"protein": "MLTVPFEEPDMMRESQFGATFTRQEDVRTLSSAELKEAEDDNTDREEEEEREEDENGLPKKKGPRKKKSEGRGDRVKMRRQEANARERSRMHGLNDALESLRKVVPCYSKTQKLSKIETLRLAKNYIWALSETLSAGKRPDLLAFVQTLCKGLSQPTTNLVAGCLQLNARNFLTDHNGDVSFSGRPAYDSLYPYPNAEMATPTGLSSGTRESVKPFRPYNYYASYESYYDSASPESSSPHFDGQMSPPINYNGIFSLKKHDEQVEYSKNCHYGMRYCNVPGRGSMYRVSPDSHFPYDLHPRSQSFQSQDELNTGYHN", "text": "FUNCTION: Differentiation factor required for neurogenesis (By similarity). Does not act as an upstream activator of isl1. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDKVNNNCCCGENAKPCCTDPNSGCCCVSETNNCCKSDKKECCTGTGEGCKWTGCKCCQPAKSGCCCGDKAKACCTDPNSGCCCSSKTNKCCDSTNKTECKTCECCK", "text": "FUNCTION: The metallothioneins are involved in the cellular sequestration of toxic metal ions. Binds 12 cadmium ions per molecule (By similarity). SIMILARITY: Belongs to the metallothionein superfamily. Type 7 family."}
{"protein": "MATNYNEKLLLNYVPVYVMLPLGVVNVENVFADPETLETQLKRLKEEAGVDGVMVDVWWGIIESKGPKQYDWTAYKTLFQLIARLGLKIQAIMSFHQCGGNVGDIVTIPIPQWVRDVGDNDPDIYYTNRKGTRDIEYLSIGVDNLPLFAGRTAVQLYSDYMSSFKENMADLIEAGVIVDIEVGLGPAGELRYPSYPQSQGWVFPGIGEFQCYDKYLKKDFKEAAAKAGHPEWDLPEDAGEYNDKPEETGFFKKDGTYVSEKGKFFMTWYSNKLIFHGDQILGEANKIFAGLKVNLAAKVSGIHWLYNHHSHAAELTAGYYNLFKRDGYRPIARMLSKHYGILNFTCLEMKDTDNTAEALSAPQELVQEVLSKAWKEGIEVAGENALETYGAKGYNQILLNARPNGVNPNGKPKLRMYGFTYLRLSDTVFQENNFELFKKLVRKMHADQDYCGDAAKYGHEIVPLKTSNSQLTLEDIADAAQPSGAFKWDSETDLKVDG", "text": "FUNCTION: Beta-amylase activity. Major cytosolic beta-amylase isoform in rosette leaves and inflorescences stems. SUBCELLULAR LOCATION: Cytoplasm Note=Present in the continuous phloem cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 14 family."}
{"protein": "MKVSYHGHSVVKIEANGKVILIDPFLTGNPKTDLKAEDVKVDAILLSHGHGDHVGDTVELAKKNNAVVVAPFELATFLSWQGVNTHPMHIGGSHEFDFGKVKFTQAFHGSSYIDEANKTITYTGMPAGILFTAEEKTVYHAGDTALFSDMKLIGELNKVDLAFLPIGDNFTMGPEDAVLAAKWINSKTVVPMHYNTFPVIEQDPYQFVEKLQNCTGKVLEAGESITL", "text": "SIMILARITY: Belongs to the UPF0173 family."}
{"protein": "MNQQPLPPQSERRALAIGRAVYEAFQDYHAQFSQITARARQRFETRDWSGAREDAVARIALYDHYISECMLRLRAVLLGQAHDRALWMRARTHYAELLTGLIDQELYKTFYNTLTRRYFRTQGVDAQIEFIALDIEPTDAITVPVARHTYAVSPGRLTEMLVRVLGDYPFEVPYAHRTRCAAAIAVRLLDDLAHWGEHPVRSVELLETVFYRERRAYLVGRLFGEHRFSPCVIALVNDDAGLRAEAVLTRRSDVAQLFSNSRSYFQADLTTVGDAVVFLRSLLTHKPIDELYTMLGRAKQGKTERYRTFFRHFQAHPAEQLVHADGTPGMVMVVFTLPSYPLVFKLIRDRFAYPKTMSRAQVEGKYELVFQLDRIGRLLDAQPYRFLRFPKARFSPALLQDLQSSCAMSLSEDGDDVLIALCYVQRRLRPLNLYLREQLPAAAHAAALDYGQAIKDMARNNIFPGDMLLKNFGITRHQRAVFYDYDELCLITECTFRDWPTPTSYEEQMAAEPWFHVGPRDVFPERFALFMGLPSSQLEAVKHMHPELFDPQWWRDLQARLREDDYPDTPPYADAQKLA", "text": "FUNCTION: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AceK family."}
{"protein": "MESVPESVPSPNSNTPSIPPPVNSVPPFLSKTYDMVDDPLTNEVVSWSSGNNSFVVWSAPEFSKVLLPKYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGRKQLLKSIVRRKPSHVQQNQQQTQVQSSSVGACVEVGKFGIEEEVERLKRDKNVLMQELVRLRQQQQATENQLQNVGQKVQVMEQRQQQMMSFLAKAVQSPGFLNQLVQQNNNDGNRQIPGSNKKRRLPVDEQENRGDNVANGLNRQIVRYQPSINEAAQNMLRQFLNTSTSPRYESVSNNPDSFLLGDVPSSTSVDNGNPSSRVSGVTLAEFSPNTVQSATNQVPEASLAHHPQAGLVQPNIGQSPAQGAAPADSWSPEFDLVGCETDSGECFDPIMAVLDESEGDAISPEGEGKMNELLEGVPKLPGIQDPFWEQFFSVELPAIADTDDILSGSVENNDLVLEQEPNEWTRNEQQMKYLTEQMGLLSSEAQRK", "text": "FUNCTION: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HSF family. Class A subfamily."}
{"protein": "MSDTSLEKGNEGPTAEAPKVAPPTVPDGGLQAWLTVAGASVALFVSFGWVNCIALFQSEYQTNQLKGYSSSDVSWITSMEFFFMLSTSPVSGRLFDSYGPHVPIAIGSFLHVFGLMMASLSTKYYQLMLSQSVVSGIGSSLIFTPAMTAPQTWFRQKRGIVGGLTVAGSSLGGVVFPLMVQHLLPQVGFGWTMRICAFMILGLLVFANVTISSNFEHKPRPFSVIHYIGPLRDTNFVLLCVASFFMYWGIFIPFDYIVVEAIHYGMSTQMAWSLVPILNGASFFGRTVPNYIADKAGRFNVMIVMTTLSAILVLALWLPARGNGALITFAALFGITSGAIIGLGPVLIVQISPMSELGYRVGTVLAFAAVGTLTSPPIGGAIAASDGGSYTYTCVFSGVSFLIGTLGLAALRVRLSGWGLTTKI", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
{"protein": "MAAPGEALTSSGYIAHHLSNLSLYKLGLVGSETSFWNVHIDSLFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPIDFLPYPAEHWLGIPYLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFNHPLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHEDPDH", "text": "FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family."}
{"protein": "MLFANLWKAIILGIIEGITEWLPISSTGHLILVDEFIKLDLSKDFMEMFNVVIQLGAIMAVVILYFHKLNPFSPKKNGEEKKDTWILWSKVLVACLPAAVIGLKFDDYLDAHFYNFLTVSIMLIVYGIAFIIIEKRNKNVAPKCTNLKDFTYKAALIVGAFQVLALIPGTSRSGATILGAILIGASRFVATEFSFFLGIPVMFGASFLKIFKFLAKGNTFGSEEIIILITGSIVAFVVSIIAIKFLLNYLKKNDFTVFGWYRVILGAILIGYWLFS", "text": "FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family."}
{"protein": "MLSFLRLSQLGRIGVQQRFKPLIHRTLSTSCRRFSVDIAYDEIPVSRIRNFSIIAHVDHGKSTLADRLLELTGTIKKNATNKQVLDSLQVEKERGITVKAQTASLLYRYEGSDYLLNLIDTPGHVDFANEVSRSLAACDGVILLVDANEGVQAQTVANYHLARGKELVIVPVLNKIDLKNARPDAVTQELFTLFGIDPDGVLRISAKQGTGCEQVLVEIVKRLPAPDVRRGEQFRALIFDSWFDRYRGALNLVYVKDGEVRVGQEIVSCHTGKVYEVKSLAMLRPDEQKIERLVAGQVGLLGCNMRTSKESNIGDTLYLKKNKNCEPLPGFKPQQPMVFAGVYPADQSQHPYLKGAIEKLVLNDSAVTVVPDSSPALGQGWRLGFLGLLHLDVFSQRLQQEYDAEPILTAPSVTYKIKLKGIKMIAAHGGKDTIFVSNPALFPDPNSVEEYYEPYVLGTIIAPTECTGPIIGLCVERRAVQKTSINIDNDRIMTTYLMPLNEIVLDFHDQLKSISSGYASFDYEDHGYVASALVRMDVLLNGTLVDELCTVVHISKAQSHARELVLKLKELIPRQMVQIAIQATVGGKVVARETLKAYRKDVTAKLYGGDVTRRMKLLKQQAEGKKKMRAIANINVPRDTFINVLKR", "text": "FUNCTION: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily."}
{"protein": "MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLPDGMEARLRSDVIHAPLPSPVDKVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLGIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNNKPWPWMPMLAALVAVTAMVLYVPGLARASP", "text": "FUNCTION: May play a role during myoblast fusion. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single- pass type IV membrane protein Cytoplasm, myofibril, sarcomere, M line. Cytoplasm, myofibril, sarcomere, Z line. Note=Membrane-associated. Distributed in the transverse tubules and near the junctional sarcoplasmic reticulum (By similarity). Detected along the Z- and M-lines in cardiomyocytes (By similarity). SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes to the centrosomes in a microtubule- dependent manner. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes to the centrosomes in a microtubule- dependent manner. SIMILARITY: Belongs to the SLMAP family."}
{"protein": "MRQPLLKLAAVTRRFPAGDKDVVVLNNVNLSIGAGEIVAIVGASGSGKSTLMNILGCLDHPSEGTYTVGGRDTHMLDSDELAQLRREHFGFVFQRYHLLPHVDAVANLEMPAIYAGTPRADRHARARELLARLGLADRAHHRPGQLSGGQQQRVSIARALMNGGQVILADEPTGALDTKSGQDVIRILHELNALGHTIVIVTHDKAVARHARRIIEISDGEIVADRPNRHYAEAFAEVGVGAAATTETAADTRSAPASGDAPPPANNDTAADPAPRARRFAAGTGRFAEACRMAWIALVSHRLRTLLTMLGIIIGITSVVSIVAVGEGAKRYMLEEIGSIGTNTISLYPGSDWGDSRADTIQTLVPADVAALAEQPYVDSATPETSRTLLLRYRNVDVHALVSGVGDSYFQTRGMRFALGVPFDDDAVRRQAQVAVIDQNTRRKLFGATRNPVGEAILVDNVPCVVIGVTADKKSAFGSVKSLNVWVPYTTASGRLFGQRYLDSITVRVRDGQPSAAAEKSLEKLMIQRHGRKDFFTYNMDSVVKTVEKTGQSLTLLLSLIAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARQSDILQQFLVEAVLVCLLGGTIGIALSFGLGALFSVFVAQWKMVFSAGAIVTAFVCSTLTGVIFGFMPARNASRLDPIDALARD", "text": "FUNCTION: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP- binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide exporter (TC 3.A.1.122) family."}
{"protein": "MDHALFTHFVGRPRHCRLEMLILDEQVSKRSWDTTVYHRRRRHLPRRRAPCGPQRPAEIPKRRKKAAVLLFWHDLCWLFRRLFFPREDSEPLMSDPARSPEEEE", "text": "SIMILARITY: Belongs to the HHV-5 UL17 protein family."}
{"protein": "MNYTETVAYIHSFPRLAKTGDHRRILTLLHALGNPQQQGRYIHVTGTNGKGSAANAIAHVLEASGLTVGLYTSPFIMRFNERIMIDHEPIPDAALVNAVAFVRAALERLQQQQADFNVTEFEFITALGYWYFRQRQVDVAVIEVGIGGDTDSTNVITPVVSVLTEVALDHQKLLGHTITAIAKHKAGIIKRGIPVVTGNLVPDAAAVVAAKVATTGSQWLRFDRDFSVPKAKLHGWGQRFTYEDQDGRISDLEVPLVGDYQQRNMAIAIQTAKVYAKQTEWPLTPQNIRQGLAASHWPARLEKISDTPLIVIDGAHNPDGINGLITALKQLFSQPITVIAGILADKDYAAMADRLTAAFSTVYLVPVPGTPRALPEAGYEALHEGRLKDSWQEALAASLNDVPDQPIVITGSLYLASAVRQTLLGGKS", "text": "FUNCTION: Involved in the conversion of folates to polyglutamate derivatives, and likely functions in the retention of cellular folate pools. Catalyzes successive MgATP-dependent additions of glutamate to a pteroylmonoglutamate substrate, with a high preference for 5,10- methylenetetrahydrofolate (mTHF). Thus, metabolizes mTHF to the tetraglutamate derivative, but longer glutamate chain length products are not observed. Tetrahydrofolate (H4PteGlu) and 10-formyl-H4PteGlu are poorer folate substrates. In contrast to E.coli FolC, this enzyme does not display dihydrofolate synthase activity. SIMILARITY: Belongs to the folylpolyglutamate synthase family."}
{"protein": "MTQIHQINDIDVHRITSGQVITDLTTAVKELVDNSIDANANQIEIIFKDYGLESIECSDNGDGIDPSNYEFLALKHYTSKIAKFQDVAKVQTLGFRGEALSSLCGIAKLSVITTTSPPKADKLEYDMVGHITSKTTTSRNKGTTVLVSQLFHNLPVRQKEFSKTFKRQFTKCLTVIQGYAIINAAIKFSVWNITPKGKKNLILSTMRNSSMRKNISSVFGAGGMRGLEEVDLVLDLNPFKNRMLGKYTDDPDFLDLDYKIRVKGYISQNSFGCGRNSKDRQFIYVNKRPVEYSTLLKCCNEVYKTFNNVQFPAVFLNLELPMSLIDVNVTPDKRVILLHNERAVIDIFKTTLSDYYNRQELALPKRMCSQSEQQAQKRLKTEVFDDRSTTHESDNENYHTARSESNQSNHAHFNSTTGVIDKSNGTELTSVMDGNYTNVTDVIGSECEVSVDSSVVLDEGNSSTPTKKLPSIKTDSQNLSDLNLNNFSNPEFQNITSPDKARSLEKVVEEPVYFDIDGEKFQEKAVLSQADGLVFVDNECHEHTNDCCHQERRGSTDTEQDDEADSIYAEIEPVEINVRTPLKNSRKSISKDNYRSLSDGLTHRKFEDEILEYNLSTKNFKEISKNGKQMSSIISKRKSEAQENIIKNKDELEDFEQGEKYLTLTVSKNDFKKMEVVGQFNLGFIIVTRKVDNKYDLFIVDQHASDEKYNFETLQAVTVFKSQKLIIPQPVELSVIDELVVLDNLPVFEKNGFKLKIDEEEEFGSRVKLLSLPTSKQTLFDLGDFNELIHLIKEDGGLRRDNIRCSKIRSMFAMRACRSSIMIGKPLNKKTMTRVVHNLSELDKPWNCPHGRPTMRHLMELRDWSSFSKDYEI", "text": "FUNCTION: Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non- identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family."}
{"protein": "MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPAVDPYDMPGTSYSTPGLSAYSTGGASGSGGPSTSTSTSGPVSARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSTSAKEDGFGWLLPPPPPPPLPFQSSRDAPPNLTASLFTHSEVQVLGDPFPVVSPSYTSSFVLTCPEVSAFAGSQRTSGSEQPSDPLNSPSLLAL", "text": "FUNCTION: Heterodimerizes with proteins of the JUN family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing their transcriptional activity (By similarity). Exhibits transactivation activity in vitro (By similarity). As part of the AP-1 complex, facilitates enhancer selection together with cell-type- specific transcription factors by collaboratively binding to nucleosomal enhancers and recruiting the SWI/SNF (BAF) chromatin remodeling complex to establish accessible chromatin (By similarity). Together with JUN, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (By similarity). Involved in the display of nurturing behavior towards newborns (By similarity). May play a role in neurogenesis in the hippocampus and in learning and memory-related tasks by regulating the expression of various genes involved in neurogenesis, depression and epilepsy (By similarity). Implicated in behavioral responses related to morphine reward and spatial memory (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Fos subfamily."}
{"protein": "MSTNAKESAGKNIKYPWWYGGAAGIFATMVTHPLDLAKVRLQAAPMPKPTLFRMLESILANEGVVGLYSGLSAAVLRQCTYTTVRFGAYDLLKENVIPREQLTNMAYLLPCSMFSGAIGGLAGNFADVVNIRMQNDSALEAAKRRNYKNAIDGVYKIYRYEGGLKTLFTGWKPNMVRGILMTASQVVTYDVFKNYLVTKLDFDASKNYTHLTASLLAGLVATTVCSPADVMKTRIMNGSGDHQPALKILADAVRKEGPSFMFRGWLPSFTRLGPFTMLIFFAIEQLKKHRVGMPKEDK", "text": "FUNCTION: Mitochondrial dicarboxylic transporter catalyzing the exchange of dicarboxylic acids like malate and succinate for inorganic phosphate. Required for growth on ethanol and acetate. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MAPIKRGDRFPTTDDVYYIPPEGGEPGAFELSKFVKTKKFVVVSVPGAFTPPCTEQHLPGYIKNLPRILSKGVDFVLVITQNDPFVLKGWKKELGAADAKKLIFVSDPNLKLTKKLGSTIDLSSIGLGTRSGRLALIVNRSGIVEYAAIENGGEVDVSTAQKIIAKL", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily."}
{"protein": "MAAGGSGAESAPPTPSMSSLPLAALNVRVRHRLSLFLNVRTQVAADWTGLAEEMNFEYLEIRRLETHPDPTRSLLDDWQGRPGASVGRLLELLAKLGRDDVLVELGPSIEEDCRKYILKQQQEAAEKPLQVDSVDSSIPWMSGITIRDDPLGQMPEHFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPVKYKSMKKEFPSILRFITVCDYTNPCTKSWFWTRLARALSLP", "text": "FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses, induces IL1B release through NLRP3 inflammasome activation (By similarity). MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MKSLHCVGLYLLSLLCQLTEAKKHCWYFEGLYPTYYICRAYEDCCGSRCCVRALSIQRLWYFWFLLMMGVLFCCGAGFFIRRRMYPPLLVDEPTFNVSYTRQPAGPPGGPQQPVMPYYSDPGGAMGNPMTPSFYVQPNSPQGNPPFPPPPSYCNTPPPPYEQVVKSYK", "text": "FUNCTION: May be involved in the transcriptional activity of NFKB1. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the VOPP1/ECOP family."}
{"protein": "MGKLPMKEAALVYLDRSGGLQKFMDDCKYYNDSKQSYAVYRFSILINPCDVVELDAELGNHILHHPLKAAQVFQSVCFVAVKTLSLIGKLQTETQINIVLKLTHLPSLPSYSLDLCEFPLNYASQRFYMMQGIVIAMTTVTKYTQGARFLCSDEVCPFSKGFQYIRVHVPGATESATVRNDFLCRLCSSSLQEDRKFRVLGDKQIIEIITTKVLHAFQGDPKNQPFRFQSLSVFLRDELVNKMKIGNEYKIIGIPVCVKTSQTALCVEANSITPYTAKVPSGISDNFRCLLSLTSSSCWRFTAILANVFASHIVPLGTYNLLKLCLLMSLVQTRDCSSERENCLDILVITSDTLLVDRLLNFSMNLVSRGIRHPVCTEVFPTVSRDKYGTGAVSIQAGSALLARGGVCFIGDLTSHKKDKLEQLQSALESRSVTVFIPGKKFGDDFDQQMTFPIQCSFWSFVDMDSSSRRNVQKASTLIGQMDCSLIPANLAEAFGLLVNCKESSPCHPLLPTVQHTLKKAVDPKGPPYLASKQFTTEDFEKLLAFAKNLNVEFSLEAERMIHGYYLASRRIRTDSIHGSKLSANALKYLVSLSEAHARLNLRNKVLREDVLIAALLFEISLTLKYGATAFCVAPNALFPFELYDEDYLEQRDLYLTQCQQQLQHFIATCGPGTAVLSSDE", "text": "FUNCTION: Plays an important role in meiotic recombination and associated DNA double-strand break repair."}
{"protein": "MNIVDSNCTIWHKARNSKFRHIVWPIRSYELTKFIPMALLMFFILLNQNLVRSLKDSFVVTLISSEVLSFIKLWGEMPMGVLFVILYSKLCNIMTTEQVFRIITGTFLFFFTIFGFILFPYKEFFHPDPELINQYITVLPHLKWFLIIWGQWSLVLFYIMGELWPVIVFTLLYWQLANKITKVEEAPRFYSFFTLFGQTNLLFSGTVIIYFAKSEHFLLPLFAHLNDTNEILLKSFITVILLSGLICLALHKLIDKSVVEADKNIKFKNQRTDILKLSLIESAKIILTSRYLGFICLLVMSYSMSINLIEGLWMSKVKQLYPATKDFISYHGEVLFWTGVLTLVSAFLGSSLIRIYGWFWGAIITPIMMFVAGVIFFSFTIFENHLGNIVNTLGYSSPLVIIVFIGGLWHVFSKSVKYSLFDATKEMVYIPLDNEIKTKGKAAVDVIGAKIGKSIGAVIQFISFSIFPNAVHNDIAGLLMFTFIIVCILWIYGVKVLSQYNNKMIQN", "text": "FUNCTION: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADP/ATP translocase tlc family."}
{"protein": "MVDFSLKKHGVSSWGRGSLSRKESSAGDSSSTFKSSRYQDMKVSDPELPKVSAKERSKAGTMMKRRLSVHQSNNFGAVKMDFDNMPALPSSAADYSFASNVGNATQTSLITEDQLPDRNTSLASLNTNTRRPDQELYSSKSLRQILSNPDFKAKKFITEKLGDATAVDIDQFTSNLNDLSLEIQDEIKFNIDKSFKEILIVNKGLETATTELKVLRTKVQEMKDIMNQFVTIAEKKLQAEQAANETADLNRTSSSASLSNHSLLPPLKPTPSATRKDRTSVYILERMWNEELMTLFKNVDGAHKYITSTPGRHILLESDNWIEINPATLKPLQKVRLFILNDVVLIAAPKPSKQTELTVSRFSPLRDVTVEVQSEHELSFNFSNKQHTLYRHRDPQVFSKVIDIIRQAKDALREISQAEEDTTRKIRNSYTLLQQERTPNRDATTSPVKVHGRQRSYGGTGTPSRHRSDAQNDALLTNITRSIHVRMGSEETTEVTKRLKRLDDALEDLDLEIGRQNFDLAITKLNHIQSSLKSLYSSATFDESVMVELLSLKCSQRKTILYTKLTNLLACETSDMTKLKSYMLNLVALNEPVDALEVFLQNRSNFINDLTLQIGIIDNVTSFITQVAIIRFQTLKKVTQQYLEVSKNLKRDYTSLLVCWCSEEVDKHFQLMERELSNSSTLSVQAIKITRKQIDELKPVGMDYVYKLDDFIRRNNNRIL", "text": "FUNCTION: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis. Also involved in assembly of the spliceosome (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle Note=Cell periphery. The polarization of EXO84 requires actin cables (By similarity). SIMILARITY: Belongs to the EXO84 family."}
{"protein": "MTQITEKELKKKYLDLLSQNFDTPEKLATEIINLESILELPKGTEHFVSDLHGEYEAFQHVLRNGSGNVRAKINDIFKERLSTKELNDLTALVYYPEDKLKLIKSDFQSCGQLNVWYITTIEHLIELIKYCSSKYTRSKLRKALPKQYVYIIEELLYKSNEYQNKKSYYETLVNQVIELKQADDLIIGLAYSVQRLVVDHLHVVGDIYDRGPQPDKIMDTLINYHSLDIQWGNHDVLWVGAYAGSKVCLANLLRICARYDNLDIIEDAYGINLRPLLTLAEKYYDADNPAFKPKKRPDKHERLTQREESQITKIHQAIAMIQFKLEIPIIKRRPNFEMEERLVLEKVNYDTNEITVYGNTYPLKDTCFQTINRNNPAELLPEEEEVMNKLLLSFQQSEKLRRHMSFLMRKGSLYLPYNGNLLIHGCIPVDENGEMESFEIDGHTYSGQELLDVFEYHVRKSFDEKENTDDLSTDLVWYLWTGKYSSLFGKRAMTTFERYFIADKASHKEEKNPYYHLREDVNMVRKMLSDFGLNPDEGRIINGHTPVKEINGEDPIKADGKMLVIDGGFSKAYQSTTGIAGYTLLYNSFGMQLVAHQQFNAKEKILSEGIDELSIKRVVDKELQRKKIRDTNIGKELQAQIDILKMLMHDRYLD", "text": "SIMILARITY: Belongs to the FBPase class 3 family."}
{"protein": "MRRPGAVVRRAGGYVTNLMPTAAGDPIGGGLGDQVYNRLLGERIIFLGQAVDDDIANKITAQLLLLASDPDKDIYLYINSPGGSITAGMAIYDTMQYIKNDVVTIAMGMAASMGQFLLSAGTPGKRFALPNAEILIHQPSAGLAGSASDIKIHAERLLHTKKRMAELTAFHTGQTVEQVTRDSDRDRWFDPVEAKEYGLIDDIMPTAAGMPGGGGTGAA", "text": "FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S14 family."}
{"protein": "MGLQETIGIEIVSVEKGKAVVQLEVTEKVHQPFGYLHGGVSVVLAEHAASIGAAKSIEPDEIVFGLEINANHLASKQAGLVTATAEAIHIGKSTQVWEIKITDETEKLLCISRCTIAVKKKRK", "text": "FUNCTION: Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A (PubMed:33619030). Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol (PubMed:33619030). SIMILARITY: Belongs to the thioesterase PaaI family."}
{"protein": "MKKAVVLSAVALLSGVCAVADESVLIDFAKLNADIMADKSGGMTHNRRTVLDYASLADTSYTDEQKALMRSSLAVAQWEVVLNSSARNPVAHAASRVIEAPVSEGAKSFAGERVLGVRVLFPTWDSNANAMIKPAFVIPAYEVMAQVDDQGNVQAPTEEEKASGKGRFEDGYGVVKNVGVLKSIAVNTYGMNYPHGLYVMMRDQDGEVHRYFMGYLLFDSWKELVWNNPSYISDVRSREVRLYPVYPASTPHVVFEGFMVTRDAAHAGGDYVGYFKDVKIIYDKAVLSTVRDFADEDLWGIQARREAERKRVEVARFGQQQVLRYIEQEKLATEVGFTPSGGAQRQEEQQ", "text": "FUNCTION: Component of the outer layer of the flagella. SUBCELLULAR LOCATION: Periplasmic flagellum. Periplasm Note=Antibody labeling only occurs after mild detergent solubilization (PubMed:25825429)."}
{"protein": "MGKNTKRNKKTKQQQQQPQQNGVTASASGTAVEDFEDQQAASSLPSLNGKKRSQLNKLVEELLDLVEKQPANPNEEWKQYGQLQELLKQIMILEEPLSQAVCPQISDSPDDQTRLAKVEAFSAWAKDGGVHSEGLEIAIFPGYQLGLRATRPLAKDELVLSVPRKLILSEENNSDCRLFGKMTQATHLNLAYDLVIEKIRGEFSEWRPYIDVLPAKYNTVLYFTTKQMELLRGTAAAALAMRQCRVIAKQYAFLYKYAHTMTEPSTGNRSHPGERGLFFTQHGLCYKLYRWAVSTVMTRQNLVPSEKQESEDGPKLISALIPYWDMANHRPGKITSFYATVSRQLECTAQEAVNTGEQFFIYYGDRSNTDLLVHNGFVDPNNTKDYVNIRVGLSLTDALAAKRASILDKLNIRHTAELRVLPAPDFISKELLAFVRVFKMSAEQLDHWCSDLDRAGDLLHIDCALETDHETRTWQFLEDRLKLLLAVFNKEMHEADEVKELELKDGQEIELMLFLYRRLERSILAGALQYAQEHRKV", "text": "FUNCTION: Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-74'. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes mainly in the cytoplasm. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. SETD3 actin-histidine methyltransferase family."}
{"protein": "MDSTALKILQDKCICYICSDFMEDPVTSRCGHNFCFACLRLLWDDLQGNIFCPVCQTPFPPKSFSRNYQFRNMTETIRLLQKRQSKRKRQEEHTVCPKHDQPLVLFCVRDRDVLCTQCSLSVEHQGHYTCPIKKASSYHRKVLESAIATLKFGVKQVEEKLAVQHRRVLGLREEAQYQKIEIRYEIGQIKLFLQSEYEAHLNESHMEELRSFSELNGYLETLLDHVSTAKDLLKEVEAIHERSDVTLLRAYHKLQNLKSPKPWLFRTKQYGLSLPAQYSGLSRIIKQFQADVTFDRDTAHPQLVISEDRKSVFYKEAWPCVCASPQKFHLWPALLGCKGFDSGRQYWEVKVGDKPRWTLGVCQAHFSGDWSNQSSGFWAIGRYAENSYVTYGPLRTEFLPVVRPSKVGIFLDYELGELSFYNMNDRSLLYTFRNSFTSTLWPYFYIGTDSESLEILTHPTPDTGSY", "text": "FUNCTION: E3 SUMO-protein ligase that mediates SUMOylation of TAB2 leading to inhibition of NF-kappa-B and MAPK pathways by suppressing the TRAF6/TAB2/TAK1 complex. SIMILARITY: Belongs to the TRIM/RBCC family."}
{"protein": "TKYYGNGVYCNSKKCWVDWGQAAGGIGQTVVXGWLGGAIPGK", "text": "FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family."}
{"protein": "MQVPSPSVREAASMYGTAVAVFLVILVAALQGSAPAESPFPFHIPLDPEGTLELSWNISYAQETIYFQLLVRELKAGVLFGMSDRGELENADLVVLWTDRDGAYFGDAWSDQKGQVHLDSQQDYQLLRAQRTPEGLYLLFKRPFGTCDPNDYLIEDGTVHLVYGFLEEPLRSLESINTSGLHTGLQRVQLLKPSIPKPALPADTRTMEIRAPDVLIPGQQTTYWCYVTELPDGFPRHHIVMYEPIVTEGNEALVHHMEVFQCAAEFETIPHFSGPCDSKMKPQRLNFCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRFLRLEVHYHNPLVITGRRDSSGIRLYYTAALRRFDAGIMELGLAYTPVMAIPPQETAFVLTGYCTDKCTQLALPASGIHIFASQLHTHLTGRKVVTVLARDGRETEIVNRDNHYSPHFQEIRMLKKVVSVQPGDVLITSCTYNTEDRRLATVGGFGILEEMCVNYVHYYPQTQLELCKSAVDPGFLHKYFRLVNRFNSEEVCTCPQASVPEQFASVPWNSFNREVLKALYGFAPISMHCNRSSAVRFQGEWNRQPLPEIVSRLEEPTPHCPASQAQSPAGPTVLNISGGKG", "text": "FUNCTION: Conversion of dopamine to noradrenaline. SUBCELLULAR LOCATION: [Soluble dopamine beta-hydroxylase]: Cytoplasmic vesicle, secretory vesicle lumen. Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type II membrane protein. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the copper type II ascorbate-dependent monooxygenase family."}
{"protein": "MYSILIACLVLLLCLVIYVGHRADHARKYLEGMWHGDPVFLKQSGLQSFYLYIQPGHTCFFSIVNKNGEKLMETKIPCTITNKIYMFFKPIFEFHVVMEDIHRYLPKQFNFLLDSAEGKLILENNHVIYAVLYKDNFATALGKTVEKYITQN", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the asfivirus EP152R family."}
{"protein": "MKDLFDESLTLDTGSAAPGTAPGRPRRRQPAGGKAPDTAAFLANFVRIGEIAAPKPPAAADVVSEPEEEAAVVAELIAEMRPMFQRDGGDIELIGLTGATVQVRLSGSCAGCMMSARTLSTVQHQLIETLGRPVRVVPEIRH", "text": "FUNCTION: May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. SIMILARITY: Belongs to the NifU family."}
{"protein": "RGIFRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYCVTGDALVRLPFGQSVRLRDVVAGARSSSDNAIDLKVLNRHGDPVVADKLFHSGEHETYTVRTAEGYEVTGTANHPLLCLVDVGGVPTLLWKLTEEIRPGDHVVLQRTPPTEFGPADWQDAFEALHLGAFISEGFVSENRAGFNNLDREFFNAVLTAYDTIVGGPRYVSSRTIASDSLLHELDVHNLTALKKSRLGELVGQRSADKAVPEWLWKAPAVVKRVFLQALFEGDGSCSALPRNTIQVSYSTRSGRLAKDIQQMLLEFGVISRRYVHATGEHKVVLTSRAQAELFAAQIGFGGIKQAKLQGLLDALPQAAAGRDGDYVPGLAQFVRKHSGSRWVDKDWLNRHNIDRLSRWQRDGAEILGRIADPDVRAIAQELTDGRFYYARVASVTDSGVQPVYSLRVDTDDHSFITNGFVSHNTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHN", "text": "FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit family."}
{"protein": "MQTPKSRPGSLELPQKKSPLPAPKVVRRLKPSGAESDPKTKTISKTQIPKVVADRRSARIPLNEIQKKRTGRIPELESTISQLQEELKKAKEELNRSEALKREAQEEAEDAKHQLMDINASEDSRIEELRKLSQERDKTWQSELEAMQRQHGMDSTALSSAINEVQKLKSKLFESESELEQSKYEVRSLEKLVRQLEEERVNSRDSSSSMEVEELKEAMNLSRQEITQLKSAVEAAETRYQEEYIQSTLQIRSAYEQTEAVKSRYSQREAELTEELNRTKDEIEGLRKELMEKVKEDESTGDLKKLESDLMEVRGSLMDKEMELQILRSAMEKKVETANTEAMEAELKRVKIQCEQWRKAAETAASILNNDEERTDSIETSKMLKKFGVLLKKNHK", "text": "FUNCTION: ROP effector binding specifically activated ROPs and linking them to the microtubule cytoskeleton. Involved in ROP-regulated polar growth. Involved in local disassembly of cortical microtubules when associated with ARAC10 and KIN13A and conversely mediates also the elimination of ARAC10 from the plasma membrane by the cortical microtubules. Accumulates at the plus end of shrinking microtubules. Targets KIN13A to microtubules. SUBCELLULAR LOCATION: Cell membrane Cytoplasm, cytoskeleton Note=In xylem cells, preferentially colocalizes with cortical microtubules located beneath the secondary wall pits (PubMed:20619818). May be associated to the plasma membrane through the interaction with ARAC10 (PubMed:22984069). SIMILARITY: Belongs to the ICR family."}
{"protein": "MTDLSEKVRAWGRRLVVGAAAAATLPGLIGIAGGAATANAFSRPGLPVEYLQVPSAGMGRDIKVQFQSGGNGSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSVIMPVGGQSSFYADWYQPACGKAGCSTYKWETFLTSELPQYLASNKGVKSTGSAAVGISMSGSSAMILAVNHPNQFVYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKADAMWGPSSDPAWQRNDPSLQIPALVGNNTRLWVYCGNGTPSELGGANMPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFNANGTHSWEYWGAQLNAMKPDLQSALGASSGGGG", "text": "FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha- trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the mycobacterial A85 antigen family."}
{"protein": "MAEDEDNQQGQGEGLKYLGFVQDAATYAVTTFSNVYLFAKDKSGPLQPGVDIIEGPVKNVAVPLYNRFSYIPNGALKFVDSTVVASVTIIDRSLPPIVKDASIQVVSAIRAAPEAARSLASSLPGQTKILAKVFYGEN", "text": "FUNCTION: May be part of the rubber biosynthesis machinery. Plays a role in rubber elongation. SUBCELLULAR LOCATION: Cytoplasm Note=Tightly bound on latex large rubber particles. Binds first to various type of lipids and then inserts into the membrane as protein rafts. SIMILARITY: Belongs to the REF/SRPP family."}
{"protein": "MIYEGKAITVKALESGIVELNFDLKGESVNKFNRLTLNDLRQAVDAIKADASVKGVIVTSGKDVFIVGADITEFVDNFKLPDEELVAGNLEANKIFSDFEDLGVPTVVAINGIALGGGFEMCMAADYRVMSTTAKVGLPEVKLGIYPGFGGTVRLPRLIGVDNAVEWIASGKENRAEDALKVHAVDAVVAPEKLQEAALDLVKRAISGELDYKAKRQPKLDKLKLNAIEQMMAFETSKAFVAGQAGPNYPAPVEAIKTIQKAANFGRDKAIEVEAAGFVKLAKTSVAQSLVGLFLSDQELKKKAKAYDKQARDVKLAAVLGAGIMGGGIAYQSAVKGTPILMKDIREEGIQMGLDEASKLLGKRVEKGRLTPEKMAQALNAIRPTMSYGDFGNVDIVVEAVVENPKVKHAVLAEVEGHVREDAIIASNTSTISISYLAQALKRPENFCGMHFFNPVHMMPLVEVIRGEKTSETAIATTVAYAKKMGKSPVVVNDCPGFLVNRVLFPYFGGFARAIAHGVDFVRADKVMEKFGWPMGPAYLMDVVGMDTGHHGRDVMAEGFPDRMKDDTRTAVDVMYDANRLGQKNGKGFYAYEMDKKGKPKKVVDPQAYELLKPIVAETRELSDEDIINYMMIPLCLETVRCLEDGIVETAAEADMGLIYGIGFPPFRGGALRYIDSIGVAEFVAMADKYADLGPLYHPTAKLREMAANGQRFYG", "text": "FUNCTION: Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family."}
{"protein": "MSASEFDDRFVTVPLRDVTKVPSHERAGEAMNIIRQHLAKQFAVDEDAVRLDPSINDAVWSEGNNNPPRKLRVHAGSFAEDGETVVEADYEG", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family."}
{"protein": "MEKLRILICDGNTEADRASFKKFVGCAPSKQFESLLKNYNSQIRTEIAFPADPGPLMTLPLGAYDGILITGSNSHIYEAQPGNLRQIEFAQKAFASGTPMFGVCWGMQLAVVAAGGEVLPSRVADCSCETPFATGVELTSYGSGHPMHHSRTSGFDVFSFHSDEVTRLPGGAVVTARNRNFIQAVEIKHGRSTFWGVQYHPELSGWDQAGFLRESARSLVEDGSYETLNHVEHAAQAISMFKAGAQISEENLVHFEGVDTNSFEFRPLEILNWLDHLVIPTAKRKFGWGGGWLQK", "text": "FUNCTION: Involved in the degradation of isopropylamine, which is a constituent of the herbicides atrazine. Catalyzes the hydrolysis of gamma-glutamyl-L-alaninol (GALO) to L-alaninol and L-glutamate. It can also uses gamma-glutamyl-isopropylamide, gamma-glutamyl-ethylamide, L- glutamine, and gamma-glutamyl-p-nitroanilide."}
{"protein": "MTHHDCAHCSSDACATEMLNLAEANSIETAWHRYEKQQPQCGFGSAGLCCRICLKGPCRIDPFGEGPKYGVCGADRDTIVARHLVRMIAAGTAAHSEHGRHIALAMQHISQGELHDYSIRDEAKLYAIAKTLGVATEGRGLLAIVGDLAAITLGDFQNQDYDKPCAWLAASLTPRRVKRLGDLGLLPHNIDASVAQTMSRTHVGCDADPTNLILGGLRVAMADLDGSMLATELSDALFGTPQPVVSAANLGVMKRGAVNIAVNGHNPMLSDIICDVAADLRDEAIAAGAAEGINIIGICCTGHEVMMRHGVPLATNYLSQELPILTGALEAMVVDVQCIMPSLPRIAECFHTQIITTDKHNKISGATHVPFDEHKAVETAKTIIRMAIAAFGRRDPNRVAIPAFKQKSIVGFSAEAVVAALAKVNADDPLKPLVDNVVNGNIQGIVLFVGCNTTKVQQDSAYVDLAKSLAKRNVLVLATGCAAGAFAKAGLMTSEATTQYAGEGLKGVLSAIGTAAGLGGPLPLVMHMGSCVDNSRAVALATALANKLGVDLSDLPLVASAPECMSEKALAIGSWAVTIGLPTHVGSVPPVIGSQIVTKLVTETAKDLVGGYFIVDTDPKSAGDKLYAAIQERRAGLGL", "text": "FUNCTION: Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH). SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Loosely attached to the inner membrane, probably via CooF. SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase family."}
{"protein": "MNTSFDPVAANSNSANVTPGYMSGFGNSFETEALPGALPIGRNSPQRCAYGLYAEQLSGSPFTAPRGANERSWLYRIRPSVRHSGHFVKIDAKLWRTAPCLEHDMPLAQLRWDPTPIPEDELTFVQSVRTMTTAGDAHTQTGMAAHIYLITRSMVDQHFYNADGEMLFVPQGGSLRFVTEFGVIDTEPGEIAVIPRGVKFRVEIPSGPARGYLCENYGGAFTLPERGPIGANCLANSRDFLTPVAAYEDDDKPTELFVKWGGALWSTALPHSPIDVVAWHGNYAPYKYDLRTFSPIGAIGFDHPDPSIFTVLTSPSEIAGTANIDFVIFPERWVVAENTFRPPWYHMNVMSEFMGLIYGVYDAKPQGFVPGGISLHNCMLPHGPDREAFDHASNTELKPVKLTGTLAFMFETRFPQRVTEYAATSDALQDDYADCWQGLERRFDPTRP", "text": "FUNCTION: Involved in the catabolism of homogentisate (2,5- dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate. SIMILARITY: Belongs to the homogentisate dioxygenase family."}
{"protein": "MKLIIFTGLVLFAIVSLIEAEEESGRGCILLYGECTKATGSCCSNLICDCYRKLKKGVQIARQCFCSEKDVIYKKDI", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 10 (U11-Lctx) subfamily."}
{"protein": "MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKNGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDDCCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR", "text": "FUNCTION: Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane (PubMed:20657014). Lethal to insect larvae (PubMed:20657014, PubMed:24717175). Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g causes reversible paralysis (PubMed:20657014). Has cytolytic activity against insect Sf9 cells (PubMed:20657014). Causes stable and irreversible depolarization of fly muscle fibers, leading to contracture at higher toxin concentrations (PubMed:20657014). Destabilizes membranes (PubMed:20657014). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Probably forms a transmembrane alpha-helix in the target cell membrane. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. Double-CSTX subfamily."}
{"protein": "MSAEYGQRQQPGGRGGRSSGNKKSKKRCRRKESYSMYIYKVLKQVHPDIGISAKAMSIMNSFVNDVFEQLACEAARLAQYSGRTTLTSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Chromosome Nucleus. SIMILARITY: Belongs to the histone H2B family."}
{"protein": "MSKLFVGSEIGQLRRVILHRPERALSHLTPTNCHNLLFDDVLSVEKALHEHDQFVATLRQQDVEVLLLQDLLEETLAHPEAKQWLLRHQISHYRFGPTFANQIRAFLLEKNNKELASILLGGLAFIELPFKAPSMLQQLSDPFDFVIDPLPNHLFTRDTSCWIYGGVSINPMAKAARKRESNHLRAIYKWHPLFSNQSFPRYFGDENRHYDNATIEGGDVLIIGKGNVLVGISERTTPQGIENLAKQLFRTEQAKQVIAIKLPENRSCMHLDTVMTHMDHNVFSVYPRVIDKNMPCWSITPCGDQQLAIQEKPNFEHSLMQALELDSLNIITTGGDSYEAEREQWHDANNVLTIKPGVVVAYERNVYTNEKYDKAGITVLPIMGDELGRGRGGARCMSCPIERDGI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the arginine deiminase family."}
{"protein": "MLILTRRVGEALMIGDQVTVTVLGVKGNQVRIGVTAPKEVTVHREEIYARIQREKEQANGRGQVSESEFTEEAFRAAPAISGSGE", "text": "FUNCTION: A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family."}
{"protein": "MAVGKNKRLSKGKKGLKKRTVDPFTRKDEYLVKAPTTFQVRDVGKTLVNRTTGLKNANDYLKGRVFEVSLADLQKDEAHSFRKVKLRVDEVQGKNCLTNFHGLDFTSDKLRSLVRKWQTLIEANVTVKTTDDYLVRLFAIAFTKRRPNQIKKTTYAQSSQIRAIRKKMTEIIQRQASSCTLTQLTKLVPEVIGREIEKSTQGIYPLQNVHIRKVKLLKSPKFDLGALLALHGEASTDDKGQKVEREFKEKVLESV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family."}
{"protein": "MSDEASAITSYEKFLTPEEPFPLLGPPRGVGTCPSEEPGCLDISDFGCQLSSCHRTDPLHRFHTNRWNLTSCGTSVASSEGSEELFSSVSVGDQDDCYSLLDDQDFTSFDLFPEGSVCSDVSSSISTYWDWSDSEFEWQLPGSDIASGSDVLSDVIPSIPSSPCLLPKKKNKHRNLDELPWSAMTNDEQVEYIEYLSRKVSTEMGLREQLDIIKIIDPSAQISPTDSEFIIELNCLTDEKLKQVRNYIKEHSPRQRPAREAWKRSNFSCASTSGVSGASASASSSSASMVSSASSSGSSVGNSASNSSANMSRAHSDSNLSASAAERIRDSKKRSKQRKLQQKAFRKRQLKEQRQARKERLSGLFLNEEVLSLKVTEEDHEADVDVLM", "text": "SIMILARITY: Belongs to the FAM199 family."}
{"protein": "MFSAQNKIHKDKGVAPTEFEERVAQAFFDLENTNQELKSDLKDLYINQAVSMDIAGNRKAVVIYVPFRLRKAFRKIHSRLVRELEKKFSGNDVIFVATRRIMRPPKKGSAVQRPRNRTLTSVHEAMLEDVAYPAEIVGKRTRYRVDGTKIMKVYLEPKERNNTEYKLETMVGVYRKLTGKDVVFEYPVADP", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS7 family."}
{"protein": "MRRPVPYHRVAAIMTILSLAGAGHQARLDARGGMLTGPTANLAPGHVQANLAILPQAVAGDFLRFCQRNPKPCPLLAVSEPGDPSLPELGLDIDIRTDVPRYRVWRDGKLVDEPLDVRGLWRDDLVAFLIGCSFSFEEAMLENGLPVRHIEQGCNVPMYRTNIATHPAGPFSGPLVVSMRPLKAADAIRAIQVTSRFPSVHGAPVHLGDPALIGIADLGRPDYGDAVEIRAGEIPVFWACGVTPQSVVAAVRPEFCITHAPGHMLVTDLLNSRLAAF", "text": "SIMILARITY: Belongs to the D-glutamate cyclase family."}
{"protein": "MIRTPTRTKTKSYNGSQSEFRFPDVEVLAHLKLPEHGLNNHHLLNEQLNKKPEDDIHSQHLSDYTTTNSNSGNSSNGYYSFANISDNTTNPDKLSAVKNTACAIGNNRYSYISSSGSSVHYPGTLAPDRTPRICPTNSPEFGRPLDGNFDMQCIPEAYSTVTSDFTLPTADNISFQFTLSSGNSTAMLKKRSTPSTKTRNATNLSEKRKSSVKRSTSTVSRRSNIKRSNAIRCKGGLLHYFTKLGKRVRLNLKKFHLALKRKLFTYKQRHFAKSDKRTTSHLLRSNGYFANIKRSQSMRSMASYSDTSSPTVPSGLDIKNTPIVKHSSNINHRSLRRTPSSIKRAASILTSSNSLIFSRSNSSVGRTDSTRLVRSQPSLNLNLAVRQPSIVVKNKVIPLSQFDHDDYCIREEDEDEEDEDEYIIDTQKMQPLKSEMGSITSSLHDGDSVFEDAMSSSASMESLSESVKILNANKAWDSYLRAVISQRILMRLQVAKFQASQDHHTYKELLDAIVTDYESDAIFSNNDAQTENDSMSECDSPHEFDTLTDSSRSTPAVVPQSLRESFSSLANFQTSVKAGVRRNLTLPVGISI", "text": "SUBCELLULAR LOCATION: Bud neck. SIMILARITY: Belongs to the AIM44 family."}
{"protein": "MGGQKIVLLSIFVCFYVFSLVSCTEFEAGGENGWIIPQSSNQSDIFNQWASKNRFKVGDTIRFKYKKDSVLVVTEDEYKKCQTTKPELYSNHDDTVFKLDRPGLFYFISGVSGHCEQGQKMIIKVMEVESTPQSPPPSSSLPASAHKKNHAVRKTSRFLGAGLVTISILVITVFSLV", "text": "FUNCTION: May act as a carbohydrate transporter. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the early nodulin-like (ENODL) family."}
{"protein": "MFARDLAECEKTERRVVSPDGNWESTRLLLKEDNMGFSFHITTIYEGKDFDMHYQNHLESVYCISGEGEVESRETGQKHHIKPGVVYVLDKHDAHTLRAFKELKLACVFNPPITGKEVHNSEGAYEILE", "text": "FUNCTION: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma- diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4- pyrimidine carboxylic acid), which is an excellent osmoprotectant. SIMILARITY: Belongs to the ectoine synthase family."}
{"protein": "MAAACRCLSLLLLSTCVALLL", "text": "SIMILARITY: Belongs to the NPY family."}
{"protein": "MSAKAAEGYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQVSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIVGRQIILGKTEIRIKHAERKEYMTVVSRKSWPAATLGHSKLFKFVLYEDWGGFRIKTLNTMYSGYEYAYSSDQGGIYFDQGTDNPKQRWAINKSLPLRHGDVVTFMNKYFTRSGLCYDDGPATNVYCLDKREDKWILEVVG", "text": "FUNCTION: Pore-forming toxin that defensively acts against parasitic microorganisms by forming pores in sphingomyelin-containing membranes (PubMed:9478988, PubMed:12676961). Has hemolytic activity and is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells (PubMed:10684578). Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction (PubMed:9210594). It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10- fold more effective than lysenin-related protein 1 (PubMed:15274631). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Forms a beta-barrel pore in the membrane. SIMILARITY: Belongs to the lysenin family."}
{"protein": "MNKKSPDTEKVSNYDYLEKMNTFELLSNINKEDHTIAENVKKQIPSIEKLVDEIIPRIDSGGRLFYIGAGTSGRLGVLDASECPPTFGVSPGIVIGLIAGGDTALRNAVENAEDDTNQAWKDLQEYDISEKDVLVGIAASGTTPYVIGGIKDARNNGIITGCITCSSGSPLAEASEYPIEVVTGPEFVTGSTRMKAGTAQKLVLNMISTSVMIKLGRVKGNKMVDMQLSNDKLVGRGIRMIMEDLNIEKEQAEKLLLEHKSVRKVLDAHKNERN", "text": "FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate. SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily."}
{"protein": "MSKGGEHKRVTLTSIIQGDAGFSRFGSNILEPDAASAAPDNSSKPTTKTAKCIRIKLDLFETDSNKYPEFNYSRLLYLEKKKTKKLKQVSTTNGSASTDPFADNDDDVARIVKELEAKYGNSYATGRGKSKKDDYRDIGMGYDESDSFIDNTEAYDEIIPEEAETLEGGFYINCGALEFKNLTKKSYTTRTDAIIKMPERSRKRMVSSSSESSSSSSGDDDENDDGNNEEDDESDSEDDSEENDESDSEDDSESESLEDEDSAATAKSSSKYKDNHQAKRAKVIVTGKSKPSSSSLTSGKKPPTKPITTSSSSNSPRPSTVEISDTEDGQDPIQTQPSSQLQSLPQSQAQAQALKKVVKTTTVKDMLKAKRDSFLKSQSGTAAVKGVGNGELKCVSTDVSSSDSSDMESEHGRADRQAGQHGKDGQENLRTADTLLPTTLDADIVTAVNSFKEAVKSRDMCGKKFNLDVKLSPLLLRVYEAVLCTDRNERNMVFSHIEYQLQLPKYYMLRKGKQVRAKEEKRKSTIMLEKLRRAVAVVMPKAVANYETELRTFAEQAAADVNSELPPKMPRKKFQWTSELRHLLYDVYQARWTSYAFLAKRKESLEEFINWYLKEKVVELWPPGWMRLDELQREITRYKNAKLKAKEKPKAPPASASPKPVGVVSAPEQMPPASSYLKAVEDPRSRGNSDTDSATSASSNSLKRKLKEMPKQTSKPPKKKVAKQVPLQPQLTPHPQFQLAPAATAAVSIPAISNNNNHLPHLDTLLSMPSTSAQAAALNAAAVAAASTVLDLASPSRKIDLNTSNNFYNLITAASLAASGNPSPHSGDGQAKVIVGARPSPHVINLDDYQCTSDILQTSKQLAATTTVITAISKAAQTTSVARESSSESDGVEIVGVFPASKPQKKVQSKPKNKTQNRGRSSLGAVGQVNGSLGYSANNMYIYNSPRTLGPVYDLTDPHIMKTMSNLKEMEKQFIQAAFSPNSVKGASGGMGSSAPSTPTRQ", "text": "FUNCTION: May play a key role in egg organization. May be a transcriptional regulator having a role in chromatin remodeling in concert with Hira, a histone chaperone. Involved in chromosome segregation by affecting kinetochores function in the first meiotic division. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Chromosome. Chromosome, centromere, kinetochore. Note=Abundant in the nucleoplasm. Only a fraction of the protein is associated with the chromosomes. Localizes to the chromosome arms and coexpresses with cid at the centromere."}
{"protein": "MAPAPAVLTRLLCAGVRRWPGFLQKAIPGPAEQNGRKVTGAPVPAVSEPQDGDDFQSRILDTPLQHSDFFNVKELFSVKSLFEARVHLGHKAGCRHRFMEPYIFGNRLGQDIIDLDQTALNLQLALNFTAHVAYRKGIILFVSRNRQFSHLIETTAQACGEYAHTRYFKGGLLTNAQLLFGPSVRLPDLIIFLHTLNNVFEPHVAVRDAAKMNIPTVGIVDTNCNPCLITYPIPGNDDSPQAIQLFCKLFRTTINRAKEKRRQMEALHRLQSPKGSEGSGTSPVPDKSHSP", "text": "FUNCTION: Required for mitoribosome formation and stability, and mitochondrial translation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MFLRHCITFTLIALLAGCAGFGSREALQGHGDPQQWRAHKEQLSSLDGWQINGKVGIRAPRDSGSGTLFWLQRQDYYDIRLAGPLGRGAARLTGRPGGVVLEVANQGRYEATSPEALLEEQLGWQLPVSHLVWWVRGLPAPDSKSKLTLDGDSRLASLDQDGWQVQYLSYTEQNGYWLPERLKLHGKDLDVTLVVKDWQPRQLGH", "text": "FUNCTION: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the LolB family."}
{"protein": "MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNAMAKVQIFEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHILAIATKDVRIFTLKPVRKELTSSGGPTKFEIHIVAQFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILKGNGSPVNGSSQQGTSNPSLGSTIPSLQNSLNGSSAGRKHS", "text": "FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. FUNCTION: As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1 (PubMed:25457612, PubMed:27487210). SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore Nucleus, nuclear pore complex Lysosome membrane. SIMILARITY: Belongs to the WD repeat SEC13 family."}
{"protein": "MGRGRGVSSGGGQSSLGYLFGGGETAPAAKAKPAAAAEKETTPAPVKKAAVAAAASPSAAEKMKEIPAGIQSTQANNYFRAQGQNCGNFLTDRPSTKVHAAPGGGSSLGYLFGGK", "text": "FUNCTION: Acts in maintaining the cortical microtubules organization essential for anisotropic cell growth. SIMILARITY: Belongs to the SPIRAL1 family."}
{"protein": "MSMEDPFFVVKGEVQKAVNTAQGLFQRWTELLQGPSAATREEIDWTTNELRNNLRSIEWDLEDLDETISIVEANPRKFNLDATELSIRKAFITSTRQIVRDMKDQMSASSVQALAERKNRQALLGDSSSQSWNAGVADRYGRLDRELQLANSHFIEEQQAQQQLIVEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAKVSHMTSDRRQWCAIAILFAVLVVVLILFLVL", "text": "FUNCTION: SNARE promoting movement of transport vesicles to target membranes. Targets endosomes to the trans-Golgi network, and may therefore function in retrograde trafficking. Together with SNARE STX12, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV membrane protein Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein Recycling endosome membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family."}
{"protein": "MLKIAFATGDGTAVDQHFGWCRRFDVYEVGPEGSHLFETRLLEAASDDEQDKIESRLAAVTDCVILNIGDIGGTAAAKVVKAKIHPVKVAKGTSVEDLLTRYVRDAGRDPPPLVRKVLKAREPQPAAQSWTRSVAAELKGDAA", "text": "SIMILARITY: Belongs to the NifX/NifY family."}
{"protein": "MSLSIDVTSLPSISSNIFKNESSSTTSTLSGKSIGRNEQYVSSDIEAFNKYMLSKSPEDIGPSDSASNDPLTSFSIRSNAVKTNADAGVSMDSSTQSRPSSNVGCDQMDFSLTKGINVSASLDSCVSISTNHKKEKSKKDKSRKHYPRIEADSDSEDYVLDDSDSDDGKCKNCKYKKKYFALRMRMKQVAMQLIEDL", "text": "FUNCTION: Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viroplasmic proteins such as capsid proteins to these factories. SUBCELLULAR LOCATION: Host cytoplasm Note=Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus NSP5 family."}
{"protein": "DTHGLPIERAVEKELSKKKIRKESLPKTEFRKLCREYANRYVNIQKEEFIRLGVLGDWENPYLTMSPEYEATEIRELGKFFEKGLAYRSKKPVYWCIYDKTAEGQAEVEYYEKEDPSIYVKFPLKKEIEGKKAYAVIWTTTPWTLPANLGIMVKEDADYSLVEVEGEVWIVAKELLENFFKNIGKTYTRVLKDVKGRDLVGLEYEHPFVDRDELKGYLSEETLKNMWRIYPSEFVSLDTGTGLVHMAPGHGQEDYTVGKRYNLEPYAPLDDSGRFVEPAPEFIRGVRVFDANKLIIALLKEKGYLVHEARIRHSYPHCWRCKNPVIFRATPQWFIGMDIEYEGKTLSGESLEEIEKVKWIPEYGKNRIKSMVENRPDWCISRQRFWGVPITVFYCENCGEVIKDKEVFERIASLVEKHPGGTDVWFEKSPEEILPEGYKCPKCGGTSFRKEEDILDVWFDSGCSHASVIRPLGFEKADLYLEGSDQHRGWFQASLLESVGSYGEAPYRSVLTHGFIVDEQGRKMSKSLV", "text": "FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily."}
{"protein": "MFVSRLAASGLLLLALLAVSLDGKPLQQWSQRWPHLEIPPLVVQNWKSPTQLQARESPAGGTTALREELSLGPEAALDTPPAGPDGGPRGSKAAAAAPQRLSKSKGASATSAASRDLRTDGKQARQNWGRLVSPDHHSAAGGGGGGGGGARRLKGLAKKRAGNGCFGLKLDRIGSMSGLGC", "text": "FUNCTION: Bradykinin-potentiating peptide both inhibits the activity of the angiotensin-converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent (By similarity). FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). FUNCTION: Bradykinin inhibitor peptide antagonizes the vasodilatory actions of bradykinin at the B2 bradykinin receptor (By similarity). Has no demonstrable hypotensive activity when injected intravenously in rats. SUBCELLULAR LOCATION: Secreted. SIMILARITY: In the N-terminal section; belongs to the bradykinin- potentiating peptide family. SIMILARITY: In the C-terminal section; belongs to the natriuretic peptide family."}
{"protein": "MSELEKAVVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDSDGDGECDFQEFMAFVAMITTACHEFFEHE", "text": "FUNCTION: Small zinc- and- and calcium-binding protein that is highly expressed in astrocytes and constitutes one of the most abundant soluble proteins in brain (PubMed:6615778, PubMed:3722149). Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer (PubMed:6615778, PubMed:3722149). Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites (PubMed:3722149). Acts as a neurotrophic factor that promotes astrocytosis and axonal proliferation (By similarity). Involved in innervation of thermogenic adipose tissue by acting as an adipocyte- derived neurotrophic factor that promotes sympathetic innervation of adipose tissue (By similarity). Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase (PubMed:14661952). Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization (By similarity). May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Secreted Note=Secretion into the medium is promoted by interaction with isoform CLSTN3beta of CLSTN3. SIMILARITY: Belongs to the S-100 family."}
{"protein": "MSHHGPRLSTRSQQIVAGYASVAANFDVEKLHREQGVNIPTSGASINQCPHAAAARAAARMADDLASAARAKKSLDAKGSLAGRPVHHKAATESTKAKHTGFDYEAFYKGELAKKHQDKSYRYFNNINRLARKFPVAHTANPRDEVEVWCSNDYLGMGNNPVVLETMHRTLDKYGHGAGGTRNIAGNGAMHLGLERELRLHRKEAALVFSSCYVANDATLSTLGTKLPGCVIFSDTMNHASMIQGMRHSTPKRVIFKHNDLEDLETKLQQYPKETPKIIAFESVYSMCGSIGPVKEICDLAEQYGAITFLDEVHAVGLYGPRGAGVAEHLDYDAHLAAGSSPDPIPGSVMDRIDIITGTLGKSYGAVGGYIAGSEEFVDMIRSYAPGFIFTTSLPPATVAGARASIVYQSEYLGDRQLKQINVREVKRRLAELDIPVVPGSSHIVPVLVGDAALARAASDKLLSEHDIYVQAINYPTVARGEERLRITVTPRHTMEQMEGLIRSLNQVFEELNINRLSDWKLAGGRAGVGIPGAADDVQPIWTDEQIGLLNGTAPRSLRNAEKSVVDMRAVTIARSRFDVLLGPVYGELQPTEDFDTPAVGATFKAPLVDREVAHDITVSA", "text": "FUNCTION: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MSHGTYYECEPRAGQQPLEFSGARAGPGELGDMCEHEASIDLSAYIESGEEQLLSDLFAVKPAPEARELKGPGTPAFPHYLPADPRPFTYPPHTFGPDRKALGPGIYSSPGSYDPRAVAVKEEPRGPEGSRGASRSGYNPLQYQVAHCGQTAMHLPPGLASPSQPLRVLKAPLAAAAPPCSPLLKAPSPAGPSHKGKKAVNKDSLEYRLRRERNNIAVRKSRDKAKRRILETQQKVLEYMAENERLRSRVEQLTQELDTLRNLFRQIPEAANLIKGVGGCS", "text": "FUNCTION: Transcriptional activator. C/EBP are DNA-binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Required for the promyelocyte-myelocyte transition in myeloid differentiation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. C/EBP subfamily."}
{"protein": "MGQKSNPNGLRLGIIRTWESKWYDVDKKVPFLVGEDFKIRPLIKNHYPKSTISQIEIKRLKKSNDEFIEIDLYTSKIGIIQGPENKNKNSLINKIEKLINKKVQINIFEVKAINKIAVLVAQNIAMQLQQRAFYKAVLKSAIQKALKSGVKGIKIIITGRLGGAEKARRDSISMGVVPLNTLRADIDYAFEEAHTTYGVLGVKVIINHGEVLPNKTIADTRQIFSSQYENKKNNNKRHFADKKNFKKSTS", "text": "FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
{"protein": "MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQEVFIKAAIETKADAILLSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE", "text": "FUNCTION: Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family."}
{"protein": "MTRSKSTTETTRAARQARIVAILSSAQVRSQSELAALLADEGIEVTQATLSRDLEELGAVKLRGADGGVGVYMVPEDGSPVRGVSGGTARLSRLLSELLVSADASANLAVLRTPPGAADYLASAIDRAALPYVVGTIAGDDTVFVAARDPMTGAELADTLEKLT", "text": "FUNCTION: Regulates arginine biosynthesis genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArgR family."}
{"protein": "MAFFTPWKLSSQKLGFFLVTFGFIWGMMLLHFTIQQRTQPESSSMLREQILDLSKRYIKALAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVNGTGANSTNSTTAVPSLVSLEKISVADIINGVQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDGTSCSFFIYLSEVENWCPRLPWRAKNPYEEADHNSLAEIRTDFNILYSMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKILVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFKKTLGPSWVHYQCMLRVLDSFGTEPEFNHASYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFSPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNREEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQENQLICEPSFFQHLNKEKDLLKYRVTCQSSELYKDILVPSFYPKSKHCVLQGDLLLFSCAGAHPTHQRICPCRDFIKGQVALCKDCL", "text": "FUNCTION: Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides (PubMed:8910328). Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2. Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration. MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N- glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity). Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (By similarity). FUNCTION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-N- acetylglucosaminyltransferase A]: Promotes proliferation of umbilical vein endothelial cells and angiogenesis, at least in part by promoting the release of the growth factor FGF2 from the extracellular matrix. SUBCELLULAR LOCATION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta- N-acetylglucosaminyltransferase A]: Secreted. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 18 family."}
{"protein": "MQQSLAVKTFEDLFAELGDRARTRPADSTTVAALDGGVHALGKKLLEEAGEVWLAAEHESNDALAEEISQLLYWTQVLMISRGLSLDDVYRKL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family. SIMILARITY: Belongs to the PRA-PH family."}
{"protein": "MRDYTKQYINGEWVESNSNETIEVINPATEEVIGKVAKGNKADVDKAVEAADNVYLEFRHTSVKERQALLDKIVKEYENRKDDIVQAITDELGAPLSLSERVHYQMGLNHFVAARDALDNYEFEERRGDDLVVKEAIGVSGLITPWNFPTNQTSLKLAAAFAAGSPVVLKPSEETPFAAVILAEIFDKVGVPKGVFNLVNGDGAGVGNPLSEHPKVRMMSFTGSGPTGSKIMEKAAKDFKKVSLELGGKSPYIVLDDVDIKEAAKATTGKVVNNTGQVCTAGTRVLVPKKIKDAFLAELKEQFSQVRVGNPREDGTQVGPIISKKQFDQVQNYINKGIEEGAELFYGGPGKPEGLEKGYFARPTIFINVDNQMTIAQEEIFGPVMSVITYNDLDEAIQIANDTKYGLAGYVIGKDKETLHKVARSIEAGTVEINEAGRKPDLPFGGYKQSGLGREWGDYGIEEFLEVKSIAGYFK", "text": "SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MDDMMRAMDCLNMAATLRNAALASATCTGRTLGEDREPIWVEGSRKTPEPPLPEESPAPEPNNEIPLLPKIDFEPNISCFPDLQAINASIVRRELEEEGKRCVRQQLKAIRDKQDAMRLSRETQQRKEERQRDQLQQKALRERNESLLIQKADQMTAAQLEAQQREQLALRQQIDQKLHKLALEGVSRCQRRFNQKYEGIAKILLSLNPETVKVCAAQNTQLKELGQKFEQLVSSVKMGNCEMQSQFLCSIIKAEEFCKSLDALELDIIKQLAEFSEQIQQQLKMEAAKKLEDERQRQQQQEEERQKLEEQQKLEEQEKLRKEKEESAAKEKQQEAETAKADAANVPAPLEPKSQDVPPAATATSTSVHPDRLKFYNDILALYQSKVDAVKPLQTEESLKQYRTGCQRAINLPLNAISAVSPQHLAQNFDKLYSFFAGQPTKVMNGTITINDHPLARDYCMLLMAKKFVSQTETAICSNPQAAFPFASVIITFWKLLPDFGKVFLAYMYKESPFLVPYVIPQQQGQTPEQYLKTIGYRLTDKNELEKPDIYLKRQTGLARLYAAVIISQGRKAAGPDECFELNEGWLWLAHMVHVKPLPDISATLIMEILQTLGFELWRTYGKQFVKLLVYIQNIYMPQLAAYDEGGPKTRLEMLLAKFLRERQIAQAVGVLPPGFW", "text": "FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nuclear pore complex. SIMILARITY: Belongs to the GLE1 family."}
{"protein": "MDIDAEDATKSGLHPIELCVYSLLSGNLESIYQSINELRESQAVLILRLKQLRETCKDEQDRINKYCSLNAEIERLDKLETKVDVVLKRYEKMVGSISE", "text": "FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex involved in endosomal cargo sorting. SUBCELLULAR LOCATION: Endosome. SIMILARITY: Belongs to the SNAPIN family."}
{"protein": "MSSNGTDAPAEAQAAMEEPVVQPSVVDRVAGLPLISSTYGMVSAAYTSTKENYPHVRTVCDVAEKGVKTLTTAAVSTAQPILSKLEPQIATASEYAHRGLDRLQESLPILQQPTEKVLADTKELVSSTVSGAQEMVSSSVSSAKETVATRVTGAVDVTLGAVQNSVDKTKSAMTSGVQSVMGSRVGQMVISGVDRVLVKSEAWADNRLPLTEAELALIATPPEDSDMASLQQQRQEQNYFVRLGSLSERLRNHAYEHSLGKLQNARQKAQETLQQLTSVLGLMESVKQGVDQRLGEGQEKLHQMWLSWNQKTPQDAEKDPAKPEQVEARALSMFRDITQQLQSMCVALGASIQGLPSHVREQAQQARSQVNDLQATFSGIHSFQDLSAGVLAQTRERIARAREALDNTVEYVAQNTPAMWLVGPFAPGITEKTPEGK", "text": "FUNCTION: Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets. Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network. SUBCELLULAR LOCATION: Lipid droplet Endosome membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Note=Membrane associated on endosomes. Detected in the envelope and the core of lipid bodies and in lipid sails. SIMILARITY: Belongs to the perilipin family."}
{"protein": "MSEFKNVTLIKKANVYYDGKVTSRTVIFADGTKKTLGIMMPGEYTFDTAAAEVMEMLGGSMEVLLPGAETWQSFHEGQSFEVPANSQFSLKIKEVADYCCSYLK", "text": "FUNCTION: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions. SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family."}
{"protein": "MAATNAVEAGYGGAAENGGCAEGLLGSPMRFSPSSKLKVNHGHFMANINNNAGPGKGGTAAGGTSPTREASYANVSGSGKVIENLHQQVDALTSTNLQLTKQSNQLLEKLEGCNAREAKYLETISSLKHENENLNSMLNRKTRRVKDLDMELVQLRTSHEEATASHNQLKYQLENKFAHETELEQQCQLLQAQYDAVVDAQRRYREHYQKEIEELREALEALKKDNDKFLGEHMARLTRSQLDIDKSMSDYNGKFHRMELSQKEAVIELNEKYDRMRADLDVDGWIVLYKQMRDIAFDYAKQLDLSLPKEFAELHGEDGYYAKMLDEDRQSSPVSTSSTAVEPMSQPSPSMSAQTLSPPPLRVPKNRTPITKRSSFYGNTMPGANISLTSATGLLPGVKRTGSIRSFHGRAPSEGLSDTPTIFTASRNASPMEFPQRSALTSAASANATVRHSSVPRHRRNQSSQVGNNK", "text": "FUNCTION: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into the emerging bud (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SHE3 family."}
{"protein": "MSGGLDILSLKEDDITKMLVATTHLGSENVNFQMEQYVYKRRADGVNILNLGKTWEKLQLAARAIVAIDNPSDIFVISSRPIGQRAVLKFAKYTDTTPIAGRFTPGAFTNQIQPAFREPRLLVVTDPNTDHQPIMEASYVNIPVIAFTNTDSPLRYIDIAIPCNNKSAHSIGLMWWLLAREVLRLRGTISRSVEWPVVVDLFFYRDPEEAEKEEAAAKELLPAPKIEEAVDHPVEETTNWADEVAAETVGGVEDWNEDTVKTSWGSDGQF", "text": "FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Required during oogenesis and imaginal development. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=May associate with nascent RNP complexes within the nucleus. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MSVYTSVSDDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVLKQEELPFFLELNRHLSMKGVAVAAPVARKDGRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMENPRYDAWWTEACARLLPVLSQDDAALLRAEIDALKDNLGNHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLDEALKKAFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLLLSLG", "text": "SIMILARITY: Belongs to the pseudomonas-type ThrB family."}
{"protein": "MGVYIPPGSGGNDNGKSGGSGDNTLTIPNPASFIPQNPSLGLRLWGPLVPASDNLPALYFLTSLQIGIGLLSFNKVRYLRRSNLARFGIENTWQRRSTKWLCAIGGSYLVYQSGIEMSRLAMPYDPWYDEAKFYRKLAIKNGDNPSWWFGATGYYKPMNYKEWYTKIDKWFNNQINIIDAEHENVDTASSQVSTRGKHPQSPLLSSLSRKGKYSEIYQSLHESNIKRYKKLLDQSLKDVNELNKAERLDLIMEGKSSIKYNEEYLKPHIQLGNHRIDTDEEFEMVWLNFEPWDELKMETDYDIRLVPRWRWSEDEDVEASSTESVPTEPTTNLVNEVDESHI", "text": "FUNCTION: Component of the mitochondrial inner membrane i-AAA protease complex required for mitochondrial inner membrane protein turnover. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MGR1 family."}
{"protein": "MRDLKTYLSVAPVLSTLWFVALAGLLIEINRFFPDALTFPFF", "text": "FUNCTION: May help in the organization of the PsaE and PsaF subunits. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaJ family."}
{"protein": "MTINIKYSSKFSSSKTSSSEELKPKTYIPAYYQPPVSMPKYYVNWLRIKLSLNKLKNIRAIYLFDQCQNFNQYQESSRKFSAGQVSSLTPWYSNFSNYSTVILRMKDTSLPPLENPSNGGTYLFNLITVFPSIALSFNYSWRGDTGPSISIFSFSLSVLFFSLFPQHKNICARAWCRPFRRSLSFSLRFIMSSEPASSSTEKVPEEPHPHSIKHKFQGPQFVIPRALSDYVLNVNNQTPESYEKALNAKYGRDDYITLCLHVTSLCTEYGPLDDGPEYVLLCDSRARVDKLIEDLVKLLEIDTDYVQLELHGGKRLHLQKPDAVLRDIAYKQSNEGSDKFFLEMKLVPSESMKAKIMKQEEEEEKARKHGQYQQYQEYHQQHQAMNDGQSSSSVPSTSSPSCSSEANRKEMETVREPAGPSELMRAINAPVAPAPVVIKIETPVALPEEDETLMDDDEMPSLTVEAPSEEASFEAEQPSPQVPQASIEGPSQQQQIPGTSQQKRQVARGSRTNMISYHDLPPGTGNAPPMACPQVTLKLEKNVPFEAKIRAVAGYTRKPISEVQKMRPSDLESIFHSICIASVQRIKRRNELVQQLQEINAQSCKSPTMTMNKKFTLAKAYQRVQNEIEKIDREQILPQQYMNMPPMPPQGQQRLPPPAYPPGILPPQQNRQQGVPPQFQRSPQFMIGPDGQRYAHPYMQLPNSNQRARILNTSSVQPSEEVRNRLVKIEAMAMNMAQLNPPRPPPPQPPHRALQGELQFLRPGAPDPCNFRPDSKQTYNNTYVTVASPATLTNSIIPWHFPPYEKSGRLNVSNTIKAINEYRLLCNSRQADPASFLEFYFLGDPMPHFNKILSIADYNMYLSRRRCDEADVKIHRMSHSDQLQLYLLELQSDESNVEKWKTFYRIMQWDLPLNNEFPRILLPSSLDIGRPVVDRKKKSIDQVMNHIHRMHSQRPPSMGNSSTSSEASSTSPTNAATATSSPASNRPTTSTAQPPTLNPT", "text": "FUNCTION: Acts synergistically with sop-2 to maintain the transcriptionally repressive state of homeotic genes throughout development. Not required to initiate repression, but to maintain it during later stages of development. Also required to repress expression of other genes. Binds RNA in a sequence-independent manner. SUBCELLULAR LOCATION: Nucleus Note=Forms subnuclear bodies. Sop-2 is required for nuclear localization."}
{"protein": "MCSNNNTSSGSYGELQLHDESSGSCRKKQKKDKVRRRGPGVAELEKIRLQEEYKPPLSSSPSLPNIDHHHHTLFAPASSVYDLVMTSPNFSFPEKLASTLPVFPISYGSLIPPAPIFQRSQHSLMMNLPNPSPGAGRFYQFIEPPSNQRSCVDSVSQFLEEENKKIFTAKKRPWPFLTDTTKPSVGPTTTSTIIRPDATQNRSMGITPVQETGTTTSNPIAIDSPTSIPRHYPRFIPLGLQYEQQQQKLKDLDETMQWRSKKPFYSFIPSGDPSNDDQEQRPCDLFGSAADHGIDLNLKL", "text": "FUNCTION: Adapter-like transcriptional repressor recruiting TPL/TPR corepressors to inhibit TCP transcription factors (By similarity). May be involved in leaf development."}
{"protein": "MPSIRAPASKQTATLQVAVKCRPLTDSEQRRSRHIIQVIDDKNVVVLDPDLSKDYLELIQNRTKERRYSFDHVYAPGCSNADVYKNISSTIAGVVQGLNATVFAYGSTGSGKTYTMVGTHSDPGLMVLSFRTIFDLVKKDDSKDTFEVSCSYLEVYNEVIYDLLEKSSGHLELREDPVHGIMVAGLRSIKVHSADKILELLNIGNSRRKTESTEANSTSSRSHAVLEITVKRKQKGQYGSQVLRGKLALVDLAGSERASETNNFGQKLRDGANINRSLLALANCINALGKQNKKGLAYVPYRNSKLTRILKDGLSGNSRTVMVATISPADDQYHHTTNTLKYADRAKEIKTHVHKNIGHLDTHVEDYKRMIDNLQVEVSQLKKELAEKEHQLSVKPTEKAADNELSWLNILSQETGENVQERINLQKALFELEETNKRNRMELQHLDDAIARQQVKDKDSAVLQALTSRRQVILDNIRDNDEAGAGYRKDIELNESRKRQLQDMIEEATSNNGNRTYLHILSQYRLLGMTNAELQIEMAMRDQVIYNQRESLRSLWNIIYGTGLNQKQISKLAAKQGLTIEGCPLPVSSPDVTTPPSFSPHGRLSPFMSFPSPQSQPYSPSACFVQHGFSTMSYLRNQHETPTVCRQEHLSSYYMMSECSPFDGDGKQKTNGRSMPYFSTPGKPKEMYNFSPGTESERTPCSKEYPTSYSRNGDSLVQIKVNSLPLYTKTMIGNL", "text": "SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-8 subfamily."}
{"protein": "MAPAAGPRTGKHAKPQRSKTLKRKRGQEELSSLIQRVEDLDLKGIFKSFSDLPLSEPTASGLASSHYKTLTDIQSRAISHALKGRDILGAAKTGSGKTLAFLVPVLENLYRKQWAEHDGLGALILSPTRELAIQIFEVLRKIGRYHTFSAGLVIGGKSLKEEQERLGRMNILVCTPGRMLQHLDQTALFDTYNLQMLVLDEADRILDLGFQQTVDAIIGHLPKERQTLLFSATQTKKVSDLARLSLQDPEYVAVHETASSATPSKLQQHYVITPLPQKLDILWSFIRSNLKSKTMVFLSSGKQVRFVYESFRHLQPGIPLMHLHGRQKQGGRLDIVTRFSQSKHCVLFSTDVAARGLDFPAVDWVIQLDCPEDADTYIHRVGRTARYEREGRAVLFLDPSEEEGMLKRLEQKKVPIEKINIKANKQQSIKDQLQNMCFKDPELKYLGQKAFISYVKSVYIQKDKEIFKLKELKLDEFAASLGLPGAPRIKFIKGDDTKQRKNAPRAAAHLLSDDDDTDEEDGEKKSKKKEEPQVRTKYDRMFERRNQDVLAEHYSKLINDDGTMVAPNAGAGADADEDDDFLSVKRRFDAGDKDLGSSGDEDDESEKGNKKNVKVRREKLLKSKKKLLKFKGKGTKLVYDDEGNPHELYELEDEEQFKARGDAKDQQAKFLAEEAERTRLADMEDKEIAKQKRREKKEKRKARERELLAEAEEEETLVQLPPYEGDQDDEAPRPSKKPKVKFTEANDREEAEPWYKKSKKSSDQAAHTPRQIQTLEDLESLATGLLG", "text": "FUNCTION: ATP-dependent RNA helicase required for ribosome biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal complexes. Required for pre-rRNA cleavage at site A2 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4 subfamily."}
{"protein": "MATDALYNEVAEIIRCVLAKEKSVRNAVYGSSYKNKKALLRLSCESLKFRPVFDEILQDKELKSMKRDANIGGSVELLYVLMYETLVGSGLTRCSQELKSVISRRIQRIKEVEHAMQDEGRGIKAMKEADDGMKKIQIPRYARINTLKWTADEAMKTLETEKWKILGTLKPENFAEMVTKMKDDEVYVDPHVENLIIFAPNIQNFYEYWMVEQRYLILQDKASCLPAFLLNPRPGSQVFDTCAAPGMKTSHAAAIMENQGKVWAMDRAADRVATMKQLLDASKVAIASSFCGDFLKTDVTDKKFSKVKFAIVDPPCSGSGIVKRMDEITGGNAEKERLEKLKNLQAMILKHALKLPGLKRAVYSTCSVHEEENEQVVDEVLLDTYVRQNYVLKKNVLPEWTYRGLKTYEVGEHCLRANPKVTLTNGFFVAVFERVKSSE", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which methylates the carbon-5 position of cytosine 2381 to 5-methylcytosine (m5C2381) in 26S rRNA (PubMed:25635753, PubMed:33289480, PubMed:33283887). Plays a role in the production of mature 5S, 5.8S, 18S and 26S rRNAs and promotes the processing of the internally transcribed spacer 2 (ITS2), which separates the 5.8S and 26S rRNAs on large pre-rRNA precursors (PubMed:33289480). May play a role in the translation of leucine and proline codons (Probable). May play a role in maintaining ribosomal frameshifting in response to osmotic stress (PubMed:30977983). Not required for global translation (PubMed:33289480). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family."}
{"protein": "MEGKDGSIDKGLLQSTELYKYILDTSVYPREEECLKELRALTWTHPRAVMGTAPETGQFMALLLKTINAKKTLEIGVFTGYSLLLTALAIPHDGKITAIDINRDTYEIGLPIIEKAGVKHKIDFIESKALPALDHLLKDGENKESFDFVFVDADKVNYANYHERVLELLRPGGIVVYDNTLWGGTVAMAPDLVAESKLQYRNAAVEFNNFIAADSRVQISQLPVGDGITVCRRK", "text": "FUNCTION: Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:23747095). May also act as a flavone 3'-O-methyltransferase (PubMed:23747095). Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV) (PubMed:23747095). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates (PubMed:23747095). Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates (PubMed:23747095). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family."}
{"protein": "MFLSHPPQVIQPTYHTVNFLPRSPLKPPSCSVALNNPSISSGAGAKISNNQLIQSLCKEGKLKQAIRVLSQESSPSQQTYELLILCCGHRSSLSDALRVHRHILDNGSDQDPFLATKLIGMYSDLGSVDYARKVFDKTRKRTIYVWNALFRALTLAGHGEEVLGLYWKMNRIGVESDRFTYTYVLKACVASECTVNHLMKGKEIHAHLTRRGYSSHVYIMTTLVDMYARFGCVDYASYVFGGMPVRNVVSWSAMIACYAKNGKAFEALRTFREMMRETKDSSPNSVTMVSVLQACASLAALEQGKLIHGYILRRGLDSILPVISALVTMYGRCGKLEVGQRVFDRMHDRDVVSWNSLISSYGVHGYGKKAIQIFEEMLANGASPTPVTFVSVLGACSHEGLVEEGKRLFETMWRDHGIKPQIEHYACMVDLLGRANRLDEAAKMVQDMRTEPGPKVWGSLLGSCRIHGNVELAERASRRLFALEPKNAGNYVLLADIYAEAQMWDEVKRVKKLLEHRGLQKLPGRCWMEVRRKMYSFVSVDEFNPLMEQIHAFLVKLAEDMKEKGYIPQTKGVLYELETEEKERIVLGHSEKLALAFGLINTSKGEPIRITKNLRLCEDCHLFTKFISKFMEKEILVRDVNRFHRFKNGVCSCGDYW", "text": "FUNCTION: Required for the intergenic processing between chloroplast rsp7 and ndhB transcripts (PubMed:14617084). Necessary for chloroplast NADH dehydrogenase-like (NDH) complex-dependent cyclic electron transport around PSI (CET) (PubMed:32978277). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. PCMP-H subfamily."}
{"protein": "MSTISINHVGLLRNPLHGKSKRASINKSWSLCLPRSSSASRLVKPCRVSSKTDTKPAEMTRRSGNYEPSLWDFDFIQSLDNHHPHVKEKQLKREEELIVEVKMLLGTKIEAVKQLELIDDLKNLGLSYFFRDEIKMVLTSIYNNFFENKNNQVGDLYFTALGFRLLRQHGFNVSQEIFDCFKNEKGSDFDETLIGEDTKATLQLYEASFHLREGENTLELARQISTKYLQKKVDEGSINDENLSSWIRHSLDLPLHWRIQRLEARWFLDAYAAREDKNPLIFELTKLDFNIIQATQQEELKEVSRWWNNSRLAEKLPFVRDRVVECYFWAVGLFDGHDYGFQRKVNAAVNILITAIDDVYDVYGTLDELRLFTDVIRRWDTQSIDQLPYYMQLCYLTLYNYVSDLAYNILKDRGINTIPHLHQSWVNTVEAYLKEAEWYESGYAPSLEEYLSIASISIGVIPIVIPLEVSIPNSTFHRRSPFEYHRYDILHLSAMVLRLADDLGTAQYEVETGDVPKAVQCYIKDTNASEEEAREHVRFMIGEVWKELNTAMAESDDCPFTEQGAWAAVNIGRAAQFIYLEGDGHGRFQIHQHMENLFFHPCV", "text": "FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products (PubMed:23246843). Monoterpene synthase which catalyzes the conversion of geranyl diphosphate (GPP) to sabinene hydrate, mainly (Z)-sabinene hydrate and to a lower extent (E)-sabinene hydrate, and the formation of minor amounts and traces of several other monoterpenes (e.g. mainly alpha-thujene, alpha-pinene and myrcene) (PubMed:23246843). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MKNFETMAEQYKTLPCVGQLNDGLLRELKNLCRFTDFPGIRLLTERHRNECLSLIWPKNLWLRLAQPVDVAGYSEQQLAELNDHYQGFKENLCLIGAIQIGRKDVPIFVGKSSRIFCHDLEDDVLYYIAEDFDKFVRFGILGTNVITCSEPVYTRFYYDGPKFEKLETLKDLGLLQEPLNLNSSLRFNRKTALALKALRRNYISMLSELDELARCKTLAEIEHFVSINTGLKLRLETPIFTALILQDRKNIHCGTSDQKRFEEQEALFEKVVVLGFLNISAEDYGLRPILCIGETGAIYYYDWIDKVLTRIADCLLTFARIGFARYCGDFGYDKIGKVTARFGRLSTLGSAPVQQYSWYLSK", "text": "SIMILARITY: Belongs to the herpesviridae US22 family."}
{"protein": "MSVTRLSEPLQNILLQDLRNFYDRASRIATLSVSAIAAIKSAWTRGSPFAAATALYPTNEEGKYVIQAEGIRMEFTNYGGAVTNLWLNNSRGEEVDIVLGLDHARDYEDYPKNPYLNGAIGRYAGFMRGGRFDMDGESYQVATNAHNGSSTFNGGDRGWGRSILDIGSHTENSITFVLFDRSWNGFPGTAASCLTHTVTPYEWRVAFGVTPTKKPGPINMSQQAFFNLDGFKKKNLTGSVPVSDKTVRDHKLHLPLSGLRFETDALGLSTGDILGNPRGSEYDFWSASRRIGDVLEKPYMGICDRCQKRQYHNHNPSGAYDTIFQLGRSQPWNKEDVPAAILSSPESGISMKLYSDQEALHVHTWSQKEFPLKLKKGQGQGMVPQHGGISFEMQDWPDGLNHPEWRRESKTIWGMDGLYTAFSSYRFSVDKTEP", "text": "FUNCTION: Epimerase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells (PubMed:22252016, PubMed:27983606). The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 (PubMed:22252016, PubMed:27983606). Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin (PubMed:27983606). Prefusarielin is oxygenated at C15 and C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme (PubMed:27983606). The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism (PubMed:27983606). SIMILARITY: Belongs to the aldose epimerase family."}
{"protein": "VQVVVLALVAQVTLSQHWSYGWLPGGKRSVGELEATIKMMDTGGVVVLPEETSAHVSERLRPYDVILKKWMPHK", "text": "FUNCTION: Stimulates the secretion of gonadotropins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the GnRH family."}
{"protein": "MTSAMEFRRPVPTDGEAILNALPNPVLLVAPDGRIVDANIAAESFFEISTQFLRRQSLKELVPFGSPLLALIEQVRTSGSPVNEYKVDLGTPRIGGDRQVDLHVAPLTERPGHIVVMLQERTIADKMDRQLTHRSAARSVIALAAMLAHEIKNPLSGIRGAAQLLEQQASSEDRLLTRLICDEADRIVTLVDRMEVFGDDRPVARGPVNIHSVLDHVKRLAQSGFARNVRFIEDYDPSLPPVLANQDQLIQVFLNLVKNAAEAVADLGTDAEIQLTTAFRPGVRLSVPGKKSRVSLPLEFCVKDNGSGVPEDLLPNLFDPFVTTKQTGSGLGLALVAKIVGDHGGIIECESQPRKTTFRVLDADVQRRQATRPKQPR", "text": "FUNCTION: Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MTSREDLVYLSKLAEQSERYEEMVQYMKQVAEMGTELSVEERNLISVAYKNVVGSRRASWRIISSLEQKEQAKGNTQRVELIKTYRAKIEQELSQKCDDVLKIITEFLLKNSTSIESKVFFKKMEGDYYRYYAEFTVDEKRKEVADKSLAAYQEATDTAASLVPTHPIRLGLALNFSVFYYEIMNDADKACQLAKEAFDEAIQKLDEVPEESYKDSTLIMQLLRDNLTLWTSDMGDDE", "text": "FUNCTION: Probable adapter protein. SIMILARITY: Belongs to the 14-3-3 family."}
{"protein": "MKMRPRYSVIASAVSLGFVLSKSVMALDRPDTGSLNRELEQRQIQSEAKPSGELFNQTANSPYTAQYKQGLKFPLKQVQILDRNNQEVVTDELAHILKNYVGKEVSLSDLSNLANEISEFYRHNNYLVAKAILPPQEIEQGTVKILLLKGNVGEIRLQNHSALSNKFVSRLSNTTVNASEFILKDELEKFALTINDVPGVNAGLQLSAGKKVGEANLLIKINDAKRFSSYVSVDNQGNKYTGRYRLAAGTKVSNLNGWGDELKLDLMSSNQANLKNARIDYSSLIDGYSTRFGVTANYLDYKLGGNFKSLQSQGHSHTLGAYLLHPTIRTPNFRLSTKVSFNHQNLTDKQQAVYVKQKRKINSLTAGIDGSWNLIKDGTTYFSLSTLFGNLANQTSEKKQYTKEDFQPQSHFTVYNYRLSHEQILPKSFAFNIGINGQFADKTLESSQKMLLGGLSGVRGHQAGAASVDEGHLIQTEFKHYLPVFSQSVLVSSLFYDYGLGKYYKNSQFLEKGVKNSVKLQSVGAGLSLSDAGSYAINVSVAKPLDNNINNADKHQFWLSMIKTF", "text": "FUNCTION: Likely functions in the release of soluble HxuA from the cell. FUNCTION: Probable member of a two partner secretion pathway (TPS) in which it mediates the secretion of HuxA. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the TPS (TC 1.B.20) family."}
{"protein": "MSKAQAVRRIGILGGTFDPVHIGHLRSALEVAELMGLDELRLLPNARPPHRDTPQVAAQDRLAMVREAVQGVACLSVDARELERDKPSYTIDTLESIRAELAGNDQLFLVLGWDAFCGLPAWHRWEELLQHCHILVLQRPDADVEPPDELRNLLAARSESDPTAMSGPAGNISFVWQTPLAVSATQIRQLLASGKSVRFLVPDAVLAYIEAHELYRAPN", "text": "FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). SIMILARITY: Belongs to the NadD family."}
{"protein": "MGDLARLPLLEKAPTTHARLLAWVEEVAELTQPDRIHWVDGSEAENKKLTDELVEAGTLKRLNPETFPNSFAAFSDPADVARVEEQTFICSENERDAGFTNNWMAPAEMKQKLRGLFAGSMRGRTMYVIPFVMGHLDAEDPKFGVEITDSAYVVASMRIMARIGTDVLDRITQTDAFFVPALHSLGAPLEAGQADVAWPCNTDKWIVHFPEERSIWSFGSGYGGNALLGKKCYALRIASVMARDEGWLAEHMLILKLTSPEQKTYYISAAFPSACGKTNLALLDPTIKGWKVETLGDDITWMRFGKEGELRAVNPEAGLFGVAPGTGWGTNPNAMRAIAKGNSIFTNVALTDDGGVWWEGMTEETPAHLTDWRGESWTPDSDAPAAHPNSRFCTPIDQIDMLAEEYFSPEGVELSAILFGGRRKTTIPLVTEARNWSNGIFMGSTLSSETTAAAAGAVGVVRRDPMAMLPFIGYDAGDYLNHWVNLSAKANPERLPKIFLVNWFRRTAEGGFAWPGFGDNARVLKWAIERLEGKADAVETPIGFVPTGESIDLEGLDMTPAEVESAVRVDPAEWATELASIEEWFANFGESLPAALQSELDGLKTRLG", "text": "FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP] family."}
{"protein": "MACSRPPSQCDPTTLPPGPPAGRWPLPFSRRRREMSSNKEQRSAVFVILFALITILILYSSNSANEVFHYGSLRGRTRRPVNLKKWSFSSAYFPILGNKTLPSRCNQCVIITSSSHLLGTKLGPEIERAECTIRMNDAPTSGYSADVGNKTTFRVVAHSSVFRVLRKPQEFVNRTPETVFIFWGPPNKMQKPQGSLLRVIQRAGLMFPNMEAYAVSPARMQQFDDLFRGETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPDYCSQRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWAQLYGITFSHPSWT", "text": "FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) (PubMed:10702226). Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
{"protein": "MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILTEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD", "text": "FUNCTION: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2- scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross- link repair. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region Mitochondrion matrix Chromosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase. Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner. SIMILARITY: Belongs to the RecA family. RAD51 subfamily."}
{"protein": "MWPLWLLASLLALSQALPFEQKAFWDFTLDDGLPMLNDEEASGADSTSGIPDLDALPPTFSAMCPFGCHCHLRVVQCSDLGLKAVPKEISPDTTLLDLQNNDISELRKDDFKGLQHLYALVLVNNKISRSTRRPSAPDGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLSRVPAGLPDLKLLQVVYLHTNNITKVGVNDFCPVGFGVKRAYYNGISLFNN", "text": "FUNCTION: May be involved in collagen fiber assembly. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily."}
{"protein": "MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF", "text": "FUNCTION: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C- terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts (PubMed:9852112). Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region Note=Colocalizes with PRKCI in the cytoplasm and nucleus (PubMed:15695176). Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (PubMed:19071173). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MERKSNLSLLLLLLVLGMPLVRGSSPLPLVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYKPSGFLKQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPAIACQKVILRIQKYYPNFFGAVICASVNGSYGAACNKLPTFTQFSFMVSNSLHNEPTEKKVDCI", "text": "FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the Ntn-hydrolase family."}
{"protein": "MADTKEMKKILFAPFLDNNPIALQVLGVCSALAVTTKLETAFVMTLAVMFVTAFSNLFVSLIRNHIPNSVRIIVQMAIIASLVIVVDQVLKAFVYDISKQLSVFVGLIITNCIVMGRAEAYAMKSAPLPSFIDGVGNGLGYGFVLITVAFFRELLGSGKLFGVEVLPLVSDGGWYQPNGLMLLAPSAFFLIGFMIWAIRIIRPAQVEAKE", "text": "FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrDE/RnfAE family."}
{"protein": "MEILMAVLAGIIFMAATYLLLSKSLLRVIIGTALLSHGVHLMLLTMGGLKKGAAPILSEHAKSFVDPLPQALILTAIVISFGVTSFILVMAFRAYQELKSDDMDQMRGNDQHE", "text": "FUNCTION: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit C family."}
{"protein": "MLAIFLAALLFGFAFNVSPGAVFSETLRRGLTGGFRPALLVQLGSLIGDAVWALLGLTGLALLLGYEQVRIPLTLACAAYLAWLGVQGLRDAWSPPLAAEDAGEQGRNAFGAGAAISLSNPKNVVYWGALGSALAGIVDGTPNQAQSLVFFAGFMLSSLIWCFCCAALVDWLRRNTSLFWHRVSYAGCGVLLLGLAGLALRGL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Rht family."}
{"protein": "MAFTFAAFCYMLTLVLCASLIFFIIWHIIAFDELRTDFKNPIEQGNPSRARERVKNVERICCLLRKLVVPEYCIHGLFCLMFMCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMFDPVSIMNVDILNYCQKEAWCKLAFYLLSFFYYLYRVGATVRYVSA", "text": "FUNCTION: Regulates the trafficking and gating properties of AMPA- selective glutamate receptors (AMPARs). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cornichon family."}
{"protein": "MVSQALRLLCLLLGLQGCLAAGGVAEASGGETRDMPWKPGPHRVFITQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDLERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETYKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILENRNASKPQGRIVGGKVCPKGECPWQXLLXVNGAQLCGGTLINTIWVASAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYIPGTTNHDIALLRLHQPVVLTDHVVPLCLPERAFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCASVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP", "text": "FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MSNKITILLAVLLAVVACAQAHASHQRRVPYPLPRFLPRPHHTVSNHRIVGGFEIDVAETPYQVSLQRSKRHICGGSVLSGKWILTAAHCTDGSQPASLTVRLGSSRHASGGSVIHVARIVQHPDYDQETIDYDYSLLELESVLTFSNKVQPIALPEQDEAVEDGIMTIVSGWGSTKSAIESNAILRAANVPTVNQDECNQAYHKSEGITERMLCAGYQQGGKDACQGDSGGPLVAEDKLIGVVSWGAGCAQPGYPGVYARVAVVRDWIRETCGV", "text": "FUNCTION: Constitutive trypsin that is expressed 2 days after emergence, coinciding with host seeking behavior of the female. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MAINGRLLCLCLVLGLVFESLGHPSVQEKRAAEDSKPSGERRQTLTTKHEVDCGGIPCQFGCCENDKCRELDCEHYPGIP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the teretoxin M (TM) superfamily."}
{"protein": "MDSDNVDESVGMLDLKTKFDVFIENGDKNLEMDTGTRATTVPNTPTSDTKNSNSHSSVSPLRSFSRRSGTGSSVGSTAGKTNLSPQLLTPVRLNEGEHPLKDIPSANGSNVKSKSNNKSKRRSLIQPITAPISPDHHGNNFSSAGPVASETRKLSGHQRVISNTSMHSRRSSSQSIMNDVSQDGSLGISSLLQSLASKELELLETKQRIEDLRRQLASEENAYNQGALELKSLKEQVSSYLNPTTFGSNNNNHSIQIADGQDYVIDSTTNELIPTISRAESETKLNIPKSSNSISSGNSKIHSRALSNLSPKQEEGQEDEANESIWSKSLSMFTRLDQIIQQEVEKSLNWESSPEPTASTFAPITEEPGQYYDQNSNSFVRESSRQQNSHNSSEANDNSYSSRSIWNFVSEVKTGLLGKPDDELKGSKPQINTKTDSLEFSNASDDANDSPTIEYNIKQFKTRRKVTGDVEVENSSSKLRDVSIGDNVEEDDNENRIRQVNNRRKVVEMIDFN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TDA11 family."}
{"protein": "MGALVIRGIRNFNLENRAEREISKMKPSVAPRHPSTNSLLREQISLYPEVKGEIARKDEKLLSFLKDVYVDSKDPVSSLQVKAAETCQEPKEFRLPKDHHFDMINIKSIPKGKISIVEALTLLNNHKLFPETWTAEKIMQEYQLEQKDVNSLLKYFVTFEVEIFPPEDKKAIRSK", "text": "FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) (PubMed:18179882, PubMed:28853723). May be involved in cell proliferation and survival of hormone-dependent tumor cells. May be a regulator of breast tumor cell invasion. SUBCELLULAR LOCATION: Mitochondrion Membrane; Lipid-anchor. SIMILARITY: Belongs to the NDUFAF4 family."}
{"protein": "RPPGFDPFR", "text": "FUNCTION: Induces relaxation of arterial smooth muscle, by targeting bradykinin receptors (BDKRB). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-related peptide family."}
{"protein": "MLFNEFCKIIEKIENTPKRLEKIDYFVEIIDFVKNHGKPENLKEICQVSIGRVFAEYENREIGIGPNLLIEAIKTTGISENDLNLKIKETGDIGISVEHLSSKIKQISLFNEPLTFEEVYSTIKKLSTIEGTSSQKKKIRIISNLLIIANPIESRYISRLILEDMRIGMNIPTILAAFSNYFGIEKEKIEKVYAVTNDIGLIGKKLLENSNFEEDPELNLTVFRPIKPMLAQLTPSIEEAVIEMKNPQFETKYDGARVQVHKSNGEVKIYSRRLEDITNSVPELVLEIKNLEVDNVILEGECVAMNLENGKPRPFQDILRRFRRKYDIDKMTEEVSLRIYFFDILYHNKGLIDLPLFERRNILENIFGTNNWDLELKKIENEIKSNKMLFTSFKVSSTDLKIAKEFFKWSLSIGHEGIMVKNLNAIYTPGSRVKTMCKIKQTLENLDVVVTRAKIGMGKRKDWYGSYEISVKGDDESLHVIGNVGSGLTEEDLEKLTKIANEIKIEDLGGEVILEPKIVLEVTYEEIQTSEKYEMGYALRFPRVVGIREDKSINDINSLDDVKKIYEIERKRK", "text": "FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
{"protein": "MVVINGVKYACETCIRGHRAAQCTHTDGPLQMIRRKGRPSTTCGHCKELRRTKNFNPSGGCMCASARRPAVGSKEDETRCRCDEGEPCKCHTKRKSSRKSKGGSCHRRANDEAAHVNGLGIADLDVLLGLNGRSSDVDMTTTLPSLKPPLQNGEIKADSIDNLDLASLDPLEQSPSISMEPVSINETGSAYTTTNTALNDIDIPFSINELNELYKQVSSHNSHSQ", "text": "FUNCTION: Trans-acting regulatory protein that activates transcription of the CUP1 gene (metallothionein) in response to copper ions. Binds to the CUP1 UAS sequence 5'-GCTTCTTTTCCGCTGA-3'. Binds DNA only in presence of copper or silver. Copper seems to alter the conformation of the protein. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSTTNTAAASQDACYISLLGLAEYFRTSQPPNVKKCIQCLQALFTFTPPSKVEARTHLQMGQILMAYTKNIDMARQHLEKAWNIAEPLMNFDDVKFDTASVLAQLHLQTDQSSHTAKAMLRRAVELSQHNVYWHCKLLLQLSQIHASDREYSLASELLAVGAESAEEAGATYLKVLFLLSRAMILMIERKTNDVLALLNTAGQIIDNNIPNPHQKEYLKVFFLVLQVCYYLALGQVKTVKPSLKQLQMSIQTIMAPNWPTDEAIFGANQLEMFVWLPKEQLYVLVYLVTVSHSMMAGYMDKAQKYTEKALTQIEKLKMQEDKPILSVFKVILLEHIVMCRMVMGNRELAIREIAAARDVCLAVPHRSLLKRHSAQLHCLIGLYSMSTSFFEHAERQFLVCVNETTERDLKLFANLNLAIIYLRTKRDADLKQILDAVSTENTHTYSSQALMGGFYYVQGLHAFHKNSFHEAKRFLRETLKMANAEDLNRLTSCSLVLLSHVFLSIGNSKESMNMVTPAMQLASKIPDIHVQLWGSAILKDLHRMSKDAQHEKDAYANHVKYSENLIADQRKCVQSAHHELVNWFQGDPPVTSGAAALILSEIPTTSALQPTTGQQFGQFY", "text": "FUNCTION: Required for association of the cohesin complex with chromatin during interphase. Plays a role in sister chromatid cohesion and normal progression through prometaphase (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Note=Binds to chromatin from the end of mitosis until prophase. SIMILARITY: Belongs to the SCC4/mau-2 family."}
{"protein": "MGDREECLSTPQPPMSVVKSIELVLPEDRIYLAGSSIKGQVILTLNSTLVDPIVKVELVGRGYVEWSEEAGASCDYSRNVICNNKADYVHKTKTFPVEDNWLSAGSHTFDFHFNLPPRLPSTFTSKFGHVFYFVQASCMGREHILAKKRMYLLVQGTSTFHKETPFQNPLFVEAEEKVSYNCCRQGTVCLQIQMERNTFTPGEKVVFTTEINNQTSKCIKTVVFALYAHIQYEGFTPSAERRSRLDSSELLRQEANTPVTRFNTTKVVSTFNLPLLLSVSSSTQDGEIMHTRYELVTTVHLPWSLTSLKAKVPIIITSASVDSAICQLSEDGVLPVNPDHQN", "text": "SIMILARITY: Belongs to the arrestin family."}
{"protein": "MMASRLSSFSSSIARWHGDEHAVASPLDDAEILSMRRTRLFGATGTVLMAIGALGAGARPVVQDPTFGVRLLNLPSRIQTVSLTMTTTGAVMMALAWLMLGRYTLGKRRMSRSQLDHTLMLWTVPLLIAPPMYSRDVYSYLAQSEIAVLGLDPYRVGPATGLGLDHVFTLSVPNLWRETPAPYGPLFLWIGQGISALTGENIVEAVMCHRLVVLIGVGLIVWATPRLARRCGVAEVSALWLGPCNPLLFMHLVAGIHNEALMLGLMLAGTEFALRGIDAAQPLLPRPLAWPSSRAQWQRWQPMAMLVLGAVLIAMSSQVKLPSLLALGFVAMALAWRWGGTVKAFVISCTSLGAISLAVMAVIGWASGLGFGWLFTLGTANVVRSWMSPPTLIALGTGQVGILLGLGDHTTAVLGLTRAIGVFMISILVSWLLFAVLRGRLHPVGGLGVALGGTVLLFPVVQPWYLLWAIIPLAAWATRPGFRGATIAITLIVGIFGPTANGDRFTLFQIVMATLASAVTVLLLIALTYRRLPWRPAPEPPARPPEQPAPADDAYAESP", "text": "FUNCTION: Catalyzes the addition of alpha-(1->6)-mannose residue. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the MptA/B family."}
{"protein": "MKPRHIPVFDGHNDALTRLWLSDHPDPVHAFIHERLVGHLDLKRCQEAGFIGGMFAIFLPPYSYVQQHHSNKLFDQNASDFTQQQIEQICLEQLDLAHQLAQYSKNIKICTSVQDIQDCRAEKKLAIVLHMEGAEALQQNPDLLDVFYERGLRSIGPLWNRPSRFGHGLNAKFPHSPDTGAGLTSDGKDFIKRCANKKMVIDVSHMNEKAFWNTVDILQQPIVATHSNSHALCPQARNLTDPQLKAIRESKGMVGVNFDVAFLRSDGQRNADTSIDVILEHLEYLMDRVAPLLHPRSKLRKGTHKRTPGRAGDAD", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family."}
{"protein": "MNKEQLKTPFFMIDEAKLIQNLEIAKQLKEISGVKLVLALKCFSTWGVFDIIKPYLDGTTSSGPFEVKLGYEKFGGETHAYSVGYSEDDVREVADLCDKIIFNSQSQLAAHRHIVEGKASIGLRLNPGVSYASQDLANPARQFSRLGVQADHIDPAVFDSINGVMFHMNCENKDVDAFIALLDSISERFGAYLNKLDWVSMGGGVFFTWPGYDVEKLGLALKAFSEKHGVQMYLEPGEAIITKTTDLVVTVVDLVENGMKTAIVDSATEAHRLDTLIYKEPASVLEASENGEHEYVIGSCSCLAGDQFCVAKFDQPLHVGQRLHILDSAGYTMVKLNWFNGLKMPSVYCERTNGEIQKLNEFGYEDFKRSLSLWSVQ", "text": "FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine. Carboxynorspermidine is decarboxylated 20-fold more efficiently than carboxyspermidine. Exhibits some activity with L- ornithine, but shows no activity with L-arginine, L-lysine or meso- diaminopimelate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. NspC subfamily."}
{"protein": "MSKLRVMSLFSGIGAFEAALRNIGVDYELIGFSEIDKYAIKSYCAIHNVSETLNVGDISKAKKDNIPYFDLLTSGFPCPTFSVAGGRDGMEYKCSNCSHEHLITYEDYKKGVKCPKCEAVSKAKDERGTLFFETALLAEEKKPKFVILENVKGLINSGNGQVLRIISETMNNIGYRIDLELLNSKFFNVPQNRERVYIIGIREDLVENEQWVVGQKRNDVLSKGKKRLQEINIKSFNFKWPLQDTVTKRLREILEDFVDEKYYLNEEKTKKLVEQLGTAPLQKQEVREPLMVGHVDLKGHDAIKRVYSPEGLSPTLTTMGGGHREPKIAEKQKEVRAVLTPEREEKRQNGRRFKENGEPAFTVNTIDRHGVAIGEYPKYKIRKLSPLECWRLQAFDDEDFEKAFAAGISNSQLYKQAGNSITVSVLESIFQELIHTYVNKESE", "text": "FUNCTION: A putative methylase, recognizes the double-stranded sequence 5'-GGCC-3', methylates C-?. There is no known cognate restriction enzyme. FUNCTION: A methyltransferase that methylates C-1 within the sequences 5'-GGCC-3' and 5'-GCNGC-3' (PubMed:12654995). Modification confers resistance against restriction enzymes that recognize these sequences (Probable). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
{"protein": "MASEGPREPESEGIKLSADVKPFVPRFAGLNVAWLESSEACVFPSSAATYYPFVQEPPVTEQKIYTEDMAFGASTFPPQYLSSEITLHPYAYSPYTLDSTQNVYSVPGSQYLYNQPSCYRGFQTVKHRNENTCPLPQEMKALFKKKTYDEKKTYDQQKFDSERADGTISSEIKSARGSHHLSIYAENSLKSDGYHKRTDRKSRIIAKNVSTSKPEFEFTTLDFPELQGAENNMSEIQKQPKWGPVHSVSTDISLLREVVKPAAVLSKGEIVVKNNPNESVTANAATNSPSCTRELSWTPMGYVVRQTLSTELSAAPKNVTSMINLKTIASSADPKNVSIPSSEALSSDPSYNKEKHIIHPTQKSKASQGSDLEQNEASRKNKKKKEKSTSKYEVLTVQEPPRIEDAEEFPNLAVASERRDRIETPKFQSKQQPQDNFKNNVKKSQLPVQLDLGGMLTALEKKQHSQHAKQSSKPVVVSVGAVPVLSKECASGERGRRMSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKERQERKQRLQENAVSPAFTSDDTQDGESGGDDQFPEQAELSGPEGMDELISTPSVEDKSEEPPGTELQRDTEASHLAPNHTTFPKIHSRRFRDYCSQMLSKEVDACVTDLLKELVRFQDRMYQKDPVKAKTKRRLVLGLREVLKHLKLKKLKCVIISPNCEKIQSKGGLDDTLHTIIDYACEQNIPFVFALNRKALGRSLNKAVPVSVVGIFSYDGAQDQFHKMVELTVAARQAYKTMLENVQQELVGEPRPQAPPSLPTQGPSCPAEDGPPALKEKEEPHYIEIWKKHLEAYSGCTLELEESLEASTSQMMNLNL", "text": "FUNCTION: Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion."}
{"protein": "MGYCSGRCTLIFICGMQLVCVLERQIFDFLGYQWAPILANFVHIIIVILGLFGTIQYRPRYITGYAVWLVLWVTWNVFVICFYLEAGDLSKETDLILTFNISMHRSWWMENGPGCTVTSVTPAPDWAPEDHRYITVSGCLLEYQYIEVAHSSLQIVLALAGFIYACYVVKCITEEEDSFDFIGGFDSYGYQGPQKTSHLQLQPMYMSK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NKAIN family."}
{"protein": "MVLTARQQEELQLAVHAYLVEAGHAEAAAAMAKSANLGDDAGDAKYTGLLEKKWTTITRLQKRNMELQAEVEELRSSARAPRSRTTTKMEEWVPRPPATVAVDGHRLPITAVAIHPSFAVMASASEDASIKLWDMESGNFERSLKGHTNAVNDIAYDREGNRLVSCSTDMTIKVWNMDNFTCTKTLSGHDHTVSSVRFDHTGDRVFSASRDKTIKIWELATGYCLQTLQGHSDWVRSIDVSADGAWICSASSDHTVRVWSVASGECKHVWSDHEHVVEHASFAPLVAHEALNLMIFGSKPSAEAASKGPFVASASRDKSICLFDVSTGQHLARLTGHDNWVRATAWSRGGRYLFSVADDKTMRVWDIATKRVSKTIPAHNHFVSCIAVHAKNTHVVTGSVDLKVKVWECN", "text": "FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to the plus end of microtubules and to the centrosome. SIMILARITY: Belongs to the WD repeat LIS1/nudF family."}
{"protein": "MVNFDEEVFRAYYEHKIKSFIKEELSNNLIKGNIFEFDIEKFLMHFPDACEVNDLIIERPKEIEEIILDIFKEAYVELFGEDKELEKIQIAFKNPKGCEKLIEEISAEDINKLVKFEGNILQAGKVNALLKKAVYYCNKRIKDENGGFLCKYTYTPCDGRVEIEIDDYFSEGEFIKDMLSPREVKKILENKKVWDKLVEKGKIPRCVDLKENDEVFKENLKEIKFILDEYDSIYVNIQEMEIQQPIDLMKNPEEPARSIRVFLENTPGIYAGRVNVIGRVMKREYRHNIPIYKIYIKSNYIKISESYNKIEVKDILRNEELIETLNELGRKKNIIDILSNYLISQIKGYELVKKAIFLQQIKGAFKFLPDGTPLRRDSHILLITDPGIGKSTMLRRIARLFPQNAYASVTTATGGGLTAIVTREATEIGDGWVVKPGVFVRANEGTACIDELTVDKNVMKYILEAMESQTIHVNKGGINVKLPARCAVLAACNPKRGRFDRNLTVIEQIDIPAPLLSRFDLIFPLMDKPNRKSDEEIAEHILNTHIETATKDYKILGAIDIDGITVDEKLLKYYIIYARSCAYIEENQDLYLGEFDETKLIMPYLTDKAKKMIKKYYLEMRKLGEGDNPIPITARQLEAIIRIAEMHAKARLSDKVEDVDAEVAISIIDDCLKQVAYDPETGTLDLDKIAGTPKSRRDKMDAVLNIIREIVSLRDDGLAPEEEIYEKAMAIGLSEKDVNDALEYLKKAGDIYNPRYGFWGLL", "text": "SIMILARITY: Belongs to the MCM family."}
{"protein": "MLEGIFDINHIFDENGIKTLKRFGWDGSVAVQNHNEYSEEKINNAVEYGENCEFKVFSGLKLSTKNQNEMEKAVKKYRNKVDILLVEGGEIKINRRVLEMNDVDILSTPELNRMDNGLDHILARLGSTNRVAIELNFGNLLKSRNYDRSKILWAFQRNLKLAKKYDTPVVISSGANDIYGIKAPGDLRGFLNTITDPLYSKKIIETPSKIVDYRLYLKKDNVLTLGIEVVE", "text": "FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 3 family."}
{"protein": "MATEVHNLQELRRSASLATKVFIQRDYSDGTICQFQTKFPPELDSRIERQLFEETVKTLNGFYAEAEKIGGSSYLEGCLACATAYFIFLCMETHYEKVLKKISRYIQEQNEKVFAPRGLLLTDPVERGMRVIEISIYEDRCSSGSSSSGSSSGSGSSSAGGGGAGAR", "text": "FUNCTION: Play a role in cell adhesion by regulating the plasma membrane localization of the palmitoyltransferase ZDHHC5. May be involved in protein transport from Golgi to cell surface. SUBCELLULAR LOCATION: Cell membrane Golgi apparatus membrane; Lipid-anchor. SIMILARITY: Belongs to the ERF4 family."}
{"protein": "MDLQRIYDRRKSRLVDELAIAKYGMLGLMLMENAGRNVAYELLARTPCRRVVIVVGKGNNGGDGWVIARHLDAAGVDVIVLLTTAPNEFRGDAAVNYAIANLAKIKIIDLSRTPTAEAIATHFAEADWLVDAMLGTGATGEPRGAMRLAIEAINQSSVRTLAVDLPTGIDCDSGGAATVAVRADVTCTFVTLKPCCQVAACRSYLGEVRVIDIGVPRALLEEIDAMP", "text": "FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. SIMILARITY: Belongs to the NnrE/AIBP family."}
{"protein": "MSGKLFIILLLLVTPGEARKSFLRFLNIQNPEMLSFTKPEETVIVRSSYEGKRPHSSYLLVKLEDPTVLQVVNVTKTSLDFTDFTINLKTFPGETNLTMQLWESEGRQTRLIEEITNIRVSVFRQTEDSLFQEPIHVNSSVFLLVLLMILLNKCAFGCKIELQVLQTVWKRPLPILLGAVTQFFLMPFCGFLLSQILGLSKAQAFGFVMTCTCPGGGGGYLFALLLEGDVTLAILMACTSTSLALIMMPVNSYLYSCLLGLAGVFHVPVLKIVSTLLFILTPVSIGIVIKHRMPKKAVCLERVVQPLSLTLMLVGVYLAFRMGLVFLRMANLEVFLLGLLVPVLGFSFGYSFAKVYLLPLPVCKTVAIESGMLNSFLALAIIQLSFPQSKAYEASVAPFTVAMCSSCEMLLLLLVYKAKKRPLLSTENEKAPLV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family."}
{"protein": "MLVKVSIHGQEYDLEVQPTDKIQEIKSKINELNGTPVEQIHPYIAGHAMKDGTTISDYPQIVEGSKIQVRVILKSQSDNSEKSEKSGKSEKDCILM", "text": "SIMILARITY: Belongs to the ubiquitin family."}
{"protein": "MLSALGGLQRCFWAILLLALTVSLLAGFLHKDVRLLMPLLKGQAEGPPITNVMFLKTHKTASSTVLNILFRFAETHNLSVALPAGQRVHLGYPWLFLARYVEGVEEGGPEQRFNIMCNHLRFNLPEVRKVMPNDTFYFSILRNPVFQLESSFIYYKGYVPAFRDVVSLEAFLASPGTYYNESQGLRNAYARNGMWFDLGFDNNAPAEDAYVRARLADVERRFQLVLIAEHFDESMVLLRHLLRWRLDDVVSFPLNLRSPGSVTSLTPEGQERAKRWCALDWRLYQHFNRTFWARLRTELGPRRLRSEVAQLQARQRELQALCVQDGAPKNKSQITDLRLRPYQSGEADILGYSLRPGLDNQTVQLCQRMVTPELQYTARLYTQQFPEKPPKNIPFLGA", "text": "FUNCTION: Transfers a sulfate group to the hydroxyl group at C3 of non- reducing beta-galactosyl residues. Acts both on type 1 (Gal-beta-1,3- GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar efficiency (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family."}
{"protein": "MGGSLRVAVLGAPGVGKTAIIRQFLFGDYPERHRPTDSPCLYRPAVLLDGAVYDLSIRDGDVAGPGSSPRSLEEWPDPKDWSLQDTDAFVLVYDICSPDSFDYVKALRQRIAENRPAGAPEAPILVVGNKRDRQRLRFGPRRALATLVRRGWRCGYLECSAKYNWHVLRLFRELLRCALVRTRPAHPTLRLQGALHPARCSLM", "text": "FUNCTION: Potent inhibitor of cellular proliferation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Nucleus, nucleolus Note=May cycle in and out of the nucleolus in a GTP- dependent manner. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
{"protein": "MDSPSSVSSYSSYSLSSSFPTSPVNSDFGFPSDSEREDKGAHGPRPDTVGQRGGSRPSPGPIRCRHRSKVSGNQHTPSHPKQRGSASPMAGSGAKRSRDGELETSLNTQGCTTEGDLLFAQKCKELQGFIPPLTDLLNGLKMGRFERGLSSFQQSVAMDRIQRIVGVLQKPQMGERYLGTLLQVEGMLKTWFPQIAAQKSSLGGGKHQLTKHFPSHHSDSAASSPASPMEKMDQTQLGHLALKPKQPWHLTQWPAMNLTWIHTTPICNPPLSSPGTISFSHGPLGTGTGIGVILFLQHGVQPFTHSAPTTPVPPTTASPVIPGEPMKLSGEGPRCYSLPVTLPSDWSYTLSPPSLPTLARKMTIGHREQQRSHPPVAADAHLLNL", "text": "FUNCTION: Transcriptional repressor which forms a negative regulatory component of the circadian clock and acts independently of the circadian transcriptional repressors: CRY1, CRY2 and BHLHE41. In a histone deacetylase-dependent manner represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Abrogates the interaction of BMAL1 with the transcriptional coactivator CREBBP and can repress the histone acetyl-transferase activity of the CLOCK-BMAL1 heterodimer, reducing histone acetylation of its target genes. Rhythmically binds the E-box elements (5'-CACGTG-3') on circadian gene promoters and its occupancy shows circadian oscillation antiphasic to BMAL1. Interacts with the glucocorticoid receptor (NR3C1) and contributes to the repressive function in the glucocorticoid response (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, PML body Note=Co-localizes with the CLOCK-BMAL1 heterodimer in the PML body."}
{"protein": "MFNWRAIYNKILYLLLKIVVRSHIIPPKLLAEICLDIQEPMMYVLPYNSKCDLLTLRILCIQYQLPDPLKPIFIXGVRFPRYLFIDQSCHIRSDVTKQQQYGRILHNFITLYRHNSCSNIQILPVWVMFGRCPGKESYKNKKTTSIQFFCLLKKIINVIWLGRDSFIYFSPIGSIPISYIANSNYTINSIMILKLFRLGRIHFLRQKRIAIGPSLLVRKHLFEKLLASQTITKLVEDEARSKKISIKQAQQKALVIIEEIAADFSYETIRLSDRVLSWIWNMLYQGLYVCNADRVRKLAEKGHEIIYLPCHRSHMDYLLLSYILYHEGLVIPYIAAGINLNFWPAGQIFRKLGAFFIHRTFKGHQKLYSAIFREYLYQLFNGGYSVAYFLEGSRSRTGRLQAPKTGTLTITIQSMLHLGKKKPIILVPVYISYEHVIEVASYTKELYGVVKKKEGLIHMISGLRNLRNLGRGYINFGEPLPLLTWLNQQVPQWQDDINSIEGNRPNWLALTVDYLAVTIMTRINNAVAVNAMNLCSSIILASRQYSCSSIVITRTRLLSQLKCYLELLRNVPYDAEVTVPNVTPEDLFQHLITLNQFTIKNNSIIYVSSEKTALITYYRNNIQHLFILPSLLAIIIIAQPGISRKLIHQKLLSLYPLLKVELFMRFSYQELPHVIDLMITELHRQDILYEQQTKIYPVPKRMDELQLLAASGGRETLYRYAITFSLLCSYTRINRYSLEKQSIIIAQHLSKIHSIYALEFIDKTIFSTLITTLRHEGYLSDSGEIHASQAKEIYKFLSALISPEIQTSITNALYHIKTVVN", "text": "SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family."}
{"protein": "MKEKIVIALGGNAIQTKEATAEAQQTAIRRAMQNLKPLFDSPARIVISHGNGPQIGGLLIQQAKSNSDTTPAMPLDTCGAMSQGMIGYWLETEINRILTEMNSDRTVGTIVTRVEVDKDDPRFDNPTKPIGPFYTKEEVEELQKEQPGSVFKEDAGRGYRKVVASPLPQSILEHQLIRTLADGKNIVIACGGGGIPVIKKENTYEGVEAVIDKDFASEKLATLIEADTLMILTNVENVFINFNEPNQQQIDDIDVATLKKYAAQGKFAEGSMLPKIEAAIRFVESGENKKVIITNLEQAYEALIGNKGTHIHM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the carbamate kinase family."}
{"protein": "MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGVASIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIEFQAPLGKRVQAWTHSLTCPALTGILALILMPTE", "text": "FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. SUBCELLULAR LOCATION: Nucleus speckle Cytoplasm Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic (By similarity). SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H subfamily."}
{"protein": "MASDQHRPKPRLSLRSSTTIRYGSMSSEHPDGDPSTPQTTSISQRRSYIAVAVLCYINLLNYMDRYTIAGVLLRIQKFFFISDSTSGLLQTVFICSFMFLAPVFGYLGDRYDRKLIMIVGLVMWIVTTLGSSFVRKSHFWVLVATRALVGTGEASYSTIAPTIIGDLFAGSKRTLMISFFYIFIPVGSGLGYIIGATVADATGDWRWALRVSPALGGLGLLLLVFLIPNPPRGASDNGGANMETTSYTEDIKYLLKNRSFVWSSLGVTAMAFVTGALAFWTPTFLSRAQVTQGLKQPCKEEPCDSVDSYIFGAITVVTGVVGVFLGTCISKKLRDRVPNADPLICAVGMLSSSPCFFIAIVLASTSIPATYTFIAIGETLLSLNWAILADILLYVVVPNRRATAEALQIMVCHLLGDAGSPYLIGAISDSLSKYNTTDPSWDFRRLEYSVLLCPFIGVLGGLFFLMTSLYIKEDRKAAELLTSGQTPQPEITTVSESV", "text": "FUNCTION: Sphingolipid transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC 2.A.1.49) family."}
{"protein": "MGKSELSGRLNWQALAGLKASGAEQNLYNVFNAVFEGTKYVLYEKPKHLKNLYAQVVLPDDVIKEIFNPLIDLSTTQWGVSPDFAIENTETHKILFGEIKRQDGWVEGKDPSAGRGNAHERSCKLFTPGLLKAYRTIGGINDEEILPFWVVFEGDITRDPKRVREITFWYDHYQDNYFMWRPNESGEKLVQHFNEKLKKYLD", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-CAATTG-3' and cleaves after C-1."}
{"protein": "MAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTNYTFEIWAVNGVSKYNPNPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGTESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHVNQEDLARIGITAITHQNKILSSVQAMRTQMQQMHGRMVPV", "text": "FUNCTION: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI- anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, also plays a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. During development of the cochlear organ of Corti, regulates pillar cell separation by forming a ternary complex with ADAM10 and CADH1 which facilitates the cleavage of CADH1 by ADAM10 and disruption of adherens junctions (By similarity). Phosphorylates CAPRIN1, promoting CAPRIN1-dependent formation of a membraneless compartment (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon Cell projection, dendrite Postsynaptic density membrane Early endosome Cell junction, adherens junction Note=Clustered upon activation and targeted to early endosome. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily."}
{"protein": "MSGSALYETFARAPLAFDHGEGTWLVTDKGERYLDFAGGIAVNSLGHSHPHLVAALTEQAAKLWHVSNLYEIPGQSRLGQRLVDATFADKVFFTNSGAEALECAIKTARRYHFVKGHPERFRVITFEGAFHGRTLATIAAGGQYKYLEGFGPKVEGFDQVGFDDIDAAEKAITPETAAILIEPVQGEGGIRPVPTQSLKRLRQLCDQHGLLLIYDEVQCGIGRTGKLFAHEWSGVAPDIMAIAKGIGGGFPMGACLATDEAAVGMTAGVHGTTFGGNPLAMAVGNAVLDVVLEDGFLEDVQRKALLMKQGLAAIADEFPDVVEDIRGTGLMLGLKCAMPNTKVNMALRDQHLLAVPAGDNVIRLLPPLTVTDAEIHEALNRIRAGAKGLADAIAVAAAK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily."}
{"protein": "MKKILFSMFYSILVGEEPDSVFLKKEGKQNQVKMIWIAPSSCAKDLTISEGTGATFPFHFHSRVSICFHALFLRPRNMKWTNSFS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf76 family."}
{"protein": "MTIIVTGAAGFIGANIVQALNVRGEKNIIAVDDLRPADKYRNLADLDIIDYLDKDEFLEAFRSGRFGKVKAVFHEGACSDTMETDGIFMMANNYRYTMDLLDICTAQKVQLLYASSAATYGGSDVFVESREHEKPLNIYGYSKFLFDQVMRKRFAEKTNTAQVVGFRYFNVYGPRESHKGRMASVAFHQYYQYKANGHVKLFGEYGGYGAGEQSRDFVSVEDVVKVNLFFLDHPEISGIFNLGSGRAQPFNDVAHAVANAMRKLDKAAPASLQELVKEKAIEYIPFPDALKGRYQCFTQADLTKLRAAGYAEPFLTVEQGVGRYIEWLEANSSFLANPL", "text": "FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D- manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily."}
{"protein": "MSYFPWLTILVVLPIFAGSLIFFLPHRGNKIVRWYTISICLLEFLLMTYAFCYHFQLEDPLIQLKEDYKWIDIFDFHWRLGIDGLSLGSILLTGFITTLATLAAWPVTRNSRLFYFLMLAMYSGQIGLFSSRDLLLFFIMWELELIPVYLLLSMWGGKRRLYSATKFILYTAGGSIFFLIGVLGMGLYGYGSNELGLDLERLINQSYPATLEILLYFGFLIAYAVKLPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLIRINMELLPHAHYLFSPWLVIIGAIQIIYAASTSLGQRNFKKRIAYSSISHMGFIIIGIGSITNIGLNGAILQILSHGFIGATLFFLAGTASDRMRLVYLEELGGISIPMPKIFTMFSSFSMASLALPGMSGFVAELVVFFGLITSPKFLLMPKMLITFVMAIGMILTPIYLLSMLRQMFYGYKLFNVPNANFVDSGPRELFILICIFLPVIGIGIYPDFVLSLSIDRVEALVSNYYPK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family."}
{"protein": "MKTVLLTGFDPFGGESINPAWEVAKSLHEKTIGEYKIISKQVPTVFHKSISVLKEYIEELAPEFIICIGQAGGRPDITIERVAINIDDARIADNEGNQPVDVPVVEEGPAAYWSTLPMKAIVKRLQAEGIPASVSQTAGTFVCNHLFYGLMHELEKQNHKVKGGFVHIPFLPEQASNYPGQPSMSLSTIRKGIELAVEVTTTVEVDIVEVGGTTH", "text": "FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C15 family."}
{"protein": "MQRLKSFYLETIIPKLKEEFGYVNSYRVPKLKKIVINRGFDESCQNSKILEVLLNELEIISGQKPIISKAKKAIANFKLKEKMPVGMFLTLRSEKMYSFLDRLINLSLPRIRDFQGINKNCFDGSGNFSFGLSEQSMFPEINFDKMIKVQGLNITIVTTAETNQEAFFLLKELGIPFRD", "text": "FUNCTION: Binds 5S rRNA, forms part of the central protuberance of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
{"protein": "MAQFAQVMAEVGDFGRFQVRLTILMGIPNFLSAFFVFSQVFMVLDEAHYCSVSWVKNHTFNLSAAEQLAVSIPNDTAGRPESCLMFRPPPDNASLEDILSHRFNETQACDSGWDYPENRPPSLKNEFDLVCERENLKRTSQSVFMAGLLVGALVFGPVCDWIGRRPSLLMQLLLSGIASMATAFVSSFELYMTLRFALATANAGFLLSSNVLLSEWVGTSRRTRAMVLAQSNFALGLMALAGLAYGVRNWRLLQIIGTTPIFLLVFYFWVLPESPRWLLSQGRTEEAKQLVQKAALVNGRPLASELLNQLVPEKTGPSGNALDLFRHPQLRKVTLILIAVWFVDSLLYYGLGFQVGDFGLDIYLTQVIFGVVEVPARLSSIPMMEKLGRKWSQLCTLTLAGVMCVIIIFIPGDLPTVATALAVVGKFASSAAFTISYVYTAELLPTIIRQTGMGLVSIFSRVGGIITPLVMLLEQYHKAIPMLIFGSLPIGAGLLCALLPETRGQTLKDTLQDLEQGQPPRSYKTAPQRKDVEASGRTSSARVAVVRSSYF", "text": "FUNCTION: Anion antiporter that mediates the transport of nicotinate (PubMed:35144162). Possibly involved in nicotinate intestinal reabsorption (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family."}
{"protein": "MRIAGAIKFVVAVALFLLTFYVISQVFEIKSYTNLGNIFVRSAIDTVAHPTTKAPRYRCGISKVCPEKHFAFKIASGAANVVGPKICVDDNILMSGVKNNVGRGINTALVNGKTGALIETTYHDLWGGEVGPFIEFLKKIPDGTIVLMATYDDGATKLNDDARKRISELGSTLINVLAFRDNWVFVGGKGIKTKSPFEQHIKNNKDTNKYEGWPEVVEMEGCIPQKLNE", "text": "FUNCTION: Involved in retinal laminar formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FAM3 family."}
{"protein": "MKRRAGLGGSMRSVVGFLSQRGLHGDPLLTQDFQRRRLRGCRNLYKKDLLGHFGCVNAIEFSNNGGQWLVSGGDDRRVLLWHMEQAIHSRVKPIQLKGEHHSNIFCLAFNSGNTKVFSGGNDEQVILHDVESSETLDVFAHEDAVYGLSVSPVNDNIFASSSDDGRVLIWDIRESPHGEPFCLANYPSAFHSVMFNPVEPRLLATANSKEGVGLWDIRKPQSSLLRYGGNLSLQSAMSVRFNSNGTQLLALRRRLPPVLYDIHSRLPVFQFDNQGYFNSCTMKSCCFAGDRDQYILSGSDDFNLYMWRIPADPEAGGIGRVVNGAFMVLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWSPYKQPGCTGDLDGRIEDDSRCLYTHEEYISLVLNSGSGLSHDYANQSVQEDPRMMAFFDSLVRREIEGWSSDSDSDLSESTILQLHAGVSERSGYTDSESSASLPRSPPPTVDESADNAFHLGPLRVTTTNTVASTPPTPTCEDAASRQQRLSALRRYQDKRLLALSNESDSEENVCEVELDTDLFPRPRSPSPEDESSSSSSSSSSEDEEELNERRASTWQRNAMRRRQKTTREDKPSAPIKPTNTYIGEDNYDYPQIKVDDLSSSPTSSPERSTSTLEIQPSRASPTSDIESVERKIYKAYKWLRYSYISYSNNKDGETSLVTGEADEGRAGTSHKDNPAPSSSKEACLNIAMAQRNQDLPPEGCSKDTFKEETPRTPSNGPGHEHSSHAWAEVPEGTSQDTGNSGSVEHPFETKKLNGKALSSRAEEPPSPPVPKASGSTLNSGSGNCPRTQSDDSEERSLETICANHNNGRLHPRPPHPHNNGQNLGELEVVAYSSPGHSDTDRDNSSLTGTLLHKDCCGSEMACETPNAGTREDPTDTPATDSSRAVHGHSGLKRQRIELEDTDSENSSSEKKLKT", "text": "FUNCTION: Is a substrate receptor for the CUL4-DDB1 E3 ubiquitin- protein ligase complex (CRL4) (PubMed:29691401, PubMed:30442713). The complex CRL4-DCAF5 is involved in the ubiquitination of a set of methylated non-histone proteins, including SOX2, DNMT1 and E2F1 (PubMed:29691401, PubMed:30442713)."}
{"protein": "MRRTFTAEEKASVFELWKNGTGFSEIANILGSKPGTIFTMLRDTGGIKPHERKRAVAHLTLSEREEIRAGLSAKMSIRAIATALNRSPSTISREVQRNRGRRYYKAVDANNRANRMAKRPKPCLLDQNLPLRKLVLEKLEMKWSPEQISGWLRRTKPRQKTLRISPETIYKTLYFRSREALHHLNIQHLRRSHSLRHGRRHTRKGERGTINIVNGTPIHERSRNIDNRRSLGHWEGDLVSGTKNSHIATLVDRKSRYTIILRLRGKDSVSVNQALTDKFLSLPSELRKSLTWDRGMELARHLEFTVSTGVKVYFCDPQSPWQRGTNENTNGLIRQYFPKKTCLAQYTQHELDLVAAQLNNRPRKTLKFKTPKEIIERGVALTD", "text": "FUNCTION: Required for the transposition of the insertion element. SIMILARITY: Belongs to the transposase IS30 family."}
{"protein": "MTDQISHLGKTLSTAASVLIGSQDIEKNVENNLLSNSPRNPYRKTLQESLTAADFMNHETFDKLRKTRAIASTLSEDSKGLYSQRSREKYFTNKVSDKKTTFKVLSHLSDDLLKDLPETAESKSNTRDQGETKLLKESDSTDASQERIFSLYQGFEASIPVINRSVEKEHLLLEQNNQESAAQILPQMGNKPRIRSGPWEDLLESKEDTYISLDFNPERISNIKSKKELERINELANNNLVMLDIRKKLSADEIDEIKKQIQDLQLKQNLLVKKIAAIEENELFLEDIIRLIGHRSADFSNDTQIEFDQAKSLSGLNNPESMIDATRPTALERKNSIDIVETSLNEIRTSFDGSKQSIEGKDNHNALNGFFEDASNKKSRKAQPTVQKYYNSGKKLSTIPKAHDDAITCLDFDPHFSTLCTAGYMDHIVKLWDYTKKRQIGAMEGHVATISCMQVDKNYNMVATGSKDATVKLWNANDVIGRYEEGNNSEALHTLDAHLDEVSSLYIDGANLMTASQDKTIRRWDLYSGKCIQVFDVNFPSLSAYKSSFMKSNEDSMILKTVNTPIIGSIQSFDAALATGTKDGLIRLWDMRTGEVVRVLEGHMDAITSLKFDATTIISGSLDGTIRLWDLRSNNLTDIISYEKPISSLDFDAKHIVVASNEHNTHIYDRNDGNKWDLQDEEQDTTSLFVKYKERYTMEGRSNGDIGIWIV", "text": "FUNCTION: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family."}
{"protein": "MYQDLIRNELNEAAETLANFLQDEANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHLSCVSNDFGYEYVFSRYVESVGRAGDVLLGISTSGNSGNVIKAIEAARAQGMKVITLTGKDGGKMAGSADVEIRVPHFGYADRIQEIHIKVIHILIMLIEKEMVKG", "text": "FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIS family. GmhA subfamily."}
{"protein": "MHTAAQFSISTLNNLYEISSVEVGQHFYWQIGSFEVHAQVLITSWIVIAILLSLAVLATRDLQTIPTSGQNFVEYVLEFIRDLTRTQIGEEEYRPWVPFIGTMFLFIFVSNWSGALLPWRVLELPHGELAAPTNDINTTVALALLTSVAYFYAGLHKRGLNYFGKYIQPTPVLLPINILEDFTKPLSLSFRLFGNILADELVVAVLISLVPLVVPIPMMFLGLFTSAIQALIFATLAAAYIGESMEGHH", "text": "FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family."}
{"protein": "MAEWLLSASRQRRVKAMTAAAGSAGRAAVPFLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYALDENYFRGYEWWLMKEAKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIVGAKRYHDLDIDYIGIWNERSYNANYIKILRKMLNSQGLQRVKIIASDNLWESISAAMLLDAELFKVVDVIGAHYPGTHSVKDARLTGKKLWSSEDFSTLNSDTGAGCWGRILNQNYVNGYMTSTIAWNLVASYYEQLPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEIPELQVWYTKLGKTSERFLFKQLDSLWLLDSNGSFTLKLQEDELFTLTTLTTGRKGSYLPPPKSQRFPSTYKDDFNVDYPFFSEAPNFADQTGVFEYFTNMEDPGEHHFTLRQVLNQRPITWAADASNTISIIGDYNWTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIFANGSYRVTGDLAGWIIYALGHVEVTAKTWYTLTLTIKGRFASGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDNFHVEATR", "text": "FUNCTION: Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine (PubMed:9192853). Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon (By similarity). SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 59 family."}
{"protein": "MRIMASPFAVLLQNVSFRYTADARFILHEVDLAIPKGAYLSVVGENGSGKSTLVKLVLKLLKPSTGTIAHFVQRVGSVPQTKMHTLYFPLTVYEMLNSYRRLLRISHKWVVDAVLEEVGMRGAKKKLVYTLSGGELQKVYIARSLIGDPDLLVLDELSTGIDSRGQKDIYALLKGLNTSRNVTVISVEHNLDAAITNSTQIFHLSEGHGHLCNPQQYVSEFLDMQKKDALACAQCRSR", "text": "FUNCTION: Part of an ATP-driven transport system TP_0034/TP_0035/TP_0036 for a metal. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MARVTIEDCLKEVDSRFTLVHLAVRRVLQLRGGAPPLTEVRNKEVVLALREIAAGKVTVDNIRRLEEAKALPEPVAVTQKEDVARLELKEIMDEATLYDASMEFDEAQQVVEPDAEPSEEG", "text": "FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. SIMILARITY: Belongs to the RNA polymerase subunit omega family."}
{"protein": "MGRLDGKVIVLTAAAQGIGRAAALAFAKEGAKVIATDINDSKLQELDKYPGIHTRVLDVTKKKQIDQFANDIERLDVLFNVAGFVHHGTILDCEETDWDFSMNLNVRSMYLMIKAFLPKMMAQKSGNIINMSSVASSIKGVVNRCVYSTTKAAVIGLTKSVAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPEEALSDFLKRQKTGRFATAEEVALLCVYLASDESAYITGNPVIIDGGWSL", "text": "FUNCTION: NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines (By similarity). Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and associates with LCN2, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MTEGEIPWGPTGELVYNRTYSRVKPDGTRETWPETVERVVSGNLALVDSRYQLPGEREDLLRLMREFKILPAGRHLWASGVKNAQHLFNCWVSGWTEKPSDHFEFTFMRLMEGGGVGANYSNRFLADYPHVKQELEVHIVCDEDHDDYADLAEAGQLSSRYDSDWVDAFVIEDSREGWAAALVDLIDTHYRDDVAHKERVYDVSRVRAAGRKLKTFGGTASGPVPLAKMLTEVSEILSRCAREGEQYRFEDGGALTGLDAMEIDHAIAQCVVAGGVRRSARMAMMHWADWQVETFTNIKQDSGSHWTTNISVEVDDAFWSLAKAPVDPLNPRSTKAHRVLKALSEGAVRNGEPGMWDSSLSNVGEPNEVVCTNPCGEITLEPWEPCNLGHINLAAFVTDAGKTDYIDLIRAHRLMTRFLIRATFSAVADPKSREVLDRNRRIGVGHLGVASYLALTGRRYSQAPGDKRFTAFLREMAAEVDRAAEEFSHELRIPVPVKKRTVAPTGTIAKMPGVSEGIHPIFSRYFIRRIRFSVLDNDQFLTASQYAADGYHVEKDQYDKSGNTWVVEIPTKDTLVEAVAARFGRDAEDIVESANELTLHQLLAFQALYQTCWADNAVSFTANVDPDAYEGVDVAADLQRFSGLIKGSTIFPEESFPQAPYERITKQQYEAAAIKAVADGVDEECANGACPIK", "text": "SIMILARITY: Belongs to the class II ribonucleoside-triphosphate reductase family."}
{"protein": "MTTTTTTSNTSNNSNAQFNFFKMCIGRPVVVKLNNGVEYRGILEVVDGNMNIVMEQTEEYLNGQLKTKYGDCFLRGNNVLYISAQPRK", "text": "FUNCTION: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2- LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily."}
{"protein": "MKSSSSIFRETSEKKSERWMMMNIGRFSPFFLSSFCITLFFTGFFVYQNPFKSIADQNVLSFQPQIDPECDLFKGHWVPDKRGSLYTNSSCATIPDSKNCIKQGRPDKDFLFWRWKPDGCDLPRFNPKAFLSMVRGKKMNFIGDSVARNHMESLLCLLSMEETPKDIYKDGEDRNRIWYFPKHDFTLSTSWTKFLVEERERRDSNNTGTGLFDLDIGKIDEGWFNGLPNTDIAIVSAAHWFFRPIFIHRGDETLGCIYCNLPNMTQISPEEGFKLVYSAVLRQINECEMCKKDLVTVLRTISPAHFENGTWDTGGTCSRTSPFGENKIDLQSNEMKIRKSQIEQLEGITKRGNKAKKFAVLDVTRVMQMRPDGHPNGYWGNKWMKGYNDCVHWCLPGPIDAWNDFLMAIIRQLR", "text": "FUNCTION: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains (PubMed:30083810). Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers (PubMed:30083810). Involved in xyloglucan specific O- acetylation in seeds (PubMed:22086088). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily."}
{"protein": "MARIAGVDLPRDKRVEIGLTYIYGIGLTRSKEILSKIELDPDTRVRDLPDNAIAQLREIIETDYQVEGDLRRFESMNIKRLADIGCYRGRRHRLNLPVRGQRTRTNARTRRGARQTVAGKKKAPSK", "text": "FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the universal ribosomal protein uS13 family."}
{"protein": "MSEGDSVGDSVHGKPSVVYRFFTRLGQIYQSWLDKSTPHTAVRWVVTLGLSFIYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFEAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRTYKGKEDAGKAFAS", "text": "FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RER1 family."}
{"protein": "MESGSMKTPLVNNQEEARSSSSITCGLLLSTSVAVTGSFVYGCAMSYSSPAQSKIMEELGLSVADYSFFTSVMTLGGMITAAFSGKIAAVIGRRQTMWIADVFCIFGWLAVAFAHDKMLLNIGRGFLGFGVGLISYVVPVYIAEITPKAFRGGFSFSNQLLQSFGISLMFFTGNFFHWRTLALLSAIPCGIQMICLFFIPESPRWLAMYGRERELEVTLKRLRGENGDILEEAAEIRETVETSRRESRSGLKDLFNMKNAHPLIIGLGLMLLQQFCGSSAISAYAARIFDTAGFPSDIGTSILAVILVPQSIIVMFAVDRCGRRPLLMSSSIGLCICSFLIGLSYYLQNHGDFQEFCSPILIVGLVGYVLSFGIGLGGLPWVIMSEVFPVNVKITAGSLVTVSNWFFSWIIIFSFNFMMQWSAFGTYFIFAGVSLMSFVFVWTLVPETKGRTLEDIQQSLGQLS", "text": "FUNCTION: Sugar transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MKNLAKLVEMKQDKTKISMITAYDFPSAKQAQDANIDMILVGDSLGMTVLGYETTTQVTLEDMIHHGKAVRRGADDTFVVVDLPIGTVGVSDEHDLKNAITLYQETNANALKAEGAHLVNFIKKSTQIGIPIVAHLGLMPQSVGVMGYRLQGSTKDAAEQLIQEAHAVQEAGAVALVLEAIPSDLAGLISEQLDIPVIGIGAGKDTDGQVLVYHDMLNYGVDRYAKFVKQFGDFSVGIDAIKHYDEEVKAGTFPAEAHTYKKKILNEVNSND", "text": "FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanB family."}
{"protein": "MTQVFQGRNFLAEKDFTREEFEYLIDFAAHLKDLKKRGVPHRYLEGKNIALLFEKTSTRTRAAFTTAAIDLGAHPEYLGANDIQLGKKESTEDTAKVLGRMFDGIEFRGFSQRMVEELGEFAGVPVWNGLTDEWHPTQMLADYLTVKENFGKLEGITLVYCGDGRNNVANSLLVAGTLMGVNVHIFSPKELFPDEEIVKLAEGFAKESGAHILVTDNADEAVKGADVLYTDVWVSMGEEDKFKERVELLQPYQVNMDLVKKANNENLIFLHCLPAFHDTNTVYGKDVADKYGVSEMEVTDEVFRSKYARHFDQAENRMHTIKAVMAATLGNLFIPKV", "text": "FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
{"protein": "MESNFIDWHPADIIAGLRKKGTSMAAESRRNGLSSSTLANALSRPWPKGEMIIAKALGTDPWVIWPSRYHDPQTHEFIDRTQLMRSYTKPKK", "text": "FUNCTION: This protein is involved in positive regulation of the metabolism of sugars. SIMILARITY: Belongs to the ner transcriptional regulatory family."}
{"protein": "MPTKKWEDEESSSGSSDESSPAVAVSVPRRKFDDEEANDSDVLDSWDAAEDSEVEREKAKKAAEAKAKAEAEAKANKKTKAARINEHKQRRKEAEESDESDDETESQRRERLRRTEKEADLAHAEDLFGDIGVPAGRKVKAASTSVSIDPSDPSKTVELSDMPIFNPKTKTQFEDMRQALIPLITASSGRKPHYNNFMEEFVRQLCADMPSENIKKISSKLTALSNEKMKQEKAAAGTKKTKAAKTKTSLVANRAGVTDTNSYEDTFGDDDFM", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit J family."}
{"protein": "MGFRLSHLSLALSFVALALAGVAIYRNTYEAIIMNNGSLLQNASPHFDSLESGVASILTLNNKKRNSDMYLRQQLTPEACVFSAVRGVVDSAIDAETRMGASLIRLHFHDCFVDGCDGGILLDDINGTFTGEQNSPPNANSARGYEVIAQAKQSVIDTCPNISVSCADILAIAARDSVAKLGGQTYNVALGRSDARTANFTGALTQLPAPFDNLTVQIQKFNDKNFTLREMVALAGAHTVGFARCSTVCTSGNVNPAAQLQCNCSATLTDSDLQQLDTTPTMFDKVYYDNLNNNQGIMFSDQVLTGDATTAGFVTDYSNDVSVFLGDFAAAMIKMGDLPPSAGAQLEIRDVCSRVNPTSVASM", "text": "FUNCTION: Suggested to catalyze the deposition of the aromatic residues of suberin on the cell wall and thus play a role in cell-suberization. FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MASEKKLSNPMRDIKVQKLVLNISVGESGDRLTRASKVLEQLSGQTPVFSKARYTVRSFGIRRNEKIACYVTVRGEKAMQLLESGLKVKEYELLRRNFSDTGCFGFGIQEHIDLGIKYDPSTGIYGMDFYVVLERPGYRVARRRRCKTRVGIQHRVTKDDAMKWFQVKYEGVILNKSQNITG", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
{"protein": "MKQRITVAGDSDNYQLLKAYDVNISGLVSTPMQNEARRLRPERWKVANQEGMAEVARFIEMNGSFADENRDW", "text": "FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system which inhibits the post-segregational killing (PSK) of plasmid-free cells, also referred to as a plasmid addiction system. Binds to and blocks the activity of CcdB; will also remove bound CcdB protein from the CcdB-GyrA complex by forming a CcdA-CcdB complex, a process termed rejuvenation. Functions as a transcriptional corepressor for the ccdAB operon, repression also requires CcdB (By similarity). SIMILARITY: Belongs to the CcdA antitoxin family."}
{"protein": "MSALKKSFIKRKLAKKQKQNRPMPQWVRMKTGNTMKYNAKRRHWRRTKLKL", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family."}
{"protein": "MSFKVSRQTYAELMGPTTGDRIRLADTELMIEIEKDFTTYGEEVKFGGGKVIRDGMGQSQHNHDQVMDTVITNAVIIDHWGIVKADVGLKNGRIAEIGKAGNPDIQPNVTMSIGAATEIIAGENMILTAGGIDSHIHFISPQQAEDAMMNGITTMLGGGTGPAAGTAATTCTPGPWHIHSMLRASDGMVMNTGFYGKGNVSLPTPLEEQILAGACGLKLHEDWGSTYAAIDNCLAVADKYDVQVAVHTDTINEGGYLENTIAAMKDRTIHTFHTEGAGGGHAPDIIAVVGQENVLPSSTNPTRPYTINTLDEHLDMLMVCHHLHANIPEDLAFAESRIRKETIAAEDILQDMGAISMMSSDSQAMGRIGEVVLRTWQTAHKMKIQRGTLQEDTSKNDNFRVKRYIAKYTINPAITHGISHALGSVEVGKYADLVLWRPAFFGVKPSVILKGGMIAASLMGDPNASIPTPQPVHYRYMFGGYGGGIKTSCFTFVSQAALAAGLVDQLKLDKNLIEVKNTRNLRKKDMIHNSATPKMEVDPETYEVRADGQLLTCGAEDVLPMAQRYFLF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family."}
{"protein": "MATEAAVVSNPNTLAKYLKLDQKGSIMAEYIWIDADGETRSKSRTLKEKEYTPEDLPMWNFDGSSTGQAPGDNSDVYLKPVAVFPDPFRGSPNILVLSECWNADGTPNKYNYRHECAKLMEAHAAHEPWFGLEQEYTLLDLSNRPFGWPANGFPAPQGPYYCGVGTGKVVQRDIVDAHYKACLYSGVKISGTNAEVMPAQWEFQVGPCVGIEMGDHLWLARFLLARIAEEFGAKVSVDPKPIPGDWNGAGLHSNFSTKEMRVEGGMKHIEAAIKKLEGRHKEHIAVYGEGNEKRLTGRHETGAIDQFSYGVANRGASIRIPREYTAKGYGYFEDRRPASNADPYRITGILMETIYGSVDN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
{"protein": "MLYFSRWKSALIWLAVLVSLIIASPNFFSRETLENLPDFLPKKQVSLGLDLSGGSRLILQVQNAGKTDLETTANIMRQRLEELGYGNPVVEGEGRNQIRVEVPGLYDAQLLKDILTIRGNLSFRAMDDTMSPDDAIRGTPPADSEIVYSFDDPPVGYLLKKTPILTGHDITDAKASISADDGQPVITLTLDDNGRRRLADLTAQGNENSFAIVVDNQVVSAPTVSGPLDTSELQIEGAFDLQAANNMAVVLRSGALPQAVTVLEERTIASALGEDYASAAVLAALLAALVVGLFMVLSYGILGVIALVALVVNIVILTAVLSLIGASISLASIAGLVLTIGLAVDAHILIYERVREDRRKGYSVVQAMESGFYRALSTIVDANLTTLIAALVLFLLGSGTVHGFALTVAIGIGTTLFTTLTFTRLLIAQWVRTAKPKEVPKRRLKLVPTVTHIPFMRLQFVTLGISVLACAIVVALFVNIGFNYGIDFRGGSMVELQARNGDANLEDINERLAELNIDSARVLPAKSPRSALVIIGSQEVGDDAEQTVAVKLRGEFEQDYSFQRVDVVGPTVSEQLSRAGVLAVILSLIGIFIYVWFRFRWQLALGAVLSTLHDVVILSGMFIVFRMEFNLWSVAAILTIIGYSLNDTVVIYDRVRENLRRYKSAPLPAIIDASINQTLSRTLLTSFVTFLAHVPLYAFGGSEIRMFALALSVGIIVASYSSIFIAAPLLVQFGLKPRETDAGDAVDAELAQSLNLES", "text": "FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily. SIMILARITY: In the C-terminal section; belongs to the SecD/SecF family. SecF subfamily."}
{"protein": "MAKQQRTVLIIGAGIAGLTTSRLLTNNGIPNIVFEASTPDRSQGFAISLQEFGYSTLLSALGDLPLSSLIKGVAPDRVIGGTGWIDQALRDNRTGELLVAPELTTTKQTVVRANRNALRQWIADCGDEELDVRYGHKLQRVEGKAGNITAVFENKAKYNGSLIIAADGVNSTVRSQVLPSVVPETIPLIHYHGEFQLSRTKFDELIRPYSGHSNILVGVGDRFNTPLSICNMSKSHVHLDWSYSRTVKEGNDLLYRPNLPSEEAKKIPLALVEELGALDLAGPWKHFLNPESLKSHRVFHWTTRCVYMTQDDARSAGEKGIVFVGDSWHAMPIFGGEGGNHALLDGVELSNAIVTAMASTEKDYWSKAVASYYSSAWKRSQEAVRRSTQRFFLLHRPAADWREIAEKKRRTT", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of neosartoricin B, a prenylated anthracenone that probably exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (By similarity). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (By similarity). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (By similarity). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (By similarity). Neosartoricin B can be converted into two additional compounds neosartoricins C and D (By similarity). Neosartoricin C is a spirocyclic compound that is cyclized through the attack of C3 hydroxyl on C14, followed by dehydration (By similarity). On the other hand, neosartoricin D is a further cyclized compound in which attack of C2 on C14 in neosartoricin C results in the formation of the acetal- containing dioxabicyclo-octanone ring (By similarity). Both of these compounds are novel and possibly represent related metabolites of the gene cluster (By similarity). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
{"protein": "MHFLLSRLLHHRQLNVSAQLFNVSHYDVITDMSNTFTCLKEILNAPSYPSNKVDQSVVEIVVARLTAAIRETGSIESYAAELVDVLDEVLRHPMTTLNEKCQDVDSPHCKIASDLLSSLFLHYGNKPVMTLTIPVALKCLNSENGELVKNTTSYISLAAIHNGKSLSSHALQIISNVVRGNYSLIRVLPHIYPDNKEPFHAQLSQLIDLLQNTEVDCSEKLSLLQLSSMVANTKPDVLIPFLPRFDVYLLSPQMSTALLNIYMSLISQNRTKSLSQFLPTLKLAAQSNEFINNRTTICKIIANIGRVSSPLASEAVDELVLMARNNSSDQQILQTVLNEIDAIGSIHPTSLRRHVSFFQTLPTSRIIERILAHLNPNNSENIMSYDIKEQSTESLLSKNSKVFGNLITSGGRTVFEVCDSPTVELCELDRNTHSLAMQYQNNRSSGSLSRRSHASIAHSLGAGTHGPYSDINESRELSMISMPSSSRTNVLLAQPTSSSTSRIQTLPHAFAPQAMTQIQMGKDGRVRPVGGGRRPVQWPAGSTETTFPAHLGPITTSKMCALNEEDEKWINNDRNDVVYKFVEHRKNKIRRYIGEVNARFPVPVQCTVEGSKNSKHRMVIHFSCQTRSSPCCVFTKEYLFAFKTKYPAFWLHFMFLQMECSAITQFGEVVGKDSQQYQTLEHCWKCLPSSITKSVPFDTMITAAFPNSKDQNKLIKELDEAGFFACFTMDSTNNMWNCISCTNPEKVKYFVEEGGAEKVLEGQLKEKKGRWRFLKRWNTKYFTLSSAALNYSTQHMPTDSRALLPSIDLRSIRSVRSLGRGKKARKSLRKAFEIFTADNTSMILKAKDEKNAEEWLHCLQIAMAHARRELA", "text": "SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the MELT/VEPH family."}
{"protein": "EQQCTPGQTKKEDCNNCTSGD", "text": "FUNCTION: Probable serine protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I19 family."}
{"protein": "MAENVPADVNTLSFELAIEELETIVKRLEDGKVALEESVAIYERGEALKRRCEELLRRAEARVEKITTDASGHVTGTEPLDVR", "text": "FUNCTION: Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the XseB family."}
{"protein": "MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH", "text": "FUNCTION: Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls (PubMed:34751132, PubMed:24855650). Cargo proteins are targeted to the interior via their C-terminal extensions; empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and Rv1762c have been identified in vivo (PubMed:24855650). Probably involved in protection against oxidative damage from the host immune response (Probable) (PubMed:34751132). A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity (PubMed:9596740). SUBCELLULAR LOCATION: Encapsulin nanocompartment Secreted Cell membrane; Peripheral membrane protein Note=Encapsulin microcompartments of this protein encapsulating DyP are found in situ (PubMed:34751132). Detected at low levels in short-term culture filtrate, the nanocompartment is very stable and may survive cell lysis, explaining its apparent secretion (PubMed:9596740) (Probable). Detected in infected host (mouse J774 cell line) exosomes (PubMed:20662102). SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily."}
{"protein": "GIEKIISRSMFDQMLKHRNNPACPAKGFYTYDAFLAAAKSFPSFGTTGSTDVRKRELAAFLGQTSHETTGGWPSAPDGPYAWGYCFLKERNPSSNYCAPSPRYPCAPGKSYYGRGPLQLSWNYNYGPCGEALRVNLLGNPDLVATDRVLSFKTALWFWMTPQAPKPSCHDVLTGRWQPSAADTAAGRLPGYGVLTNLLNGGLECGKGPNPQVADRLGFFRRYCGLLGVGTGNNLDCYNQRPFG", "text": "FUNCTION: Defense against chitin-containing fungal pathogens. Shows activity on chitin, tetra-N-acetylglucosamine and chitosan. SUBCELLULAR LOCATION: Vacuole Note=Vacuolar and protoplast. SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily."}
{"protein": "MAVPTLSETLTTLLHRVLQGEDLTPEEGVFLLQQWDPEALTVIRQTSDRLRQQQVGDTVTYVVNRNINFTNICEQHCSFCAFRRDEDQPGAYWLGFDEILAKTGEAVERGATEICMQGGLHPGAKLQGHSLAYYLKLVETIKTTFPTLHLHAFSPQEVQFIAREDGLSYAQVITALRDAGVNSMPGTAAEVLVDEVRRVICPEKINTATWLEIISTAHALGVPTTSTMLSGQIETPQQQIEHLFLLRSLQQKAIQQDYPARFTEFILLPYVGQSAPKPLRKRVGRDQPVLQDALLLTAVARIFLGNWIVNHQPSWVKLGLAGATEALIWGCNDLGGTLMEEHITSMAGAQGGTCRSVENLQQAIASLNRPYRERTTLYGYL", "text": "FUNCTION: Catalyzes the radical-mediated synthesis of 5-amino-5-(4- hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D- ribitylamino)uracil and L-tyrosine. SIMILARITY: Belongs to the radical SAM superfamily. CofH family."}
{"protein": "MEELSQALASSFSVSQELNSTAAPHPRLSQYKSKYSSLEQSERRRQLLELQKSKRLDYVNHARRLAEDDWTGMESGEEEKKKDEEEMDLDPVKKLPKRYANQLMLSEWLIDVPSDLGQEWIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTTAKDYTILDCIYSEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMNSKLPEEEGLGEKTKINPFKFVGLKNFPCTPESLCKVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDILGVAVPAGPLTTKPEYAGHQLQQIIEHKRSQEDTKEKLTHKASENGHYELEHLSTPKLRSPPHSSESLMDS", "text": "FUNCTION: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta. It is re-exported to the cytoplasm by the XPO1-dependent nuclear export receptor pathway. SIMILARITY: Belongs to the snurportin family."}
{"protein": "MGPEAAGPGRGAAPRLQVRTWIEPVVAATQVASSLYEAGLLLVVKASFGAGAGAGAGAASNHSAGPPRGAPEDQQQRAISNFYIVYNLVVGLTPLLSAYALGWLSDRRHRKVAICVALLGFLLSRVGLLLKVLLDWPVEVLYGAAALNGLCGGFSAFWAGVMALGSLGSSEGRRSVRLVLIDLILGLAGFCGSMASGHLFKQVAGHSGQGLVLTACSVSCATFALLYSLLVLKVPEAAAGSGQALSAGDSVAGTVGTYRTLDPDHSDKQSVQGLHPPSPGKAKPRRTIIALLFLGAIVYDLAVVGTVDVMPLFVLREPLSWNQVQVGYGMAAGYTIFITSFLGVLVFSRCFQDTTMIMIGMVSFGSGALLLAFVKETYMFYIARAVMLFALIPITTIRSAMSKLIKGSSYGKVFVILQLSLTLTGVVTSTVYNKIYQVTMEKFIGTCFALSSFLSFLAIIPIGIVAYKQASWLQYGDVRET", "text": "FUNCTION: May act as a transporter (By similarity). May be involved in establishing and maintaining the luminal fluid microenvironment. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=Apical membranes of organs. SIMILARITY: Belongs to the major facilitator superfamily. SLC46A family."}
{"protein": "MSGTGVLLLTLLLLVAMAASDMLSSLIQAHERDSEESCKSYGGGPCPSGEDCCCPPGRSTGTCKRTCNNGSVCA", "text": "FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MNSHNITNESLALALMLVVVAILISHKEKLALEKDILWSVGRAIIQLIIVGYVLKYIFSVDDASLTLLMVLFICFNAAWNAQKRSKYIAKAFISSFIAITVGAGITLAVLILSGSIEFIPMQVIPIAGMIAGNAMVAVGLCYNNLGQRVISEQQQIQEKLSLGATPKQASAILIRDSIRAALIPTVDSAKTVGLVSLPGMMSGLIFAGIDPVKAIKYQIMVTFMLLSTASLSTIIACYLTYRKFYNSRHQLVVTQLKKK", "text": "FUNCTION: Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0014 family."}
{"protein": "MHHKALLISLASTALALHGSSSHSHLGKRFTFPLPSSKGSVTFDAPKIISGNTTFDGGMKTYGRGVECTEGEGGDSDAVFWVENGGTLKNAIIGADQIEGVHCMGACTIENVWWEAVCEDALSLKEGSGPFTVIGGGAQGAEDKVIQHNSGGTVSIDGFTVYNFGKLYRSCGNCDEMFERHVTVSGVTAVQGSTLVGINSNYGDTATIKGDVCATDVDTICQEYEGNSSGEEPPETGSGPSSACKYSEPLPAC", "text": "FUNCTION: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 3 family."}
{"protein": "MDLSVKSQENVEHMVEAIKEKLRMVNAGAMKAANFDEDMYEDLRDIYDHVMKRETFSISEMQAITEELGTLMKK", "text": "SIMILARITY: Belongs to the UPF0435 family."}
{"protein": "MLRKLLIGTALATSFAFSAHAADVKEVQMLHWWTSGGEAAALNVLKGDLAKEGFAWKDVPVAGGGGDAAMTALKAMVAAGNYPTASQMLGYTVLDYAAAGVMGDLTETAKKEGWDKSVPAALQKFSVYEGKWVAAPVNVHSVNWLWINKAVMDKIGGTEPKTFDDFVALLDKAKAAGVIPLALGGQNWQEATMFDSVVLSTGGPEFYKKAFNDLDDASLKSDTMKKSFDNLAKLVTYVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFHAAKKTPGTDFLCYRFPGTDGSVIYNSDMFGMFNVPDDRKAAQVALATATLSKSFQSAFNVVKGSVPARTDVPDTDFDACGKKGIADLKKANEGGTLFGSLAQGYGAPPAVANAYKDVVSKFVHGQIKTSDEAVTELVKAIDDAK", "text": "FUNCTION: Part of a binding-protein-dependent transport system for a sugar. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
{"protein": "MALRSITKLETFLKRYSAPTLYYCLHRSTQSSTCNSTNTDNGSHNTNYNSSNNNNNNNDNKRFSWRSAIRFLVPFSLGALASSVVAGDRELMPTISAKTLTNNRRDFNFIADVVASCADSVVYIEIKDTRHFDYFSGQPITASNGSGFVIEQNGLILTNAHVVINKPNTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVTNLSVMKLGKSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRASQELGLRNRDINYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVTAGISFAIPIDYVKLFLERAAARRKKGSAYKTGYPVKRYMGITMLTLTPDILFELKSRTQNMPETLSHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADGKKDLDMVILRGVKQMRVTITPEDP", "text": "FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase- independent and serine protease activity-dependent mechanism. Can antagonize antiapoptotic activity of th by directly inducing the degradation of th (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space; Single-pass membrane protein Mitochondrion membrane; Single-pass membrane protein Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment. The extramitochondrial protein does not diffuse throughout the cytosol but stays near the mitochondria. SIMILARITY: Belongs to the peptidase S1C family."}
{"protein": "MNGGQAHQRFGMQIPKFQSQNHHPHHTQQPHHHTHHNQASHNINHQHQFSSGALASATPHFTPSHMQNGAHTNVDEDIDDSMNEHWQQQLQLAAESRQANSPHYHARSVAQQAKGIQIAPSQPDTQEQGSDGQNGVGKTKAVSRQGWHALDFGGQGLRALSTSLFNYVFLEKLYLNHNKLKSLPPTIGHLRKLSHLDLSGNDLTELPDEIGMLTNLRKLYLFDNNIRTLPYEMGYLYRLDTLGIEGNPLNDVLKSHIMKEGTKALIKYLKEEMPVHLPPPDRDWVVLDETASASTEKITVLSYNTLCDSSATQSHYGYAPARVLSWEFRRELILSELRSHGSDIVCLQEIDQGSYNEYFREQLAYNDYKGVYWPRGRAMGMQEEDAKGVDGCATFFKGSKFILLDKQLINFGQTAVRRPDAKGQDDIYNRLWQKDHIAVVVFLENRQTGSRFIVVNAHLYWDPAFKDVKLIQTAILMEEITKLSETYAKWPACTDKAAFRFSKEEGQTEAPPPEEPAPSVQYSSGDQIPLLMCGDLNSSPGSAAYNLIAHGRLDEEHPDLEKRLYGNLSKVGMTHPFKLKSAYGSIGELPFTNYTPDFKDILDYIWYSSNSLHVSALLGEVDKDYLQKVPGFPNYHFPSDHIALFAEFTVKGKKGKVVEADFGPQRN", "text": "FUNCTION: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CCR4/nocturin family."}
{"protein": "MPSDYAEIRNRVEHYFDRTATRAWARLTTADEKVSKVRQTVREGRDTMRAVMLSRLPDDLTGCRVMDAGCGTGLTTVELARRGADVVAVDISPQLIDIAKDRLPPELRGKVSFHVGDMADPALGQFDYVVAMDSLIYYRAPDIGRVLTELGKRTHSAIVFTVAPKTAFLMAFWWLGKLFPRSNRSPVMIPHALDKLQRHAGDSLIKIDRVARGFYISECLEYRP", "text": "FUNCTION: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Magnesium protoporphyrin O-methyltransferase family."}
{"protein": "TPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLQQQQRSAEPMRLSMDPPLPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADG", "text": "FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Positively regulates the transcriptional repressor activity of FOXP3. Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (By similarity). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation (By similarity). SIMILARITY: Belongs to the histone deacetylase family. HD type 2 subfamily."}
{"protein": "MAQKKKSSGSGLMSSAGLMTYYDADKKAIHVQPKTVFIFGAICGIVILAFSAGFGLWP", "text": "FUNCTION: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SEC61-beta family."}
{"protein": "MPRSFLVKSKKAHTYHQHRFVEDDLPIFTWDPITSAFTAAGDRDKTPEDGKKQDLEWVVPKQEKDSFQPKEESVPVQYLSRMLPGPSAQDMSISGLQVKDCTNPTSMPTFYKTGFSWDAFQLPYSYRQMSSTMQSALLEHPVSLYGSHLLPSAEPPLDYSMRYSSDMETYHCVKCNKVFSTPHGLEVHVRRSHSGTRPFACEVCGKTFGHAVSLEQHTNIHSQERSFECKMCGKTFKRSSTLSTHLLIHSDTRPYPCQYCGKRFHQKSDMKKHTYIHTGEKPHKCQVCGKAFSQSSNLITHSRKHTGFKPFSCELCAKGFQRKVDLRRHRETQHSLK", "text": "FUNCTION: Essential transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSKLEQYFDYVKINLASPQRIKKWGERRLPNGQVVGEVTKPETINYRTLKPEMDGLFCERIFGPVKDWECHCGKYKRVRYKGIVCERCGVEVAESKVRRHRMGYIELAAPVTHVWYLKSLPSYISILLDIPLKDVEQVVYFNSYVVTKPGNCTNLRYKQLLSEDEWIAIEDQLYQEDSELTGVEVGIGAEAIQKLLRDIDLEVEAESLREEILVVKGIKKDKSIKRLRVIDNFIATRSDPTWMILTVLPVIPPDLRPMVQLDGGRFATSDLNDLYRRVLNRNNRLIRLQEILAPEIIIRNEKRMLQESVDALIDNGRRGRTVMGANNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIVVGPQLELNQCGLPREMALELFQPFVIHKLIQQGLVNNIKAAKRLIQKNELIVWNVLEEVIQGHPILLNRAPTLHRLGIQAFEPILVEGRAIKLHPLVCPAFNADFDGDQMAVHIPLSLEAQAEARMLMLAPYNFLSPATGDPIIMPSQDMVLGCYYLTAENPSQQVNRSLYFSNFDDVLLAYETKLIKLHSYVWVRFNGNVDDDDEKIEEKKLDGNKKLHIYPSRIKKLDQDNNLMVQYILTTPGRILLNNVLFDSLQLQF", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily."}
{"protein": "FDFSFLPQPPQEGLMGPRGPPGASGAPGPQGFQGPAGEPGEPGQTGPAGARGPGPPGKAGEGVVGPQGARGFPGTPGLPGFKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGSRGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNTGPGPAGPRGEQGLPGVSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRTGARGLVGEPGPAGSKGESGGKGEPGSAGPQGPPGSSGEEGKRGPSGESGSTGPTGPPGLRGGPGSRGLPGADGRAGVIGPAGARGASGPAGVRGPSGDTGRPGEPGLMGARGLPGSPGNVGPAGKEGPAGLPGIDGRPGPIGPAGARGEAGNIGFPGPKGPAGDPGKGEKGHAGLAGNRGAPGPDGNNGAQGPPGLQGVQGG", "text": "FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). SUBCELLULAR LOCATION: Secreted. Secreted, extracellular space. Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the fibrillar collagen family."}
{"protein": "MAKKKSKSRSKSSRRVLDALQLAEREINGEFDNSSDNDKRHDARRNGTVVNLLKRSKGDTNSDEDDIDSESFEDEELNSDEALGSDDDYDILNSKFSQTIRDKKENANYQEEEDEGGYTSIDEEDLMPLSQVWDMDEKTAQSNGNDDEDASPQLKLQDTDISSESSSSEESESESEDDEEEEDPFDEISEDEEDIELNTITSKLIDETKSKAPKRLDTYGSGEANEYVLPSANAASGASGKLSLTDMMNVIDDRQVIENANLLKGKSSTYEVPLPQRIQQRHDRKAAYEISRQEVSKWNDIVQQNRRADHLIFPLNKPTEHNHASAFTRTQDVPQTELQEKVDQVLQESNLANPEKDSKFEELSTAKMTPEEMRKRTTEMRLMRELMFREERKARRLKKIKSKTYRKIKKKELMKNRELAAVSSDEDNEDHDIARAKERMTLKHKTNSKWAKDMIKHGMTNDAETREEMEEMLRQGERLKAKMLDRNSDDEEDGRVQTLSDVENEEKENIDSEALKSKLGKTGVMNMAFMKNGEAREREANKETLRQLRAVENGDDIKLFESDEEETNGENIQINKGRRIYTPGSLESNKDMNELNDHTRKENKVDESRSLENRLRAKNSGQSKNARTNAEGAIIVEEESDGEPLQDGQNNQQDEEAKDVNPWLANESDEEHTVKKQSSKVNVIDKDSSKNVKAMNKMEKAELKQKKKKKGKSNDDEDLLLTADDSTRLKIVDPYGGSDDEQGDNVFMFKQQDVIAEAFAGDDVVAEFQEEKKRVIDDEDDKEVDTTLPGWGEWAGAGSKPKNKKRKFIKKVKGVVNKDKRRDKNLQNVIINEKVNKKNLKYQSSAVPFPFENREQYERSLRMPIGQEWTSRASHQELIKPRIMTKPGQVIDPLKAPFK", "text": "FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP14 family."}
{"protein": "MSAVTQVVETAIGCVIPSCIEFGSSMRIATSLGSPSVTQSPCVNRDVEDIARTARESIRFFLAELSIECVPYTQDPALEAQVASATRCWPDRERLAPHIRTGIVIAATAYAHNSLATRTLIALYTAIGVALDEPDILESANAIGFHHSLCTETSERPSAILDEWRRILARMWDHFPRFGASCILTSTLQFLNMTMLENETKGKVLNRTAMPFVEYRRMTDGFPEVYTAFIWEKGRFPDVQVYMQAIPNAMRFINFGNDILSFYKEEAAGETGTYIHDRARLTGLSSVETLREVVEETVSAWRQVCEILGEGIARDAWNSFVRGYVTFHVHNPRYRLSELL", "text": "FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to a single major terpene scaffold whose chemical structure is still unknown. SIMILARITY: Belongs to the trichodiene synthase family."}
{"protein": "MTQIKVDAIISKQFLAADLNEIRQMQEESKKQVIKMEIVWKNVALFVALHIGALVGLYQLVFQAKWATVGWVFLLHTLGSMGVTGGAHRLWAHRAYKATLSWRVFLMLINSIAFQNDIIDWARDHRCHHKWTDTDADPHSTNRGMFFAHMGWLLVKKHDQLKIQGGKLDLSDLYEDPVLMFQRKNYLPLVGIFCFALPTFIPVVLWGESAFIAFYTAALFRYCFTLHATWCINSVSHWVGWQPYDHQASSVDNLWTSIAAVGEGGHNYHHTFPQDYRTSEHAEFLNWTRVLIDFGASIGMVYDRKTTPEEVIQRQCKKFGCETEREKMLHKLG", "text": "FUNCTION: Delta(9)-fatty acid desaturase that acts preferentially on palmitoyl-CoA (hexadecanoyl-CoA) producing the monounsaturated palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA), which can be elongated to (11Z)-octadecenoyl-CoA (the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols). Also acts on pentadecanoyl-CoA, heptadecanoyl-CoA and myristoyl-CoA (tetradecanoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used as substrates to synthesize polyunsaturated fatty acids (PUFAs) by several other desaturases and elongases (PubMed:16839188, PubMed:10872837, PubMed:29237573). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
{"protein": "MLFHAAEKTGHHFTIGAAGVDVFFVISGFIMWVISDRRSVTPVEFIADRARRIVPVYWLATGVMVAGALAGLFPNLVLTLEHVLASLFFVPARSPSSGEIWPVLVQGWTLNFEMLFYAVFAGSLFMPRNWRLPVVSGLFLALVIAGRVVAFDDAVMLTYTRPVILEFVAGMIIGEFWLKGRVPPLAVGSALFACSLGGFALIGVLGLPFDELTTGPLAVLLVIGVLSLEANGCVRALSLPGLLGDASYSIYLWHTFAISVVAKAGLAIGLGAPATMFAAVLSGTLIGIAAYMMLERPLLRRGRARRVTAGLAGRAAE", "text": "FUNCTION: Required for the acetyl modification of the third sugar (glucose) of the octasaccharide subunit of succinoglycan (EPS I). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acyltransferase 3 family."}
{"protein": "MKLSWSLFCGLASLALSQFDEAPPSQSDYFVRHIPGLDSVDNYTMHSGNILTDAAHNGNLFFWLVEAQYKITERPKTIVWFNGGPGCSSMDGALLEVGPFRIVDDKLRVDPNKGSWHKYANVLFVDQPYGTGYSYSDTDSYLTGLGQVGDEMDSFMTQFLKLFPERAHDDFYLAGESYAGQYIPYIATKLQQTRTVDLKGLLIGNGWMDPANQYYQYVPYALDYGVIEKTEEHVKDLKELTDTCERAINIAKDKNNGRLPVHIRACEDIMNGIVELSRNERSAPESEGICVNYYDVSKEDKWPSCGMNWPEILPYVTDWLRQDATVQALNVNNDKQESWQECNGAVGSRMRQGNDDAAVYLLPDLLESMEILFFNGDRDLICNHYGNERMIEQLEWNGKKGWTEGLELDDWVVDGVSKGKKQSDRNLTYVRIYNASHMVPYDEPEACLTMLNDFIGVSKALSDLSGNKPGRGSENPSDLDDQKSGDQKSDDDSSSDDDDDAEHDKKIASDAMWKAYYQAGFTALIVVLIILGLAGFLFWRKNRGHIYQEETSLLGSCFGGISRWRNSSGGPLSNQQGTFDSRQRLMEPGEYYDLGEIAEEDEDAEELVIRRPEV", "text": "FUNCTION: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MNNQSENYYHGAQFEALKSAGAIEMLGDGLTGDDLAAIPEHWLSYPAPPASAHTALALLYIFFTFAALVGNGMVIFIFSTTKSLRTSSNFLVLNLAILDFIMMAKAPIFIYNSAMRGFAVGTVGCQIFALMGAYSGIGAGMTNACIAYDRHSTITRPLDGRLSEGKVLLMVAFVWIYSTPWALLPLLKIWGRYVPEGYLTSCSFDYLTNTFDTKLFVACIFTCSYVFPMSLIIYFYSGIVKQVFAHEAALREQAKKMNVESLRANQGGSSESAEIRIAKAALTVCFLFVASWTPYGVMALIGAFGNQQLLTPGVTMIPAVACKAVACISPWVYAIRHPMYRQELQRRMPWLQIDEPDDTVSTATSNTTNSAPPAATA", "text": "FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May play a role in photoperiodic photoreception. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MRRISVKKLCSFCLCACAFAFLVMTFQVIELLGQFEQTEHRQQIKRFEDIKVQANAHVSDVQYPVIVWWSPLTGELGRLGECGHNRCFFTVNKSYYSHPQTKAFLFYGTDFSIESLPLPRHKQHQWALFHEESPKNNYKLFHKPLITQFNHTATFSRHSHLPLTTQHLEDINTLTAQTHLLPLSYKNHLRQTLAPVVYVQSDCDPPSDRDTYIRELMQHIQVDSYGQCLHNKDLPPHLRDSTAMDDQDFYKILAQYKFILAFENAVCDDYITEKLWRPLKLGVVPVYYGAPNIHMWLPDNQSAIVVNPNEPPKKLAQYLKRLDKNDWEYLKYLEWKHKREITNINLLKELKERPWGVQDITQDNFIDVFECMVCSRVWENIHRQEEKLPPKVWRAEESHLTCPPPKLFDFALSSSSSLRQMWGASYEQSKREARALAQMLHTNTNFTITQFWREVFTD", "text": "FUNCTION: Probable fucosyltransferase. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 10 family."}
{"protein": "MATNKPANLNDLQKAINDISKDALKYLTDNKASVTTFHDQIGYAGYDAATLIGILKDKGGATLAQDVVKMIVMRYVRGTGFVKDVTKKTKATAGSEEAAALVARYGLVSSVGSNANAITLGRVAQLFPNVSFEVTKQFTGLKMAIDSSDLSMSGTDSLLWDFVPQYITLDSSSAPYCTTKSVAHILFSIHVIHAFLVTKKTMPEAKKKERGLLKDIDIIKYTTGLLVITCQSKNLNEAKKKSGRTKVCEPYCVNEKFKESFLALLASFGKNVVCSYGTQVKQFLAEQCSLMKTIVDNSSKTQDEMKALIIEFFEEE", "text": "FUNCTION: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC), and serves as template for viral transcription and replication (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the tenuiviruses nucleocapsid protein family."}
{"protein": "MSYKHLISACIFSSLCLGQVNAVLAEDKLPPSNTSTGQHSELSVDNDNLWQRLLRNISLAWDSPNQELYIPLNTWHNRWTYDDDKIESYNERPWGIGYGKYRYDENNNWHAVYAMAFMDSHNEVEPIIGYGYQKMWIPAEMDGWRFGVGFTASITARHEYHYIPIPLPLPLISIEYNKFSLQTTYIPGTYNNGNVLFTWMRWQF", "text": "FUNCTION: Transfers a fatty acid residue from the sn-1 position of a phospholipid to the N-linked hydroxyfatty acid chain on the proximal unit of lipid A or its precursors. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the lipid A palmitoyltransferase family."}
{"protein": "MQYNLTRIDPDAPNEQYPIGKRETVSDPLEDQVHKNIYMGKLEDVLNGAVNWGRKNSLWPYNFGLSCCYVEMTTAFTAPHDIARFGAEVIRASPRQADFMVIAGTCFIKMAPIIQRLYEQMLEPKWVISMGSCANSGGMYDIYSVVQGVDKFLPVDVYVPGCPPRPEAFLQGLMLLQESIGKERRPLSWVVGDQGVYRAEMPSQKEQRREQRIQVTNLRSPDEV", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MKIIVKIPVWMLLSLFILSPTTETIYTSGLPSLTKYFSIDGCITQITSTLYFLGFAVGILSLGRLSDIYGRRPIVLLGLFIYIVSSIISIFSVNIEMLMIARFIQAFGVSVGSVIGQSMARDSYQGAELSYVYAILSPWLLFIPSLGSYIGGYIIEYSSWHYVFVFFSLIGTILLALYYKILPETNYYIDFSQSSKYFEVFNIIIKDKILWLYAFIIGAFNGIYYGFFIEAPFILIDKMKVLPSFYGKLAFLLSFSAIFGGFLGGYLIKKRQVHDKKVMSIGFIFSLCGCILFVVNAFILEFILVSNGLAISMIFVPMMIHIIGHSLLIPITLRYALEDYAKVTGTAGSIFGAIYYIVIAAVTYCVSKIHGETISNFSLLCLVSSISSVISFYYICILYKKKSIVANEK", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Bcr/CmlA family."}
{"protein": "MNIWLNMLITTGLGAIIGGYTNHLAIKMLFRPHRPIYIGKFQVPFTPGLIPKRRDELAVQLGKMVVDHLLTPEGIGKKLTNKEFQTSLIRWTQVEVDKVITNEQSLRDMLEKWNLEHVEEEAIGKIEHVITEKIHAFLAEYYTYTWEQALPHSVHEKVENAIPNVASFILKRGISFLESEEGKERLSKMIDDFFASRGTLLNLVGMFLGNVSLVDRVQPEVIKFLGQDGTERLLTDVLQKEWEKLKGRDVKELETFVEKEMIVNSILSAVKVEETVSRFLNQSVQQVCEPVRETIVGKVVPSAVEKGLKWGTENVGSILGNLQLAEIVQQEVSTFSTERLEDLVLSITKNELKMITYLGALLGGTIGFIQGLLLLFLK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0754 family."}
{"protein": "MDSGGRIVYALNVEKTGFLRILSVTVLQRLYRRVFWFLFKCVAGIDVPRHAGSLAVFSFFFLSILYSISSGGYMNHFMKVAISNSGFLVTHVDMSGNKRMMEQDILKVLGLDEYPSMISFDIDKARFILEQQPWVRLADVQKIYPDRLRISLVEREPYAIWQHNGEMNIIDDTGYVIAPFQAGLVQNLSFVVGQGAQKTAKLFIQALSVYPQLQNHVRAYVRVGDRRWDLFLANGMRIMLPENGAIERLASFIEQGVAEDLFSRDISDIDLRLSDRITVSLSDEALTRRRAVVLEEERLLKMLKAGSV", "text": "FUNCTION: Essential cell division protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily."}
{"protein": "MATECIATVPQIFSENKTKEDSSIFDAKLLNQHSHHIPQQFVWPDHEKPSTDVQPLQVPLIDLAGFLSGDSCLASEATRLVSKAATKHGFFLITNHGVDESLLSRAYLHMDSFFKAPACEKQKAQRKWGESSGYASSFVGRFSSKLPWKETLSFKFSPEEKIHSQTVKDFVSKKMGDGYEDFGKVYQEYAEAMNTLSLKIMELLGMSLGVERRYFKEFFEDSDSIFRLNYYPQCKQPELALGTGPHCDPTSLTILHQDQVGGLQVFVDNKWQSIPPNPHAFVVNIGDTFMALTNGRYKSCLHRAVVNSERERKTFAFFLCPKGEKVVKPPEELVNGVKSGERKYPDFTWSMFLEFTQKHYRADMNTLDEFSIWLKNRRSF", "text": "FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA12 and GA53 to GA9 and GA20 respectively, via a three-step oxidation at C-20 of the GA skeleton, and GA25 is also formed as a minor product. GA53 is less effectively oxidized than GA12. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family. GA20OX subfamily."}
{"protein": "MSSSNRELVIDFVSYKLSQRGHCWSELEEEDENRTDTAAEAEMDSVLNGSPSWHPPAGHVVNGATVHRSSLEVHEIVRASDVRQALRDAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFHDGVNWGRIVAFFSFGGALCVESVDKEMRVLVGRIVSWMTTYLTDHLDPWIQENGGWERFVDLYGNNAAAELRKGQETFNKWLLTGATVAGVLLLGSLLSRK", "text": "FUNCTION: Dominant regulator of apoptotic cell death. The long form displays cell death repressor activity, whereas the short isoform promotes apoptosis. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein Nucleus membrane; Single- pass membrane protein; Cytoplasmic side Mitochondrion matrix Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytosol Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. SIMILARITY: Belongs to the Bcl-2 family."}
{"protein": "MASKLLRAVILGPPGSGKGTVCQRIAQNFGLQHLSSGHFLRENIKASTEVGEMAKQYIEKSLLVPDHVITRLMMSELENRRGQHWLLDGFPRTLGQAEALDKICEVDLVISLNIPFETLKDRLSRRWIHPPSGRVYNLDFNPPHVHGIDDVTGEPLVQQEDDKPEAVAARLRQYKDVAKPVIELYKSRGVLHQFSGTETNKIWPYVYTLFSNKITPIQSKEAY", "text": "FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates (PubMed:19073142, PubMed:19766732, PubMed:23416111, PubMed:24767988). Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor (PubMed:19073142, PubMed:19766732, PubMed:23416111). Also displays broad nucleoside diphosphate kinase activity (PubMed:19073142, PubMed:19766732, PubMed:23416111). Plays a role in controlling cellular ATP levels by regulating phosphorylation and activation of the energy sensor protein kinase AMPK (PubMed:24767988, PubMed:26980435). Plays a protective role in the cellular response to oxidative stress (PubMed:19130895, PubMed:23474458, PubMed:26980435). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily."}
{"protein": "MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFSDPRDADDARYYLDGRDFDGSRITVEASRGAPRGSRDNGSRGPPPGSGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPSPKKARQGGSYSRSPVKSRSPRRRRSPSRSRSYSRGRSYSRSRSPVRREKSVEDRSRSPKAMERSVSPKGRDQSLSPDRKVIDASPKRGSDYDGSPKENGNGRNSASPIVGGGESPVGLNGQDRSPIDDEAELSRPSPKGSESP", "text": "FUNCTION: Probably involved in intron recognition and spliceosome assembly. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family. RS2Z subfamily."}
{"protein": "MATATLNFITFNQDHGCLAVGTSRGFRIYHTEPFSKIFSSEDGNVSIIEMLFSTSLVALILSPRHLIIQNTKRGSVICELTFPSAVLAVRLNRKRLAVVLEDEIYLYDIANMSLLFTIATSPNPSAICALSPSSENCFLAYPLPKPREDKDDKRPSHAPPLPTYIPPTSGDVLIFDAITLKAVNVIEAHRSPLSCIAINSEGTLLATASETGTIIRVFTVPKGQKLYQFRRGTYPSTIYSMSFNLSSTLLCVSSTSDTVHIFRLGGPNNGASGAAGAGSAGEVLAASPGQDITGSPRADRWSRSRSYDSGNESPGSGSEANDIAGSPSPRDRPTAANRRQSGSFSNILRRSSQIMGRSVAGVVGSYLPQTVTEMWEPARDFAFIKIPKSSAARQHNNPGATPSLPIAGEPLRSVVAMSSSSPQVMVVTSDGKFYVYNINMETGGEGYLVRQYSILENDDKHDSSSTYES", "text": "FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation- induced autophagy. Involved in correct ATG9 trafficking to the pre- autophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the WD repeat PROPPIN family."}
{"protein": "MTSPSTSKNHRCLNLISKCKSLQNLKQIHAQIITIGLSHHTYPLSKLLHLSSTVCLSYALSILRQIPNPSVFLYNTLISSIVSNHNSTQTHLAFSLYDQILSSRSNFVRPNEFTYPSLFKASGFDAQWHRHGRALHAHVLKFLEPVNHDRFVQAALVGFYANCGKLREARSLFERIREPDLATWNTLLAAYANSEEIDSDEEVLLLFMRMQVRPNELSLVALIKSCANLGEFVRGVWAHVYVLKNNLTLNQFVGTSLIDLYSKCGCLSFARKVFDEMSQRDVSCYNAMIRGLAVHGFGQEGIELYKSLISQGLVPDSATFVVTISACSHSGLVDEGLQIFNSMKAVYGIEPKVEHYGCLVDLLGRSGRLEEAEECIKKMPVKPNATLWRSFLGSSQTHGDFERGEIALKHLLGLEFENSGNYVLLSNIYAGVNRWTDVEKTRELMKDHRVNKSPGISTLN", "text": "SIMILARITY: Belongs to the PPR family. PCMP-E subfamily."}
{"protein": "MAASIARGCQAAKGLGPSFRSARALLPVSTSVASRVLAGPGRRQITGPSEPGVFQPPPKPVIVDKRGPQRRESRFLSPEFIPPRGRTNPLKFQIERKDMLERRKILHIPEFYVGSILRVTTADPYANGKTSQFLGICIQRSGKGLGATFILRNTIEGQGVEICFELYNPRIQEIQVVKLEKRLDDSLLYLRDALPEYSTFDMNMKPVAQEPSREVPINQLKVKMKPKPWSKRWERPKFNVKGIRFDLCLTEEQMKEAQKWSQPWLEFDMMREYDTSKIETAIWNEIEASKSS", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family."}
{"protein": "MSHHKRRVYPQAQFGLAQAGQTGYQDVQQPGVLPSQANYQEPVPLVTPIQEVLNNQIDQTADSLHNMQLHNVPDFNQPLQGQLNGPQSPALYQNYNENGMNNYNAAFGNGGTSVKQVNQLYPIDLLSDLPPPIKDLGLPPPPINLSPDIMSVPSDKSNASPDYIRSTLNAVPKTNSLLKKTKLPFALVIKPYQHLNDDVNAPPLNEECLIVRCRRCRSYINPFAKFIEQGRRWRCNFCRLANDLPMQFDQSSIDTNIVNRLDRTEIKNAVMEYVAPKEYTVRPPPPSIYTFIIDVSQNAIKNGLFVSTIETLKQQLEYLPNRDNRTKISIILVDHALHILSIPADDVSNKFRILDVADIDEPYIPLPNSLVVSLSRCKQNVQLALEKIKQLFEINVSTKFALGPALRTAQKLIGGVGGKLIVISASLPNAGIGSLQRRNESGVSGTTKESSQLLSCQDSFYKTFTVECSKTQITIDLFLASDDYVDVATLSNLPRYTAGQTHFYPGYNASNISDFNKFTTEFSKHITMDISFETVMRARGSTGLKTSAFYGHFFNRSSDLCAFSTMPRDQSYVFDISIEDTITTDYCYFQVAVLLSLNNGQRRIRVITLALPTTQSISEVFACVDQQAVAAQITQRAVQKANSSSIDDARDLIQKTTLDILSTYKKELVVTNTGGVVPLKLSTNLRILPLLMHALMKHMAFRAGVVPSDHRAYSLNVLESVPIKSLITSIYPSIYSMHDMGDDCGYTDETGNVILPECINDTAILMEKYGLYLIDNGSELFLWVGGEAVPELLSDVFGVPEMSQVPVGKHDLFRVEGSQFNERVCNIIDQLRTSDDTTVYKTLYIVSGPTINDSFSQGTRELASLRMWAATAFVEDNIMKTLSYREFLEKMKKEVSK", "text": "FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily."}
{"protein": "MLEEEILQKLQKFGLTKYESLAYLTLLKLGPSKATDVTKESGIPHTRIYDVLSSLARKGFVDIVHGTPRLYAPVNPEIVLEKIREDLISDIERLKKAFQELYREVHGEELPEIWTVHGFENTIDRAQHIIRSAKHDILINTPYEFLEYLRGVLEKRNDVLIIVISNFSEIPLWLRNKNNVILARSGQAPWLLGTWVIGDINYALFFGTLPEDKGKERFYSFWVKSTRLIQNYVHWFYTMYFDNSEIVKPLNYERMEKPLTLSHIRTVITVLKQAGLPRNIEVIGRSLADKKQVTIKGKVIDYEYTPLTANITVKTDNKKIKVGGLGSYLEDIEGESFILLD", "text": "FUNCTION: Global transcriptional repressor of the maltodextrin transport gene cluster (mdxE operon) and most likely of all genes encoding glycolytic enzymes. Acts by binding to the conserved TGM (Thermococcales-Glycolytic-Motif) sequences in their promoter region. Can also interact with non-TGM sequences. SIMILARITY: Belongs to the transcriptional regulator TrmB family."}
{"protein": "MDMQNITDLYKIDKKTTLYPNIINKYNYMAYLLFPNNATIFNSYITKKEVFEYPMQFAIALYPVYKLYWHNINICLNNRFIYLSNEFKNNISINTVYNLLYNNELKFEDDNIIINGKNLKISYSAYSYVTIISQITINISSLNKYQIYGIIESANYLGILSSYKQNKYFDKNLFSFTKSELRSTMIDVQLKIFEIFISKKNCIISGGTGIGKTTVIPKLFWWFNLLFDGYEFWNTSNENKNINDFIFKPNFEKNKTILSLPRKALIRQMGINYIKSLGFDNISGSPIILKYKDVKKEKEYYNNNPILYPFVLSVNRITINNIKHSNSVIIDEIHEHDKFGDIAIAIARTKKKKYNIRNIVLISATIESDIDNIRIYFKNIVEIYIPGVSLFPVKEIECEDKDVISILKNYMPSVGKSVIIFYETIKKINEYKEILESILIDKIYKIYTIHSKITNINAIINKLQNDKKHIHIILSTNYLESSITITNATLVIDNGKMYQKKFLTGSTMYITESMYIQRKGRVGRISKGTYIRTYSKDLLQTTFKHINYQYLWEYILVFKYNNMDYYNDLFIKPDDPSRIENTLNYLKNINIDIDKYISLLYSKFNKYEINMVEYLSIYINNSTSDIILLNEFIDNIRNSDKYIFPYRLTEIFHKLNVRCRCINITETEEGNINCSFVILNNYDGDPFFKLSFEKSNLICRYNKIYYIVSMSPLYLID", "text": "FUNCTION: NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles (By similarity). SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily."}
{"protein": "MVFGSAASEKTPEEILKGVALMLDEIINDTTVPRNIRAAAEKAKEAVLKEGEEPIVRSATAIHILDEISNDPNMPLHTRTQIWSIVSELERVK", "text": "SIMILARITY: Belongs to the UPF0147 family."}
{"protein": "MPDHSLFRLRILPWCIALAMSGSYSSVWAEDDIQFDSRFLELKGDTKIDLKRFSSQGYVEPGKYNLQVQLNKQPLAEEYDIYWYAGEDDVSKSYACLTPELVAQFGLKEDVAKNLQWSHDGKCLKPGQLEGVEIKADLSQSALVISLPQAYLEYTWPDWDPPSRWDDGISGIIADYSITAQTRHEENGGDDSNEISGNGTVGVNLGPWRMRADWQTNYQHTRSNDDDDEFGGDDTQKKWEWSRYYAWRALPSLKAKLALGEDYLNSDIFDGFNYVGGSVSTDDQMLPPNLRGYAPDISGVAHTTAKVTVSQMGRVIYETQVPAGPFRIQDLGDSVSGTLHIRIEEQNGQVQEYDISTASMPYLTRPGQVRYKIMMGRPQEWGHHVEGGFFSGAEASWGIANGWSLYGGALGDENYQSAALGVGRDLSTFGAVAFDVTHSHTKLDKDTAYGKGSLDGNSFRVSYSKDFDQLNSRVTFAGYRFSEENFMTMSEYLDASDSEMVRTGNDKEMYTATYNQNFRDAGVSVYLNYTRHTYWDREEQTNYNIMLSHYFNMGSIRNMSVSLTGYRYEYDNRADKGMYISLSMPWGDNSTVSYNGNYGSGTDSSQVGYFSRVDDATHYQLNIGTSDKHTSVDGYYSHDGSLAQVDLSANYHEGQYTSAGLSLQGGATLTTHGGALHRTQNMGGTRLLIDADGVADVPVEGNGAAVYTNMFGKAVVSDVNNYYRNQAYIDLNKLPENAEATQSVVQATLTEGAIGYRKFAVISGQKAMAVLRLQDGSHPPFGAEVKNDNEQTVGLVDDDGSVYLAGVKPGEHMSVFWSGVAHCDINLPDPLPADLFNGLLLPCQHKGNVAPVVPDDIKPVIQEQTQQVTPTDPPVSVSANQ", "text": "FUNCTION: Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. Probably involved in the export and assembly of fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
{"protein": "MRSIRSFANDDRHVMVKHSTIYPSPEELEAVQNMVSTVECALKHVSDWLDETNKGTKTEGETEVKKDEAGENYSKDQGGRTLCGVMRIGLVAKGLLIKDDMDLELVLMCKDKPTETLLNTVKDNLPIQIQKLTEEKYQVEQCVNEASIIIRNTKEPTLTLKVILTSPLIRDELEKKDGENVSMKDPPDLLDRQKCLNALASLRHAKWFQARANGLKSCVIVLRILRDLCNRVPTWAPLKGWPLELICEKSIGTCNRPLGAGEALRRVMECLASGILLPGGPGLHDPCERDPTDALSYMTIQQKEDITHSAQHALRLSAFGQIYKVLEMDPLPSSKPFQKYSWSVTDKEGAGSSALKRPFEDGLGDDKDPNKKMKRNLRKILDSKAIDLMNALMRLNQIRPGLQYKLLSQSGPVHAPVFTMSVDVDGTTYEASGPSKKTAKLHVAVKVLQAMGYPTGFDADIECMSSDEKSDNESKNETVSSNSSNNTGNSTTETSSTLEVRTQGPILTASGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFRGAGPNKKVAKASAALAALEKLFSGPNAANNKKKKIIPQAKGVVNTAVSAAVQAVRGRGRGTLTRGAFVGAAAAPGYIAPGYGTPYGYSTAAPAYGLPKRMVLLPVMKFPTYPVPHYSFF", "text": "FUNCTION: Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth. Binds to double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Microtubule- associated that localizes to the manchette in developing spermatids."}
{"protein": "MLKKNDIVEVEISDLSHDGAGIAKVDGLVFFVDNALPTEKIRMRVLKVKKNIAFGKVESYLAKSAYRSDNLTVDYLRTGIADLGHLTYGQQLNFKRKQVINSLSKIAGISDIEVADTLGMDNPTAYRNKAQVPVRRVNGQLETGFFRKNSHALMPIEDYYIQDKEIDRLINFTRDLLRRFDLKPYDEKEQTGLIRNLVVRRGHYTGQIMLVLVTTRSKIFRIEQMIEKIISEFPAVKSIIQNINDRNTNAIFGSEFRTLYGEDTIEDTMLGNRYIISAQSFYQVNTVMAEKLYQTAIDFSDLTPDDTVIDAYSGIGTIGLSFAKKVKDVYGVEVIEAAVRDAEKNAALNNITNVHYVADSAEKAMASWSKRGIKPDVILVDPPRKGLTESFIEASTAMQPRKITYISCAPATMARDVKLYEELGYKLVKVQPVDLFPQTHHVECVALLVKA", "text": "SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family."}
{"protein": "MIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELVHLSELPPTPLHISEDSSSPERTVPQDSSVIATLVDQTIKNKVDDLEVSEPKSCVEEKSQEVQTYRNVESINVENPDFKAVGSSTGDKNERTSVAETVRKCWPNRLAKEQISKRLDGNQYLFVPPNRYIFHGAEVYSDSEDDALSSSSCGSNSDSGTCQSPSLEEPLEDESEIEEFYNGLEDDADRPECAGGSGADGGDQEAVNEAIAMKQELTDVNCTPDKSEHY", "text": "FUNCTION: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy- dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of H1-4. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa- B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates p300/EP300 and PRMT1. Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation. Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Promotes DNA double-strand breaks by mediating deacetylation of SIRT6. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacetylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome. Protects cardiomyocytes against palmitate-induced apoptosis. Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity. Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis. Involved in the CCAR2-mediated regulation of PCK1 and NR1D1. Deacetylates CTNB1 at 'Lys-49'. In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling. In addition to protein deacetylase activity, also acts as protein-lysine deacylase by mediating protein depropionylation and decrotonylation. Mediates depropionylation of Osterix (SP7). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase. Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity. Involved in the regulation of centrosome duplication. Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (By similarity). Deacetylates NDC80/HEC1 (By similarity). SUBCELLULAR LOCATION: Nucleus, PML body Cytoplasm Nucleus Note=Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane (By similarity). Shuttles between nucleus and cytoplasm (By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (By similarity). SIMILARITY: Belongs to the sirtuin family. Class I subfamily."}
{"protein": "MFRWSCAHRLSRSLCQTRFLSTDPLLDQLKICISEDQVFQLVGKNKARLSVTHVGHAINLLWKFQKEKPRMLRTIDQVRGHPEFIALRILAENKIEFMEDNALVEILYNILRFSVEPHDSLVQQLVMEGWRRLERFNLKEISKFAVCLGEQHMHMSPLMGHIASIVDGILDDVQDARILSSLMVNIHGVITPMLRDRLVDKADSLMDTLDVSHFNHPRRIVQFLRNMKHTYRPLLEKCNNAFLQNIGQMDPENLSIIIGLYQSLQYNNSEFRLMARNRLIEMVDQCNNVASYTKLFAALGPMAGQETREKLEEGILTMVDGMNPNQLLAVLGTMEEMECRNTLLIARIASLLQKYLGIYRPVELARITQAIVNLRCQTPELFSMLQKILERNLKSSFIPGDVAMLARVISSLPAARVDEEVFSKVDAILPQCSLSDLSSLALAIVKWVRTEQPSRYSTSGGLGNLLHKLNTCGHERITKIDKIDLFLEELKYITGDWLEEVLLKDAISTCERLIDQITWKNLPEFALFITRTNYLCAPVLNKIASVATEDITKIHYNATYAILLPFVVLNYEPPNGEAFFDACIQHVLPHLNSLDPHLVVLLAYSLALAEYFPEELIKAVFNIDFLGRLDAQLETFSSTLNLRIRLRLMELNRAVCLECPEFQIPWFHDRYCKQLQHRANAGISSVQRQIHQLLGEILGGINYAKVSVMTPYYHTIDFECILDKNKKPILYLDQNVLSADLSKVQWGNGGQLQETKSLPPGAQRVAIEFLDSKAFSKNSSNIKGEYMMKKRHLEILGYHVLQISSLEWNSMELSTKDAWMDYLRKRIFTDDL", "text": "FUNCTION: May regulate the stability of some mitochondrial mRNA species. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the FAST kinase family."}
{"protein": "MRAILPIPVLIAWAMVVCGGAYAVTTCSGAATATADASQQDLAALKARFRRPESVPHPKANPLTPEKVALGKALFFDPRLSRSGSVSCATCHNPSLGWSDGLTRAVGFGMVPLPRRTPPVLNLAWGTAFQWDGRADSLEAQARMPITAPDEMNMSMDLVVERLKAVPGYAPLFRNAFGSEEPIGARHVTAALATFQRTLVSGEAPFDRWALGDESAIGADAKRGFALFTGKAGCAACHSTWRFTDDSFHDIGLKAGNDLGRGKFAPPSVTAMRYAFKTPSLRDLRMEGPYMHDGQLGSLEAVLDHYIKGGEKRPSLSFEMKPFEMSERERRDLVAFLETLKAEPAAITLPQLP", "text": "FUNCTION: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MAMKLNALMTLQCPKRNMFTRIAPPQAGRVRSKVSMASTLHASPLVFDKLKAGRPEVDELFNSLEGWARDNILVHLKSVENSWQPQDYLPDPTSDAFEDQVKEMRERAKDIPDEYFVVLVGDMITEEALPTYMSMLNRCDGIKDDTGAQPTSWATWTRAWTAEENRHGDLLNKYLYLSGRVDMRMIEKTIQYLIGSGMDTKTENCPYMGFIYTSFQERATFISHANTAKLAQHYGDKNLAQVCGNIASDEKRHATAYTKIVEKLAEIDPDTTVIAFSDMMRKKIQMPAHAMYDGSDDMLFKHFTAVAQQIGVYSAWDYCDIIDFLVDKWNVAKMTGLSGEGRKAQEYVCSLAAKIRRVEEKVQGKEKKAVLPVAFSWIFNRQIII", "text": "FUNCTION: Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. Note=In green tissue, found in chloroplasts. In non-photosynthetic tissue, found in plastids. SIMILARITY: Belongs to the fatty acid desaturase type 2 family."}
{"protein": "MAPPVRLERPFPSRRFPGLLLAALVLLLSSFSDQCNVPEWLPFARPTNLTDDFEFPIGTYLNYECRPGYSGRPFSIICLKNSVWTSAKDKCKRKSCRNPPDPVNGMAHVIKDIQFRSQIKYSCPKGYRLIGSSSATCIISGNTVIWDNKTPVCDRIICGLPPTIANGDFTSISREYFHYGSVVTYHCNLGSRGKKVFELVGEPSIYCTSKDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFGMKGPSHVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQEVFYSCEPGYDLRGSTYLHCTPQGDWSPAAPRCEVKSCDDFLGQLPNGHVLFPLNLQLGAKVDFVCDEGFQLKGSSASYCVLAGMESLWNSSVPVCERKSCETPPVPVNGMVHVITDIHVGSRINYSCTTGHRLIGHSSAECILSGNTAHWSMKPPICQQIFCPNPPAILNGRHTGTPLGDIPYGKEVSYTCDPHPDRGMTFNLIGESTIRRTSEPHGNGVWSSPAPRCELPVGAGSHDALIVGKFYEVFAEEFCHL", "text": "SUBCELLULAR LOCATION: Cytoplasm Membrane Secreted Note=Predominantly found in association with the membrane fraction, but also located in the cytoplasm and in the supernatant. SIMILARITY: Belongs to the receptors of complement activation (RCA) family."}
{"protein": "MKAKREALQSLFTAMRDGKVDGDIIDLLLLINSIKGIYTTSSCSGRIGIIEEPALGAKPLSRWLIKVHRPIEFEEAKEALKNAKEGIIFLKSQPPIFHVVAEDLEKARKLHELGLASGFKYTTFKVISKRYLVEINATEYLTAPLGRDGRVLVDDGYLRFAVEIGNEMLRRSKGRLPRLEENFRRLREELGTDELFYELVEEYKIRENWELP", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72. SIMILARITY: Belongs to the TYW3 family."}
{"protein": "MSFRDLRNFTEMMRALGYPRLISMENFRSPNFPLVAEILIWLVKRYEPQMEIPSDVDTESDRVFFIKAVAQFMATKAHVKLNLKRLYQADGYAVKEMLKITSILYNAMKTKENAGGDQNNDENSKFKFDLGSKIADLKLARQLGSEITAKGAALFDLLGQEEDLRESRTAAIARPLEITETERAMRAAVKDVTESIQMTKDLLNNVSSDEASLEAKIEKKKQDLERNQKRLQTLQSVRPAFMDEYEKIEEDLEKQYQTYVEKYRNLSFLEQQLDDYHRVEQERFEEAEMAMKMRQNKLKEEEKRLMRSGVARDEDSDVDIPEDEGSDSDIDDGQQARPHHPRHTQISGRGGARFIGSMRGGDSEETEDSEIDVDDDDEDDDEDGEEDEEENEDLDEDNDSLEGSSGKPGRTNQSLHPQILEESDNDF", "text": "FUNCTION: Required for cilia biogenesis and maintenance in the kidney, the lateral line organ and eye. Appears to function within the multiple intraflagellar transport complex B (IFT-B). SUBCELLULAR LOCATION: Nucleus Cell projection, cilium. SIMILARITY: Belongs to the CLUAP1 family."}
{"protein": "MIRLSLFISLLLTSVAVLADVQINIRGNVYIPPCTINNGQNIVVDFGNINPEHVDNSRGEVTKTISISCPYKSGSLWIKVTGNTMGGGQNNVLATNITHFGIALYQGKGMSTPLILGNGSGNGYGVTAGLDTARSTFTFTSVPFRNGSGILNGGDFQTTASMSMIYN", "text": "FUNCTION: Adapter that links the PapG adhesin to the distal end of the tip fibrillum. PapF is required for the correct presentation of the adhesin at the distal end of the tip fibrillum. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs. SUBCELLULAR LOCATION: Secreted. Fimbrium. Note=At the tip of the pili."}
{"protein": "MVFGSRPPALTEANIGDQSGKVFIVTGATSGYGLLLSTYLYQNNGTVYLAARNAKKTAEVIADLKQRFPASRGRLDSISLNLSDLSTIKKSAEEFLAKETRLHVLWNNAGVMFPPAGSTTSQGYELQLGTNNVGPHLFTKLLYPTLAATAKEAPKNTVRVVWVSSDAASWAPKPAIDFNNLDYRRNESDRSKYGRSKAGTVMQAVELARRARKDGSGIVSIALDPGIANTGLQRDMGRLMSTMVKLIANKPEIGAYTQLFAGLSPEITAEVAEKEWVVPPGKIGCPRRDLFTDTETSRKWWEWNEEQVKAYL", "text": "FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non- reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MTVFKRVVALSVLALAIVPFVSAGTVASKTNTSSSKTSESCSKSEFYFKEKDCCLPSGGPTPSSTHTPTPTPPSGKSCPPNGWYWNDEKTCCLPKWPTSTPTPTPSSAHHTSTHTSPSSTPTSTPPPQCSNGWDWISSLLCCTPSSPSKPSSTPKPSATPNKGNGHHYKRAHVARAVPACPKGLDACPIAGSSLGDYECLDTSAELESCGGCASVGEGQDCTAIEGAWNVGCDRGSCKVYSCFAGFKLSSDGTSCIAL", "text": "FUNCTION: May play a role during the beginning of fruiting."}
{"protein": "MKIKKIKLLKALALTGAFGIVATVPVIVYSCSSTDNNGGTGDNNTGGGGSGTDQQQGTTYTPAIKSDVTLSGALSKIYDTTNTGDSRKNTNTLIAEDIKANPENYFTNGEDLKKVEGWSVTVDGSFDSNSVWTGDAYSKWSAVADTHKGVYKSTSKQLNINSLKDLKSQLDTSAKIKAICDESNLVFSTADADSYKIQNELGFTGGDLLHINVTATQAGKTLNMDLGIPVSDLNLKITDLKVSVTASNNSTGNNVAAVSDLTTNFTYNIGIKEEVTAPTEKPNLAKTDKGEVMKVLKALGYTQTGDETKLDNDKVSNSLGLYNCEFTAVSATPVEGSEDKFTIKLKAKPLTDYVWEDGTNTEKEISFEATFTMTGN", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the p35 lipoprotein family."}
{"protein": "MEKLRRVLSGQDDEEQGLTAQVLDASSLSFNTRLKWFVICFVAGIFFSFLGTGLLWLPNGMKLFAVFYTLGNLAALASTCFLMGPVKQLKKMFETTRLLATIIMLLCLVFTLCAALWWRKKGLALLFCILQFLSMTWYSLSYIPYARDAVLKCCSSLLG", "text": "FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SFT2 family."}
{"protein": "MGTLATRAACHGAHLALALLLLLSLSGPWLSAVVPGTPPLFNVSLDAAPEQRWLPMLRHYDPDFLRTAVAQVIGDRVPQWVLGMVGEIVSKVESFLPQPFTDEIRSICDSLNLSLADGILVNLAYEASAFCTSIVAQDSQGHIYHGRNLDYPFGKILRKLTANVQFIKNGQIAFTGTTFVGYVGLWTGQSPHKFTISGDERDKGWWWENMIAALSLGHSPISWLIRKTLSESESFEAAVYTLAKTPLIADVYYIVGGTSPKEGVVITRDRGGPADIWPLDPLNGEWFRVETNYDHWKPAPKVDDRRTPAIKALNATGQAHLNLETLFQVLSLFPVYNNYTIYTTVMSAAEPDKYLTMIRNPS", "text": "FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N- myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine. SUBCELLULAR LOCATION: Lysosome Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the acid ceramidase family."}
{"protein": "MTVLHSVDFFPSGKAPVAIEPRLPQAAFPEHHHDFHEIVIVEHGTGIHVFNGQPYTISGGTVCFVRDHDRHLYEHTDNLCLTNVLWRSPDAFQFLAGLDQLLPQEQDGYYPSHWRVNQSVLQQVRQLVGLMERAGDGMDAPAVANREILFMQLLVLLRRSSLMEGATNNDAKLNQLMAWLEDHFAEEVCWEAVAEQFSLSLRTLHRQLKQHTGLTPQRYLNRLRLIKARHLLRHSDHSVTEIAYRCGFGDSNHFSTLFRREFNWSPRDIRQGRDAIIQ", "text": "FUNCTION: Activates expression of the rhaBAD and rhaT operons. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MIIGAVEAGGTKFVDGVGNEKGEIFER", "text": "SIMILARITY: Belongs to the ROK (NagC/XylR) family."}
{"protein": "MIQHLALDALQRHLAGSPLYGWATSLPAQISARIEEGHGDLARWWSAVQRLPQVPAPKVDLAQRFALHSDHDAALQAQMKEALQGLIPWRKGPFDFFGVQVDTEWRSDWKWERVSPHVELRGKRVLDVGCGNGYYQWRMLGAGAESVVGVDPNWLFLCQFLAAKRYLPELPAWHLPLALEDLPEKLEGFDTVFSMGVLYHRRSPIDHLLALKDCLKRGGELVLETLVVEGDASTVLVPEDRYAQMRNVWFLPSVAALELWLRRAGFADARCVDVSLTSVEEQRSTEWMRFQSLPEFLDPQDRSRTVEGLPAPMRATLVARKP", "text": "FUNCTION: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L- methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5- carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoB family."}
{"protein": "MEGQGCCGGGGGKTEMIPTEEALRIVFGVSKRLPPVIVSLYEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGVTVTPGTVAYVTTGGPIPDGADAVVQVEDTKVIGDVSTESKRVKILIQTKKGTDIRRVGCDIEKDATVLTTGERIGASEIGLLATAGVTMVKVYPMPIVAILSTGDELVEPTAGTLGRGQIRDSNRAMLVAAVMQQQCKVVDLGIVRDDRKELEKVLDEAVSSGVDIILTSGGVSMGDRDFVKPLLEEKGKVYFSKVLMKPGKPLTFAEIRAKPTESMLGKTVLAFGLPGNPVSCLVCFNIFVVPTIRQLAGWTSPHPLRVRLRLQEPIKSDPIRPEFHRAIIKWKDNDGSGTPGFVAESTGHQMSSRLLSMRSANALLELPATGNVLSAGSSVSAIIVSDISAFSIDKKASLSEPGSIRKEKKYDEVPGPEYKVAILTVSDTVSAGAGPDRSGPRAVSVVDSSSEKLGGAKVVATAVVPDEVERIKDILQKWSDVDEMDLILTLGGTGFTPRDVTPEATKKVIERETPGLLFVMMQESLKITPFAMLSRSAAGIRGSTLIINMPGNPNAVAECMEALLPALKHALKQIKGDKREKHPKHIPHAEATLPTDTWDQSYKSAYETGEKKEEAGCSCTH", "text": "FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. SIMILARITY: In the C-terminal section; belongs to the MoeA family. SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family."}
{"protein": "MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVNDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKTSLEKFAVKSCLSQLYQTEPKTSVVRVRRELLPTQGPTQQLKTTKSWLQKIPLQWFKCTVKEGKLQCRI", "text": "FUNCTION: [Delta-peptide]: Viroporin that permeabilizes mammalian cell plasma membranes. It acts by altering permeation of ionic compounds and small molecules. This activity may lead to viral enterotoxic activity. FUNCTION: [Small/secreted glycoprotein]: Seems to possess an anti- inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. Does not seem to be involved in activation of primary macrophages. Does not seem to interact specifically with neutrophils. SUBCELLULAR LOCATION: [Delta-peptide]: Secreted. SUBCELLULAR LOCATION: [Small/secreted glycoprotein]: Secreted. SIMILARITY: Belongs to the filoviruses glycoprotein family."}
{"protein": "MGQKFNHGVLFYHEHSGLKDIYEGLGEVTKSLTTMCKHLSIQLSENEGDIIKYCERIKNQEYSSDVDIVFILGGDGTVNELVNGVLANDLNVPIGIIPGGTFNDFTKTLNLNPNFSKASEQLKTSHLESYDVMKVNGTYVLNFVGLGLIVQNAENVQEGRKDIFGKLSYVGSTVKTLMNPEDFDYTLTVDDKELNGNTSMLVVANGPNIGGSRIPLMDLSPQDGKLNSFIFDKQSFTILNDVFKKRDSMDWNEITNGIDHIAGKHITLSTDPVMKVDIDGEISLETPITIEVLPKALQILTFPENAEQ", "text": "FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids other than diacylglycerol (DAG). SIMILARITY: Belongs to the diacylglycerol/lipid kinase family."}
{"protein": "MSTFPVLAEDIPLRERHVKGRVDPHFRAPKMEMFQRLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
{"protein": "MALLQISEPGMSSAPHQRRLAAGIDLGTTHSLVATVRSGQPETLADHQGRHLLPSVVHYQAQGYNVGYDARAQAADDPVNTISSVKRLMGRSLADIQARYPHLPYQLRASENGLPMIDTPAGLLNPVRVSADILKALAERAREALAGDLDGVVITVPAYFDDAQRQGTKDAARLAGLHVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISVLRLSRGVFEVLATGGDSALGGDDFDHLLADYIREQAGIADRSDNRIQRQLLDAATQAKIELSDADVAQVNVAGWQGSITREQFNELIAPLVKRTLLSCRRALKDAGVEASDVLEVVMVGGSTRVPLVRERVGEFFGRTPLTSIDPDRVVAIGAAIQADILVGNKPDSEMLLLDVIPLSLGLETMGGLVEKVIPRNTTIPVARAQEFTTFKDGQTAMAIHVMQGERELVQDCRSLARFTLRGIPAMPAGGAHIRVTFQVDADGLLSVTAMEKSTGVEASIQVKPSYGLTDGEIASMIQDSMSFAEQDVQARMLAEQKVEAARVLESLDGALKSDGALLSAAERAAIDDAMAQLRAAAEGNDASAIEDAIKNTDKQTQEFAARRMDESIRQALKGHSVDEV", "text": "FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MQVLHVCSELFPLLKTGGLADVVGALPAAQIAAGDDTRVLLPAFPDLKKGITQIQVVAQLQTFAGYVELHFGHFNGVGIYLIDAPGLYDRPGSPYHDESQYAYSDNYLRFALLGWVSCELACGLDPWWRPEVVHAHDWHAGLSCAYLAARGRPAKSVFTVHNLAYQGLFNARHMEQIQLPHSFFDVYGMEFHGQISYLKAGLFYADHVTAVSPTYAREITQPEFGYGMEGLLKQRLLEGRLSGILNGVDPAIWNPAHDLLLAARYNRDVLDAKRENKRQLQIAMGLKIDEKAPIFAVVSRLTKQKGLDLVLEALPGLLEQGGQLVVLGAGDAELQQGFLAAAAENPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQLYALKYGTLPLVRRTGGLADTVNDCSLENLADGIASGFSFEDSNAWSLLRAIRRSFVLWSRPSLWRYVQRQAMGMDFSWQVAAVAYRDLYQRLL", "text": "FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. SIMILARITY: Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily."}
{"protein": "MSVKIFNGEFDIPENSRSLYILVIATTDISLIPGLTVAGATPELTHFTPAADAEFLIKGKCSVINTVPVTPNGIPTPAIITRASLEFVKIPRLVVNAGSRIKPNLPLIDLGGEPGGDIRKGSLRKEVAERILNNGVSLGEEFSNSFDFLIIGESIPAGTTTAMAVLVGLGYDALDKVSSASPENPKELKKKIVYEAIKDLPSDLMGKLAKLSDPMLLGVSGIALGFKGKILLAGGTQMTAAAAIIKEFNKNKLKDIAIGTTKWIINDRSSDIIGLAKAVGIPILAAWLDFTNSKFEGLKVYEKGFVKEGVGAGGASIYAMKRGVTNEQILGKVEEIYQRITTNLM", "text": "SIMILARITY: Belongs to the UPF0284 family."}
{"protein": "MNSKKIGAMIAAAVLSLIVMTPAATRKIVQRQTRNSSTAVENSAADESETENVPVSQTHTNDTMTVTSAKDLVAKMTNGWNLGNTMDATAQGLGSEVSWLPLKVTTNKYMIDMLPEAGFNVLRIPVSWGNHIIDDKYTSDPAWMDRVQEIVNYGIDNGLYVILNTHHEEWYMPKPSEKDGDIEEIKAVWAQIADRFKGYDEHLIFEGLNEPRLRGEGAEWTGTSEAREIINEYEKAFVETVRASGGNNGDRCLMITGYAASSAYNNLSAIELPEDSDKLIISVHAYLPYSFALDTKGTDKYDPEDTAIPELFEHLNELFISKGIPVIVGEFGTMNKENTEDRVKCLEDYLAAAAKYDIPCVWWDNYARIGNGENFGLMNRADLEWYFPDLIETFKTYAEKDPASAE", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MLYSLAQKFMFQMDAEQAHDLAIKSLKFTANSPLACGYSQALQSSPVNCMGITFPNPVGLAAGLDKDGEAIDAFHAMGFGFVEVGTVTPKPQAGNDKPRLFRLTKAKAIINRMGFNNKGVDNLVRNLQAKKTDILVGVNIGKNKDTPVEQGKDDYLICMDKVYPYAAYITVNISSPNTPGLRTMQYGALLDELLASIKAKQAELAEKYHRYVPVALKIAPDLTADEIESIAMSLISNQFDAVIATNTTLSRDGVEGMTHGTEMGGLSGAPLTAASTMVIKQLASFLNKKIPIIGVGGINSAQDALDKFDAGANLVQIYSGFIYQGPKIIKEIVNAVKMK", "text": "FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily."}
{"protein": "MGSELESAMETLINVFHAHSGQEGDKYKLSKKELKDLLQTELSGFLDVQKDADAVDKVMKELDENGDGEVDFKEYVVLVAALTVACNNFFWETS", "text": "FUNCTION: Small calcium binding protein that plays important roles in several biological processes such as Ca(2+) homeostasis, chondrocyte biology and cardiomyocyte regulation (PubMed:11909974, PubMed:16952982). In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers conformational changes. These changes allow interactions with specific target proteins and modulate their activity. Regulates a network in cardiomyocytes controlling sarcoplasmic reticulum Ca(2+) cycling and mitochondrial function through interaction with the ryanodine receptors RYR1 and RYR2, sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and mitochondrial F1-ATPase (PubMed:17438143). Facilitates diastolic Ca(2+) dissociation and myofilament mechanics in order to improve relaxation during diastole (By similarity). SUBCELLULAR LOCATION: Cytoplasm Sarcoplasmic reticulum Mitochondrion. SIMILARITY: Belongs to the S-100 family."}
{"protein": "MREIVHLQTGQCGNQIGAAFWQTISGEHGLDASGVYNGTSELQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTVSLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAHHFRAVSVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGKVSMKEVEDQMRNVQNKNSSYFVEWIPNNVQTALCSIPPRGLKMSSTFVGNSTAIQELFKRIGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDAGVDEEEEEYEEEAPLEGEE", "text": "FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the tubulin family."}
{"protein": "MANVLCNRARLVTYLPGFYSLVKRVVNPKAFSTAGSSGSDEPHVAATPPDLCPRTVWPDEVMGPFGPQDQRFQLPGNIGFDCHLNGTAAQRKSQASKSLPDILAEPSPNERHEFVMAQYINEFQGSDVPQKQQVNNAETYFENAKVECAVQACPELLRKDFESMFPEVNANHLTVLTVTQKTKNDMTVWSQEVEDEREMLLENFINGAKEICYAICSEGYWADFIDPSSGLAFFGPYTNNTLFETDERYRHFGFSVDDLGCCKVIRHNIWGTHVVVGSIFTNAEPDSPIMRKLSGN", "text": "FUNCTION: Involved in cobalamin metabolism and trafficking. Plays a role in regulating the biosynthesis and the proportion of two coenzymes, methylcob(III)alamin (MeCbl) and 5'-deoxyadenosylcobalamin (AdoCbl). Promotes oxidation of cob(II)alamin bound to MMACHC. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR (methionine synthase) which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion."}
{"protein": "MEEVPHDCPGADSAQAGRGASCQGCPNQRLCASGAGAAADPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFLEDNLGVMSVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVQYLTAAHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENMSGFICPKCQKESQIFPPTTGGAEAMCQDLKIPLLGKVPLDPRIGKSCDKGQSFLVEAPDSPATVAYRSIIQRIQEFCSQRLPEGENLVGS", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Implicated in the regulation of centrosome duplication. Negatively regulates cilium formation and structure. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell projection Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis. Localized at centrioles and in the nucleus at interphase. Colocalizes with nubp-2 at prometaphase. Specifically localizes to the axenome of motile cilia as opposed to primary non- motile cilia. Localization is independent of NUBP2 and KIFC1. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily."}
{"protein": "MVALKSFRHSGPSFADLVPYAGLVDNGVILLKDGSLMAGWYFSGPDSESSTDAERNDVSRQINAILSRLGSGWMIQVEAVRVPTADYPKESDCHFPDLVTRAIDAERRAHFQKERGHFESRHALILTWRPPEPRRSGLTRYIYSDTASRSATYADKALESFSTSIREVEQYLANVVSIRRMMTRETSERGCFRVARYDELFQFIRFCVTGQNHPVRLPEIPMYLDWLVTAELQHGLTPLIENRFLGVVAIDGLPAESWPGILNALDLMPLTYRWSSRFVFLDAEEARANLERTRKKWQQKVRPFFDQLFQTQSRSLDQDAMMMVAETEDAIAEASSQLRAYGYYTPVIVLFEEDQARLQEKCEAVRRLIQAEGFGARIETLNATDAFLSSLPGVSYANIREPLINTRNLADLIPLNSVWSGSAVAPCPFYPPASPPLMQVASGSTPFRLNLHVDDVGHTLIFGPTGSGKSTLLSLIAAQFRRYSGAQIFAFDKGGSMLSLTLGIDGDHYQIGGDATEGGDGKALSFCPLADLTTDGDRAFAAEWIEMLVALQGVTITPDYRNAISRQVGLMAESRGRSLSDFVSGVQMREIKDALHHYTVDGPMGQLLDAEEDGLALGSFQCFEIEELMNMGERNLVPVLTYLFRRIEKRLTGAPSLIILDEAWLMLGHPVFRDKIREWLKVLRKANCAVVLATQSISDAERSGIIDVLKESCPTKICLPNGAAREPGTREFYERIGFNERQIEIVATAIPKRDYYVVSPEGRRLFDMALGPVALSFVGASGKEDLKRIRALHSEHGAAWPLQWLQQRGIAHADTLFPAD", "text": "SIMILARITY: Belongs to the TrbE/VirB4 family."}
{"protein": "MIKSNRITACALAALFAGASFSASAWWGGPGYGNGLWDNMGDMFGDGYGDFNMSMGGGGRGYGRGYGRGNGYGYGAPYGYGAPYGYGAPYGYGAPYGYGAPYGAMPYGAMPPQMPAAPAQPQAAPSR", "text": "FUNCTION: Structural protein of the sulfur globules, which are intracellular globules that serve for sulfur storage in purple sulfur bacteria. SIMILARITY: To C.vinosum CV2 and T.roseopersicina TR0."}
{"protein": "MVSMTFKRSRSDRFYSTRCCGCFHVRTGTIILGTWYMVVNLLMAILLTVEVTHPNSMPAVNIQYEVIGNYYSSERMADNACVLFAVSVLMFIISSMLVYGAISYQVGWLIPFFCYRLFDFVLSCLVAISSLTYLPRIKEYLDQLPDFPYKDDLLALDSSCLLFIVLVFFVVFIIFKAYLINCVWNCYKYINNRNVPEIAVYPAFETPPQYVLPTYEMAVKIPEKEPPPPYLPA", "text": "FUNCTION: May function in the transport of nucleosides and/or nucleoside derivatives between the cytosol and the lumen of an intracellular membrane-bound compartment. SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Note=May reside in an intracellular membrane-bound compartment. SUBCELLULAR LOCATION: [Isoform Short]: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LAPTM4/LAPTM5 transporter family."}
{"protein": "MESEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRYTGVMVGMGQKDSYIGDEAQSRKGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYSLPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAELQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYSNVVLSGGSTMFPGIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLPTFQQMWISKEEYDESGPSIVHRKCF", "text": "FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
{"protein": "MASRVICFLSLNLLLLDVITRLQVSGQLQLSPKKVDAEIGQEVKLTCEVLRDTSQGCSWLFRNSSSELLQPTFIIYVSSSRSKLNDILDPNLFSARKENNKYILTLSKFSTKNQGYYFCSITSNSVMYFSPLVPVFQKVNSIITKPVTRAPTPVPPPTGTPRPLRPEACRPGASGSVEGMGLGFACDIYIWAPLAGICAVLLLSLVITLICCHRNRRRVCKCPRPLVKPRPSEKFV", "text": "FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T- lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=CD8A localizes to lipid rafts only when associated with its partner CD8B."}
{"protein": "MEDDEDIRSQGSDSPDPSSSPPAGRITVTVASAGPPSYSLTPPGNSSQKDPDALALALLPIQASGGGNNSSGRPTGGGGREDCWSEAATAVLIDAWGERYLELSRGNLKQKHWKEVAEIVSSREDYGKIPKTDIQCKNRIDTVKKKYKQEKVRIANGGGRSRWVFFDKLDRLIGSTAKIPTATSGVSGPVGGLHKIPMGIPMGSRSNLYHQQAKAATPPFNNLDRLIGATARVSAASFGGSGGGGGGGSVNVPMGIPMSSRSAPFGQQGRTLPQQGRTLPQQQQQGMMVKRCSESKRWRFRKRNASDSDSESEAAMSDDSGDSLPPPPLSKRMKTEEKKKQDGDGVGNKWRELTRAIMRFGEAYEQTENAKLQQVVEMEKERMKFLKELELQRMQFFVKTQLEISQLKQQHGRRMGNTSNDHHHSRKNNINAIVNNNNDLGNN", "text": "FUNCTION: Transcription regulator that may repress the maturation program during early embryogenesis. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAIPEEFDILVLGGGSSGSCIAGRLANLDHSLKVGLIEAGENNLNNPWVYLPGIYPRNMKLDSKTASFYTSNPSPHLNGRRAIVPCANILGGGSSINFMMYTRGSASDYDDFEAEGWKTKDLLPLMKKTETYQRACNNPEIHGFEGPIKVSFGNYTYPVCQDFLRATESQGIPYVDDLEDLVTAHGAEHWLKWINRDTGRRSDSAHAFVHSTMRNHDNLYLICNTKVDKIIVEDGRAAAVRTVPSKPLNAKKPTHKVYRARKQIVLSCGTISSPLVLQRSGFGDPIKLRAAGVKPLVNLPGVGRNFQDHYCFFSPYRIKPQYESFDDFVRGDANIQKKVFDQWYANGTGPLATNGIEAGVKIRPTPEELSQMDESFQEGYREYFEDKPDKPVMHYSIIAGFFGDHTKIPPGKYMTMFHFLEYPFSRGSIHITSPDPYATPDFDPGFMNDERDMAPMVWSYKKSRETARKMDHFAGEVTSHHPLFPYSSEARAYEMDLETSNAYGGPLNLTAGLAHGSWTQPLKKPAGRNEGHVTSNQVELHPDIEYDEEDDKAIENYIREHTETTWHCLGTCSIGPREGSKIVKWGGVLDHRSNVYGVKGLKVGDLSVCPDNVGCNTYTTALLIGEKTATLVGEDLGYTGEALDMTVPQFKLGTYEKTGLARF", "text": "FUNCTION: Minor isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts. FUNCTION: Minor isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts. SUBCELLULAR LOCATION: Peroxisome matrix. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MSRNVDKSQTVLALYQEHKAESRRDYNRYKRPRVESVRDPAEAREWYKQTLREVGECTNRLYDPLLSEEQVRECNARVNQLIQESQRWSRHLRRFKQRQRPPVYGGVVVNGVRYIGRARELPEARKRPTAARQFTVKRAKYVDFSDNGDFSDNGDYRGTSERLRKAHGIAQQESVLVEPPTQQQMEEYLVERRKRQLLHQLNL", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ISY1 family."}
{"protein": "MSYKNRLTACFDDILKVSAEMMMQQQLKNVQLDPYMVNGFSAQQQNTLKEKIHMFHGILDDLENMLSKSTYYVDTLANLGKESKRQKELELEKQREQEEEEKKQKLLELERKKKEQEEEEEKKKKQKEEEEKRKKELEEQERKKKEQEEEEKRRRQQEQDGDKQQSMFDGLDFTNADLDTSQPGTSGQNDIKSPTMGAGPQTAGTDKPNTADGPDKTNPPIAAFGLGDSQSGGLYNDLNTMDLSMFSELDGGGFDASGFDTANTSNANATTNSVPNNNNPATNDSNMNNDPTAAINAFDGTAAGNNETLGQGEKLEFDQSNPSAMLGNDINMGDNGEDYLTLNDFNDLNIDWSAAGEGGDLDLNGFNI", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 2 family."}
{"protein": "MGDIVLSARAITKRFTEGRLDVTVLQGVDLDVRAGETLAIVGASGSGKSTLLHLMGGLDAPTSGSVFLHGQDLAHQSAAAQGRLRNQYLGFVYQFHHLLPEFSALDNVAMPLWIRRLAPAESTHTATEMLAKVGLQERLAHRPSELSGGERQRVAIARALVTRPACVLADEPTGNLDRSTANGVFELMLELARVQGTAFVMVTHDESLAERCSRRIRLVQGRLLEAF", "text": "FUNCTION: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Lipoprotein translocase (TC 3.A.1.125) family."}
{"protein": "MSVPAFIDVTEEDQAAELRAYLKSKGAEISEENSEGGLHIDLAQIIEACDVCLKDDDKDVESSMNSVVSLVLILETDKQEALIESLCEKLVKFREGERPSLRLQLLSNLFHGMDKSIPARYTVYCGLIKVAATCGAIIYIPTDLDQVRKWISDWNLSTEKKHIVLRLLYEALVDCKKSDEAAKVMVELLGSYTDDNASQARLDAHKCIVRALKDPKAFLLDHLLALKPVKFLEGELIHDLLTIFVSAKLSSYVKFYQNNKDFIDSLGLSHEQNMEKMRLLTFMGMAVDNKEISFDTIQQELQIGADEVEAFIIDAVKTKMVYCKIDQTQKRVVVSHSTHRTFGKQQWQQLYDTLNTWKQNLNKVKNSLYSISDA", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit M family."}
{"protein": "MAFLKKSLFLVLFLGLVSLSICEEEKRENEDEEEQEDDEQSEMKRGLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAVGEQ", "text": "FUNCTION: Cationic amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-negative and Gram-positive bacteria, fungi and protozoa (PubMed:8306981, PubMed:12709067, PubMed:16401077, PubMed:18637027, PubMed:19113844). Acts in a synergistic effect in combination with Plasticin-B1 at doses that are not active alone (PubMed:12709067). Acts by disturbing membrane functions (PubMed:19113844). On model mebranes, induces a strong perturbation of anionic lipid bilayers, resides at the hydrocarbon core-water interface, parallel to the plane of the membrane, and interacts preferentially with the polar head groups and glycerol backbone region of the anionic phospholipids, as well as the region of the lipid acyl chain near the bilayer surface (PubMed:19113844). It induces a positive curvature of the bilayer and clustering of anionic lipids, consistent with a carpet mechanism, that may lead to the formation of mixed peptide-phospholipid toroidal, transient pores and membrane permeation/disruption once a threshold peptide accumulation is reached (PubMed:19113844). Also enhances binding of agonists to adenosine A1 receptors (ADORA1), adenosine A2a receptors (ADORA2A), alpha-2 adrenergic receptors (ADRA2A) and 5-hydroxytryptamine 1A receptors (HTR1A) (PubMed:1438301, PubMed:8565049). In addition, it enhances guanyl nucleotide exchange which may result in the conversion of receptors to a high affinity state complexed with guanyl nucleotide free G-protein (PubMed:7842473). It affects human behavior eliciting profound malaise, followed by listlessness and then euphoria. It does not show cytotoxic activity on CHO cells (PubMed:19113844). It does not act as a chemoattractant (PubMed:18637027). It does not show hemolytic activity (PubMed:8306981, PubMed:19113844). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Firstly parallelly oriented to the membrane surface, the peptide may mix to phospholipids, forming toroidal and transient pores in the membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MATGFSFGSGTLGSTTVAPGGTGTGSGFSFGASSTPSVGLNFGTLGSSATPASTSTSASGFGTGLFGSKPGTGFTLGGTSAGTTATTSASTTGFSLGFSKPAASATPFALPVTSTTASGLTLSSALTSAPAASTGFTLNNLGATPATTTAASTGLSLGGALAGLGGSLFQSGNTATSGLGQNALSLSLGTATPTSAASSEGLGGIDFSTSSDKKSDKTGTRPEDSKALKDENLPPVICQDVENLQKFVKEQKQVQEEISRMSSKAMLKVQEDIKALKQLLSLAASGLQRNTLNIDKLKLETAQELKNAEIALRTQKTPPGLQHENTAPADYFRVLVQQFEVQLQQYRQQIEELENHLATQANNSHITPQDLSMAMQKIYQTFVALAAQLQSIHENVKVLKEQYLSYRKMFLGDAGDVFEARRTEAKKWQNAPRVTTGPTPFSTMPNAAAVAMAATLTQQQQPATGPQPSLGVSFGTPFGSGIGTGLQSSGLGSSNLGGFGTSSGFGCGTTGASTFGFGTTDKPSGSLSAGFGSSSTSGFNFSNPGITASAGLTFGVSNPASAGFGTGGQLLQLKRPPAGNKRGKR", "text": "FUNCTION: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. SIMILARITY: Belongs to the NUP58 family."}
{"protein": "MSREQIIKDGGNILVTAGAGSGKTTILVSKIEADLKENKTHYSIAAVTFTNKAAKEIEGRLGYSSRGNFIGTNDGFVESEIIRPFIKDAFGNDYPDNFTAEYFDNQFASYDKGLQVLKYQNILGTYSNPKKNFKFQLALDILKKSLVARQYIFSKYFKIFIDEYQDSDKDMHNLFMYLKDQLKIKLFIVGDPKQSIYIWRGAEPENFNGLIENSTDFNKYHLTSNFRCCQDIQNYSNLFNEETRSLIKEKNEVQNVISIADDMPISDILLKLTEEKQVLNIEAELVILVRRRNQAIEIMKELNEEGFNFIFIPQTPLDRATPNATLLKEVIKYVKNDRYSIYDLAAEIVGNLSSREIKEIQKIINELLVPNINQVLINQVLINLFAKLEITLDTREITAFTEVMMTNEFDIAFDTNEYLHKIFTVHSAKGLEFNQVIITASDYNVHYNRDTNEHYVATTRAKDKLIVIMDNKKYSDYIETLMKELKIKNIIKSI", "text": "FUNCTION: Component of antiviral defense system Gabija type I, composed of GajA and GajB. Expression of Gabija type I in B.subtilis (strain BEST7003) confers resistance to phages phi105, phi29, rho14, SpBeta and SBSphiC (PubMed:29371424). Expression of Gabija type I in E.coli B (strain ATCC 11303) confers resistance to phage T7 (PubMed:33885789). May be a helicase or contribute to GajA activation (Probable). SIMILARITY: Belongs to the helicase family."}
{"protein": "MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKAFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK", "text": "FUNCTION: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop- containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. SUBCELLULAR LOCATION: Cytoplasm Microsome Endoplasmic reticulum Nucleus Note=The tyrosine phosphorylated form bound to RNA is found in microsomes (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleoplasm Note=Expressed predominantly in the nucleoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm Note=Expressed predominantly in the nucleoplasm. SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm Note=Expressed predominantly in the nucleoplasm."}
{"protein": "EIQRRFLTCGDPSLQCDYGVIMVYGVQFSTIELSSNERPKACSDTEAKNGPSNRCDGNEKCDVATSGSVCDLCNSAYLTNIFLDVTYGCLESKKVTTCEGVVHLECGDGVVFLQKALYGRIDSQTCSQGRPQSQLTNTKCSQEGTLALWSQRCDGKQTCEVNMRVNQISDPCVGTYKYLDVTYICLPAKTSITCEGSTSSLDCGKGVIKVFHANYGRRDGSTCSAGRHELSNQNCLQPKTLDVVKQWCEGKSQCTLGLDPVFGDPCFGTYKYLEVSYTCLGGSPTV", "text": "FUNCTION: L-rhamnose binding lectin. Has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. Hemagglutinating activity is inhibited by smooth-type lipopolysaccharide (LPS) from K.pneumoniae, E.coli K-235, S.flexneri 1A, A.salmonicida and S.minnesota and rough-type LPS from S.flexneri, but not by rough-type LPS from E.coli K12 and E.coli EH100. Agglutinates E.coli K12 and B.subtilis."}
{"protein": "MPELPEVETVRRTLTGLVKGKTIKSVEIRWPNIIKRPAEPEEFARKLAGETIQSIGRRGKFLLFHLDHYVMVSHLRMEGKYGLHQAEEPDDKHVHVIFTMTDGTQLRYRDVRKFGTMHLFKPGEEAGELPLSQLGPEPDAEEFTSAYLKDRLAKTNRAVKTALLDQKTVVGLGNIYVDEALFRAGVHPETKANQLSDKTIKTLHAEIKNTLQEAIDAGGSTVRSYINSQGEIGMFQLQHFVYGKKDEPCKNCGTMISKIVVGGRGTHFCAKCQTKK", "text": "FUNCTION: Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base. SIMILARITY: Belongs to the FPG family."}
{"protein": "MAMSNTSALASKLLPSCKPHQPTLTFFSPSTTCQKKPRSSRPISAAVHVTQPPKTPISSATATKRRLSLLNGVWESWKSKKALQLPEYPDEGKLDGVLKTIEAFPPLVFAGEARSLEEKLAQAAMGNAFLLQGGDCAESFKELMPLYSRYFQNTASDECRLTFGGQCPVIKVGRMAGQFAKPRLDPFEEKDGLWLSGANGWPVAWEAYCKLQQLSPSRALLLVVCCYAESHPMDLDFVEHSEQGDRYQELAHRVDEALGFMDACGLTVDHPIMATTEFWTSHECLLLPYEQALTREDSTSGLFYDCSAHMLWVGERTRQLDGAHVEFLRGVANPLGIKVSQKMDPNELVNLIEILNPTNKPGRITVIVRMGAENMRVKLPHLIRAVRGAGQIVTWVCDPMHGNTIKAPCGLKTRAFDAILAEVRAFYDVHEQEGTLPGTECVGGSRTITYDDRQTRYHTHCDPRLNASQSLELAFIIAERLRKEESVLNAHSP", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-II DAHP synthase family."}
{"protein": "MSAPINGTVEKSYVPGAELWCQEDETAITEPYTYVNSMPGKDVRGRFIEAANHWLHVEPEPLAVICKIVAMLHNASLVIDDIEDNSQLRRGQPVAHKIYGLAQAINSANYVYFLALKEADQLKPYQREGYNSHEIILGALTSVSDFAAQDLLYSVFSDELVNLHRGQGLELVWRDSLRCPTEEQYIDMVNKKTGGLFRLAIKLLTACSSNPSTIDYVPLFNLFGVFFQIRDDLMNLDDNEYEKNKGFAEDLTEGKFSFPVIHGITAQKDNSVLINVLQKRPTTPPLKLHAIHHLRNNTGSFKYTETILNSLETRLRGEIDALGGNPGLLKLVDLLSVRK", "text": "FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of erinacines, cyathane- xylosides that show unique biological activities, including leishmanicidal activity, stimulating activity for nerve growth-factor synthesis, and agonistic activity toward the kappa opioid receptor (PubMed:28371074, PubMed:31535864). The geranylgeranyl diphosphate (GGPP) synthase eriE catalyzes the first step in erinacines biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (By similarity). GGPP is then substrate of the diterpene cyclase eriG for the production of cyatha-3,12-diene. The cytochrome P450 monooxygenase eriI then hydroxylates cyatha-3,12-diene at C-14 of the seven-membered ring to produce erinacol, which is further hydroxylated at C-15 by the cytochrome P450 monooxygenase eriC to yield cyathadiol. The cytochrome P450 monooxygenase eriA then catalyzes C-11 hydroxylation in the presence of the short chain dehydrogenase/reductase (SDR) eriH, which leads to the production of cyathatriol. The acetyltransferase eriL converts cyathatriol into 11-O-acetyl-cyathatriol. The SDR eriH catalyzes further oxidation of 11-O-acetyl-cyathatriol into 1-O- acetylcyathin A3. Finally, the glycosyl transferase eriJ tranfers xylose from UDP-xylose onto C-14 of 11-O-acetyl-cyathatriol to form eracine Q. EriJ is also able to convert 11-O-acetyl-cyathatriol to eracine Q2 by using UDP-D-glucose as cosubstrate, but at a lower rate. In the absence of eriL and eriJ, the SDR eriH is able to convert cyathatriol to cyathin A3; this is likely a switching mechanism in the biosynthesis of cyathins (C-14 ketogroup)and erinacines (C-14 glycosylated group). The roles of the SDR eriB, the polyprenyl transferase eriF and the dehydrogenase eriK have still to be identified (Probable). SIMILARITY: Belongs to the FPP/GGPP synthase family."}
{"protein": "MEMTNAQRLILSNQYKMMTMLDPDNAERYRRLQTIIERGYGLQMRELDREFGELTEEVCRTIINIMEMHHALQVSWTNLKDKQDLDERRLTFLGFDAATEARYLGFVRFMVHVEGRYPHFDAGTHGFNAQTKMWEKYNRMLAVWQSCPRQYHLSAVEIAQIINA", "text": "SIMILARITY: Belongs to the UPF0304 family."}
{"protein": "MACGFRRSIACQLSRVLALPPESLIKSISAVPVSKKEEVADFQLSVDSLLEDNNHKSQVDTQDQARRLAEKLKCDTVVTAISAGPRTLNFKINRELLTKAVLQQVTEDGCKYGLKSELFSDLPKKRIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEEKLQTNPLQHLFDVYVQVNKEATDDKNVTKLAHEFFHRLEMGDTQALSLWQRFRDLSIEEYTQIYKRLGIYFDEYSGESFYREKSQDVLKLLDSKGLLQKTAEGNVVVDLSGTGDLSSVCTVMRSDGTSLYATRDLAAAIHRMDKYNFDTMIYVADKGQRRHFQQVFQMLKIMGYDWAERCQHVPFGIVKGMKTRRGGVTFLEDVLNEVQSRMLQNMASIKTTKQLENPQETAERVGLAAVIIQDFRGTLLSDYQFSWDRVFQSRGDTGVFLQYTHARLCSLEETFGCGYLNDSNVACLQEPQSVSILQHLLRFDEVLYLSSQDLQPKHIVSYLLTLSHLAAVAHKTLQVKDSPPDVAGARLHLFKAVRSVLANGMKLLGITPVCRM", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MSEWDYKIFWDEAVNQFKEELAFSIFSMWFLPSKYEKSTENTVYLSVPSKFFRDQMIHNYKNGIEKKLFELSGKKISIDFIIKPNTSEDLSKAENEGGNDKKEDAAKPSSAESKKKSVKTEGGRGQHPDLRPEYNFEDFVVGPNNNFGVNAAIAVSTNPGSAYNPFLIYGGVGLGKTHLMQAIGNKIWDTTKLKVIYVTAENFTNEFVECVQKKMMPAFKSKYRKADVLLIDDIHFFQGKVETQEELFHTFNELYEKNKQIVFTCDRPPAELKNLSQRLKSRFERGLNVDLQTPAYEIRYAILLKKMEKHSTKIPNEFIDMVAKNVSSNVRDLEAALTKLIAYTELTKKTMDEATAKNLLRDIFGSTRQRNVTIDLIQRTVADYFSISISDIKSKKRTKSFSFPRQIAMFLCREMTECSTTELGNDFGGRDHTTILHGCNKIEEQIAADPSLEKIIHELRNTIKENTNK", "text": "FUNCTION: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaA family."}
{"protein": "MAGIKHRRDSAESINTDIITLSRFILDQQHLSAKNATGEFSMLLNSLQFAFKFISQTIRRAELVNLIGLAGASNSTGDQQKKLDVLGDEIFINAMKASGNVKVLVSEEQEDLIVFRNSPGKYAVCCDPIDGSSNLDAGVSVGTIVSLFKIHENQNGNSGEEDSEGTINDVARCGREMVAACYTMYGASTHLVLTTGAGVNGFTLDNNLGEFILTYPELRLPEQKSIYSINEGNTCYWEPTIADFIAKLKENSEENNGKPYSARYIGSMVADVHRTLLYGGLFSYPGDKKNPNGKLRLLYEAFPMAFLVEQAGGKAVNDRGERILDLVPQHIHDKSSIWLGSSGDVDKYLKHIGKL", "text": "SIMILARITY: Belongs to the FBPase class 1 family."}
{"protein": "MQKRIALSFPEEVLEHVFSFIQLDKDRNSVSLVCKSWYEIERWCRRKVFIGNCYAVSPATVIRRFPKVRSVELKGKPHFADFNLVPDGWGGYVYPWIEAMSSSYTWLEEIRLKRMVVTDDCLELIAKSFKNFKVLVLSSCEGFSTDGLAAIAATCRNLKELDLRESDVDDVSGHWLSHFPDTYTSLVSLNISCLASEVSFSALERLVTRCPNLKSLKLNRAVPLEKLATLLQRAPQLEELGTGGYTAEVRPDVYSGLSVALSGCKELRCLSGFWDAVPAYLPAVYSVCSRLTTLNLSYATVQSYDLVKLLCQCPKLQRLWVLDYIEDAGLEVLASTCKDLRELRVFPSEPFVMEPNVALTEQGLVSVSMGCPKLESVLYFCRQMTNAALITIARNRPNMTRFRLCIIEPKAPDYLTLEPLDIGFGAIVEHCKDLRRLSLSGLLTDKVFEYIGTYAKKMEMLSVAFAGDSDLGMHHVLSGCDSLRKLEIRDCPFGDKALLANASKLETMRSLWMSSCSVSFGACKLLGQKMPKLNVEVIDERGAPDSRPESCPVERVFIYRTVAGPRFDMPGFVWNMDQDSTMRFSRQIITTNGL", "text": "FUNCTION: Auxin receptor that mediates Aux/IAA proteins proteasomal degradation and auxin-regulated transcription. The SCF(TIR1) E3 ubiquitin ligase complex is involved in auxin-mediated signaling pathway that regulate root and hypocotyl growth, lateral root formation, cell elongation, and gravitropism. Appears to allow pericycle cells to overcome G2 arrest prior to lateral root development. Plays a role in ethylene signaling in roots. Confers sensitivity to the virulent bacterial pathogen P.syringae. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPKPHDNDHMPFPVLVGDIGGTNARFWILMDAHAAPKEFANIHTADFPTIDQAIQDCILDKSGFQPRSAILAVAGPIKDDEIPLTNCPWVIRPKAMIADLGFDDVLVVNDFEAQALAAASLGRNDREPIGPLTETSLNSRVILGPGTGLGVGGLLYTHHTWFPVPGEGGHVDIGPRSDRDWQIFPHIERIEGRISGEQILCGRGILHLYNAICAADGIEPVWTDPADVTQHALKGNDPVCVETMTLFVTYLGRIAGDMALVFMARGGVFLSGGISQKIIPLLKSPVFRAAFEDKAPHTEMMKTIPTFVAIHPQAALSGLAAYARTPSSYGVKHEGRRWQR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the bacterial glucokinase family."}
{"protein": "MPRHHAGGEEGGAAGLWVRSGAAAAAGAGGGRPGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAAALGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFVYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGIDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQMTSDKKSREKITAEHETTDDPSMLARVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALTLASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLTRSASANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPMSQNDGSSVVATNNIANQISAAPKPAAPTTLQIPPPLSAIKHLSRPEPLLSNPTGLQESISDVTTCLVASKESVQFAQSNLTKDRSLRKSFDMGGETLLSVRPMVPKDLGKSLSVQNLIRSTEELNLQFSGSESSGSRGSQDFYPKWRESKLFITDEEVGAEETETDTFDGTPPPAGEAAFSSDSLRTGRSRSSQNICKTGDSTDALSLPHVKLN", "text": "FUNCTION: Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.5/KCNQ5 sub-subfamily."}
{"protein": "MSRGSSAGFDRHITIFSPEGRVYQVEYAFKAINSTNLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKKIKKKSELTSTEAIELAIEALQTSLGIDVRSKDLEVVVVTKDNSKFTKLTSDQVEHHLNQIANRD", "text": "FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1A family."}
{"protein": "MQPALTTAIPARKFKLTLLGPAFIAAIGYIDPGNFATNIQAGSTFGYQLLWVVVWANLMAMLVQTLSAKLGIVTGKNLAEHIRDRLPKPAVWAYWVQAEIIAMATDLAEFIGAAVGFKLLLGVTLLEGAGITAVVTWGILMLQSRGQKPLEFVVGGLLLFVAAAYIVELVFSRPHLPSLLEGALFPGLPNSDAVYLAAGVLGATVMPHVIYLHSALTQHTQDQGSVPQRLHTTRVDVAIAMTIAGFVNLAMMAMAAAAFHSSGNQQVAELESAYQTLTPLLGQAAATLFGLSLVASGISSTVVGTLAGQVVMQGFVRFTIPLWLRRAITMAPAFVVIAMGLNTTEILVLSQVVLSFGIALALIPLLILTGDRALMGEYRNHPVTQAVGRLIVALVIGLNAYLLVAMI", "text": "FUNCTION: H(+)-stimulated, divalent metal cation uptake system. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP family."}
{"protein": "MSQRTEHNGSWLRNAGSLLSVLACVAVLASPASATPASAAAAAAPRTDDYLKRAERILKFTPLIDGHNDLPNFIRKTTKNQIYEGKIPFEDELPGHTDLKRLRKGRVGGQFWSVYTPCPDPPVPIDNPTWSVRDTLEQIDVTKRLIEKYSRDLQFCGDARCARRAFRRGKIASFLGIEGGHQIGNSLGDLRRVYELGVRYITVTHNCDNAFATAQSTVADGLPDTGLMKPFGIEFVKEMNRLGMLVDLSHVSANTMRDTLKVARAPVIFSHSSAYAVSNHLRNVPDDVLKEVAKNNGVVMVTFVSRFVNVENPDAADINTVVDHIFHIAKVAGWDHVGIGGDYDGTVYLPKGLEDVSKYPHLIARVLERGATTQQVRKLVGENILRVWTEVERIAKRLQKTELPNEAYWEGRNWTRPAKRDLNADFEGRSVPLFTSASNGDFCD", "text": "FUNCTION: Hydrolyzes a wide range of dipeptides. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family."}
{"protein": "MKCYFTDHRGEQSPTDGTTLSLTSPESTEESVEVFWPGTIQREGSSPRPGPAIPREEGLYFAARDRGMRDWSSSPSSESSEYQSYSQYQSCCSCMCDEDNAAPQSVCAFYTHVQTVRGVAVAWETEAGFEPVTRKPRIHEAQFIKRQRWNGSSFEMASNTDMRWDLEACKSNCSPEPEDIDLLECCLQELREPPDWLVTTNYGVRCVACCRVLPSLDALLEHAQHGIREGFSCQIFFEEMLERRRAQGQAHDQQLEEEQSPSDNSECSRPQGEVLSAQQQEKQ", "text": "FUNCTION: Plays a role in fertilization through the acrosome reaction. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane. SIMILARITY: Belongs to the FAM170 family."}
{"protein": "MLTSHFPLPFAGHRLHIVDFDASSFHEHDLLWLPHHDRLRSAGRKRKAEHLAGRIAAVHALREVGVRAVPGIGDKRQPLWPDGLFGSISHCASTALAVISRQRVGVDIEKIMSQHTATELAPSIIDSDERQILQASSLPFPLALTLAFSAKESVYKAFSDRVTLPGFDSAKITSLNATHISLHLLPAFAAMMAERTVRTEWFQRGNSVITLVSAITRFPHDRSAPASILSAIPR", "text": "FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3- dihydroxybenzoate (DHB) and L-serine, respectively. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the P-Pant transferase superfamily. EntD family."}
{"protein": "MKVAVLGAGAWGTALAGHLAARHDTLLWARDAALIAGLQARHENSRYLDGIALPDALRYDADLGAALAHGAADDALCVIAAPVAGLRTLCHAMRDAGCVPAHVVWVCKGFEADTHLLPHQVIAAELPEQQSNGVLSGPSFAREVGRSLPVALTVASASAECRERTLAAFHHGAMRIYTGDDVVGVEVGGAVKNVLAIATGISDGLGLGLNARAALITRGLAEMSRLGVALGGRAETFTGLTGLGDLILTATGDLSRNRTVGLQLAAGRTLNDILGALGHVAEGVRCAQAVLALARAQSIDMPITQAVCGVLFDGIAPRDAVSGLLRRDARAE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MSALGRYDRHCDSINSDFGDSVRSCGPEQEELHYIPIRVLGHGAYGEATLYRRTEDDSLVVWKEVGLARLSEKERRDALNEIVILSLLQHDNIIAYYNHFLDSNTLLIELEYCNGGNLFDKIVHQKAQLFQEETVLWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKQLSSEYSMAETCVGTLYYMSPEICQGVKYSFKSDIWAVGCVLYELLTLTRTFDATNPLNLCVKIVQGNWAVGLDNTVYTQELIEVVHACLEQDPEKRPTADEILERPILSWRRRDMEEKVSMLNRSNKKPRTGTVTEAPIAVVTSRSSEVYVWGGGKTTPQKLDVFKGGWRARQVCAGDAHFAVVTVEKELYTWVNMQGGSKLHGQLGHGDRASYRQPKHVEKLQGKSVQKVSCGSDFTVCITDEGQLYSFGSDYYGCLGVNQSAGSEVLEPLLVDFFLNEPVDQVSCGDSHIMALTRSKSVYSWGCGEYGRLGLDSEDDVYSPQKVEVQRGLCIVNVCCGSDGSFLLTLTGKVLACGLNEHNKLGLNQYTAGIINHEAFQEVPYTTSLTLAKQLSFYKIRSISPGRTHTAAIDERGRLLTFGSNKCGQLGVGDYRKHLGINLLGGPLGGKQVIRVSCGDEFTTAATADNHIFAWGNGGNGRLAMTPNERPQGSDICTSWPRPIFGSLHHVTDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTLAQSCSSGGSGSREEDSDRESLTSDPSRGFRGTIEAEPETGPFNTTENMESSSCPSWLRQELEEAEFIPMPDTPNFVSAESSQNGTTSMQDVRETPPDALEKPSFQACTCSTLQEEVRKLQDLVSTYRHEQELLCRENSRLALEVQELNGKLQSAMQMNQVVNKHGEAIHQIQKQLSLHWKSSPPSSGNPEMSREDSDAESWCFLGTEACRSSSGTPM", "text": "FUNCTION: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Important for G1/S transition and S phase progression. Phosphorylates nek6 and nek7 and stimulates their activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily."}
{"protein": "MSELKTVGLFAITALAEIAGCYLPYLWLREGKSIWLLIPGALSLVAFVWLLSLHPTAAGRTYAAYGGVYISMAILWLWTVNGIRPTTWDIVGSVVALIGMAIIMFAPRSV", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0060 family."}
{"protein": "MTSSTPLYDENEDYIDENHINTFAKALLWEDDDHDGLASPPLPAYEGDKLAEVNAEELSSVLTPEPNNESEKSRPEFVVSHNDWYPINAPEKSKAKADAKGRKKRASTRDEFRSSAAYTLLRWPFLIIITVWILLLCILYTVVRAYVALSEYMLTWVGERKVLRNKLRASKTYEEWIENALELDRYLHLDKWSSIPRFSYYDYRTVKRTTSKLRMLRMRGMDEELMVFLQGCLKKNFAGIENRQLYAHRYYGTKNVVHVYIDEVVASIDHVTESENITPEDKRRFFRSVSRNYGRTALCLSGGACFAYTHFGIVKALLDNDLLPSIITGTSGGGLVAALACTRTDDELKQLLVPRLARKITACEDPWYVWIPRWWRTGARFDSTAWARKSNYFTLGSLTFQEAYHRTGRRLNISTVPADPHSPVILCNNITAPNCIIWSCLLASSAVPGILNPVVLMMKDSKKNTIVPFSLGSKWKDGSLRTDIPIDALKTYYNVNFTVVSQVNPHISLFFFAPKGSVGRPVASSRRKTRREKYASLRGGFIATALEHLFKLEIKKWLEMIKTLDLLPRLSESDWSSIWLQRFTGSITIWPRNNFRDFWYILSDPSEEGLGEMIRKGERYMFPKILFLKHRLSIENAIERGRTKSKLSTAHLEHSPRFSGTPEFAGPEFQLQTVHYDDDYDSESSAEETLSPGFSQGTHAVLTDESDDDSSDDEIDD", "text": "FUNCTION: Probable lipid hydrolase. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PLPL family."}
{"protein": "MNINMKDNFKKWLDLQQKKTLLKFLTCGSVDDGKSTLIGRLLHDTKQIYDDQLFFLKSDSKRHGTQGNEIDLALVVDGLQSEREQGITIDVAYRYFSTNKRKFIIADTPGHEQYTRNMATGASTCDLSILLVDARKGLSEQTYRHSFISTLLGIKYLIVAINKMDLVNYKQEIFENIKKDFLIFSKKLANDLNIIFIPMSALLGENIVFKTKLMPWYQGVTLLSFLETIKIKNSISSEELRFPVQYINRPNSDFRGYSGILLSGRMHVGQTIKILPENINSRVSRIVTFDKELKKAEIGESITVVLKDEIDINRGDFFVNIDSILQPSQEAIIDIVWMTDNILLAGESYNVKLSGKKIRVYIKEILFRLDVNTLKKVKSHSLVLNSIGRVKIYFSKPVIFDNYSENRMTGNMIFIDLLTNITVGAGMIVNSLDKKGKIPSNKQKDFESDFYDLIIRHFPHWNIPKILMKKVYK", "text": "FUNCTION: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric- sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily."}
{"protein": "MSNLHLYTSARFRNFPTTFSLRHHHNDPNNQRRRSIFSKLRDKTLDPGGDLITRWNHIFLITCLLALFLDPLYFYLPIVQAGTACMSIDVRFGIFVTCFRNLADLSFLIHILLKFKTAFVSKSSRVFGRGELVMDRREIAIRYLKSEFVIDLAATLPLPQIMIWFVIPNAGEFRYAAHQNHTLSLIVLIQYVPRFLVMLPLNRRIIKATGVAAKTAWSGAAYNLILYLLVSHVLGSVWYVLSIQRQHECWRRECIKEMNATHSPSCSLLFLDCGSLHDPGRQAWMRITRVLSNCDARNDDDQHFQFGMFGDAFTNDVTSSPFFDKYFYCLWWGLRNLSSYGQSLAASTLSSETIFSCFICVAGLVFFSHLIGNVQNYLQSTTARLDEWRVRRRDTEEWMRHRQLPDELQERVRRFVQYKWLTTRGVDEEAILRALPLDLRRQIQRHLCLALVRRVPFFAQMDDQLLDAICERLVPSLNTKDTYVIREGDPVNEMLFIIRGQMESSTTDGGRSGFFNSITLRPGDFCGEELLTWALVPNINHNLPLSTRTVRTLSEVEAFALRAEDLKFVANQFRRLHSKKLQHAFRYYSHQWRAWGTCFIQAAWRRYMKRKLAMELARQEEEDDYFYDDDGDYQFEEDMPESNNNNGDENSSNNQNLSATILASKFAANTKRGVLGNQRGSTRIDPDHPTLKMPKMFKPEDPGFF", "text": "FUNCTION: Putative cyclic nucleotide-gated ion channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family."}
{"protein": "MSTSVPQGHNWTRPVKKDDDEEDPLDQLITRSGCAASHFAVQECMAQHQDWRQCQPQVQAFRDCMSAQQARRREELQRRKEQASAQH", "text": "FUNCTION: Putative COX assembly factor. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the COA4 family."}
{"protein": "MLEILKKSLKKAPIVKRGKYPYFIHPITDGVPAIDPKLLDEISDYIIEYSDMDVDRILSIEAMGIPLATAISLKTGIPFSIVRKRQYQLPGEIKISQSTGYSKGELYINGIEKGNRILLVDDVISTGGTLRFLVKALEEKGVTISDIIVIVGRGDGVQQLAGEGIRVKTLVDINVSEDGVSILEDTGETN", "text": "FUNCTION: Catalyzes a salvage reaction resulting in the formation of IMP that is energically less costly than de novo synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. Archaeal HPRT subfamily."}
{"protein": "MADHHFYLKANWPGNRNDVGTIESGNLITSISIPKEMDGPGEGTNPDEMLLGAAATCYIITLAAMMERSGLEKEDLQMESEGIVNVTKGVFTYKKIIHRPSVVLKHDASQDDVALAHKLCKKAESSCMISRAIQGNVELQLEASVKLGGE", "text": "SIMILARITY: Belongs to the OsmC/Ohr family."}
{"protein": "MRFSTAFLALLSVGFSSARLQGRDQVPVALDDDHKIPGESPLKLCDGDHKDDILKITKVDLSPNPPKAGESLVIKASGDVTQKIEEGAYINLSVKYGLIRLINTKADLCEQIKNVDLECPIDEGKLDIVKSVDLPNEIPPGKYTVFADVYTKDNKKISCLTAEVRFERNSIATPWGDL", "text": "FUNCTION: Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol. SIMILARITY: Belongs to the NPC2 family."}
{"protein": "MVHLTPDEKNAVCALWGKVNVEEVGGEALGRLLVVYPWTQRFFDSFGDLSSPSAVMGNPKVKAHGKKVLSAFSEGLNHLDNLKGTFAKLSELHCDKLHVDPENFRLLGNVLVVVLAHHFGKDFTPEVQAAYQKVVAGVATALAHKYH", "text": "SIMILARITY: Belongs to the globin family."}
{"protein": "MSAQSRKSNSHNGKNSRVNPEIKFKLETLTELFPDWTNDDLIDLVHEYDDLETIIDKITSGAVTRWDEVKKPSKKERLEKRLEQQQQLQKEQQQHQLQQQHYHAQDLDGHHGGSSSHHHTKAGQGSGSRYSRDNNGTHSSSGGSNAKSKKQQQQQQQQQNGKPSLPSDNARAAISRGKPASGGGSWAAVASSDSKKHQQEEEEEEDQQQQRPESSPEEPSATTVQASETKTDGVEASASATSTAQSSTHATATASTGNAAHNEKPKKMSWAAIAAPKPKVVQKKQSSLNNVGGLKKEINEVAKETETPAAGQAQREPVSETNDKATNNQGKKADAQHEDTASKLSEQQQQQQEQLQAQQQEQQQTQQQDQSPIEFQSQGTNQEDTAQHNRPEEQKDTREITSNQVQIDEQEVAATSEPQEPSQTAQAVATEVNDGSKVKQQQQQPTVGVEAGKPQQQQQQEAYYQQQQQQQQQQQQQYFAQQQQYAQSQTPQHAPQQLSGQQAAVGQPNANANASANANAAAAATAAQQQYYMYQNQFPGYTYPGMFDSPSYAYGQQQAYQQPSQPSAQAGFGTGTASQYSIPQGYAAAPAADMTTASTATASPVAGHAQPQQQQPYGGSFLPYYAHFYQQSFPYAQPQYGMAGQYPYQVPKAGYNYYQPQRQTQGRNVQQGQQSPGHSPSQQGEDVQQQSQPTQQNQLQNGQQPLNPQQLQFQQYYQFQQQQQAAAAAAAAAAAQQGLPYGYTGYDYTSQASRGFY", "text": "FUNCTION: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, telomere Note=During transcription stress, localizes to the nucleus following proteolytic cleavage by the proteasome. SIMILARITY: Belongs to the DEF1 family."}
{"protein": "MMTSVPPRKSWWTSKKTVKVIRSYPTFPSLNAWEKFRGLLPVDGETNPGVGLGVEEGLLCQMVHSPEFNLFPNSVVFESNFVQVRRSRNWKEIYKASNTMALGVTSSVPCLPLPNILLMARVKWHQGQSQTWNRPSRAPSINLKSILPLKFVELQIWDDQERVLRLRTVTEKIYYLKLHPDHPETVFHFWIRLVQILHKGLSITTKDPTILVTHCLVPKSLCSPGGKTELVQKKSKGLQPSESLTHLMAQGESETLSQIFSDLHQQKQYRSEKMHINKTSSEKATPCEDSIPCTCDLNWRDAFMFGEWERENPSGPQPLSLLGTLAASSRPRLSLTGGNSI", "text": "FUNCTION: RAB2B effector protein required for accurate acrosome formation and normal male fertility (PubMed:34714330). In complex with RAB2A/RAB2B, seems to suppress excessive vesicle trafficking during acrosome formation (PubMed:34714330). SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the GARIN family."}
{"protein": "MQALPTILPPPPLPDDSEAPARTPEKHANLVRFQSELEFIQCLAHPQYLHELHIQGYLGKPAFLNYLKYLEYWREPQYVRFIIYPTCLVYLTLLQTELFRSRLGDMGFITELMRVGSRHHATWRVGKPAEDKQSEEKPAVSMAPLDDDEEEDEPERGQETKGKRKKKKSRSGNVGAGQAL", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 31 family."}
{"protein": "MASKDFHIVAETGIHARPATLLVQTASKFASDITLDYKGKAVNLKSIMGVMSLGVGQGADVTISAEGADADDALAAIEETMTKEGLA", "text": "FUNCTION: P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite- regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity). FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HPr family."}
{"protein": "MAEVLLFEALRDALDEEMQRDPSVLVMGEDVGHYGGSYKVTKGFHEKYGDLRLLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFNQIANNAGMLHYTSGGNFKIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQMVACSTPYNGKGLLKSAIRNDNPVIFFEHVLLYNLNENLIEQEYLLCLEKAEVVRPGNDITILTYSRMRHHVLQAAKVLVNKGYDPEIIDILSLKPLDMGTISLSVRKTHKVLIVEECMRTGGIGASLRAAILEDLFDYLDAPIQCLSSQDVPTPYSGPLEELTVIQPNQIIQAVEEMCKIE", "text": "FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MELEHESKRPLYIPYSGPILLEFPLLNKGSAFTEEERRNFNLHGLLPEAVETIEEQAERAYRQYLDFKNDADKHIYLRNIQDTNETLFYRLLDAHLNEMMPIIYTPTVGEACEHFSDIYRRARGLFISHPNKAHIDDMLQNATKQNVKVIVVTDGERILGLGDQGIGGMGIPIGKLSLYTSCGGISPAYTLPVVLDVGTNNPQRLNDPLYMGWRHPRITGKEYDEFVDEFIQAVKRRWPNVLLQFEDFAQKNAMPLLNRYRHEICCFNDDIQGTAAVTLGSLIAASRAAGRQLKDQTVTFLGAGSAGCGIAEQIVAQMKSEGLSDEQARARIFMVDRFGLLTDKLPNLLDFQNKLVQKSSSLAKWDVNNDSISLLDVVRNAKPTVLIGVSGQAGLFTEEIIREMHKHCERPIVMPLSNPTSRVEARPEDIINWTDGAALVATGSPFNPVKYKDQEYPIAQCNNAYIFPGIGLGVIASGAKLVTDGMLMAASRTLANCSPLAQEGQGPLLPLIDDIQEVSRKIAKQVAKEAQIQGVATVTSDGALDEAIERNFWKPEYRVYKRTSF", "text": "SIMILARITY: Belongs to the malic enzymes family."}
{"protein": "MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQPQGSIINPGSTGSAPWDEKDNDVDEEDEEDELDQSQHHVPIQDTFPFLNINGSPIAPASVGNCSVGNCSPEAVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCKVYWSGPCAPSLVAPNLIERQKKVKLFCLETFLSDLIAHQKGQIEKQPPFEIYLCFGEEWPDGKPQERKLILVQVIPVVARMIYEMFSGDFTRSFDSGSVRLQISTPDIKDNIVAQLKQLYRILQTQESWQPMQPAPSMQLPTTLPAQ", "text": "FUNCTION: Probable DNA-binding transcriptional activator. It is a key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development. Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Translocates to nucleus in response to an activating signal. SIMILARITY: Belongs to the IRF family."}
{"protein": "MDRVTRLASQKAVVVFSKSSCGMSHAVTRLLRELGVDARVVELDEEPAGADMENALAGMLLAGTAANGGGRGRGVVVPTVFIGGRLVGSTDRVMSLHVAGGLVPLLRDAGALWV", "text": "FUNCTION: May only reduce GSH-thiol disulfides, but not protein disulfides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily."}
{"protein": "MSRKLARELTMKVLFEMHINNDFNIQRVEHHLFEGSIEEQQKEYIHKVLNEAILNLEAIDSIIEEYSTSWKLNRIANVDLAILRLAFSEIIYMKDIPYRVSINEAIELAKIYGSDETPNFVNGILGKYVEQEGLMLNE", "text": "FUNCTION: Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons. SIMILARITY: Belongs to the NusB family."}
{"protein": "MNKEEQYLLFALSAPMEILNQGCKPAHDSPKMYTGIKEFELSSSWGINNRDDLIQTIYQMTDDGHANDLAGLYLTWHRSSPEEWKALIAGGSERGLIYTQFVAQTAMCCGEGGIKAWDYVRMGFLSRVGVLNKWLTEEESLWLQSRVYVRAHHYYHSWMHYFSAYSLGRLYWQSSQCEDNTSLREALTLYKYDSAGSRMFEELAAGSDRFYATLPWQPLTVQSECPVTLKDVSDL", "text": "SIMILARITY: To E.coli YbeR."}
{"protein": "MANNPSQLLPSELIDRCIGSKIWVIMKGDKELVGILKGFDVYVNMVLEDVTEYEITAEGRRVTKLDQILLNGNNIAILVPGGSPEDGE", "text": "FUNCTION: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development- related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression (PubMed:23221597, PubMed:23620288). Involved in the control of plant sensitivity to abscisic acid (ABA) and drought (PubMed:11740939). Functions with ABH1 as negative regulator of ABA signaling in guard cells (PubMed:12427994). Required for regulation of splicing efficiency of many stress-responsive genes under stress conditions (PubMed:24393432). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family."}
{"protein": "MKAKEIRELTTAEIEQKIKALKEELFNLRFQLATGQLENTARIRQVRKDIARMKTIIRERELAANK", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL29 family. SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MAKQTPLYDQHVACGARMVDFHGWMMPLHYGSQIDEHHIVRQDAGMFDVSHMTIVDLHGARTREFLRYLLANDVAKLTQPGKALYTAMLNASGGVIDDLIVYFLREDYFRLVVNSATREKDLNWIIQHAEPYQVDVTVRDDLALVAVQGPTAQQKVATLLTSEQQQAIAGMKPFFGIQADDLFIATTGYTGEAGYEIALPKERVVEFWQQLLAAGVKPAGLGARDTLRLEAGMNLYGQEMDEGVSPLAANMGWTVAWLPEDRQFIGREALEQQRANGTEQLVGLIMTEKGVLRNELPVHFSDDSGNQHVGVITSGSFSPTLGFSIALARVPAGIGENAVVQIRNREMPVRVTKPGFVRAGKPVAL", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. SIMILARITY: Belongs to the GcvT family."}
{"protein": "MMIIVMLILSYLIGAFPSGLIIGKLFFKKDIRQYGSGNTGATNSFRVLGRPAGFIVTFLDIFKGFITVFFPLWFSVHADGVISTFFTNGLIVGLFAILGHVYPIYLKFNGGKAVATSAGVVLGVNPILLLILAIIFFSVLKIFKYVSLSSIIAAISCVIGSIIIHDYILLAVSGIVSIILIIRHKSNIVRIFKGEEPKIKWM", "text": "FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PlsY family."}
{"protein": "MLTKGVRALAWSPRRYITLDAEAAKPVVAKRRRMTEFTDKLNKGPSFEDFLTGKAAQMTLDPLEEARQNAEESKKLPAWLKVPIPKGKNFHKLKEDVRDLKLSTVCEEAKCPNIGECWGGNKGSATATIMLLGDTCTRGCRFCSVKTNRTPAKPDPKEPENTAEAISRWGLGYVVLTMVDRDDLPDGGAHHLAETVQRIKQKAPHILVETLAGDFRGNLEMVDVMARSGLDVYAHNVETVEALTPHVRDRRATYQQSLSVLKRAKQTVPTLVTKTSIMLGMGETDEQVLQTMKDLRAVDCDVVTFGQYMRPTRRHMKVVEYVKPEKFDYWKEKALELGFLYCASGPLVRSSYKAGEAYIENVLRNRRQA", "text": "FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase family."}
{"protein": "MEAACLVRRLGLPQGEEALKARLRRPGHPRLREALAAYLKRLQAPEEVFRALERLEVGAVVTGQQAGLLGGPALTFYKAHTALCLADRAGAAGVFWVASQDHDVEEVRHLHLLRDEVPETLSLDLPPLPSGRIPLAPHRERLRAFLGPWAKDYRLGYALEAETLSEFFARVLLAFLGERGLVPFDPMAEELAPLFLEALERELSDPLGSAEAINREAERIRALGGKPPLRRKPGATNLFLETDQRRLLFYEGGAFTDGVRRYTAKELWEIARADPSRLTPAAGLRPVFQDLVLPTAGFVVGPNELRYVAELSGVYARYGLAMPALFLRAFGVVVEPPVRRILEKYRLDPWAFVDEGEAAFLRAAEAWLAPFRAFRDRVEGLLQEASRLVEEAEALEPNLVRPLRRFRARVRGEAERLRRKLLAAQAARDEVLARHLRRLKVHLLPFGLPQERVYPYAMYALRHGEALRRLAEAPWEGRVALYLG", "text": "SIMILARITY: Belongs to the BshC family."}
{"protein": "MPINVPDGLPAAEILTKEDVFIMEEKRAEHQDIRPLSIVILNLMPNKIITETQILRLLGNSPLQVDITLLYPETHRSKNTPEEYLIKYYQTFDSIKDQKFDGMIITGAPIEQMPFEEVDFWPELQKIMDWSKANVFSTLFICWGAQAGLYHFFGVPKYPLPAKMFGVFPHTLNRRDIRLLRGFDDIFYVPHSRHTEVRKEDIVKVPELEILSESEESGVYLVGTKGGRQIFVTGHSEYDPYTLKAEYDRDISYELPINIPQNYYPGDDPRQTPVVRWRGHSNLLFANWLNYYVYQETPYNLEELGNR", "text": "FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MetA family."}
{"protein": "MNQIQVFISGLILLLPGAVDSYVEVKGVVGHPVTLPCTYSTYRGITTTCWGRGQCPSSACQNTLIWTNGHRVTYQKSSRYNLKGHISEGDVSLTIENSVESDSGLYCCRVEIPGWFNDQKVTFSLQVKPEIPTRPPTRPTTTRPTATGRPTTISTRSTHVPTSIRVSTSTPPTSTHTWTHKPEPTTFCPHETTAEVTGIPSHTPTDWNGTVTSSGDTWSNHTEAIPPGKPQKNPTKGFYVGICIAALLLLLLVSTVAITRYILMKRKSASLSVVAFRVSKIEALQNAAVVHSRAEDNIYIVEDRP", "text": "FUNCTION: Phosphatidylserine receptor that plays an important functional role in regulatory B-cells homeostasis including generation, expansion and suppressor functions (PubMed:21821911, PubMed:25645598, PubMed:32668241). As P-selectin/SELPLG ligand, plays a specialized role in activated but not naive T-cell trafficking during inflammatory responses (PubMed:24703780). Controls thereby T-cell accumulation in the inflamed central nervous system (CNS) and the induction of autoimmune disease (PubMed:24703780). Regulates also expression of various anti-inflammatory cytokines and co-inhibitory ligands including IL10 (PubMed:25582854, PubMed:25645598). Acts as regulator of T-cell proliferation (PubMed:15793576). May play a role in kidney injury and repair (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family."}
{"protein": "MSERIIMDDAAIQRTVTRIAHEILEYNKGTDNLILLGIKTRGEYLANRIQDKIHQIEQQRIPTGTIDITYFRDDIEHMSSLTTKDAIDIDTDITDKVVIIIDDVLYTGRTVRASLDAILLNARPIKIGLAALVDRGHRELPIRADFVGKNIPTSKEETVSVYLEEMDQRNAVIIK", "text": "FUNCTION: Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. FUNCTION: Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily."}
{"protein": "MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS", "text": "FUNCTION: Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis. SIMILARITY: Belongs to the pyruvate kinase family."}
{"protein": "MTDILAKIAAYKREDVADRKRRRSIAQLEAAAKAANSPRGFKAALEADHAPGKLALIAEIKKASPSKGLIRADFDPPALARAYAAGGASCLSVLTDGPSFQGADGYLIDVRAAVSLPCIRKDFLVDPWQVAESRALGADAILVILAMIDDAVAADLMSEAARLGMDALVEVHDEAEMERAGKLGSTLVGINNRDLKSFVVDLAVTERLAVQAPSDALLVTESGLFVAADVARMEAAGAKAMLVGESLMRQADVAAATRALLG", "text": "SIMILARITY: Belongs to the TrpC family."}
{"protein": "MTEYKPTVRLATRDDVPRAVRTLAAAFADYPATRHTVDPDRHIERVTELQELFLTRVGLDIGKVWVADDGAAVAVWTTPESVEAGAVFAEIGPRMAELSGSRLAAQQQMEGLLAPHRPKEPAWFLATVGVSPDHQGKGLGSAVVLPGVEAAERAGVPAFLETSAPRNLPFYERLGFTVTADVEVPEGPRTWCMTRKPGA", "text": "FUNCTION: Detoxification of puromycin."}
{"protein": "MVRFEKVHLVLGLALVLTLVGAPTKAQGPVCGAGLPDKFSRLNFPEGFIWGTATAAFQVEGAVNEGCRGPSMWDTFTKKFPHRCENHNADVAVDFYHRYKEDIQLMKDLNTDAFRLSIAWPRIFPHGRMSKGISKVGVQFYHDLIDELLKNNIIPLVTVFHWDTPQDLEDEYGGFLSGRIVQDFTEYANFTFHEYGHKVKHWITFNEPWVFSRAGYDNGKKAPGRCSPYIPGYGQHCQDGRSGYEAYQVSHNLLLSHAYAVDAFRNCKQCAGGKIGIAHSPAWFEPQDLEHVGGSIERVLDFILGWHLAPTTYGDYPQSMKDRVGHRLPKFTEAEKKLLKGSTDYVGMNYYTSVFAKEISPDPKSPSWTTDSLVDWDSKSVDGYKIGSKPFNGKLDVYSKGLRYLLKYIKDNYGDPEVIIAENGYGEDLGEKHNDVNFGTQDHNRKYYIQRHLLSMHDAICKDKVNVTGYFVWSLMDNFEWQDGYKARFGLYYIDFQNNLTRHQKVSGKWYSEFLKPQFPTSKLREEL", "text": "FUNCTION: Hydrolyzes abscisic acid glucose ester (ABA-GE) which represents the predominant form of conjugated ABA (biologically inactive). No activity with beta-D-glucopyranosyl zeatin. The hydrolysis of ABA-GE in the endoplasmic reticulum (ER) forms free ABA and contributes to increase its cellular levels under dehydration conditions. ABA-GE hydrolyzing activity is enhanced by dehydration stress-induced polymerization into higher molecular weight forms. The ABA produced by BGLU18 contributes to the initiation of intracellular signaling as well as the increase in the extracellular ABA level. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Note=Located in ER bodies. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MPRPSRESYGEQKPPYSYISLTAMAIWSSPEKMLPLSDIYKFITDRFPYYRKNTQRWQNSLRHNLSFNDCFIKVPRRPDRPGKGAYWALHPQAFDMFENGSLLRRRKRFKLHKNDKDLLNEELTALANLNRFFFTTRNGGSAAHMSPLDMNNAAAMRLDPLPRSTAHMPNSLGPGVPLPHVMPASMSGADHTNLADMGLTNLPALTSSEIEGPLSLRPKRSFTIESLITPDKPEHPSEDEDDEDDRVDIDVVECSGISRYPTTPAASEEYMSASRSSRTEDPLPPMHTINAGAHVPFLHYATGANVAGLPASGIPNSPTTYELAISHPLFMMAAPIANMHNIYYNNVTLVAPAQQYRSPEVQNRIDNDMRTI", "text": "FUNCTION: Involved in development during embryogenesis. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKKPH", "text": "SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the filoviruses glycoprotein family."}
{"protein": "MFCSALRNILRNSQNAAKNATITSQIRNLRGQQSVHHEVEVLTSPGITTKQNDKKTEPAECEGSKEVALDFRNREAHVPSFNLAAYVNNSSTLQQFLSLGVDLHSIERRKGLGDFVLKLDFEKNVKPYITFLVDQGVSPDDFGRMFTKNPLLFKEDLDDLQTRVNYLKSKRFSDEARQRILTQNPYWLMFSTRRVDRRLGYFQKEFKLSGHDLRLLATREPNAITYNMEHLRKSVFTLKEEMGFNAKELSDLVVRKPRLLMIPPDDLVERFSYIHQDMGLPHAQIVQCPELLASREFRLRERHEFLKLLGRAQYDPQKDLYISPKTIVEGNNFYFVRNVAKSDLETFDLFLKTR", "text": "FUNCTION: Binds promoter DNA and regulates initiation of transcription (By similarity). Regulator of mitochondrial ribosome biogenesis and translation that is essential for development (PubMed:16787637, PubMed:23300484). Required for normal mitochondrial transcription and translation (PubMed:16787637, PubMed:23300484). Required for assembly of mitochondrial respiratory complexes and normal mitochondrial function (PubMed:23300484). Maintains 16S rRNA levels and functions in mitochondrial ribosome assembly by regulating the biogenesis of the 39S ribosomal subunit (PubMed:23300484). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mTERF family."}
{"protein": "MEKRKIILDCDPGHDDAIAIMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADNIHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGEMFSDIMNFTLKTQFENYGLAGGPVHDATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH", "text": "FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides. SIMILARITY: Belongs to the IUNH family. RihB subfamily."}
{"protein": "MELLDVDGAWLYTPEIMRDERGEFLEWFRGRTFQEKIGHPLSLAQANCSVSRKAFCAASTSPTPPPGQAKYVTCASGTVLDVVVDVRRGSPTFGRWAAVRLDAARHQGLYLAEGLGHAFMALTDDATVVYLCSQPYVAEAERAVDPLDPAIGIEWPTDIDIVPVGEGTPTHRPWRRPRRPGILPDYEGVPGALHRGGGRRGTGP", "text": "FUNCTION: Involved in the biosynthesis of one of the two 2,6- deoxysugars, dTDP-L-oleandrose, attached to the macrolactone ring oleandolide to produce the aglycone antibiotic oleandomycin (PubMed:10770761). Probably catalyzes the conversion of dTDP-4-keto- 2,6-dideoxy-alpha-D-glucose to dTDP-4-keto-2,6-dideoxy-beta-L- galactose. SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family."}
{"protein": "MSGSVTSTTTETRLCPSNQGSAKKYRPWNDFRSDTLTVPTDEMRRIMYEASDGDCVYEEDEDTRKLEVYVAKLTGKEAALFVTSGTQGNQLCIRSHLHQPPHSIICDDRAHIYNWEAGAIGLFTQAIVRPISPKNNVYITAEEIENKLILGNDIHFSPTGLICLENTIKGAVVPLDEVARISGLAKAHKIPLHCDGARLWDAAVASNVSIKEYCSYFDSVSLCLSKGLAAPVGSIIVGPRDFIAKAKWFRKAYGGGLRQSGMLAAAGLYSIQHNFPLLKQVHKYAIEVAEYAESLGIELEVPTQSNMVTLANINVAILCDEAKKSGIILMGPRIVFHIQITPDAVEILKNVLRRTVERQAVETHIVAKPGEFCVGY", "text": "SIMILARITY: Belongs to the threonine aldolase family."}
{"protein": "FSPNSPSDVARCLNGALDVGCGTFACLENSTCDTDGMHDI", "text": "FUNCTION: Its primary function is the prevention of hypercalcemia. Upon release into the circulation, it lowers calcium transport by the gills, thereby reducing its rate of influx from the environment into the extracellular compartment. STC also stimulates phosphate reabsorption by renal proximal tubules. The consequence of this action is increased levels of plasma phosphate, which combines with excess calcium and promotes its disposal into bone and scales. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the stanniocalcin family."}
{"protein": "MTSQFKNSINDYLEGLPEAVLTRLYQSPATCLAVFRLLPALARTLIMGMIFNPDPIAVADVDALVKPSSQRLKLETQKKLRLLHIFTETQAHIIINPTFKKNLRAALVGGDQNISFGVPCDTEDKHKVDVAFLDAHAVSQWEMILHFMVGTSIGRTPSDGVLNLLKHSGLMEPERGGLRITNAGFQFLLQDVNAQIWTLLLQYLNMSEYLQMDPVDVLNFIFMLGSLELGQDYSLSALSETQKHMLEDLRDYGIVYQRKASSRRFYPTRLATTLTSETAALRTASQSMEAATQDTISSSVAADSGFIILETNFRLYAYTESPLQIAVLNLFVNLKTRFANMVTGQINRDSVRFALSNGITAEQIITYLSVHAHPRMKGMEHVLPPTVVDQIKLWQLEMDRIRATDGYLFSEFKNFDEYKDVSTYAKELGVLLYENPGKRKFVSTLAGSQQIVEFVKRRNQKHRSSAN", "text": "FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFB2 family."}
{"protein": "MAASPKIGIGIASVSSPHRVSAASSALSPPPHLFFLTTTTTTRHGGSYLLRQPTRTRSSDSLRLRVSATANSPSSSSSGGEIIENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGGVPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPEDVESLSVTTAPFTVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGASPLFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYLTSNNLLVEFHQPQTEEAKKEFTQRDVQEKFDITLTKHKGQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREFIEANK", "text": "FUNCTION: Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark. Required for chlorophyll biosynthesis and biogenesis of the photosynthetic apparatus. Activates aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into protochlorophyllide. Involved in a light-dependent regulation of starch biosynthesis by redox activation of the ADP-glucose pyrophosphorylase (AGPase), a central enzyme of starch synthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MKIHKCSFCGAEIPPGYGIMYVRNDGTIQRYCSRKCFVSATKYGRNPRKLAWVRKRQK", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family."}
{"protein": "MNDDNQQSAHDVDASGSLVSDTHHRRLSGAQKLIVGGVVLALSLSLIWLGGREKKENGDAPPSTMIATNTKPFHPAPIDVTLDPPAAQEAVQPTAPPPARSEPERHEPRPEETPIFAYTSGDQGTSKRVQQGETDRRREGNGEDSPLPKVEVSAENDLSIRMKPTELQPTRATLLPHPDFMVTEGTIIPCILQTAIDTSLAGYVKCVLPWDVRGTTNNVVLLDRGTTVVGEIQRGLQQGDARVFVLWDRAETPDHAMISLASPSADELGRSGLPGTVDNHFWQRFSGAMLLSVVQGAFQAASTYAGSSGGGTSFNSVQNNGEQTADTALKATINIPPTLKKNQGDTVSIFVARDLDFSGIYQLRMAGRAARGRDRRP", "text": "FUNCTION: VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TrbI/VirB10 family."}
{"protein": "MPLPDFHVSEPFTLGIELEMQVVNPPGYDLSQDSSMLIDAVKNKITAGEVKHDITESMLELATDVCRDINQAAGQFSAMQKVVLQAAADHHLEICGGGTHPFQKWQRQEVCDNERYQRTLENFGYLIQQATVFGQHVHVGCASGDDAIYLLHGLSRFVPHFIALSAASPYMQGTDTRFASSRPNIFSAFPDNGPMPWVSNWQQFEALFRCLSYTTMIDSIKDLHWDIRPSPHFGTVEVRVMDTPLTLSHAVNMAGLIQATAHWLLTERSFKHQEKDYLLYKFNRFQACRYGLEGVITDPHTGDRRSLTEATLRLLEKIAPSAHKIGASSAIEALHRQVVSGLNEAQLMRDFVANGGSLIGLVKKHCEIWAGE", "text": "FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily."}
{"protein": "MFLLHEYDIFWAFLMISSVIPILAFLISGVLAPISQGPEKVSSYESGIEPMGDAWIQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSVFIEALIFVLIPIVGSVYAWRKGALEWS", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family."}
{"protein": "MGDEGKKEKRRQTKEDAVYGFVFESDSNSDDSGGSRRKKRRKTKPVKFSSAGNIDQVLKQNRGNCKIDENDDTILPIALGKKIADKAHVREKNNKKENFEKFSGGIGMKLLEKMGYKGRGLGKNQQGIVAPIEVQLRPKNMGMGYNDFKEKNAPLFPCLNKVEEKKKSVVVTVSENHGDGRRDLWKKKNVRKEVYITAEEFLGKKQEEGFGCDQLIIDKRGPQDRVVNSLRNLYAEEKATDANVQQPELQHNLRFIVKSLEHGILKTDKDLRNEKGLALSLQQEKEKFKMGVKKQKTLFDNLGYVAEEIDRIEVEIASGNLTLDSLANRFKDLRSSYPDDYKCCNLSCIASSLALPLFIRMFQGWDPLSDAEHGIEAISSWKMLLEVEDNQSISTPYSQLVSEVILPAVRVSGINTWEPRDPEPMLRLLETWEKMLPSLIFETILTTVVLPKLSIAIESWEPRLETVPIHFWVHPWLPVLGQKLESAYQIIRMKFGNLLDAWHPSDVSVHTILSPWKTVFDAASWEQLMRRYIVPKLQVALQEFQINPADQNLDEFNLVMGWVSSVPIHLMTDLMERFFFPKWLDVLYHWLCSEPKFDEIMKWFLGWKGTFPQELSANRRIEIQFKRGLDMAREAVERMEMSQPGARENISYHKAQEQRQSEGRAKVQAQVDDPEELSFKEAVELFAQEKELLLKPKPHRMHNGLQIYRFGNVSVLLDSANSKLLAQEEGRWFPVDLDSLLKMHYSAVTGKQ", "text": "FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFP11/STIP family."}
{"protein": "MGTELFNQAKPILEKIEQHGFEAYFVGGSVRDYLMNRHIHDIDITTSATPDEIESIFEKTIPIGREHGTINVVYQGTNYEVTTFRAEAEYVDHRRPSEVYFVRDLKEDLQRRDFTINAIAMDKNFNIYDYFEGDVALNQHIIKTVGDAKERFKEDALRILRGLRFQSQLNFTIEGDTFEAMKHQIADVEHLSIERIVVELKKLIKGQNVSQSYLNLIDLNFFNYVPFFRSLDMKQTKVNSPISFELWIAILLTVEQTNTSLSDLKISNNEKTKINQYHKIMIEMPQVSSKEQLKLFVYDYGMNNIIDIIAINSILEDNNIKIASPLIFNLQSIKEIDQHLPIRSRRELNINGGDILRITSKKSGPWLKEVLRQIEIDVLTNKVPNLKDELLKWVKENVKI", "text": "FUNCTION: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 3 subfamily."}
{"protein": "MSGTILENLSGRKLSILVASLLLCQVFCFLLGGLYAPLPAGHVTVLGSLCREDHTRQNDTSFLLYSRGAGACIPVSREEVERDPMKMANELVHVFQMPLPRDLRDLDYSRWQQNLIGVLQVEFGYDSTSELREPPKELQLTIDMRLAYRNKGDPDQAWKLYAHGVEQRYLDCVTAHVGPTETLYSCDMIPLFELGALHHSFYLLNLRFPLDTPRQMNLQFGHMHDLTLTAIHQNGGFTQIWLMLKTVLFPFVVGIMIWFWRRVHLLQRSPALLEYMLIYLGGALTFLNLPLEYLSLVVEMPYMLLLSDIRQGIFYAMLLSFWLVFAGEHMLIQDAPNKSTIRSRYWKHLSAVVVGCISLFVFDICERGVQLRNPFYSIWTTPLGAKVAMTFIILAGVSAAIYFLFLCYMIWKVFRNIGDKRTSLPSMSQARRLHYEGLIYRFKFLMLATLLCAALTVAGFIMGQMAEGQWQWNDNVEIQLTSAFLTGVYGMWNIYIFALLILYAPSHKQWPTMHHSDETTQSNENIVASAASEEIEFSHLPSDSNPSEISSLTSFTRKVAFD", "text": "FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity). SUBCELLULAR LOCATION: Presynaptic cell membrane; Multi-pass membrane protein Postsynaptic cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Note=In non-neuronal cells, wls binds to wg in the Golgi and accompanies it to the plasma membrane where the two proteins dissociate. Wg is secreted and wls is then internalized and returns to the Golgi apparatus in a retromer-dependent manner. Wls and wg colocalize in the Golgi apparatus in wg-producing cells, and reduced expression is seen in non-producing cells. Endoplasmic reticulum expression is unchanged in wg-producing versus non-producing cells. In neuronal cells, wls is localized both pre- and postsynaptically and is transferred trans-synaptically from the pre- to the postsynaptic compartment (By similarity). SIMILARITY: Belongs to the wntless family."}
{"protein": "MIIWILPCRMPMNLRKDERINISKTSSSKIKEINQLRHIIRKKNRQIQILIIMLNILRCCHRMKE", "text": "FUNCTION: May play a role in viral pathogenesis or transmission by insects vectors. SIMILARITY: Belongs to the rhabdoviruses C protein family."}
{"protein": "MLNFFRRLLGDSNEKEIRRLQPIVEEINRLGPEFARLSDAELRAKTDEFRQRLADGETLDDILPEAFATVREAAARTIGLRHYDVQLIGGIVLHQGKIAEMKTGEGKTLVATLPLYLNALEGKGVHLVTVNDYLAKVGAGWMGPIYHFLGLSVGFIAHDQSALYDPDYIDPNANPEDQRLVHWRPCTRREAYLADITYGTNNEFGFDYLRDNMAYDKSQLVQRELHYAIVDEVDNILIDEARTPLIISGPAQKSSDLYRQMAKLVRQLRRSSVTAKQVKEEGLEPDGDFFVDERTKSIYLSEKGIEKLEKLLNIPPGESLFDPEHYEKTHYVENALKAQFIYQRDRDYMVTPNGEVVIIDEFTGRAMPGRRWSDGLHQAIEAKEGVPIKNENVTLATITFQNYFRMYKKLAGMTGTAYTEREEFAKIYNLDVVVIPTHKPMIRKDLPDQIYATEEAKFRAVLREVQEMHEIGRPVLIGTTSVETSERLSAMLKQAGIPHNVLNAKHHEREAAIVAQAGRKGAVTVATNMAGRGTDILLGGNPDGLVEEFLRKEGLTLETATPEQKRAAWEKAKALTEAEGEEVRQLGGLHVIGTERHEARRIDNQLRGRAGRQGDPGSSRFFLSLEDELLRRFGPVERIKGLMERFVDSDVPLQAGLLDRTIESAQTRVEGYNFDIRKHTVEFDDVMNKQRQIIYADRKAILDEADMRERVLDLMAEEIQRQIDEHLSDGVDEFGLTELLRVYRRIDPTLPATVTAETLKGKTKEEIEQFLLDHLETTYAEREKAIGPEVMRTVERRVMLGAIDRQWVDYLTAMDELRQNILLQAYAQKDPLVEFKRESFRMFDELKANIAHDIVYNIIPASFQYEAYLRQIAEEQARRLATAQIAGGSSEVEQTRKPQRRTVQQIGRNDPCPCGSGKKFKHCHLGREHELAAFMNNAPATTPKVEPQPVKPAIAEEAAKIKAAIDNGTLPAASPKTPRGRQPQAVPRGKKR", "text": "FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Note=Distribution is 50-50. SIMILARITY: Belongs to the SecA family."}
{"protein": "MADIWTDYGVPGAIIVAQILALMVPILVSVAFLVYAERKVLGLMQLRQGPNMVGPWGILQSFADALKMIGKETIIPAGANRIIFLAAPMLTMMLALAAWAVIPFGEGLVISDINVGILYLLAISSQGVYGIIMAGWASNSKYAFLGGLRSAAQMVSYEVSIGLVIITVLLCVGSLNLSDVVEAQKTVWFAIPLLPMFVIFFISALAETNRAPFDLPEGESELVGGFHTEYSGMAFGLFFLGEYANMILMSAMTSVLFLGGWLPPLDVAPLNWVPGPIWFILKICFCLFLFVWVRATVPRYRYDQLMRLGWKVFLPFSLVWVILTAGVLVTFDWLPK", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MPTALCPRVLAPKESEEPRKMRSPPGENPSPQGEPPSPESSRRLFRRFRYQEAAGPREALQRLWELCRGWLRLERHTKEQILELLVLEQFLAILPWEIQSWVRAQEPESGEQAVAAVEALEREPGRPWQWLKHCEDPVVIDDGDGPAAPQDLEQERMSAESQSYPDAPPGALVQGTGLLSRSPGQPSEDLVPQDAFVVQEQSIRDAQPVATCQLPPNRVSPFKDMILCFSEEDWSLLDPAQTGFYGEFIIGEDYAVSMPPNEPPVQPGHSHEEENGLRVTEWTTDLQDKEIPQASCLDLSSLQPFQGEERRKWEELQVPELQPCPQVVLSQSPCPAGGDPPALKSSLDQEVTIEIVLSSSGDEDSQHSPYCTEELRSPPEDLHSVPAHQSNASAEGEVQTSQKSYVCPNCGKIFRWRVNFIRHLRSRREQKPHKCSVCGELFSDSEDLDGHLETHEAQKPYRCTACGKSFRLNSHLISHRRIHLQPASQQPMKKSEEEALETEGTGASDLLEKSKAKLSFQCGDCEKSFQRHDHLVRHRRHCHLKDETRPFQCRYCVKTFRQNYDLLRHERLHMKRRSKQALNSY", "text": "FUNCTION: DNA-binding transcription factor that can both act as an activator and a repressor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MMNLLNKSLEENGSFLTALYIIVGFLALYLLGRALQAFVQAADACCLFWYTWVVIPGAKGTAFVYKYTYGRKLNNPELEAVIVNEFPKNGWNNKNPANFQDAQRDKLYS", "text": "FUNCTION: Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis. SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass type III membrane protein Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. SIMILARITY: Belongs to the gammacoronaviruses E protein family."}
{"protein": "MEALIPVINKLQDVFNTVGADIIQLPQIAVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVDPEDRRKTSEENGVDGEEWGKFLHTKNKIYTDFDEIRQEIENETERVSGNNKGISDEPIHLKIFSPHVVNLTLVDLPGITKVPVGDQPKDIELQIRELILKYISNPNSIILAVTAANTDMATSEALKVAREVDPDGRRTLAVVTKLDLMDAGTDAMDVLMGRVIPVKLGLIGVVNRSQLDINNKKSVADSIRDEHGFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLSAQYQSLLSSYGEPVEDMSATLLQLITKFATEYCNTIEGTAKYIETAELCGGARICYIFHETFGRTLESVDPLGGLTTIDVLTAIRNATGPRPALFVPEVSFELLVKRQVKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTSLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRMRELPTSVPRDKMAGGAQAEQEGGTGTWRGMLKKGDEGQGEEKTKLQSSIPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDSLQSELVGQLYKPALLDDLLTESEDMAQRRNEAADMLKALQKASQVIAEIRETHLW", "text": "FUNCTION: Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes. While the recruitment by the membrane receptors is GTP- dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (By similarity). May play a role in the circadian control of mitochondrial ATP production (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus Endomembrane system; Peripheral membrane protein Mitochondrion outer membrane; Peripheral membrane protein Peroxisome Membrane, clathrin-coated pit Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MNNMDGSENNAKVSDSAYSNSCSNSQSRRSHSSKSTHSGSNSSGSSGYGGQPSTSSSSNDLSDQKKEKELKKKKQVETLMPDTQIEVECRPEEDVINIPSEEGGAADDVLVPSPKQTLQTDNDIADIEVAIPDTNNDKEEAIVYNTSLINPGTACPFGRPALSNCNGFSCVISMHDGVVLYATASLTSTLGFPKDMWVGRSFIDFVHPRDRNTFASQITNELAIPKIVSLTEETDQTMENPGSTMVCRIRRYRGLSCGFSVKNTTTAYLPFLLKFKFKNVNEDKGNVIYLVIQAVPFFSAFKTSNEVLAKTVSFVIRHSADGNLEYIDAESVPYLGYLPQDITNRDALLLYHPGDLGYLQEIYGSLVKEGNVTRSKTYRMMTQNGHYMKVETEWSAFINPWSKKLEFVTGKHYIIEGPANPDVFQNPENVLKLTEEQKNQAKMYRDSIIRIMKDVLTKPAEIAKQQMSKRCQDLAHFMEMLIEEQPKPVDDLRLEIQDADHSYYERDSVILGGISPHHEYDSKSSTETPLSYNQLNYNDNLQRYFNSHQSNAFVDNNLLPSRNPLYLSAPHFSESIKNVPSAMEYSGDVIDLTGPGETSGVIVFNKSPTMGLKTGKPIRLTESSLTKHNAEMEKELMKIHREHRCYSKGDRVKVSNEARQKKKEHLARCNAGFQTISAANNTPSVYEKPHNLKRSSKQMESEPIANKHHCPSSRQFRRKQTTCSGGFAQPPSATNPVSTSSQWSSSPVNNVNPFILGVRMQPPMPILSPLPVVSGMFPMYYTPVTATVTTSEGRPSEPNYHRNNMNNNQFQQPLGNSRLPTTICVIQCGTSRIIHSFRGTRTTGGTRYT", "text": "FUNCTION: Involved in the generation of biological rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the tim-per complex. Light induces the degradation of tim, which promotes elimination of per. Nuclear activity of the heterodimer coordinatively regulates per and tim transcription negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). Expression exhibits prominent circadian variation in adult heads and in particular in the photoreceptor nuclei. SUBCELLULAR LOCATION: Nucleus. Note=Nuclear at specific periods of the day. Interaction with TIM is required for nuclear localization (By similarity)."}
{"protein": "MDARKEGLPLETLFSDQYPQVRRWLAPFILACSLYFLLWIPVDQPSWVSALIKCQPILCLVVFLWAVAPGGSSTWLLQGALVCSAVGDACLIWPEAFFYGTAAFSVAHLFYLGAFGLTPLQPGLLLCTTLASLTYYSFLLLHLEQGMVLPVMAYGLILNSMLWRSLVWGGSASWGAVLFTFSDGVLAWDTFVYSLPFARLVTMSTYYAAQLLLILSALRNPGLKTH", "text": "FUNCTION: Enzyme catalyzing the degradation of lysoplasmalogen. Lysoplasmalogens are formed by the hydrolysis of the abundant membrane glycerophospholipids plasmalogens. May control the respective levels of plasmalogens and lysoplasmalogens in cells and modulate cell membrane properties. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the TMEM86 family."}
{"protein": "MPNGSRCPDCGSSELVEDSHYSQSQLVCSDCGCVVTEGVLTTTFSDEGNLREVTYSRSTGENEQVSRSQQRDLRRVRDLCRILKLPLTFEETAVSYYQKAYQLSGIRAARLQKKEVVVGCCVLITCRQHNWPLTMGAICTLLYADLDVFSSTYMQIVKLLGLDVPSLCLADLVKSYCSSFKLFQASPSMPAKYVEDKDKMLSRTLLLVELANETWLVTGRHPLPIITAATFLAWQSLRPSDRLTCSLARFCKLANVDLPYPAASRLQELLAVLLQMASQLAWLQVLRLDKRSVVKHIGDLLQHRHMLVRMAFQDGTAEVETKQQQPQGRGQQEEVGDSTFDLPKRKRPASPALLLPPCMLKPPKRTHTMPPDSVVTGDEDISDSEIEQYLRTPQEVRDFERAQAASRAAMSVPNPP", "text": "FUNCTION: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIB family."}
{"protein": "MNKLKSSQKDKVRQFMVFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELYIRESVKGSLDRKKLEQLYNRYKDPQDENKIGIDGIQQFCDDLALDPASITVLIIAWKFRAATQCEFSKLEFMDGMTELGCDSIEKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDLEMAIAYWNLVLNGRFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNYDEEGAWPVLIDDFVEFARPQIAGTKSTTV", "text": "FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation. Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes. Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MVLSPADKTNVKATWDKIGGHAGEYGGEALERTFASFPTTKTYFPHFDLSPGSAQVKAHGKKVADALTTAVGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPAEFTPAVHASLDKFFSAVSTVLTSKYR", "text": "FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. SIMILARITY: Belongs to the globin family."}
{"protein": "MNIKSLLLGSAAALVAASGAQAADAIVAPEPEAVEYVRVCDAYGAGYFYIPGTETCLRVHGYVRYDVKGGDDVYSGTDRNGWDKSARFALRVSTGSETELGTLKTFTELRFNYAANNSGVDGKYGNETSSGTVMEFAYIQLGGLRVGIDESEFHTFTGYLGDVINDDVISAGSYRTGKISYTFTGGNGFSAVIALEQGGDNDGGYTGTTNYHIDGYMPDVVGGLKYAGGWGSIAGVVAYDSVIEEWAAKVRGDVNITDQFSVWLQGAYSSAATPNQNYGQWGGDWAVWGGAKFIATEKATFNLQAAHDDWGKTAVTANVAYELVPGFTVAPEVSYTKFGGEWKNTVAEDNAWGGIVRFQRSF", "text": "FUNCTION: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the alphaproteobacteria porin family."}
{"protein": "MSRFFVSGYNSESSSEEEDLLSSEEELLTSSGEENEDSDFFNDDDESSSDEEDGRPSGPAYFLKKSFLKGAGGDSDSDSDDEGRKVVKSAKEKLLDDMKASIEVINVNKRTNNWIVVLSEFEKLGKLINRANQQNFGTPKFYVKLLASLDDSITETVNNEKDDKTMKADEARAFNTLRQRVKKQIKEFQVYFDLYKDVPENFDQEDESLDSFAKNQETREETRTLSPIFHNLKLINESRGKKNIDKSEQVTTLEGLISDEASDFELISLYQSLLSVRFDASSNQSFMAIQDWRSNKRDLNNLLDILVKSKVYQLSEEGQTTDDIDIEPTANEDGVKVIYGSVTSLIDRLDDEFTKSLQNTDPHSMEYVERLKDETEIYNLIVRGQAYIESIVADKQQSNQLARVVLRRLEHIYYKPNQLIKANEEEAWKNIKPSTQTPSEVIESLTQFLQSNKVFAKQALLYSIYYYAVNGDYNKAKELFLSAHFNLSDSALQVSYNRALVQLGLSAFRSGAIEESHKILNEMVNSQRSKELLGQGFNSKFPNQATVVEKQRLLPFHQHINLELLECVYMTCSLLIEIPALASNKDPKRRNASLKSFKSKLEFHDRQYFTGPPESIKDHIVHASIALQKGDWSKAYNLLSSIKIWHLFPDHDNLLAMMKNQLQIEGLRTYIFTYKAVYSKLSISKLSSIFGLLQENVSEVLTQMIEKLDINGEVSGDYIVFTTDSQRSKLQELAIVMNDKIQLLTEKNEKTSSNGYAKKNQSQTQPQAQSKEVEENKFRYANVNTNTDEF", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit C family."}
{"protein": "MNPTSIVLIVIATVAVCLIIMQIYYIYENYDNIKEFNSTHSTLEYSKTINVFSLDRRIYDPNDHIYDVKQKWRCVNYKNNYVSVSVFGFKSNKDKNIKMFTTINDCINYTFSKSTHSDIYNPCILDDGFQNQDCIFLKSVI", "text": "FUNCTION: Envelope protein required for virus entry into host cell and for cell-cell fusion (syncytium formation). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the intracellular mature virion (IMV) membrane. SIMILARITY: Belongs to the poxviridae A28 protein family."}
{"protein": "MATNFSDIVKQGYVKMKSRKLGIYRRCWLVFRKSSSKGPQRLEKYPDEKSVCLRGCPKVTEISNVKCVTRLPKETKRQAVAIIFTDDSARTFTCDSELEAEEWYKTLSVECLGSRLNDISLGEPDLLAPGVQCEQTDRFNVFLLPCPNLDVYGECKLQITHENIYLWDIHNPRVKLVSWPLCSLRRYGRDATRFTFEAGRMCDAGEGLYTFQTQEGEQIYQRVHSATLAIAEQHKRVLLEMEKNVRLLNKGTEHYSYPCTPTTMLPRSAYWHHITGSQNIAEASSYAGEGYGAAQASSETDLLNRFILLKPKPSQGDSSEAKTPSQ", "text": "FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK4 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway (By similarity). Putative link with downstream effectors of RET in neuronal differentiation. May be involved in the regulation of the immune response induced by T-cells. SIMILARITY: Belongs to the DOK family. Type B subfamily."}
{"protein": "MGVTVENISAGDGKTFPQPGDNVTIHYVGTLLDGSKFDSSRDRGTPFVCRIGQGQVIRGWDEGVPQLSVGQKANLICTPDYAYGARGFPPVIPPNSTLKFEVELLKVN", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily."}
{"protein": "MDAGRRRLVINDCMKPERGRRSPLPRRPTRPPDERSSGIGNLAMTPAKLHMTTSLAPIAVHSPYDGSLLGSVEATDPADIDRLLATARRGAEISRNLPRHKRASILEGAAQMVESRHDAFAEIIVREAGKTIVQARKEVLRCVNTLKLSAEEAKRNAGEIVPFDAYTGSEQRQGWFTRDPLGIITAITPYNDPLNLVAHKLGPAIAGGNAVMLKPSNLTPFSAIKLVGALREAGLPEEVITISHGDRELVTAMIAAREVRMVSFTGGFATGEAISRAAGLKKLAMELGGNAPVIVMNDCDFDKAVEGCVSGAFWAAGQNCIGAQRILIQSELYGRFRDAFVAATKKLKAGDPLQEDTDVGPMISKQVAERTEAAVNEAIKAGATLLCGNYREGSLYHPTVLEGTPLTCRLWHEEVFAPVVMLAPFDTLDKGIEMANDPDYSLHAGIFTNDLNVALEAANRIEVGGVMINDSSDYRFDAMPFGGFKYGSMGREGVRFAYEDMTQPKVVCINRG", "text": "FUNCTION: Could be a succinate-semialdehyde dehydrogenase (NADP(+)). SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MPKKVFQQEDVEQKITENFEPKQEFEQDELDIEMDCSQFETTMDRQNTDIPFQHMVRPKVTMWQKLLMATICLFSCGILAQSVQWLVDSWRDNQWIAFVFAMVSLFLVLLGLGAIIKEWRRLVQLKKRLILQEKSREIRSKSAVNLTEVSSEGKELCLKIASLMGIDDKSPQLIAWQEQVHEAYTEQEILRLFSQNVLIPFDRVAKKLISKNAVESALIVAVSPLAIVDMFFIAWRNIRLINQLAKLYGIELGYVSRLRLLRMVFVNMAFAGAADVIQDLGLEWLSQDITAKLSARVAQGIGVGILTARLGIKAMEFCRPIAVAPEEKLRLSHIQTELLGTLKTTLFSANKVKEKVR", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0283 family."}
{"protein": "MFLSPGEGPATEGGGLGPGEEAPKKKHRRNRTTFTTYQLHQLERAFEASHYPDVYSREELAAKVHLPEVRVQVWFQNRRAKWRRQERLESGSGAVAAPRLPEAPALPFARPPAMSLPLEPWLGPGPPAVPGLPRLLGPGPGLQASFGPHAFAPTFADGFALEEASLRLLAKEHAQAMDRAWPPA", "text": "FUNCTION: May be involved in modulating the expression of photoreceptor specific genes. Binds to the Ret-1 and Bat-1 element within the rhodopsin promoter (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MQDNSSHSRESASAGDDPLGIDKLTVDYDYLLYKIRDYVQSIQLDTTELCKKQNEVMVNGIIENTIDKNIAKFKELLEKCDTLENHYEMLNQLAIDNRYFQGKNRRGRK", "text": "FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that is involved in endosomal cargo sorting. SUBCELLULAR LOCATION: Cytoplasm Note=Punctate pattern. SIMILARITY: Belongs to the BLOC1S4 family."}
{"protein": "MPTRVNDGVDADEVTFVNRFTVHGGPAEFESVFARTAAFFARQPGFVRHTLLRERDKDNSYVNIAVWTDHDAFRRALAQPGFLPHATALRALSTSEHGLFTARQTLPEGGDTTGSGHR", "text": "FUNCTION: Involved in the biosynthesis of the anthracycline (aromatic polyketide) antibiotic nogalamycin (PubMed:8760909, PubMed:8668120). Catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid (PubMed:19255477, PubMed:20052967)."}
{"protein": "MSPTVQCGAVSQVVVVGGTHGNEMSGVCLAKHWLQDPSELHRKSFTAEVLLANPIAVERCVRYIDRDLNRSFSHELLSASGSESDSYEAKRAREIYQKYGPKQSSLNFVIDLHNTTSNMGTTFLLFKGDNFALHLANYLQTKCVDPSFPCHILLIDIPEGGHVHLQSMGKHSVSLELGPQPQGVARADVLTRMRALVNCSLDFLDLFNQGTEFPSFETDVHQVLYRADFPRNEDGEIEAVIHSELQDKDYLPLKPGDPIFQRLNGEDILYNGEKQIYPVFINEAAYYEKKVAFIATEKTHCLVPALKVQN", "text": "FUNCTION: Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. SUBCELLULAR LOCATION: Apical cell membrane; Peripheral membrane protein. Cytoplasm. SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily."}
{"protein": "MVQCLDGVRQLLAVVFKCCDLELKQPRGLEDPQVLARETVFSVSEVEALYELFKKISSAVIDDGLINKEEFQLALFKTSKKESLFADRVFDLFDTKHNGILGFDEFARALSVFHPSAPLDEKIDFSFQLYDLKQQGYIERQEVKQMVVATLAESGMNLSDEIIESIIDKTFEEADTKHDGRIDKEEWRNLVLRHPSLLKNMTLQYLKDITTTFPSFVFHSQVDDT", "text": "FUNCTION: Acts as a calcium sensor. May promote vacuolation of aleurone cells in response to signal induced by gibberellin. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). SUBCELLULAR LOCATION: Vacuole, aleurone grain membrane Note=Tonoplast. SIMILARITY: Belongs to the calcineurin regulatory subunit family."}
{"protein": "NLIDFKNMIKCTNTRHWVSFTNYGCYCGYGGSGTPVDELDKCCQVHDKCYDTAKHVCKCSPSMTMYSYDCSEGKLTCKDNNTKCKDFVCNCDRTAALCFAKAPYNNKNFKIDPTKGCQ", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that has only a weak enzymatic activity. It has a myotoxic activity in vivo (dystrophic effect). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
{"protein": "MNQRGEAPISVIKRLPVYLRVLDNLVKRDIEVVSSKSLSKETGFTAEQIRKDLAFFGAFGTRGTGYNTNYLRERVLRIIGLDKQTNVAIVGAGHLGTAFARYNVRENPYTSVVGLFDVSPDIVGENIEGVPVYHLNDLQEIVRKERVQVGVITVPAVHAQEVVDRLVEENVKALLNFAPAKLTAPEDVRIHNVDLTIELQSLIYFAKDELNEESTQDLE", "text": "FUNCTION: Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transcriptional regulatory Rex family."}
{"protein": "MPPRELSEAEPPPLRAPTPPPRRRSAPPELGIKCVLVGDGAVGKSSLIVSYTCNGYPARYRPTALDTFSVQVLVDGAPVRIELWDTAGQEDFDRLRSLCYPDTDVFLACFSVVQPSSFQNITEKWLPEIRTHNPQAPVLLVGTQADLRDDVNVLIQLDQGGREGPVPQPQAQGLAEKIRACCYLECSALTQKNLKEVFDSAILSAIEHKARLEKKLNAKGVRTLSRCRWKKFFCFV", "text": "FUNCTION: Plays a role in the control of the actin cytoskeleton via activation of the JNK pathway. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Endosome membrane; Lipid-anchor; Cytoplasmic side Note=Treatment with TNF activates endosomal but not plasma membrane RHOV. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MSADDVVYDLVGLGFGPANIAIGAALTEKWQQDPTFSIKNTLFIEKHEVFRWHPGMLLPDAKMQISFLKDLATLRTPNSPYTFLSYLHSEDRLLSFINRGSTVPSRKEYSDYLAWAAQKVQDNGVKVKFGHEIIALDDGPDGTIEVRYRNVRTQEETLIRARDLIIAPGGTPCIPDFLQPFVNHPRVSHSSSYALKIGDMFDSLNHLSRPLRVAIIGSGQSAAEVTIDVRNRLASIPSTGRHEVDMLIRKGSLKPSDDSPFANEIFDPASTDAWFSTGSKHLRDAILAEYKQTNYSVVNPRTLEALYEIIYGQRLNAAVSRRTNVEEPSDPVINIKPYTSVLSIQTVGSQGERVRGELLLSPEGASASKDEGFVMVTKHMMTGAESQTNYDVILYATGYQRTAWVELFKNTGIAKHFGITPSTSKVVLRPSADLVGGRQHQEFFHDSSPSTASSSTVSTPPTSPETSRFSSPISSRIVSQDLYLSRSYQLLPKDGENTLRPRVYLQGVEEATHGLSDTLLSVLGVRAGEVVADLASRYHSSA", "text": "FUNCTION: L-ornithine N(5)-monooxygenase; part of the gene cluster that mediates the biosynthesis of coprinoferrin, an acylated tripeptide hydroxamate siderophore (PubMed:31496254). The biosynthesis of coprinoferrin depends on the hydroxylation of ornithine to N(5)- hydroxyornithine, catalyzed by the monooxygenase cpf2 (PubMed:31496254). The second step, the acylation of N(5)-hydroxy-L- ornithine to yield N(5)-hexanoyl-N(5)-hydroxyl-L-ornithine is catalyzed by a not yet identified acyltransferase (Probable). Finally, assembly of coprinoferrin is catalyzed by the nonribosomal peptide synthase (NRPS) cpf1 via amide bond formation between three N(5)-hexanoyl-N(5)- hydroxyl-L-ornithine molecules to release the linear trimer (PubMed:31496254). Interestingly, proteins seemingly not directly related to biosynthesis, such as transcription factors, replication factors, and autophagy-related proteins, are conserved among the clusters homologous to the coprinoferrin cluster, suggesting that the cluster may also play developmental and cell biological functions (Probable). SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)- oxygenase family."}
{"protein": "METGPRGCPSGRKESQEICSPGLLVFTGCSEQDANLAKQFWLGASMYPTTESQLVLTRGSSQRLPVARNSKVVLREKSSVQPFPFDQDKDAIIFAKAQRIQESEERAKYLQKAKTRDEILQLLRKQREERISKELISLPYKPKDKVPKSKEVLSESGLRDQEEVKALE", "text": "FUNCTION: Required for motile ciliogenesis and flagellar genesis by mediating the maturation of the glycolytic enzyme ENO4. SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium. SIMILARITY: Belongs to the HOATZ family."}
{"protein": "MKQSTVFTLLLLLIGMAAYSFGWVQAVAEAAAQYVQMINNDAVRLGLLACTAALLMLPAFLYLHYVTQSVKNMTAAFQKLTQSHQSCCDFQQHNLCSRYAEDVKSLRDSYKNVRQTYVMAAVLCQVIIFGCMFEIVKAVPFRLHTPPAFSMGLAMLLILYLLFCMRTYLRQLFRHGSLFRKVFAGALAAAGIWWMLSFSISELLFLIILAAIQQIGSFIYKRFSYHSTASLDL", "text": "FUNCTION: Involved in the production of the bacteriocin subtilosin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MYDNLKSLGITNPEEIDRYSLRQEANNDILKIYFQKDKGEFFAKSVKFKYPRQRKTVVADGVGQGYKEVQEISPNLRYIIDELDQICQRDRSEVDLKRKILDDLRHLESVVTNKISEIEADLEKLTRK", "text": "SIMILARITY: Belongs to the UPF0325 family."}
{"protein": "MELAVQRTDTDALSSKVSAIHTKYLSGGISQQFAYEEVYGEYLASLRQVSRRVFGKCRYSGASFPVMNYGTYLRTVAIDERVLEFLQCNSGSQVQIVNIGCGSDLRMVSVLAKHSNVKYIDLDFKESVELKRQVLEKSSTLSSYLKNDNYVLRSCDLRDVPDTLELLNEECKPELPTLIISECVLCYMPEKETQSLIDGIIRLFKNGSWVSYDPMGGSDKNDRFGVIMQQNLRDSRQLEMPTLLINNSPEIYASRWTPNSDEQFERVVTDMWTYYNDKVPAEEKQRIKRLQFLDELEELKVMQSHYVIFFCKWNANPN", "text": "FUNCTION: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha- leucine ester residues. SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family."}
{"protein": "MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSGVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAVFTGHSAVVEDVAWHLLHESLFGSVADDQKLMMWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTTSELEGQGS", "text": "FUNCTION: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
{"protein": "MRYRAVFPMLIIVFALSGCTLSTINPMKKSRIDNIHHTQILFFSDENQIDQEAPYYDALLDLEKDYPEQIDKMKVYDKKEGWEDEIETVPTLMVVDQRHVVVKIEGCVKKKEDIIKPLQHVLSK", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
{"protein": "MMKKGKGKNSGLLPNSFKIISSCLKTVSANATNVASSVRSAGASVAASISAAEDDKDQVTWAGFGILELGQHVTRHVLLLGYQNGFQVFDVEDASNFNELVSKRGGPVSFLQMQPLPARSGDHEGFWNSHPLLLVVAGDETNGTGLGHSFSQNGSLARDGSSDSKAGDAINYPTTVRFYSLRSHSYVYVLRFRSSVCMIRCSSRVVAVGLANQIYCVDALTLENKFSVLTYPVPQPVRQGTTRVNVGYGPMAVGPRWLAYASKSSMTMKTGRLSPQTFTSSPSLSPSSSSGGSSFMARYAMESSKQLANGLINLGDMGYKTLSKYCQDMLPDGSTSPASPNAIWKVGGVSGSDAENAGMVAVKDLVSGALVSQFKAHTSPISALCFDPSGTLLVTASVCGNNINVFQIMPSRSHNAPGDLSYEWESSHVHLFKLHRGITSAIVQDICFSQQSQWVAIISSKGTCHIFVLNSSGSDAAFQPCEGEEPTRLPASSLPWWFTQSLSSNQQSLSPPTAVALSVVSRIKYSSFGWLNTVSNATTAATGKVFVPSGAVAAVFHKSVTHDLQLNSRTNALEHILVYTPSGHVVQHELLPSVCTESPENGLRVQKTSHVQVQEDDLRVKVEPIQWWDVCRRSDWLETEERLPKSITEKQYDLETVSNHLTSHEDACLSLDMNSHFSEDKYLKSCSEKPPERSHCYLSNFEVKVTSGMLPVWQNSKISFHVMDSPRDSSSTGGEFEIEKVPAHELEIKQKKLLPVFDHFHSTKATLEDRFSMKCYHTSATGSHQVNGKICQDIINCHSKPGSIESAESSEEGSTKQMENLHDSDHMSNSIKSSLPLYPTVNGIYKEIEKNNANGWMEKPVTAKLSTLKETRITNGFTTPPILTDSVNEQMLSTGKPPMGFGFALHEEHCKAVADPKEEHLKKKLDEVTNVHHLNVNNNNTEKLQGDKMVHGMVSFVGD", "text": "FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Required for autophagy (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Note=Peripheral membrane protein of pre-autophagosomal structure (PAS) and vacuole. SIMILARITY: Belongs to the WD repeat PROPPIN family."}
{"protein": "MADPDPRYPRSSIEDDFNYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIFALILNRHKYPLNLYLLFGFTLLEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGALLFCGFIIYDTHSLMHKLSPEEYVLAAISLYLDIINLFLHLLRFLEAVNKK", "text": "FUNCTION: Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family. LFG subfamily."}
{"protein": "MELPSNLLPDEASPEWMNKGDNAWQLTAATMVGLQSIPGLVILYGSLVKKTWAINSAFMAFYAFASVLLCWVSWAYQMSFGEKMVFFLGKPNVALDEKFLLGKAFLGNFPNATMVFYQGVFAGLTLILIAGALLGRMNIRAWMLFVPLWVTFSYTVVAFSIWCPDGWLAKRGVIDFAGGYVIHLSAGVAGFTAAYWVGPRADKDRETFPAATNNMIMVLAGAGLLWMGWSGFNGGAPFVASTIASLAILNTHVCTAASITVWVMLDTFYFGKPTVFGAVQGMITGLVCITPAAGVVQGWAAILMGFISGSIPWYTMMVLHNKVNFLKKIDDPMAVFHTHAIAGALGGILTGFFAVPKLCRLFYMVPDWEKYIGLAYGLQNKGATQAGLKQMVIQIEAIVFVICYNVLMTSLICLIVRVIVPLRLNGDALQMGDKAIHGEDAFALHSEATKFVNIKRNQVYDTQDFSSIPESRSLGELQMV", "text": "FUNCTION: Involved in ammonium transport (PubMed:25841038). May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family."}
{"protein": "MAGVNGSHASPSPAKQRAKMDDIVVVAPGTQSSRNVSNDPDVIKLQEIPTFQPLLKGLLSGQTSPTNTKLEKLDPHQVLQLCLRYQDHLHQCAEAVAFDQNALVKRIKEMDLSVETLYSFMQERQKKYAKYAEQIQKVNEMSAILRRIQMGIDQTVPLMERLNSMLPESEQLEPFSMKPDREIKS", "text": "FUNCTION: As part of a BORC-like complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, this complex may couple lysosomes to microtubule plus-end-directed kinesin motor. SUBCELLULAR LOCATION: Lysosome membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the BORCS5 family."}
{"protein": "MLQWRRRHCCFAKMTWSPKRSLLRTPLTGVLSLVFLFAMFLFFNHHDWLPGRPGFKENPVTYTFRGFRSTKSETNHSSLRTIWKEVAPQTLRPHTASNSSNTELSPQGVTGLQNTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNETLAPGIQIIRVFLLGISIKLNGYLQHAIQEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHTPYVMKTDSDMFVNTEYLIHKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFSGDLAEKIFKVSLGIRRLHLEDVYVGICLAKLRVDPVPPPNEFVFNHWRVSYSSCKYSHLITSHQFQPSELIKYWNHLQQNKHNACANAAKEKAGRYRHRKLH", "text": "FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family."}
{"protein": "MLISDRDIRRHLDSGRVRLEPSDPAMVQPASVDVRLDRWFRLFDNHKYAHIDPEQEQPELTRLVEVAPDEPFVLHPGEFVLGATYEKVTLPDDIAARLEGKSSLGRLGLLTHSTAGFIDPGFSGHVTLELSNMATLPIKLWPGSKVGQLCFFQLSSPTEHPYGSGAYGNRYQGQRGPTASRSHLNFHRTVIE", "text": "FUNCTION: Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. SIMILARITY: Belongs to the dCTP deaminase family."}
{"protein": "MASSSSLYLLAALLALASWQAIAFDPSPLQDFCVADMKSPVRVNGFPCKNPMEVNSDDFFNAAKFDMPRSTMNKVGSNVTNLNVLNFPGLNTLGISLARIDYAPLGVNPPHIHPRATELLTVLEGTLYVGFVTSNPNRLFSKVVHKGDTFVFPKAMIHFQMNLDHNKPAVAQSSLNSQNPGVITIASAVFGSKPPISDDVLTKAFQVEKKVIDWLKSQFWESNY", "text": "FUNCTION: Plays role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the germin family."}
{"protein": "MTATLDVPEQNPDLVLDQSADDYWNHYQLTFALYSVSDRAIPSAYDGLKPGQRRLLYQMHDSKLLPGNKPQKSSKVCSAVTGNLHPHGGASMYGAAALMAADFQRVKVIDGQGAFPRIQGDIPAADRYTEMRLSAPGAALTAELNDHAVPMVPTFDGEWVEPTVLPAQWPVLLCNGAVGIAEGWATKVPAHNPREVMAACRALLKTPNMTDDRLCKLIPGPDWGSGASVVGTAGLREYITTGRGHFTVRGTISVEGKNCIITELPPGVASNTVQDRIRALVESGEMSGVADMSDLTDRRNGLRIVVTAKRGHNAEQIRDQLLALTPLESTFAASLVALDENRVPRWWSVRDLIMAFLQLRDSVVLHRSEYRLEKVTARRHLVAGLMKIHLDIDAAVAVIRGSETVDEARKGLQERFKIDAEQADYVLSLQLRRLTKLDVIELQAEAEKLDAEFAELNDLVTNPESRRKVIDKELVETAKLFKGPEYDRRTVLDFDATPVSRGDEDGSRERKVNTAWRLDDRGVFSDSHGELLTSGLGWAVWSDGRIKFTTGNGLPFKIRDIPVAPDITGLVRSGVLPEGYHLALVTRRGKILRVDPASVNPQGVAGNGVAGVKLAADGDEVIAALPVSCANGEAILSIAEKSWKVTEVADIPVKGRGGAGVAFHPFVKGEDALLAASISKTGYVRGKRAVRPENRAKASIKGSGADVTPAPAE", "text": "FUNCTION: Catalyzes the relaxation of negatively supercoiled DNA in the presence of ATP or dATP but not other nucleotides. Individual subunits have no activity. Not able to negatively supercoil DNA, it can however introduce positive supercoils in DNA. Relaxes positive supercoils in an ATP-dependent manner. Catenates and decatenates DNA. Generates dsDNA breaks in the presence of the quinolone antibiotic ciprofloxacin, showing it is a topoisomerase (PubMed:16313624). SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit family."}
{"protein": "MSIRVTQKSYKVSTSAPRSFSSRSYTSGPGSRISSSAFSRVGSSSSFRGGLGTGMSMAGSYGGAPGLGGITAVTVNQSLLSPLKLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRHLEQQNKVLETKWNLLQQQKTARSNIDNMFESYINNLRRQLETLAQEKLKLEVELGNMQGLVEDFKTKYEDEIQKRTDMENEFVIIKKDVDEAYMNKVELESRLEGLTDEINFYRQLYEEEIREMQSQISDTSVVLEMDNNRNLDLDGIIAEVKAQYEEIANRSRAEAEAMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEGLKGQRASLEAAIADAEQRGEMAVKDAQAKLAELEAALRNAKQDMARQLREYQELMNVKLALDVEIATYRKLLEGEESRLESGMQNMSIHTKTTSGYAGGLTSSYGTPGFNYSLSPGSFSRTSSKPVVVKKIETRDGKLVSESSDVLSK", "text": "FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Nucleus matrix. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MDKSSGELVTLTPNNNNTVQPVALMRLGVFVPTLKSLKNSKKNTLSRTDATEELTRLSLARAEGFDKVEITGPRLDMDNDFKTWVGIIHSFARHNVIGDKVELPFVEFAKLCGIPSSQSSRRLRERISPSLKRIAGTVISFSRTDEKHTREYITHLVQSAYYDTERDIVQLQADPRLFELYQFDRKVLLQLKAINALKRRESAQALYTFIESLPRDPAPISLARLRARLNLKSPVFSQNQTVRRAMEQLREIGYLDYTEIQRGRTKFFCIHYRRPRLKAPNDESKENPLQPSPAEKVSPEMAEKLALLEKLGITLDDLEKLFKSR", "text": "FUNCTION: This protein is essential for plasmid replication; it is involved in copy control functions. In vitro, binds to the DNA repeat units, BCDD'D'', EFG and HIJ (By similarity). SIMILARITY: Belongs to the initiator RepB protein family."}
{"protein": "MGRCEFYHPFTPYRIQLELMQQIYGLLESGKKMGIFESPTGTGKTLSLICSTFTWLREHKAGYLQGSTGAQDSEEDSEDEPAWVKENYEQSVLADVTASMRAYEQRLAAVDTDLLVKGAAKRQRVEVAVERPDDGAEFLPDAYHSDVEERPSHAGGRGQLRKQLDADIKRLLRKLDEPDAADKSRLAANPLKVYFASRTHTQLGQFAAQLRLPQFPPSLAGLEQERVKFLPLGSRKQLCIHKKVSKVKSDGINEACMDAVSKSECSFFSAAREPDIIRQFQDQAFSTIQDIEDLVGIGNTLHACPYYSSRELIEGAEVITLPYQHLLLENARKTMGIDLRDSIIVIDEAHNLIDTINSIHSASISLTELRQCKLALQAYLAKFKTRLNSGNRVNLLKLIKMVDVLSQFIETQYKNGKRINDPNDIFMGTSMDVVNIHKLEKYMKTSKVAYKIDKYIQATTSNDLQDRGSRDIKQPILFKVASFLKTLANPSEEGQFFFENGHVLKYMLLEPSEVLKSIVTEAKCVILAGGTMEPVNDFFTQLVPYLAPTDVTTYSCGHVIPDDNLNAFIVSENFEFTFANREDIALIERLFHFIYQLASRVPFGMVVFFSSYKYIDFVVKTWTDRGLLSRLDAIKRIYHETSDGADVLKGYSETIQSEKKGAILLAVVGGRLSEGINFENELARAVVLVGLPFPNMFSGEMIVKQQHIKEKVIRNGGTQEDVNKAVREFYENICMKAVNQSVGRAIRHASDFANVYLIDKRYSGPRIQQKLSDWVRKRIQSASNIPKILSDTEAFFSGKGL", "text": "FUNCTION: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a specific role in chromosome segregation during meiosis II (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily."}
{"protein": "MSTLLRGGKVLVNDELVSKDIRIEDGKIVEMGEKLNVYNSEIIELDGKFVSQGFVDVHVHLREPGGEHKETIESGTRAAARGGFTTVCPMPNTRPVPDSVEHIEALNQSIKQHAKVRVLPYASITERQLGKDLVDFKALKEHGAFAFTDDGVGVQTASIMYEAMQQAAQLNMAIVAHCEDNSLIYGGAMHEGKVSKALNIPGIPSICEAVQIARDVLLAEAADCHYHVCHVSSKESVRVIRDAKRAGIKVTAEVTPHHLLLNETAITEDDAILKMNPPLRSEEDHQALIEALLDGTIDFIATDHAPHAADEKNQPMTKAPFGIVGSETAFPLLYTRFVKNGDWTLGQLIDYLALKPGQVFGLPYGKSLEVGSIADITVIDLDEKYEIKSEDFLSKSSNTPFIGEHVYGNVKLTLVEGQIAYQEGQHA", "text": "FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily."}
{"protein": "MANMLRSWMMLAALAVCLLVCLSSFADAYPPKPESPGSNASPEDWAKYHAAVRHYVNLITRQRYGKRSTPEQAVAWLLFGADSSQDAEPRLDYSDQW", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
{"protein": "MASGCALHGGCPSDYVAVAISVICFFVLLSRSVLPCLIHKAPRTNSSSFWIPVIQVISSFNLLFSIMMSVNLLRFRTKHWWRYCYLWAVWIEGPLGFGLLMSCRITQAFQLYFIFVKKRLPPVKSYIFLPLVLLPWIFGAAIIHATKPLNDKCHMGLQWTFPVAGLHALYVLALIAFTRAVRHVEFRFDELRDLWKGILVSATSIVIWVTAFVLNEIHEEISWLQVASRFVLLVTGGILVVVFFSISSNQPLLSQISLKKRQNFEFQRMGQALGIPDSGLLFRKEEFRPVDPNEPLDKLLLNKRFRHSFMEFADSCYAGETLHFFEEVYEHGKIPEDDSIRRIYMARHIMEKFIVAGAEMELNLSHKTRQEILTTQDLTHTDLFKNALNEVMQLIKMNLVRDYWSSIYFIKFKEEESCHEAMHKEGYSFSSPRLSSVQGSDDPFYQEHMSKSSRCSSPG", "text": "FUNCTION: Glucose-regulated GTPase-accelerating protein (GAP) for the GTP-bound self-activating heterotrimeric G alpha protein GPA1. Cooperates with G beta-gamma dimers to maintain an unactivated but fully functional pool of GPA1. Phosphorylation-dependent endocytosis of RGS1 physically uncouples the two proteins, resulting in signal activation. Free AGB1 is essential, but not sufficient, for RGS1 endocytosis. Modulates cell proliferation, abscisic acid (ABA) and drought stress signal transduction by acting in a hexokinase- independent glucose-signaling pathway (PubMed:26528314). Involved in the shapes of leaves, the development of floral buds, the elongation of stems, siliques, and hypocotyls, the time of flowering and the regulation of guard-cell K(+) and anion channels. Important for the kinetics of voltage activation of inward K(+) current but not for the current amplitude. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Note=accumulates at the nascent cell plate during cytokinesis."}
{"protein": "MASISYLLAPLVLAAVLQPTAGAPLDAPTESPAGETSGEEAETGSPDDALAVALESVLGATKLHKNEFLVEFQGEVKYDFLDRYKIPSLPAKCPYSNFGKDACLRRLLEGLLIYSVLLKRVEEEFPSSSILSEVRFYSNILIKELENKVRDRDQVMRLTSSQEEQLLKDTDYPDTFHRKMTAHGILYNLHYFLVDCRRVINKRAKHRESAGSRVVRAVTFYHPKKRS", "text": "FUNCTION: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane- bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily."}
{"protein": "MIAFTDIVGMDLAKQALMLLAVDPSLGGVVIPSTVGSGKSTLARAFADILPEGTPFVELPLNVTEDRLIGGVDLEATLASGQRVVQHGVLSKAHKGVLYVDSLSLLDSSAVSHIMDAMSRGAVIVEREGLSEVHPADFMLVGTYDPSDGEVRMGLLDRIGIIVPFTPVNDYRARKQIVSLVMGTRNEEDTQDELRMLRGIIGAAREQLHHVSITNEQIKGLIQTAISLGVEGNRVDIFAIRAALANAALGQRTEVDDEDLKLAVKLVLVPRATRMPEREPSEEEMQQEEPPPPEEQPEQEGEDENAPPDETDSDADEEQEETPDMIEELMMDAIETDLPENILNISLASKKKAKSGSRGEALNNKRGRFVRSQPGEIKSGKVALIPTLISAAPWQAARKAEKAKKGIKTGALVISTDDVKIKRFRDKSGTLFIFMVDASGSMALNRMRQAKGAVASLLQNAYVHRDQVSLISFRGKQAQVLLPPSQSVDRAKRELDVLPTGGGTPLASALLTGWETAKQARTKGITQIMFVMITDGRGNIPLAAAVDPAAAKAPKEELEKEVEALALSIQSDGIASIVVDTQMNYLSRGEAPKLAQKLGGRYFYLPNAKAEQIVEAALS", "text": "FUNCTION: Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. SIMILARITY: Belongs to the Mg-chelatase subunits D/I family."}
{"protein": "MIKIDFEKMGGLIPAVIQDNESGEVLMVAFMDEKTLNLTLESGKTWFFSRTRNKYWMKGEESGNTQDVVEVLTDCDADTVVIKVKQNGPAACHTGNRSCFYVRYENGAWVEHSNPLFDPNTVYKK", "text": "FUNCTION: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-CH family."}
{"protein": "MTMLNGLRILDTLPLAALEVGKHWYWEIGNLKLHGQVFMASWVVIALLIIASLLATRNIQRVPSGMQNFMEYVLEFLRDLARTQLGEKHYRPWLPFIGTLFLFIFVSNWSGSLIPWRLIEIPEGELAAPTNDINTTVALALLTSLAYFYAGLSKKGLGYFANYVQPIPVLLPIKILEDFTKPLSLSFRLFGNILADELVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYIHEAIESEEEEEHA", "text": "FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family."}
{"protein": "MSHLLRKPQANELSQGVKLVHEVKKSNSDLSYVEFKVLDLAPGSSYEESLSKQECCIVALTGKITATDHEQTFENIGTRESVFERKPTDSVYVSNDRKFGITAVTEARVALCYSPSENQLPTKLIKAEDNGIENRGKFSNKRTVHNILPDSDPSANSLLVVEVYTESGNWSSYPPHKHDQDNLPEESFLEETYYHELDPQQGFVFQRVYTDDRSIDETMTVENGNVVIVPAGYHPVGVPDGYTSYYLNVMAGPTRKWKFHNDPDHEWILER", "text": "FUNCTION: Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate). SIMILARITY: Belongs to the isomerase IolB family."}
{"protein": "MRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINFCANNYLGLANHPDLIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLAAFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMQELEARLKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRDRLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQITRAVEAFTRIGKQLGVIA", "text": "FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MAELKLGYKASAEQFAPRELVELAVLAESAGMDSATVSDHFQPWRHEGGHAPFSLAWMTAVGERTKNLVLGTSVLTPTFRYNPAVIAQAFATMGCLYPGRIFLGVGTGEALNEIATGYAGEWPEFKERFARLRESVRLMRELWLGDRVDFDGEYYRTKGASIYDVPEGGIPVYIAAGGPVVAKYAGRAGDGFICTSGKGEELYAEKLIPAVKEGAAAADRDADAIDRMIEIKISYDTDPELALENTRFWAPLSLTAEQKHSIDDPIEMEKAADALPIEQVAKRWIVASDPDEAVEKVGQYVKWGLNHLVFHAPGHDQRRFLELFKRDLEPRLRKLA", "text": "FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. SIMILARITY: Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family."}
{"protein": "MEVLESGEQSVLQWDRKLSELSEPGETEALMYHTHFSELLDEFSQNVLGQLLSDPFLSEKSESMEVEPSPTSPAPLIQAEHSYSLSEEPRTQSPFTHAATSDSFNDEEVESEKWYLSTEFPSATIKTEPITEEQPPGLVPSVTLTITAISTPFEKEESPLDMNAGGDSSCQTLIPKIKLEPHEVDQFLNFSPKEASVDQLHLPPTPPSSHSSDSEGSLSPNPRLHPFSLSQAHSPARAMPRGPSALSTSPLLTAPHKLQGSGPLVLTEEEKRTLVAEGYPIPTKLPLTKSEEKALKKIRRKIKNKISAQESRRKKKEYMDSLEKKVESCSTENLELRKKVEVLENTNRTLLQQLQKLQTLVMGKVSRTCKLAGTQTGTCLMVVVLCFAVAFGSFFQGYGPYPSATKMALPSQHPLSEPYTASVVRSRNLLIYEEHAPLEESSSPASAGELGGWDRGSSLLRASSGLEALPEVDLPHFLISNETSLEKSVLLELQQHLVSSKLEGNETLKVVELERRVNATF", "text": "FUNCTION: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis by activating the transcription of SEC23A, which promotes the transport and secretion of cartilage matrix proteins, and possibly that of ER biogenesis-related genes (PubMed:19767744). In a neuroblastoma cell line, protects cells from ER stress-induced death (PubMed:17178827). In vitro activates transcription of target genes via direct binding to the CRE site (PubMed:17178827). SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 2]: Nucleus Note=Upon ER stress, translocated into the nucleus. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-binding protein 3-like protein 1) is transported into the nucleus. SIMILARITY: Belongs to the bZIP family. ATF subfamily."}
{"protein": "MTVAITDVVLRDAHQSLFATRLRLDDMLPVAAQLDDVGYRSLECWGGATFDACIRFLGEDPWVRLRELKKAMPKTPLQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNMQAALQAVRRHGAHAQGTLSYTTSPAHTLQTWLDLTEQLLETGVDSVAIKDMSGILTPHAAFELVSEIKKRYDVTLHLHCHATTGMAEMALLKAIEAGVDGVDTAISSMSATYGHPATEALVATLAGTPYDTGLDIHKLESIAAYFREVRKKYHAFEGQLKGTDSRILVAQVPGGMLTNLEGQLKQQSAAHRLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNVLTGERYKTIAKETAGILKGEYGRTPAPVNAALQARVLDGADPVTCRPADLLKPELAQLEADVRRQAQEKGITLAENAIDDVLTVALFPQPGLKFLENRHNPAAFEPVPQAEAAQPVAKAEKPAASGVYTVEVEGKAFVVKVSDGGDVSQLTAAAPAPAPAPAPASAPAAAAPAGAGTPVTAPLAGTIWKVLASEGQTVAAGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLMTLA", "text": "FUNCTION: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation."}
{"protein": "MTACSTAIRAQQLLLPVLSALGLLAAGAPQPPNIVLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKVKPNIPVYRDWEMVGRFYEEFPINLKTGEANLTQLYLQEALDFIRTQHARQSPFFLYWAIDATHAPVYASKQFLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPKEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLQGHIIDRPIFYYRGNTLMAVTLGQYKAHLWTWTNSWEEFRQGIDFCPGQNVSGVTTHTQEEHTELPLIFHLGRDPGERFPLRFTSNEYQDALSRTTQVIQQHQKSLVPGQPQLNVCNQAVMNWAPPGCEKLGKCLTPPESVPEKCFWAH", "text": "SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the sulfatase family."}
{"protein": "MTTAQTQELDVQPTPLALLLLGREADPRSERGVECPGDLPSPSDPDLVARARAAKEKLGDKVFVLGHHYQRDEVIQFADVTGDSFKLARDAAARPEAEYIVFCGVHFMAESADILTSNDQKVVLPDLAAGCSMADMATAEQVAECWDVLTEAGIAEQVVPVSYMNSSADIKAFTGKHGGTICTSSNAERALNWAFEQGEKVLFLPDQHLGRNTAVRDLGMSLEDCVVYNPHRPNGGLTAKELRDANMILWRGHCSVHGRFSLDSVNDVRERIPGVNVLVHPECKHEVVAAADYVGSTEYIIKALEAAPAGSKWAIGTELNLVRRLANRFAAEDKEIVFLDKTVCFCSTMNRIDLPHLVWTLESLAEGTLVNRIEVDQETEAFAKLALERMLALP", "text": "FUNCTION: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the quinolinate synthase family. Type 3 subfamily."}
{"protein": "MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQVHAQRVAIASTGIIRDGSLLALNPHNLGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGDITEMVFITVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGANAKTIFTHAGQGDEQAQQLIHRSARTLARLIADIKATTDCQCVVVGGSVGLAEGYLALVETYLAQEPAAFHVDLLAAHYRHDAGLLGAALLALGEKL", "text": "FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily."}
{"protein": "MIVLHARDCDPKACTALRAHRMGLVELTRHPGDVPTGAVVLDPTVEKALSREDRDAALERGLVAVDCSWEHVHRYFGPLRRRCRHRILPYLIAANPVNYGKPCKLSTVEALAAALYILGFRREAEEFISRFKWGPAFLELNRERLEAYRRAETSAEVVRVQEEFLPDGL", "text": "FUNCTION: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3- carboxypropyl) pseudouridine (m1acp3-Psi). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TDD superfamily. TSR3 family."}
{"protein": "MAYKHILIAVDLSPESKVLVEKAVSMARPYNAKVSLIHVDVNYSDLYTGLIDVNLGDMQKRISEETHHALTELSTNAGYPITETLSGSGDLGQVLVDAIKKYDMDLVVCGHHQDFWSKLMSSARQLINTVHVDMLIVPLRDEEE", "text": "FUNCTION: Required for resistance to DNA-damaging agents. FUNCTION: Required for resistance to DNA-damaging agents. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal stress protein A family."}
{"protein": "MKLTCMMIVAVMFLTASIFITADNSRNGIENLPRMRRHEMKKPKASKLNKRVCIADDMPCGFGLFGGPLCCSGWCLFVCL", "text": "FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
{"protein": "MSIDIDWERATSGPDGELLAERIRSFIHDKFQQMVLPRFIRSVQVTSFNFGTIPPELEIRDLTDPFPDFYEDGDEDLSVSSEEQSPMREQADRYRERIDSWQANSPGGLEVQMSGRMGFGHPLQLAPDEDGSRLHPLRSPINLGDINPYLFPRSGTPGIPGGTSNLGYFMPLSGLSGSQTPLRAVTRGNPFSGGWPDSPLENESRIGHGQGPPRRRSEVNVDAIQSRPSTANTGNTLFSRGSVSTGDPRHSHSSQTVLANNPGQAPEANDSPVSAVPPLSGTPPRRMREQKAEDFQVFCRTKYAGNISLSLTAEILLDYPMPSFVGLPLKLNITGLTFDAVAVLAYIRRRIHFCFLSPEDAYALIGPETGGGGGDTMEPNSLRRKNLSLLRKIRVESEIGRKENGKQALKNVGKVEKFVLEQVRRIFEEEFVYPSFWTFLV", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MDM12 family."}
{"protein": "MDIAAAREIGAGIAVIALAGVGIGLGNIFSTLVSSIARNPAARPHVFGLGMLGFALTEAVALYALLIAFLILFV", "text": "FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family."}
{"protein": "MALLQIAEPGQSAAPHEHKLAIGIDLGTTNSLVATVQSGEARTLTDDLGEAMLPSVVRYQAGGITVGSEAVKSATQDPVNTLISVKRFLGKTQAEIEQSYGQLPYQFCQHDGALAIETAAGKISPVKASSHILAALKARAEQSFGNQEILGAVITVPAYFDDAQRQSTKDAAELAGINVLRLLNEPTAAAVAYGLDSGQEGIIAVYDLGGGTFDISILRLHQGVFEVLATGGDSSLGGDDFDSLIVDYLKQQTGVTTLSPAVLRLFINKAKACKEALSQYSTVNVGLEFDDEKHMVEVTREKLDELAIPLVKKTLRSCRRAVKDAGIENEEVLQVIMVGGSTRMPLVRSQVSEFFNKEALTSIDPDRVVALGAALQADVLIGNKPDSDMLLLDVLPLSLGLETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSLHVLQGERELVDDCRSLAKFSLKGIPPMTAGAAHIRVTFKVDADGLLSVSAMEKSTGVQADIQVKPSFGLSDDQVSNMLKESMSNAKGDMQARMLKEQQVEALRVIEALEASLASDSGLLDEAQLAYLRAEIAELVKVRENAQQPNEIKTAIEKMDNASSDFAARRMDASIKKVLTGQSVDNI", "text": "FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MAQNLKDFAGRLPAGPRGMGTAMKLLLGAGAVAYAVKESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRFPWFQYPIIYDIRARPRKISSPTGSKDLQMVNITLRVLSRPLASELPFMYQRLGLDYDERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSIILDDVAITELSFSREYTAAVESKQVAQQEAQRAQFLVEKAKQDQKQKIVQAEGEAAAAKMIGDALSKNPGYLKLRRIRAAQSIAKTIASSQNRVYLNADSLVLNLQDDTFTRGSDSLVAKQTKK", "text": "FUNCTION: Protein with pleiotropic attributes mediated in a cell- compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus. FUNCTION: In the mitochondria, together with PHB, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan. FUNCTION: In the nucleus, serves as transcriptional co-regulator. SUBCELLULAR LOCATION: Mitochondrion inner membrane Cytoplasm Nucleus Cell membrane. SIMILARITY: Belongs to the prohibitin family."}
{"protein": "MSMVSAFLKQAWFIENEEQEYIKAVKGSKGGPGSAVSPYPSFNPSSDVDALHKAITVKGVDEATIIEILTKRNNAQRQQIKAAYLQEKGKPLDEALKKALTGHLEDVALALLKTPARFDADELRAAMKGLGTDEDTLIEILTSRTNKEIREINRVYREELKRDLAKDITSDTSGDFQKALLSLAKGDRSEDFGVNDDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPHLRRVFQMYTKYSKHDMNKVLDLEMKGDVENCFTAIVKCATSKPMFFAEKLHNAMKGAGTRDKILIRIMVSRSEVDMNDIKACYQKLYGISLCQAILDETKGDYEKILVALCGRD", "text": "FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2. FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)- dependent binding to phospholipid membranes (By similarity). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, cilium Basolateral cell membrane Lateral cell membrane Cell membrane; Peripheral membrane protein Apical cell membrane Membrane; Peripheral membrane protein Early endosome Cytoplasmic vesicle membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Secreted Secreted, extracellular space Cell membrane; Peripheral membrane protein; Extracellular side Secreted, extracellular exosome Cytoplasmic vesicle, secretory vesicle lumen Cell projection, phagocytic cup Note=Colocalizes with actin fibers at phagocytic cups. Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles. Secretion is increased in response to wounding and inflammation (By similarity). Alternatively, the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in the protein translocation from the cytoplasm into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (By similarity). Detected in gelatinase granules in resting neutrophils. Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect. Displays calcium-dependent binding to phospholipid membranes (By similarity). SIMILARITY: Belongs to the annexin family."}
{"protein": "MVCKRWILYGRVQGVGLRHFLRVHGVRLQLEGYVRNLPDGSVEVVAQGEKEKVLKLKTIILQGNGFSRLEDVQEEDFPIGNYGSFHIEY", "text": "SIMILARITY: Belongs to the acylphosphatase family."}
{"protein": "MFKNAFANLQKVGKSLMLPVSVLPIAGILLGVGSANFSWLPAVVSHVMAEAGGSVFANMPLIFAIGVALGFTNNDGVSALAAVVAYGIMVKTMAVVAPLVLHLPAEEIAAKHLADTGVLGGIISGAIAAYMFNRFYRIKLPEYLGFFAGKRFVPIISGLAAIFTGVVLSFVWPPIGTAIQAFSQWAAYQNPVVAFGIYGFIERCLVPFGLHHIWNVPFQMQIGEYTNAAGQVFHGDIPRYMAGDPTAGMLSGGFLFKMYGLPAAAIAIWHSAKPENRAKVGGIMISAALTSFLTGITEPIEFSFMFVAPILYIIHAILAGLAFPICILLGMRDGTSFSHGLIDFIVLSGNSSKLWLFPIVGAGYAIVYYTVFRVLIKALDLKTPGREDTTDDAKAGATSEMAPALVAAFGGKENITNLDACITRLRVSVADVAKVDQAGLKKLGAAGVVVAGSGVQAIFGTKSDNLKTEMDEYIRNS", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport. Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration. It can also phosphorylate mannose, methyl alpha-glucoside and 2-deoxy-glucose. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MNALHRIGAGTLLAVLLAFGLTGCGEKEEVQQSLEPVAFHDSDECHVCGMIITDFPGPKGQAVEKRGVKKFCSTAEMLGWWLQPENRLLDAKLYVHDMGRSVWEKPDDGHLIDATSAYYVVGTSLKGAMGASLASFAEEQDAKALAGMHGGRVLRFEEIDQALLQEAASMQHGGMHDHAPNGAHNAHAGH", "text": "FUNCTION: May act as a metallochaperone involved in nitrous oxide reductase assembly. Specifically binds Cu(+). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the NosL family."}
{"protein": "MFKAKVLVVGPTESGKTILANFISDATETIGGEYNPTQGVRILEFECPNGNKGSSCEVELWDCGGDSKFESCWPVIMKDSHGVIIVFSADIPSHLKEIEMWHLNFIQKQRLQENRCLLIAHKKPGSGDERERLNLSPALAKLTLIYSNLEDDPEDVRMELMKYLRGIVSSLSESRDREEMSIIT", "text": "SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MTPILFVDRDGTLIVEPADYQIDAYEKLRLVDHVIPAMLKLRDAGYQFVIVSNQDGLGSESYPRASFDGPNNLMLQIFASQGIEFREVLIDCSWPADNAPTRKPGIGLMVPYLQDRTIDWARSAMVGDRITDIQFAQNLNIRGFQLRTDEFGGEWDWSGIAHELADAPRRALVQRNTKETRIRVELDLDRVAEPKTATGLPFFDHMLEQIGKHGGFALEIRAEGDLHIDEHHTIEDTGLALGQALREALGDKRGIGRYGFDPESSPWRVAGDTPQHGFTLPMDETIASAALDFSGRPYFVFEGEFKRERVGDMPTELVPHFFRSICDASGLNLHLTVRGENDHHKVEACFKALARALRQAIRREGTALPTTKGTL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family. SIMILARITY: In the N-terminal section; belongs to the histidinol- phosphatase family."}
{"protein": "MRGGAGMCFASMEAAGSRGMGKGASRRRTARSTAPVGALVERVVVAPAPVEQQRGAGRPEAHPQSVAARAVVTVRRRRKEDAKDRFAEQLDALADRVGRSVLLELVSTETDPRKGTPKKSKPSALVGWFDKKDVKAERVVYTAEFAVDAGFGEPGAVTVLNRHQREFYIESIVVEGFPTGPAHFTCNSWVQPTRVSRDRRVFFSNRPYLPSETPPGLRELRLRELADLRGDGTGERRITDRVYDYDVYNDLGNPDKGVASARPVLGGEQMPYPRRMRTGRPSTATDASAESRVEYPEPIYVSRDEEFEEGKNEMLSEGAIKALLHNFMPLLVSSVSPDIRDFAGFHDVDNLFKEGLRLKQALHDQLFQKIPFVRKIQENSEGLLRYDTPDIIKKDKFAWLRDDEFARQALAGINPVNIERLQAFPPVSKLDPAVYGPPESAITEEHIIGHLDGMSVQEAVEGSRLYMLDYHDIFLPFLDRINAQDGRKAYGTRAVFFLTAAGTLKPIAIELCLPPMTDGCKRAKRVFTPPADATSNWLWQLAKAHVCSNDAGVHQLINHWLRTHACMEPFIIAAHRQMSAMHPIFKLLKPHMRYTLKINALARQILINGDGVIESGFTPGNVCMEMSAFAYRELWRLDQEGLPADLIRRGMAVEDPSQPHGLRLLIEDYPYAADGLLLWSAISRWCEAYVAAYYPSDEAVQADYELQSWYAEAVQSGHADKRGAPWWPRLSTPGDLASLLTTLVWLCSAQHAALNFGQYPLGGYIPNRPPLMRRLVPAEGDPEYAHLVADPHRFFLSALPSLTQTTTFMTVIDTLSTHSADEEYLGERPDEAWTADPAALAAAREFAADVRRAEEEIERRNADPSRRNRCGAGVLPYELMAPSSGPGITCRGVPNSVTI", "text": "FUNCTION: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (By similarity). SIMILARITY: Belongs to the lipoxygenase family."}
{"protein": "MVTILIYLLILLIINVVLLLLGLIINKRSYSDREKNSPFECGFDPSIHTRAPFSMRFFLLAVIFLIFDVEIILLLPLTSNILNSNTHWPLTSSMIFLTILLIGLFHEWNQGSLDWMK", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family."}
{"protein": "MLTQESEDLLKQIEKLSPDFFYFKSNSLVYRAILETVNPIDKIALVSLLTALNTNNLIRQLGRLETIMKLIENSPASNIIYEYSKVILDNYVKRLLLKSGDSLCLISCSKKQITQSVITSVASQLTIAYEILEDEGTYTLAEIFASLLVSLDTKKKISINSGIFSGFWQLDLITNGFQKSDLIIIAGRPSMGKTAFAINITRHIIKTSQYYVILFSLEMSTEQLLRRILAQECHLNSQKIQSGQLTNVEWQRIVEESKILANLNFYIDDSAEISCDIIKVKVKLLRLQGKKIKLIIIDYLQLLQESKKSENRSQELSLITRSLKILARELNLPILVLSQLNRNLESRHNKRPLLSDLRESGCISKFSHIMWSHVSKPLFNFSIKKSHMHNFNKNIYQLLDQGEAFISRQDKKTTYKIRTNSEKYLELTSNHKILTLRGWQRCDQLLCNDMITTQIGFELSRKKKYLLNCIPFSLCNFETLANINISNFQNVFDFAANPIPNFIANNIIVHNSIEQDADLVIMLYRESYYNKEMEMEDMTEIIVAKHRNGPLGTFQLKFDANLANFLNV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the helicase family. DnaB subfamily."}
{"protein": "MLALRCGPRLLGLLSGPRSAPLLLSTTRTCSDGGARGANSSSQNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS", "text": "FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (By similarity). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:8567677, PubMed:9309684, PubMed:9820802). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:8567677, PubMed:9309684, PubMed:9820802). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:8567677, PubMed:9309684, PubMed:9820802). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (PubMed:8567677, PubMed:9309684, PubMed:9820802). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
{"protein": "MDEADRQLLRRCRVRLVSELQVAELWDALLSRELFTRDMIEDIQQAGSGSRRDQARQLVTDLETRGRQALPLFISCLEDTGQGTLASLLQSGRQAAKQDPEAVKPLDHLVPVVLGPMGLTAKEQRVVKLDPSQPAVGNLTPVVLGPEELWPARLKPEVLRPETPRPVDIGSGGAHDVCVPGKIRGHADMAYTLDSDPCGHCLIINNVNFCPSSGLGTRTGSNLDRDKLEHRFRWLRFMVEVKNDLTAKKMVTALMEMAHRNHRALDCFVVVILSHGCQASHLQFPGAVYGTDGCSVSIEKIVNIFNGSGCPSLGGKPKLFFIQACGGEQKDHGFEVACTSSQGRTLDSDSEPDAVPYQEGPRPLDQLDAVSSLPTPSDILVSYSTFPGFVSWRDKKSGSWYIETLDGILEQWARSEDLQSLLLRVANAVSAKGTYKQIPGCFNFLRKKLFFKTS", "text": "FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates effector caspases caspase-3 (CASP3) or caspase-7 (CASP7). Promotes DNA damage- induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). SIMILARITY: Belongs to the peptidase C14A family."}
{"protein": "MDKVELSDLSFNKDWSFYLLAHREFVPTATDKYACRVSHITLKEPKVVTWERDM", "text": "FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-2-microglobulin family."}
{"protein": "MFRSFSTAAKQAVKGTYVQRAIVGGAAVVGIGASTMLYADSLTADAMTAAEHGLHAPGYGWSHNGPLETFDHSSIRRGYQVYREVCAACHSLDRVAWRTMVGVSHTNAEVRAMAEEFEYDDEPDDQGNPKKRPGKLADYVPGPYPNEQAARAANQGALPPDLSLIVKARHGGPDYIFALLTGYPEEPPAGVVLPPGANYNPYFPGGSIAMGRVLFDDLVEYEDGTPATTSQMAKDVTTFLHWCSEPEHDERKRLGLKAMIVLSSLYLLSVWVKKFKWASIKSRKIVFNPPKK", "text": "FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MQDNKMKKMLFSAALAMLITGCAQQTFTVGNKPTAVTPKETITHHFFVSPIGQRKLLMQPKFVGGAENVVKTETQQTFVNALPGFITFGIYTPRETRVYCSQ", "text": "FUNCTION: Increases serum survival and confers group II surface exclusion."}
{"protein": "MHPSEMQRKAPPRRRRHRNRAPLTHKMNKMVTSEQMKLPSTKKAEPPTWAQLKKLTQLATKYLENTKVTQTPESMLLAALMIVSMVVSLPMPAGAAAANYTNWAYVPFPPLIRAVTWMDNPIEVYVNDSVWVHGPIDDRCPAKPEEEGMMINISIGYHYPPICLGRAPGCLMPAVQNWLVEVPTVSPISRFTYNMVSGMSLRPRVNYLQDFSYQRSLKFRPKGKPCPKEIPKESKNTEVLVWEECVANSVVILQNNEFGTIIDWAPRGQFYHNCSGQTQSCPSAQVSPAVDSDLTESLDKHKHKKLQSFYPWEWGEKGISTPRPKIISPVSGPEHPELWRLTVASHHIRIWSGNQTLETRDRKPFYTVDLNSSLTVPLQSCVKPPYMLVVGNIVIKPDSQTITCENCRLLTCIDSTFNWQHRILLVRAREGVWIPVSMDRPWEASPSIHILTEVLKGVLNRSKRFIFTLIAVIMGLIAVTAMAAVAGVALHSFVQSVNFVNDWQKNSTRLWNSQSSIDQKLANQINDLRQTVIWMGDRLMSLEHRFQLQCDWNTSDFCITPQIYNESEHHWDMVRRHLQGREDNLTLDISKLKEQIFEASKAHLNLVPGTEAIAGVADGLANLNPVTWVKTIGSTTIINLILILVCLFCLLLVCRCTQQLRRDSDHRERAMMTMVVLSKRKGGNVGKSKRDQIVTVSV", "text": "FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). FUNCTION: SU mediates receptor recognition. SUBCELLULAR LOCATION: [Endogenous retrovirus group K member 21 Env polyprotein]: Virion. SUBCELLULAR LOCATION: [Surface protein]: Cell membrane; Peripheral membrane protein Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the beta type-B retroviral envelope protein family. HERV class-II K(HML-2) env subfamily."}
{"protein": "MVVHPSPKLELAFVTIGFVLLASSPALAQQGQVLTTLENSVVTAAKGWETTVMNAARSLFWILAGIEVGIAAVWLAINAASLDSWFAELVKRIMFIGLFAFILDRGLEFAKAVVDSLYQIGAGGGSASPANIFDAGIRVATKMSEQAKFGLWEDNALAIAAVFAMVVVVVSFSLVAAIFVAVMVEMYVGLLAGMIMLGLGGSSYTKDFAVKYLVYAFSVGMKLMALVMIARIGSDILLGLAEAPTATSEQFITTLAIAGISVVVFVIAMYVPPILQGLVQGASVGGGMEAIRHGGQAASAALGAGFLTIGAANRGFAAASAARAGGASLAGAAMRGLEAGVGGAAGAVGSAAKDKAIGSPGAYAGSMLGLANAKLDQQSGRPGTPPPPPPINDKK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TrbL/VirB6 family."}
{"protein": "MAEIAVEVVYALPERQALLRLSVPAGTSAREAVLLSGIAEAFPGLDVQGCPLGIFGKLLARPEERVLEAGERVEIYRPLIADPKEVRKQRAARARSEREGG", "text": "SIMILARITY: Belongs to the UPF0125 (RnfH) family. SIMILARITY: Belongs to the UPF0125 (RnfH) family."}
{"protein": "METVPPSPITWPDGGALTNDWVHGLMSCFEWSSWNLPPSQLPSLLPVNVFDSLVLTAHKILHKERNCVHIDDLDSVSNVVVVGDIHGQLHDLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKGKHVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSPVLPKRTTRGKKNRRVVLLEPEPSSMKLGTLDELMQARRSVLDPPWEGSNLIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELKLIIRSHEGPDAREKRTGLGGMDNGYTIDHNVESGKLITIFSAPDYPQFQATEERYKNKGAYIILQAPDFSDPQFHSFEAVKPRPKAHPYYDFENVIDSDDEMDKSAMDTNNEQPNS", "text": "FUNCTION: Phosphatase active on para-nitrophenylphosphate (pNPP) and on various phosphoproteins such as myelin basic protein. Seems to act as a positive regulator of cryptochrome signaling involved in hypocotyl growth inhibition and cotyledon expansion under white and blue light conditions. Confers thermotolerance. Required for heat shock mediated- signaling pathway that leads to the expression of heat shock proteins (HSPs). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the PPP phosphatase family. PP-7 subfamily."}
{"protein": "MQPVQILTLVLLALGAWAAQESTEKAGYCPDFRQVLLDRRDCKQLCNDDASCPQNMRCCQRGCSWLCMNTTQEKDGLCPVATSHSSSSEEQQRKQLCDKTCKTDLGCEGKAKCCASSCGQTCFMPVKAKPGRCPAVTGICPEKKSWFHTCQRDDQCKENKKCCSSACGRRCTNPFPEEYEASQDESTLLAL", "text": "FUNCTION: Could be a protease inhibitor. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MFLQNILSVLAFALLIDAAPVKRSTGFVTLDFNVKRSLVDPKDPTVEVKRSPLFLDIEPTEIPVDDTGRNDVGKRGPVAVKLDNEIITYSADITIGSNNQKLSVIVDTGSSDLWVPDSNAVCIPKWPGDRGDFCKNNGSYSPAASSTSKNLNTPFEIKYADGSVAQGNLYQDTVGIGGVSVRDQLFANVRSTSAHKGILGIGFQSNEATRTPYDNLPITLKKQGIISKNAYSLFLNSPEASSGQIIFGGIDKAKYSGSLVDLPITSDRTLSVGLRSVNVMGQNVNVNAGVLLDSGTTISYFTPNIARSIIYALGGQVHYDSSGNEAYVADCKTSGTVDFQFDRNLKISVPASEFLYQLYYTNGEPYPKCEIRVRESEDNILGDNFMRSAYIVYDLDDRKISMAQVKYTSQSNIVGIN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MVVGKIIKISGPVVVAEGMKGSQMFEVVKVGNEGLTGEIIQLTEDEAIIQVYEETAGIKPGEGVEGTGAPLSVELGPGMLKAMYDGIQRPLNEIENATDSIYIPRGVSVPSISREIKWDFEPTAAAGDEVITGDVIGTVQETASIVHKIMIPFGVSGKIKEIKAGSFTVEETVAVVETAEGEKEIMMMQKWPVRKPRPSKGKQAPVIPLITGQRVEDTFFGLAKGGASAIPGPFGSGKTVTQHQLAKWSDVDVVVYIGCGERGNEMTEVIEEFPHLDDIKTGNKLMDRTVLIANTSNMPVAAREASVYTGITIAEYFRDQGLGVLLTADSTSRWAEAMREISGRLEEMPGEEGYPAYLSSKLAQFYERAGRVECLGSENKQGFVCIVGAVSPPGGDFSEPVTSNTLRIVKVFWALDANLARRRHFPAINWLTSYSLYIDDIAGWWQQNTAADWRSLRDEAMSLLQKEAELQEIVQLVGPDALPDRERVILEIARMLREDFLQQDAYHEVDSYCSPLKQYNMLKIIMTFYKKGLDAVAKGADPAGISAVTVKGDIARMKYLTDDEFINTKVPEIINKMESELGALIK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MGNSPSTQDPSHSTKKEHGHHFHDAFNKDRQGSITSQLFNNRKSTHKRRASHTSEHNGAIPPRMQLLASHDPSTDCDGRMSSDTTIDKGPSHLFKKDYSLSSAADVNDTTLANLTLSDDHDVGAPEEQVKSPSFLSPGPSMATVKRTKSDLDDLSTLNYTMVDETTENERNGKPHHERHRSSIIALKKNLLESSATASPSPTRSSSVHSASLPALTKTDSIDIPVRQPYSKKPSIHAYQYQYLNNDETFSENSQMDKEGNSDSVDAEAGVLQSEDMVLNQSLLQNALKKDMQRLSRVNSSNSMYTAERISHANNNGNIENNTRNKGNAGGSNDDFTAPISATAKMMMKLYGDKTLMERDLNKHHNKTKKAQSKKIRSASNSRRSSFASLHSLQSRKSILTNGLNLQPLHPLHPIINDNESQYSAPQHREISHHSNSMSSMSSISSTNSTENTLVVLKWKDDGTVAATTEVFIVSTDIASALKEQRELTLDENASLDSEKQLNPRIRMVYDDVHKEWFVPDLFLPAGIYRLQFSINGILTHSNFLPTATDSEGNFVNWFEVLPGYHTIEPFRNEADIDSQVEPTLDEELPKRPELKRFPSSSRKSSYYSAKGVERPSTPFSDYRGLSRSSSINMRDSFVRLKASSLDLMAEVKPERLVYSNEIPNLFNIGDGSTISVKGDSDDVHPQEPPSFTHRVVDCNQDDLFATLQQGGNIDAETAEAVFLSRYPVPDLPIYLNSSYLNRILNQSNQNSESHERDEGAINHIIPHVNLNHLLTSSIRDEIISVACTTRYEGKFITQVVYAPCYYKTQKSQISN", "text": "FUNCTION: Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source- regulated subcellular location and substrate specificity of the SNF1 kinase complex. Promotes the PKA-regulated relocalization of the SNF1 kinase complex to the vacuolar membrane in response to various types of carbon stress (By similarity). SUBCELLULAR LOCATION: Cytoplasm Vacuole membrane; Peripheral membrane protein; Cytoplasmic side Note=Resides in the cytosol during growth in glucose and relocalizes to the vacuolar membrane in response to carbon stress. SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit family."}
{"protein": "MGRKWANIVAKKTAKDGANSKVYAKFGVEIYVAAKKGDPDPETNSALKFVIDRAKQAQVPKHIIDKAIDKAKGNTDETFVEGRYEGFGPNGSMIIVDTLTSNVNRTAANVRSAFGKNGGNMGASGSVSFMFDKKGVVVFAGDDADAIFELLLEADVEVDDVEAEDGTITIIQLQLDLHKAIVALKESGIQEFNVTELEMIPQSEVSLEGDDLATFEKLYDALEDDEDVQKIYTNVDGF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TACO1 family. YeeN subfamily."}
{"protein": "MKKVWLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGKVDNKA", "text": "FUNCTION: Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. FUNCTION: Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms (PubMed:15213221). Is involved in the aerobic beta- oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source (PubMed:12535077). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Note=Partially membrane-associated. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Note=Partially membrane-associated. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MRHSTTLTGCATGAAGLLAATAAAAQQQSLEIIGRPQPGGTGFQPSASPVATQIHWLDGFILVIIAAITIFVTLLILYAVWRFHEKRNKVPARFTHNSPLEIAWTIVPIVILVAIGAFSLPVLFNQQEIPEADVTVKVTGYQWYWGYEYPDEEISFESYMIGSPATGGDNRMSPEVEQQLIEAGYSRDEFLLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWFRAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWLEQARGGTYELSSVLPATPAGVSVE", "text": "FUNCTION: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
{"protein": "MRVLFFVFGVLSLMFTVPPARSFISNDECPSEYYYHCRLKCNADEHAIRYCADFSICCKLKIIEIHGQKKW", "text": "FUNCTION: Has antibacterial activity (Probable). Upon stimulation with lipoteichoic acid, promotes cytokines and chemokines production and secretion (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MVLSRLAASGLLLLALLALSVDGKPVQQWAQSWPGPNIPQLLVQQWAQGGWPRPGPEIPPLTVQQWAQNWPHPQIPPLTVQQWAQGRPPGPPIPPLTVQQWAQARPPHPPIPPAPLQKWAPVQKWAPVQKWAPVQKWAPLLQPT", "text": "FUNCTION: [Bradykinin-potentiating peptide AP]: Acts as indirect hypotensive agent. Potently induces vasodilation of arterioles, with only a small increase in leukocyte rolling flux. FUNCTION: [Bradykinin-potentiating peptide 10c]: Peptide with several activities. It inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain (PubMed:11994001). It evokes transient hypotension (-14 mmHg) similar to that evoked by 0.5 ug of bradykinin, when injected alone into rats. It has a high bradykinin-potentiating effect (120%), when 60 nmol of BPP-10c are coinjected with 0.5 ug of bradykinin into rats (PubMed:22869554). Does not affect angiotensin-1 pressor effects. Shows potent and long-lasting antihypertensive activity as well as a reduction of the heart rate (PubMed:17475904). It also binds and dose- dependently promotes the activation of cytosolic argininosuccinate synthase (ASS1), an enzyme that catalyzes the conversion of citrulline, L-aspartate and ATP to argininosuccinate, AMP and pyrophosphate. It also enhances ASS1-dependent arginine production in HEK 293 cells, as well as in spontaneous hypertensive rat (SHR) and Wistar rat plasma. In addition, it induces the production of nitric-oxide (NO) by HUVEC cells via the endothelial nitric-oxide synthase (NOS3), which use arginine as a substrate and produce NO. It has been shown to be internalized by ASS1-expressing endothelial (HUVEC) and kidney (HEK 293) cells, and is detected homogenously distributed within the cell cytoplasm for up to 2 hours (PubMed:19491403). FUNCTION: [Bradykinin-potentiating peptide 11e]: Acts as indirect hypotensive agent. Increases leukocyte rolling flux and adhesion by five-fold in post-capillary venules, without any increments in vasodilation of arterioles. SUBCELLULAR LOCATION: Secreted Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of prey cells. SIMILARITY: In the N-terminal section; belongs to the bradykinin- potentiating peptide family."}
{"protein": "MAALQMDPELAKRLFFEGATVVILNMPKGTEFGIDCNSWEVGPKFRGVKMIPPGIHFLYYSSVDKANPKEVGPRMGFFLSLYQRGLTVLRWSTLREEVDLSPAPESEVEAMRANLQELDQFLGPYPYATLKKWISLTNFISEATVEKLQPENRQICAFSDVLPVLSMKHTKDRVGQNLPRCGTECKSYQEGLARLPEMKPRAGTEIRFSELPTQMFPAGATPAEITKHSMDLSYALQTVLNKQFPSSPQDVLGELQFAFVCFLLGNVYEAFEHWKRLLNLLCRSEAAMVKHHTLYINLISILYHQLGEIPADFFVDIVSQDNFLTSTLQVFFSSACSIAVDATLRKKAEKFQAHLTKKFRWDFAAEPEDCAPVVVELPEGTEMG", "text": "FUNCTION: Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing. SIMILARITY: Belongs to the AAR2 family."}
{"protein": "MADTATTASAASAAASASNASSDAPPFQLGKPRFQQTSFYGRFRHFLDIIDPRTLFVTEKRLREAVQLLEDYKHGTLRPGVTNEQLWSAQKIKQAILHPDTNEKIFMPFRMSGYIPFGTPIVVGLLLPNQTLASTVFWQWLNQSHNACVNYANRNATKPSPASKFIQGYLGAVISAVSIAVGLNVLVQKANKFTPATRLLVQRFVPFPAVASANICNVVLMRYGELEEGIDVLDADGNLVGSSKIAARHALLETALTRVVLPMPILVLPPIVMSMLEKTALLQARPRLLLPVHSLVCLAAFGLALPLAISLFPQMSEIETSQLEPEIARATSSRTVVYNKGL", "text": "FUNCTION: Mitochondrial amino-acid transporter (By similarity). Transports citrate (PubMed:12150972). Does not act as a serine transporter: not able to mediate transport of serine into mitochondria (By similarity) (PubMed:12150972). In brown adipose tissue, plays a role in the regulation of UCP1-dependent thermogenesis probably by supporting mitochondrial glycerol-3-phosphate utilization (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sideroflexin family."}
{"protein": "MADSLKMGNLSLNESQHAPAPAPSTGRAAYIPPHLRGRQMGGNMDGAAAAAPPPGPAAGPGNSWGGPRGGPRGGQWANANAPDFSPRGPNGNTSWSPHEARRPFNPNAYGHPGHGGSYGSGGGSARGSGDGQWRDGKHIPGPANPRLERELFGLPNDPTKQNTGINFANYDDIPVEASGHDVPEPVNAFTNPPLDDHLIENIKLAHYQTPTPVQKYSIPIVMNGRDLMACAQTGSGKTGGFLFPILSQAYQNGPSAAPAQAGGQFGYGRQRKAYPTSLILAPTRELVSQIFDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLVNIKYLILDEADRMLDMGFEPQIRRIVEGEDMPHVNDRQTLMFSATFPRDIQMLARDFLKDYVFLSVGRVGSTSENITQKVEYVEDHDKRSVLLDILHTHGTSGLTLIFVETKRMADSLSDFLLNQRFPATAIHGDRTQRERERALEMFRSGRCPILVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGVVRDLIDLLKEAHQEVPSFLESIAREGSGYGGRGGRGGRGRGANATRDMRRMGGGMGGPPSFGGSSYGAPGGSYGGGGGGSSSYGAPPSYGGGGGYGGGGSYGGGYGNPSGPTGPSSWW", "text": "FUNCTION: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1 subfamily."}
{"protein": "MTKTLHARPSAATDTTFAPPVITGTATEDALEILFHALLDVARRHDPELEDVLHGRADISSFTPEMLARALQVQGIWFQLVSIAEQNAAMRRRRHVERDQGREALNGSFAKVLAEASARGIGPQQIHALLKDLRIRPTITAHPTEGKRVTVLEKLRRIYLVLRELELPRWTERERNGLMNELRDQIELIWMTGELHLEKATVEREVAWGLHFFDETLFEMLPEMLLSLEESLAQYYPDETFEVPPFFQFGSWIGGDRDGNPYVTASVTRETLQRNALASLRRYRDGITHLGRVLSITERSLPVPETFRSELAHMLAESGDARAIANRNPGEAYRQFLSCVLRKLEATIARNKGARSVGPDYPSADGLINDLRTLEKGLADAKCGALATDIVRPVRRMVEIFRFSTVRLDLRENSTRTTKTLHALWKLRNGDREPPALDSPAWKDWLLTELARPRTPETSFEDFADRLPDDARETLATFALVGEMRDTLDREAFGAFILSMTRSTVDVLGAYLLAKEAGIFLDTTGTEICPLPIVPLFETIDDLRAAPAIMKELLGIPVVRRSTRWQGGVQEVMIGYSDSNKDGGFIASNWELYKAQVRLTTLGNHLGVPIAFFHGRGGSVSRGGVPTHRGIAAQPPGSIQGRFRITEQGEVVSFKYANRGTAAYQMELLAASVFEHALLSEGNGNGSRAEFDDALEALSGASRAAYVNLLQAEGLVDYFQAASPLDEISLLNIGSRPARRFGAKSLSDLRAIPWVFAWSQNRHVITGWYGVGSGLKSFIDVRGEAGEALLRRLFRDCRVFRLVLDEVEKTLLMVDLEIARDYAGLVEDAGIRARIFGMIEAEYALTREMVLRVSGDSELAQRFPQFSERLRGRLPTINQVSREQVELLRRYRSETDEDKREAVKSALLLSINCIAVGFGATG", "text": "FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. SIMILARITY: Belongs to the PEPCase type 1 family."}
{"protein": "MDTRSGSQCSVTPEAIRNNEELVLPPRISRVNGWSLPLHYFRVVTWAVFVGLSLATFRIFIPLLPHSWKYIAYVVTGGIFSFHLVVHLIASCIDPADSNVRLMKNYSQPMPLFDRSKHAHVIQNQFCHLCKVTVNKKTKHCISCNKCVSGFDHHCKWINNCVGSRNYWFFFSTVASATAGMLCLIAILLYVLVQYLVNPRVLRTDPRYEDVKNMNTWLLFLPLFPVQVQTLIVVIIRMLVLLLDLLGLVQLGQLLIFHIYLKAKKMTTFEYLINTRKEESSKHQAVRKDPYVQMDKGFLQQGAGALGSSAQGVKAKSSLLIYKCPCHFCTSVNQDGDSKAQEADDAPSTSTLGLQQETTEPMKTDSAESED", "text": "FUNCTION: Probable palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (By similarity). May play a role in cell proliferation (PubMed:28331227). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MAAAAAAPGPGSGPGDSPEGPEAEGPERRRKAHGMLKLYYGLSEGEAAGRPSGPDPLDPTDLNGAHFDPEVYLDKLRRECPLAQLMDSETDMVRQIRALDSDMQTLVYENYNKFISATDTIRKMKNDFRKMEDEMDRLATNMAVITDFSARISATLQDPHERITKLAGVHALLRKLQILFELPSRLTKCVELGAYGQAVRYQGRARAVLQQYQHLPSFRAIQDDCQVITARLAQQLRQRFREGGSGAPEQAECVELLLALGEPAEELCEEFLAHARGRLEEELRSLEAELGPSPLAPDVLEFTDHGGSGFVGGLCQVAAAYQELFAAQGPAGAEKLAAFARELGSRYFALVERRLAQEQGSGDNSLLVRALDRFHRRLRAPGALLAAAGLAEAATEIVERVARERLGHHLQGLQAAFLGSLTDVRQALAAPRIAGKEGPGLAELLANVASSILSHIKASLASVHLFTAKEVSFSNKPYFRGEFCSQGVRESLIVGFIRSMCQTAQSFCDSPGEKGGATPPALLLLLSRLCLDYETATISYILTLTDEQFLVQDQSPVTPVSTLCAEARETARRLLTHYVKVQGLVISQMLRKSVETRDWLSTLEPRNVRAVMKRVVEDTTAIDVQVGLLYEEGVRKAQSSDSSKRTFSVYSSSRQQGRYAPSYTPSAPMDTNLLSNIQKLFSERIDVFSPVEFNKVSVLTGIIKISLKTLLECVRLRTFGRFGLQQVQVDCHFLQLYLWRFVADEELVHLLLDEVVASAALRCPDPVPMEPSVVEVICERG", "text": "FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome- derived carriers to the TGN. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network Recycling endosome Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. SIMILARITY: Belongs to the VPS51 family."}
{"protein": "MSSVKIECVGSDRYRLGESPVWDEKENSLLCVDITGRKVCRWDAASGQVQALSVDAPVSSVALRKSGDYVITLGTRFAALKWKEQLVTTIAQVDRDKANNRFNDGKVDPAGRYFAGTMAEEIRPAVLERRQGSLYTLCPDHSVVKHFDQVDISNGLDWSLDHKTFFYIDSLSYSVDAFDYDLQTGKIGNRRSVYKLEKEESIPDGMCIDTEGKLWVACYDGGRVIRLDPETGKRIQTVKLPVDKTTSCCFGGKDYSEMYVTSASDGMDREWLSRQPQAGGVFKITGLGVKGIPPYPFAG", "text": "FUNCTION: Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium- binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SMP-30/CGR1 family."}
{"protein": "MKILVAVKRVVDYAVKIRVKPDKTGVETQNVKMSMNPFCEIALEEALRIKEAGFAKEVIAVSIGPSQCVDTLRTGLAMGADRGIHVETNSIFLPLTIAKILKSLADVENPGLIFLGKQAIDDDCNQTGQMVAALLGWPQATFASKVVLDKDKNVATVDREVDGGLETLNVDLPAVITTDLRLNQPRYASLPNIMKAKSKPIKKMTVQDLKVDIKSDIEILEVTEPPKRKSGVMVSSVDELIDKLKNEAHVV", "text": "FUNCTION: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF- ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). Involved in leucine catabolism and in phytol degradation. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the ETF beta-subunit/FixA family."}
{"protein": "MEQLAQRVEDLEMKLAFQESTIDVLDQQVIKLNDLLAEQQHQLRVLISKLQSVEPSNMATQAEETPPPHY", "text": "SIMILARITY: Belongs to the SlyX family."}
{"protein": "MAGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFPAILSFPLDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQSVEKILLSVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'- linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD). Required for sterol-induced ubiquitination of 3- hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent proteasomal degradation. FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed:20061386). In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed:20061386). Involved in endoplasmic reticulum-associated degradation (ERAD) (PubMed:22607976). Required for sterol-induced ubiquitination of 3- hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent proteasomal degradation (PubMed:23223569). SUBCELLULAR LOCATION: Endoplasmic reticulum Lipid droplet. SUBCELLULAR LOCATION: Endoplasmic reticulum Lipid droplet. SUBCELLULAR LOCATION: Endoplasmic reticulum Lipid droplet. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MATEAAPMDEKAKRMRDLLSSFYAPDPSISTSGSSINASFDNINSTSFDADQYMDLMIKKSNLEVLLQRHVQMAAEIKNLDTDLQMLVYENYNKFISATDTIKRMKSNIFGMEGNMDQLLQKIMSVQSKSDGVNTSLFEKREHIEKLHRTRNLLRKVQFIYDLPARLQKCIKSEAYGDAVRFYTGAMPILKVYGDTSFQDCRRASEEAIEIIIKNLQTKLFSDSESIQARAEAAVLLKQLDVPVDSLKAKLLEKLEQSLDGLQIKPEEASTLVEDDDSSNDTESNDQHPAKIHEDAVRGFSEAIRAYREIFPDSEERLFKLARALTAMHFEYMELYIKKRVSAADFLGIFRIVWEDVVLMDEVLPEAALSDLSAEAAQVTLKQFVARMFSHLQQDISDTLLKFDINQKEAVEGELLKVVLEASQKAVLQGTTNIFQDFRQLLDEKTGIFIKMKDLISGWIQKGSQDFFRSLEAQFLVLSGKTSSSNDIEGKSSDKIHAGLILVLAQLSVFIEQKVIPRVTEEIAASFSGGNSQAFENGPAFIPGELCRVFHAASEKLLQHYIDTRTQKVSVLLRKRFKTPNWVKHKEPREVHMYVDMFLHELEEVGKEVKQVLPQGTFRKHKRTDSNGSNTTTSSRSNTLHNDKMARSNSQRARSQLFETHLAKLFKQKVEIFTKVEFTQESVVTTTVKLCLKSLQEYVRLQTFNRSGFQQIQLDIQFLKAPLKEAVEDEAAIDFLLDEVIVAASERCLDVIPLEPPILDKLIQAKLAKSKEHNNNTVSS", "text": "FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome- derived carriers to the TGN. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (By similarity). Required for vacuolar targeting and cellular trafficking. Involved in the regulation of vascular tissue patterning, probably by regulating PIN1 expression pattern, thus modulating auxin flux. Important to prevent PIN1 accumulation within margin cells, possibly by targeting PIN1 to the lytic vacuole. Regulates PIN1 and ATHB8 expression pattern in secondary veins (PubMed:24757006). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network Recycling endosome Prevacuolar compartment Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. SIMILARITY: Belongs to the VPS51 family."}
{"protein": "MESFDNIYLDLSNQPGKCKLAETGLGWRPSGGGDTFTLDSSNIGAAQWSRAAKGYELKILSRSSGVIQLDGFDQEDFERLSKAFKIWYGINVESREHALRGWNWGKAEFTKAELAFNVQNRPAFEVPYSEISNTNLAGKNEVAVELSLSVDPNGSKPAGSTKNRGRKAAAGPDELVEMRFYIPGTAVKTENGIKGENADEKNGGEGEENGEEQNAANLFYELLMEKAEIGDVAGDTFATFLDVLHLTPRGRFDIDMYESSFRLRGKTYDYKIQYSSIKKFFLLPKNDDTHTLIVLGLEPPLRQGQTRYPFLVMQLKLDEEISLELNMTEELLETRYKDKLEPRYEEPIHQVITKIFRGLSGKKVIMPSKDFVSHHGHSGVKCSIKANEGLLYFLDKSLIFVPKPATYIQMENVAVVTMSRVGGAISASRTFDITVSLKAGMGEHQFSNINREEQQPLEEFFKAKNIRIKNEMSDDTNALIAAALDNDDMMSSDEDGGGRPDRGSADEDEESVDEDFQADSDSDVAEEYDSAHESSGSGSDAEMDDASDAGVDEDEDADADMSEEERPKKKSKTGK", "text": "FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. SIMILARITY: Belongs to the SSRP1 family."}
{"protein": "MANRGGRHARTEETENAINYVQCDGLAVMKMVKHCHEESNNMDLAQGALLGLVVDKCLEITNCFPFPKSGDETMDEEMYQLTVMRRLRRVNVDHLHVGWYQSSDVGNSLSLALLESQYHYQTSIEESVVVVYDTQKSSRGFLCLKAYRLTPQAIQMYKDGDFTPEAFRNLKVGYESLFAEIPIVIKNSPLTNIMMSELNELLPEDKGHNFLDLGTASVLENHMRSLIERVDELYQEAVRYNKYQQVVFKQDTEKHRALAKLAAENAVRTSKGEPTVSEEEVIKQFRPMPVPARLTATITSGQINTHAQHIAQFCSQSLAKLFITESLQNAKEAKEIK", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit H family."}
{"protein": "MELLRAKRMAEAGEIVPVMYKGKQVVIQHVDDEREMARVYFTDEPEHEQDVPVRLLEEQ", "text": "SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspH family."}
{"protein": "MKNDNQTLKRTMTSRHIMMMALGGAIGAGLFKGSSSAIDVAGPSVIIAYLLGGIILLFIMQGLAEMAVRNRNARTFRDLVQQVLGNYAAYFLDWIYWKMWVLNIAAEAVVAAIFIQYWLPGCPIWVLALGISLIVTIVNLLSVKIFAETEYWLAMIKITVIIIFIILGLLLLFVSFGDHTASGFSNLTDHGGFFPHGGTGLITAMLVVIYSYGGTEIIGVTLAETKNPEKVVPKAVRSTLTRIVAFYLLPFFIIVSLIPWNQVNSVPESPFVMVFKMVGIPGADHIMNAVILLAIISSMNSGLYGSSRILYTQASDGRLPKVFSKLSSKNVPMFAILMCTSSLYIGVLISLFAGSQTFNYLMGSLGYTVLFIWLIIGFAHLKSRKQQTETPAYYVKWFPYTTWFAIVALLAILIGVIMTTSIVITGITAAIYLLITVAYLVKGRKHQ", "text": "FUNCTION: May participate in leucine metabolism. May transport leucine or a compound related to leucine metabolism. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily."}
{"protein": "MNGTEPAEPTNGTNATAWPAGLLLAYYGDDFTGSTDAMEAMQAAGVPTVLCLQKPTPELLARFPEVRCVGMAGSSRGRSSAWMDDELPDVLASLAALGAPILQYKVCSTFDSSPEVGSIGRAIDIGVRHMPGNWSPMVIGAPRLKRYQMFGNLFAAVDGVGYRLDRHPTMSRHPVTPMNEADLRLHLARQTARRIELIDMLELRGADVATRVRALCAPDMPVVLIDVLDEETLAEAGRLVWEQRGEGIFTASSSGLQYALAAHWRARGLLPPTPSLPAADPVQAIAAVSGSCSPVTAAQIGWARAHGFHTERLDLPRALDSRDGAAEIERVVTAATQALTRGISVIVHSAEGPDDPAVTGFDAIASAAGFARHDAARKVGRALAEVMRRLLDSVELTRVVVAGGDSSGEVASVLGIDALSVMAGLVPGAPLCRAWSAEPRRDGLQIVLKGGQIGDATFFGMVREGRLAGA", "text": "FUNCTION: Involved in catabolism of D-apiose. Catalyzes the phosphorylation of 3-oxo-isoapionate to 3-oxo-isoapionate 4-phosphate. SIMILARITY: Belongs to the four-carbon acid sugar kinase family."}
{"protein": "MSEENVQEFVLKEDCELRFAAGDDSDVCLELVKGYAEIFGTELLLNKKYTFPAKSRVAAFTWKGATIELVGTTESAYVAESTPMVIYLNIHAAMEEVRKKREEQAAGNSNKAKGPRLLLVGPTDVGKTTVSRILCNYSVRQGRTPIFVELDVGQNSVSVPGTVAAVLVQKTADVIDGFERNQPIVFNFGHTSPSANLSLYEALFKEMATTLNAQIQENDEAKIGGMIINTCGWVDGEGYKCIVKAASAFEVDVVIVLDHERLYSDLSKELPEFVRLTHVPKSGGVEQRTGQIRSKMRGENVHRYFYGTRANNLYPFTFDVSFDDVTLCKIGAEQLPDSCLPFGMEVENHETKLVIMEPSADIKHHLFAFSRSTKADENVLKSPVFGFCLVTEVDLEKRTMSILCPQRTIPSKVLVFSDITHLDDQIKR", "text": "FUNCTION: Required for endonucleolytic cleavage during polyadenylation- dependent pre-mRNA 3'-end formation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily."}
{"protein": "MTPPSGVGHTTRPLRATWRDYLALTKPKVISLLLWTTLTAMFMAARGWPGLGLLVVVSLAGYMSAGSAGVFNMIIDRDIDLRMKRTATRPTSSGLISTRDAAIFGGALQVLSFGMLWVWATPLAAWMSLAGFLTYVVVYTLWLKRNTWHNIVLGGAAGCFPPLVGWAAVTGDLNLFAWFLFAIIFFWTPVHFWALALMIKDEYREVGIPMLPVVHGDRLTVAQIGLYAIYTVVLSVMPVFLGEVGWLYFLSALVLGWLLLQRSWVLYRHVMAGNKVERKVAVPLYLYSMLYLALLFVAGAVDRVLLG", "text": "FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily."}
{"protein": "MSSTERLQRYLTDERGGCGDEEVAQRLDELEELDAAAGGPALEADVGVLSALANETRYKIIRILHIAGEELCVCEFSPLLDVSDSAISHSLSQLTEAGLVTRRKDGKWRKYQTTMRGDALLVALNGSRR", "text": "FUNCTION: Transcriptional repressor for the arsADRC operon."}
{"protein": "MNKTELINAVAEASELSKKDATKAVDSVFDTILDALKNGDKIQLIGFGNFEVRERSARKGRNPQTGEEIEIPASKVPAFKPGKALKDAVAGK", "text": "FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Binds evenly across chromosome, does not display a preference for AT content (PubMed:21085634). SUBCELLULAR LOCATION: Cytoplasm, nucleoid Note=Evenly distributed in the nucleoid (PubMed:21085634). SIMILARITY: Belongs to the bacterial histone-like protein family."}
{"protein": "MRLFALVLIFFFSTRTCTEDVKSCPNGCECTDWKGYYVSCTDIATLPIFPGNTETLRLYETRLSSVPQDAFVNMVNISLIYLSVDVTLRSLEKHSFFNLKKITHVEIRNTRSLMSIDPEAFKDLPELKYLGLFNTGLTIFPALTRIHSHESNFMLEITDNLYITEIPANAFQGITKDALTVMLYSNGFTKIQHHAFNGTKLDAIYLHRNKELTELSEDMFAETISGPVLLDVSDSGVTSLPATGLESLRELSARNVWALKKLPSVKTFRHLIGADMTYPSHCCAFKNLKKKKGYLDYIICNLTAMRGQHYERSVGRITVPAVMDGTDKGIDISDPLLGNTYDHHDFLRSLHYHEFLGGHADYDMGFGDTLKNPQIATSQDFDSHYDYVVCEDGEAVTCAPAPDDFNPCEDIMGFSFLRVSVWFVSLLAVLGNMVVLFVLLTSHYKLSVSRFLMCHLAIADLCMGIYLLLIASVDLYTQSEYYNHAIDWQTGPWCTLAGFISIFATELSVYTLTTITLERWHAINFAMQLDRKLRLSHASAVMLGGWLLCLLLALMPVLGVSSYQKVSICLPMSTQNLLDQVYILFILVINIVAFVAICACYIKIYCAVHNPNYTSSRKDSSIAKRMAVLIFTNFLCIAPISFYAISAALDHPLITISNSKILLVLFYPLNSCANPFLYAIFTKAFQGDVFILLSKIGLCEQQAKLFRGQTISTRASSGDTNRRGIKTKILTRWNVQATATCHQSSVNKDNNTSRGRKCEPTANKSKHIQGMNSTMVFY", "text": "FUNCTION: Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin (PubMed:19523396). Also acts as a receptor for the heterodimeric glycoprotein hormone thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily."}
{"protein": "MATSAPGVPSSAAVREESPGSSWKEGAFERPYVAFDPDLLALNEALCAELLAACHVVGVPPASALDEDVESDVAPAPPRPRGAAREASGGRGPGSARGPPADPTAEGLLDTGPFAAASVDTFALDRPCLVCRTIELYKQAYRLSPQWVADYAFLCAKCLGAPHCAASIFVAAFEFVYVMDHHFLRTKKATLVGSFARFALTINDIHRHFFLHCCFRTDGGVPGRHAQKQPRPTPSPGAAKVQYSNYSFLAQSATRALIGTLASGGDDGAGAGAGGGSGTQPSLTTALMNWKDCARLLDCTEGKRGGGDSCCTRAAARNGEFEAAAGALAQGGEPETWAYADLILLLLAGTPAVWESGPRLRAAADARRAAVSESWEAHRGARMRDAAPRFAQFAEPQPQPDLDLGPLMATVLKHGRGRGRTGGECLLCNLLLVRAYWLAMRRLRASVVRYSENNTSLFDCIVPVVDQLEADPEAQPGDGGRFVSLLRAAGPEAIFKHMFCDPMCAITEMEVDPWVLFGHPRADHRDELQLHKAKLACGNEFEGRVCIALRALIYTFKTYQVFVPKPTALATFVREAGALLRRHSISLLSLEHTLCTYV", "text": "FUNCTION: Plays a role in efficient localization of neo-synthesized capsids to nuclear replication compartments, thereby controlling cleavage and packaging of virus genomic DNA. SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus. SIMILARITY: Belongs to the herpesviridae UL32 protein family."}
{"protein": "MDFELEPTLEELIKQDTLKWIFVGGKGGVGKTTTSSSIAVQLALQHPEDEFLLISTDPAHNLSDAFCQKFGKDARKVEGLSNLSCMEIDPEAAMSDLQQQAQQYNNDPNDPLKSMMNDMTGSIPGIDEALSFMEVLKHIKNQKVTESDTKDKVSYRTIIFDTAPTGHTLRFLQLPTTLQKLLGKFQQLSGKLGPMMSMLGGGAQGQQDMFAKLNEVQKNVEEVNEQFTNPDLTTFVCVCISEFLSLYETERMIQELMSYKMDVNSIVVNQLLFADDDENPCKRCVARWKMQKKYLDQMAELYEDYHLVKMPLLGSEIRGVDNLKRFSQFLIKPYDPKVDRAIITDLKEQ", "text": "FUNCTION: ATPase required for the post-translational delivery of tail- anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum Golgi apparatus Note=GET1 and GET2 are required for targeting GET3 to the endoplasmic reticulum. SIMILARITY: Belongs to the arsA ATPase family."}
{"protein": "MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV", "text": "FUNCTION: [Isoform 2]: Forms toxic aggregates that disrupt spore maturation. FUNCTION: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele. FUNCTION: [Isoform 1]: Localizes isoform 2 to the vacuole thereby facilitating its degradation (By similarity). In addition to suppressing isoform 2, also suppresses S.pombe strain FY29033 wtf18 isoform 2 (PubMed:32032353). SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm Cytoplasm Spore membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. SIMILARITY: Belongs to the WTF family."}
{"protein": "MATTLISKLTLSSAFLGQQFSSRGNSMRSAPAGLFLRGPRCAATDTPYGGNIPQFPRVNVWDPYKRLGISRDASEEEVWSSRNFLLNQYYNHERSAESIEAAFEKILMASFINRKKTKINLKTRLKKKVEESPPWVQNLLSFVELPPPVIILRRLFLFGFMACWSVMNSTEAGPAFQVAISFGACVYFLNDKTKSLGRAALIGFGALVAGWFCGSLLVPMIPPNLLHPTWSLELLTSLFIYVSLFLGCTFLK", "text": "FUNCTION: Exhibits holdase chaperone activity involved in the stabilization of POR proteins against photooxidative stress in chloroplasts. Required for chloroplast development. SUBCELLULAR LOCATION: Plastid, chloroplast envelope Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chaperone-like protein of POR1 protein family."}
{"protein": "MYAFYSLLIYIFYSLFRRDGGAAAAAEPGDPAQRARKPRGRRRPDLPAPELWTELTGLAASSEPEDGSEGAAEGRAAAVSLEEALLRLAEFLSVQLGAEESCGGPADLGQSGEVPSLLTVTSQLLALLAWLRSPRGRQALLQGTQPAPRVRPPSPDGSTSQEESPSHFTAVPGEPLGDETQGQQPLQLEEDQRAWQRLEQLILGQLEELKQQLEQQEEELGRLRLGVGATDSEKRVQHLTLENEALKQSLSLMRDLLLHWGPGPPIRAPQEEAEALLELQGRLQEAQDTTEALRAQLGVQEVQLQGLQGALQQLQQETEQNCRRELQQMHGQLAGLRARMASLRQGCGDLRGLVSTFTQSCQGSLSEARGQVSWALGALSSGGPGTQLPEGQQGPPAGCPGRLPELKGNIRVLCRLRPGTSSSLVSVEPGPGGTVTTCYRGRHRRFRLDWVFPPDASQEEVFRELEPAVLSCLRGYSVCIFTYGQTGTGKTYSMEGPPEDPGIVPRALQSLFREMGAGRQHRVTLSMVEIYNEAVRDLLAPGPPERLAVRQGPEGQGGIQVAGLTHWDVPNLETLHQMLKLGRSNRATAATAMNQRSSRSHALVTLTLRAASPPRAPGTAGTLHLVDLAGSERARKAGAAGPPRGDPDGARRLREAQTINRSLLALGGVMAALRAHRPHVPFRDSQLTRLLQPALGPGTTAVLLLQVGAGAGQVCACRSPPTRARPPAPLARRSPRGRRISGRQSAPSSSPTEWVKWSWGQPGAAGSRAPPGRLLPSAPTLRSPGPPAPLRRPLAVLHAPVPTTARARLSRPQRACPSSPGSRPCPWGLRPGLCWQRR", "text": "FUNCTION: May play a role in microtubule-dependent retrograde axonal transport. May function as the motor for the transport of multivesicular body (MVB)-like organelles in dendrites (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family."}
{"protein": "MTTLFDILNTLNNNNNNNNNYAGCKRQHSINKRVDIIPSMDVTLTNDKLIIETELTGVSKNDIDINIKDSILIIQGEKKKSIIKHQQQQQHQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLENSNKENDEPSIEEFEEDVKSKSELNKTTLNTTENKDEDKTTQNISKKFISERSFGNFKRYLNLSEILYQLDLNSINTQFENGLLTITIKKKFDSSNTIKININ", "text": "SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
{"protein": "MAEPVGDLVVDLSLDAARFDEQMARVRRHFSGTESDAKKTAAVVEQSLSRQALAAQKAGISVGQYKAAMRMLPAQFTDVATQLAGGQSPWLILLQQGGQVKDSFGGMIPMFRGLAGAITLPMVGATSLAVATGALAYAWYQGNSTLSDFNKTLVLSGNQAGLTADRMLVLSRAGQAAGLTFNQTSESLSALVKAGVSGEAQIASISQSVARFSSASGVEVDKVAEAFGKLTTDPTSGLTAMARQFHNVSAEQIAYVAQLQRSGDEAGALQAANEAATKGFDDQTRRLKENMGTLETWADRTARAFKSMWDAVLDIGRPDTAQEMLIKAEAAYKKADDIWNLRKDDYFVNDEARARYWDDREKARLALEAARKKAEQQTQQDKNAQQQSDTEASRLKYTEEAQKAYERLQTPLEKYTARQEELNKALKDGKILQADYNTLMAAAKKDYEATLKKPKQSSVKVSAGDRQEDSAHAALLTLQAELRTLEKHAGANEKISQQRRDLWKAESQFAVLEEAAQRRQLSAQEKSLLAHKDETLEYKRQLAALGDKVTYQERLNALAQQADKFAQQQRAKRAAIDAKSRGLTDRQAEREATEQRLKEQYGDNPLALNNVMSEQKKTWAAEDQLRGNWMAGLKSGWSEWEESATDSMSQVKSAATQTFDGIAQNMAAMLTGSEQNWRSFTRSVLSMMTEILLKQAMVGIVGSIGSAIGGAVGGGASASGGTAIQAAAAKFHFATGGFTGTGGKYEPAGIVHRGEFVFTKEATSRIGVGNLYRLMRGYATGGYVGTPGSMADSRSQASGTFEQNNHVVINNDGTNGQIGPAALKAVYDMARKGARDEIQTQMRDGGLFSGGGR", "text": "FUNCTION: Serves as a ruler that controls the length of tail by stopping the tail tube polymerization and is probably released from the tail shaft during infection to facilitate DNA translocation into the host cell (PubMed:2150582). Assembles into a multimeric linear form possibly stabilized by the covering tail assembly proteins G and GT (PubMed:23911548). Its C-terminus fixes the tail tip complex (J, I, L, K), thereby forming the tail assembly initiator complex (PubMed:23911548). Tail tube proteins polymerize around tape measure protein, displacing the tail assembly protein G and GT (PubMed:23911548). When the tail reaches the length specified by the tape measure protein, it stops and becomes capped by the tail terminator protein (Probable). Upon tail assembly, tape measure protein is cleaved into a form called H*, that plays a role later during virion entry in a new cell (Probable). Once assembled, the virion is released and can infect new cell by binding to the entry receptor LambB (Probable). After opening of a pore on the external membrane, the entry protein H* protein is probably released in the periplasmic space for successfull DNA injection (PubMed:23911548). SUBCELLULAR LOCATION: Virion Note=There are 6 copies of entry protein H* per mature phage. SIMILARITY: Belongs to the Lambdavirus tape measure protein family."}
{"protein": "MENNRNFPARQFHSLTFFAGLCIGITPVAQALAAEGQTNADDTLVVEASTPSLYAPQQSADPKFSRPVADTTRTMTVISEQVIKDQGATNLTDALKNVPGVGAFFAGENGNSTTGDAIYMRGADTSNSIYIDGIRDIGSVSRDTFNTEQVEVIKGPSGTDYGRSAPTGSINMISKQPRNDSGIDASASIGSAWFRRGTLDVNQVIGDTTAVRLNVMGEKTHDAGRDKVKNERYGVAPSVAFGLGTANRLYLNYLHVTQHNTPDGGIPTIGLPGYSAPSAGTAALNHSGKVDTHNFYGTDSDYDDSTTDTATMRFEHDINDNTTIRNTTRWSRVKQDYLMTAIMGGASNITQPTSDVNSWTWSRTANTKDVSNKILTNQTNLTSTFYTGSIGHDVSTGVEFTRETQTNYGVNPVTLPAVNIYHPDSSIHPGGLTRNGANANGQTDTFAIYAFDTLQITRDFELNGGIRLDNYHTEYDSATACGGSGRGAITCPTGVAKGSPVTTVDTAKSGNLMNWKAGALYHLTENGNVYINYAVSQQPPGGNNFALAQSGSGNSANRTDFKPQKANTSEIGTKWQVLDKRLLLTAALFRTDIENEVEQNDDGTYSQYGKKRVEGYEISVAGNITPAWQVIGGYTQQKATIKNGKDVAQDGSSSLPYTPEHAFTLWSQYQATDDISVGAGARYIGSMHKGSDGAVGTPAFTEGYWVADAKLGYRVNRNLDFQLNVYNLFDTDYVASINKSGYRYHPGEPRTFLLTANMHF", "text": "FUNCTION: Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family."}
{"protein": "MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPAGKPLEFSKPAAWQNNLPLTPVDKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYADQVASLYRGLDLRENF", "text": "FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit MsrP is non- stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. SUBCELLULAR LOCATION: Periplasm Note=Is attached to the inner membrane when interacting with the MsrQ subunit. SIMILARITY: Belongs to the MsrP family."}
{"protein": "MQLNTRQARIFKLANLLGTGKPVSAADIITSLECSEPTLTRALKELRESYSAEIKYSKAGHSYHLVNPGQLDKKTLRRMNEALAQNAELKTGESTGKVVLDKDKKTAVSLSLRMRILRKIDRLAALSGSTRSEAVEKLALHSVDELIKEYSAKKS", "text": "FUNCTION: Involved in tellurite resistance (PubMed:8981981). TerW binds specifically to the potential promoter region of the terZABCDE operon and probably regulates expression of the genes (By similarity). FUNCTION: Involved in tellurite resistance (Ref.2). TerW binds specifically to the potential promoter region of the terZABCDE operon and probably regulates expression of the genes (Ref.2)."}
{"protein": "MKIVVDENMPYAEALFGRLGEVVAVRGRPLPAAALVGADALMVRSVTTVNQALLAGQRVRFVGTATAGTDHVDTAWLAQAGIGFSAAPGCNAIAVVEYVFSALMLLAERDGFALRDKTVGIVGVGNVGSRLQRRLTALGIRTLLCDPPRADRGDDEQFHSLADLQREADIITFHTPLNKSGPYRTLHLADADFLRGLPPGRILINAGRGAVVDNAALLQALEAGQDLRVVLDVWEPEPMLSLPLLARVDIATPHIAGYSLEGKARGTTQVFEAFSTFLGQPQSVVLPSLLPPPPVASVRIHGHPDQAMLKRLMHLVYDVRRDDVPLRRVAAQEGEFDRLRKHYPARREWSSLQVLCDDCTSASLLTALGFDARVA", "text": "FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily."}
{"protein": "MIDQKIFETTLNIDDPTNFCTNVEAHLLKELENIYVGKCFKNSFILNITGVIQRSPCFIMRTNNSGRGYMHVRFSAVVSYLNAFDLIAAVKIIKNDSNIILGESLLTEPVTIVIPSSESQNNVAEVGQIVPVQLANSSVYYIPGRQQASATGSIFIPKHTFSVYHVQEELTQEQALNLTKLVNIIEMLLESRSKKDFKQICFFEKLYYTYSISSDEILDLKIWKGPKGKEMSRLKPCNVLSFLYDALKNKSSSLGFWARPPNLLKSSPLAYQQDQNSFNATELPIICSAEVMFVTLLKEIINYLQFMNDLCDTFNNEQLIKRHENIWMLIEQRKIGHDF", "text": "FUNCTION: Component of the DNA-directed RNA polymerase (RNAP) that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Host cytoplasm Virion Note=Found in association with viral nucleoid. SIMILARITY: Belongs to the Asfivirus DNA-directed RNA polymerase RPB7 homolog family."}
{"protein": "MVFLKNKVKKKLILGIDFGTTYSLLASVQNERVVLLTDDKKRYLLPSIVNFNKKKPLIGWEAEKKIIKDPINTITSVKRLIGRSIDFIKKEFPILPYVIEDNKDGGILFHTNSGLVTPIDVTSEILKFLKEKSCEFFNKKIDATVITVPAYFDNLQRDSIKKAAISAKINLIRLLNEPTSAAVAYGLQLNTEGLVVVYDLGGGTFDISVLKLNKGIFEVLGTAGHANLGGDDFDTLLSKYIYKKLNLSNQCDNFFQSLLLKKAKEIKIKLTKYEKVEVNFFNWKGIIFRDEFNLIIKDLIQKTLFICSNLLKEIDLKIESIKEVIMVGGSTRVPLVYQEVKKFFRKSPLISINPDQVVAIGAAIQSDMLMKNTIQKRTILLDVTPLSLGIEVMGGFVEKIIFRNTPIPISKTKEFTTAKDNQTIIVIHILQGERELVKDCISLSRFILKDIPSKKAGVVRILVTFEIDTDGLISVKILEKFSHKEKKIQIENVTFLQNKNIHKIIKESTINAKEDYYLRVRKEKKIESKYILDLLNNALQEDRNLITSEELKKIKSHQIKLQKSIDEDDFFSMKLNLKKLEEVSKNFLSLRLKKNMDSFSIKNLSDEIT", "text": "FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU (By similarity). SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MAWRGSISKSMKELRILLCQSSPASAPTRTFVEKNYKDLKSLNPKLPILIRECSGVQPQMWARYDMGVERCVNLDGLTEPQILKALENLVKSGATKA", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFA2 subunit family."}
{"protein": "MNHIHEHLKLVPVDKIDLHETFEPLRLEKTKSSIEADDFIRHPILVTAMQHGRYMVIDGVHRYTSLKALGCKKVPVQEIHETQYSISTWQHKVPFGVWWETLQQEHRLPWTTETRQEAPFITMCHGDTEQYLYTKDLGEAHFQVWEKVVASYSGCCSVERIAQGTYPCLSQQDVLMKYQPLSYKEIEAVVHKGETVPAGVTRFNISGRCLNLQVPLALLKQDDDVEQLRNWKQFLADKFANMRCYTEKVYLVEQ", "text": "FUNCTION: Free serine kinase that uses ATP to phosphorylate L-serine to yield O-phospho-L-serine and ADP. O-phospho-L-serine serves as a substrate for SbnA and is a precursor for staphyloferrin B biosynthesis (PubMed:29483190). Is also a DNA-binding regulatory protein that senses heme to control gene expression for siderophore biosynthesis. Binds to DNA within the sbnC coding region and is required for expression of genes in the sbn operon from sbnD onward (PubMed:26534960)."}
{"protein": "MTSSLKIWGILLALLCILCRLCVYSNNIYWREFIKLHYLSPSREFKEYKCDVLMREKEALKGKSFHMFIYSLWFKIQRACINEKGSDRYRNAYVWAPGALKVLECHWEKYNNRYTESRSFSYIEFHCGVDGYVDNIEDLRIIEPISN", "text": "FUNCTION: Possible function in sperm maturation. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MRKIRANAIAILTVAWILGTFYYLWQDNRAHAASSSGRGAQRAGGRPEQLREDRTIPLIVTGTPSKGFDEKAYLSAKQLKPGEDPYRQHAFNQLESDKLSSDRPIRDTRHYSCPSLSYSSDLPATSVIITFHNEARSTLLRTVKSVLNRTPASLIQEIILVDDFSSDPEDCLLLTRIPKVKCLRNDKREGLIRSRVRGADVAGATVLTFLDSHCEVNVEWLQPMLQRVMEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTKPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYNFPEGNALTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMDCKSFRWYLENVYPELTVPVKEVLPGVIKQGVNCLESQGQNTAGDLLLGMGICRGSAKSPPPAQAWLFSDHLIQQQGKCLAATSTLMSSPGSPVILQTCNPKEGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQTDAQAQQWQLLPHT", "text": "FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily."}
{"protein": "MSSYGGGGYSSRGGGGGYSGGYDRNGGGGGGYSGSNGYSGGGGGYGGGGYGGGGGGYGGGGGGYGGGYGGGGGDRMSNLGAGLQKQNWDLDTLPKFEKSFYQEHPNVAARSQAEVDKFRRDHAMTVAGNNVPSPVETFDEAGFPRYVMDEVKAQGFPAPTAIQSQGWPMALSGRDVVGIAETGSGKTLTYCLPAIVHINAQPLLAPGDGPIVLVLAPTRELAVQIQQEITKFGKSSRIRNTCVYGGVPKGPQTRDLSRGVEVCIATPGRLIDMLESGRTNLRRVTYLVLDEADRMLDMGFEPQIRKIIGQIRPDRQTCMWSATWPKEVRALASDFLTDFIQVNIGSMDLAANHRITQVVEVVNESEKRDKMIKHLEKIMEDKESQNKILIFTGTKRVADEITRFLRQDGWPALSIHGDKQQNERDWVLDQFKTGKSPIMVATDVASRGIDVRNITHVLNYDYPNNSEDYIHRIGRTGRAGAKGTAITFFTTDNSKQARDLVGVLQEAKQHIDPRLAEMVRYGGGGGNSRYGGYRGRGGGGFRGGRSQGANGPNAMPMGNRRW", "text": "FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily."}
{"protein": "MHEWALADAIVRTVLDYAQKEGASRVKAVKVVLGELQDVGEDIVKFAMEELFRGTIAEGAEIIFEEEEAVFKCRNCGHVWKLKEVKDKLDERIREDIHFIPEVVHAFLSCPKCGSHDFEVVKGRGVYISGIMIEKEGEE", "text": "FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. SIMILARITY: Belongs to the HypA/HybF family."}
{"protein": "MSKRLLLFDFDETYFKHNTNEEDLSHLREMEKLLEKLTNNNEVITAVLTGSTFQSVMDKMDQVNMTFKPLHIFSDLSSKMFTWNNGEYVESETYKKKVLSEPFLFEDIEDILRHISAQYNVEFIPQRAFEGNETHYNFYFHSTGNHNNDSRILEALVRYANDQNYTARFSRSNPLAGDPENAYDIDFTPSNAGKLYATQFLMKKYNIPVKSILGFGDSGNDEAYLSYLEHAYLMSNSRDEALKQKFRLTKYPYYQGITLHVKEFVEGKYDY", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily."}
{"protein": "MKKTANKVVLIGAGAVGTSFLYAAINQGIAEHYVLIDAFPQPAEGNALDLSDTLAVIPHSFTSIKAGSYEDCKDADVVVITAGRPQKPGETRLEMVAGNAEIMKNIATEVKKSGFDGITVIASNPVDVITHVYQKVTGFDPHKVIGSGTTLDSARLRRLVGQKLNVKPESVQAYVAGEHGDSSVAIWSQANIMGRPILDYVKCGCLTLEDLDQIQKDTVDMAYKIINLKRATFYGIGACLTKIVNAVLRDEKATLMVGAQLNGEYKNKDLYTGVPAIIGSNGWEKIIEWDLTKEEQEKFDKSCETLHKTIDSVKHLF", "text": "FUNCTION: Catalyzes the conversion of lactate to pyruvate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family."}
{"protein": "MEAKFGSQISLHFRTNSFPLRKLYGFPLTTFSGTSLNHLRLKATNTLKGDDQESIRKFKKLPTSEWTHYFHSFVVDVSEMDALRNEIDALKPKVKNTIMSSQGIDSTKKRILMIYMLVSLGLAHHFEEEIYETLRDGFGKIEEMMEDEDDLCTVSIIFWAFRRYGHYISSDVFRRFKGSNGNFKESLTGYAKGMLSLYEAAHLGTTKDYILQEALSFTSSHLESLAACGTCPPHLSVHIQNVLSVPQHWNMEILVPVEYIPFYEQEKDHDEILLKFAKLSFKLLQLQYIQDLKIVTKWYKELEFASKLPPYFRDNIVVNYFYVLAVIYTPQHSYERIMLTQYFTCLAILDDTFDRYASLPEAISLANSLERWAPNDAMDKQPDYLKIVLNFILKTFEVFQKELEPEGRSYTVKATIEEFKTVTKGNFDLAKWAHAVHVPSFEEYMEVGEEEISVCSTLAGIFMCMEQKATKEDYEWLKSRPKFIQTLCARCRLKNDITGFEDDMSRGYVTNAVNCYMKQYGVTKQEAFGELNKIIVEADKILNEEFLTTVGVRHCVLKATFDLARMIFITYNGYEGFTYPQGKIKEYMTSLFVDRIGL", "text": "FUNCTION: Involved in terpene biosynthesis in roots. Possesses sesquiterpene (C15) synthase activity and diterpene (C20) synthase activity in vitro. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily."}
{"protein": "MRLWQWSIAVAICLVMVTEARLRRHHRKRRFVSSNFDEFYCGESAHAQSQFEEERESNSSKVSSVHSTQFNWGLDNTICIKLQNVVHVLKYERLEQRYPIENSYTFSVPLIDTNCKCHCYGFGTNDVCNVEKYADDRNCTTSSEFPTCYTKYHPAVEPLDCPVTSIPAKACCDIKLKPRDGRMFRAVKLQQPINDMIISHSIFANNSGKMMKVLGPDEFRINLLKGKEQFELTEYHRISVQLVASSPQQQLREGMYYFPEENHNDLREGKINEITESDLDKLGWYRRVGNDWQVATSGLLLRNAHKVVIKNCKGQVHMDQFSGTKNFVLRGTQYNDTYNERRVSDNNFVRSVKVDESSREITIVHEHGTAAQVSLKTDTRPNLTKSQSLLANFTGSITLDHDGNRMLNVTFFGVKGTVHIKMYVNDRKLIATFACTAQFGTSLKDDGSRISLPSTINQAQWVCILPDEQPTKSEICKWIPYEEKAMRTPRQEQSWSKGHSPCSQAECNSLKSGVSDLFPWIMNFDYFMAHGGDFTEWLKIGIHIVIAVGLLLLLILLFTKCLVPLACCSLSIPFKNRNKKKKKKNSSDY", "text": "FUNCTION: Required for cell fusion events during development including the fusion of anchor cells (AC), vulval A and vulval D rings, and late epidermal seam cells (PubMed:17488621). Required for amphid sheath cell fusion induced by entry into dauer stage (PubMed:21350017). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Apical cell membrane. SIMILARITY: Belongs to the EFF/AFF cell fusogen family."}
{"protein": "MGQEKLYTEKELSWLSFNERVLQEAADKSNPLIERMRFLGIYSNNLDEFYKVRFADLKRRILINEEQGSAVTSRHLLKKIQSKVVKADQEFDGLYNDLLLEMARNQIFLVNERQISENQQTWLKQYFKQHLRQHITPILINHDTNLVQFLKDDYTYLAVEIIRGQDIAYALLEIPSDKIPRFVNLPPEAPRRRKPMILLDNILRFCLDEIFKGFFDYDALNAYSMKMTRDAEYDLVTEMESSLLELMSSSLKQRLTAEPVRFVYQRDMPDEMVELLRNKLGISNDDSVIAGGRYHNFKDFINFPNVGKSNLVNRPMPRLRHVWFDKFRNGFDAIREQDVLLYYPYHTFEHVLELLRQASFDPSVLAIKINIYRVAKDSRIIDSMIHAAHNGKKVTVVVELQARFDEEANIHWAKSLTAAGVHVIFSAPGLKIHAKLFLISRLENDEIVRYAHIGTGNFNEKTARIYTDYSLLTADARITNEVRRVFNFIENPYRPVTFDNLMVSPQNSRLILYQLIDQEIIHAQAGESAGITLKINNLVDKGLVDRLYSASSAGVKIRLLVRGMCSLIPNMPGISDNIQVTSIVDRFLEHDRVYVFENKGDKLVYLSSADWMTRNIDYRIEVAVSLLDPKLKQRVLDILEILFNDTVKARYIDKELSNRYVPRGNRRKVRAQIAIYDYLKALEQPEQ", "text": "FUNCTION: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family."}
{"protein": "MKCLCFIVLLAIVIAQSYVGVEAAPSDGFVSRNGVQFILNGKPFYANGFNAYWLAYEATDPATRFKITNVFQNATSLGLTIARTWGFRNGAIYRALQTAPGSYDEQTFQGLDFGIAEAKRVGIKLIIPLVNNWDDYGGKKQYVDWARSKGEMVSSNDDFYRNPVIKEFYKNHVKTMLNRVNTFTKVAYKDEPASMAWQLMNEPRCGVDRSGKTLMAWINEMALFVKSVDPNHLLSTGHEGFYGDSSPERKNSLNPVSANTVGADFIANHNIDAIDFASMHCGSDLWFQRLDQNSRLAFIKRWLEGHIEDAQNNLKKPVILAEFGLGSDTPRYTLANRDDVFTTTYDIIYISTQKGGSAAGALFWEVISEGVSNFAGPSSIILSDKSSTVNIISEQRRKMGLLGGTKGK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "GSIPCAESCVYIPCFTGIAGCSCKNKVCYYN", "text": "FUNCTION: Probably participates in a plant defense mechanism. SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
{"protein": "MVFGQVVIGPPGSGKTTYCNGMSQFLSLMGRKVAIVNLDPANDALPYECGVNIEELIKLEDVMSEHSLGPNGGLVYCMEYLEKNIDWLESKLKPLLKDHYILFDFPGQVELFFIHDSTKNVLTKLIKSLNLRLTAVQLIDSHLCCDPGNYVSSLLLSLSTMLHMELPHVNVLSKIDLIGSYGKLAFNLDFYTDVQDLSYLEHHLSQDPRSAKYRKLTKELCSVIEDYSLVNFTTLDIQDKESVGDLVKLIDKSNGYIFAGIDASVVEYSKIAIGQTDWDYNRVAAVQEKYMEDEEIQD", "text": "FUNCTION: Small GTPase that is essential for the correct formation of the tangential divisions in early embryos. Associates with microtubule during mitosis and may function in the positioning of the division plane. May participate in the patterning of the early embryo at the octant-dermatogen transition (PubMed:17419841). Is crucial for normal development of the plant (PubMed:28475733). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, phragmoplast Note=During interphase, mainly expressed in the cytoplasm and weakly in the nucleus. Associated with microtubules during cell division. SIMILARITY: Belongs to the GPN-loop GTPase family."}
{"protein": "MKLADLSSPAFLENPYPLYETLRRQGSFVSIGPNALMTGRYSIVDGLLHNRNMGKSYMESIRVRYGDDALDMPLFQGFNRMFLMLNPPVHTHLRGLVMQAFTGRESESMRPLATDTAHRLIDDFEQKSSVDLVTEFSFPLPMRIICRMMDVDISDAISLSVAVSNIAKVLDPAPMSPDELVHASAAYEELAHYFTRLIELRRAQPGTDLISMLLRAEEEGQKLTHDEIVSNVILLLLGGYETTSNMIGNALIALHRHPKQLARLKSDLSLMPQAILECLRYDGSVQFTMRAAMDDVSIEGDVVPRGTIVFLMLGAANRDPAQFTDPDHLDITRKQGRLQSFGAGVHHCLGYRLALVELECALTVLLERLPHLRLANLDTLSWNQRGNLRGVNALIADLHS", "text": "SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MGHFSEELQQVQTRINRFLEAQFEGIESHNAPLLEAMKYALLLGGKRVRPFLVYATGQMLGAEKQTLDYAAAAIEAIHAYSLIHDDLPAMDDDNLRRGHPTCHIQFDEATAILAGDALQSFAFEILTKTPNISTEQKLALIQILAQGAGVQGMCLGQSLDLISEHKQISLSELELIHRNKTGALLIAALKLGFICSPHFTDKRLEQSLTQYAEAIGLAFQVQDDILDIEGDSAEIGKQVGADLDLDKSTYPKLLGLSGAKQKAQDLYQSALSELEKIPFDTTVRALAEFIITRKS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
{"protein": "MFNGLMDPEMIRLAQDQMSRMTPADFARIQQQMMSNPDLMNMATESMKNMRPEDLKQAAEQLKHTRPEDMAEISEKMAKASPEDIAAMRAHADAQFTYQINAAQMLKKQGNELHSRGNFSDAAEKYLRAKNNLKEIPSSKGGAILLACSLNLMSCYLKTNQHEECIKEGSEVLGYDARNVKALYRRGQAYRDLGLFEDAVSDLSKAHEVSPEDETIADVLRDVKERLAVEGPGKASRGVVIEDITEENNVTSGENKKPSKEANGHAQGVKTDVDGLQALRDNPEAIRTFQNFISKTDPDTLAALSGGKAGDMSPDMFKTASSMIGKMSPEEIQKMVQTASSFKGDNPFAPTAPSTENGFTPTPDMLKLASDMMGKMSPEERERMFNMASSLKANAPASTSYGNAEASEPRESLGASGSSSGNSFVAPRSGFEPSIPSAPPADLQEQMRNQMKDPAMRQMFTSMIKNMNPEMMASMSEQFGMKLSQEDAAKAQQAMASLSPDALEKMMRWADRAQTGMEKAKKAKKWLFGKGGLIFAILMLVLAMVLHRLGYIGN", "text": "FUNCTION: Plays a role in protein import into the endoplasmic reticulum (ER). May function as chaperone docking protein during post- translational protein translocation into the ER. Chaperone receptor mediating Hsp70-dependent protein targeting to chloroplasts. Interacts specifically with some chloroplast precursors, but not with mitochondrial precursors. Able to select precursors for delivery to the chloroplast translocase independently of Hsp70. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Plastid, chloroplast outer membrane; Single-pass membrane protein Note=Resides most likely exclusively in the ER membrane."}
{"protein": "MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAHERLAELEEKLPVAVNEQTGNGERDEMDLLGDHEENLAERLSKMVIENELEDPAIMRAVQTRPVLQPQPGSLNSSIWDGSEALRRIRGPLLAQEMPTVSVLEYALPQRPPQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMAVPSFTQQILCPKPVHVRPPMPPRYPAPYGERMSPNQLCSVPNSSLLGHPFPPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMFRPDTTHLHPQHRRLLHQRQQQNRNQHRNLNGAGDRGSHRSSHQDHLRKDPYANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEEIQGDGPKKERTKLITPQVAKLEHTYKPVQFEGSLGKLTVSSVNNPRKMIDAVVTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEERPALMDERKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARILPFLSTEQAADILMTTARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSVTITSLLQQLMNLPQSAATPAPSNPHLTAVLQNKFGLSLLLILLSRGEDLQSSDPATESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRYVDRQKLNLLETKLQLVQGIR", "text": "FUNCTION: RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly. SUBCELLULAR LOCATION: Cytoplasm, P-body Nucleus Nucleus, PML body Nucleus speckle Note=Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Enriched in splicing speckles. Localization to nuclear foci and speckles requires active transcription. Excluded from the nucleolus. SIMILARITY: Belongs to the PAT1 family."}
{"protein": "MIVRRQNRRFTIMAAGPRGSGKSSFFNSLIGKEIVTSRGHEGIDLYMLNLDCEGIMQRITLIDTPGFGEGFDDSEIQETICNFIKAQLDMFIAEESKIRRNPKYEDTRVHCLLYFIPSTSSSLKSRDIAFLRKVSGLVNIIPVISKSDGLSITERIEVKRQVMEQIKHYNISIFDLDDPEVYSSPAAGNDLNSLVPFLVVSADRENFESRARNYQWGDVSIDNPDHCDLPALRELLLSTHIYGLIDYTASEIYENYRAAVLEGGVRK", "text": "FUNCTION: Septins are GTPases involved in cytokinesis. The septins localize to the site of cleavage and act as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Septins are also involved in cell morphogenesis, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation (By similarity). SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
{"protein": "MDAKASNKTATLTVGNKNYDLPIHSGSVGPDVIDIGKLYGQSGLFTYDPGFTSTASCQSKITYIDGDAGVLEYRGYPIEQLAENGDFLETCYLLLYGNLPTAAQKKDFDDRVIHHTMVHEQMARFFQGFRRDAHPMAVMVASVGALAAFYHDSTDINDPKQRMIASMRMIAKIPTLAAMAYKYTIGQPFVYPKNSLKFAENFLHMCFAVPCEEYKINPVLADALDKIFILHADHEQNASTSTVRIAGSSGANPFACIAAGIACLWGPAHGGANEAALAMLAEIGSVDKIPEFIAKVKDKNSEVRLMGFGHRVYKNYDPRAKIMQKMCHAVLKETGHGDDPMLKVAMELEKIALSDQYFIDRKLYPNVDFYSGITLKAMGFPVSMFTVLFAVARTVGWISQWSEMIEDPQQKIGRPRQLYTGVTRRDYVAIKDRK", "text": "SIMILARITY: Belongs to the citrate synthase family."}
{"protein": "MMSATSLLVMNGPNLSRLGKREPEVYGSLTLDEINRGIAVAFPEVSFEFFQSEHEGALIEKLFEIEGRGGFSGVVLNAGALTHYSIALRDAISAVTMPVVEVHLSNVHKREEFRHKSVISAVCIGVIAGFGVESYHLGVRALLGRGNR", "text": "FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
{"protein": "MVDQLEDSVIETNYDEVIDTFDDMNLKPELLRGIYAYGFERPSAIQQRAIMPILGERDVLAQAQSGTGKTATFSISVLQKIDTSLKQCQALILAPTRELAQQIQKVVVALGDLMNVECHACIGGTLVRDDMAALQAGVHVVVGTPGRVHDMIQRRALPTDAVQMFVLDEADEMLSRGFKDQIYDIFQLLPPTAQVVLLSATMPQDVLEVTTKFMRDPIRILVKKDELTLEGIKQFYVAVEKEEWKLDTLCDLYETVTVTQAVIFCNTRRKVDWLTEQLTERDFTVSSMHGDMDQAQRDTLMHEFRTGSSRILITTDLLARGIDVQQVSLVINYDLPANRENYIHRIGRGGRFGRKGVSINFVTNDDVRMMREIEQFYNTHIEEMPMNIADLI", "text": "FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily."}
{"protein": "MPMKSLRNDHGTLKAMIGSDFNELTIAAKNLATHAFTLTGLGFGTSVLEWVASIAAIYLLVLDRTNWKTNMLTSLLIPYIFFSLPSLIFGIFRGEIGKWIAFVAVVVQLFFPKHAREYLELPVALVLLAVVAPNLIAGTFRDSWIGLAICLGIGCYLLQEHIRASGGFRNAFTKANGISNTVGIICLVVFPVWALIF", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Cold-regulated 413 protein family."}
{"protein": "MIEDTMTLLSLLGRIMRYFLLRPETLFLLCISLALWSYFFHTDEVKTIVKSSRDAVKMVKGKVAEIMQNDRLGGLDVLEAEFSKTWEFKSHNVAVYSIQGRRDHMEDRFEVLTDLANKTHPSIFGIFDGHGGETAAEYVKSRLPEALKQHLQDYEKDKENSVLTYQTILEQQILSIDREMLEKLTVSYDEAGTTCLIALLSDKDLTVANVGDSRGVLCDKDGNAIPLSHDHKPYQLKERKRIKRAGGFISFNGSWRVQGILAMSRSLGDYPLKNLNVVIPDPDILTFDLDKLQPEFMILASDGLWDAFSNEEAVRFIKERLDEPHFGAKSIVLQSFYRGCPDNITVMVVKFRNSSKTEEH", "text": "FUNCTION: Acts as a suppressor of the SAPK signaling pathways by associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the PP2C family."}
{"protein": "MVTNLYQNMRANALADAELRRKAADELTCMTARINRGETIPEPVKQLPVMGGRPLNRAQALAKIAEIKAKFGLKGASV", "text": "SIMILARITY: Belongs to the phage P protein family."}
{"protein": "MVSWMISRSVVLVFGNLYPAYYSYKAVKTKNVKEYVRWMMYWIVFALFTVVETVADLTIAWFPLYYEIKIAFVIWLLSPYTRGASVIYRKALHPLLSSKEREIDDYIVQAKERSYETMVNFGKQGLTIAATAAVSAAVKGQGAITEKLRSFSMHDLTQIPQDDGYSSYASNPARRAIMDQPDGAEYYHGDDDDRSDEDSKPVFSEDEAVSHHGLRRSQSVKVTRSKLRRDARYGSLKIKGRKRPGINATTYSNMES", "text": "FUNCTION: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DP1 family."}
{"protein": "MEQYTANSNSSTEQIVVQAGQIQQQQQGGVTAVQLQTEAQVASASGQQVQTLQVVQGQPLMVQVSGGQLITSTGQPIMVQAVPGGQGQTIMQVPVSGTQGLQQIQLVPPGQIQIQGGQAVQVQGQQGQTQQIIIQQPQTAVTAGQTQTQQQIAVQGQQVAQTAEGQTIVYQPVNADGTILQQVTVPVSGMITIPAASLAGAQIVQTGANTNTTSSGQGTVTVTLPVAGNVVNSGGMVMMVPGAGSVPAIQRIPLPGAEMLEEEPLYVNAKQYHRILKRRQARAKLEAEGKIPKERRKYLHESRHRHAMARKRGEGGRFFSPKEKDSPHMQDPNQADEEAMTQIIRVS", "text": "FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-YA positively regulates the transcription of the core clock component BMAL1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NFYA/HAP2 subunit family."}
{"protein": "MKIAAFDIGGTALKMGVMARDGRLLETARQSINDSDGDRILQAMLSWLAAHPSCEGIAISAPGYIDPHSGLITMGGAIRRFDNFAMKSWLETRTGLPVSVENDANCVLLAERWQGKAAEMANFLVLTIGTGIGGAIFCQHQLINGARFRAGEFGYMLTDRPGGRDPRRYSMNENCTLRVLRHRYAQHIGAPLDSVTGELIFDRYDAGDPVCQRLVAEFFNGLGHGLYNLVHIFDPQTIFIGGGVVERPGFLTLLRQHLAWFGIADYLDTVSHGNDAGLIGAVYHFNQLYRSPDDDRH", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of a wide variety of beta-D-glucosides, to produce 6-phospho-beta-D-glucosides including cellobiose-6'-P, gentiobiose-6'-P, cellobiitol-6-P, salicin-6-P, and arbutin-6-P. Is not able to phosphorylate alpha-D-glucosides. May have a dual role of kinase and transcriptional regulator of the cellobiose- PTS operon. SIMILARITY: Belongs to the ROK (NagC/XylR) family."}
{"protein": "MGGSQLKNLKAALKANGLTGQTNVKKSSKKKGKSPREFDREERQKTIERIREQFNPFDVKTNRNKKVGVMRESAAKLAVGKPGITKQAGEDQRKMFYEAKKSSKNRSGGVLDKRFGEKDKNLTSEEIMLERFTKERQRQSSTKRSLFNLDDSDGGEDENVYGEKLTHYGKSLSLEDDFDEGDLGLQHSDSEDFRLKQAGKRNMADQYGDEGLGDDALQEPARKKTKAEVMQEVIAKSKFYKHERQKAQEKLVQDIEGLDDDFESIMSELRTLPKTKPSQTEISTSTDIAPDYDIKVKELVLEKRAAPADRTKTDEEIKKEYEDKQKELEQKRLDRMNGIFNIEDQKDAGVEDLGEEFWEDSDSEEGEYGEYIKAIPDSDDDVDFEKDNNDDNEYDATSNGRPSARVIPSVPCPQIHDDLLNFLKSYPIEEHPSLVKRIVKTYQPKLAEGNKEKLGKFTAVLLRHILFLAEEDYSVNVKEIASLQNELVSILKTLSEKFTIPLSEDCRNIISDIQTRFKESQFYGLSPSDLVFFSVVGMLFSTSDHYHLVITPCLLLIAEFLEQIRFNSLQKLIFGSILVRIAIQYQRISKRYIPELTYFLQTSLRSLIPSTKGETLENKEKQEDNLSIVGSDINWSKVAPSLELHSLFSEDLEKQESIKLSVLVNNLESIDWCITNIWKDLTAFPEIINPFKDILNVAAEVYPGTSKPKQLVEKIEKLLKFQERLPLTLQQHKPLAIPSNTPKFEENFNPDKKSYDPDKTRSELNKMKAQLKKERKFTMKEIRKDTRFEARQGIEEKKKEYADYHSKMARIVNQISTEEGAEKNKYEREKKLRNTKR", "text": "FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP14 family."}
{"protein": "MSKTYIGIDIAKNTFDACFIAHNTWQNCTFTNNQQGFMELTLWIQAHHYNTSTLHLIIEATGTYWEKLAHWAISHHHKVSIVNPLYIHAYAKSLGIRTKTDKQDAILLARYGAKENPPLWQPKSDNEIKLTALLKQREHHKRQLIKERTRQEALSIYVKSYTDDNIRHWSDSITQLDHQIWQLINCTPELNHRASLLATIPGIGKKTLPHLLVAIGDGSSFQSAKHLASYAGLAPRHHQSGISIHKQSSIGFSGQKELRSALFMPAVIVSFGRYPAFQKFVKRMEQKGKTKKQIIIAIMRKLLTISYAVIRQNRPFDKRIHE", "text": "FUNCTION: May be the site-specific invertase required for pilin gene inversion. Moraxella can express either a Q or I pilin; the inversion of 2 kb of DNA determines which pilin is expressed."}
{"protein": "MADNMTTTQIEWRMKKMAIGSSTHSSSVLMKDIQSQFEQLKLRWESYPNLVKSTDYHQRRETIRLVTEELYLLSKRIDDNILFHKTVIANSSIIADMIVSLSLLETLYEMKDVVEVYSRQCL", "text": "FUNCTION: Mediates the nuclear export of encapsidated genomic RNAs (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs complexes and the nuclear export machinery of the cell. Possesses no intrinsic RNA-binding activity, but includes a C-terminal M1-binding domain. This domain is believed to allow recognition of RNPs bound to the protein M1. Since protein M1 is not available in large quantities before late stages of infection, such an indirect recognition mechanism probably ensures that genomic RNPs are not exported from the host nucleus until sufficient quantities of viral mRNA and progeny genomic RNA have been synthesized. Furthermore, the RNPs enter the host cytoplasm only when associated with the M1 protein that is necessary to guide them to the plasma membrane. May down-regulate viral RNA synthesis when overproduced. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the influenza viruses NEP family."}
{"protein": "MNDPNSCVDNATVCSGASCVVPESNFNNILSVVLSTVLTILLALVMFSMGCNVEIKKFLGHIKRPWGICVGFLCQFGIMPLTGFILSVAFDILPLQAVVVLIIGCCPGGTASNILAYWVDGDMDLSVSMTTCSTLLALGMMPLCLLIYTKMWVDSGSIVIPYDNIGTSLVSLVVPVSIGMFVNHKWPQKAKIILKIGSIAGAILIVLIAVVGGILYQSAWIIAPKLWIIGTIFPVAGYSLGFLLARIAGLPWYRCRTVAFETGMQNTQLCSTIVQLSFTPEELNVVFTFPLIYSIFQLAFAAIFLGFYVAYKKCHGKNKAEIPESKENGTEPESSFYKANGGFQPDEK", "text": "FUNCTION: Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine (PubMed:7592981, PubMed:9458785, PubMed:9856990). Transports various bile acids, unconjugated or conjugated, such as cholate and taurocholate (PubMed:7592981, PubMed:9458785, PubMed:9856990). Also responsible for bile acid transport in the renal proximal tubules, a salvage mechanism that helps conserve bile acids (Probable). Works collaboratively with the Na(+)-taurocholate cotransporting polypeptide (NTCP), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation (PubMed:33222321). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family."}
{"protein": "MSSFFLTGTDTNVGKTVASRAIIQALQNQGIQIVGYKPVAFSREECVYTDMENQQAAESDYDSQNNSDVLTLMKSTHEKVSYQEINSYTFRHSLPVFSVQGKHIRIEKMDADLARLNQKYQSVLVEGSYGWLTPINKTYCFADWAKSHQMPVVLVVGIKEGCLNHALLTVESIQQKGLPLLGWIANRINPCLGHYAEIIDLLSEKIDAPLLGQIPYLHKPEEQDLARYIHNLDRLTYMETVLAD", "text": "FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dethiobiotin synthetase family."}
{"protein": "MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA", "text": "FUNCTION: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4- mannans from different sources, yielding principally mannobiose (PubMed:21037302). Also has transglycosylation activity (PubMed:23558681). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "LLMPVKPNDDRVIGCWCISRGYLCGCMPCKLNDDSLCGRKG", "text": "FUNCTION: Has two active sites that simultaneously bind and inhibit trypsin."}
{"protein": "MGCSVSKKKKKNAMRPPGYEDPELLASVTPFTVEEVEALYELFKKLSSSIIDDGLIHKEEFQLALFRNRNRRNLFADRIFDVFDVKRNGVIEFGEFVRSLGVFHPSAPVHEKVKFAFKLYDLRQTGFIEREELKEMVVALLHESELVLSEDMIEVMVDKAFVQADRKNDGKIDIDEWKDFVSLNPSLIKNMTLPYLKDINRTFPSFVSSCEEEEMELQNVSS", "text": "FUNCTION: Acts as a calcium sensor involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Binding of a CBL protein to the regulatory NAF domain of a CIPK serine-threonine protein kinase lead to the activation of the kinase in a calcium-dependent manner. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. Involved in salt stress responses by mediating calcium-dependent microfilament reorganization. The CBL4/CIPK6 complex mediates translocation of AKT2 from the endoplasmic reticulum to the plasma membrane. Both myristoylation and S-acylation are required for AKT2 activation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Cytoplasm Nucleus Note=The cell membrane localization is S-acylation dependent. SIMILARITY: Belongs to the calcineurin regulatory subunit family."}
{"protein": "MFRKQNLKWLGVLATIIMTFVQLGGALVTKTGSEDGCGSSWPLCNGALLPENLPIQTIIELSHRAVSAISLIVVLWLVITAWKNIGYIKEIKPLSIISVGFLLVQALVGAAAVIWQQNPYVLALHFGISLISFSSVFLMTLIIFSIDKKYEADILFIHKPLRILTWLMAIIVYLTIYTGALVRHTKSSLAYGAWPIPFDDIVPHNAHDWVQFSHRGMAFITFIWIMITFIHAIKNYSDNRTVRYGYTASFILVILQVITGALSVITNVNLIIALFHALFITYLFGMIAYFILLMLRTTRSLK", "text": "FUNCTION: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the COX15/CtaA family. Type 1 subfamily."}
{"protein": "MEIQGLTIAYKQKVAIDNVTLQIASGKLTGIVGPNGAGKSTLLKGMMGLIPREQGQVTLADKPLTYWRKKIAYVPQRSEVDLTFPITVFDMVLLGTYPALGLIKRPGKKEKQLALDALEQVEMTGFMKRQIGELSGGQLQRVFIARALAQHAEIFFLDEPFAGIDMTSEALIMRLLKKLRDNGKTIVVVHHDFHKVAAYFDDIILLNKKLVAHGPVEQTFTEEKIQFAYGDAPVAFAAGV", "text": "FUNCTION: This protein is probably a component of a manganese permease, a binding protein-dependent, ATP-driven transport system. Probably responsible for energy coupling to the transport system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "KKYSCLEGETHKLKPSPEPNMQECTLYSGSSCCYA", "text": "FUNCTION: Required for the transport of riboflavin to the developing oocyte. SIMILARITY: Belongs to the folate receptor family."}
{"protein": "LHMIHLHWYQYPPMNPMMYPLLLIFMLFTGILCLAGNFVTIWVFMNTKSLRTPANLLVVNLAMSDFLMMFTMFPPMMVTCYYHTWTLGPTFCQVYGFLGNLCGCASIWTMVFITFDRYNVIVKGVAGEPLSTKKASLWILIVWVLSLAWCMAPFFGWNRYVPEGNLTGCGTDYLSEDILSRSYLYIYSTWVYFLPLTITIYCYVFIIKAVAAHEKGMRDQAKKMGIKSLRNEEAQKTSAECRLAKIAMTTVALWFIAWTPYLLINWVGMFARSYLSPVYTIWGYVFAKANAVYNPIVYAIS", "text": "FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Can use both retinal and 3-dehydroretinal as visual pigment. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Signaling via GNAQ probably mediates the activation of phospholipase C. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Note=Detected on the rhabdomere membrane in the photoreceptor outer segment. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MVYHWRGDLGSWRLLLLLLLLAAWKVGSGQLHYSVPEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKRHRDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVDVEVKDVNDNPPVFRVKEQKLFVSESRMPDSRFPLEGASDADVGANSVLTYRLSFHDYFMLDVNSKNDENKLVELVLRKSLDREDAPAHDLFLTATDGGKPELTGTVQLLVTVLDVNDNAPNFEQSEYEVRIFENADNGTTVIKLNASDRDEGANGAISYSFNSLVETMVIDHFSIDRNTGEIVIRGNLDFEQENFYKIRIDATDKGHPPMAGHCTVLVRILDKNDNVPEIALTSLSLPVREDAQFGTVIALISVNDLDSGANGQVTCSLMPHVPFKLVSTFKNYYSLVLDSALDRESVSAYELVVTARDGGSPSLWATASLSVEVADVNDNAPAFAQPEYTVFVKENNPPGCHIFTVSARDADAQENALVSYSLVERRVGERSLSSYVSVHTESGKVYALQPLDHEELELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLEPRVGGTGGSASELVPRSVGAGHVVAKVRAVDADSGYNAWLSYELQPAASSPRIPFRVGLYTGEISTTRVLDEADSPRHRLLVLVKDHGEPALTATATVLVSLVESGQAPKASSRQSAGVVGPEAALVDVNVYLIIAICAVSSLLVLTLLLYTALRCSALPTEGGCRAGKPTLVCSSAVGSWSYSQQQSQRVCSGEGPPKTDLMAFSPCLPPDLGSVDVGEERDLNVDHGLKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ", "text": "FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MDNKKYKRACVMVRNIKISVVKVRRILDHVRKYSLRNALMLLEFLPYKGSLVIYKAIKSSYFNYKNFWDFNVTLDNLYITKAKADSGPMLKRSCPHSRGKAFPIRKRTCHITSMI", "text": "FUNCTION: This protein binds specifically to 23S rRNA. FUNCTION: The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uL22 family."}
{"protein": "MGAAASIQTTVNTLSERISSKLEQEANASAQTKCDIEIGNFYIRQNHGCNLTVKNMCSADADAQLDAVLSAATETYSGLTPEQKAYVPAMFTAALNIQTSVNTVVRDFENYVKQTCNSSAVVDNKLKIQNVIIDECYGAPGSPTNLEFINTGSSKGNCAIKALMQLTTKATTQIAPRQVAGTGVQFYMIVIGVIILAALFMYYAKRMLFTSTNDKIKLILANKENVHWTTYMDTFFRTSPMVIATTDIQN", "text": "FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Note=Localizes to the membrane surrounding the core of mature virus particles (MV). SIMILARITY: Belongs to the orthopoxvirus OPG095 family."}
{"protein": "TDPDADEGEFLAEGGGVR", "text": "FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTVQNEPSAKTHGVILTEAAAAKAKSLLDQEGRDDLALRIAVQPGGCAGLRYNLFFDDRTLDGDQTAEFGGVRLIVDRMSAPYVEGASIDFVDTIEKQGFTIDNPNATGSCACGDSFN", "text": "SIMILARITY: Belongs to the HesB/IscA family."}
{"protein": "MLRREARLRREYLYRKAREEAERTAQERKDKVRRALEENRLIPTELRREALALQGSLEFDDAGGEGVTNHVDDEYRWAGVEDPKVMITTSRDPSSRLKMFAKELKLVFPGAQRMNRGRHEVGALVRACKANGVTDLLVVHEHRGTPVGLIVSHLPFGPTAYFTLCNVVMRHDIPDLGTASEAKPHLIMHGFSSRLGKRVSDILRYLFPVPKDDSRRVITFANQDDYISFRHHVYKKTNHRNVELTEVGPRFELKLYMIRLGTLEQEATADVEWRWHPYTNTAHKRVFLSAE", "text": "FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
{"protein": "MAWNTNLRGRLPITCLILQVTMVVLFGVFVRYDIQADAHWWLEKKRKNISSDVENEFYYRYPSFQDVHAMVFVGFGFLMTFLQRYGFSAVGFNFLLAAFGIQWALLMQGWFHYFEEGHIVLSVENIIQADFCVASSCVAFGAVLGKVSPMQLLIMTFFQVTLFTVNEFILLNLIEAKDAGGSMTIHTFGAYFGLTVTWILYRKNLDQSKQRQSSVYHSDLFAMIGTLFLWIYWPSFNSASSFHGDAQHRAALNTYLSLAASVLTTVTVSSIVHKKGKLDMVHIQNATLAGGVGVGTAAEMMLTPYGALIVGFFCGIFSTLGFAYLTPFLESRHRIQDTCGIHNLHGIPGIIGGIVGAVTAAYSSPDVYGEPGIVHSFGFGSYKMDWNKRMQGRSQIFGLLLSLAMALVGGIIVGFILKLPFWGQAADENCFEDSIYWEVHEEVNTVYIPEDLAHKHSTSLVPAMPLVLPTTSASIVPPVPPTPPVSLATSAPSAALVH", "text": "FUNCTION: Ammonium transporter involved in the maintenance of acid-base homeostasis. Transports ammonium and its related derivative methylammonium across the plasma membrane of epithelial cells likely contributing to renal transepithelial ammonia transport and ammonia metabolism. Postulated to primarily mediate an electroneutral bidirectional transport of NH3 ammonia species according to a mechanism that implies interaction of an NH4(+) ion with acidic residues of the pore entry followed by dissociation of NH4(+) into NH3 and H(+). As a result NH3 transits through the central pore and is protonated on the extracellular side reforming NH4(+) (PubMed:16131648) (By similarity). May act as a CO2 channel providing for renal acid secretion (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=Also detected at the basolateral membrane and in subapical vesicles. SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily."}
{"protein": "MDEATGETETQDFMNVESFSQLPFIRRPKDKNPKPIRVFGKDFTGRDFSITTGQEDYTDPYQTKNKEEEEEEDQTGDNSTDNNSISHNRRFECHYCFRNFPTSQALGGHQNAHKRERQLAKRGVSSYFYHPDNNPYSYRHYPSWTNGPLTAARSYGGFSSGPKPSGYYTRPSYGSQLGLWRLPPRVQGVYNSNAAFTSNGSSSSSNSTLPLLTRSQTQLSSQVGGSAAQNRMSSYGYGLSPNVQDHVSLDLHL", "text": "FUNCTION: Probable transcription factor required for the initiation of inflorescence trichomes in response to gibberellin (GA) (PubMed:16679458, PubMed:17507408). Mediates the induction of GL1 expression by GA in inflorescence organs and is antagonized in its action by the DELLA repressor GAI. Acts upstream of the trichome initiation regulators GL1 and GL3, and downstream of the GA signaling repressor SPINDLY (SPY) (PubMed:16679458). Does not play a significant role in the cytokinin response (PubMed:17507408). Controls trichome branching through GA signaling (PubMed:22210898, PubMed:23825141). Acts downstream of the key regulator STICHEL (STI) in an endoreduplication- independent pathway (PubMed:22210898). Controls trichome cell division indirectly by acting downstream of a key endoreduplication regulator SIAMESE (SIM) (PubMed:23825141). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSPSLQEGAQLGESKPSTCSFSIERILGLDQNKDCVPLMKPHRPWADTCSSSGKDGNLCLHVPNPPSGISFPSVVDHPMPEERALKYENYFSASERLSLKRELSWYRGRRPRTAFTQNQIEVLENVFRVNCYPGIDIREDLAQKLNLEEDRIQIWFQNRRAKLKRSHRESQFLMAKKNFNTNLLE", "text": "FUNCTION: Required for the normal development of the forebrain, eyes and other anterior structures such as the olfactory placodes and pituitary gland. Possible transcriptional repressor. Binds to the palindromic PIII sequence, 5'-AGCTTGAGTCTAATTGAATTAACTGTAC-3'. HESX1 and PROP1 bind as heterodimers on this palindromic site, and, in vitro, HESX1 can antagonize PROP1 activation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ANF homeobox family."}
{"protein": "MAGWSCLVTGGGGFLGQRIICLLVEEKDLQEIRVLDKVFRPEVREEFSKLQSKIKLTLLEGDILDEQCLKGACQGTSVVIHTASVIDVRNAVPRETIMNVNVKGTQLLLEACVQASVPVFIHTSTIEVAGPNSYREIIQDGREEEHHESAWSSPYPYSKKLAEKAVLGANGWALKNGGTLYTCALRPMYIYGEGSPFLSAYMHGALNNNGILTNHCKFSRVNPVYVGNVAWAHILALRALRDPKKVPNIQGQFYYISDDTPHQSYDDLNYTLSKEWGFCLDSRMSLPISLQYWLAFLLEIVSFLLSPIYKYNPCFNRHLVTLSNSVFTFSYKKAQRDLGYEPLYTWEEAKQKTKEWIGSLVKQHKETLKTKIH", "text": "FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the 3-beta-HSD family."}
{"protein": "MGPGFQDAYHAFHTAQDERQLFRQIASVVRQLGFDYCCYGIRVPLPVSKPAVAIFDTYPAGWMEHYQASGFLEIDPTVRTGASSSDLIIWPVSIRDEAARLWSDARDFGLNIGVARSSWTAHGAFGLLTLARRADPLTAAELEQLSATTNWLANLAHALMSPFLMPKLVPESSAALTAREREVLCWTGEGKTAYEIGQILRISERTVNFHVNNVLLKLAATNKVQAVVKAIAIGLI", "text": "SIMILARITY: Belongs to the autoinducer-regulated transcriptional regulatory protein family."}
{"protein": "MPAFFEGEFWQIANPELWVGVGLILFIAIVIWAKAPAMIAGKLDETAAKIQTDLDEAARIRAEAEALLATIRAEREETERQAIAMLAAAKADVAQMEIEAKAKLEDQIKRRAEMAERKIAQSEAQAQADVKAAAVDLAAQIAEQVLMARLAAGGSDGLVDTAIGQIGAKLQ", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MRIGVGVSTAPDVRRAAAEAAAHAREELAGGTPALAVLLGSRSHTDQAVDLLAAVQASVEPAALIGCVAQGIVAGRHELENEPAVAVWLASGPPAETFHLDFVRTGSGALITGYRFDRTAHDLHLLLPDPYSFPSNLLIEHLNTDLPGTTVVGGVVSGGRRRGDTRLFRDRDVLTSGLVGVRLPGAHSVSVVSQGCRPIGEPYIVTGADGAVITELGGRPPLHRLREIVLGMAPDEQELVSRGLQIGIVVDEHLAVPGQGDFLIRGLLGADPTTGAIGIGEVVEVGATVQFQVRDAAAADKDLRLAVERAAAELPGPPVGGLLFTCNGRGRRMFGVTDHDASTIEDLLGGIPLAGFFAAGEIGPVAGHNALHGFTASMALFVD", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.tuberculosis Rv0874c."}
{"protein": "MSDGVKHINSAQEFANLLNTTQYVVADFYADWCGPCKAIAPMYAQFAKTFSIPNFLAFAKINVDSVQQVAQHYRVSAMPTFLFFKNGKQVAVNGSVMIQGADVNSLRAAAEKMGRLAKEKAAAAGSS", "text": "FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. SIMILARITY: Belongs to the thioredoxin family."}
{"protein": "MFDTKKVLELANKDFEKAWITTKDLIKDAPINKKYPRIKPSFGKTNPVMDTIEQLRQAYLRMGFEEYINPVIVDEKDIYKQFGPEAMAVLDRCFYLAGLPRPDIGLSNDKIEQIEKLGIKIDSNEKKENLRKTLHLYKKGVLEGDDLVYEIANSLGLSNEMGLKILEEVFPEFKNLKAESLPLTLRSHMTSGWFITISEMMGKKPLPYALFSIDRCFRREQKEDKSHLMTYHSASCVLVGEDITLDDGKAIAEGLLSQFGFTDFQFRPDEKKSKYYTPETQTEVYAYHPKLKEWLEVATFGIYSPIALSKYNISVPVMNLGLGVERLAMINHNYEDVRKMVYPQFYEQTLSDRDIAYSIKVDKVPVLDELKDLTGELIELCVKNKDKQSPCEVFIEKKIKFYNTTKTIKITLFEKEEGKNLLGPSILNKIFVHNGNIFGVPESFDNVKEEFVKVLSEAKNKGAPTNLTYIDTICYKITSKIEEALISNTKKLKIRAPIVRSLSDVNLKIDELALKQIMGNNKVIDIRGPVFLNVKCEIND", "text": "FUNCTION: Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys). SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. O-phosphoseryl-tRNA(Cys) synthetase subfamily."}
{"protein": "MKIGAQVWRALAKSCLLCATLGCLHFPGSRGGKPDFFETKAVNGSLVKSRPVRSVAEAPAPIDCELSTWSSWTACDPCQKKRYRHTYLLRPSQFYGELCDLSDKEVEDCVTNQPCRSQVRCEGFVCAQTGRCVNRRLLCNGDNDCGDQSDEANCRRIYKNCQREMEQYWAIDRLASGINLFTNTFEGPVLDHRYYAGGCSPHYILDTNFRKPYNVESYTPQTKCEYEFTLTEYESYSDFERLVIEKKTHMFNFTSGFKVDGVMDLGIKVESNEGKNYVTRTKRFAHTQSKFLHARSVLEVAHYKLKSRSLMLHYEFLQRVKSLPLEYSYGEYRDLLRDFGTHFITEAVLGGIYEYTLIMNKDAMEQGDYTLSHVTACAGGSFGIGGMVYKVYVKVGVSAKKCSDIMKEINERNKRSTMVEDLVVLVRGGTSEDITALAYKELPTPELMEAWGDAVKYNPAIIKIKAEPLYELVTATDFAYSSTVKQNLKKALEEFQSEVSSCRCAPCRGNGVPVLKGSRCECICPGGFQGTACEVTYRKDIPIDGKWSCWSDWSACSGGHKTRHRQCNNPAPHKGGSPCSGPASETLNC", "text": "FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the complement C6/C7/C8/C9 family."}
{"protein": "MINQTYRLVSARQFEVTYKDKVVHSDKVVVRPTHLSICAADQRYYTGSRGKEAMDKKLPMALIHEGIGKVMFDPTGTFKVGTRVVMVPNTPVEEHEVIAENYLRSSRFRSSGYDGFMQDYMFMAPDRLVELPDSINPHVAAFTELITIAVHALSRFERMAHKKRDTFGVWGDGNLGFIMTLLLKKKYPDSKVFIFGKTPYKLDHFSFVDAAYQINDIPEDVRLDHAFECVGGRGSESAIEQIIAHVHPEACVALLGVSEYPVEIETRMVLEKGITLIGSSRSGREDFARTVDFLAQYPEVVDYLETLVGGRFPVRSIEEITNAFEADLTSSWGKTVIEWEI", "text": "FUNCTION: Catalyzes the NADPH dependent reduction of D-ribulose 5- phosphate to D-ribitol 5-phosphate. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MSVGMAAPRAAFACDPDASRGRLFDELPSKTRSPFRRDCDRVIHSTGFRRLKHKTQVFVYHEGDHYRTRLTHSLEVAQIARAIARQLGLDEDLTEALALAHDLGHPPFGHAGERALDACLQRYGGFDHNAQSLRVVTALEHRYPEFNGLNLTWETLEGIVKHNGPLTDRSGAPLGRYQAHGVPTGIVEFNRCFDLELWSHASLEAQVAGIADDIAYDAHDIDDGLRAGLFGVDDLGEMPLTAQMTAAIDVRYPGLDPARRGAELVRELISFLIGAAVAEAERRLIAAQPASVQAVREAGQDLIMFAPDAAEAEALIKAFLKRHMYRHPRVMRVMDDAETVVFELFARYRDHPADLPAEWLPANAGQGETEADRLRRICNFIAGMTDRYALTEHQRLFDLTPELR", "text": "SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily."}
{"protein": "EDLPHVDAATNPIAQSLHYIEDANASERNPVTKTELPGSEQFCHNCSFIQADSGAWRPCTLYPGYTVSEDGWCLSWAHKTA", "text": "FUNCTION: Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP) family."}
{"protein": "MAEAALEAVRRALQEFPAAARDLNVPRVVPYLDEPPSPLCFYRDWVCPNRPCIIRNALQHWPALQKWSLSYLRATVGSTEVSVAVTPDGYADAVRGDRFVMPAERRLPISHVLDVLEGRAQHPGVLYVQKQCSNLPTELPQLLSDIESHVPWASESLGKMPDAVNFWLGDASAVTSLHKDHYENLYCVVSGEKHFLLHPPSDRPFIPYNLYTPATYQLTEEGTFRVVDEEAMEKVPWIPLDPLAPDLTQYPSYSQAQALHCTVRAGEMLYLPALWFHHVQQSHGCIAVNFWYDMEYDLKYSYFQLMDTLTRATGLD", "text": "FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase (PubMed:28847961) (By similarity). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery. Acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys- 21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MKFLSTAAALLVCLAPVSTTARSLDFFKSSQSPIQAQAKSVPGNNPLEYCNDPSGDILDIKQVDLSPNPPLPGKTLAITASGTLREKIEDGAYVLLEVKYGLITLVRQTADLCEQLVNVELKCPLGPGDMTLTKQVDLPKQIPPGKYTVQADVFNSDGEHITCLKALNIEFKGPF", "text": "FUNCTION: Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle Golgi apparatus Note=Also associated with Golgi-like vesicles. SIMILARITY: Belongs to the NPC2 family."}
{"protein": "MKKKEIKQLKNEIKIALLNSDVETLSHIGKEGHGFLMKSLRKSVWVSLCGLSCRHRMECLSRSTSQSSYADQNQVHLDSERSFFQYKLNPFLLRKHRSQLTKLLSVVFKHYPELCYYQGLHDIAQILLLTLPFSHALPLMEHLVFYRLRDFMLPTLDGTVKQLQLILAVIKARDPTLYEYLIKADIQCYFALSWLITWFAHDVSDISVVCRLFDFFISSHPLTVVYTCAQVVLDNRTSIIELLWDNSGADLLHSYLCKLPASINVNQLIKNTCATISAVPFSSLPLDRYQISPYSCLRNTGDPWEYMSRSNGLLLFRLQLAELQEEKHKPGTKVPAVFLQENIFNGCNMLAAITVIGIGIVASQLIPKSTSNS", "text": "FUNCTION: Has a role in vesicular trafficking and septation during cytokinesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein."}
{"protein": "MKILLEELPHQEESLKAILENFTGIDNAANDSDVDYVYANPLIRGRYNEISNIDVKMETGTGKTYVYTRLMYEMHQQYGIFKFVIVVPSPAIKEGAKNFIQSDYAKQHFSQFYENVRIELNVINAGDFKSKSGRRNFPAQLLNFVEGSRQNSNTIEVLLINADMLRSKSMRNNDYDQTLIGGTTSPIEAIQDTRPVVIIDEPHRFPRDKANYQSIEAIKPQVIIRFGATFPEVTTGKGSNKITKKDYYRKKPQFDLNAIESFNNGLVKGIDIYYPNLTEEQAKNRYVVDSVKAKELVLKQNSKSWILHVGDNLAEVDSGFEGDIEYAGSKMLSNELELEKGMTLIPGTYRSTYQELIIKDAIDKHFEIEQANFLRANQRENNVPRIKTLSLFFIDSITSYRQDDGWLKATFERLLKEKLSRLVAEYEFKRLPREKEYLEFLRATQSSLASDNQNVHAGYFGEDRGSGDESIQAEVDDILKNKEKLLSFKDENGNWQTRRFLFSKWTLREGWDNPNVFVIAKLRTSGSDNSKIQEVGRGLRLPVDETGHRIQQDEWPTRLAFLIGYDEKDFAQKLIGEINSDAKLQLNEEKLTEDMIQLIVTKRKKVNPEFTDERLLEHLDNLGIINRKNEFKESIDIGGVQKSGFEWLVELYPELNTNRLREGKVIDTKKHSIKVRVKLRKENWEKVKELWQQFSNRYMLEFQRIPETISFMAEQIVGNHSLYEREVPMQMKESLHASDDNESVVLREQENEYQRIYLPGMAYGKFVKRINIATGIPIKEIHANLFKLMKSSLKGDARYLSELSLNNIIREFKKRFDEIFAQAYEYKKLDFQARTAIYNPEMDSFVDDINAEVIGVNIDEQAQEDNRYLYELPPMRYDSVTPERDLLRHGYNDKVTVFGKLPRRAIQVPKYTGGSTTPDFIYMIEKDNDSSVYVLVETKAENMRLEDQRIIDIQKKFFDTLKEHHIEFIEATSAQQVYSIIRKLSEE", "text": "FUNCTION: A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CGAAG-3' and cleaves 25-27 base pairs downstream. After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs. DNA restriction requires both the Res and Mod subunits (By similarity). SIMILARITY: Belongs to the type III restriction-modification system Res protein family."}
{"protein": "HSHSEVSQISGEWYSVLLASDHREKIEYNGSMRVFVEYIH", "text": "FUNCTION: Binds the chemical odorant, 2-isobutyl-3-methoxypyrazine. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MPEIHLGAHTIRSHGVTVARFHMHDWLILLLLIVIEIVLNVIEPFHRFVGEDMLTDLRYPLQDNTIPFWAVPLIAVVLPFAVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIGIFHNVTKNVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQFFPPPYDPDGWGPHAYFQMLADSRNDVQDSAGMNHLSVRQTELESVR", "text": "FUNCTION: May play a general 'housekeeping role' in lipid metabolism. Exhibits both diacylglycerol pyrophosphate (DGPP) phosphatase and phosphatidate (PA) phosphatase activities with no preference for either substrate. May play a role downstream of the ABA signaling pathway during seed germination and in stomatal movement in leaves. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
{"protein": "MTVRLLLASASPRRRELLSQIGVAFEVKPSAFEERMDPALPPEQLVVQNALGKALNVQKRAPAELILGADTVVVFNRRIYGKPTGPADAGRMLGELQGQWHTVYTGIALVEERRWRVAERATRVKLRAMTPAQIAAYVAGGEPLDKAGSYAIQGLGAALVEQIDGCYSNVVGLSLPLLVDLLAEFDRRVF", "text": "FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Maf family. YhdE subfamily."}
{"protein": "MDTSRVYGNVKTFRSPGHKQASFPSLSTDACRCPHWHHLALKLGCATLILLLLTLIGLSVFVRFLVQKPLIEKCSMAAQENGTEPTGRSAILECPRHWQPHRNKCLIISQISRPWAEGLVACSMKEATLLIIENEEELKFVQNILKGRQQLFFIGLNYVQTEMTWKWINGSVLKPNILRITGSEVENSCALISHTEVFSDSCSSDNHWICQKTLKHV", "text": "FUNCTION: Binds CLEC2I/Clr-g leading to activation of natural killer cells or stimulation of IL-2 production and proliferation of T-cells in response to antigen stimulation. May contribute to the formation of the immunological synapse between T-cells and antigen-presenting dendritic cells (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein."}
{"protein": "MRARYMLGFGVLCLLTWAVYVSESSPTDKQAKLRLMSVRRARQNKSRQGQIIKTRASSTWINDKRQQMQGDEGVQFRRNVQSRKVLAQRRPAQGGTRNPIQQDDGTPGARARVSRMPSSAGSPNLLASFAGKNRLLVISAPHDSDGYYRLMMSLLKPEVYCELAERHVHQIVMFHQEGELGGKIRRITNEGKVMEEPLDTALIPRLMTFLKLEKGKFGMVLLKKTLQVEERYPYPVRLEAMYEVIDQSPMRKMEKVRQKGFVQKCKGAGVEGQVVEGVLTTDSQVDPPTERRKEIRKPIRRPTTTTTPAPTRPTTTTTTTKATTTTTTRPPTTTRSTTTTTTTTTTTTRPTTTTTRTTTTPRTTRANTTPQWIPAHKTTAEPYYYNRRDRYQTTSPPTDSARYRDNHTSKKEYNHRHTNTIPTQHKPTKVRPTKKKNGDKDISNAYEEKYDVGVPTDAYPEEKEEEIVPTKRGKGKTDKKKKKDKTDKLSKKDKAERRGKDGKGGKKNGKKVPKILEKEDYQKPTKRPPPPPPPKGTLATFLDYFESRRRLILITSPTEENSMYIQQRDEYLEHVCEMAIRKVTIITIFGTFRNSTMKIDHYQLEKDKPMKGLRQEDLENQDLIMELRKEYGMTYNDFYVVLTDLDMKAKQYYEVPIAMKAVFDYIDTFSSRIREMEQQKRDGVTCKKEDKPRSLENFLSRFRWRRRLFVISAPNDEEWAYQQQLYALTSQACNLGLRHVSVLKLVGTDLLDMGGVLELYPINGSATVEREGISATLVRDIRNYFQISPEYFSMLLVGKDGNVKSWYPSPMWSMAIIYDLIDSMQLRRQEMAIQQSLGMRCPEDEYGGYGYHHHEGYQEGYHQGYGY", "text": "FUNCTION: Promotes cell adhesion and matrix assembly. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the CCDC80 family."}
{"protein": "MRILPEPRGSVPCLLLLVSVLLSATLSLARVVEVVGYAESKIKTPHAFSGLRVTIDCKVNKGHFVTKGSGNIDDKGKFGLNIPHDIVSDNGALKEECYAQLHSAAGTPCPAHDGLESTKIVFLSKSGDKHILGLKQNLKFSPEICVSKFFWPMPKLPPFKGFDHPFPLPPPLELPPFLKKPCPPKYSPPVEVPPPVPVYEPPPKKEIPPPVPVYDPPPKKEVPPPVPVYKPPPKVELPPPIPKKPCPPKPPKIEHPPPVPVYKPPPKIEKPPPVPVYKPPPKIEHPPPVPVHKLPKKPCPPKKVDPPPVPVHKPPTKKPCPPKKVDPPPVPVHKPPPKIVIPPPKIEHPPPVPVYKPPPKIEHPPIYIPPIVKKPCPPPVPIYKPPVVIPKKPCPPPVPVYKPPVVVIPKKPCPPLPQLPPLPKFPPLPPKYIHHPKFGKWPPLPPHP", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the plant proline-rich protein superfamily."}
{"protein": "MYRALRLLARSRRLLRVPSAGAAVSGEATTLPRCAPNVARMASQNSFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYGLDPKIASAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK", "text": "FUNCTION: [Isoform Mitochondrial]: Catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH. FUNCTION: [Isoform Cytoplasmic]: Catalyzes the dehydration of L-malate to fumarate (PubMed:23643539). Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by- product of the urea cycle and amino-acid catabolism (PubMed:23643539). Also plays a role in DNA repair by promoting non-homologous end-joining (NHEJ) (By similarity). In response to DNA damage and phosphorylation by PRKDC, translocates to the nucleus and accumulates at DNA double- strand breaks (DSBs): acts by catalyzing formation of fumarate, an inhibitor of KDM2B histone demethylase activity, resulting in enhanced dimethylation of histone H3 'Lys-36' (H3K36me2) (By similarity). FUNCTION: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (PubMed:23643539). Experiments in different species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable). SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol Nucleus Chromosome Note=Translocates to the nucleus in response to DNA damage: localizes to DNA double-strand breaks (DSBs) following phosphorylation by PRKDC. SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase subfamily."}
{"protein": "MKIAIYSTKSYDRKYIELINAKYNFDLEFFDFMLNESTVRLAEHCEVVCIFVNDNGSRKVLEKLAALGVKIVALRCAGFNNVDLKAAQELGIQVVRVPAYSPEAVAEHTIGLMMTLNRRIHRAYQRTREANFSLEGLIGFNMYGRTVGVIGTGKIGIAVMRILKGFGMNILAYDPFKNPVVEELGGQYVELDELYAKSHVITLHCPATPENYHLLNCEAFAKMKDGVMIVNTSRGSLIDTQAAIDALKQRKIGALGMDVYENERDLFFEDKSNEVIQDDIFRRLSSCHNVLLTGHQAFLTEEALTNIADVTLSNIYKLKSGKVCENIVLPS", "text": "SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family."}
{"protein": "MAFKYQLLLSAAVMLAILVATATSFGDSCAPGDALPHNPLRACRTYVVSQICHQGPRLLTSDMKRRCCDELSAIPAYCRCEALRIIMQGVVTWQGAFEGAYFKDSPNCPRERQTSYAANLVTPQECNLGTIHGSAYCPELQPGYGVVL", "text": "FUNCTION: Inhibits trypsin in vitro. Probably plays a protective role through inhibition of insect midgut proteases. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha- amylase inhibitor) family."}
{"protein": "MSDLNQSKKMNVSEFADAQRSHYTVYPSLPQSNKNDKHIPFVKLLSGKESEVNVEKRWELYHQLHSHFHDQVDHIIDNIEADLKAEISDLLYSETTQKRRCFNTIFLLGSDSTTKIELKDESSRYNVLIELTPKESPNVRMMLRRSMYKLYSAADAEEHPTIKYEDINDEDGDFTEQNNDVSYDLSLVENFKRLFGKDLAMVFNFKDVDSINFNTLDNFIILLKSAFKYDHVKISLIFNINTNLSNIEKNLRQSTIRLLKRNYHKLDVSSNKGFKYGNQIFQSFLDTVDGKLNLSDRFVEFILSKMANNTNHNLQLLTKMLDYSLMSYFFQNAFSVFIDPVNVDFLNDDYLKILSRCPTFMFFVEGLIKQHAPADEILSLLTNKNRGLEEFFVEFLVRENPINGHAKFVARFLEEELNITNFNLIELYHNLLIGKLDSYLDRWSACKEYKDRLHFEPIDTIFQELFTLDNRSGLLTQSIFPSYKSNIEDNLLSWEQVLPSLDKENYDTLSGDLDKIMAPVLGQLFKLYREANMTINIYDFYIAFRETLPKEEILNFIRKDPSNTKLLELAETPDAFDKVALILFMQAIFAFENMGLIKFQSTKSYDLVEKCVWRGI", "text": "FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC3 family."}
{"protein": "MNVGVAHSEVNPNTRVMNSRGIWLAYIILVGLLHMVLLSIPFFSIPVVWTLTNVIHNLATYVFLHTVKGTPFETPDQGKARLLTHWEQMDYGLQFTSSRKFLSISPIVLYLLASFYTKYDAAHFLINTASLLSVLLPKLPQFHGVRVFGINKY", "text": "FUNCTION: Negative regulator of sphingolipid synthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ORM family."}
{"protein": "MSKQPRKQRKALYNAPAHARGKHMSATLSKDLRADIGKRSLPIRKGDKVQVLRGDFKGHEGAVLGVDYGSYKITIEEVTLSKPDGTAVFLPVDPSNVMIIDADMDDDRRIKNVTGDN", "text": "FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. FUNCTION: Located at the polypeptide exit tunnel on the outside of the subunit. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
{"protein": "METLANRLDVCQDKMLELYEKDSNKLEDQIMHWQLMRVENALLYKARECGLTHIGHQVVPPLSVTKAKARSAIEVHVALLQLQESAYAQDSWTLRDTSREMWDTVPKKCWKKRGVTVEVRYDGDETKSMCYVHWRDIFTQNYSDDKWVKVAGHVSYEGLYYIHEGEQTFYVKFKDDAYVYGETGKWEVHVGGKVIHHHAFDPVSSTREIPAAGPLCTGDTTKASTETSVGATEGPQQKRQRLETLNWEQQQRQYPQTPSTQTTERASQPLDVTRTSDCDTTCPYTVGHPSDPDCAPVVHLKGDPNCLKCFRYRLHKGKRKLYCKTSSTWRWSCESENQAAFVTIWYTSYSQRNEFLSTVKVPPGIQVILGHMSMFV", "text": "FUNCTION: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the papillomaviridae E2 protein family."}
{"protein": "MVIKFLSALILLLVTTAAQAERIRDLTSVQGVRQNSLIGYGLVVGLDGTGDQTTQTPFTTQTLNNMLSQLGITVPTGTNMQLKNVAAVMVTASLPPFGRQGQTIDVVVSSMGNAKSLRGGTLLMTPLKGVDSQVYALAQGNILVGGAGASAGGSSVQVNQLNGGRITNGAVIERELPSQFGVGNTLNLQLNDEDFSMAQQIADTINRVRGYGSATALDARAIQVRVPSGNSSQVRFLADIQNMQVNVTPQDAKVVINSRTGSVVMNREVTLDSCAVAQGNLSVTVNRQANVSQPDTPFGGGQTVVTPQTQIDLRQSGGSLQSVRSSASLNNVVRALNALGATPMDLMSILQSMQSAGCLRAKLEII", "text": "FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Periplasm Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgI family."}
{"protein": "MAMTVKKDNNEVRIQWRVADIKIPTSEIKNISQDQNIHEVPKLDRDKVSRIGSTFGKTNRVIIDTDDHEYIIYTQNDQKVYNEVTK", "text": "SIMILARITY: Belongs to the UPF0457 family."}
{"protein": "MGVFNYETETTSVIPAARLFKAFILDGDNLFPKVAPQAISSVENIEGNGGPGTIKKISFPEGFPFKYVKDRVDEVDHTNFKYNYSVIEGGPIGDTLEKISNEIKIVATPDGGSILKISNKYHTKGDHEVKAEQVKASKEMGETLLRAVESYLLAHSDAYN", "text": "FUNCTION: May be a general steroid carrier protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the BetVI family."}
{"protein": "MGFDYALVHLKYTIPPAVLLTWLYRPFFTKLDVYKVGYLVSIAVASTIPWDSYLIRTGIWSYPTHVIIGPKLCDIPLEEVFFFIIQTYNTSLLYLLLSRPTFQPVYLNTERGAARRQWRYMRLAGQVFFLALIAWGWRCIRHGGLGTYTGLILVWAGPFLLMLWSLAYQFILALPVTNTALPIFLPTLYLWVVDTLALRRGTWVISTGTKYGLHLWDGLEIEEALFFLATNALIVFGQLAFDNALAVLYTFPHLFTGPSLLPSPVLLMRALLTPCSKYHDARIKGLDEAVNRLKRKSRSFYLASATFPGPLRADLLLLYSFCRVADDLVDNASDADEARAWIAKMRKFLNNVYSDKLPQSVVHSQICDDFPPSTQSALLQLPATKLSPQPLEDLLHGFEMDLAFQQGPIIRTMEDLRVYSERVAGTVAQMCIQLIFYWYPSTLDTEEKNVIVAAGNSMGVALQYVNIARDIEVDAQIGRVYLPLNWLSEAGLSYDDVLKKPNQAQIQTLRKHLLNHAFSVYEKAKDSIERLPIEARGPIRVAVESYMEIGRILRSEQYQVKAGRATVPKSRRIMVAWRTLNSK", "text": "FUNCTION: Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: In the C-terminal section; belongs to the phytoene/squalene synthase family. SIMILARITY: In the N-terminal section; belongs to the lycopene beta- cyclase family."}
{"protein": "MSDFFNSGWSLYVAGITVVSLIFCLVVLIVASRRKVMADDNTTGHVWDEDLQELNNPLPRWWAGLFLVTIAFAVIYLALYPGLGSNKGTLDWTSTGQHSAEMEKARAQMAPLYAKFVSQPAEALAKDPQAMAIGERLFANNCAQCHGADARGSKGFPNLTDNDWLHGGTHDKIKETITGGRVGNMPPMAAAVGTPEDVKNVAQYVLSLSGAPHNEVAAQLGKAKFAVCAACHGPDGKGMQAVGSANLTDKIWLHGLRRTGHHRLINNGKTNIMPAQASRLSPEQIHVLGAYVWSLSQTSTVAAR", "text": "FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. CcoP subunit is required for transferring electrons from donor cytochrome c via its heme groups to CcoO subunit. From there, electrons are shuttled to the catalytic binuclear center of CcoN subunit where oxygen reduction takes place. The complex also functions as a proton pump (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CcoP / FixP family."}
{"protein": "MRDPLTDCSYNKVYKSLKEFAQNGDNFCKQITSVLQQRANLEISYAKGLQKLAVKLSKALQSTKKNCLSTAWAWASESMKSAADLHQKLGKAIELEAIKPTHQVLSMQEKKRKSLDNEVEKSANLVINNWNQQIKAKKKLMMSTKKHEALFHLIESSKQSMTQKEKQKLLNKLKKSTEKLEKEDESYYQKNMAGYSTRLKWESTLEKCYKSMLELEKERIQLLCNNLNQYSQHISLFGQTLTTCHTQIHCAISKVDVEKDIQALMEETAVLSLENKSELLLADYFEEDPKNPMDKERRKSLIKPKLWRLQKDIEKASRDKEGLEQKLKALASSASFSDAKSQKDAETLMDENSLKLDLLQANSYKLSTVLADLEQRPKPCHPCSNCIFKWKEKEHSHSYVKISRPLLTKRLEKAESKAPAGEQNNPSSSRPGSSVSQGNNQLCKALYTFQARQDDELNLEKGDIVTIHEKKEEGWWFGSLNGKKGHFPAAYVEELPPKAGQA", "text": "FUNCTION: Multivalent adapter protein which may decrease NOS3 activity by inducing its translocation away from the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle Cytoplasm, cytoskeleton Cytoplasm Nucleus Note=Enriched in selected actin structures."}
{"protein": "MDSKVSNGSSLQDERITNLLVFGFLQSCPHASFHKELEVLGHELPVHTSGSDELQTDGNRCSYFMEDAAETDSESQEAVIRDIARHLARIGDRMEYGIRPGLVDSLAAQFRNQSLSEEDRRQGLAAVLQQLVHSYPADMGQEKTLLVLTMLLARKVAEHSPALLRDVFHTTVNFINQNLLTYLRNLVQSEMD", "text": "FUNCTION: Induces caspases and apoptosis. Counters the protective effect of BCL2. FUNCTION: [BH3-interacting domain death agonist p15]: Induces caspase activation and apoptosis (By similarity). Allows the release of cytochrome c (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion membrane Mitochondrion outer membrane Note=When uncleaved, it is predominantly cytoplasmic (By similarity). SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p13]: Mitochondrion membrane Note=Associated with the mitochondrial membrane. SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p15]: Mitochondrion membrane Note=Translocates to mitochondria as an integral membrane protein."}
{"protein": "MRPSPALAGGGRTVANLLSATEWMLPSPATQVHTISVLPSHSPPSPPHHFAFSNLTTAPKRNGGKGEEEGRPRFEVVRDDLLHPLANGNKARKLDALLPLLRRRGATDVVTCGGCQSAHAAATAVHCAEWGMRPHILLRGEQPDIPTGYNLISLMFGNVAYASRSVYAHRDEMLYNHARKVAGTGGTVLWADDISKEDFVLDEDNGCEIGSRRVVIIKEGAGDVQALLGVIRLVEYLYNLSSFHKHENVHVVVDAGTGTTAVGLALGAVCLGLHWRVTAVMLADTLERYKEREKSLISDFKKLCHNNYHEMVGENDIGDSLVEWVERFSPRRFGKVLNGEIALCRQIAQQTGILLDPMYTLAGWEQAVDLCVGDSRTKVVMIHTGGTLGFCGLAQRYSSHFTSDEQT", "text": "FUNCTION: Catalyzes the production of hydrogen sulfide (H2S) from cysteine. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase family."}
{"protein": "MYECMFFSHRLTIGFYIPLIVLTTMSSLSESLGERQKTACTVAAISCANSDTYNRTTVSNHTFFYISDRWKYSELIRYEKPTGDLRHDKLIHVDREFLDIVSLLHNNENQLRTLLTIFRSDSAPPWVKFMRGYSQCLDHPIIYTCVEEKCQQYNLEELPYGKDIFLENVVGFDLGAPPHNMSVLIAVSNTKPKITKVLRITSTSLTLFDALYNTVLTFFRSIGARNVDVVRRLILYQASLSGPHRDAPIHNYLNRDLS", "text": "FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH (By similarity). In human cytomegalovirus, forms two distincts complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA. The gH-gL- UL128-UL130-UL131A pentamer is essential for viral entry in epithelial, endothelial and myeloid cells via interaction with host NRP2 (By similarity). SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein; Extracellular side Host cell membrane; Peripheral membrane protein; Extracellular side Host Golgi apparatus, host trans- Golgi network Note=gL associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the host trans- Golgi where secondary envelopment occurs. SIMILARITY: Belongs to the herpesviridae glycoprotein L family."}
{"protein": "MAELKYISGFGNECASEDPRCPGSLPKGQNNPQVCPYNLYAEQLSGSAFTCPRNTNKRSWLYRILPSVSHKPFESIDQGHVTHNWDEVGPDPNQLRWKPFEIPKASEKKVDFVSGLYTLCGAGDIKSNNGLAVHIFLCNSSMENRCFYNSDGDFLIVPQKGKLLIYTEFGKMSLQPNEICVIQRGMRFSVDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPVAWYEDRRVPGGYTVINKFQGKLFACKQDVSPFNVVAWHGNYTPYKYNLENFMVINAVAFDHADPSIFTVLTAKSLRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIKGHYEAKQGGFLPGGGSLHSAMTPHGPDADCFEKASKAKLEPERIADGTMAFMFESSLSLAVTKWGLKTCSCLDENYYKCWEPLRSHFTPNSRSPTEPK", "text": "FUNCTION: Catalyzes the conversion of homogentisate to maleylacetoacetate. SIMILARITY: Belongs to the homogentisate dioxygenase family."}
{"protein": "MSYQGKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIVSAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSDYVYKRIKARRKMADLHAVPRGMYDGPVFDLTTTPKGGTPAGSARGSPTRPNPPVRNLHQSGFSLSGTQVDEGVRSASKRIVAPPGGRSNITSLS", "text": "FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, growth cone Note=Colocalizes with synaptic vesicle protein 2 in the central region of the growth cone. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family."}
{"protein": "MKKLLPLCCWHSWLLLFYCDFQVRGAHTRSHVHPGFEVLASASHYWPLENVDGIHELQETTGASRTHNLTVLPSHNSTFVYTNDSAYSNFSATVDIVEGKVNKGIYLKEGKGVTFLYYRKNKTSCISNPAQCGPEGVSFSFFWKTQGEQSTSIPSAYGGQVISNGFKVCSRGGKGSVELYTHNKSVTWEASFSPPGHYWTHVLFTWKSEEGLKVYVNGTLRTSDPSGKASPAYGESNDNLVLDLTKSYENRAFDEFIIWERALTPDEIAMYFTAAIGEQLSLSSTPPSFSVTPTVNTMAPTNAYHPIITNLTEERKNFRRPGVVLSYLQNMSLSLPNKSLSEETAFNLTKTFLNTVGEVLRLPSWTAVSEDSAVVPGLIDTIDTVMSHITYNLQASKPQVAIVGSSSMADFSVAKVLPKTMNSSHYRFPARGQNYIEIPHEAFHSQAWTTIVGLLYHSVHYYLSNIQPASTKIAEAANYKNCLLSATSYLISLEVSPTPKLSQNLSGSPLITVHLRHHLTQRQYTEATNESNRIFLYCAFLDFSSGEGIWSNQGCALTEGNLSYSICRCTHLTNFAILMQVVPLELTRGHQVALSSISYIGCSLSVLCLAITLVTFAVLSSVSTIRNQRYHIHANLSCAVLVAQVLLLISFRFEPGTAPCQVLAMLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGIGWGFPLLICIISIVFAMDSYGTSKNCWLSLGNGAIWAFVAPALFIIVVNIGILIAVTRVISQISAENYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNNQAMVFQYMFAILNSLQGFFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSSRQANVKPFSSDIMNGTRPATGSTRLSPWDKSSHSGHRVDLSAV", "text": "FUNCTION: Orphan receptor. Signals via G(s)-alpha family of G-proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily."}
{"protein": "MAVNPLDFLKNMSSVKNNIDNIKKEISKITVCGKAGSNIVTIEMDGEFNVKKVSINKEFFDDLDNDAFEQMIKSALNDAVSKVKEEIKLKTMGVLPFGM", "text": "FUNCTION: Binds to DNA and alters its conformation. May be involved in global regulation of gene expression. Binds specifically and non- specifically to DNA, preferentially to the 4 bp broken palindrome 5'- GTnAC-3'. Affects expression of a wide variety of genes, encoding both structural and metabolic proteins. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the YbaB/EbfC family."}
{"protein": "MKKLLLLLILLIFAAKVTAEEWAGADEKAEEVIKELKPDYEPWFSPIFEPPSGEIESMLFSLQAAIGSLIIGYFLGYYRGLKHARNA", "text": "FUNCTION: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiN family."}
{"protein": "MEKNDVINFKALEKELQAALAADEKYKRENAAKLRAVEQRVPSYEEFRGIVLASHLKPLEQKDKMGGKRFVPWNCHTTRERTSQDVVTEIPQEKSPFQPTTSAEFYRDWRRHLRSGPERYQALLQLGGPKLGHLFQMDVGFGLLGELLVALAEHARLSDRTAVLGILHSLANTGRFNLNLSLLSHAERESCQRLFQKLQAMSTTRPMQEGLTVEEPSAGLQGEEGLLQELLELYGVH", "text": "FUNCTION: Dynein-attachment factor required for cilia motility. SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium, flagellum. SIMILARITY: Belongs to the CCDC103/PR46b family."}
{"protein": "MFFKTLKEAFKVKDVRARILFTIFILFVFRLGAHITAPGVNVQNLQQVADLPFLSMMNLVSGNAMQNYSLFAMGVSPYITASIIVQLLQMDILPKFVEWSKQGEIGRRKLNQATRYITLVLAMAQSIGITAGFQAMSSLNIVQNPNWQSYLMIGVLLTTGSMVVTWMGEQINEKGFGSGVSVIIFAGIVSGIPSAIKSVYDEKFLNVRPSEIPMSWIFVIGLILSAIVIIYVTTFVQQAERKVPIQYTKLTQGAPTSSYLPLRVNPAGVIPVIFAGSITTAPATILQFLQRSQGSNVGWLSTLQNALSYTTWTGMLFYALLIVLFTFFYSFVQVNPEKMAENLQKQGSYIPSVRPGKGTEKYVSRLLMRLATVGSLFLGLISIIPIAAQNVWGLPKIVALGGTSLLILIQVAIQAVKQLEGYLLKRKYAGFMDNPLETK", "text": "FUNCTION: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family."}
{"protein": "MAEACRVRRMKLGSQGLEVSAQGLGCMALSARYGAPKPETDAIALLHHAINSGVTFFDTSDMYGPETNELLLGKALKDGVKEKVELATKFGFFIVEGEISEVRGDPEYVRAACEASLKRLDIACIDLYYQHRIDTRVPIEITMRELKKLVEEGKIKYIGLSEASASTIRRAHAVHPITAVQIEWSLWSRDAEEDIIPICRELGIGIVAYSPLGRGFLAAGPKLAENLENDDFRKTLPRFQQENVDHNKILFEKVSAMAEKKGCTPAQLALAWVHHQGDDVCPIPGTTKIENLNQNIRALSVKLTPEEISELDSLAKPESVKGERYMASMSTFKNSNTPPLSSWKAT", "text": "SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto reductase 13 subfamily."}
{"protein": "MGIRAIVVDTAGTTTDLNFIKDTLFTYSAKALPDFLKENETNVLVDNCICDVRDIALEPDASLERVVEILQQWVEEDRKATPLKTLQGLIWKQGYARGEFTGHIFPDFIDTIESIKQQNIRIYSFSSGSAEAQKLLFSHSDGGDLTPHFDGHFDTRTGNKLFKQAYCNIINTISLAPKQVLFISDVIEELKAAEEAGMRTLQMVRSADQRTGNFKQIASFKELTF", "text": "FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3- diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK- MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family."}
{"protein": "MKQQVEVKDLKEGKYVIIDDEACVIKSISKSKPGKHGAAKARVEAIGLFDNQKRSYIGSVANKIYVPIVERKSAQVISITGDIAQLMDMGDFSTFEIVIPDEYKDKVKEGEEVSYITALGKIKLDIRT", "text": "FUNCTION: Functions by promoting the formation of the first peptide bond. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-5A family."}
{"protein": "MAHATSSAYEVKITLPGNLTRDEEDRLRCLTGTILMAPSLRRCLFLHDVDRNSYYVHGSEPDYATSLAAYRRRFPLLVTAVGRQELSAVSLSIGCPKGLNFRNTGPFQLLNGSNVSLIPPIGGRWRVELLSCGSVIEPAMTIPTEVGSELLGKILAGMTYEFCARNQIPADRPAEVYRVACDNKALDLTQAIRGGDSDLQDTMKTLFASVLFAMNEGVLQVMTLMPALLAGGNTNPFLNALLQMQSATRLSAQIFNPPTLPVHDPTGGARRYNVFDAFASWLTMSHRLGELFHMKPALKVVMFYSDVSAIDEGQTANAIVP", "text": "FUNCTION: Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae TRX2 protein family."}
{"protein": "MSLTEEKPIRPIANFPPSIWGDQFLIYEKQVEQGVEQIVNDLKKEVRQLLKEALDIPMKHANLLKLIDEIQRLGIPYHFEREIDHALQCIYETYGDNWNGDRSSLWFRLMRKQGYYVTCDVFNNYKDKNGAFKQSLANDVEGLLELYEATSMRVPGEIILEDALGFTRSRLSIMTKDAFSTNPALFTEIQRALKQPLWKRLPRIEAAQYIPFYQQQDSHNKTLLKLAKLEFNLLQSLHKEELSHVCKWWKAFDIKKNAPCLRDRIVECYFWGLGSGYEPQYSRARVFFTKAVAVITLIDDTYDAYGTYEELKIFTEAVERWSITCLDTLPEYMKPIYKLFMDTYTEMEEFLAKEGRTDLFNCGKEFVKEFVRNLMVEAKWANEGHIPTTEEHDPVVIITGGANLLTTTCYLGMSDIFTKESVEWAVSAPPLFRYSGILGRRLNDLMTHKAEQERKHSSSSLESYMKEYNVNEEYAQTLIYKEVEDVWKDINREYLTTKNIPRPLLMAVIYLCQFLEVQYAGKDNFTRMGDEYKHLIKSLLVYPMSI", "text": "FUNCTION: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:11032404, PubMed:11185551, PubMed:11289612, PubMed:10626375, PubMed:27488942). Catalyzes the formation of both olefinic and oxygenated sesquiterpenes, with amorpha-4,11-diene being the major product (PubMed:11032404, PubMed:11185551, PubMed:11289612, PubMed:10626375). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MEDIEKLLLQEKILMLELDLVRAKISLARAKGSMQQGGNSLHRETPVKEEAVHSALATFAPIQAKAIPEQTAPGKESTNPLMVSILPKDMKSVQTEKKRLVTPMDFLRPNQGIQIPQKSEPNSSVAPNRAESGIQHPHSNYYVVYNGPHAGIYDDWGSAKAATNGVPGVAHKKFATITEARAAADVYTTAQQAERLNFIPKGEAQLKPKSFVKALTSPPKQKAQWLTLGVKKPSSDPAPKEVSFDQETTMDDFLYLYDLGRRFDGEGDDTVFTTDNESISLFNFRKNANPEMIREAYNAGLIRTIYPSNNLQEIKYLPKKVKDAVKKFRTNCIKNTEKDIFLKIKSTIPVWQDQGLLHKPKHVIEIGVSKKIVPKESKAMESKDHSEDLIELATKTGEQFIQSLLRLNDKKKIFVNLVEHDTLVYSKNTKETVSEDQRAIETFQQRVITPNLLGFHCPSICHFIKRTVEKEGGAYKCHHCDKGKAIVQDASADSKVADKEGPPLTTNVEKEDVSTTSSKASG", "text": "FUNCTION: Enhances the ribosomal termination-reinitiation event leading to the translation of major open reading frames on the polycistronic viral RNAs. SUBCELLULAR LOCATION: Host cytoplasm. Note=Found in cytoplasmic occlusion bodies. SIMILARITY: Belongs to the caulimoviridae viroplasmin family."}
{"protein": "MTTPFKRIHLIVMDSVGIGEGPDAAAFNDEGSHTLKHTLEGFKQKLPHLEQLGLGNIAPLPVVSKVTHPGAFYTKLSEASVGKDTMTGHWEIMGLNIMQPFKVYPNGFPEELVKEIESMTGRKVVANRPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQIAAHEDVIPLEELYEICEKVRELTKDPKYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGRTVMNSLKDNGYDVIAIGKINDIYDGEGVTEAIRTKNNMDGMDQLIEVVKKDFEGISFLNLVDFDALYGHRRDKEGYAQAIKDFDLRLPELMNHLREDDLVIITADHGNDPIAKGTDHTREYIPLLMFSPKIKDYHELSQDTTFSSIGVTIADNFNVELPKYGKSYLKEMGVEHQ", "text": "FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of pentose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphopentomutase family."}
{"protein": "MLRRDFLKYSVALGVASALPLWSRAAFAAERPALPIPDLLTADASNRMQLIVKAGQSTFAGKNATTWGYNGNLLGPAVQLHKGKSVTVDIHNQLAEDTTLHWHGLEIPGIVDGGPQGIIPAGGTRTVTFTPEQRAATCWIHPHKHGKTGRQVAMGLAGLVLIEDDEIRKLRLPKQWGIDDVPVIIQDKRFSADGQIDYQLDIMTAAVGWFGDTLLTNGAIYPQHSAPKGWLRLRLLNGCNARSLNIAASDNRPLYVIASDGGLLAEPVKVTELPLLMGERFEVLVDISDGKAFDLVTLPVSQMGMAIAPFDKPHPVMRIQPLRITASGTLPDTLTTMPALPSLEGLTVRNLKLSMDPRLDMMGMQMLMKKYGAQAMSGMDHDSMNAHMQGGNMGHGEMDHGNMDHSGMNHGAMGNMNHGGKFDFHNANFINGQVFDMNKPMFAAQKGRHERWVISGVGDMMLHPFHIHGTQFRILSENGKAPAAHRTGWKDTVRVEGGISEVLVKFDHDAPKEHAYMAHCHLLEHEDTGMMLGFTV", "text": "FUNCTION: Multicopper oxidase involved in copper homeostasis and copper tolerance under both aerobic and anaerobic conditions (PubMed:12442888, PubMed:17768242). Is responsible for the oxidation of Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing Cu(+) from entering the cytoplasm (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MNKKIPKAILSDNERLKVASNFLRGTIAQDLQDNITGGFKGDNIQLIRFHGMYQQDDRDLRVERTCQKLEPLINMMLRCRLPGGIITPQQWLGIDSFATKHTLYGSIRLTTRQTFQFHGVLKPNLKNMHKLLHSLGLDSIATAGDMNRNVLCTSNPVESVLHQQVCNYAKMISEHFLPKTRAYAEIWLDGEKTETTEQEPILGANYLPRKFKISIVVPPLNDVDLHANDLNFIAISNLGQLVGFNVLVGGGLAMTHNDKSTYPRTASELGYISVVDTIKIAEAVITTQRDLGDRSNRKHAKTKYTIERVGVEFFKKEVEVRAGIKFKHIRPYSFTERGDRFGWVQGIDNQWHLTLFIENGRIIDDSHRKLKTGMLEIARIHQGDFRITANQNIIIAGVEKKHKATIELLARQYGLINNNITLQRKASMACVAFPTCPLAMAEAERFLPQFVTKVENIMSRHGLGQEKIILRVTGCPNGCGRAMLAEIGLVGKTIGRYNLYLGGDSIGTRIPRIYRENLTEEEILSIINDTTGRWARERQPDESYGDYVVRAGIIRPVINSALDFHN", "text": "FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family."}
{"protein": "MENFPIINLEKLNGAERVATMEKINDACENWGFFELVNHGIPHEVMDTVEKLTKGHYKKCMEQRFKELVAKKGLEGVEVEVTDMDWESTFFLRHLPSSNISQLPDLDDVYREVMRDFRKRLEKLAEELLDLLCENLGLEKSYLKNTFYGSKGPNFGTKVSNYPPCPKPDLIKGLRAHTDAGGIILLFQDDKVSGLQLLKDGRWIDVPPMRHSIVVNLGDQLEVITNGKYKSVMHRVIAQKDGTRMSLASFYNPGNDALIYPAPALVDKEAEEHNKQVYPKFMFDDYMKLYANLKFQAKEPRFEAMKAMESDPIAIA", "text": "SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MSIQNSSARRRSAGRIVYAAGAVLWRPGSADSEGPVEIAVIHRPRYDDWSLPKGKVDPGETAPVGAVREILEETGHRANLGRRLLTVTYPTDSPFRGVKKVHYWAARSTGGEFTPGSEVDELIWLPVPDAMNKLDYAQDRKVLCRFAKHPADTQTVLVVRHGTAGSKAHFSGDDSKRPLDKRGRAQAEALVPQLLAFGATDVYAADRVRCHQTMEPLAAELNVTIHNEPTLTEESYANNPKRGRHRVLQIVEQVGTPVICTQGKVIPDLITWWCERDGVHPDKSRNRKGSTWVLSLSAGRLVTADHIGGALAANVRA", "text": "FUNCTION: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8- oxo-GTP to 8-oxo-GDP. FUNCTION: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8- oxo-GTP to 8-oxo-GDP (PubMed:23463507, PubMed:16585780). Functions in concert with Rv1700 to detoxify 8-oxo-dGTP to 8-oxo-dGMP and plays an important role in supporting cellular growth under oxidative stress (PubMed:23463507). SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MEVTGRLFIWAILAVSCGAQLNSTEAEGKSRCTASLGGANLGETHKALVLQLSANENCTWTIERPENRSIRIIFSYIKLDPGSRCETENIKVFDGSSTSGPLLGKACSRNDFVPVFESSSNSMTFQIVTGLTKFPRSVFIFYYFFSAATVIPNCGGDLRALEGSFSSPNYPKPHPELAYCVWHIQVGKGYKIQLKFTDLLLEMDENCKFDFIAVYDGPSTTAGLLKQLCGRGKPTLESSSDAMTVVLSTDYANSYKGFSASYTSIYIHDVNTTSLSCVSDKMRVIISKSYLPALNYNESNLQLNDPTCRPNVSNVIEFSIPLHECGTVKKIEDHAISYTNRITFIESPVSAVITRQKLLQIVVTCEMEYNSTVEIMYITEDDIIQNQSVLGKYNTSLALYESDSFENLVQESPYYVDLNQTLFVQATLHTSDPSLVVFLDTCRASPTSDFASPTYDLISSGCCQDETCKVYPLFGHYGRFQFNAFKFLKHLNSVYLKCKILICDNNDQTSRCNQGCVPRRKRDIPSYKWKTDSVIGPIRLKRDRSASRDSGLLPQIHEAEISNQPLSRLYLFSFMVLALNVVIVAITTVKHFLNRWMDHRYQKLQVY", "text": "FUNCTION: Localized to zymogen granules, where it functions in trypsinogen activation (PubMed:12401800). May indirectly regulate cell motility, cell-cell and cell/extracellular matrix interactions (By similarity). SUBCELLULAR LOCATION: Zymogen granule membrane; Single-pass type I membrane protein."}
{"protein": "MRVLALLLAVKAACVLLVSSLTGTGAVNNSGRWWGIVNVASSGNLLTNSKNVQLVLDPSLALLSRRQRKLIRQNPGILHAIAAGLHTAIKECKWQFRNRRWNCPTTHSPNVFGKIVNRGCRETAFVFAITSAGVTHAVARSCSEGAIESCTCDYRRRGPGGPDWHWGGCSDNVEFGRMFGREFVDSSERGRDLRYLTNLHNNEAGRMTVASEMQQECKCHGMSGSCTVRTCWMRLPSFRLVGDYLKDRFDGASRVVYANKGSNRASHRADPRHLEPENPAHKLPSSRDLVYFEKSPNFCSYNGKTGTHGTSGRTCNSSSPALDGCELLCCGRGYKTRMEQVTERCHCTFHWCCHVSCLNCTSTQTVHQCL", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Acts in the canonical Wnt signaling pathway by promoting beta-catenin-dependent transcriptional activation (By similarity). Involved in neurogenesis. Performs a partially redundant function with wnt10b in the formation of the midbrain-hindbrain boundary (MHB) organizer. In the hindbrain, mediates lateral inhibition of boundary cell specification, probably via up-regulation of proneural and Delta gene expression in non-boundary cells; localized expression of wnt1 in boundary cells is maintained via rfng-mediated modulation of Notch activity. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
{"protein": "MAAAQRWLPGILRRGDGLARRLYSSASSLLFDDTQEQFKESVHKFAQETIAPHAAAIDASNHFPKDVNLWKLMGDFNLHGLTAPEEYGGMGLGYMYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRHGSPAQKLKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAEKVDGGYVINGNKMWCTNGPSAQTLVVYAKTDIAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPHENVLGEEGKGVYVMMSGLDLERLVLAAGPIGLMQACLDVAVPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSFVYSVARDCDNGKVDRKDCAGVILFAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLFEIGAGTSEIRRMIIGRELFKEE", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MSRQMGDGHRLFLQNMMTNGIVSAAQAGMLHKKCCELHGGQEKIDDFINVVNTHLQPLFMHIRKGMSEEDGQEHFVLMDLIVESDSGSASSTAILNSADKLISKKLKKKEAELVLNKFVQDKWLKEQDGEYTLSVRCIVEMEPYMRTIYQDMIKVCYVCHNIALQCQVCENPSCEIKVHLPCVARYFRARSDPHCPACNDFWPHEIPEMQAAQSQSSQNLPSSSKENTAPTQTRRSRRV", "text": "FUNCTION: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the NSE1 family."}
{"protein": "MPLSRSLSVSSLPGLEDWEDEFDPENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYYLVGPYTEQGVRTQVELLEPPTPELKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQNEEKPYVVAHFHEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKYLGRYYMSARHMALAKAFPDHFTYEPHEVDATQGYRYPRPASVPPSPSLSRHSSPHQSEDEEEPRDGPLGEDSERYDEEEEAAKDRRNIRAPEWPRRASCSSSTGGSKRSNSVDTGPSSSLSTPTEPLSPTSSLGEERN", "text": "FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. SIMILARITY: Belongs to the glycosyltransferase 3 family."}
{"protein": "MAPRSFPENPYILLTPGPLSTSPTVKAVMMRDWCTWDRDYNAIVQDIRERLVALATAGAGYTSVLMQGSGTFAVEAALGTALPHDGKLLVISNGHYGDRMALIAGYLGMRSAKLDFGETGRPDPDRVRDTIESDPAITHVAVVHCETTTGMLNPVEEIGRAVKSLGRVFIVDAMSSFGGIPMDIATLGADFLISSANKCIQGVPGFGFVIARRSELEQCAGRSRSLSLDLFQQWKEMETKGGKWRFTSPTHVVRAFAQALNELDDEGGVACRNARYRENRRILTAGMRALGFECLLPEALQSPIITSFLTPGRPGFNFNSLYQELKSRGFVIYPGKVSEADTFRIGTIGHVFPEDMHRLVKAAKDAMHRFG", "text": "FUNCTION: Involved in phosphonate degradation. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. PhnW subfamily."}
{"protein": "MVSDAEIKRINELVKKSREEGLTEEEKLEQKALRQKYIDAVKLSLRANLDSIRYVEDLEENKPKQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0291 family."}
{"protein": "MQKGNVWVVDDDSSIRWVLERAITREGMLCRAFEHANDVLKALNSEQPDVLLSDIRMPDMDGLSLLKIIKEQYPTLPVIIMTAHSDLDAAVNAYQQGAFDYLPKPFDIDETLALIERAITHYREQKQPNNAENILQSVSDMIGEAPAMQEVYRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRALAPFIALNMAAIPKDLIESELFGHEKGAFTGASQVRQGRFEQANGGSLFLDEIGDMPLDIQTRLLRVLAEGQFYRVGGYAPVKVDVRIIAATHQDLEKRVNEGDFREDLYHRLNVIRIQLPPLRDRTEDIPSLARYFLQKTAKELGVETKSLHEQSLKTMMEYVWSGNVRQLENVCRWLTVMTASQEIMPQDLPSEIRLADEKAKNINRLTSQHWSQHLSLWADEALGEGKENILNDALPQFERTLLLSALAYTQGHKQDAARLLGWGRNTLTRKLKELGIEDY", "text": "FUNCTION: Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGGEDYYLELCERPVQFEKANPVNCVFFDEANKQVFAVRSGGATGVVVKGPDDRNPISFRMDDRGEVKCIKFSLENKILAVQRTAKAVDFCNFIPDNSQLEYTQECKTKNANILGFCWTSSTEIVFITDQGIEFYQVMPEKRSLKLLKSHNINVNWYTYCPESAVILLSTTVLENVLQPFHFRAGTMSKLPKFEIELPAAPKSTKLSLSERDIAMATIYGQLYILFLRHHSRTSNSTGAEVVLYHLPREGACKKMHILKLNRTGKFALNVVDNLVVVHHQDTETSVIFDIRLRGEFDGTVTFHHPVLPARSIQPYEIPLAGPAAVTSQSPVPCKLYSSSWIVFQPDIIISASQGYLWNLQVKLQPIVNLLPDKGRLMDFLLQRKECKAVVLSVCSQMLSESDRATLPVIATVFDKLNHEYKKYLDADQSYTMAVEAGQSRSNPPLKRPVRTQAVVDQSDVYTQVLSPFVENKEMPHKFVIAVLMEYIRSLNQFQIPVQHYLHELVIKTLVQHNLFYMLHQFLQYHVLSDSKPLACLLLSLESFYPPAHQLSLDMLKRLSTANDEIVEVLLSKHQVLAALRFIRGIGGHDNISARKFLDAARQTDDVMLFYTIFRFFEQRNQRLRGNPNFTPGEHCEEHVAFFKQVFGEQALMRPTTF", "text": "FUNCTION: Componement of the CCZ1-MON1 RAB7A guanine exchange factor (GEF). Acts as a positive regulator of CCZ1-MON1A/B function necessary for endosomal/autophagic flux and efficient RAB7A localization. SUBCELLULAR LOCATION: Lysosome membrane Late endosome membrane. SIMILARITY: Belongs to the RMC1 family."}
{"protein": "MKQGLISIIIPSYNEGYNVKLIHESLKKEFKNIHYDYEIFFINDGSVDDTLQQIKDLAATCSRVKYISFSRNFGKEAAILAGFEHVQGEAVIVMDADLQHPTYLLKEFIKGYEEGYDQVIAQRNRKGDSFVRSLLSSMYYKFINKAVEVDLRDGVGDFRLLSRQAVNALLKLSEGNRFSKGLFCWIGFDQKIVFYENVERKNGTSKWSFSSLFNYGMDGVVSFNHKPLRLCFYTGIFILLLSIIYIIATFVKILTNGISVPGYFTIISAVLFLGGVQLLSLGIIGEYIGRIYYETKKRPHYLIKEANIPNKDLPETNELKSMRRLTKMH", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. GtrB subfamily."}
{"protein": "MKPMYRSRSWRRKYVRTPGGRVVVHFERKKPKIAHCAICGRPLNGIPRGRPVEMRKLPKTKKRPERPMPYLCPRCMRRVMKEQIRSQIMKG", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL34 family."}
{"protein": "MPEIKIFHNPRCSKSRAALSLLEERGIAAEVVKYLDTPPDLSELKDIFNKLGLASARGMMRVKDDLYKELGLDNPNLDNDALLRAIADHPALLERPIVLANGKAAVGRPLENIEAVL", "text": "FUNCTION: Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. SIMILARITY: Belongs to the ArsC family."}
{"protein": "MFLRPTSIPSAVSQIRAQLFAGPSSLASQIQVRWASKAAGGKSKNGRESAGRRLGVKRYGDQYVTPGTIIVRQRGANFHPGQNVAVGKDFTIYALQPGYVKFYQHHLPYPHLSRPDQPGPQNVPSVKRPRQFRQFVGIARDREDKLPRDERAVGRERRFWGWPKEKVEVVPEAAVESAAGIQA", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family."}
{"protein": "MIIRSPEPEVKILVDRDPIKTSFEEWAKPGHFSRTIAKGPETTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQLWRASGITSELQLYCTAIGALVFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLNAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYAEFLTFRGGLDPVTGGLWLTDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSLTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHALAPGATAPGATTSTSLAWGGGDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIVQGRTVGVTHYLLGGIATTWAFFLARIIAVG", "text": "FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family."}
{"protein": "MSIPNSFIIVGSGVFGLSLAYALSLDDRFADKKIILVDRWNFEPPNATGSVHNPAAANADTSRVIRRDYPHGPYASLALEAMKHWRGKFGENNRYVNQRLLFSGEGSSLTTPPKALETVNYIKKAYAISCELTPGGRDAVQVLDSLDEVRAFLGNTPSHPPHLPVNKDPAARDLRGYVSNDCGWADAGASIEWLRQEVLRLGRVECVVGEVESLVYSDDQRAVKGVKLVDGKVLTAELTVIAAGARSSHILGIPKLCDVYSEFVAYIQLTKEEADELRRRQWPILVNCHRGVFAVGPDHDNCLKFGHFSYSGIVDVLREASIQVPTRPDGWEAQQKYWSDPRFAFGGEVKVSALGDVDDYENPAAQRALADYRLFLLELLGPTGLQGVDTLGLDQSDNLLNNIANRPFTRVRKCWYNDTPALDFVVDYHPSYGKTLFVATGGCDHAFKFLPIIGEKTLALILRNRGDSAVSLPAGVEPSLEELSELWRFPVELLQDN", "text": "FUNCTION: Is able to convert N-methyl-3,4-dihydroxy-DL-phenylalanine (N-methyl-DOPA) directly into cyclic isoquinoline, in vitro (PubMed:27065235, PubMed:30194285). The absence of the meta-hydroxyl group, as in L-N-methyl-tyrosine, leads to a 25-fold lower rate of reduction and the formation of the demethylated product L-tyrosine, instead of a cyclic product (PubMed:30194285). Does not accept the D- stereoisomer of N-methyltyrosine, in contrast to N-methyl-DOPA, for which both stereoisomers are oxidized with similar rates (PubMed:30194285). FUNCTION: Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235, PubMed:30194285). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336). The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation (PubMed:27065235). A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2- monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins (PubMed:27065235, PubMed:30194285). FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5- (methylamino)hexanoyl into isoquinoline (PubMed:27065235, PubMed:30194285). The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable). SIMILARITY: Belongs to the MSOX/MTOX family."}
{"protein": "MMKKLLIVSVKAYQKYISPLSPPSCRYKPTCSAYMLTAIEKHGTKGILMGIARILRCHPFVAGGVDPVPEDFSLMRNKNTSKNAEKA", "text": "FUNCTION: Could be involved in insertion of integral membrane proteins into the membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the UPF0161 family."}
{"protein": "MLYIEVLLLAIGLSMDSLAVSVTGGAVLKNNCTAGNIIKIASVLGIFQAGMTVIGYTMGLGFEKYICAFDHWIAFTLLLYLGGKMIYDSTKEEEEDGKFDPLCNRTLCGLGIATSIDALAVGISLAILKSPLLLQASTIGVVTFAISAFGVYFGNRFGKRIDLKLDLIGGLILIGIGTKILIEHLFFS", "text": "FUNCTION: Probably functions as a manganese efflux pump. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MntP (TC 9.B.29) family."}
{"protein": "MVSVQKVPAIALCSGVSLALLHFLCLAACLNESPGQNSKDEKLCPENFTRILDSLLDGYDNRLRPGFGGPVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWIDKRLKYDGPIEILRLNNMMVTKVWTPDTFFRNGKKSVSHNMTAPNKLFRIMRNGTILYTMRLTISAECPMRLVDFPMDGHACPLKFGSYAYPKSEMIYTWTKGPEKSVEVPKESSSLVQYDLIGQTVSSETIKSITGEYIVMTVYFHLRRKMGYFMIQTYIPCIMTVILSQVSFWINKESVPARTVFGITTVLTMTTLSISARHSLPKVSYATAMDWFIAVCFAFVFSALIEFAAVNYFTNIQMQKAKKKISKPPPEVPAAPVLKEKHTETSLQNTHANLNMRKRTNALVHSESDVKSRTEVGNHSSKTSAVQESSEATPKAHLASSPNPFSRANAAETMSAAARGLSSAASPSPHGTLRPASLGSASTRPAFGSRLGRIKTTVNTTGAAGNVSATPPPPAPPPSGSGTSKIDKYARILFPVTFGAFNMVYWVVYLSKDTMEKSESLM", "text": "FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA4 sub- subfamily."}
{"protein": "MPGSSLWLLPPKSHRLNSILPTLIDQTSSHFGSAHRFLPHVTITSEISPSTHSPNPQAWLDSLEISSGDKIEVMFEKLASEDVFFRKLYIKCHKTEGLKKLAVLCRREVEGFGEEREAAKWATESYNPHLSLLYHDCPSIDASGLAEIEKLAQSTGVNLNGQSDLGGWSGGRLVLVPTDKSIDQWSPIAEREL", "text": "FUNCTION: Involved in the metabolism of ADP-ribose 1',2'-cyclic phosphate which is produced as a consequence of tRNA splicing. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CPD1 family."}
{"protein": "MTYRDAGVDIDAGNALVERIKPLVKRSFRPEVMGGLGGFGALFDLSGKYKEPVLVSGTDGVGTKLKLAQQLGRHDTIGIDLVGMCVNDVLVQGAEPLFFLDYFATGKLDIDTAAAVVGGIARGCELSGCALIGGETAEMPDMYPPGEYDLAGFTVGAVEKSQLLDGAQVREGDVLIGIASSGPHSNGYSLIRKIYERAGAPADLVLDDGVALIDALMAPTALYVKPILALLKSHGEAIHAMAHVTGGGLTENIIRVIPDGLGLDIDATAWILPPVFAWLQREGAVADAEMWRTFNCGIGFVLVAAPAQAAALEQALDAQSLAHWRIGQVVTAQGDERVRIG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family."}
{"protein": "MEDQKEALRKIITTLAVKNEEIQSFIYSLKQMLLNVEANSAKVQEDLEAEFQSLFSLLEELKEGMLMKIKQDRASRTYELQNQLAACTRALESSEELLETANQTLLATDSKDFPQAAKQIKDGVTMAPAFRLSLKAKVSDNMSHLMVDFAQERRMLQALTFLPVPSAPVIDLTESLVADNCVTLVWRMPDEDNKIDHFVLEYRRTNFEGPPRLKEDQPWMVIEGIRQTEYTLTGLKFDMKYMNFRVKACNKAVSGEFSEPVTLETPAFMFRLDASTSHQNLRVDDLSVEWDAMGGKVQDIKAREKDGKGRTASPVNSPARGTPSPKRMPSGRGGRDRFTAESYTVLGDTLIDGGEHYWEVRYEPDSKAFGVGVAYRSLGRFEQLGKTAASWCLHVNNWLQVSFTAKHANKAKMLDAPVPDCLGVHCDFHQGLLSFYNGRTKQLLHTFKAKFTQPLLPAFTVWCGSFHVTTGLQVPSSVRCLQKRGSATSSSNTSLT", "text": "FUNCTION: May be involved in microtubule organization and stabilization. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm Cleavage furrow Note=Cell-cycle-dependent association with the centrosome. Colocalizes with a subpopulation of microtubules. Does not associate with microtubules during mitosis but reassociates with microtubules during cytokinesis. Localizes to the central portions of a small subset of microtubules in interphase cells and a subpopulation of microtubules in the cleavage furrow, not present in the mitotic spindle (By similarity)."}
{"protein": "MGKAAAPSRGGGCGGRSRGLSSLFTVVPCLSCHTAAPGMSASTSGSGPEPKPQPQPVPEPERGPLSEQVSEAVSEAVPRSEPVSETTSEPEPGAGQPSELLQGSRPGSESSSGVGAGPFTKAASEPLSRAVGSATFLRPESGSLPALKPLPLLRPGQAKTPLGVPMSGTGTTSSAPLALLPLDSFEGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRGTINLSTAHIDTEDSCGILLTSGARSYHLKASSEVDRQQWITALELAKAKAVRVMNTHSDDSGDDDEATTPADKSELHHTLKNLSLKLDDLSTCNDLIAKHGAALQRSLTELDGLKIPSESGEKLKVVNERATLFRITSNAMINACRDFLELAEIHSRKWQRALQYEQEQRVHLEETIEQLAKQHNSLERAFHSAPGRPANPSKSFIEGSLLTPKGEDSEEDEDTEYFDAMEDSTSFITVITEAKEDSRKAEGSTGTSSVDWSSADNVLDGASLVPKGSSKVKRRVRIPNKPNYSLNLWSIMKNCIGRELSRIPMPVNFNEPLSMLQRLTEDLEYHHLLDKAVHCTSSVEQMCLVAAFSVSSYSTTVHRIAKPFNPMLGETFELDRLDDMGLRSLCEQVSHHPPSAAHYVFSKHGWSLWQEITISSKFRGKYISIMPLGAIHLEFQASGNHYVWRKSTSTVHNIIVGKLWIDQSGDIEIVNHKTNDRCQLKFLPYSYFSKEAARKVTGVVSDSQGKAHYVLSGSWDEQMECSKVMHSSPSSPSSDGKQKTVYQTLSAKLLWKKYPLPENAENMYYFSELALTLNEHEEGVAPTDSRLRPDQRLMEKGRWDEANTEKQRLEEKQRLSRRRRLEACGPGSSCSSEEEKEADAYTPLWFEKRLDPLTGEMACVYKGGYWEAKEKQDWHMCPNIF", "text": "FUNCTION: Binds 7-ketocholesterol. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the OSBP family."}
{"protein": "MRAYWFDNLEGDQRQPHDSGRAVDPAYLSKLGVLYHHISSQSEVDELAKARDYKNRDEITVSPEKMGDIYEEKVKSFFHEHLHEDEEIRYILDGAGYFDVRSEGDDWVRIWLEKGDLIILPSGIYHRFTTDEQNYTKAMRLFKDEPKWTPLNRGEETDENQFRQEYLKLRQGLAA", "text": "FUNCTION: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family."}
{"protein": "MRCPFCHNDDTQVLDTRVSDEGDTIRRRRRCAKCDKRFTTYERVELVLPAIVKKNGSRVEYSHDKLASSLKLALRKRPVSSDSVDESIARIEEKLLSLGEKEIPSERVGELVMRELKRLDKVAYIRFASVYRSFADIESFESALKELK", "text": "FUNCTION: Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR- boxes. SIMILARITY: Belongs to the NrdR family."}
{"protein": "MRLFNWRRQAILHAMPVVKPDQIRTPWREFWRRFRRQHVALVAGGFVLALILVAIFARWLTPYDAENYFDYDSLNNGPSLQHWFGVDSLGRDIFSRVLVGAQISLAAGVFAVFIGAIIGTVLGLLAGYYEGWWDRFIMRICDVLFAFPGILLAIAVVAVLGSGIANVIVAVAIFSIPAFARLVRGNTLVLKQQTFIESARSIGASDTTILFSHILPGTVSSIVVFFTMRIGTSIISAASLSFLGLGAQPPTPEWGAMLNEARADMVIAPHVALFPAVAIFLTVLAFNLLGDGLRDALDPKIKG", "text": "FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family."}
{"protein": "MVKCLLLSFLIIAIFIGVPTAKGDVNFDLSTATAKTYTKFIEDFRATLPFSHKVYDIPLLYSTISDSRRFILLNLTSYAYETISVAIDVTNVYVVAYRTRDVSYFFKESPPEAYNILFKGTRKITLPYTGNYENLQTAAHKIRENIDLGLPALSSAITTLFYYNAQSAPSALLVLIQTTAEAARFKYIERHVAKYVATNFKPNLAIISLENQWSALSKQIFLAQNQGGKFRNPVDLIKPTGERFQVTNVDSDVVKGNIKLLLNSRASTADENFITTMTLLGESVVN", "text": "FUNCTION: Irreversibly relaxes supercoiled DNA and catalyzes double- stranded breakage. Acts also as a ribosome inactivating protein. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
{"protein": "MQVLRTPESRFAGLADWPFAPHYAEITDAGGARLRLHYVDEGPRDGAPVLLMHGEPSWAYLYRKIIPALAARGHRVIAPDLIGFGRSDKPAARGDYTYERHVAWMSAWLEGLDLRGLTLFCQDWGGLIGLRLVAAFPERFAGLVIANTGLPTGAGMTDGFKAWLDFSQNVPEMPIGLIVNMGTGRDLTPAEIAAYDAPFPDETYKEGARQFPMLVPVTPEHASVAENLAAWKVLEHFPGPVVTAFSDGDPVTRGGEAIFQSRMPGALGQPHRTLRGGHFLQEDCPDDIVDIVDAVARPESQS", "text": "FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1 subfamily."}
{"protein": "MKKHLLASLLGASLLLPTAVNAADYVIDTKGAHASIQFSVSHLGYSFVVGRFNEFDGKFSFDAAKVSDGKVEVNINTNSVDSNHAERDKHLRSDDFLNTAKFPAAKFVSTSVADKGNGDLWITGDLSLNGVTKPVTIKAHTVGEGQDPWGGYRAGFVGSTEFTMKDFGIKMDLGPASANVKLDLVVEGIKQ", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0312 family. Type 1 subfamily."}
{"protein": "MTRIILILTATFFACALGASTGGSHPLRPWWNALRSSGRIVGGFEVPVEEVPFQVSLSGVGSSHFCGGSLLSERWVMTAGHCAASGQTNLQVRIGSSQHASGGQLIKVKKVNRHPKYDEVTTDYDFALLELEETVTFSDSCAPVKLPQKDAPVNEGTCLQVSGWGNTQNPSESSEVLRAAYVPAVSQKECHKAYLSFGGVTDRMVCAGFKEGGKDSCQGDSGGPLVHDNTLVGVVSWGYGCAQAGYPGVYARVASVRDWVKEVSGL", "text": "FUNCTION: Major function may be to aid in digestion of the blood meal. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MTVLIIGMGNIGKKLVELGNFEKIYAYDRISKDIPGVVRLGEFQVPSDVSTVVECASPEAVKEYSLQILKSPVNYIIISTSAFADEVFRERFFSELKNSPARVFFPSGAIGGLDVLSSIKDFVETVRIETIKPPKSLGLDLKGKTVVFEGSVEEASKLFPRNINVASTIGLIVGFEKVKVTIVADPAMDHNIHIVRISSAIGNYEFKIENIPSPENPKTSMLTVYSILRALRNLESKIVFG", "text": "FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. SIMILARITY: Belongs to the L-aspartate dehydrogenase family."}
{"protein": "MSRINKFVLTVSLLIFIMISAVACGIYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECIQVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLAMDSENLMFSLFKNGKPVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVCTLIIFFAALVAVISGASCLYLVRRVINRGIVEKEAIINNHFERVLDGGLFFSAADVKKLYSMYNSAFLDDLTKAMGRKSFDEDLKALPEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPVDKGKVYRFGGDEFAVIYTGGTLEELLSILKEIVHFQVGSINLSTSIGVAHSNECPTVERLKMLADERLYKSKKNGRAQISWQ", "text": "FUNCTION: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
{"protein": "MIQSDEDNLDSSETTASTSYSGTSSVSSRLQLRTSLFFENLNGAHGNPDAETEMATVAYETTSRGQGFAVYINNERFSQIMGASTSSSSSSNSSSITQFHDTQDNNIPSNTTVRPTSLRRDNEDTVPLRNVTPSQNAAVRPERAVNSPSSQRLSCALTISTSVLMGEDVEGSPIEQEHSRVVSSLYSSLANRGNDESKNGTPPRPTSIEPNETTEHSFFSYHYDDTLEPDVEEAVRLTKNKTSNVNFISSTGSKGEGETEDEVIDQYEPVNESKFIPHKLKIPEKAGSIKSSTSDDSHSPGAPGTSARKIKIPQSPSLIGNILIPSHNSDSSNESSPKDHIGHNNEEKFSSKSTRKPSTSLEEEGPPIGLPSIPVLRSVSGPSKWTKTPLRLESGNSTKSDPFSRYEGHKTPSPLTKMNKKKNKTLPEHGQPLVLAPIKSQSSESDTGQNSIIEKPARSIRRKQQEKTDNRKEDRHDAENIDLEARMPIQHIDTASIHSFDSGQNGFRDVYSIENIIVILLCCSIVPPLFFIIGCSSRRKLVSDYRLMRLLMNKEHRAALLQGFIWDVDLRWFRMFCLILGAAETVIVMAGIAIGFGVGITRE", "text": "FUNCTION: May be involved in positioning the distal bud pole signal. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Found at presumptive bud sites, bud tips, and the distal poles of daughter cells. SIMILARITY: To yeast BUD9."}
{"protein": "MASALGAQASVAAPIGAGGYGRSSSSKGSNTVNFCNKSWIGTTLAWESKALKSRHMNKIFSMSVQQASKSKVAVKPLELDNAKEPPLNLYKPKEPYTATIVSVERLVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGENPKKPGSPNTVRLYSIASTRYGDSFDGKTASLCVRRAVYYDPETGKEDPTKKGICSNFLCDSKPGDKVQITGPSGKIMLLPEDDPNATHIMIATGTGVAPYRGYLRRMFMEDVPSFKFGGLAWLFLGVANTDSLLYDEEFTNYLQQYPDNFRYDKALSREQKNKNGGKMYVQDKIEEYSDEIFKLLDGGAHIYFCGLKGMMPGIQDTLKRVAEQRGESWEQKLSQLKKNKQWHVEVY", "text": "FUNCTION: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family."}
{"protein": "MKLSWKTLLLWSLPIFVVGFFFWQGFLGPTTTDVGSNIASSRMTYGRFLEYLDMGWVKRVDLYENNHTAIVEAVGPELGNRVQRIRVELPASAPELITKLRKANVDLDAHPPKSTSAVWGLLGNLLFPLILVGGLAFLFRRSNNASGGPGQAMSFGKSKALFQMEAKTGVVFNDVAGVEEAKEEFQEVVTFLKQPESFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKDNAPCIVFIDEIDAVGRQRGTGVGGGNDEREQTLNQLLTEMDGFEGNTGVIVIAATNRADILDSALLRPGRFDRQVSVDVPDFRGRLAILEVHAKNKKMESKVSLETIARRTPGFSGADLANLLNEAAILTARRRKSAMTMSEIDTSIDRVVAGLEGTPLIDSKSKRLIAYHEVGHAIIGSLLEHHDPVQKVTLIPRGQARGLTWFTPSDDQSLISRSQILARIVGALGGRAAEEIIFGDAEVTTGASNDLQQVTSMARQMVTRFGMSKIGPLSLESQGSDPFLGRGMGGGSEYSDEVATNIDKQVREIVSECYKEAKKIVKDNRVVMDRLVDLLIEKETIEGNEFRHIVKEYTAIPEKNYYISQF", "text": "FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein; Stromal side. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family. SIMILARITY: In the central section; belongs to the AAA ATPase family."}
{"protein": "MAGRGGAARPNGPAAGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNTDTFARAKNWVKELQRQASPNIVIALAGNKADLASKRAVEFQEAQAYADDNSLLFMETSAKTAMNVNEIFMAIAKKLPKNEPQNAAGAPGRTRGVDLQESNPASRSQCCSN", "text": "FUNCTION: Protein transport. Probably involved in vesicular traffic. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Early endosome membrane; Lipid-anchor Melanosome. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MAAGGRLEDGSLDILQSTDDDPLLDTQPLPHHSLHAHFRPRFHPLPTVIIANLLLLIHVVFVTLAFLTGVLCLYPDPNEDKCPENYTNPLKVQTAIILGKVILWILHLLFERYIQYHHRKVRSRGYSQIYRSTRHLKALALTIHSSGNTALLLLLCVQYSFPEPNKLYLELILAVLALELICSLSCLVLYTVKIRRFNKAKPQPDVLEEEKCYAYPSNIASETGFRTVSSLEEIVEKQGDIIVYLKRHNALLSKRLLELATQPART", "text": "SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Late endosome. SIMILARITY: Belongs to the TMEM192 family."}
{"protein": "MASSSATLVGSTASDLLRSSTTGFTGVPLRTLGRAGLVLKRRDLTVSVTAKLRKVKRREYPWSSNPDPNMKGGRLRHLSTFQPLKQPPKPVILEFEKPLINMEKKINDFRKVAEKTGVDLSDQILALEAKYQKALVELYTNLTPIQRVTVARHPNRPTFLDHMYNMTEKFVELHGDREGYDDPAIAAGLGSIDGKTYMFIGHQKGRDTKENIKRNFAMPTPHGYRKALRLMEYADHHGFPIVTFIDTPGAFADLKSEQLGQGEAIAHNLRSMFALKVPVISIVIGEGGSGGALAIGCANKLLMLENSVFFVAMPEACGAILWKSNKAAPKAAERLKITASALLDLEIADGIIPEPLAGAHTDPSWMSQQIKIAINEAMDELTKLSTEDLIKDRMHKFRKLGVDGIQEGIPLVPSKKVNTKKREIGVPPKRQEVPIPDSQIEAEIEKLKKAIFEGEDSSAAKKNPGSQIGSAIDKLKGLFLEGKDSSAAKKTPGSQIVAELDKLKGLYLEAKDSSAAKVPGSQIVAEIEKLKNSIFEDEDSSSAVLPEKIPGSEIAVEIAKLKKNILEGKDSSSEPSKLDLDKTIETLKREVNREFSEAVKAAGLTKTLTKLRGEISKAKAGNQPLTPLLKVEIKSFNQRLSAAPNSRKLLKKRGLLREVTKVKLLLDKNKAATRKQELKKKSDEHKEAARLEQELKKKFDEVMDTPRIKEKYEALRSEVRRVDASSGSGLDDELKKKIIEFNKEVDLELATAVKSVGLEVESVKPGHGWNKSSVPEIEELNKDVQKEIEIVANSSPNVKRLIEQLKLEVAKSGGKPDSESKSRIDALTQQIKKSLAEAVDSPSLKEKYENLTRPAGDTLTDDKLREKVGVNRNFS", "text": "FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the AccA family."}
{"protein": "MPSFWDSFAVYNRNKHAKGDVHGGHMSQNMGGQPMYLQAKEHADIKKKEDGTLEAKIETPDGPRLVDVSNMTQQEFERTYNSLRKGEPNNRVNF", "text": "FUNCTION: Stationary phase-essential protein not required for growth on nonfermentable carbon sources. SIMILARITY: Belongs to the SPG4 family."}
{"protein": "MGKAQIIQHQARRILSQSNRNCLFRRSYETLPAANQTLPSRIKTDINQKASIIPLLEQWRKQGYEVNPSHLRGLIKNLSDCKNFTTALEASKWMFKHSVFDNFPEDCAAQLHLVNTVLGLEEAEKMFKNIPEKMRDYSVLLSSYTKPVRTVDKAEATFKKMRELGFLLKPYLFNSMICLYGQLQRLDMVEKLLYKLKKNNMEVGSLKVNNVSRVYANINAMEKFKTWVSKEGIELERDTIVAMAKAYHRAGSIEKAR", "text": "SIMILARITY: Belongs to the PPR family. P subfamily."}
{"protein": "MRHGDISSSRDCVGVAVVNYKMPRLHTKAEVLDNARRIADMVVGMKQGLPGMDLVVFPEYSTHGIMYDRQEMFDTASTIPGEETDIFAAACRKANVWGVFSITGERHEAHPHKVPYNTLVLIDNRGEIVQKYRKIMPWTPIEGWYPGDRTYVTDGPKGLKISLIICDDGNYPEIWRDCAMNGAELIVRCQGYMYPAKEQQVMVAKAMAWMNNTYVAVANATGWDGVYSYFGHSAIVGFDGRTLGECGEEEMGVQYAELSLGMIRDARRNMQSQNHLYKLLHRGYTGTINSGDGVNGVAECPFGFYRDWITDPDATRRRVEALTRTTPGTPECPIEGIPHEG", "text": "FUNCTION: Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Aliphatic amidase family."}
{"protein": "MEPFSSKSLALQAEKKLLSKMAGRSVAHLFIDETSSAVLDELYRVSKEYTHSRPQAQRVIKDLIKVAVKVAVLHRSGCFGPSELALAARFRQKLQQGAMTALSFGEVDFTFEAAVLAGLLTECRDMLLELVEHHLTPKSHNRIRHVFDHFSDPGLLTALYGPDFTQHLGKICDGLRKMLDEGKL", "text": "FUNCTION: Acts as a negative regulator of innate and adaptive immunity by maintaining immune homeostasis. Negative regulator of Toll-like receptor and T-cell receptor function. Prevents hyperresponsiveness of the immune system and maintains immune homeostasis. Inhibits JUN/AP1 and NF-kappa-B activation. Promotes Fas-induced apoptosis (By similarity). SIMILARITY: Belongs to the TNFAIP8 family. TNFAIP8L2 subfamily."}
{"protein": "MSSIELLIIAVGLSMDAFAVAICKGLSMKKMSYRNAVLTGCFFGGFQALMPLLGYLLGTQFKDYITSIDHWIAFGLLSLIGINMIKESKNTCEITDEDDTFSLKSLTVMAFATSIDALAIGVTFAFLQVNIIPAVTMIGITTFTFSFLGVKIGNLFGVKFQSKAEIVGGLILIGMGCKILFDHLGVISFVFDSLNKFN", "text": "FUNCTION: Probably functions as a manganese efflux pump. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MntP (TC 9.B.29) family."}
{"protein": "MTAPWRRLRSLVWEYWAGLLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQYLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPVDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWSMERLQAAPRAESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFVYKLRKTAEREQRSFCSTVADEIRFSLTCQRRVKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMACSTSLAPVFP", "text": "FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK3 subfamily."}
{"protein": "MASVTLKNVCKAYGDVLISKNVDLQIDEGEFVVFVGPSGCGKSTLLRCIAGLEDITSGDLYIGDQRMNDVEPSKRGVGMVFQSYALYPHLNLYDNMSFGLKLAKADKAEIDKRVEHAAEILQLGHLLERQPKALSGGQRQRVAIGRTLVSQPNVFLLDEPLSNLDAALRVNMRAQITKLQRQLGCTMIYVTHDQVEAMTMADKIVVLDGGYVSQVGKPLELYHYPQNRFVAGFIGSPKMNFMSVFIDEVESERVKVQLSNGVSFWIPVDGTTVNRGDRMSLGIRPEHLLSATEADATIHGEVMIVEKLGNETQVYLNLEGADADVIYRQPDTLAVDTGDKLEIGIPAHRCHLFHSDGRACKRLFKENGVDFE", "text": "FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Maltooligosaccharide importer (TC 3.A.1.1.1) family."}
{"protein": "MFRINVDAGSDFLLVLEELVGKLSTNDIQSIYISDKPNSKGEQANSLCGRSVNDLGFKNGDLLFVTYESTGEPPKTESSAPLTTAKTTNGANVSINMNDISIPINKGPGPLKVDQLPVDGLLDKEEGMIMRPRSDLCRHGDKGMCEYCSPLPPWDKDYRKEKGFKHMSYHAHLNEINESKNNRNNATSYMAPLEEPNYNINLNCPSGSHAPYPKGICSKCQPPVITLQQQQFRMVDHVEYADSTILNKFIDSWRTTGVQRFGILYGRYEQFDKVPLGIKAVVEAIYEPPQSGELDGLTLLPWENERQVDEIAASLGLYKVGMTFTDLTDSGAKNGTVLCKRHKNSYFLSCLEVIMAAKYQVSNPNITKHSNSGRFSSKFVTCVISGGMNGEIEPRSYQVSNSAEALIKADIITGSTQPSMLYINDSEGKRYVPDVFYSKINEYGLEVKTNAKPAFPVEFLLVSLSDSFPLDPSPMFRENFPIENRDFMGDLQDLKSAYNYLNADPGDGSQLFDFHFLTYIAKTGILSHDELKLVLSYVRNKDQTDYLQLVESPGWMTFITILEQSV", "text": "FUNCTION: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. SIMILARITY: Belongs to the NPL4 family."}
{"protein": "MQVVSRRLVQRPLVGGASIYSSSSLRSLYGVSNHLNGTDNCRYSSSLATKGVGHLARKGTGGRSSVSGIVATVFGATGFLGRYLVQQLAKMGSQVLVPFRGSEDSPRHLKLMGDLGQVVPMKFDPRDEDSIKAVMAKANVVINLIGREYETRNFSFEDANHHIAEKLALVAKEHGGIMRYIQVSCLGASVSSPSRMLRAKAAAEEAVLNALPEATIMRPATMIGTEDRILNPWSMFVKKYGFLPLIGGGTTKFQPVYVVDVAAAIVAALKDDGSSMGKTYELGGPDVFTTHELAEIMYDMIREWPRYVKLPFPIAKAMAAPRDFMVNKVPFPLPSPQIFNLDQINALTTDTLVSDNALKFQDLDLVPHKLKGYPVEFLIQYRKGGPNFGSTVSEKIPTDFYP", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I NDUFA9 subunit family."}
{"protein": "MRVLPLALAAAIFSGVTAILVYLSGLSSYGGARVSDADLAALGALQSGFSKCVDANGLGLKAIPGEDYCRVVIQYPSDTDSKWKDPKTGEPEGLSFEFNLCEAVASWEQVRNSTTILTKEYIDALPNGWEEYAWRRINKGIHLNKCQNRTLCMEKLSLVLPETPPYVPRQFGRCAVVGNSGDLLKTKFGDEIDSYDVVIRENGAPIQNYTEYVGTKSTFRLLNRGSAKALDKVVELDETKKEALIVKTTIHDIMNQMIREIPITNPVYLMLGTSFGSSAKGTGLKALEFALSMCDSVDMYGFTVDPGYKEWTRYFSESRKGHTPLHGRAYYQMMECLGLVKIHSPMRGDPGRVVKWAPTKDTIEAARVASEKLLKRPGAGSEGPLSSCTMIKKREKGKTPKRSVVRHAALKHLEYMRGATRYPLERNAGGGYLCMINER", "text": "FUNCTION: May possess sialyltransferase-like activity in vitro. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
{"protein": "MYRARAARAGPEPGSPGRFGILSTGQLRDLLQDEPKLDRIVRLSRKFQGLQLEREACLASNYALAKENLALRPRLEMGRAALAIKYQELREVAENCADKLQRLEESMHRWSPHCALGWLQAELEEAEQEAEEQMEQLLLGEQSLEAFLPAFQRGRALAHLRRTQAEKLQELLRRRERSAQPAPTSAADPPKSFPAAAVLPTGAARGPPAVPRSLPPLDSRPVPPLKGSPGCPLGPAPLLSPRPSQPEPPHR", "text": "FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the VPS37 family."}
{"protein": "MENLAPLYVNHINEQNRRVADVLAREQLEGLAIHSGQYHRQFLDDINYPFKANPHFKAWLPVLDIPNCWILTNGRDKPVLVFYRPVDFWHKVSDVPESFWTEHFEIKLLTKAEKVADLLPKNLDTWAYIGEHLDVADVLGFKNRNPDGVMNYFHWHRSFKTDYELACMREANRVAVAGHNAAREAFYKGASEFEIQQQYLSAIGQGENDVPYGNIIALNQNAAILHYTALEHAAPANRHSFLIDAGASFNGYAADITRTYAFEKNVFDELIKAMDKMQRELVDMMRPGVRFTDLHLATHHKLAQLLLEFGIARGEASDLVEQGVTSVFFPHGLGHMLGLQVHDVAGFAHDERGTHLAAPERHPFLRCTRVLAPRHVLTIEPGFYIIDSLLTELKADGRAEAVNWDMVNTLRPFGGIRIEDNVIVHQERNENMTRDLGLN", "text": "FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal position. SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily."}
{"protein": "MAFTGKYEFESEKNYDEFMKRLGLPDEVIERGRNFKIITEVQQDGENFTWSQSYSGGNIMSNKFTIGKECEMQTMGGKKFKATVKMEGGKVVADFPNYHQTSEVVGDKLVEISTIGDVTYERVSKRVA", "text": "FUNCTION: Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (By similarity). Stimulates gastric acid and pepsinogen secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MCGECYAYLTCIWCKKGLDKVDAKRCHEKKIRIACRNGKHCAVCTSCLENGLYLERSLFPGRPIYPGDLYEPDPWVMFNDIRCMYCGGCLTRDEKERHRLFCEDFWIFRHQVRGRCYLCTRHGSRPPYKETPAAV", "text": "FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin- protein ligase and modulates its activity. Protects host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the papillomaviridae E6 protein family."}
{"protein": "MDRLQRLMMSQRSNMIGAAATEMPLDDTKETVYISSLALLKMLKHSRAGVPMEVMGLMLGDFVDEYTVNVVDVFAMPQSGTGVSVEAVDDVFQAKMMDMLKQTGRDQMVVGWYHSHPGFGCWLSSVDVDTQRSFEQLNSRAVAVVVDPIQSVKGKVVIDAFRLISPATVVRNQEPRQTTSNVGLLNKPNIQSLIHGLNRHYYSLNIDYHKTSAELNMLMNLHKEQWQSGLKMHDYKEKERINLEATKKSVRIAEQYTKRIEEEKELTEDELKTRYVGKQDPKKHLSETAERVLEENIVSVLTAGVNSVAIK", "text": "FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. SIMILARITY: Belongs to the peptidase M67A family."}
{"protein": "MAFAWKKNFSYSKYASICSQTVRQALKPEIKNEVKTHGDAEFLYTRWKNGAQEKTESYNSAKSADKE", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase epsilon family."}
{"protein": "MARVSSLLSFCLTLLILFHGYAAQQGQQGQQFPNECQLDQLNALEPSHVLKSEAGRIEVWDHHAPQLRCSGVSFARYIIESKGLYLPSFFNTAKLSFVAKGRGLMGKVIPGCAETFQDSSEFQPRFEGQGQSQRFRDMHQKVEHIRSGDTIATTPGVAQWFYNDGQEPLVIVSVFDLASHQNQLDRNPRPFYLAGNNPQGQVWLQGREQQPQKNIFNGFGPEVIAQALKIDLQTAQQLQNQDDNRGNIVRVQGPFGVIRPPLRGQRPQEEEEEEGRHGRHGNGLEETICSARCTDNLDDPSRADVYKPQLGYISTLNSYDLPILRFIRLSALRGSIRQNAMVLPQWNANANAILYVTDGEAQIQIVNDNGNRVFDGQVSQGQLIAVPQGFSVVKRATSNRFQWVEFKTNANAQINTLAGRTSVLRGLPLEVITNGFQISPEEARRVKFNTLETTLTHSSGPASYGRPRVAAA", "text": "FUNCTION: Seed storage protein. SUBCELLULAR LOCATION: Protein storage vacuole. SIMILARITY: Belongs to the 11S seed storage protein (globulins) family."}
{"protein": "MTWRSDDIWIELITGSRKISNFCWALILFLGSLGFLLVGTSSYLGRNLLSFFPPQQIIFFPQGIVMSFYGIAGLFISSYLWCTISWNVGSGYDRFDRKEGIVCIFRWGFPGKNRRIFLRFLIKDIQSVRIEVKEGIYARRVLYMDIRGQGSIPLTRTDENLTPREIEQKAAELAYFLRVPIEVF", "text": "FUNCTION: Seems to be required for the assembly of the photosystem I complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ycf4 family."}
{"protein": "MIKIPKIGFVSLGCPKNLVDSERIITKLKAEGYDLVDSYDNADMVIVNTCGFLNSAIDESLEVIGEAIAENGKVLVTGCLGNKADLIKEKHSEVLSITGPQDYENLIEAVHTHAPIFVNDFVSLVPPQGIKLTPRHYSYLKISEGCNNTCTFCIIPDIRGKLKSRSIDNIMKEAEKLKNAGVKELLVISQDTSAYGVDIKYKSGIWNDKEYQSNILDLATALGDLDMWTRLHYVYPYPHVDKIVPLMAQGKILPYLDVPLQHSSPEVLKRMKRPAHTQKTLDRINKWRDICPDITIRSTFIVGFPGETEADFEHLLDFAEKAQLDRVGCFKYSEVEGAKANQFDNLISEEVKQQRLDEFMGLQAQISADKLQRFVGTEQQVIIDVINKDENYAIGRTKYDAPEVDGQVIIGDALERNLKVGEFATVEITESTEYDLIAD", "text": "FUNCTION: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methylthiotransferase family. RimO subfamily."}
{"protein": "MNASGRSHSKGPIIRSVSLEDLKRNSSFKGNLKYKDEVTSHKEPQVGTLSNEELLKDLDNMLRGKLNMGRNSFHADKRNKSDGNISALTFKARSGLEGDIRTIDIQQDSSDENDNFKFSDDGVNKDRNNEKDNNTDNAVEFQDDAEEAEEENEDESFANVDELDGFDLNKVSDGKHVPINEKGEVDYNMPVDKEFQKSLDQCAASLEERSSAPYALQRAVDWELKMFYSLEDELSEWFCSSDYMHFGQTQTLFKQKITQPQLFFDDENYAASVVECLIEDIPNSLASNLLALSYISMGCFAFTNSKSEHTKIIRRNNLMLVPHIQEIVHAFKKIAISCRDDNRNLKKQTILLFHSSTILYFICSICIEGRGENPEAVNVVIDAFEKTDLLEFLTKYIENWRWNSRLAMRIRNMISLLFKLIVLQFGDSSVYKQTKSSIYNLHGLTYPSKHPEKLSISPLHYQAFREDITSRFPDYNMPSSGLPKDVDKSESLSQFLEIPRPKSKNPLNMALIVPEKHIATPAPSPPSSPQLMHLGEGPRPRKSFQTNMAYPCLYPSDNEGSEDDTLEDRIDLNIERKPDNDIVIPFSTEEAARILSESLEIKLSTKQLWYERDLFMITERGWKQQLENEPYDYAALNHDANSSKEEKSAICIMQRIDKYYKSCLSSFNSLVFVLLQTMESSLTNNFHRKSEVSDKNLLNMLTPQLEIVRAKELSLKSAAGILHALLKWFKLSHILKFEHLAVVIHDSRYINTCASILSKYSEVYPERVFNKYVQTPNSFWKECSLSNESYRESYSVDDSGEVDTEIMPSFAYLLRILRKVTGNKTQRLKELPLSIGILFKRYYRLFNLDMYHPILKITRELTPFKNKRWKSEHMELISGVYLYEKLELTDNWVTGKDISGELSDACGQEIALRALLQFYNFQHYEISMEDLGYGHRNSSSQDLLNKESEYLNI", "text": "FUNCTION: Participates in the control of the reentry into the cell cycle following pheromone treatment. SIMILARITY: Belongs to the FAR11 family."}
{"protein": "MYICLLTLVLIHAAAAFVAQNATGILAGKDHCVCEVLLPDSSFPAKRVGALEDETIRLSNRVEDEMQKLEEQDIILDTYSEKIINLTRRVEYLEKLHPESLVEISFEVLKREIRELEMYISAMRVKPNGNSVQVETLYNEVKNMSKTVGQLETLDKNNVLQAKREIVNLKKRLVDCEKNLKAKPSLMVPLGSCQHQGLAHISKPNLMQLNWKGNAYKSGAWGKDAAWNTTKKSLYWVAPLNTDGRVLESIRIYPSMSDLQMYKNPIDLPLSMLIKNKLNNTFAGQGAGVVVHNNNLYYNCFNSHDMCRASLTSGVYQKKPLLNALFNNRFSYAGTMFQDMDFSSDEKGLWVIFTTEKSAGKIVVGKVNVATFTVDNIWITTQNKSDASNAFMICGVLYVTRSLGPKMEEVFYMFDTKTGKEGHLSIMMEKMAEKVHSLSYNSNDRKLYMFSEGYLLHYDIALKP", "text": "FUNCTION: May influence the maintenance, growth, or differentiation of chemosensory cilia on the apical dendrites of olfactory neurons. Major component of the extracellular matrix of the olfactory neuroepithelium. SUBCELLULAR LOCATION: Secreted, extracellular space."}
{"protein": "MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMIEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPALSQYQTPLFVWSVLITAVLLLLALPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNQTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTISSMGSFISLTAVMLMIFMIWEAFASKREVSTVELTSTNLEWLHGCPPPYHTFEEPAYVNLK", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the heme-copper respiratory oxidase family."}
{"protein": "TARYTALVAKDAKRAAADMGKVLHVEIDPEDAKVERMAKDESNQFGLFSWEFVRRHGLHLFGTCSTWFLLDIAFYSQNLFQKDVFTAIGWIPPAKTMNAVQEVYKIARAQTLIALCSTVPGYWFTVAFIDIIGRFAIQLMGFFFMTVFMFAIAIPYHHWTLQENRIGFVIMYSLTFFFANFGPNATTFV", "text": "FUNCTION: Low-affinity transporter for external inorganic phosphate (Pi). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. phosphate:H(+) symporter (TC 2.A.1.9) family."}
{"protein": "MDPKEKNYDASAITVLEGLQAVRERPGMYIGDTGITGLHHLVYEVVDNSIDEAMAGYCSRIDVRILEDGGIVIVDNGRGIPIEVHERESAKQGREVSALEVVLTVLHAGGKFDKDSYKVSGGLHGVGVSCVNALSEKLVATVFKDKKCYQMEFSRGIPVTPLQYVSVSDRQGTEIVFYPDPKIFSTCTFDRSILMKRLRELAFLNRGITIVFEDDRDVSFDKVTFFYEGGIQSFVSYLNQNKESLFSEPIYICGTRVGDDGEIEFEAALQWNSGYSELVYSYANNIPTRQGGTHLTGFSTALTRVINTYIKAHNLAKNNKLALTGEDIREGLTAVISVKVPNPQFEGQTKQKLGNSDVSSVAQQVVGEALTIFFEENPQIARMIVDKVFVAAQAREAAKKARELTLRKSALDSARLPGKLIDCLEKDPEKCEMYIVEGDSAGGSAKQGRDRRFQAILPIRGKILNVEKARLQKIFQNQEIGTIIAALGCGIGADNFNLSKLRYRRIIIMTDADVDGSHIRTLLLTFFYRHMTALIENECVYIAQPPLYKVSKKKDFRYILSEKEMDSYLLMLGTNESSILFKSTERELRGEALESFINVILDVESFINTLEKKAIPFSEFLEMYKEGIGYPLYYLAPATGMQGGRYLYSDEEKEEALAQEETHKFKIIELYKVAVFVDIQNQLKEYGLDISSYLIPQKNEIVIGNEDSPSCNYSCYTLEEVINYLKNLGRKGIEIQRYKGLGEMNADQLWDTTMNPEQRTLIHVSLKDAVEADHIFTMLMGEEVPPRREFIESHALSIRINNLDI", "text": "FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II topoisomerase GyrB family."}
{"protein": "MGEEAAMATMESAYHDELAPAAAPAPAKGGGSKKKRKQQKREEKRKECRLVSYHELPDYMKENEFILDYYRSEWPILNALLSLFSWHNETINIWTHLLGFVLFFGLTVLHLGQYFPQVADLIGHLSWPISKVAENVSSNIGDVLSGAASFMQASPASSAGAMAAAWPVTAAAAATTRWPFFVFLAGAMFCLLSSAACHLLSCHSHRLNLFLIRLDYTGIAVMIVVSFFPPIYYIFQCEPRWQVVYLSAITAAGVATVYALMSPRLSAARYRAHRALLFVAMGLSGVVPAAHAVAVNWHEPRRNVTLAYEGAMAASYLAGTAFYLTRVPERWRPGMFDLCGHSHQIFHALVIAGALAHYAAAIVFIQARDEMGCPAP", "text": "FUNCTION: May play a role in abiotic stress response. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADIPOR family."}
{"protein": "ADGYVKGKSGCKISCFLDNDLCNADCKYYGGKLNSWCIPDKSGYCWCPNKGWNSIKSETNTC", "text": "FUNCTION: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active on insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MWHNVGLTLLVFVATLLIVLLLMVCGWYFVWHLFLSKFKFLRELVGDTGSQEGDNEQPSGSETEEDPSASPQKIRSARQRRPPVDAGH", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMIM13 family."}
{"protein": "MMKLLLIAAAAFVAVSADPIHYDKITEEINKAVDEAVAAIEKSETFDPMKVPDHSDKFERHIGIIDLKGELDMRNIQVRGLKQMKRVGDANVKSEDGVVKAHLLVGVHDDVVSMEYDLAYKLGDLHPNTHVISDIQDFVVELSLEVSEEGNMTLTSFEVRQFANVVNHIGGLSILDPIFAVLSDVLTAIFQDTVRAEMTKVLAPAFKKELERNNQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the mite group 7 allergen family."}
{"protein": "MAHLLEKTRKITSILKRSEEQLQDELPYNAITRQLADIIHCNACIINSKGRLLGYFMRYKTNTDRVEQFFQTKIFPDDYVQGANMIYETEANLPVEHDMSIFPVESRDDFPDGLTTIAPIHVSGIRLGSLIIWRNDKKFEDEDLVLVEIASTVVGIQLLNFQREEDEKNIRRRTAVTMAVNTLSYSELRAVSAILGELNGNEGKLTASVIADRIGITRSVIVNALRKLESAGIIESRSLGMKGTYLKVLISDIFEEVKKRDY", "text": "FUNCTION: DNA-binding global transcriptional regulator which is involved in the adaptive response to starvation and acts by directly or indirectly controlling the expression of numerous genes in response to nutrient availability. During rapid exponential growth, CodY is highly active and represses genes whose products allow adaptation to nutrient depletion. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CodY family."}
{"protein": "MAAQRGMPSSAVRVLEEALGMGLTAAGDARDTADAVAAEGAYYLEQVTITEASEDDYEYEEIPDDNFSIPEGEEDLAKAIQMAQEQATDTEILERKTVLPSKHAVPEVIEDFLCNFLIKMGMTRTLDCFQSEWYELIQKGVTELRTVGNVPDVYTQIMLLENENKNLKKDLKHYKQAADKAREDLLKIQKERDFHRMHHKRIVQEKNKLINDLKGLKLHYASYEPTIRVLHEKHHTLLKEKMLTSLERDKVVGQISGLQETLKKLQRGHSYHGPQIKVDHSREKENAPEGPTQKGLREAREQNKCKTKMKGNTKDSEFPIDMQPNPNLNVSKESLSPAKFDYKLKNIFRLHELPVSCVSMQPHKDILVSCGEDRLWKVLGLPKCNVLLTGFGHTDWLSDCCFHPSGDKLATSSGDTTVKLWDLCKGDCILTFEGHSRAVWSCTWHSCGNFVASSSLDKTSKIWDVNSERCRCTLYGHTDSVNSIEFFPFSNTLLTSSADKTLSIWDARTGICEQSLYGHMHSINDAIFDPRGHMIASCDACGVTKLWDFRKLLPIVSIDIGPSPGNEVNFDSSGRVLAQASGNGVIHLLDLKSGEIHKLMGHENEAHTVVFSHDGEILFSGGSDGTVRTWS", "text": "FUNCTION: Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, flagellum axoneme Cytoplasm, cytoskeleton, cilium axoneme Cell projection, cilium, flagellum Note=Detected on the sperm flagellum axoneme. Detected in the central apparatus of the axoneme. Colocalizes with SPAG6 on microtubules (By similarity)."}
{"protein": "MKAIVFAYHDIGCVGLNALAEAGYDIQAVFTHTDNPGENRFFSSVARVAADLALPVFAPEDVNHPLWVERIRELQPDIIFSFYYRNMLSDEILSLAPQGGFNLHGSLLPQYRGRAPINWVLVNGETETGVTLHQMVKKADAGPIAGQYKVAISDVDTALTLHAKMRDAAQELLRNLLPRMKEGPLPLTPQKEADASYFGRRTAADGEIHWQKSAFTINNLVRAVTEPYPGAFSYLGQRKLTIWRSRPLDLVHNKLPGTVLSTAPLTVACGEGALEIITGKGEAGLYVQGDRLAQEMGIVTDVRLGNKPSNTLKRRTRVLILGVNGFIGNHLTERLLQDDRYEVYGLDIGSDAISRFLGNPAFHFVEGDISIHSEWIEYHIKKCDVILPLVAIATPIEYTRNPLRVFELDFEENLKIVRDCVKYNKRIVFPSTSEVYGMCDDKEFDEDTSRLIVGPINKQRWIYSVSKQLLDRVIWAYGVKEGLKFTLFRPFNWMGPRLDNLDAARIGSSRAITQLILNLVEGSPIKLVDGGAQKRCFTDIHDGIEALFRIIENRDGCCDGQIINIGNPTNEASIRELAEMLLTSFENHELRDHFPPFAGFKDIESSAYYGKGYQDVEYRTPSIKNARRILHWQPEIAMQQTVTETLDFFLRAAVIEKTAAPKDELNA", "text": "FUNCTION: Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SIMILARITY: In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily. SIMILARITY: In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily."}
{"protein": "MTHPVPIQFQSPDLEAIASSAGRIVVFAGEGGAMGVAAKRVNRLMRGALERAAASEAFGKLKQGEAMELGFPAGMAADAVQLVKLDRRCDVATARKAGGAIGRSLSKAGTLVLADTIQRAAEVSFGIALRAYDFTPHKTGEKTVPGPVTMMVANPETVAAEAGPMAALAEGIFFTRDLVNEPANVLSTFDFAARLAAMHELGLEVEILEEEDMEKLGMRALLGVGQGSEHPSKLVVMQWKGGPEDQVPLALVGKGVVFDTGGISIKPAAGMEDMTMDMGGAAVVAGVMRTLAMRKARANVVGLVGIVENMPDGNAQRPGDVVRSMKGDTIEVINTDAEGRLVLADVLWYAQERFNPRGVIDLATLTGAIIVALGHENTGVFSNDDAFCAAFLKAAQSEGEGAWRMPMGERYDEMLKSRIADMRNSTGREAGSITAAHFLRRFVKPETPWIHLDIAGTALLKGDTALAPKGATGWGVLSLDRLIRDMLEK", "text": "FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M17 family."}
{"protein": "MGQTKSKTKSKYASYLSFIKILLKRGGVRVSTKNLIKLFQIIEQFCPWFPEQGTLDLKDWKRIGEELKQAGRKGNIIPLTVWNDWAIIKAALEPFQTKEDSVSVSDAPGSCVIDCNEKTGRKSQKETESLHCEYVTEPVMAQSTQNVDYNQLQGVIYPETLKLEGKGPELVGPSESKPRGPSPLPAGQVPVTLQPQTQVKENKTQPPVAYQYWPPAELQYLPPPESQYGYPGMPPALQGRAPYPQPPTVRLNPTASRSGQGGTLHAVIDEARKQGDLEAWRFLVILQLVQAGEETQVGAPARAETRCEPFTMKMLKDIKEGVKQYGSNSPYIRTLLDSIAHGNRLTPYDWESLAKSSLSSSQYLQFKTWWIDGVQEQVRKNQATKPTVNIDADQLLGTGPNWSTINQQSVMQNEAIEQVRAICLRAWGKIQDPGTAFPINSIRQGSKEPYPDFVARLQDAAQKSITDDNARKVIVELMAYENANPECQSAIKPLKGKVPAGVDVITEYVKACDGIGGAMHKAMLMAQAMRGLTLGGQVRTFGKKCYNCGQIGHLKRSCPVLNKQNIINQAITAKNKKPSGLCPKCGKGKHWANQCHSKFDKDGQPLSGNRKRGQPQAPQQTGAFPVQLFVPQGFQGQQPLQKIPPLQGVSQLQQSNSCPAPQQAAPQ", "text": "FUNCTION: The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Note=Cytoplasmic membrane (in a transfection system). SIMILARITY: Belongs to the beta type-B retroviral Gag protein family. HERV class-II K(HML-2) gag subfamily."}
{"protein": "MPQISRYSDEQVEQLLAELLNILEKHKAPTDLSLMVLGNMVTNLINTSIAPAQRQAIANSFARALQSSINEDKAH", "text": "SIMILARITY: Belongs to the UPF0352 family."}
{"protein": "MAEKRDVLNYLEMVIRSYDIULSCAAHVLDRVKFRIERKDED", "text": "SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family."}
{"protein": "MKSALKKSVVSTSISLILASGMAAFAAHAADDVKLKATKTNVAFSDFTPTEYSTKGKPNIIVLTMDDLGYGQLPFDKGSFDPKTMENREVVDTYKIGIDKAIEAAQKSTPTLLSLMDEGVRFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDAQDGIPLTETFLPELFQNHGYYTAAVGKWHLSKISNVPVPEDKQTRDYHDNFTTFSAEEWQPQNRGFDYFMGFHAAGTAYYNSPSLFKNRERVPAKGYISDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLPNDNPAPDQYQKQFNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPLPLNGAQKGYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDLKLDGVSLLPWLQDKKQGEPHKNLTWITSYSHWFDEENIPFWDNYHKFVRHQSDDYPHNPNTEDLSQFSYTVRNNDYSLVYTVENNQLGLYKLTDLQQKDNLAAANPQVVKEMQGVVREFIDSSQPPLSEVNQEKFNNIKKALSEAK", "text": "SIMILARITY: Belongs to the sulfatase family."}
{"protein": "MLTADIPPNQSIYIKHINEKIKKEELKRSLYCLFSQFGRLLDVVALKTPKLRGQAWVVFTEVTAASNAVRQMQNFPFYDKPMRIQYAKSKSDYVTKAEGSFVPKEKKMKQEEKVERKRHAEETQQPSMPNGATTQNGMPVPPFQPSGQDTMPPNNILFIHNLPIETNSMMLQLLFEQYPGFKEIRMIEAKPGIAFVEYEDDVQSSMAMQALQGFKITPQNPMVVSFAKK", "text": "FUNCTION: Involved in nuclear pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus, Cajal body Nucleus, nucleoplasm Cytoplasm Note=Present in coiled bodies and an interchromatin network. Redistributed throughout the cytoplasm upon entry into mitosis. SIMILARITY: Belongs to the RRM U1 A/B'' family."}
{"protein": "MIKTWIRCLTTEVRYHQPNAHGRSLVMSVLNSTVTKREAKDYLNKYTDENNHHYCLVFLRHLSEYSDNVLSGFSKTVSRIQTLGLRPILIVDPLCQDISYQSQRLDNHLHDQSLKSIIVLDPITIGERGSIDVKLPILNPHIIPIIEPYQYHEKEAFKKLAGDPSRFLSSLVSNLPINIDKVFLISKYGGLPSVERHTNSHVFVNLSQEYRELRNSYQNQLEKLESIQVDNTEKNLVESLQLFLNQDKILSNSDQLKCHMEDLEIMNKTLSVLPHSSTGLITTILAGSKLSDNNPLVYNILTDRSLISSSLPRFKRSAAAQSKSWYELPSSNVEEEVTSANDSVLVTTVFKKGIDIHIFDFRTLTDDNSIGLPPSQATQTGKSDPVSKKLDLNKLNGIINSSFKRSLDLSHYLGRINGNIASIIVIGDYEGIAILTYEGPKDKQFVYLDKFAVAQKLKGSLGISDIIFNLMFRKFPHELIWRSREDNVVNKWYFQRSTGVLHLSLDLGNDDQKQSIFKLFYYGNPESESFHNVERLRDYAKYVRDITPSWHK", "text": "FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acetyltransferase family."}
{"protein": "MAVSVQDLLDKIHFHVIYSTETALQKEITTSEIMRPGLEMAGYFDYFTPERIQLFGMKEWSYMMTVVGDNRYDLLKKVMAKETPVVIVARNLEIPSEMVAAAKKADIVLLQSREATSRLNSVLTSFLDERLAERTTVHGVLMDIFGVGVLIQGASGIGKSETGLELVKRGHRLVADDRVDVFQRDAFTLSGEPAEILRNMIEIRGVGIIDVMSLFGAGAVKDSTDIDMVIYLEYYDKEKAFDRLGNAPTIVEFSDVEVPQTRIPVKTGRNVSVIVEAAVMNFRAKQMGFDATKTFEDRLTDLISHNKESQ", "text": "FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion. SIMILARITY: Belongs to the HPrK/P family."}
{"protein": "MKTTLIKVIAASVTALFLSMQVYASGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQEAIEHLRASEHKSH", "text": "FUNCTION: Is capable of binding multiple equivalents of a variety of divalent and trivalent metals, including Cu(2+) and Fe(3+) but also Mn(2+), Ni(2+), Mg(2+) and Zn(2+). Is able to bind up to six Cu(2+) atoms. It is proposed to be a metal scavenging protein that has a role in cellular copper management in N.europaea. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MASAATAGLTLLSGGASIAADIASIVTEQQRLALQKEQIRNNYELGKQSLSLQQQAMENSRDRIRLSAAQIKELGLDPKSELNMLMGLTAGAQPPISTPISSEQLFLNSSNLARSVRWDARNFGEAINTFAGLRAKHQANPNRPDMMLGSDNPNWGARATGDALSVSGLSVRSNHFGSGPSSLGSLSSVRSNPFSSISSGSVGGISLRTVGSRPSIRSVFSTTSV", "text": "FUNCTION: Minor structural protein present in one or two copies per virion. Does not seem to play a role in capsid assembly, but is essential for production of infectious virus (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm."}
{"protein": "MGGLEKKKYERGSATNYITRNKARKKLQLSLPDFRRLCILKGIYPHEPKHKKKVNKGSTAPRTFYLLKDIKFLLHEPIVGKFREYKVFVRRLRKAYGKREWDAVDRIRDNKPAYKLDHIIKERYPTFIDAVRDLDDALSMCFLFSTFPRTGKCHVQTIQLCRRLSVEFLNYVIASRSLRKVFLSIKGIYYQADILGQTVTWITPYAFSHDHPTDVDYRVMATFTEFYTTLLGFVNFRLYQTLNLQYPPKLDYFSEADLKSDNEDKYALETEAYMEKLAALSASLSRVIPSEPEEENEVDEFPADPENAGQEEEQKKQLQEEEKHKSMFVGLKFFLNREVPRDALAFIIRSFGGEVSWDASVCIGATYNSANPSITHHIVDRPSIQTQIINRYYLQPQWVFDCVNARMLLPVEDYFPGVLLPPHLSPFVQEKEGDYIPPEKLRLMALQKGENPEDDDDDDEEDDEDEEEDDEDEDDEENEEEEEDKKLRHLENKKVGQNKLNVRITAGKVKVEDRTQAAEQEKTEEKRLAIMMMKKKEKYLYNKIMFGKKRKVREANKLALKRKAHDESVKVERKKKAKKH", "text": "FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the pescadillo family."}
{"protein": "MKHIINSYENINNTARNNSDCPRVVLPEEIFFTISIVGVLENLIVLLAVFKNKNLQAPMYFFICSLAISDMLGSLYKILENILIILRNMGYLKPRGSFETTADDIIDSLFVLSLLGSIFSLSVIAADRYITIFHALRYHSIVTMRRTVVVLTVIWTFCTGTGITMVIFSHHVPTVITFTSLFPLMLVFILCLYVHMFLLARSHTRKISTLPRANMKGAITLTILLGVFIFCWAPFVLHVLLMTFCPSNPYCACYMSLFQVNGMLIMCNAVIDPFIYAFRSPELRDAFKKMIFCSRYW", "text": "FUNCTION: Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTASMRLK", "text": "FUNCTION: May regulate expression of the erythromycin resistance protein."}
{"protein": "MPGLAAASPAPPEAQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI", "text": "FUNCTION: Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Cytoplasm. SIMILARITY: Belongs to the COX17 family."}
{"protein": "MSLRKVRSLPSLRVLAEVSNPLVRVPPPSFTYQTRQVHNTKKNEHSPMLSSDSHASFTRMSLKTLKNECRTRGLKVSGKKTELVERILLFEGSSSKKLHTSAIQRAKNDSSHIDSMKIPNVAKLEAEAESRKTDYIVKVPSIVNNAATEPKTKIEKDYEKKLQPADKKPLAENVGTVATPDADNVIQTPSVSDSIKVVNPEEELRSGSSEQGRSYSQQDEELTSRDKKFLLGFAGTVAAWWSLRFWKKEESKK", "text": "SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the AIM34 family."}
{"protein": "MTEQYYKIALLFNANKVYDRQVVEGIGQYIQASQCMWDIFVEDEFIYHTDTINQLSIDGIIADFDDPKTVELLQHTLIPTIAVGGSYKQADFYPHFPYIATDNMALVEMALSHLQEKGLSQFAFYGLQVNTHKHWSIERRDAFVELMEKNHYPIYLYEGVQVHAQNWLEEQQKLIVWLKSLPSHTGIIAVTDARARHLLQACEYSKIAVPEELCVVGIDNEELIQYLSRMSLSSVEQGTREIGYQAAKLLHKLLNGQKVSHTPILIPPITVHSRNSTDYRSLTDPLVIQAMHYIRHRACHRIKVGQVLDHLETSRSNLEQRFKNEMNKTIHQVIHEEKISRAKNLLQQTDISIKEITEICGYPSIQYFYSVFKKEFEMTPKEFRLNC", "text": "FUNCTION: Regulatory protein for the xylBAFGHR operon."}
{"protein": "MSWLVGALQTFGSLADVAGTVSNIVYQQRQAAQLEKQNELMETWMNKQEALQKSQMELTRDLSINGPAARVQSALDAGFDEVSARRIAGSGERVIWGNLDRPIMHAGTMDSIRQTRHLDSLSHSLATFKNGTPFGKPAPPTAKSGRPQATTAQITIGHNPGSTSV", "text": "FUNCTION: Minor structural protein present in one or two copies per virion. Does not seem to play a role in capsid assembly, but is essential for production of infectious virus (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the vesivirus VP2 protein family."}
{"protein": "MEIVGCRAENNSCPFRPPAMLFHGISGGHIQGIMEEMERRSKTEARLTKGTQLNGRDAGMPPLSPEKPALCAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESELTCFAKDGSIYCKEDYYRRFSVQRCARCHLGISASEMVMRARDSVYHLSCFTCSTCNKTLTTGDHFGMKDSLVYCRAHFETLLQGEYPPQLSYTELAAKSGGLALPYFNGTGTVQKGRPRKRKSPALGVDIVNYNSGCNENEADHLDRDQQPYPPSQKTKRMRTSFKHHQLRTMKSYFAINHNPDAKDLKQLAQKTGLTKRVLQVWFQNARAKFRRNLLRQENGGVDKADGTSLPAPPSADSGALTPPGTATTLTDLTNPTVTVVTTVTSNMDSHEPGSPSQTTLTNLF", "text": "FUNCTION: Involved in gonadal development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSQLLTARQAEELHKSIIAYLASVNLTESSAALRAELGDSVSIDDATLKKYEGLLEKKWTSVVRLQKKIMDLESRCAALQSELDSATPTSLLRKNQDPTSWLPRSPARHILEGHRNPVTCVAFHPVFSSLASGSDDTTIKIWDWELGELERTVKGHTKAVLDVDYGGPRGGTLLASCSSDLTIKLWDPSDNYKNIRTLPGHDHSVSSVRFIPSGAAGSPMSGNLLVSASRDKTLRIWDVTTGYCVKTLSGHVDWVRAVAPSIDGRFLLAAGDDRIPRLWDLSSAETKSTFLGHEHVIECVAIAPAASYPHLAVLSGLKKPPPASSSAEFFATGSRDKTIRLWDSRGNLIKTLVGHDNWVRALAFHPGGKHLLSVADDKTIRCWDLTQECKCVRVISDAHGHFVTCLRWAPPLIKDGGANGEAETNGTPAATSTTNGVRPDPNVATKISIRCVIATGSVDQKVRIFAT", "text": "FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules at the hyphal tip and the mitotic spindle poles. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules at the hyphal tip and the mitotic spindle poles. SIMILARITY: Belongs to the WD repeat LIS1/nudF family."}
{"protein": "MENAKMNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAQQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHGFSAEQLRNATHLVWATGGGMVPEEEMEQYLAKGH", "text": "SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA subfamily."}
{"protein": "MQWNGVRRAHSIWCKRLTNNTHLHHPSIPVSHFFTMSSLEEPLSFDKLPSMSTMDRIQRFSSGACRPRDDVGMGHRWIEGRDCTTSNSCIDDDKSFAKESFPWRRHTRKLSEGEHMFRNISFAGRTSTVSGTLRESKSFKEQKYSTFSNENGTSHISNKISKGIPKFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWVPQLADAKDVMDAVNTLDGARLPVLTPNLKGFQAAVSAGAKEVAIFASASESFSLSNINCTIEESLLRYRVVATAAKEHSVPVRGYVSCVVGCPVEGPVLPSKVAYVVKELYDMGCFEISLGDTIGIGTPGSVVPMLEAVMAVVPADKLAVHFHDTYGQALANILVSLQMGISIVDSSIAGLGGCPYAKGASGNVATEDVVYMLNGLGVHTNVDLGKLIAAGDFISKHLGRPNGSKAAVALNRRITADASKI", "text": "FUNCTION: Involved in the catabolism of branched amino acids such as leucine. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the HMG-CoA lyase family."}
{"protein": "MTAGAGGSPPTRRCPATEDRAPATVATPSSADPTASRAVSWWSVHEHVAPVLDAAGSWPMAGTPAWRQLDDADPRKWAAICDAARHWALRVETCQEAMAQASRDVSAAADWPGIAREIVRRRGVYIPRAGVA", "text": "SIMILARITY: To M.tuberculosis Rv2656c."}
{"protein": "MPTSDPGLRRVTVHAGAQAVDLTLPAAVPVATLIPSIVDILGDRGASPATAARYQLSALGAPALPNATTLAQCGIRDGAVLVLHKSSAQPPTPRCDDVAEAVAAALDTTARPQCQRTTRLSGALAASCITAGGGLMLVRNALGTNVTRYSDATAGVVAAAGLAALLFAVIACRTYRDPIAGLTLSVIATIFGAVAGLLAVPGVPGVHSVLVAAMAAAATSVLAMRITGCGGITLTAVACCAVVVAAATLVGAITAAPVPAIGSLATLASFGLLEVSARMAVLLAGLSPRLPPALNPDDADALPTTDRLTTRANRADAWLTSLLAAFAASATIGAIGTAVATHGIHRSSMGGIALAAVTGALLLLRARSADTRRSLVFAICGITTVATAFTVAADRALEHGPWIAALTAMLAAVAMFLGFVAPALSLSPVTYRTIELLECLALIAMVPLTAWLCGAYSAVRHLDLTWT", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EccD/Snm4 family."}
{"protein": "MARLEDPTALTQLPDESARVRYTSSELQDYFETLKFPQRFLDLGNSVLKDPSLARTKENGLPLLQAITRYHTCNVPFENLVLHYDPHKIVTLDPAELYTKIVTRRRGGRCMENNIFLGTALRSLGYEVRNCGGRVSRAMSPYPEVRKNQSATYDGWNHMLLLVFLGDEWYGVDVGMGSMGPNLPFPLQDGFESLSIAPREIRIQKRSISETHATGPSHATKMWCYDVCYNPAESKKTWTPVYCFTETEFLPQDYEVMSWFTSTNPRSFFTRYITCTKMIMDEDKEVIIGNLTLFKDTVRETIGSDRKVVKKFETEEERIKGLVEIFDVNLTEEEKNSLPQEKRLA", "text": "FUNCTION: N-malonyltransferase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2- AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N- malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N- malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable). SIMILARITY: Belongs to the arylamine N-acetyltransferase family."}
{"protein": "MQLKTEVFLVEKEILVYIQTKSIGIEDNSIKLKMTPLLKKFANIGDKVYLKHSTFMLPTKIKAKKEDEVLLEFPSLTPEKPLGDRRNVRVLSDPENPVKVRFNEITKEVYDISEVGFSIKCGMEEIDEILKNKEISEVEIYLPNLEEWIKGSARLVNVREFENGDILCGYELFLDTPDEVKVRFYIYERVKEILKGEK", "text": "SIMILARITY: To A.aeolicus aq_1211 and aq_1583."}
{"protein": "MAVFPWHSRNRNYKAELASCRLETVPLECGDYHPLKPITVTESKTKKVSRKGSTSSTSSSSSSSVVDPLSSVLDGTDPLSMFAATSDPAATVTVTESSRKKRDKDDNSFVGPDFEPWANKRGEILARYTTTEKLSINLFMGSEKGRAGAAASAMSEKVRTRLEELDDFEEGSQKELLNLTQQDYVNRIEELNQSLKDAWASDQKVKALKIVIQCSKLLSDTSVIQFYPSKFVLITDILDTFGKLVYERIYSMCVDSRGALPDHFSPENVNDTAKETCLNWFFKIASIRELIPRFYVEASILKCNKFLSKTGISECLPRLTCMIRGIGDPLVSVYARAYLCRVGMEVAPHLKESLTRNFFDFLLTFKQIHGDTVQNQLVAQGVELLSYLPLYSPAMGWIFQCVSYHAPEALLTEMMERCKKLGNNALLLNSVMSAFRAEFIATRSMDFIGMIKECDESGFPKHLLFRSLGVNLALADPPENDRLQILNEAWKVITKLKSPQDYINCAEVWVEYTCRHFTKREVNTVLADVIKHMTPDRAFEDSYPQLQSIIKKVIAHFHDFSVLFSVEKFLPFLDMFQKESVRVEVCKCIMEAFINALTLEDEKRMLAHLINGFIKMVSFGRDFEQQLSFYVESRSMFCNLEPVLVQLIHSVNRLAMETRKVMKGNHSRKTAAFVRACVAYCFITIPSLVGIFTRLNLYLHSGQVALANQCLSQADAFFKAAISLVPEVPKSISIDGKLRPSEPFLLEFLCNFFSTLLIVPDHPEHGVLFLVRELLNVIQDYTWEDSSDDKIRIYTSVLHLLSAMSQDTYLYHIDKVDSNDSLYGGDSRFLAENSKLCEAAMVQILEHLKTLAKDEALKRQSLLGLSFFNSILAHGDLRNNKLNQLSVNLWHLAQRHGCADTRTMVKTLDYIKKRSKQPDMNHLSELALRLPLQTRT", "text": "FUNCTION: Acts as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. In the endosomes, drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association with the CCC complex and cooperation with the WASH complex on early endosomes. Seems not to be required for CCC complex stability. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Endosome Note=Endosome location is dependent of the association with the CCC and WASH complexes. SIMILARITY: Belongs to the VPS35L family."}
{"protein": "MSPGLQKGSRLMENRSPPSSFSIEHILGLDKKTEVASSPIIKHHRPWIQCNSEGVDGTFWHIPVISCDLPVQVHALRRSMGEETQVRLEKCCGEEDRLTYKRELSWYRGRRPRTAFTRSQIEILENVFRVNSYPGIDIREELAGKLALDEDRIQIWFQNRRAKLKRSHRESQFLMVKDSLSSKIQE", "text": "FUNCTION: Regulates the earliest stages of development of the anterior neural plate. Plays a role in forebrain development by inhibiting the expression of otx2 and pax6 in the rostral region of the anterior neural plate. Necessary for both neural differentiation and neural patterning. Controls Spemann organizer development. May act as a transcriptional repressor (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Enters the cytoplasm in the presence of zyx. SIMILARITY: Belongs to the ANF homeobox family."}
{"protein": "MGKYIRKSKIDGAGAGAGGGGGGGGGGESSIALMDVVSPSSSSSLGVLTRAKSLALQQQQQRCLLQKPSSPSSLPPTSASPNPPSKQKMKKKQQQMNDCGSYLQLRSRRLQKKPPIVVIRSTKRRKQQRRNETCGRNPNPRSNLDSIRGDGSRSDSVSESVVFGKDKDLISEINKDPTFGQNFFDLEEEHTQSFNRTTRESTPCSLIRRPEIMTTPGSSTKLNICVSESNQREDSLSRSHRRRPTTPEMDEFFSGAEEEQQKQFIEKYNFDPVNEQPLPGRFEWTKVDD", "text": "FUNCTION: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity. May target specifically CDKA-1. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Note=Distributed in a ponctuate pattern. SIMILARITY: Belongs to the CDI family. ICK/KRP subfamily."}
{"protein": "MSRPAHRRPEYHKINKDLFVLTYGALVAQLCKDYEKDEDVNQYLDKMGYGIGTRLVEDFLARSCVGRCHSYSEIIDIIAQVAFKMYLGITPSVTCNNSSKNEFSLILEKNPLVEFVEELPAGRSSLCYCNLLCGIIRGALEMVHLAADVTFLQDRLKGDSVTEIGITFLKKRDEKKYRGKK", "text": "FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network Endoplasmic reticulum. SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily."}
{"protein": "MQNDAGEFVDLYVPRKCSASNRIIGAKDHASIQINIAEVDKVTGRFNSQYKTYAICGAIRRMGESDDSIMRLAKNDGIVSKNF", "text": "FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Rough endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family."}
{"protein": "MDKADFLKGLPVYNKTNFSRFHADSVCKASNRRPSVYLPTREYPSEQIIVTEKTNILLRYLHQQWDKKNAAKKREQEQAEGEGGSPAPPRKIARTDSQEMNEDS", "text": "FUNCTION: Functions as a component of numerous distinct DCX (DDB1-CUL4- X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. In the DCX complexes, acts as a scaffolding subunit required to stabilize the complex. SIMILARITY: Belongs to the DDA1 family."}
{"protein": "MRLFLLALLATLAVTQALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEVASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTAVRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPMHLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLPQDFWDKSIIEKPTDGRDLVCHASAWDFYLTDDVRIKQCTRVTQDQLFTVHHELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGLLKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWNCAFWKLRDEYSGIEPPVVRSEKDFDAPAKYHISADVEYLRYLVSFIIQFQFYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPDALEAFNGERIMSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVSS", "text": "FUNCTION: May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase M2 family."}
{"protein": "MRIHYLLFAVLFLFLMPVPGEGGIINTIQRYFCRVRGGRCAALTCLPRETQIGRCSVKGRKCCRTRK", "text": "FUNCTION: Has antibacterial activity against Gram-positive bacterium S.pneumoniae Serotype 14. Is also active against Gram-negative bacteria M.catarrhalis 1857, and non-typeable H.influenzae strains 86-028NP and 1128. Has antifungal activity against C.albicans. May have a role in maintaining sterility in the middle ear (PubMed:14996845). May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility (By similarity). SUBCELLULAR LOCATION: Secreted Membrane Note=Associates with tumor cell membrane-derived microvesicles. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MSEVIPSSEYGRLLLENRPLIDVRAPIEFTKGAFGHSINLPLMQDGEREKVGTCYKKRGQEAAIALGHELVKGKVKQQRIDAWLAQLSQHPDSYLYCFRGGLRSKLSQQWIKESGMDIPYIEGGYKAIRSFLINTIEQAPSQSKVLILSGITGSGKTEVIHQRDESVDLEGLANHKGSSFGKNIDPQPSQINFENNLAVALLKHQQQQHNHLLLEDESMLIGRSALPKHFYSAMQQADIIVLDEPLDARLPRLLNDYVEQKLTDYVSGLGEQAGFDAFKAYLAQSLLGIRKRLGGKQHQELQDLVDNALNVQQSQNDTSKHLDWINLLLDIYYDPMYLYQLEKKQDRVIFQGDRQAIHQWLDKHKS", "text": "FUNCTION: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2- selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain. SIMILARITY: Belongs to the SelU family."}
{"protein": "MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF", "text": "FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB. FUNCTION: Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Note=Found predominantly at cell poles. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family."}
{"protein": "MKPYEGLYSFYKILTRTKHVTLEGTGSSDLCRCLSTLDLVALGVGSTLGAGVYVLAGEVAKVDSGPSIIISFLIAALASVLAGLCYAEFGARVPLTGSAYLYSYVTVGELWAFITGWNLILSYVIGTSSVARAWSATFDELVGKKIGNFLGNTMHMDLPGLAEYPDIFAVCLIILLAGLLSFGVKESTAVNKVFTAINILVLLFVIASGCVTGNLKYWKMSKEDLWATKQSVSNHSIGNETGLDFGAGGFMPFGFSGTLAGAATCFYAFVGFDCIATTGEEVKNPQKSIPLGIVLSLSICFFAYFGVSASLTLMMPYHLLDSQSPLPAAFEYVGWNVAKYIVAVGSLCALTTSLLGSMFPMPRILFAMARDGLLFQPLSRVSSRQSPVIATIVSGVVAALMAFLFNLKALVDMMSIGTLLAYTLVSTCVLLLRYQPQTDFGKSPDGNLQEQNISSISHLPETPSVHSSALVTRCVIAITLLVCVASVVSTVGSQCLLSGRAWCLSLLVLSLLGIIIALVIIWRQPQNQSKATFMVPFVPVLPVVSILVNIYLMVQLSTDTWLRYAVWMAVGFVIYFGYGIRHSIERLHLKETCTQKMAISSTETLCKAQCLELQLGEAKPMD", "text": "FUNCTION: Low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family."}
{"protein": "MLKQVTPLVLIAAVTACSSPVERRQANGGDEYTNVKVQPALTIPEGLNAPTYSKEFDIPKLNSKADDKLVGKLLDIRPPLQVLPMAEGTHVEESGDSIKIVVESIDKDVDLKQELYTVLNNYLASQSINVLSEDYDKGLIETDWIENEEVIDSSFWGSDEIYQLRQRYQFEVDVRPHGRSGNIAINLIDHEESFDGKQQNILLSGEDKRRYTIDMLNNAVAYMSVKRSQAIKAKRLRESLGIDVNVVKGAPATVEGEAAEQSYWLADAPFERTWDRLRIVLPEMGFEIVDMDSNKGLYYINVNDDSGFWSSLWSEKKLPVEEGSYRMLLKEGDSEDKTRIYLHNSEDKPLDNVVVEAVYEGFSELMQEDRKIR", "text": "FUNCTION: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the BamC family."}
{"protein": "MKKTPLLNSSICEVVSKMGHTDMIAIGDSGLPIPDDTKRIDLALIKGVPTFMQTLKAVLLEQQVEEVIIAHETKEVSPETFENIKKEIGDVKITFISHEELKKELSNCKAVIRTGEQTPYANIILKSGVVF", "text": "FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RbsD / FucU family. RbsD subfamily."}
{"protein": "MPEFQLQRRLAADIAGVGLNNIKFNPERLEEVEEALTREDIKKLIKERAVIVNPKRGISSGRLKERKHKRRSKGEGRKHGSRKGKSGARTGDKEIWINKIRKIRRYIRWLRDNNVIDKHTYRLLYKRAKGNYFKNLSDVKSYLRQMGHKV", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family."}
{"protein": "MSNIYIQEPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEFHSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLTEVDIDDEERPRNPHRIKSCEVLFNPFDDIIPREIKKPKKEKAEEEIKKLKPKGTKNFSLLSFGEEAEEEEEEVNRVSQSMKGRSKSSHDLLKDDPHLSSVPAVESEKDDATGDLEDDAEDDSVEHDGSMEEDEKNLMRERIAKRLKKDASANVKSAGDGEKKPASRSEELRKEARQLKRELLAAKQKKESATKAEKGSEEEEAVPDGPVAEYRREKQKYEALRKQQPKKGTSREDQTLALLSQFKSKLTQAITEMPENCAEAEVEDDEGWMSHVLQFEDKTRKVKDASMQDSDTFEIYDPRNPVNKRRREESKKLLREKKERR", "text": "FUNCTION: As part of the spliceosome, plays a role in pre-mRNA splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
{"protein": "MERLLIVNADDFGLSKGQNYGIIEACRNGIVTSTTALVNGQAIDHAVQLSRDEPSLAIGMHFVLTMGKPLTAMPGLTRDGVLGKWIWQLAEEDALPLEEITQELASQYLRFIELFGRKPTHLDSHHHVHMFPQIFPIVAKFAAEEGIALRIDRQPLSNDGDLPANLRSSQGFSSAFYGEEISEALFLQVLDDSSHRGERSLEVMCHPAFVDNTIRQSAYCFPRLTELDVLTSASLKYAIAERGYRLGSYHDV", "text": "FUNCTION: Involved in the degradation of chitin. ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YdjC deacetylase family. ChbG subfamily."}
{"protein": "MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQEQQEQDKKKKSNH", "text": "FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1A family."}
{"protein": "MGSLFRSETMCLAQLFLQSGTAYECLSVLGEKGLVEFRDLNQNVSSFQRKFVGEVKRCEELERILAYLVQEINRADIPLPEGDTSPPAPPLKQVLEMQEQLQKLEVELREVTKNKEKLRKNLLELIEYTHMLRVTKTFVKRNVEFEPTYEEFPPLENESLLDYSCMQRLGAKLGFVSGLINQGKVEAFEKMLWRVCKGYTIVTYAELDEPLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHVYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVYSRVIQVKKMKAIYHMLNMCSFDVTNKCLIAEVWCPEADLHELRRALEEGSRESGGTIPSFMNTIPTKETPPTLIRTNKFTEGFQNIVDAYGVGSYQEVNPALFTIITFPFLFAVMFGDFGHGFVMFLFALLLVLNENHPRLNQSQEIMRMFFNGRYILLLMGLFSVYTGLIYNDCFSKSVNLFGSRWNVSAMYSSSHSPEEQRKMVLWNDSIVRHHSVLQLDPSVPGVFRGPYPFGIDPIWNLATNRLTFLNSFKMKMSVILGITHMTFGVILGIFNHLHFRKKFNICLVSIPELLFMLCIFGYLIFMIIYKWLVYSAETSRTAPSILIEFISMFLFLASDTGGLYPGQEHVQRLLLLITVLSVPVLFLGKPLFLLWLHRGRSCFGVGRSGYTLVRKDSEEEVSLLGGQDIEEGNNQMEDGCREVTCEEFDFGEILMTQIIHSIEYCLGCISNTASYLRLWALSLAHAQLSEVLWAMLMHVGLRVDTAYGVLVLLPVIAFFAVLTIFILLIMEGLSAFLHAIRLHWVEFQNKFYVGAGTKFVPFSFRLLSSKFSDDLA", "text": "FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery (By similarity). May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endosome membrane. SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family."}
{"protein": "LEVLLGSGDGSLVFVPSEFSVPSGEKIVFKNNAGFPHNVVFDEDEIPAGVDAVKISMPEEELLNAPGETYVVTLDTKGTYSFYCSPHQGAGMVGKVTVN", "text": "FUNCTION: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Loosely bound to the inner thylakoid membrane surface in chloroplasts (PubMed:1920431). SIMILARITY: Belongs to the plastocyanin family."}
{"protein": "MAAVRGLRISVKAEATATTAEPRGPEPEPMEVEEGELETIPVRRSLRELIPDTSRRYENKAGSFITGIDVTSKEAIEKKEQRAKRFHFRAEVNLAQRNVALDRDMMKKAIPKVRLDTIYICGVDEMSTQDIFAYFKEYPPAHIEWLDDTSCNVVWLDEVTATRALINMSSFPDQEKPKGGENNEEKTAEKNKKEKQEESTDDETEEGEVEDENPSDIELDALTQVEEDSLLRNDLRPANKLAKGNKLFMRFATKDDKKELGAARRSQYYMKYGNPNYGGMKGILSNSWKRRYHSRRIHRDVIKKRTLIGDDVGLTPPYKHRHSGLVNVPEEPIEEEEEEEEVQDMDEDDRVVVEYRDDLQPFKQSRDRGAARRSSASASDSDEMDYDLELKMISTPSPKKSMKMTMYADEVESQLKNIRNSMRADSIATSNVKNRIGSKGLSDKVVDVRLLLEEKRQNNNGLRQPNSIVKSDVRQRLGKRPHSPEVKPPSSISAPRREPISDVHSRLGIPKQDVKGLYSDTREKKSGNLWTRLGSAPKTQEKTSDKPENSVASPEEDDSELQRVWGALIKEKGESRQKKSRLDNLPSLQIEISRESSSGSDTES", "text": "FUNCTION: Associates with NCBP1/CBP80 to form an alternative cap- binding complex (CBC) which plays a key role in mRNA export. NCBP3 serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA) to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus, the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role in only mRNA export. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the NCBP3 family."}
{"protein": "MNSNVENLPPHVIRQVYKEVSTLTPDPPEGIKIIPNEEDITDVQVSIEGPEGTPYAGGIFRMKLILGKDFPAAPPKGYFLTKIFHPNVSSNGEICVNVLKKDWKAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYASRARLMTEIHAHSSSLRGKDPTDPCSSASVTGALGDGPMAKKHAGDRDKKLAAKKKTDKKRALRRL", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme ube2c/ubch10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MLMPKKNRIAIYELLFKEGVMVAKKDVHMPKHPELADKNVPNLHVMKAMQSLKSRGYVKEQFAWRHFYWYLTNEGIQYLRDYLHLPPEIVPATLRRSRPETGRPRPKGLEGERPARLTRGEADRDTYRRSAVPPGADKKAEAGAGSATEFQFRGGFGRGRGQPPQ", "text": "FUNCTION: Component of the 40S ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. FUNCTION: Component of the 40S ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family."}
{"protein": "MHKLAHISFGIVGMFVNTCMVAKYVIINWEMYSMKKVNNDTVFGILQLETLLGDINSIFSEIESEYKMSREEILILLTLWQKGSMTLKEMDRFVEVKPYKRTRTYNNLVELEWIYKERPVDDERTVIIHFNEKLQQEKVELLNFISDAIASRATAMQNSLNAIIAV", "text": "FUNCTION: Global regulator with both positive and negative effects that mediates modulation of several genes involved in virulence. Also, modulates the expression of genes not previously implicated in pathogenesis (By similarity). SIMILARITY: Belongs to the rot family."}
{"protein": "MRYWYLRLAVFLGALAMPAWWLYQAWIFALGPDPGKTLVDRLGLGALVLLLLTLAMTPLQKLSGWPGWIAVRRQLGLWCFTYALLHLSAYCVFILGLDWGQLGIELSKRPYIIVGMLGFICLFLLAITSNRFAMRKLGSRWKKLHRLVYLILGLGLLHMLWVVRADLEEWTLYAVVGASLMLLRLPSIARRLPRLRGRPGVS", "text": "FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MsrQ family."}
{"protein": "MPELPEVETVKRTLTELVIGKTIAGITVKWANIIKEPADVLEFETLLMNQTIRSIRRRGKFLLFEFDDIVMVSHLRMEGRYGLYEKEEPLPPHTHVIFHFTDGEELRYQDVRKFGTMHLFPKGSEEKVLPLAHLGVEPFSEQFTSELLMNAFQKTNRKIKVALLDQKTVVGLGNIYVDEALFRARIHPERLAHSLSKEEMAVLHKAIVSTLEEAVEMGGSSIKSYVNGQGEMGMFQQKLGVYGRKNEPCRQCGTDILKTVVGGRGTHFCPNCQL", "text": "FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity). SIMILARITY: Belongs to the FPG family."}
{"protein": "MKDKAYDITIIGGGPIGLFAAFYAGLRGVTVKIIESLSELGGQPAILYPEKMIYDIPAYPSLTGVELTENLIKQLSRFEDRTTICLKEEVLTFDKVKGGFSIRTNKAEHFSKAIIIACGNGAFAPRTLGLESEENFADHNLFYNVHQLDQFAGQKVVICGGGDSAVDWALALEDIAESVTVVHRRDAFRAHEHSVELLKASTVNLLTPYVPKALKGIGNLAEKLVIQKVKEDEVLELELDSLIVSFGFSTSNKNLKNWNLDYKRSSITVSPLFQTSQEGVFAIGDAAAYNGKVDLIATGFGEAPTAVNQAINYIYPDRDNRVVHSTSLID", "text": "SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family."}
{"protein": "MSLSLLLRGAVRCNAANLVKSARITPLKSYSTLVANVQRKAVVQPLAVAKIVAPVVREISVSAPRMASAGSSHTLLWTVERIVSAGLLAVIPAAFIAPSQVLDALMAISVVIHTHWGVEAMVVDYMRPSVVGNVLPKVAHIALIIISVATLGGLFYFIQNDVGLANGIKRFWAIKGKDAEKA", "text": "FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CybS family."}
{"protein": "MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYSSVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRSTLRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCREKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWRTE", "text": "FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal- beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. Prefers O-glycans to glycoproteins or glycolipids. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
{"protein": "MNKQAIQSIVAEVVQQLSQTTKQSNTVPMAVSARHCHLSIEDVEALFGAGYELTKKSDLSQPGQFAANETVTIVGPKGSIEKVRVLGPARSITQVEVSKTDSIKLGAVPPLRESGDIKNSEAITLVGPKGSIYKKEGLIIARAHIHMTPDDAEAYGVKNGQCVRITSQGERPTTLERVLIRVSPKFKLEMHIDTDEANAGLISTGDTGILSLYEEAL", "text": "FUNCTION: Involved in 1,2-propanediol (1,2-PD) utilization within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the PduL family."}
{"protein": "MEKLSNGVRDHCLISDYVSPSAPAPLKQPFVIGVAGGTASGKTTVCNMIMSQLHDQRVVLVNQDSFYHSLTKEKLNKVHEYNFDHPDAFNTEVLLSCMEKLRSGQPVNIPSYDFKIHQSIESSSPVNPGDVIILEGILVLNDPRVRDLMNMKIFVDTDADVRLSRRIQRDTVERGRNIQNVLEQYTKFVKPSFDEYIQPSMKYADIIIPRGGDNDVAIDLIVQHIRTKLCQHNLCKIYSNIFIISSTFQIKGMHTLIRDINTTKHDFVFYADRLIRLVVEHGLGHLPFTEKQITTPTGSVYTGVDFCKRLCGVSVIRSGESMENALRACCNGIKIGKILIHRENNDGRQLIYEKLPKDISSRHVFLLDPVLASGYSAVKAITLLLSKGVPESHIIFLNLIAAPQGIHALCKKFPMLKIVTSEIDSSLNEDSRVIPGLGEFADRYFGTNNINSKVSSLSTNLKLRS", "text": "FUNCTION: Involved in the pyrimidine salvage pathway. SIMILARITY: In the N-terminal section; belongs to the uridine kinase family. SIMILARITY: In the C-terminal section; belongs to the UPRTase family."}
{"protein": "MTLWINGDWVTGQGALRVKCNPVSGELLWQGNDADAAQVGQACRAARAAFPRWARLSFGDRQVRVERFAGLLESNKVELTAIIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTVIFKPSELTPWSGEAVMRLWQQAGLPSGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKILALEMGGNNPLIIDDVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQGDAFLARLVAVSQRLTPGNWDDEPQPFIGGLISEQAAHQVVTAWQELEAMGGRTQLAPRLLRAGTSLLTPGIVEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSSRRDKFEQLLLEARAGIVNWNKPLTGAASTAPFGGVGASGNHRPSAWYAADYCAWPMASLESDSLTLPTTLNPGLDFSEEVER", "text": "FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD subfamily."}
{"protein": "MTKTVSTSKKPRKQHSPEFRSEALKLAERIGVTAAARELSLYESQLYNWRSKQQNQQTSSERELEMSTEIARLKRQLAERDEELAILQKAATYFAKRLK", "text": "FUNCTION: Involved in the transposition of the insertion sequence IS3. FUNCTION: Involved in the transposition of the insertion sequence IS3. SIMILARITY: Belongs to the transposase 8 family."}
{"protein": "MVCLKLPGGSCMTALTVTLMVLSSPLALSGDTRPRFLWQPKRECHFFNGTERVRFLDRYFYNQEESVRFDSDVGEFRAVTELGRPDAEYWNSQKDILEQARAAVDTYCRHNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFLNGQEEKAGMVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS", "text": "FUNCTION: Allele DRB1*07:01: Upon EBV infection, presents latent antigen EBNA2 peptide (PRSPTVFYNIPPMPLPPSQL) to CD4-positive T cells, driving oligoclonal expansion and selection of a dominant virus- specific memory T cell subset with cytotoxic potential to directly eliminate virus-infected B cells (PubMed:31308093). May present to T- helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (VPYVNAVPMDSMVRHNNWSL), contributing to viral clearance (PubMed:27591323). In the context of tumor immunesurveillance, may present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (MTEYKLVVVGAVGVGKSALTIQLI), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:22929521). In metastatic epithelial tumors, presents to intratumoral CD4-positive T cells a KRAS neoantigen (MTEYKLVVVGAVGVGKSALTIQLI) carrying G12V hotspot driver mutation and may mediate tumor regression (PubMed:30282837). FUNCTION: Allele DRB1*03:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance (PubMed:27591323). Displays self- peptides derived from retinal SAG (NRERRGIALDGKIKHE) and thyroid TG (LSSVVVDPSIRHFDV) (PubMed:25413013). Presents viral epitopes derived from HHV-6B gH/U48 and U85 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection (PubMed:31020640). Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and long-term protection (PubMed:19830726). FUNCTION: Allele DRB1*13:01: Presents viral epitopes derived from HHV- 6B antigens to polyfunctional CD4-positive T cells implicated in control of HHV-6B infection. FUNCTION: Allele DRB1*04:01: Presents an immunodominant bacterial epitope derived from M. tuberculosis esxB/culture filtrate antigen CFP- 10 (EISTNIRQAGVQYSR), eliciting CD4-positive T cell effector functions such as IFNG production and cytotoxic activity (PubMed:15265931). May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance (PubMed:27591323). Presents tumor epitopes derived from melanoma- associated TYR antigen (QNILLSNAPLGPQFP and DYSYLQDSDPDSFQD), triggering CD4-positive T cell effector functions such as GMCSF production (PubMed:8642306). Displays preferentially citrullinated self-peptides derived from VIM (GVYATR/citSSAVR and SAVRAR/citSSVPGVR) and ACAN (VVLLVATEGR/ CitVRVNSAYQDK) (PubMed:24190431). Displays self- peptides derived from COL2A1 (PubMed:9354468). FUNCTION: Allele DRB1*04:02: Displays native or citrullinated self- peptides derived from VIM. FUNCTION: Allele DRB1*04:05: May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. FUNCTION: A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA- DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:29884618, PubMed:22327072, PubMed:27591323, PubMed:8642306, PubMed:15265931, PubMed:31495665, PubMed:16148104). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor- resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819). FUNCTION: Allele DRB1*01:01: Displays an immunodominant epitope derived from Bacillus anthracis pagA/protective antigen, PA (KLPLYISNPNYKVNVYAVT), to both naive and PA-specific memory CD4- positive T cells (PubMed:22327072). Presents immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (PHQFINLRSNNSATLIVPYV), contributing to viral clearance (PubMed:27591323). Displays commonly recognized peptides derived from IAV external protein HA (PKYVKQNTLKLAT and SNGNFIAPEYAYKIVK) and from internal proteins M, NP and PB1, with M-derived epitope (GLIYNRMGAVTTEV) being the most immunogenic (PubMed:8145819, PubMed:9075930, PubMed:25413013, PubMed:32668259). Presents a self- peptide derived from COL4A3 (GWISLWKGFSF) to TCR (TRAV14 biased) on CD4-positive, FOXP3-positive regulatory T cells and mediates immune tolerance to self (PubMed:28467828). May present peptides derived from oncofetal trophoblast glycoprotein TPBG 5T4, known to be recognized by both T-helper 1 and regulatory T cells (PubMed:31619516). Displays with low affinity a self-peptide derived from MBP (VHFFKNIVTPRTP) (PubMed:9075930). FUNCTION: Allele DRB1*05:01: Presents an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load. FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr virus on lymphocytes. FUNCTION: Allele DRB1*15:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SNNSATLIVPYVNAVPMDSM), contributing to viral clearance (PubMed:27591323). Displays a self- peptide derived from MBP (ENPVVHFFKNIVTPR) (PubMed:9782128, PubMed:25413013). May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. FUNCTION: Allele DRB1*11:01: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SDRIIQITRGDSTITSQDVA), contributing to viral clearance (PubMed:27591323). Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and longterm protection (PubMed:19830726). In the context of tumor immunesurveillance, may present tumor-derived neoantigens to CD4-positive T cells and trigger anti-tumor helper functions (PubMed:31495665). FUNCTION: Allele DRB1*15:02: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:19120973). FUNCTION: Allele DRB1*04:04: May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (HIVMQYMYVPPGAPIPTTRN) and VP2 (RGDSTITSQDVANAVVGYGV), contributing to viral clearance (PubMed:27591323). Displays preferentially citrullinated self-peptides derived from VIM (SAVRAR/citSSVPGVR) (PubMed:24190431). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Late endosome membrane; Single-pass type I membrane protein Autolysosome membrane Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation (PubMed:18305173). Component of immunological synapses at the interface between T cell and APC (PubMed:29884618)."}
{"protein": "MKRFLLCSFALVLLYPAGIDMYLVGLPRIAADLNASEAQLHIAFSVYLAGMATAMLFAGKIADQSGRKPVAIVGAIVFMMASLLCSRASEGSLFLSGRFLQGIGAGGCYVVAFAILRDTLDEHRRAKVLSLLNGITCIVPVLAPVVGHLIMLRFPWQSLFYTMSAMGIIVGLLSLFILRETRPVRLAPRDLSRSSPAAESLINRFFVSRLAITTLSVSVILTFVNASPVLLMEVMGFSRGDYAITMALTAGVSMVVSFSTPFALGLFKPRTLMLVSQGLFLTAGVTLSLAHTNTVTLFGLTLICAGFSVGFGVAMSQALGPFSLRAGVASSTLGIAQVCGSSLWIWLAAILGISAMNMLIGILIGCSIVSILLIFSVTPNRSVAEHEEIPYQSRP", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. MdtL (TC 2.A.1.2.22) subfamily."}
{"protein": "FLGTINLSLCEQERDADEEERRDEPDESDVEVEKRFLPIVTNLLSGLLGK", "text": "FUNCTION: Amphipathic alpha-helical peptide with no antimicrobial activity (PubMed:18584916, PubMed:18795798). Does not display anti- leishmania activity (PubMed:18584916). Does not show hemolytic activity (LC(50)>116 uM) (PubMed:18584916, PubMed:18795798). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
{"protein": "MTHISNNRPRIAVIGGGIAGLTVAASLLRAGIECTVYEQATVFADAGAGIQIAPNSARILHRLGLAGALERRATRAHAIETRRWQDGAPLARTELGEPCVERYGAPYYLIQRADLHRSLLELLPPGVVRHSAACTAVEERPDGVTLRFADGTSEEAGVVVGADGIHSALRNHLVGDRPRFSGHTVHRGLVAADRLPSLFEVPKVLFWLGPNGHVTSYPIAQHGLVHFSAVITSPEWDPEVWSAPSRPGEAAAAFAGWNAEVAELIGAAEQAHHWALFDRDCVGGWSTGRMTLAGDAAHPMVPYLSQGANQAIEDAWVLADLLGAADLDPGPALRRYEELRLPRVREVHRRSRERGHEFHLPDGPQQRLRDRSMPTAERLDDYAWIYGFEAAPVGSR", "text": "FUNCTION: Part of a gene cluster involved in the biosynthesis of thioplatensimycin (thioPTM) and platensimycin (PTM), potent and selective inhibitors of bacterial and mammalian fatty acid synthases (PubMed:21825154, PubMed:29915173). Catalyzes the hydroxylation of 3- amino-4-hydroxybenzoate (3,4-AHBA) to 3-amino-2,4-dihydroxybenzoate (3,2,4-ADHBA) (Probable). SIMILARITY: Belongs to the 6-hydroxynicotinate 3-monooxygenase family."}
{"protein": "MATCWQALWAYRSYLIVLCLPIFLLPLPLIVQTKEAYCAYSIILMALLWCTEALPLAVTALFPIILFPLMGIMEASKVCLEYFKDTNILFVGGLMVAIAVEHWNLHKRIALGVLLIIGVRPALLLLGFMLVTAFLSMWISNTATTAMMLPIGYAVLEQLQGSQKDVEEGNSNPSFELQEASPQKEETKLDNGQAVSVSSEPRAQKTKEHHRFSQGLSLCICYSASIGGIATLTGTTPNLVLQGQVNSIFPENSNVVNFASWFGFAFPTMVILLLLAWLWLQVLFLGVNFRKNFGFGEGEEERKQAAFQVIKTQHRLLGPMSFAEKAVTFLFVLLVVLWFTREPGFFPGWGDTAFANKKGQSMVSDGTVAIFISLIMFIIPSKIPGLTEDPKKPGKLKAPPAILTWKTVNDKMPWNILILLGGGFALAKGSEESGLSKWLGDKLTPLQHVPPSATVLILSLLVAIFTECTSNVATTTLFLPILASMAQAICLHPLYVMLPCTLAASLAFMLPVATPPNAIVFSFGGLKVSDMARAGFLLNIIGVLTITLSINSWSIPIFKLDTFPTWAYSNTSQCLLNPPNSTVPGH", "text": "FUNCTION: Low-affinity sodium-dicarboxylate cotransporter, that mediates the entry of citric acid cycle intermediates, such as succinate, citrate, fumarate and alpha-ketoglutarate (2-oxoglutarate) into the small intestine and renal proximal tubule (PubMed:10966927) (By similarity). Can transport citrate in a Na(+)-dependent manner, recognizing the divalent form of citrate rather than the trivalent form which is normally found in blood (PubMed:10966927). Transports the dicarboxylate into the cell with a probable stoichiometry of 3 Na(+) for 1 divalent dicarboxylate, rendering the process electrogenic (By similarity). Has a critical role in renal dicarboxylate transport (PubMed:17410095). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. NADC subfamily."}
{"protein": "MSSPPLHGLSSVGHLSRDPPPRSWSPRDKCSYLGLSHGNLRVHYKGHGKTSKDAASVRSTHPIPAACGIFYFEVKIISKGRDGYMGIGLSTQGVNLNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLIDNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFGQSPFVFDIEDYIREWRSKIQAQIERFPVAGEWQSMIQRMVSSYLVHHGYCSTAEAFAKSTDQTVQEELASIKNRQRIQKLVLSGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGNRSLKSPDGCLGSDSNCSNGIISNKAHQTHCHSKSQSSNLNVTELNSINMTMSHQLNSYSSNDVEMETDHYSNGFSASTSNGFLNGSSRHEPELEECDTEMEVDTSHGRRQLCGGSQAAVERMICFGRELQAMSEQLRRERGKNATNKNMLKDAFSLLAYSDPWNSPVGYQLDPIQREHVCSSLNSAILDIHNLPKQPPLSLALEQASQCLEMMAQCGIGSCAFARVADYLH", "text": "FUNCTION: May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways. Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that mediates ubiquitination and subsequent proteasomal degradation of target proteins. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Nucleus Note=Predominantly cytoplasmic. SIMILARITY: Belongs to the RANBP9/10 family."}
{"protein": "MKITKLEKKKRLYLMELDNGDKCYITEDTIVRFMLSRDKVISEEELKEIQDFAQFSYGKNLALYHLSFKARTEKEVREYLKKYDIDENIVSQVIANLKEDKWINDGQYAYAIINTNQLSGDKGPYVLTQKLAQKGISKSTIEENLKEFDFSEVAQRVANKLLKKYEGKLPARALQDKIIQNLTNKGFSYSDAKIAFDDLDSQVEQETTQELIFKELDKQYTKYARKYEGYELKQRLTQVLARKGYDFSDIASALREYL", "text": "FUNCTION: Modulates RecA activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecX family."}
{"protein": "MYQSKKVLLLGSGELGKEVVIEAQRLGVQTVAVDSYEHAPAMQVAHNSYVVDMLDPEQIRTIIEKENPDLIVPEVEAIATDELLKLEEEGFHVIPNARAAKLTMDREGIRRLAAETLGLATAGYEFANTYDEFIQAAAQIGFPCVVKPLMSSSGKGQSVCRSEADLESCWETAMEGGRVKNGRVIVEEFIPFESEITLLTVRAVNGTAFCEPIGHVQKDGDYIESWQPHDMTEQQIEEAKHIAKTITDELGGYGLFGVELFLAKDRVYFSEVSPRPHDTGLVTLVTQNLSEFALHVRAILGFPITEITQLSPGASRPLKAPEELADYTVEGLENALAVPKTQVRVFGKPITKAGRRMAVALSAADSVETARENAKKALDQLILK", "text": "FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. FUNCTION: Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP. SIMILARITY: Belongs to the PurK/PurT family."}
{"protein": "MMENYITSFQLRFCPAAYLHLEQLPSLWRSILPYLPQWRDSAHLNAALLDEFSLDTDYEEPHGLGALPLQPQSQLELLLCRLGLVLHGEAIRRCVLASPLQQLLTLVNQETLRQIIVQHELLIGPWPTHWQRPLPTEIESRTMIQSGLAFWLAAMEPQPQAWCKRLSLRLPLATPSEPWLVAESQRPLAQTLCHKLVKQVTPTCSHLFK", "text": "FUNCTION: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function. FUNCTION: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function."}
{"protein": "MRTTNVWLVVIVWVTVGWSSCTGRFVVEKNNLRVTSPESIRGVYECALGNFGVPQYGGSMSGAVVYPKTNQKACKNFDDFEISFRSRVAGLPTFVLVDRGDCYFTLKAWNAQRAGAATILVADNRPEQLITMDAPEDETSDADYLQNITIPSALVSRSLGSAIKTAIAHGDPVHISLDWREALPHPNDRVAYELWTNSNDECGSKCDAQIRFLKRFKGAAQILEKGGYTRFTPHYITWYCPEAFLASRQCKTQCINGGRYCAPDPEQDFSRGYNGKDVIIQNLRQACFFRVTNESGKPWLWWDYVTDFAIRCPMKEEKYNKKCADQVIQSLGVDVKKIDKCIGDIDANAENPVLKEEQVAQVGKGSRGDVTILPTIVINNRQYRGKLQRSAVLKALCSGFRETTEPPICLTEDIETNECLQNNGGCWEDKTTNITACRDTFRGRVCQCPIVQGVKFLGDGYTHCEASGALRCGINNGGCWKQTQMGKTYSACRDDHSKGCKCPPGFIGDGLKECKDVNECEEKTACQCRDCKCKNTWGSYECSCSGSLLYIREHDICINRDARGDFSWGVIWIIIMGLGAAALGAYTVYKYRIRTYMDSEIRAIMAQYMPLDNNPNTQLSSQLEL", "text": "FUNCTION: Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Golgi apparatus membrane; Single-pass type I membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type I membrane protein Prevacuolar compartment membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the VSR (BP-80) family."}
{"protein": "MKVAILGAGCYRTHAASGITNFSRAAQVAKEVGIPEITMTHSTITMGAELLHLIPEITEVVVSDPCFAEEPGIVVLDQFDYKTVMEAHLAGDAEKVMPEIREAVKAKAKETPKPPKGCIHFVHPETIGLKVTASDVEAVKNADIVITWLPKGGSQPAIIEKFVGAIKKGAIVTHACTIPTPKFAKIFKDMGRDDLNIIAYHPGAVPEMKGQAFLSEGLADAEKVEEFYCMAKTARGEAFKMPANLISPVCDMGSAVTAPVYAGILAYRDAVTQILGAPADFAQMMADEAITQLLELMRSEGIKNMEDKLNPKALTGTADSMCFGPLADILPTSLKVLEKHTNENKCECSCSIKP", "text": "FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT. SIMILARITY: Belongs to the HMD family."}
{"protein": "MKILTKFFLLLVVTTCSLHYYCQIGQCSTQLQRVCHYTTPSVWDELLVEKNEFYREQLNPKVKVLKSHISQINSHYQDKVLPKLVDLGNRFYFDIVSPRIDNVCEFWEEFELKPYRERSLNQIRKVRQRIWFYYSVYLKPNLTKLDNQYALSDKYGKVHNKIAPFVAEIAQNFQNVYHQAAAKVHPHWENLRRTVNAKWEPISSSLWQRCRTNEICFKTNAQLKNIWKNLKLGCDYLSIYVHDALSPYSDGLESNVRATKAKSKSKPRVNASASARGNARAGAKAGAKAGTSEISASATADPTTSASATVTAGFEDDYDDEEPLYTSTSTIMLTVTMSTDQNELSPSQNTANAELGISEQDAIKDEFEAWFKVVDQKSSGVVKTFNKEVNKYLHHRVQQLDSIFQNKTKTVSEVLQNRYKNLNRAIQDINCTCETDTGAGNQTCFDSTGTTQLSEYITRSKMRELFAEAHSTLDQSMLQLKQDLEPIAQEVESRVSLIREEMVEVYEEWGDAMVSEWSKRLAYIDVVAGHLDDNGASTDEESSENWRKFLNLKKQVIKARDELAEHPADLHEIKQFVKKVHYLIEVLAKEAGEYLYILRARANLAFQAREQESKQREDSPRMDRDSTQNVENSNTTTASAEKSGKKAKKVKRVAQNGTNSTEKFSAGPDSSSKEPSMETTVQNNVTLQI", "text": "FUNCTION: Involved in spore wall assembly. May be a component of the mitochondrial RNase MRP (MtMRP), a ribonucleoprotein endoribonuclease involved in the cleaving RNA transcripts to generate primers for DNA replication in mitochondria. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the SHE10 family."}
{"protein": "MQKASTSAGAKTAGNRKMQKSPNNGAAKAQKSAKTVDTVTDSELLYNPPAFLTAAEKERRKYLQARVRAEGESASTSSKSNATRPTDRKRHLQAEDPLPADANNNDTNKGGKVAQESASTQAAGTTKRKQPRSQGLEQTSPIMVNGEALACPLVRKSLPAAEAAKSCPLPSKKDSVTKSPMTVHEAPKVDSATSNSNEKQLATMPVDIHKTDSIEEGRRVLEWLINPVAVNQFFADFWENNACVVQRKNPNYYSKLMSFKMIDDILMRNRVEFGTNLDVTIYRNGKRETLNPEGRAFPSVVWDFYAEGCSIRILNPSTYLLGLRQVCSIMQEFFHCLVGANVYLTPPNSQGFAPHYDDIEAFVIQVEGRKRWRLYEPPEKADQLSRTSSGNYDQKQLGEPIIDEVLEAGDLLYFPRGTVHQAITEKGHFSLHITLSVYQQQAYANLLETLMPIVLKKAVKKSVALRRGLPLHTFHVLGEVQRTNRCESRDQLVENVQKLVSKYLMPSTQDIDEAVDQLAKKFQHEALPPIILPEEKVRTVFGSRSISDQEGNSVCDYEFDTDTSVRLLRANILRLVNEDDGSVKIYHHVNNALEYCKYEPNFLEILQEEAIAVEVLISAYPYYITVDQLPLKTVARKVEVATALWEHGLLMTEKPFK", "text": "FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys- 4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ROX family. NO66 subfamily."}
{"protein": "MTCCNQQSSQPKTTTNCAESSCYKKTWSDHRGTRIERGCGCPQVKPGIKLECCHTNECNN", "text": "FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type I alpha-neurotoxin sub-subfamily."}
{"protein": "MAAATQFLSQPSSLNPHQLKNQTSQRSRSIPVLSLKSTLKPLKRLSVKAAVVSQNSSKTVTKFDHCFKKSSDGFLYCEGTKVEDIMESVERRPFYLYSKPQITRNLEAYKEALEGVSSVIGYAIKANNNLKILEHLRSLGCGAVLVSGNELRLALRAGFDPTKCIFNGNGKSLEDLVLAAQEGVFVNVDSEFDLNNIVEASRISGKQVNVLLRINPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDQVKAHPKELKLVGAHCHLGSTITKVDIFRDAAVLMIEYIDEIRRQGFEVSYLNIGGGLGIDYYHAGAVLPTPMDLINTVRELVLSRDLNLIIEPGRSLIANTCCFVNHVTGVKTNGTKNFIVIDGSMAELIRPSLYDAYQHIELVSPPPAEAEVTKFDVVGPVCESADFLGKDRELPTPPQGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITKIRHAETFDDHLRFFEGL", "text": "FUNCTION: Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily."}
{"protein": "SVIELGKMILQETGKNPVTHYGA", "text": "FUNCTION: Snake venom phospholipase A2 homolog that lacks catalytic activity (By similarity). Shows myotoxic activities (By similarity). Induces local edema a few hours after injection (5-10 ug) in the hind paw (PubMed:12959640). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily."}
{"protein": "MNKANMLRTDKDMQIILFSEVSVGISANSILFIAHVCMILGENRPKPIDLYIAFLSLTQLMLLITMGLIAVDMFLSQGIWDSTTCQSLIYLHRLLRGLSLCATCLLNILWTITLSSRSFCSTKFKHKSPHHISGAFIFFCVLYMSFSSHLFISIIATHNLTSENFIYVTQSCSLLPLSYSRTSMFSAPMAIREAFLVSLMALSSGYMVALLWRHKKQAQHLHSTSLSSKASPEQRATRTILLLMSFFVVLYILENAVFYSRIKFKDGSILYCVQIILCHSYATVNPFVFICTEKHIIKFWESKCGRIVNI", "text": "FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MCRRAEDLVLLLIPILFGYFSHASEHECKCVLFNVTSGNFHSPEFPAPLEGVPCLFYHFQAPPDHIIRLTFDVFQLPPRIGVCSSSIMLFDHSTDGLIEFGERADFEFCGKEISSGRQFFSKDQHFLLQISSGKESSRGFRGSFLAIPKKNFTSDAVEMAECSYRVEKQKAIIYSPDYPYYYPSKVNCTYHIPQRKGFQIVVNSIVMDIGRDAILQIFESVEGKFEKRLIEMVTSVQKSIYVSSTSSLLIYFSAGNNDVERAVGFVIELQYSNAVWSQSPETASECQLNINSENFKEGQLSSDKIGRFTSSSLPTKCQIVLQGYPNEKISVKFTHFNLYVPDNKNVTKRCTEVDNLSADVRVGSRLSRIDEWCGKRAPPNLMSSSNLLQLEYNTKSSKAIRESTNDDIGFRLDYKFHTDWNMGNMKAKVDKKKECRFSFNSSEHTNGKLWSANYPGLYPRNLYCEYIFHGRNDQVVHIHFEYFDIEGFNQCDETTQSDYILFSNYQTHDRTNRRFCGKTAPKGPILSESNYFRMIFSTNDIFDATGFYAHYQFITQEKSQISRVKLTISSSQTPFSSFFLVILLFTFRYIANIF", "text": "FUNCTION: Accessory protein required for glutamate-gated currents. May participate in the gating of non-NMDA (N-methyl-D-aspartate) ionotropic glutamate receptors such as glr-1. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Single- pass type I membrane protein Synapse Note=Colocalizes with glr-1 at the cell surface. Enriched at postsynaptic membranes."}
{"protein": "MHQLFRLVLGQKDLSKAGDLFSLDDAEIEDSLTEALEQIKVISSSLDYQTNNNDQAVVEICITRITTAIRETESIEKHARALVGLWDSCLEHNLRPAGKDEDTPHAKIASDIMSCILQNYNRTPVMVLAVPIAVKFLHRGSKELCRNMSNYLSLAAITKADLLADHTEGIIKSILQGNAMLLRVLPAVYEKQPQPINRHLAELLALMSQLEQTEQYHLLRLLHVAAKRKDVEVVQKCVPFLIRNLKDSTYNDIILNILIEIAGHEPLALNSFLPMLKEIAEQFPYLTGQMARIFGAVGHVDEERARSCLRYLVSQLANMEHPFHHILLLEIKSITDAFSSILGPHSRDIFRMSNSFTNIAKLLSRQLENSKADSSRRKTSTEVSIPEKLRELNSMEPESEDHEKLQVKIQAFEDKINAESNTPGSGRRYSLDHISKEERKSIRFSRSRSLALNTVLTNGVSVEDNEVEEKAGMHASISLSQIDPLSHGIGKLPFKTDTHGSPLRNSSASHPSIIHTEPETMPETFKENIQEEILEAATSPIEYQDKLYLHLRENLSKVKAYALEIAKKVPIPDQCTIEDTMRSCVAKLFFTCSLKGHYCLYSKSSFILVSQAPQPWIQVMFLSQQSLFPEPLSIQSGSVQFLKALWEKTQDTGAHSFEVAMTESTFPQQKDLEQLQLHLEEVRFFDVFGFSETAGAWQCFMCNNPEKATVVNQDGQPLIEGKLKEKQVRWKFIKRWKTHYFTLAGNQLLFQKGKSKDDPDDSPIELSKVQSVKAVAKKRRDRSLPRAFEIFTDSKTYVFKAKDEKNAEEWLQCINVALAQAKERESREVTTYL", "text": "FUNCTION: Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits dissociation of activated SMAD2 from TGFBR1, impeding its nuclear accumulation and resulting in impaired TGF-beta signaling. May also affect FOXO, Hippo and Wnt signaling. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the MELT/VEPH family."}
{"protein": "MRLLTRRAGHGAATLALRVIHMQRVPVLRLPAILDMERKIPSRESPRRLSAKPGRGTEMKKLARPLGVVAADSDKDSGFSDGSSECLSSAEQMESEDMLSALGCKREDKRRQPSKAADTALPTLPPMVVMKSVLVKQGSSSSQLQSWTVQPSFEVISAQPQLFVLHPPVPSPVSSCQTGEKKSESRNYLPILNSYTKIAPHPGKRGLNSEDRGTSGVSKKLCTERPGPSLSSSEPAKTGRVLSSPSTPAPPSSKLTEDSTLQGVPSLGAGGSPQTLQPVSSSHVAKAPSLTLASPASPVCASDSTLHGLESSSPLSPLSASYTSPLWAAEHLCRSPDIFSEQRQNKHRRFQNTLVVLHKSGLLEITLKTKELIRQNQATQAELDQLKEQTQMFIEATKSRAPQAWAKLQASLTSGSSHSGSDLDTLSDHPDV", "text": "FUNCTION: Transcriptional repressor which may act as a negative- feedback regulator of CLOCK-BMAL1 transcriptional activity in the circadian-clock mechanism. May stimulate BMAL1-dependent phosphorylation of CLOCK (PubMed:17310242, PubMed:19414601). However, the physiogical relevance of these observations is unsure, since experiments in knockout mice showed that CIPC is not critially required for basic circadian clock (PubMed:25862660). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Predominantly localizes to the nucleus, where it co-localizes with CLOCK. At the G1/S boundary, partially translocated to the cytosol."}
{"protein": "MKFLLFCCLFGTFLATGMCIDCEHCVVWGQNCTGWKETCGENEDTCVTYQTEVIRPPLSITFTAKTCGTSDTCHLDYVEANPHTELTLRAKRACCTGDECQTLPPPVLEPQVNRPNGLQCPGCIGLTSTECNEYLVSCQGSENQCLTIILKKPDFSLSEMSFKGCASENLCLLFEKKFWRFLEASEVDVKCTPAVPQTSQ", "text": "FUNCTION: Inhibits the enzymatic activity of phospholipase A2 (PA2). SUBCELLULAR LOCATION: Secreted Note=Secreted in blood plasma. SIMILARITY: Belongs to the CNF-like-inhibitor family."}
{"protein": "MPEQVQHGEDEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDTGKDLKIDIVPNPRDPTLTLLDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRTDHGEPIGRGTKVILYLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVEKEREKEVSDDEAEEEKVEKEEEESKDEEKPKIEDVGSDEEEEEGEKSKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFTELAEDKENYKKFYEAFSKNLKLGIHEDSTNRKRLSELLRYHTSQSGDEMTSLSEYVSRMKESQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKTLVSVTKEGLELPEDEEEKKNMEESKAKFETLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKADANKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVIAEESSIAPPDEIPPLEGDEDTSRMEEVD", "text": "FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. SUBCELLULAR LOCATION: Cytoplasm Melanosome Dynein axonemal particle. SIMILARITY: Belongs to the heat shock protein 90 family."}
{"protein": "MDPGVSSHLRTASLDEARRLPELERVLKSGWLIKKGHATSTKKQLWAVLRRDQLSFYKDEKEYKTKFIFPTQDISAVAYYKEKSPKTFFLYLNEKIIRLIATSNEDAEEWVHVLRSTTGYRAPFSRHPISYILANSSSRTESEPNVQISDTDFDNISTEPRNQTTSPLDLETGQGDHFCTSLYDLIQFGKLRPPGINEENANYPFNPQEVNTLNKHRHSASLQNLYKLLDENKVLMQGTIHWLHGNLHRWSKCWAVVRGYGMTIYNTNREYKPVKVIPIADIQDVAEINVPESSHKYFFTVITQNKPIEFRVDNEDSLILWVAALKTSIDKANGTFTAC", "text": "SUBCELLULAR LOCATION: Cytoplasm Cell septum Cell tip."}
{"protein": "MKEDMEVLSLASLPVGFRFSPTDEELVRYYLRLKINGHDNDVRVIREIDICKWEPWDLPDFSVVKTTDSEWLFFCPLDRKYPSGSRMNRATVAGYWKATGKDRKIKSGKTKIIGVKRTLVFYTGRAPKGTRTCWIMHEYRATEKDLDGTKSGQNPFVVCKLFKKQDIVNGAAEPEESKSCEVEPAVSSPTVVDEVEMSEVSPVFPKTEETNPCDVAESSLVIPSECRSGYSVPEVTTTGLDDIDWLSFMEFDSPKLFSPLHSQVQSELGSSFNGLQSESSELFKNHNEDYIQTQYGTNDADEYMSKFLDSFLDIPYEPEQIPYEPQNLSSCNKINDESKRGIKIRARRAQAPGCAEQFVMQGDASRRLRLQVNLNSHKSETDSTQLQFIKKEVKDTTTETMTKGCGNFTRSKSRTSFIFKKIAAMGCSYRGLFRVGVVAVVCVMSVCSLVA", "text": "FUNCTION: Transcription activator essential for the anti-viral defense called virus basal resistance response pathway (PubMed:11041886, PubMed:15629774, PubMed:18785827, PubMed:24418554). Not involved in HRT-mediated hypersensitive response (HR) and resistance to TCV (PubMed:18785827). Binds DNA non specifically (PubMed:15629774). Activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) (By similarity). FUNCTION: (Microbial infection) Compromised function in defense response pathway when interacting with the invading viral capsid protein (CP) of turnip crinkle virus (TCV) due to abnormal subcellular localization. SUBCELLULAR LOCATION: Nucleus Endomembrane system; Single-pass membrane protein Note=(Microbial infection) Nuclear localization is blocked by its interaction with the coat protein (CP) of turnip crinkle virus (TCV), thus leading to its accumulation in inclusion-like structures peripheral to the nuclei."}
{"protein": "MKVLALRHSVAQVYADTQIYTHDETKDDYENAFLISNLTTHNILYLNYSVKTLQILNKSGIAAVEIQKMDELFTLIRCNFTYDYIEDIVYLHDYSYYTNNEIRTDQHWVTKTNIEDYLLPGWKLTYVGYNGSDTRGHYNFSFKCQNAATDDDAIIEYIYSNELDFQNFILKKIKERMTTSLPIARLSNRVFRDKLFKTLVSDHSKVVNVGPRNESMFTFLDHPSIKQFSNGPYLVKDTIKLKQERWLGKRLSQFDIGQYKNMLNVLTTLYQYYDMYHEKPIIYMIGSAPSYWIYDVKQYSNLKFETWDPLDTPYSDLHHKELFYISDVTKLKDNSILYVDIRTDRENMDWKTWRKIVEEQTINNLNIAYRYLSTGKAKVCCVKMTAMDLELPISAKLLHHPTTEIRSEFYLIMDIWDSKNIKRFIPKGVLYSYINNVITENVFIQQPFKLKTLRNEYVVALYALSNDFNNREDVIKLVNNQKNALITVRINNTFKDEPKVGFKDIYDWTFLPTDFETNESIITSYDGCLGMFGLSISLASKPTGNNHLFILSGTNKYFKLDQFANHMSISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNVENSVSGHVYNALIYYRYNYSFDLKRWIYLHSTNKASIEGGRYYEHAPIELIYACRSAREFARLQDDLTVLRYSNEIENYINKVYSITYADDPNYFIGIKFKNIPYEYDVKVPHLTFGVLNISNSMVPDVVAILKKFKSELFRMDVTTSYTYMLSDEIYVANVSGVLSTYFKLYNAFYKEQITFGQSRMFIPHITLSFSDKKVVRIDSTRLNIDFIYLRKIKGDTVFDMAE", "text": "FUNCTION: Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not. FUNCTION: Counteracts the host innate immune response thanks to its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell IFN-inducible 2',5'- oligoadenylate synthetase (OAS). The host RNaseL is therefore not activated. SUBCELLULAR LOCATION: Virion Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. SIMILARITY: Belongs to the rotavirus VP3 family."}
{"protein": "MPEISLRHVVSCSSQDSTHRAENLLKADTYRKWRSAKAGEKTISVVLQLEKEEQIHSVDIGNDGSAFVEVLVGSSAGGATAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRIFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPYGLSFVKFHSPPDKDEAEAPSQKVTVTKLGQFRVKEEDDSANSLRPGALFFNRINKAASASASDPAGPSYAAATLQASSAASSASPVPKVGGSSSKLQEPPKGKRKLDLGLEDKKPPSKPSAGPPAPKRPKLPVPSRTPAATPASTPAQKAVPGKPRGEGTEPRGARAGPQELGKILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTPDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCYRMRRRLPSRRYLMAGLGSSSEDEGDSHSESGEDEAPKLPRKRPQPKAKTQAAGPSSPPRPPTPEETKAPSPGPQDNSDTDGEQSEGRDNGAEDSGDTEDELRRVAKQREQRQPPAPEENGEDPYAGSTDENTDSEAPSEADLPIPELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPNFEEALMENPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA", "text": "FUNCTION: Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity. Recognizes and binds poly-ADP-ribose chains: specifically binds auto- poly-ADP-ribosylated PARP1, limiting its activity. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Moves from the nucleoli to the global nuclear chromatin upon DNA damage. Recruited to DNA damage sites fowwing interaction with poly-ADP-ribose chains."}
{"protein": "MLSVAARSGPFAPVLSATSRGVAGALRPLLQSAVPATSEPPVLDVKRPFLCRESLSGQAATRPLVATVGLNVPASVRYSHTDIKVPDFSDYRRAEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNAVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPTYEFTSGDVVVVG", "text": "FUNCTION: [Cytochrome b-c1 complex subunit 9]: Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII). UQCRFS1 undergoes proteolytic processing once it is incorporated in the complex III dimer. One of the fragments, called subunit 9, corresponds to its mitochondrial targeting sequence (MTS) (By similarity). The proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer, but the persistence of UQCRFS1-derived fragments may prevent newly imported UQCRFS1 to be processed and assembled into complex III and is detrimental for the complex III structure and function (By similarity). FUNCTION: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b- c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1 (By similarity). Incorporation of UQCRFS1 is the penultimate step in complex III assembly (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Rieske iron-sulfur protein family."}
{"protein": "MALLWLLSVFLLVPGTQGTEDGDMRLVNGASANEGRVEIFYRGRWGTVCDNLWNLLDAHVVCRALGYENATQALGRAAFGPGKGPIMLDEVECTGTESSLASCRSLGWMVSRCGHEKDAGVVCSNDTTGLHILDLSGELSDALGQIFDSQQGCDLFIQVTGQGYEDLSLCAHTLILRTNPEAQALWQVVGSSVIMRVDAECMPVVRDFLRYFYSRRIEVSMSSVKCLHKLASAYGATELQDYCGRLFATLLPQDPTFHTPLDLYAYARATGDSMLEDLCVQFLAWNFEPLTQSESWSAVPTTLIQALLPKSELAVSSELDLLKAVDQWSTETIASHEDIERLVEQVRFPMMLPQELFELQFNLSLYQDHQALFQRKTMQALEFHTVPVEVLAKYKGLNLTEDTYKPRLYTSSTWSSLVMASTWRAQRYEYNRYNQLYTYGYGSVARYNSYQSFQTPQHPSFLFKDKQISWSATYLPTMQSCWNYGFSCTSNELPVLGLTTSSYSNPTIGYENRVLILCGGYSVVDVTSFEGSKAPIPTALDTNSSKTPSLFPCASGAFSSFRVVIRPFYLTNSTDMV", "text": "FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells (By similarity). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space, extracellular matrix."}
{"protein": "MTDISVSKIRNFCIIAHIDHGKSTLADRLLQDTGTVQQRDMQEQFLDSMDLERERGITIKLQAARMKYKADDSQEYVLNLIDTPGHVDFSYEVSRSLQACEGALLVVDASQGVEAQTLANVYLALENNLEIIPVLNKVDLPGADAEKIKQEIEEIIGLDTSNAINCSAKTGVGIKDILEAIVRRVPPPQDEIKLPTKALIFDSYYDPYRGVIVYFRVISGSLNKREKILLMASKKNYELDEIGIMAPDQQQVDELHAGEVGYLAASIKSVADARVGDTITLLNSPANEPLPGYKTANPMVFCGLFPTDADQFPDLRVSLEKLQLSDAALKYEPETSSAMGFGFRCGFLGLLHMEIVQERLEREYDLDLIVTAPSVIYKVNLNQQENIFIDNPSTIPDPQLRESIEEPYVKMEIYAPNEFNGTLMGLCQERRGVFIDMKYITTDRVTLIYEIPLAEVVTDFFDQMKSRTQGYASMEYHLIGYRKNDLVRLDVLINSERADPLTSIVHKDKAYGIGRSLVEKLKELIPKQQFKIPIQASIGSRIIASESISALRKDVLSKCYGGDISRKKKLLKKQAKGKKRMKAMGKVEVPQEAFMAVLKLNQ", "text": "FUNCTION: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily."}
{"protein": "MSTRYHQAASDSYLELLKEATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAAASREQNECVALLDKAATAQNIMNPKKVTRLKEQAQKNARRQIKECERLQEKHQNKMAHTYSKEESGTLSSSKGTFSRSSPSNASAPGTFGSLSKGIKDTFKIKFKKNKDTAEQVGKEGRSGQRNVMEVFREEEEDSFSGDFKEKLQLSAEEDGSVHHESILNRPGLGSIVFRRNRISSPEDISDSKREFGFKLPSELLQRQGASEADEGAADEEGEENGLKDDLPWDDDEVEWEEDVVDATPLEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQVLQQPGQLVDTSL", "text": "FUNCTION: As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. Plays a role in assembly of the complex (PubMed:26812018). May play a role in cellular response to endoplasmic reticulum stress (By similarity). SUBCELLULAR LOCATION: Cell projection, microvillus Note=Localizes at the tip of microvilli (PubMed:26812018). May associate with endoplasmic reticulum membranes (By similarity)."}
{"protein": "MKFGPETIIHGDCIEQMNALPEKSVDLIFADPPYNLQLGGDLLRPDNSKVDAVDDHWDQFESFAAYDKFTREWLKAARRVLKDDGAIWVIGSYHNIFRVGVAVQDLGFWILNDIVWRKSNPMPNFKGTRFANAHETLIWASKSQNAKRYTFNYDALKMANDEVQMRSDWTIPLCTGEERIKGADGQKAHPTQKPEALLYRVILSTTKPGDVILDPFFGVGTTGAAAKRLGRKFIGIEREAEYLEHAKARIAKVVPIAPEDLDVMGSKRAEPRVPFGTIVEAGLLSPGDTLYCSKGTHVAKVRPDGSITVGDLSGSIHKIGALVQSAPACNGWTYWHFKTDAGLAPIDVLRAQVRAGMN", "text": "FUNCTION: A beta subtype methylase that recognizes the double-stranded sequence 5'-GANTC-3' and methylates non-modifed A-2 on the hemimethylated, post-replicative DNA (Probable) (PubMed:12654995) (By similarity). Opens a bubble in the DNA at the recognition site, allowing precise recognition of the sequence and ensuring enzyme specificity (PubMed:31601797). Functions only in the predivisional cell. Responsible for 5'-GANTC-3' methylation in the cell; methylation of hemimethylated sites generated after replication fork passage occurs late in the predivisional cell, near completion of chromosome replication but prior to cell division. Contributes to the accurate cell-cycle control of DNA replication and cellular morphology (By similarity). FUNCTION: A beta subtype methylase that recognizes the double-stranded sequence 5'-GANTC-3' and methylates non-modifed A-2 on the hemimethylated, post-replicative DNA (PubMed:12654995) (Probable). Functions only in the predivisional cell. Responsible for 5'-GANTC-3' methylation in the cell; remethylation of hemimethylated sites generated after replication fork passage occurs late in the predivisional cell, near completion of chromosome replication but prior to cell division. Constitutive expression of the methylase leads to morphologically aberrant cells as well as cells that have undergone additional chromosome replication. Contributes to the accurate cell- cycle control of DNA replication and cellular morphology (PubMed:8289276, PubMed:8577742). Opens a bubble in the DNA at the recognition site, allowing precise recognition of the sequence and ensuring enzyme specificity (By similarity). Can fully replace its ortholog in R.meliloti (PubMed:9294447). SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MKKKLKLTSLLGLSLLIMTACATNGVTSDITAESADFWSKLVYFFAEIIRFLSFDISIGVGIILFTVLIRTVLLPVFQVQMVASRKMQEAQPRIKALREQYPGRDMESRTKLEQEMRKVFKEMGVRQSDSLWPILIQMPVILALFQALSRVDFLKTGHFLWINLGSVDTTLVLPILAAVFTFLSTWLSNKALSERNGATTAMMYGIPVLIFIFAVYAPGGVALYWTVSNAYQVLQTYFLNNPFKIIAEREAVVQAQKDLENRKRKAKKKAQKTK", "text": "FUNCTION: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily."}
{"protein": "MVAAAAVAVAAVGARSAGRWLAALRSPGASRAAMSSDAQWLTAEERDQLIPGLKAAGWSELSERDAIYKEFSFKNFNQAFGFMSRVALQAEKMNHHPEWFNVYNKVQITLTSHDCGGLTKRDVKLAQFIEKAAASL", "text": "FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity. FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity). SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family."}
{"protein": "MEEGSNKREGLPPQLLDLIPDEKEWKLREALGLGRSRNAGFDGEEDKKLDLKLGLPGFIEDDEAETLRDYRLQQESPSLSLSFFPKHSKTTSSTTTTTGAKRGFIDTVEDKTEGYNDQKQQARAGCGKELAVEEMIAAVSERKKGCCPPPPPPHGAPATPARNRPQTQGRGAAAPVVGWPPIRSFRRNLASSSSSKHSPEPQNDNANAKVTLTCKKNPLVKINMDGIPIGRKIDLAAYNSYDGLSSAVKQLFHGFLQAQKDQTNAQIAQQGADDKIFYQLLDGSGEYTLVYEDSEGDRMLVGDVPWKVFVSTAKRLRVLRSSELSHTLIGATARV", "text": "FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Aux/IAA family."}
{"protein": "MTTSWVLQSKDLSNTDLVHIAKLAEQAERYDDMAAAMKRYTEASGNLGNEERNLLSVAYKNVVGARRSAWRVIHGSEMKAVNDRTKKQIAEEYRIKMEKELNTICNQVLALLEDYLLPNASPDDSKVFFLKMQGDYYRYLAEVATDDARTEVVQKSLDAYTKATTAAENLPTTHPIRLGLALNFSVFFYEIQNDAAKACELAKSAFDSAIAELDQLQDDSYKDSTLIMQLLRDNLTLWASDQTAEGDVENDS", "text": "SIMILARITY: Belongs to the 14-3-3 family."}
{"protein": "MASEKPQDLMVTCTAPVNIAVIKYWGKRDEALILPINSSLSVTLHQDQLKTTTTVAISKDFTEDRIWLNGREEDVGQPRLQACLREIRRLARKRRSTEDGDTLPLSLSYKVHVASVNNFPTAAGLASSAAGYACLAYTLAQVYGVEGDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKDSIARQIAPEWHWPQLRILILVVSADKKQTGSTVGMQTSVETSTLLKFRAESVVPERMKEMTRCIQEQDFQGFAQLTMKDSNQFHATCLDTFPPISYLNDTSRRIIQLVHRFNTHQGQTKVAYTFDAGPNAVIFTLEDTVAEFVAAVRHSFPPAANGDKFLKGLQVAPVLLSDELKAALAVEPSPGGVQYIIATQVGPGPQVLDDTHDHLLGQDGLPQRDL", "text": "FUNCTION: Catalyzes the ATP dependent decarboxylation of (R)-5- diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family."}
{"protein": "MAVLAPLIALVYSVPRLSRWLAQPYYLLSALLSAAFLLVRKLPPLCHGLPTQREDGNPCDFDWREVEILMFLSAIVMMKNRRSITVEQHIGNIFMFSKVANAILFFRLDIRMGLLYITLCIVFLMTCEPPLYMGPEYIKYFNDKTIDEELERDKKVTWIVEFFANWSNDCQSFAPIYADLSLKYNCTGLNFGKVDVGRYTDVSMRYKVSTSPLTKQLPTLILFQGGKEVMRRPQIDKKGRAVSWTFSEENVIREFNLNELYQRAKKPSKAGDSIPEEQPVASAPTTVSDGENKKDK", "text": "FUNCTION: Endoplasmic reticulum and mitochondria-associated protein that probably functions as a regulator of cellular redox state and thereby regulates protein post-translational modification, protein folding and mitochondrial activity. Indirectly regulates neuronal proliferation, migration, and organization in the developing brain. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Mitochondrion membrane Note=Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria."}
{"protein": "GLWFGPRIGKRSLRMATEDNRQAFFKLLEAADALKYYYDQLPYEMQADEPETRVTKKVIFTPKLGRSLAYDDKVFENVEFTPRLGRRLADDMPATPADQEMYRPDPEQIDSRTKYFSPRLGRTMNFSPRLGRELAYEMVPSKIRVVRSTNKTQST", "text": "FUNCTION: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pyrokinin family."}
{"protein": "MARRWSTKESPRWRSALLLLFLAGVYGNGALAEHSENVHISGVSTACGETPEQIRAPSGIITSPGWPSEYPAKINCSWFIRANPGEIITISFQDFDIQGSRRCNLDWLTIETYKNIESYRACGSTIPPPYISSQDHIWIRFHSDDNISRKGFRLAYFSGKSEEPNCACDQFRCGNGKCIPEAWKCNNMDECGDSSDEEICAKEANPPTAAAFQPCAYNQFQCLSRFTKVYTCLPESLKCDGNIDCLDLGDEIDCDVPTCGQWLKYFYGTFNSPNYPDFYPPGSNCTWLIDTGDHRKVILRFTDFKLDGTGYGDYVKIYDGLEENPHKLLRVLTAFDSHAPLTVVSSSGQIRVHFCADKVNAARGFNATYQVDGFCLPWEIPCGGNWGCYTEQQRCDGYWHCPNGRDEINCTMCQKEEFPCSRNGVCYPRSDRCNYQNHCPNGSDEKNCFFCQPGNFHCKNNRCVFESWVCDSQDDCGDGSDEENCPVIVPTRVITAAVIGSLICGLLLVIALGCTCKLYSLRMFERRSFETQLSRVEAELLRREAPPSYGQLIAQGLIPPVEDFPVCSPNQASVLENLRLAVRSQLGFTSVRLPMAGRSSNIWNRIFNFARSRHSGSLALVSADGDEVVPSQSTSREPERNHTHRSLFSVESDDTDTENERRDMAGASGGVAAPLPQKVPPTTAVEATVGACASSSTQSTRGGHADNGRDVTSVEPPSVSPARHQLTSALSRMTQGLRWVRFTLGRSSSVSQNQSPLRQLDNGVSGREDDDDVEMLIPISDGSSDFDVNDCSRPLLDLASDQGQGLRQPYNATNPGVRPSNRDGPCERCGIVHTAQIPDTCLEVTLKNETSDDEALLLC", "text": "FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Membrane, coated pit. SIMILARITY: Belongs to the LDLR family."}
{"protein": "MGEEQSTVSGGGGPQESQTLASGTAGHPEPPRPQGDSARAPPLRAASAEPSGGGCGSDWGCADTSAPEPARSLGPPGWSKSRAPAQPAGLALTGPLNPQTLPLQLELEEEEEEAGDRKEGGDEQQEAPPGEELEPRTRVGAADGLVLDVLGQRRPSLAKRQVFCSVYCVESDLPEAPASEQLSPPASPPGAPPVLNPPSTRSSFPSPRLSLPTDSLSPDGGSIELEFYLAPEPFSMPSLLGAPPYSGLGGVGDPYVPLMVLMCRVCLEDKPIKPLPCCKKAVCEECLKVYLSAQVQLGQVEIKCPITECFEFLEETTVVYNLTHEDSIKYKYFLELGRIDSSTKPCPQCKHFTTFKKKGHIPTPSRSESKYKIQCPTCQFVWCFKCHSPWHEGVNCKEYKKGDKLLRHWASEIEHGQRNAQKCPKCKIHIQRTEGCDHMTCSQCNTNFCYRCGERYRQLRFFGDHTSNLSIFGCKYRYLPERPHLRRLVRGSVCAGKLFIAPLIMVLGLALGAIAVVIGLFVFPIYCLCKKQRKRSRTGMHW", "text": "FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the degradation of the iron exporter ferroportin/SLC40A1 and thus regulates iron homeostasis. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the RBR family. RNF217 subfamily."}
{"protein": "MGGALPPEIVDYMYRNGAFLLFLGFPQASEFGIDYKSWKTGEKFMGLKMIPPGVHFVYCSIKSAPRIGFFHNFKAGEILVKKWNTESETFEDEEVPTDQISEKKRQLKNMDSSLAPYPYENYRSWYGLTDFITADTVERIHPILGRITSQAELVSLETEFMENAEKEHKDSHFRNRVDRENPVRTRFTDQHGLPIMKIREGYEIRFQDIPPLTVSQNRVGIEYSDRLYRLLRALGGDWKQLLAEMQIAFVCFLQGQVFEGFEQWKRIIHLMSCCPNSLGSEKELFMSFIRVLFFQLKECPTDFFVDIVSRDNFLTTTLSMLFANVRDSAHAGDDLKKKTAQFKQYLTNQFKWDFNCD", "text": "SIMILARITY: Belongs to the AAR2 family."}
{"protein": "MSNSAIPLNVVAVQEPRLELNNERTWVVVKGGQQVTYYPFPSTSFSSNQFNFICNPPSAQTVLDRLVFIQVPYDITFTANPSHAGITENLLQPGRDAFRAFPISSITNTLNATINGFPVNIELAQIIHALSRYHTPLKVKNGWMSMQPSFEDNYQSYRDADGANNNPLGVFTSAAGLSELPRGSYTMNVVTNTTTTARITGVLYEQVFLPPFLWDGEQAGGLANLTSLTFNWVLNNNLARIWSHSDITNDVSGNSTIGSMNISFQQPSMYLGFVTPRLNIPIPPRITYPYFKLSRYTTQFQNTLAPNASSTFKSNVVQLDSIPRKLYLFVKQSDNVIYQNLNNQITTPDVFLQINNLNLTWNNQQGILSGASSQNLYDFSVQNGYNKTWSEFNGVTQQFNGVSGQPTKVIGLEGGIVCLELGKDVGLRDDEAEGVIGNFNLQVQMTVTNTNQYVTVTPDMYIVAVYDGTLVISNTSAMASIGVASKEEVLNARITHGVSYNELQRIYGGDFFSSFKNFLGKVGNVAGKVNNFLKDSKIASSVLGAIPHPYAQVPGQILKNVGYGESHVGGGKKKGGVLIGGRQLTKAELRKELKM", "text": "FUNCTION: May self assemble to form an icosahedral capsid. Most abundant protein in the virion. SUBCELLULAR LOCATION: Virion."}
{"protein": "MRLHTGEKPYQCLHCDRHFVQVANLRRHLRVHTGERPYACEICPSR", "text": "FUNCTION: Krueppel is a gap class segmentation protein. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MLVLTRKKNESIIINDNIEITVVDIQGEQVRIGINAPKSISIYRKEIYLEIQAENKKAAEIKNVDLKEDLKDFLK", "text": "FUNCTION: A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family."}
{"protein": "MPPKRIAKRRSPPEDAIPKSKKVKVSHRSHKTEPGLVLTLGQGDVGQLGLGESVLERKKPALVPLLQDVVQAEAGGMHTVCLNQSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTEDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDMPVVKVASGNDHLVMLTTDGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVLLKSRGSRGRVRFQDAFCGAYLTFAISREGHVYGFGLSNYHQLGTPGTASCFIPQNLTSFKNSTKSWVGFSGGQHHTICMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPVVSSVACGASVGYAVSKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMTGKQLENRVVLTVSSGGQHTVLLVKDKEQS", "text": "FUNCTION: Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis. Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis. Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import (By similarity). Involved in the regulation of onset of chromosome condensation in the S phase (PubMed:2300055, PubMed:2022190). Binds both to the nucleosomes and double-stranded DNA (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Predominantly nuclear in interphase cells. Binds to mitotic chromosomes."}
{"protein": "MASDQDNSGLDAPGSQFHRPILQSMPDTRQQSFDEIYGPPENFLEIEVRNPRTHGMGRHMYTDYEILCRTNIPAFKLRQSSVRRRYSDFEYFRDILERESARVTIPPLPGKVFTNRFSDDVIEGRRAGLEKFLKIVVGHPLLQTGSKVLAAFVQDPNWDRNAW", "text": "FUNCTION: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family."}
{"protein": "MKFNIDHYIASVLQWILNIALIILSIVLSIFLINETITFIQYIFSTKEYTSYKLVESIIVYFLYFEFIALIIKYFKSNYHFPLRYFIYIGITALIRLIIVSHEEPMETLLYAGAILILVIALYISNMRDLRKE", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsiE family."}
{"protein": "METANGNAGSAATAQNGQQEDASGFKLKFCTVCASNQNRSMEGHLRLAQANYPVISFGTGSLVRLPGPTITQPNVYKFNETSYDSIYRELEAKDPRLYRANGLLNMLGRNRVIKWGPERWQDWQVGMPRVKHEKDQGSIGMEAGVPDIVITCEERCWDAVVDDLLNRGSPLNRPVHVINIDIKDNHQDASIGGGAMVDLADSLNRAAMEERDKVGAAVFDAGGAASRASFDERVPEVLGEWQERWPGLPSTWTLSWF", "text": "FUNCTION: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. SSU72 is required for 3'-end formation of snoRNAs (By similarity). FUNCTION: Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SSU72 phosphatase family."}
{"protein": "MTTSIFTLTPGKITLSDLRDFYFGQMDVRLDDGTFEALQRAAESVERIVGRGEPVYGVNTGFGKLAKTRIPDDRLRDLQRNLVLSHAAGIGQPMPERVVRLILLLKANGLARGYSGVRPQIVQLLLDMLNQGVVPVIPEKGSVGASGDLAPLAHMSAVVIGEGEAFYQGKRLKGDEALKAAGLEPLVLGAKEGLALLNGTQASTALAIAALLDAERLFHAALITGGLTLDAARGTDAPFDPRLHELRGQKGQIECAAVYRALMQGSAIRASHLEDDERVQDPYCLRCQPQVMGACLDNLRQAARVLVIEANAVSDNPIHFPDTDEMISGGNFHAEPVAIAADLMAIAVSEVGAIAERRLALLVDAQMSGLPPFLVQDSGLNSGFMIAQVTAAALASENKTLAHPASVDSLPTSANQEDHVSMATFAARRVGDIVDNVRTIIAVEYLAAVQGLDFLAPLETSAPLLEVAKTLRKTVPFFAQDRLFTPDMEAARALIIDGALGSCVGSGVALPALEG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAL/histidase family."}
{"protein": "MAATAVEFQRAQSLLSTDRNASIDILHAIVKRDVQDDDEEAVRVKEQSILELGGLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDMFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALQLGSQLLQELKKMDDKALLVELQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQAALDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPRAITALKYMLLCKIMLNSPEDVQSLISGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTEYKAELRDDPIISTHLTKLYDNLLEQNLIRVIEPFSRVQIEHISELIKLSKGDVERKLSQMILDQKFHGILDQGEGVLIVFDEPPVDKTYEASLETIQNMSKVVDSLYNKAKKLT", "text": "FUNCTION: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, psmd11a is required for proteasome assembly (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the proteasome subunit S9 family."}
{"protein": "MIFGTPNSTFLENRLGSSTGMPFSSATSLNSGVDQMMNELNIQQPTSHTVLFDLSWEVAKKVGGIYTVLKTKAPVTVEEYKSRYALIGPYNASTAPTEFEPLIPGPLSSPIIENMMKKYGIHVHFGKWLVEGYPKVFLIDLHSSMHKLGEWRWDLMSGFEQAGDNETNETIVFGYQSALLLKEFAEANPNDKYIAHFHEWQASVGLILLKKWKVPVSTIFTTHATLLGRYLAAGGVDLYNQMQVLNMDFEASKRGIYHRHWIEKKSAADSHVFTTVSEITGYESEHILMRKPDVILPNGLKLDKFTALHEFQNLHAKYKGVLNEFVRGHFYGHYSDFDLDNTLYVFTAGRHEYFNKGVDMFLDSLAGLNKLLQQSGSKMTVVAFIIMPAATNNFNVESLKGHSYLKDMRRTCNTIVEAMGERLFEATSRGKMISPEELLSQEDLVMLKRRIFALKQKSSGPPVVTHNMINDNDEILQHIRRIKLFNSQEDRVKVIYHPEFLTSTNPLIPLDYTEFVRGCHLGIFPSYYEPFGMTPAECCASGCPSITSNLTGFANYMSRALQDTDSKGIFIVDRRFKSSRETVDQMTQYLWKFTQLDRRQRIELRNATEKLSELLDWRTLGKFYKTARALALERAFPPKPISRSPSPSPSSSLKLSTGLSNQIELQQQQQQQQPQPIGTTINLIPPSSNVSVTPTTTPTTTTTATTATTAPITTPKPNVIPINTGKENITLLSPNSMSSLLSDSLNEFKKQQQQQQQSKTPTTPTTTSTTTTTPSTTAAATNKSVLSNPTPTPSPNTSSFIPTNKGSTATTTTTTATPTPTPSNNTNGKPFNPIEALTKSNSSSNFATTSTASVNTNNGGTNSPVSKSIPIPSSKSLK", "text": "FUNCTION: Catalyzes the formation of apha-1,4 glycosidic bonds adding glucose residue from UDPG to the growing chain of glycogen. SIMILARITY: Belongs to the glycosyltransferase 3 family."}
{"protein": "MKTLIARHKAGEHIGICSVCSAHPLVIEAALAFDRNSTRKVLIEATSNQVNQFGGYTGMTPADFREFVFTIADKVGFARERIILGGDHLGPNCWQQENADAAMEKSVELVKAYVRAGFSKIHLDASMSCAGDPIPLAPETVAERAAVLCFAAESVATDCQREQLSYVIGTEVPVPGGEASAIQSVHITHVEDAANTLRTHQKAFIARGLTEALTRVIAIVVQPGVEFDHSNIIHYQPQEAQALAQWIENTRMVYEAHSTDYQTRTAYWELVRDHFAILKVGPALTFALREAIFALAQIEQELIAPENRSGCLAVIEEVMLDEPQYWKKYYRTGFNDSLLDIRYSLSDRIRYYWPHSRIKNSVETMMVNLEGVDTPLGMISQYLPKQFERIQSGELSAIPHQLIMDKIYDVLRAYRYGCAE", "text": "FUNCTION: Component of the tagatose-1,6-bisphosphate aldolase GatYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of GatY. When expressed alone, GatZ does not show any aldolase activity. Is involved in the catabolism of galactitol. SIMILARITY: Belongs to the GatZ/KbaZ family. GatZ subfamily."}
{"protein": "MEYNTSALCDIYMDQVDVVEPMFSNFGGRASFAGQITTVKCFEDNALIRETLEQDGVGRVLLVDGGGSLRRALLDGELAAIAEENEWEGIVVYGCVREVDELEDMNIGIQALASIPVGAAMQGVGEVDVPVNFGGVTFLPEDYLYADTTGIILSQEPLSADLEEDEEEPELLD", "text": "FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RraA family."}
{"protein": "MPQNEYIERAQKLHGKRLDTEERARKKAAREGHKQSENAQNLRGLRAKLFAKERHAQKIQMRKAIKQHEERNVKGAPEEKDPSNPVPAYLLDRSNPTSAKALSSQIKSKRAEKAARFSVPIPKVKGISEEELFKVVKTGKKVHKKGWKRVVTKPTFVGPDFTRRPVKYERFIRPMGLRYKKANVTHPTLNVTVQLPILGVKKNPSNPLYTQLGVLSKGTIIEVNVSDLGMVTASGKIAWGRYAQITNNPENDGCLNAVLLV", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family. Ribosome biogenesis protein NSA2 subfamily."}
{"protein": "MNIEATLKNYDLSKLNVVTIASHSSLQILRGAKRHGLGTVAVAKPGSGWFYRRFNFIDNVIEIDLGSMEQLAGDLVKNNAILIPHGSYVEYVGWRRALSMPIPTFGNRYIIEWEADQRKKMRLLEYAGIPIPRSFNDPTQVDRPVIVKLSGAKGGRGYFIAKDAGELAGKLSSINTDDYIIQEYVIGVPAYYHYFDSKVYDRVELFGMDLRYESNVDGRLFNLAEPTFVVTGNIPLVLRESLLPTVQKYGEDFSRAVAELVPPGMIGPYSLESIIKDDLSIVVFEFSGRIVAGTNVYMGVGSPYSVLYFNEPMDMGERIAHEIVNAVKRGKLINVLT", "text": "FUNCTION: Catalyzes the ATP- and formate-dependent formylation of 5- aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "FLPIIAGMAAKVICAITKKC", "text": "FUNCTION: Antimicrobial peptide with activity against Gram-negative and Gram-positive bacteria (MIC=50 uM against E.coli, MIC=6 uM against S.aureus) and fungi (MIC=13 uM against C.albicans) (PubMed:15556063). Shows hemolytic activity on human erythrocytes (HC(50)=25 uM) (PubMed:15556063). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MQPIQIAIVALVVAIIIAIVVWSIVIIEYRKILRQRKIDRLIDRLIERAEDSGNESEGEISALAEMGVEMGHHAPWDVDDL", "text": "FUNCTION: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down- regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo. SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the HIV-1 VPU protein family."}
{"protein": "MSEIVNLSSSLRSLNPKISPLVPPYRQTSSSFSRPRNFKYHSFTDKICLAAERIRAVDIQKQDGGLQELDDSPVSVELGPICGESHFDQVMEDAQKLGESVVIVWMAAWCRKCIYLKPKLEKLAAEFYPRLRFYHVDVNAVPYRLVSRAGVTKMPTIQLWRDGQKQAEVIGGHKAHFVVNEVREMIENDSIT", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the thioredoxin family."}
{"protein": "MKLSKKYLLAVPFFVLMVIFFVVPMAWIIVSGLQNENGASITEKYQPLVGGYSFFQSFWTSLWTATVTVLVALLVAFPFCYFLSQSKNKVFRSFVIALATAPIWSSFLIKLIGLKTLLDLVLGLALNRVGDNNLTFGSGYTLIGMIYLFTPFMFLPLYNNFCILPKNLILASQDLGYNWITSFIKVVIPFSKTAILSGIALTFFPSLTSVAIAQFLDNSNQNNTLGNYVFTLGNNGYDSAIERGRASGAIIIAALITFAFYFVVIFAPRIVRLIQTKCLKYRRVNV", "text": "FUNCTION: Required for the activity of the bacterial transport system of putrescine and spermidine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily."}
{"protein": "MLTVGCTLLVALLAAPAVALVLGSCRALEVANGTVTSLPGATVTLICPGKEAAGNVTIHWVYSGSQNREWTTTGNTLVLRDVQLSDTGDYLCSLNDHLVGTVPLLVDVPPEEPKLSCFRKNPLVNAICEWRPSSTPSPTTKAVLFAKKINTTNGKSDFQVPCQYSQQLKSFSCQVEILEGDKVYHIVSLCVANSVGSKSSHNEAFHSLKMVQPDPPANLVVSAIPGRPRWLKVSWQHPETWDPSYYLLQFQLRYRPVWSKEFTVLLLPVAQYQCVIHDALRGVKHVVQVRGKEELDLGQWSEWSPEVTGTPWIAEPRTTPAGILWNPTQVSVEDSANHEDQYESSTEATSVLAPVQESSSMSLPTFLVAGGSLAFGLLLCVFIILRLKQKWKSEAEKESKTTSPPPPPYSLGPLKPTFLLVPLLTPHSSGSDNTVNHSCLGVRDAQSPYDNSNRDYLFPR", "text": "FUNCTION: [Interleukin-6 receptor subunit alpha]: Signaling via the membrane-bound IL6R is mostly regenerative and anti-inflammatory (Probable). Drives naive CD4(+) T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells (PubMed:27893700). FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. FUNCTION: [Soluble interleukin-6 receptor subunit alpha]: Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity (PubMed:11113088). The IL6:sIL6R complex (hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling also on cells that do not express membrane-bound IL6R in a process called IL6 'trans- signaling'. sIL6R is causative for the pro-inflammatory properties of IL6 and an important player in the development of chronic inflammatory diseases (By similarity). In complex with IL6, is required for induction of VEGF production (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (PubMed:11113088). 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis (PubMed:28402851). SUBCELLULAR LOCATION: [Soluble interleukin-6 receptor subunit alpha]: Secreted. SUBCELLULAR LOCATION: [Interleukin-6 receptor subunit alpha]: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 3 subfamily."}
{"protein": "SGSKTANIGDGCFGVPIDHIGSTSGMGCGSPRPKPTPGGS", "text": "FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family."}
{"protein": "MRGAHYVAIVLLVAAGGQTAAGFDQDEPQHAPDNGYMASVDLRNEFLQSRALQASRNPKDDLMFSAGDEERTPLARSNYLKKVTIPDSIINTANAMRMEGKQVRL", "text": "FUNCTION: Secreted effector that partially suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus Host cytoplasm. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MAEAPQVVETDPDFEPLPRQRSCTWPLPRPEFNQSNSTTSSPAPSGSTAANPDATASLASASAVSTDFMSNLSLLEESEDFARAPGCVAVAAAAAASRGLCGDFQGPEAGCVHSAPPQPPPTGPLSQPPPVPPAAAGPLAGQPRKTSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGPGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGDGDVHSLVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGSMMQQTPCYSFAPPNTSLNSPSPNYAKYTYGQSSMSPVPQMPMQTLQDSKSSYGGLNQYNCAPGLLKELLTSDSPPHNDIMSPVDPGVAQPNSRVLGQNVLMGPNSVMPAYGSQAPHNKMMNPSSHTHPGHAQQTSSVNGRALPHVVNTMPHTSAMNRLTPVKTPLQVPLSHPMQMSALGNYSSVSSCNGYGRMGVLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG", "text": "FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (By similarity). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC- 3'. Activity suppressed by insulin (By similarity). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (PubMed:26436652). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the cytoplasm and nucleus (By similarity). Largely nuclear in unstimulated cells (By similarity). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus. Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). Insulin-induced phosphorylation at Ser-253 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteasomal pathway (By similarity). Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation (By similarity). Phosphorylation by NLK results in nuclear export (By similarity). Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1 (By similarity). SGK1-mediated phosphorylation also results in nuclear translocation. Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide. Methylated form is nuclear (By similarity). PPIA/CYPA stimulates its nuclear accumulation (By similarity). Deacetylation by SIRT6, promotes its translocation into the cytoplasm (By similarity)."}
{"protein": "MAPTQNLFLVAIAFAVIFTASTVHGRHNGAEDIVHSSCEHASYPSLCVRTLSSYSGPTITNRRDLAQAAIKISLSHAQSAAKKLAVVRDSVGKKKQEKAALVDCVEMIGDSVDELSRTLGVLKHLRVSGGSAKEFRWQMSNAQTWASAALTDDDTCLDGFQGMDDGEIKTEVKQWMTKVARVTSNALYMVNQLDETRGKPHDVHL", "text": "FUNCTION: Pectin methylesterase (PME) inhibitor that regulates de- methylesterification of pectins in the apical meristem and affects primordia formation and phyllotactic patterning. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the PMEI family."}
{"protein": "MSATVSTVSADLHKAIDAGDEDKITKITASYGSEQRDKIIPAYHANYGIPPSEAIRKAFKTGFYETMIVHAWTSRFELRAKLIHESIKGKIDVITLLDLVIACMPDDWYGTKVCYTKLYGRELVREIDEVIGVGTPWQSLVSGWVKHDRKYRKSIKSDAEAFRMALDSDNYEVLGSMLATSVPDEWMRIAAAYEETTGMPIDQAIASRYVKVDQTALILAHHWLCDPGQAAAYICSQCCAERKGNYARICRFTSMMYDHCLKCKYAYRAYGSLAMDIRKCFEPKLAKHLLVFWRVE", "text": "FUNCTION: Giardins are involved in parasite attachment to the intestinal mucosa and in the cytoskeletal disassembly and reassembly that marks the transition from infectious trophozoite to transmissible cyst. They may interact with other cytoskeletal proteins such as microtubules in the microribbons or crossbridges, to maintain the integrity of the ventral disk (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the annexin family. Giardin subunit alpha subfamily."}
{"protein": "MNKQKFYTNLSKEVSYALRHAQWKYELELDENGWVSVEQLLHALHQSIEWRDVKIEDLKIMIEKSEKKRHELKENKIRALYGHSIPMKIVKEEGVPPEFLYHGTSPRFLNSIESNGLSPMSRQYVHLSEDIITAELVGKRKDKHPIILEVNTGKAREEGVKFYLGNEKVWLADEIPSEFIAINKN", "text": "FUNCTION: Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''- cyclic phosphate (APPR>P). May function as an ADP-ribosylase. SIMILARITY: Belongs to the KptA/TPT1 family."}
{"protein": "MIAYCGTTTMSDDIDWLHSRRGVCKVDLYSPKGQQDQDRKVICFVDVSTLNVEDKDSKGAAGSRSEGELNLETLEEKEIIVIKDTEKQDQSKTEGSVCLFKQAPSDPISVLNWLLNDLQKYALGFQHALSPSASSCKHKVGDLEGDYSKIPSENCYSVYADQVNFDYLNKGPQNLRLEMAASKNTNNNQSPSNPATKSPSNQRSVATPEGECSMDDLSFYVNRLSSLVIQMARKEIKDKLEGGSKCLHHSMYTSGDKGKTSPRSAVSKIASEMAHEAVELTSSEMRGNGEDCRDGRKTFLYSEMCNKNKCGEKQQMCPKDSKEFADSISKGLMVYANQVASDMMVSVMKTLKVHSCGKPIPACVVLKRVLLKHTKEIVSDLIDSCMKNLHNITGVLMTDSDFVSAVKRNLFNHGKQNAADIMEAMLKRLVSALLGEKKETKSQSLAYATLKAGTNDPKCKNQSLEFSAMKAEMKGKDKCKSKADPCCKSLTSAERVSEHILKESLTMWNNQKQGNQGKVTNKVCCTSKDEKREKISPSTDSLAKDLIVSALMLIQYHLTQQAKGKDPCEEECPGSSMGYMSQSAQYEKCGGGQSSKSLSMKHFETRGAPGPSTCMKENQLESQKMDMSNMVLSLIQKLLSESPFSCDELTESDNKRCCDPRSSKAAPMAKRPEEQCQDNAELDFISGMKQMNRQFIDQLVESVMKLCLIMAKYSNNGAALAELEEQAALVGSGSRCGRDAMMSQNYSETPGPEVIVNNQCSTTNLQKQLQAVLQWIAASQFNVPMLYFMGDDDGQLEKLPEVSAKAAEKGYSVGDLLQEVMKFAKERQLDEAVGNMARKQLLDWLLANL", "text": "FUNCTION: Major structural component of sperm fibrous sheath. Plays a role in sperm motility (PubMed:12167408). SUBCELLULAR LOCATION: Cell projection, cilium, flagellum Note=Localizes to the principle piece of the sperm flagellum. SIMILARITY: Belongs to the AKAP110 family."}
{"protein": "MDVVLEVVDTFIADYAYAYFYPKRLAPYDFPSPSNTTDTSAKAFSTWIYKPATQFITLEPPEQAYMSSWDRDNPLRQALTLYLITWIFGLLVYFIVATLSYIFIFDKRTFEHPRFIKNQVRMEIIAANKAMPVMAIITAPFFLLEVQGYGKLYDTTEDGPGLWYDFFQFPLFLLFTDFCIYWAHRWLHHRLVYKYLHKLHHKWIMPTPFASHAFHPLDGFTQSLPYHIFPFIFPLQKMAYVALFVFVNLWSVMIHDGEYLTNNPVVNGAACHSLHHSRFEVNYGQFFTAFDRMGGTYRMPEQWMFERDMKMSEGRWKKEIEKVDELIEEIEGSDNRTYTDSAPIMKKTQ", "text": "FUNCTION: C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:24785759). ERG3A and ERG3BB catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase ERG1 and the lanosterol synthase ERG7. Then, the delta(24)-sterol C-methyltransferase ERG6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by CYP51A, CYP51B and CYP51C, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. CYP51B encodes the enzyme primarily responsible for sterol 14-alpha-demethylation, and plays an essential role in ascospore formation. CYP51A encodes an additional sterol 14-alpha-demethylase, induced on ergosterol depletion and responsible for the intrinsic variation in azole sensitivity. The third CYP51 isoform, CYP51C, does not encode a sterol 14-alpha- demethylase, but is required for full virulence on host wheat ears. The C-14 reductase ERG24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases ERG25, the sterol-4-alpha-carboxylate 3-dehydrogenase ERG26 and the 3-keto-steroid reductase ERG27, leads to the production of fecosterol via 4-methylfecosterol. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum. The C- 8 sterol isomerase ERG2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases ERG3A and ERG3BB then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturases ERG5A and ERG5B further convert 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen- 3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C- 24(28) sterol reductase ERG4 to produce ergosterol (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MNGTANPLLDREEHCLRLGESFEKRPRASFHTIRYDFKPASIDTSCEGELQVGKGDEVTITLPHIPGSTPPMTVFKGNKRPYQKDCVLIINHDTGEYVLEKLSSSIQVKKTRAEGSSKIQARMEQQPARPPQPSQPPPPPPPMPFRAPTKPPAGPKTSPLKDNPSPEPQLDDIKRELRAEVDIIEQMSSSSGSSSSDSESSSGSDDDSSSSAGEDNGPASPPQPSHQQPYNSRPAVANGTSRPQGSSQLMNTLRNDLQLSESGSDSDD", "text": "FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, Cajal body. SIMILARITY: Belongs to the EAF family."}
{"protein": "MSEVTITGFRSRDVRFPTSLDKTGSDAMNAAGDYSAAYCILETDSAHSGHGMTFTIGRGNDIVCAAINHVADRLKGKKLSSLVADWGKTWRYLVNDSQLRWIGPEKGVIHLALGAVVNAVWDLWAKTLNKPVWRIVADMTPEEYVRCIDFRYITDAITPEEAVAMLREQEAGKAKRIEEALQNRAVPAYTTSAGWLGYGEDKMKQLLRETLAAGYRHFKVKVGGSVEEDRRRLGIAREILGFDKGNVLMVDANQVWSVPEAIDYMKQLSEYKPWFIEEPTSPDDIMGHKAIRDALKPYGIGVATGEMCQNRVMFKQLIMTGAIDICQIDACRLGGVNEVLAVLLMAKKYGVPIVPHSGGVGLPEYTQHLSTIDYVVVSGKLSVLEFVDHLHEHFLHPSVIKDGYYQTPTEAGYSVEMKPESMDKYEYPGKKGVSWWTTDEALPILNGEKI", "text": "FUNCTION: Mediates the conversion of L-galactonate to 2-dehydro-3- deoxy-L-galactonate, the second step in D-galacturonate catabolic process. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
{"protein": "MKAYAKKRISYMPSSPSQNVINFEEIETQKENILPLKEGRSAAALSKAIHQPLVEINQVKSSFEQRLIDELPALSDPITLYLEYIKWLNNAYPQGGNSKQSGMLTLLERCLSHLKDLERYRNDVRFLKIWFWYIELFTRNSFMESRDIFMYMLRNGIGSELASFYEEFTNLLIQKEKFQYAVKILQLGIKNKARPNKVLEDRLNHLLRELGENNIQLGNEISMDSLESTVLGKTRSEFVNRLELANQNGTSSDVNLTKNNVFVDGEESDVELFETPNRGVYRDGWENFDLKAERNKENNLRISLLEANTNLGELKQHEMLSQKKRPYDEKLPIFRDSIGRSDPVYQMINTKDQKPEKIDCNFKLIYCEDEESKGGRLEFSLEEVLAISRNVYKRVRTNRKHPREANLGQEESANQKEAEAQSKRPKISRKALVSKSLTPSNQGRMFSGEEYINCPMTPKGRSTETSDIISAVKPRQLTPILEMRESNSFSQSKNSEIISDDDKSSSSFISYPPQR", "text": "FUNCTION: Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: To yeast protein kinase BUB1 in its non-catalytic N- terminal domain."}
{"protein": "MSENVMTLQVITPAGVVYDHHANYITARTTNGEIGILPNMISTIAGLEIDELKVRRPDDETHVDYIAVNGGIIEIKDSLVTIVADSAERNRDIDVSRAERAKIRAEKALEVAKAEKKSDEIKRVEVALHRALNRLNVSSHN", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family."}
{"protein": "MTVSTAPLLSASGLAILRGERVLFRGIGLTLQPGEAIVLRGANGAGKTTLLRMLAGLTRPEAGEIARPAAHHWIGHKEGIKPQETPRIHLALWAKAWGSSASIADILDQLALTRAADVPGRYLSAGQRRRTAFARLLLEARPLWLLDEPYTALDAAGKTMLDQVISGHLRTGGAIIASMHDAAGFPVTAEVTL", "text": "FUNCTION: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. CcmA exporter (TC 3.A.1.107) family."}
{"protein": "MEGAEKVKVVVRCRPISTTEKLQGHKIAVTCNDEEKAVNIKSLSQEDPPRTFYFDAVFSPNTDQMTVYNVAARPIVENVLKGYNGTIFAYGQTGTGKTFTMAGDLEPVEMRGIIPNSFAHIFDHIAKCQHDTTFLVRVSYLEIYNEEIRDLLSKDHNGNLEIKERPDVGVYVRNLSNPTVENASKMQALMEFGSKNRKVGATAMNLESSRSHAMFTVTIESCRNGLVTQGKLQLVDLAGSERQSKTGAQGERLKEAAKINLSLSTLGNVISSLVDGKSTHIPYRNSKLTRLLQDSLGGNSKTVMIANVGPATYNYDETLSTLRYANRAKNIQNVAKINEDPKDAQLRKFQLEIEALRKILDEENPGDDENQEEAWEAKMQEREVEMEKKRKILEERVNSAVNDEETHRLVKEMMENEAELKKARSEHEKLRSKLEKIEKKLIVGGENLLEKVEEQAKLLEVNNKELEQSKFQEAHLRTQLEERTAVKVEIEERYSSLQEEAFVKSKKIKKVSNELKDARAELKDLEEDHQRQVEAMLDDIRQLRKELLLNIAIIDEYIPVEHVELIEKYVSWSEEHGDWQLKAIAYTGNNMRASAPPAKKEFSNNNQTVPMYYSYRADLGASTAEHRPRTSSKKHRASIRLQQLLT", "text": "FUNCTION: Component of the kinesin II motor complex (composed of kap-1 and the heterodimeric motor proteins klp-11 and klp-20) which is required for intraflagellar transport (IFT) (PubMed:20833139, PubMed:20498083). Heterodimerizes with klp-11 to form a 'processive' molecular motor upon IFT cargo binding, which, within the kinesin II motor complex, binds to and moves along microtubules in a unidirectional manner (without dissociation of the heterodimer), and in turn, is responsible for the IFT of cargo (PubMed:20498083). Specifically, the kinesin II motor complex, together with the kinesin motor protein osm-3 moves along microtubules and is required for anterograde IFT along the middle segment of the sensory neuron cilia (PubMed:17000880, PubMed:20833139, PubMed:28479320). In particular, the kinesin II motor complex delivers specific ciliary cargo proteins such as che-3 which are related to motility to ciliary tips (PubMed:28479320). This is likely mediated by IFT complexes A and B (PubMed:28479320). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton Note=In particular, localizes to the base and transition zone of cilia. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily."}
{"protein": "MMMMSLNSKQAFSMPHAGSLHVEPKYSALHSASPGSSAPAAPSASSPSSSSNAGSGGGGGGGGGGGGGGRSSSSSSSGSGGGGGGGSEAMRRACLPTPPSNIFGGLDESLLARAEALAAVDIVSQSKSHHHHPPHHSPFKPDATYHTMNTIPCTSAASSSSVPISHPSALAGTHHHHHHHHHHHHQPHQALEGELLEHLSPGLALGAMAGPDGTVVSTPAHAPHMATMNPMHQAALSMAHAHGLPSHMGCMSDVDADPRDLEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEKSHREKLTKPELFNGAEKKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKYSAGI", "text": "FUNCTION: Tissue-specific DNA-binding transcription factor involved in the development and differentiation of target cells. Functions either as activator or repressor modulating the rate of target gene transcription through RNA polymerase II enzyme in a promoter-dependent manner. Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3' of promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Binds to an octamer site to form a ternary complex with ISL1; cooperates positively with ISL1 and ISL2 to potentiate transcriptional activation of RGC target genes being involved in RGC fate commitment in the developing retina and RGC axon formation and pathfinding. Inhibits DLX1 and DLX2 transcriptional activities preventing DLX1- and DLX2-mediated ability to promote amacrine cell fate specification. In cooperation with TP53 potentiates transcriptional activation of BAX promoter activity increasing neuronal cell apoptosis. Negatively regulates BAX promoter activity in the absence of TP53. Acts as a transcriptional coactivator via its interaction with the transcription factor ESR1 by enhancing its effect on estrogen response element (ERE)-containing promoter. Antagonizes the transcriptional stimulatory activity of POU4F1 by preventing its binding to an octamer motif. Involved in TNFSF11-mediated terminal osteoclast differentiation. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm. SIMILARITY: Belongs to the POU transcription factor family. Class-4 subfamily."}
{"protein": "MAAPSPTKTTWKLQEIVAHGCSVSSVVLGRSSGRLVATGGDDCRVHLWSVNKPNCIMSLTGHTTPVESVRFNNSEELIVAGSQSGSLRIWDLEAAKILRTLMGHKANVSSLDFHPYGEFVASGSLDTNIKLWDVRRKGCVFRYKGHTQAVRCLRFSPDGKWLASASDDHSVKLWDLTAGKMMAELSEHKGPVNIIEFHPNEYLLASGSADRTVRFWDLEKFQLVGCTEGETIPVRAILFSNDGGCIFCGGKDSLRVYGWEPDQCFDTVPVGWGKVSDLAICNNQLIGVSSAQSNISSFVVDLTRVKMTGCAPQGPVPAEIPISQPAPTGTSLRRIYERPSTTCSKPNRVSPTSDDEEKESRAEIQNPEDYKEIFQPKNAISRTPPRNSEPFPAPPEDDISIVKEAVAPTPDVVTPATSNKKNTEQLQRPPVAASTPIVCQEPSPVPAPQSKPPVISAARNEPIGLKAADFLPAVKSSSPTEVVDDEAVSQIRKGHDTMCMVLTSRMRNLDTVRAVWSSGDIKTSIDSAVAINDLSVVVDLLNIINQKASLWKLDLCMTVLPQIEKMLQSKYESYVQTGCISLKLILQRFLPLITDILAAPPSVGVDISREERLSKCKLCYKQLRILSPLVKSKASQSGRYGSAFRELHLLMSGLE", "text": "FUNCTION: Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles. SIMILARITY: Belongs to the WD repeat KATNB1 family."}
{"protein": "MKKAGLLFLVMIVIAVVAAGIGYWKLTGEESDTLRKIVLEECLPNQQQNQNPSPCAEVKPNAGYVVLKDLNGPLQYLLMPTYRINGTESPLLTDPSTPNFFWLAWQARDFMSKKYGQPVPDRAVSLAINSRTGHTQNHFHIHISCIRPDVREQLDKNLANISSRWLPLPGGLRGHEYLARRVTESELVQRSPFMMLAEEVPEAREHMGSYGLAMVRQSDNSFVLLATQRNLLTLNRASAEEIQDHECEILR", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Cdh family."}
{"protein": "MIIFKNLILKISSLKFAITLIIFIAITSGVGTFIPQGNDPQEYIDFYNETPIFGLINGYQVIKLQLNHVYTSNWFLFSLILLCISLAACSFRRQIPSLKAALKWTDYKNEKRFYKLQLTTNYKVSQDVNHILKADSLLRKKGWSISKFENRLSARKGLVGKLGPIIVHIGLIILLIGSAYGNFSSQSKEQYLRLGESLDLINENKNSKFTIKLNNFLIERESDGKPKQFISYLNFFSEEQHLNEIKTTQVNHPIRFRGLTIYQADWSVSNIVLEIDSVLYQLKLKPIPEIGDQIWGLLIELGRENKKNYLLTIDNENGPLKVSNIKDFSEMFIYLNDDPIEINSSKLSLKKIIPSSGLIIKNDPSIPFIYLAFTLIILGTIFSLIPTNQIWILFNENSNKLFVGGLSNRNLLGFKKEFQKLSDEIKNN", "text": "FUNCTION: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ccs1/CcsB family."}
{"protein": "MKTIQGQSATTALTMEVARVQAISSITKCMDTIPSEYIRSENEQPAATTLQGVVLEVPVIDISNVDDDEEKLVKEIVEASKEWGIFQVINHGIPDEVIENLQKVGKEFFEEVPQEEKELIAKKPGAQSLEGYGTSLQKEIEGKKGWVDHLFHKIWPPSAINYRYWPKNPPSYREANEEYAKWLRKVADGIFRSLSLGLGLEGHEMMEAAGSEDIVYMLKINYYPPCPRPDLALGVVAHTDMSYITLLVPNEVQVFKDGHWYDVNYIPNAIIVHIGDQVEILSNGKYKSVYHRTTVNKYKTRMSWPVFLEPSSEHEVGPIPNLINEANPPKFKTKKYKDYVYCKLNKLPQ", "text": "FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MRRLIPILLGSLVLSLSILVAPAASWAYPFWAQQNYDNPREATGKIVCANCHLAQKTTQAEVPQSVLPDSVFKAVVKIPYKKDTTEISSDGSDVPLQVGAVVMLPDGFRLAPQDRWSEEIKEETKGVFFTQYSEEKENILLVGPLPGDNNKEIVFPILSPDPATDSSIQFGKYSIHVGGNRGRGQILPTGEKTNNNAFTATEAGTITSIKSGKNGESDIKLKTDSGKVISETIPAGPSLLVKVDDKVEAGAPLTSDPNSGGFGQLDTEVVLQNPVRIYGLLAFFVAVSLAQILLVLKKKQVEKVQAAEGI", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome f family."}
{"protein": "MMMTKQKPTLTERLNIGGDEVRELKLGATFNPKNTATAFHTIKYDFKPASVDTSRMATVDVGSNNQVTVTVPNLESSGVPQTVYKGNHKKYTKECLIIFDKETGAITLEKLNHNIQVKKTRSEMTNKPSLMPATNAAPMSSGPNGVPMPSGAMAGTGSGPKLENSTMRITSKTKVSTGSRRNNIIDFKPRNSPMQQSSPSRPVASHRSPQSAPAWHANNAQQTLPSIPMIMDDDDFGLSAALHNGGGGGGGQANISGSSTGSSVGQPDYGSVNMGKQRQASSQGHAKRQQQTQRSSPPMQQQQQQQNYGRGGANNNYAQQLHQQQQQQQQQQLQQQQQQMQQRASFSHSNHSNSMPLDLDSPTHHEQAAQSMAQAAAVLEQQIGGELSASSSSSESESSDSDSGSDSDDSTEDDRSTHQQQQPPGQLSQHHHHHMQQQQHMHQLPNLGLGSISPTYNSHQHHQQQQQQHQQQQQQQSHHHHHQQQQQQSSIYASNGGFPNDLLQNDLQLSSNSSDDDD", "text": "FUNCTION: Promotes transcriptional elongation by Su(Tpl)/ELL. Essential for development (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EAF family."}
{"protein": "MEKCFNIIPSLLLISLLIKSSNAAGIAVYWGQNGNEGSLQDACNTNNYQFVNIAFLSTFGNGQNPQINLAGHCDPSTNGCTKFSPEIQACQAKGIKVLLSLGGGAGSYSLNSAEEATTLANYLWNNFLGGTSTSRPLGDAVLDGIDFDIESGGQHYDELAKALNGFSQQKVYLSAAPQCPYPDAHLDSAIQTGLFDYVWVQFYNNPQCQYSNGNINNLVNAWNQWTSSQAKQVFLGVPASDAAAPSGGLIPADVLTSQVLPAIKTSPKYGGVMIWDRFNDAQSGYSNAIKGSV", "text": "FUNCTION: This protein functions as a defense against chitin containing fungal pathogens. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily."}
{"protein": "MFLLPRFVLVSCIIGSLGFDNPPTNVVSHLNGDWFLFGDSRSDCNHVVTTNPRNYSYMDLNPALCGSGKISSKAGNSIFRSFHFTDFYNYTGEGQQIIFYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIAREANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGNYLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSILSGLLYDSPCFSQQGVFRYDNVSSVWPLYPYGRCPTAADINTPDVPICVYDPLPIILLGILLSVAVIIIVVLLLYFMVDNGTRLHDA", "text": "FUNCTION: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. May become a target for both the humoral and the cellular branches of the immune system. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface. SIMILARITY: Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family."}
{"protein": "MRVFTLAPLALLPLVLARPSQRSSSPQKPIMADNGDLVMIPEGHEKSNLDEIIASSKLLSLHRSLSQIESISNNEGSVGDFLVEYLERHGFTVQKQAVPLDGHEVDEEERKPSRFNVYAYPASSPSPEIILTSHIDTVPPYIPYSLSLPPTASTGSSSIDRRAIHISGRGTVDAKASVACQIIATLSHLESNPDTPLGLLFVVSEETGGQGMHHFSNSPLNTSPPTFHTVIFGEPTESKLVSGHKGMLHFDVHVRGKPAHSGYPWLGRSAVSEILPILSKVDSLGDIPESEGGLPSSEKYGKTTLNIGVMEGGVATNVVPASASARVAVRLAGGTVTHAKETILAAVRSASKNPEDVHVSFSAGGAYPPVDLDSDVEGFDVMTVNYGTDVPNWDIHDHDLPDHGKVKRYLYGPGSIFVAHGENEGLSVGDMEDAVEGYARLIRAAVGRSERK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M20A family."}
{"protein": "MTLKVILGEHQITRTELPVGIATVSGCGAVVYCISKFWGYGAIAPYPQSGGNRVTRALQRAVIDKTKTPIETRFYPLDSLRTVTPKRAVDNGHAVSGAVRDAARRLIDESITAVGGSKFEVNPNPNSSTGLRNHFHFAVGDLAQDFRNDTPADDAFIVGVDVDYYVTEPDVLLEHMRPVVLHTFNPKKVSGFDADSPFTIKNNLVEYKVSGGAAWVHPVWDWCEAGEFIASRVRTSWKEWFLQLPLRMIGLEKVGYHKIHHCRPWTDCPDRALVYTIPQYVIWRFNWIDTELHVRKLKRIEYQDETKPGWNRLEYVTDRNELLVSIGREGEHAQITIEKEKLDMLSGLSATQSVNVRLIGMGHKDPQYTSMIVQYYTGKKVVSPISPTVYKPTMPRVHWPVTSDADVPEVSARQYTLPIVSDCMMMPMIKRWETMSESIERRVTFVANDKKPSDRIAKIAETFVKLMNGPFKDLDPLSIEETIERLNKPSQQLQLRAVFEMIGVEPRQLIESFNKNEPGMKSSRIISGFPDILFILKVSRYTLAYSDIVLHAEHNEHWYYPGRNPTEIADGVCEFVSECDAEVIETDFSNLDGRVSSWMQRNIAQKAMVQAFRPEYRDEIISFMDTIINCSAKAKRFGFRYEPGVGVKSGSSTTTPHNTQYNGCVEFTALTFEHPDAEPEDLFRLIGPKCGDDGLSRAIIQKSINRAAKCFGLELKVERYNPEIGLCFLSRVFVDPLATTTTIQDPLRTLRKLHLTTRDPTIPLADAACDRVEGHLCTDALTPLISDYCKMVLRLYGPTASTEQVRNQRRSRNKEKPYWLTCDGSWPQHPQDAHLMKQVLIKRTAIDEDQVDALIGRFAAMKDVWEKITHDSEESAAACTFDEDGVAPNSVDESLPMLNDAKQTRANPGTSRPHSNGGGSSHGNELPRRTEQRAQGPRQPARLPKQGKTNGKSDGNITAGETQRGGIPRGKGPRGGKTNTRRTPPKAGAQPQPSNNRK", "text": "FUNCTION: RNA-dependent RNA polymerase, which replicates the viral genome composed of 2 RNA segments, RNA1 and RNA2. Does not need an exogenous primer. Also possesses a terminal nucleotidyl transferase (TNTase) activity. The TNTase catalyzes the addition of nucleotide to the 3'-end of plus- and minus-stranded RNAs, probably to repair the 3'- end nucleotide loss. Forms the open necked connection to the cytosol of the virus-induced replication vesicles. Mediates viral RNA1 recruitment. SUBCELLULAR LOCATION: Host mitochondrion outer membrane; Single-pass membrane protein Note=Part of the 30- to 90-nm invaginations of the host mitochondrial outer membrane that form the viral replication complexes vesicules. Has a N-terminal membrane- spanning mitochondrial anchor. SIMILARITY: Belongs to the nodaviridae RNA polymerase family."}
{"protein": "MKPPILIIIMATIMTGTMIVMLSSHWLLIWIGFEMNMLAIIPILMKKYNPRAMEASTKYFLTQATASMLLMMGVTINLLYSGQWVISKISNPIASIMMTTALTMKLGLSPFHFWVPEVTQGITLMSGMILLTWQKIAPMSILYQISPSINTNLLMLMALTSVLVGGWGGLNQTQLRKIMAYSSIAHMGWMAAIITYNPTMMVLNLTLYILMTLSTFMLFMLNSSTTTLSLSHMWNKFPLITSMILILMLSLGGLPPLSGFIPKWMIIQELTKNNMIIIPTLMAITALLNLYFYLRLTYSTALTMFPSTNNMKMKWQFEYTKKATLLPPLIITSTMLLPLTPMLSVLD", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."}
{"protein": "MKTTRKCRALLSVGLNLLALLFSTTAFITTYWCEGTQRVPKPNCSKDRRHNCIDYGVNETDPSKVHYSWETGDDRFLFRHFHTGIWYSCEENIHGGGEKCRSFIDLAPASERGVLWLSVVSEVLYIMLLVVGFSLMCLELFHSSNVIDGLKLNAFAAVFTVLSGLLGMVAHMMYTQVFQITVSLGPEDWRPHTWDYGWSFCMAWGSFTCCMAASVTTLNSYTKTVIEFRHKRKLFEQGLREEQTFLDPETFHYFRDRSVQSISSSVDVYPSHGSSHGNSRGKMRSPPAPVDQGDNTESLGEEQC", "text": "FUNCTION: As a component of the AMPAR complex, modifies AMPA receptor (AMPAR) gating. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Synapse. SIMILARITY: Belongs to the GSG1 family."}
{"protein": "MTEQSAHEKYEFKKKLESLRDKKGRSTELISLYIPADKQIFDVTNQLKDEHGQAANIKSKLTRTNVQGAIESLLSRLRYLDKVPENGIVYFTGAVDIGANKTSMESEVIIPPEPITVYKYHCDSSFYLEPLEDMLKDKSTFGLLVLDRREATIGLLVGKRIQAFRNLTSTVPGKQRKGGQSAHRFQQLRLIAIHDFYKRIGDAASEIFMAVDHKDLKGVLIGGPSPTKEEFYGGEFLHHELQKKILGLFDTAYTDESGLSELVNAAGEKLQDLELMGQKNAVRDFFKELIADSGKVAYGETQVRANLEINAVDVLLLSEDLRAERVTTKCSVCGYENKWTRRWKPGEPAPTAGNCPKCGSSLEVTDVIDVVDEFSELADKSNAKVVFVSTDFDEGSQLMNAFGGIAAILRYSTGV", "text": "FUNCTION: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family."}
{"protein": "MTKILIVEDEQNLARFIELELEHENYDVDIEYDGKPGLEKALSNTYDLILLDLMLPNINGLEICRQIRQNQTTPIIIITAKSDTYDKVAGLDYGADDYIVKPFDIEELLARIRAMLRRQPQKNLIDIKGIIIDKDAFKVTVDGQPLDLTKTEYDLLFLLVENRNHVLQREQIITDVWGYDTEVETNVVDVYIRYLRNKLKPFGKDKCIETVRGVGYVVRQ", "text": "FUNCTION: Member of the two-component regulatory system ArlS/ArlR. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAEPSFARLFLLFFSFLLIFATYSWVFGPDSGFLFGTRVRKTLGSNRQVHVDHSLEKPHHPLDPLTVREINRVRTILSNHDPGFGSGSATIHSMALDEPEKSRVVQWKKGNKLLSRRAAVVAYWGGQTHEITVDLDSGRVVSDVINRTSGYPILTLNDVFAASQVPLKSLEFNRSIEARGVKFSDLACITPFAGWFGSEEEGRRVIRVQCFTLQGTTNYFMRPLEGLYVTVDLDKLEVIKIIDKGPIPIPKASGTEYRFGVQNKPVHMDRINPISMEQPDGPSFRVEDGHLVKWANWVFHVKADQRAGMIISQATVRDSETGEPRSVMYKGFPSELFVPYMDPEEGWYYKGYMDAGELGLGPTAMPLVPLNDCPRNSYYIDGVFASPDGKPIVQPNMICLFERYAGDISWRHSEILFANADIRESRPKVTLVARMATSVGNYDYIFDWEFQTDGLIRVTVAASGMLMVKGTPYDNVDDLGDREDDAGPLISENVIGVVHDHFITFHLDMDIDGPMNNSLVKVHLEKQRVPTGKSPRKSYLKVKKYIAKTEKDAQIKLSLYDPYEFHIVNPNRKSRVGNPAGYRIVPGGNAASLLDHDDPPQIRGAFTNNQIWVTPYNRSEQYAGGVLIYQSQGDDTLQVWSDRDRSIENKDIVLWYTLGFHHVPCQEDYPVMPTVAASFELKPANFFESNPILGSAPFFEKDLPVCRPFASS", "text": "FUNCTION: Copper amine oxidase that can use putrescine and spermidine as substrates (PubMed:23915037). Required for abscisic acid- (ABA) and polyamine- (PA) and H(2)O(2)-dependent induced nitric oxide (NO) biosynthesis (PubMed:21471330). Involved in ABA signal transduction and in responses to osmotic stress (PubMed:21471330). SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the copper/topaquinone oxidase family."}
{"protein": "MAREVVDAMTMRRALTRITYEIIEQNKGVGNLVFIGIKTRGIFLAQRLAQRLKQLEGVDVPVGSLDITLYRDDHHAVDVAGQAKLNGADIPVDINGKHVILVDDVLFTGRTVRAALDALMDHGRPAKISLAVLVDRGHRELPIRPDFIGKNIPTALDEQVSVALEEHDGHDGISIEKLEE", "text": "FUNCTION: Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. FUNCTION: Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes (Probable). SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily."}
{"protein": "MANKTKKPIYPFEDWVIRETQFSIDTNYRNETIFTLANGYIGMRGTFEERYSGPKNTSFNGTYINGFYEIHDIVYPEGGYGFAKIGQTMLNVADSKIIKLYVDGEEFDLLQGKILFYERVLDMKKGFVERKVKWESPTGKILEVKIKRIVSLNRQHLAAISFTMQPVNFTGKIRFVSAIDGNVSNINDSEDVRVGSNLKGKVLKTIDKSVEGLKGWIVQKTQKSNFSYACAIDNVLVADSKYEVSNSLEEDGVKVIVDLEAEKGTSYTLNKFISYYTSKDFDENKLVALALEEIEKAKNDGFETIEKEQEEFLNSFWKDADVIIEGDKALQQGIRFNEFHLLQSVGRDGKTNIAAKGLTGGGYEGHYFWDSDIYIMPFFLYTKPEIAKALVMYRYNLLDAARSRAKELGHKGALYPWRTIDGPECSAYFPAGTAQYHINADIVYALKRYVEATNDVDFLYDYGCEILFETARFWEDLGAYIPLKGNKFCINCVTGPDEYTALVDNNAYTNYMAKMNLEYAYDIANKMKKEVPQKYQKVASKLNLKDEEIVAWKKAADNMYLPYSKELDIIPQDDSFLYKERITVDEIPEDQFPLLLHWHYLNIYRYQICKQPDVLLLMFLQREKFTKDELKKNYDYYEPITTHDSSLSPAIFSILANEIGYTDKAYKYFMMTARMDLDDYNDNVKDGIHAASMAGTWSAVVNGFGGMRVYTNELHFEPRLPKEWNLLSFNVRYKGRKINVKLTKENVVFALLEGEPIEIYYFDKKILLEKGEIK", "text": "FUNCTION: Catalyzes the reversible phosphorolytic cleavage of trehalose. Phosphorolysis is specific for trehalose, but D-xylose, D- galactose, L-arabinose, D-fucose, L-fucose, D-glucosamine and 2-deoxy D-glucose can act as substitutes for D-glucose in the synthetic reaction. SIMILARITY: Belongs to the glycosyl hydrolase 65 family."}
{"protein": "MSRSDWIFISLQGFFCLAGVIWKSREGYPIIDFPCPLQFIDSSDATLSYGTTSPWFGFRAVASMQSIWDNGPWFWLHLMLYIAQLVGLILIILHETVPHGAFLRKFESLAALGYLSYTVGLSTAFPVFSLWILNQYRAEKLVTAWPRRQEKAFLRTIFWCTGISHIGIFMVAIVATLLHRDATAPFHIGNSLLGVPDCSQFPCSEIAARHARLRQINEMTGTSSGFFLTVGLFSQALEAENKHLSLRVMVRMFFVSLIAGPAAGSADVLLLRDSITRSKKDCG", "text": "FUNCTION: Part of the gene cluster that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts (PubMed:23468653). The geranylgeranyl diphosphate (GGPP) synthase ltmG is proposed to catalyze the first step in lolitrem biosynthesis (PubMed:16765617, PubMed:15991026). LtmG catalyzes a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (PubMed:16765617, PubMed:15991026). GGPP then condenses with indole-3- glycerol phosphate to form 3-geranylgeranylindole, an acyclic intermediate, to be incorporated into paxilline (PubMed:16765617). Either ltmG or ltmC could be responsible for this step, as both are putative prenyl transferases (PubMed:16765617). The FAD-dependent monooxygenase ltmM then catalyzes the epoxidation of the two terminal alkenes of the geranylgeranyl moiety, which is subsequently cyclized by ltmB, to paspaline (PubMed:16765617, PubMed:15991026). The cytochrome P450 monooxygenases ltmQ and ltmP can sequentially oxidize paspaline to terpendole E and terpendole F (PubMed:22750140). Alternatively, ltmP converts paspaline to an intermediate which is oxidized by ltmQ to terpendole F (PubMed:22750140). LtmF, ltmK, ltmE and ltmJ appear to be unique to the epichloe endophytes (PubMed:16765617, PubMed:15991026). The prenyltransferase ltmF is involved in the 27-hydroxyl-O-prenylation (PubMed:22750140). The cytochrome P450 monooxygenase ltmK is required for the oxidative acetal ring formation (PubMed:22750140). The multi- functional prenyltransferase ltmE is required for C20- and C21- prenylations of the indole ring of paspalanes and acts together with the cytochrome P450 monooxygenase ltmJ to yield lolitremanes by multiple oxidations and ring closures (PubMed:22750140). The stereoisomer pairs of lolitriol and lolitrem N or lolitrem B and lolitrem F may be attributed to variations in the way in which ring closure can occur under the action of ltmJ (PubMed:22750140). While the major product of this pathway is lolitrem B, the prenyl transferases and cytochrome P450 monooxygenases identified in this pathway have a remarkable versatility in their regio- and stereo-specificities to generate a diverse range of metabolites that are products of a metabolic grid rather than a linear pathway (PubMed:22750140). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ltmS family."}
{"protein": "MFSTLIFLTAVTLLMMPSQTVPAPLKDVNDIRVKGLLPLLRQRQLQIMPSQTIPALKDVNDIRVKGLLSLLRQRKQEIMPSQTIPALKDVNDIRVKGLLSLLRQRKQEECDDPDGLMCCTISEMPTC", "text": "FUNCTION: Acts as a neurotoxin by inhibiting an ion channel. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MAQKPKVDPHVGRLGYLQALVTEFQETQSQDAKEQVLANLANFAYDPSNYEYLRQLQVLDLFLDSLSEENETLVEFAIGGLCNLCPDRANKEHILHAGGVPLIINCLSSPNEETVLSAITTLMHLSPPGRSFLPELTATPVVQCMLRFSLSASARLRNLAQIFLEDFCSPRQVAEARSRQAHSALGIPLPRSVAPRQR", "text": "FUNCTION: As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs."}
{"protein": "MNKRDKALQLIKELEDNQDRPISPNLKENLENLTLLTEGCSDIVFRQFDFGNGLCGFIVYIEGIVKSEHIQDHALRPFLMHLTDQIDEHEEALQNTLSISSVALETSMSKVAASIIEGNAVLFADGHSKGLILNIKGGQRRSIEEPITESTIRGSREGFTESLRVNTALVRFRVKTFQLKMISFKIGTKTKTDVVLAYIDGLADPKVIDKAKKRIKKIKIDAVLESGYIEEFIEDDTYSPFPQLQYTERPDTVAAQLLEGRFAIFTDNTPFVLTGPITFWQLMQASEDYYERYLMSNLIRWLRYMFLFVALYLPAIYVAVITYHQDLMPTNLMFSVASAREPIPFPAIIEALIMEISFEALREAGVRLPKTIGQTVSILGALVIGTAAVEAGIVSAPMVIIVSLTGIASFTIPRFNLAISIRMLRFPLMFLASIFGIFGIMLGTIILVLHLCKLQSFGIPYLSGISPFKRDEVKDIFVRAPWWTMTRRPGTYSRGNGQKGAKREDPKDEENNI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GerABKA family."}
{"protein": "MSVNRCIYLLSRSHIRYRVCASTNLSTVSTLSTTQHSTRRTFDKLSTRHSSSGSSRPLDTSLFIPLPVKTDEDAEGSVGAELTKPLDKNELLKVLNRFYKRKEMQKLASDQGLDARLFHQAFVSFRKYVLEMNSLNADLHIILNDICCGAGHIDDIFPYFMRHAKQIFPMLDCIDDLRKISDLRVPANWYPEARAIQRKIVFHAGPTNSGKTYHAIKRYLEAKSGVYCGPLKLLAHEIYEKSNAAGVPCDLVTGEERIFVDPEGKPSGHIASTIEMCSVTTPYEVAVIDEIQMIKDPARGWAWTRALLGLCAEEIHVCGEAAAVDFITELMFTTGEEVEVHNYKRLTPFSISNHAVESLDNLKPGDCIVCFSKNDIYSISRQIEIRGLECAVIYGSLPPGTKLAQAKKFNDPDDPCKILVATDAIGMGLNLSIRRIIFNSLVKHSLNEKGEKEVDTISTSQALQIAGRAGRFSSVFKEGEVTTMHRDDLPVLKEILGKPVDPIATAGLHPTAEQIEMFAYHLPQATLSNLIDIFVSLSQVDGLYFVCNIDDFKFLADMIQHIPLNLRSRYVFCTAPINKKQPFVCTSFLKFARQFSRDEPLTFNWVCRQVNWPLSPPKNIKDLVHLEAVHDVLDLYLWLSYRFMDMFPDSNQIREIQKELDENIQIGVRNITRLIRAIDSQPTDTESNSSSTVPESETSQRKGRVLRSQNQRKELPRKSSLSSRLLRDGLLTKELLSQLQKEWAREQNEDNSIPVNNGKRKKK", "text": "FUNCTION: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA (By similarity). SUBCELLULAR LOCATION: Nucleus Mitochondrion matrix Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the helicase family."}
{"protein": "MTKVVAPVERVVFELNGERQEVAAADVEPSTTLLEFIRTRTPFRGPKLGCGEGGCGACVILIAKYNPKTDEVTEFNVNSCLTLLYSIHFCSIITTEGLGNTKDGFHSIQKRMSGFHASQCGFCTPGMCMSIFSSLVNADKSKKPAPPKGFSKLSISEAERSFSGNMCRCTGYRPIVDACKSFESDVDLEDLGLNIFWKKGDKHPDPTKLPSYTLGGGICTFPDFLKSEIKSSLDFNDASISGPREGWYCPKSIKQYYKLVNSGLFSESSVKVVVGNTSTGVYKDQDLYDKYIDIAGIPELSAIVRKDKGIEIGAATSISRTIEILNQESELTSSPNGSVVFRKLAEHMSKVASPFVRNTASIGGNIILAHKYPFRSDIATILLGAAATVNLQVSSKTLHVNLEQFLEQPPLDHSTLLLSIFIPHWASDCKKEHTLVFETYRAAPRPLGNAVSYVNSAFLGHVSLDKSSGDNILSNLHLAFGAYGTKHAIRARKVEEYLTGKILSASVVLEAIRLLRETIVPVEGTTHPEYRVSVAVGFLFSFLSPLCKGVIESGKTLSISEDLVDTDNVHNKPLSSRRETLSDDEYTPVGDPIKKYKVEVQASGEAIYVDDIPAPKNCLYGEFIYSTQPLANVKSIKFKPSLASKKIITVVSAKDIPTGGRNIGSTFWFGDEEPLFGDPIAEFAGQVLGVVIAETQPYADMAAKQAVVEYTTDGLKAPILTVEQAVQSNSYFQVPPERAPKQVGDFSNGMAEADHKIMSEEVKLSSQYYFYMETQTALAIPDEDNTMTVYSSSQFSELAQNVISKCLGIPFNNVRVITRRAGGGFGGKVVRSLHVRI", "text": "SIMILARITY: Belongs to the xanthine dehydrogenase family."}
{"protein": "MTVQINKLDPDAAIDIAYDIFLEMAPENLDPADIMLFNLQFEERGAVEFVETADNWDEEIGVLIDPDEYAEVWVGLVNENDEMDDIFAKFLISHREDDREFHVVWKE", "text": "SIMILARITY: Belongs to the UPF0263 family."}
{"protein": "MKFVLFAQLAAVAAPAIAIDLAVQAGQHVMYSYPGLTPPESLYKLTSEGKVGGLIIFKENVNSNLPAIMDKFQALYKASPAYNGHPMIITTDQEGGNVRRVPGGPSQSARQIGDSSTPMQAASQAGRDAAAALKAQKINGNLAPVLDIYREEGNFIDEFGRSFGNNTEIVTSCGSAFAISQSRSGVLSTVKHFPGLGAAKKGENTDLVPIKIDLSLDEIRTFDEVPYRTAIRNGVDLIMTSWAVYPSLDAKYPAGLSRKWTTDELRTRLGYKGVIITDAIEAGSLKSFGNDGQRGVLAAKAGVDILLASGRNATQGEAIVNEIVAALKKGTLSMTEFQESSKRIQALQSRLSA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 3 family."}
{"protein": "MEEEFPTISLLGIDFNLSNILMITVTCVIVLLIAIICTRNLQRRPTGKQNFIEWVMDFVRGIINSNMDWKTGGRFHVLGITLLMFIFVANMLGLPFQIAINDEVWWRSPTADPIVTLTLAIMVLGLTHYYGIKMRGFKHYFVGTYFSPMKFLFPLKLVEEFANTLTLGLRLYGNIFAGEVLLTIIATQLAHMNIFVGVLAIIPALLWQGFSIFIGAIQAYIFTMLTMVYMSHKVSDEH", "text": "FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family."}
{"protein": "MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHVDEPGIRTVQIAGSDPVEMADAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDLVKSILIGVVNAVDVPVTLKIRTGWAPEHRNCVEIAQLAEDCGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPIIANGDITNPHKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDTGELLPPLPLAEVKRLLCTHVRELHDFYGQAKGYRIARKHVSWYLQEHAPDDQFRRTFNAIEDASEQLEALEAYFENFA", "text": "FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. SIMILARITY: Belongs to the Dus family. DusB subfamily."}
{"protein": "MAARKGRRRTCETGEPMEAESGDTSSEGPAQVYLPGRGPPLREGEELVMDEEAYVLYHRAQTGAPCLSFDIVRDHLGDNRTELPLTLYLCAGTQAESAQSNRLMMLRMHNLHGTKPPPSEGSDEEEEEEDEEDEEERKPQLELAMVPHYGGINRVRVSWLGEEPVAGVWSEKGQVEVFALRRLLQVVEEPQALAAFLRDEQAQMKPIFSFAGHMGEGFALDWSPRVTGRLLTGDCQKNIHLWTPTDGGSWHVDQRPFVGHTRSVEDLQWSPTENTVFASCSADASIRIWDIRAAPSKACMLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRQFKSGSPVATFKQHVAPVTSVEWHPQDSGVFAASGADHQITQWDLAVERDPEAGDVEADPGLADLPQQLLFVHQGETELKELHWHPQCPGLLVSTALSGFTIFRTISV", "text": "FUNCTION: Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness (PubMed:25990725). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus Chromosome Note=Present in the nucleus throughout interphase and is detached from chromatin at the onset of mitosis and rebinds at telophase when the pre-replication complexes (pre-RC) is formed (PubMed:25990725)."}
{"protein": "MAPKKKGKKGKAKGTAIVDGVAPEDMTKEQVEEHVARIREELDREREERNYFQLERDKIHTFWEITRRQLEEKKAELRNKDREMEEAEERHQVEIKVYKQKVKHLLYEHQNNLAEVKAEGTVVMKLAQKEHRTQEGALRKDMRVLKVELKEQELANEVVIKNLCLKQAEEITKMRNDFERQVREIEAKYDKKMKMLRDELDLRRKTEIHEVEERKNGQISTLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEEHMEREMAEVTLQNRRLADPLQKAKDEMNEMQKRLGNHERDKQILVCTKARLKVAERELKDLKWEHEVLEQRFIKVQQEREELYRKFADAIQEVQQKTGFKNLLLERKLQALNAAVEKREVQFNEVLAASNLDPTALTLVSRKLEDVLESKNTTIKDLQYELARVCKAHNDLLRTYEAKLLAFGIPLDNVGFKPLETAVIGQTLGQGPAGLVGAPT", "text": "FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper motile cilia functioning. Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity in a GRK2-dependent manner (PubMed:17366626, PubMed:21659505, PubMed:27472056). May play a role in the spermatozoa motility (PubMed:11751847). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cell projection, cilium, flagellum Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body Golgi apparatus Cell projection, cilium Cytoplasm, cytoskeleton, flagellum axoneme Note=Associates with microtubules (PubMed:17366626). Localized to the cytoplasm of round spermatids, the tails of elongating spermatids, and mature spermatid tail bundles protruding into the lumen, and in the flagellum of epididymal spermatozoa (PubMed:11751847). SIMILARITY: Belongs to the DRC4 family."}
{"protein": "MTSVKLSTPQTGEFEQPTGLFINNEFVKAVDGKTFDVINPSTEEVICSVQEATEKDVDIAVAAARKAFNGPWRKETPENRGKLLNKLADLFEKNADLIAAVEALDNGKAFSMAKNVDVPAAAGCLRYYGGWADKIEGKVVDTAPDSFNYIRKEPIGVCGQIIPWNFPILMWSWKIGPAIATGNTVVLKTAEQTPLSAYIACKLIQEAGFPPGVINVITGFGKIAGAAMSAHMDIDKIAFTGSTVVGRQIMKSAAGSNLKKVTLELGGKSPNIVFADADLDEAIHWVNFGIYFNHGQACCAGSRIYVQEEIYDKFIQRFKERAAQNAVGDPFAADTFQGPQVSQLQFDRIMGYIEEGKKSGATIETGGNRKGDKGYFIEPTIFSNVTEDMKIQQEEIFGPVCTISKFKTKADVIKIGNNTTYGLAAAVHTSNLTTAIEVANALRAGTVWVNSYNTLHWQLPFGGYKESGIGRELGEAALDNYIQTKTVSIRLGDVLFG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MMSPQEQLERIKFGTADFINDEDMLKKLKRSIETKKPLNIKLGADPTRPDIHLGHTVVINKLKTFQDLGHKVSFLIGDFTAMIGDPSGKNSTRPMLTREEIEENGRSYAKQIFKILDPEKTEIVYNSSWIMKMTPAEFITMTSKYTVAQLLEREDFTKRYRSGTPIGIHEFIYPLTQGYDSVALKTDVELGGTDQKFNLLVGRAMQAAYGMEAQCVLTMPILEGIDGVNKMSKSLDNYISVVDTPKDMFGKTMRISDELMYRWYELLTDVGAAGLNQLRADVAEGRKHPRTVKVELAKFLIKRFHSQAEAQAAEDEFNRIFVEKGLPDEVPDFEVEAETQMGLAALMVKAQLAASNSEAGRLIQGGGVQIDGEKVSDPRLKIDLKSGASFVLKAGKKKFVKIVVK", "text": "FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily."}
{"protein": "MNVVNTLQIIVANMLIYSTPLIFTSIGGVFSERGGIVNVGLEGIMTIGAFSSVVFNLTTAGMFGSMTPWLSILFGALIGALFSSLHAVATVNLRADHIVSGTVLNLMAPALGVFLLQVFYQQGQININEQIGYWNVPLLSNIPVIGKIFFTQTSLPGFLAIVVAILAWYVLFKTRFGLRLRSVGENPQAADTLGINVYAYRWAGVLLSGVLGGVGGAIYAQAISGNFSVSTIAGQGFISLAAMIFGKWNPIGAMLSSLLFGLFTSLAVVGGQIPGIKEIPSSFLQMAPYVFTIIVLALFLGKAIAPKADGVNYIKSK", "text": "FUNCTION: Part of an ABC transporter complex involved in the uptake of all common nucleosides (PubMed:20595258). Responsible for the translocation of the substrate across the membrane (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family."}
{"protein": "MSKVWVGGFLCVYGEEPSEECLALPRDTVQKELGSGNIPLPLNINHNEKATIGMVRGLFDLEHGLFCVAQIQSQTFMDIIRNIAGKSKLITAGSVIEPLPPDPEIECLSSSFPGLSLSSKVLQDENLDGKPFFHHVSVCGVGRRPGTIAIFGREISWILDRFSCISESEKRQVLEGVNVYSQGFDENLFSADLYDLLADSLDTSYIRKRFPKLQLDKQLCGLSKCTYIKASEPPVEIIVAATKVAGDQVQLTTEPGSELAVETCDVPVVHGNYDAVESATATTAMSNQNLPNTTPLLSSPPFSDCVFLPKDAFFSLLNVTTGQQPKIVPPVSVHPPVTEQYQMLPYSESAAKIAEHESNRYHSPCQAMYPYWQYSPVPQYPAALHGYRQSKTLKKRHFQSDSEDELSFPGDPEYTKKRRRHRVDNDDDKEMAREKNDLRELVDMIGMLRQEISALKHVRAQSPQRHIVPMETLPTIEEKGAASPKPSILNASLAPETVNRSLAGQNESTDLLKLNKKLFVDALNKMDS", "text": "FUNCTION: [Assembly protein]: Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging. FUNCTION: [Assemblin]: Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging. FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging. SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus. SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm. SUBCELLULAR LOCATION: [Assemblin]: Host nucleus. SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein family."}
{"protein": "MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP", "text": "FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MAKKKFVENTNWKKIDTDNQLIFEQGGFLGLEEIDPNDYFLTDKNVDKIEKQQKQKQKQEQEQEQKPTNKLTTKSTTKSTPVQNKNQKPVDKKRKSKKGNDDSDNEYSGYQDDSDQDDEYSAAKKKPRIIKPTETVDMGTELLNSFVEGTVHNKKKQRKGIKVKQIIDDNDNDFEDEEEEVKPQQKLQKQKQQEQKQKQPQKQPQQPNKKNNKKELQKEEEEQMEEEKEEEEVQQEEEEEKEIKKPIKEKKVKTQKQIEAAKKNINKLEKIKKRKEISEQKTISKEEQDQLDMSEWNSYNLDPLILKGLRSLGFSKPTEIQSSVIPVAVSSGYDVIGAAQTGSGKTLAFGIPMVQRILQHLRKHGQNVENKANKQQNDNDDENEDVEEEEEEEEEEGRSKEYRKLFSLVICPTRELAIQVTNHIKSIISHTNLKVISIVGGMASQRQQRVLSKRPEIVVATPGRLWELITEGHQHLVELESLLCLGIDEADRMVEQGHFAELESILKTLPIHRTAMSKKERLKKKETEEKRNKRRKVDKLNDKGEMIKGDQDDMDDQIPDEEMEELEQEEQNHLTTTHKRQTFVFSATLVNIPGDGAPTSQKKKYRKLTPIENLIEKVRFQRDYKLIDVTQKRLTAKNLLETKIFCNLEEKDMYLYYFVERYPGRTLVFVNSIDCARRLIPIFNILEVPVFALHAQMQQKQRLKNLDRFRTLDNVVLIATDVAARGLDIPLVQHVIHYQVPRTTQLYIHRSGRTARSDQDGISVVLVTPKERPLYIKLDSSIEHDIGNFPTDIRYMEGVRDRIELAKEIDKLSHQSLKDNREKSWFKKQAEEMDIELDGDFFGENSDDEQSEDTRIAEQKKQFKLKQLRAQLKHLLSRSLLPRGVSQSYITASAIQELESKSQSSAATDFSNKAKNVIGKKAKQLAIENHSKFLTKNKKK", "text": "FUNCTION: ATP-dependent RNA helicase. SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily."}
{"protein": "MENIPTVGLGTWKASPGEVTDAVKLAINLGYRHFDCAYLYHNESEVGMGISEKIKEGVVKREDLFVVSKLWCTCHKKSLVKTACTNTLEALNLDYLDLYLIHWPMGFKPGEKDIPLDRNGKVIPSHTSFLDTWEAMEDLVFEGLVKNLGVSNFNHEQLERLLDKPGLRVRPITNQIECHPYLNQKKLIDFCHKRNVSVTAYRPLGGSGGGFHLMDDTVIRKIAKKHGKSPAQILIRFQIQRNLIVIPKSVTPSRIRENIQVFDFELTEKDMEELLSLDKNLRLATFPTTENHQDYPFHIEY", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D- fructose (AF) to 1,5-anhydro-D-glucitol. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MSWVQLRGHRFHFIQASFDAESNEAVQVIHITDLVRVWSCTCSRNQIVNQAESERCPIDPFQTFETLVDVLAEVLVNVSSESRIQLRGSNDEGSLKIFCTSKIAKDIFLEWNWTLWLTPPETIAKMVWFPLINHHLFESETDTSPGSLMSIIRDQKSLLNDKTWFKEALNERSSSSNPSTPRKRSAFADIISPKRPRTRYDFV", "text": "FUNCTION: Involved in non-homologous end joining (NHEJ) in the repair of double-strand DNA breaks (DSB). Has a role in meiosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XRCC4-XLF family. XLF subfamily."}
{"protein": "MPRSNRNDNFIDKSFTVMADLIVKLLPINARSKEAYVYYRDGLSAQNDGDYAEALENYDEALKLEDNPTDRGETLKNMAIIYMSNGEEERAIETYRRALDENSNQPSCLKNMGLIFEKWGRIAEEDGRQDDADRWFDQAAEAWTQAVRLNPGGYLDIENWLKSTGRSNVDVYF", "text": "FUNCTION: Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the Ycf3 family."}
{"protein": "MSANGRSILLVDDDQEIRELLETYLSRAGFQVRSVSRGADFRQALCEEEASLAILDVMLPDEDGFSLCRWIRSHQRLACMPIIMLTASSDEADRVIGLELGADDYLGKPFSPRELLARIKALLRRAQFTQVRGGDVLAFEDWRLDTVSHRLFHEDGEEFFLSGADFALLKLFLDHPQQILDRDTIANATRGREVLPLERIVDMAVSRLRQRLRDTGKAPRLIQTVRGSGYLLAAQVRPHLQP", "text": "FUNCTION: Contributes to modulation of the type III secretion system (T3SS) in response to host cells via the regulation of the OprB transport system. FUNCTION: Member of the two-component regulatory system GtrS/GltR involved in the regulation of glucose metabolism and transport, as well as regulation of the exotoxin A gene expression (PubMed:24920832). GltR controls the transcription of genes involved in glucose metabolism (glk and edd/gap-1) and transport (oprB) as well as the expression of toxA that encodes exotoxin A, the primary virulence factor (PubMed:8830708, PubMed:24920832). Acts as a repressor that is released from its target operators upon phosphorylation (PubMed:24920832). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MNLNIETITHDDFYEVKVGGELDVYTVPELEEVLVPMRQEGTHDVHVNLANVSYMDSTGLGLFVGTLKALNQNDKNLYILGVSERIGRLFDITGLKDLMHVNEGTEVE", "text": "FUNCTION: Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B (By similarity). SIMILARITY: Belongs to the anti-sigma-factor antagonist family."}
{"protein": "MAACTARRALAVGSRWWSRSLTGARWPRPLCAAAGAGAFSPASTTTTRRHLSSRNRPEGKVLETVGVFEVPKQNGKYETGQLFLHSIFGYRGVVLFPWQARLYDRDVASAAPEKAENPAGHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYTSTDQVPIQHELFERFLLYDQTKAPPFVARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW", "text": "FUNCTION: Involved in DNA damage tolerance by regulating translesion synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG and abasic sites (PubMed:24191025). May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1) (PubMed:24191025, PubMed:26984527). SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Note=Mainly localizes to the mitochondrial matrix; a small fraction localizes in the nucleus."}
{"protein": "MILPFLVLAIGTCLTNSFVPEKEKDPSYWRQQAQETLKNALKLQKLNTNVAKNIIMFLGDGMGVSTVTAARILKGQLHHNTGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERTRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIKDIDVIMGGGRKYMYPKNRTDVEYELDEKARGTRLDGLDLISIWKSFKPRHKHSHYVWNRTELLALDPSRVDYLLGLFEPGDMQYELNRNNLTDPSLSEMVEVALRILTKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDEAIGKAGTMTSQKDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMVSDTDKKPFTAILYGNGPGYKVVDGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFAKGPMAHLLHGVHEQNYIPHVMAYASCIGANLDHCAWASSASSPSPGALLLPLALFPLRTLF", "text": "FUNCTION: Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis. Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural substrates. Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate: it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration. Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix. Also promotes dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite crystallization in its phosphorylated state; it is however unclear whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or indirect manner. Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters. Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (By similarity). Also capable of dephosphorylating microbial products, such as lipopolysaccharides (LPS) as well as other phosphorylated small-molecules, such as poly-inosine:cytosine (poly I:C) (By similarity). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating hydrolysis of N- phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation. During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Extracellular vesicle membrane; Lipid-anchor, GPI- anchor Mitochondrion membrane; Lipid-anchor, GPI-anchor Mitochondrion intermembrane space Note=Localizes to special class of extracellular vesicles, named matrix vesicles (MVs), which are released by osteogenic cells (PubMed:32710882). Localizes to the mitochondria of thermogenic fat cells: tethered to mitochondrial membranes via a GPI- anchor and probably resides in the mitochondrion intermembrane space (By similarity). SIMILARITY: Belongs to the alkaline phosphatase family."}
{"protein": "MEPDPKKVKLDIFDFPTARETRTPEEVAESYAEAVKSHPFYDNVHSAIDFYDSGTIKDGRGQIIGVVLREALPKYAASMASELLASAAVRTSLRSMMFGGESPLSGIAGYFDYRGSPVELKSRKTSFTYEHEAAWPAVFPVVDYVSELYRHVAPERWKAQNDAIPDVVRIHGTPFSTLTINSRFRTASHTDVGDFDGGYSCIACLDGQFKGLALAFDDFGINVLMQPRDVMIFDSHHFHSNTEVELSFSGEDWKRLTCVFYYRAALGEPASYAEYRRRLEKSKQDTSFTPVVSNVRVKENGTNLNRPSPVYPIFLSPFWVPMVAHCLQHCASEAQCVHDAMTADGSRLAEVMFGEPLSTSDGIPLRGEEEKLKANSDSASRPLSRLGGFSETNLMVSTAVEKKKYLNSEFLSHFISAQLLDMWKQARGKWLELVGREWTHMLALNPERKDFLWRNQSEMNSAFFDLCEVGKQVMLGLLGKEAALPKEEQAFWTMYAVHLNAACAEELNMPHVAMSLRKLNVKLKDFNFGGTRYFKDMPPEEQKRRMERKQRIEEARRHGMSSGAHEKRANWLTNDSFDYQTEDCVFDYAQHKWVPPALHAKEITKNVRSGELPTREGVVRVLVVLPDPQSKVDCVDCKLEVSETVRCSCEWERLMSSPAVHRVLAAAQRNLQLPDSVTHDNIEIRFAFHSRLPTDMCDFVVLQHVLSCIPDDVLASAYIRRSAALCSGCVFVVETDVQCRQYYTLKCSVRCDYDAVAPLFFQQLHRVSYGTKAARVRTKGELESLIPTVCCARYKLQGSPLNTTVHVVAPAPPR", "text": "FUNCTION: Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5- hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TET family. JBP1 subfamily."}
{"protein": "MKLFVPALLSLGALGLCLAAPRKNVRWCTISQPEWFKCRRWQWRMKKLGAPSITCVRRAFALECIRAIAEKKADAVTLDGGMVFEAGRDPYKLRPVAAEIYGTKESPQTHYYAVAVVKKGSNFQLDQLQGRKSCHTGLGRSAGWIIPMGILRPYLSWTESLEPLQGAVAKFFSASCVPCIDRQAYPNLCQLCKGEGENQCACSSREPYFGYSGAFKCLQDGAGDVAFVKETTVFENLPEKADRDQYELLCLNNSRAPVDAFKECHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQRDLLFKDSALGFLRIPSKVDSALYLGSRYLTTLKNLRETAEEVKARYTRVVWCAVGPEEQKKCQQWSQQSGQNVTCATASTTDDCIVLVLKGEADALNLDGGYIYTAGKCGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANEGLTWNSLKDKKSCHTAVDRTAGWNIPMGLIVNQTGSCAFDEFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADWAKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSRSDRAAHVKQVLLHQQALFGKNGKNCPDKFCLFKSETKNLLFNDNTECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEACAFLTR", "text": "FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. FUNCTION: Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. The most effective inhibitory activity is seen against E.coli and P.aeruginosa. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated TLR4 signaling, but cannot directly stimulate the TLR4 signaling pathway and subsequent NF-kappa-B activation. FUNCTION: Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). SIMILARITY: Belongs to the transferrin family."}
{"protein": "MILHAQAKHGKPGLPWLVFLHGFSGDCHEWQEVGEAFADYSRLYVDLPGHGGSATISVDGFDDVTGLLCKTLVSYNILNFWLVGYSLGGRVAMMAACQELAGLCGVVVEGGHPGLQNAEQRAERQRSDRQWAQRFRTEPLTAVFADWYQQPVFASLNDDQRRGLVALRSNNNGATLAAMLEATSLAVQPDLRANLSARTFAFYYLCGERDSKFRALAAELAADCHVIPRAGHNAHRENPAGVIASLAQILRF", "text": "FUNCTION: Catalyzes a proton abstraction reaction that results in 2,5- elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). SIMILARITY: Belongs to the AB hydrolase superfamily. MenH family."}
{"protein": "MESSPESLQPLEHGVAAGPASGTGSSQEGLQETRLAAGDGPGVWAAETSGGNGLGAAAARRSLPDSASPAGSPEVPGPCSSSAGLDLKDSGLESPAAAEAPLRGQYKVTASPETAVAGVGHELGTAGDAGARPDLAGTCQAELTAAGSEEPSSAGGLSSSCSDPSPPGESPSLDSLESFSNLHSFPSSCEFNSEEGAENRVPEEEEGAAVLPGAVPLCKEEEGEETAQVLAASKERFPGQSVYHIKWIQWKEENTPIITQNENGPCPLLAILNVLLLAWKVKLPPMMEIITAEQLMEYLGDYMLDAKPKEISEIQRLNYEQNMSDAMAILHKLQTGLDVNVRFTGVRVFEYTPECIVFDLLDIPLYHGWLVDPQIDDIVKAVGNCSYNQLVEKIISCKQSDNSELVSEGFVAEQFLNNTATQLTYHGLCELTSTVQEGELCVFFRNNHFSTMTKYKGQLYLLVTDQGFLTEEKVVWESLHNVDGDGNFCDSEFHLRPPSDPETVYKGQQDQIDQDYLMALSLQQEQQSQEINWEQIPEGISDLELAKKLQEEEDRRASQYYQEQEQAAAAAAAASTQAQQGQPAQASPSSGRQSGNSERKRKEPREKDKEKEKEKNSCVIL", "text": "FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins (PubMed:27292798). Binds to polyubiquitin chains of different linkage types, including 'Lys-6', 'Lys-11', 'Lys- 29', 'Lys-33', 'Lys-48' and 'Lys-63' (PubMed:28082312). May play a regulatory role at the level of protein turnover (PubMed:27292798). SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63 subfamily."}
{"protein": "MPTHVSKTRKLRGHVSAGHGRIGKHRKHPGGRGKAGGLQHLRSHFDKYHPGYFGKVGMRRFHLMKNPLWRPTVNLDRLWTLLPNEARDKYLGKNTEVAPVINVLQSGYGKVLGKGRLPETPVIVQTRYVSRRAEEKIKQAGGVVELIA", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MYSWKSKFKFGKSKEEKEAKHSGFFHSSKKEEQQNNQATAGEHDASITRSSLDRKGTINPSNSSVVPVRVSYDASSSTSTVRDSNGGNSENTNSSQNLDETANIGSTGTPNDATSSSGMMTIKVYNGDDFILPFPITSSEQILNKLLASGVPPPHKEISKEVDALIAQLSRVQIKNQGPADEDLISSESAAKFIPSTIMLPGSSTLNPLLYFTIEFDNTVATIEAEYGTIAKPGFNKISTFDVTRKLPYLKIDVFARIPSILLPSKTWQQEMGLQDEKLQTIFDKINSNQDIHLDSFHLPINLSFDSAASIRLYNHHWITLDNGLGKINISIDYKPSRNKPLSIDDFDLLKVIGKGSFGKVMQVRKKDTQKVYALKAIRKSYIVSKSEVTHTLAERTVLARVDCPFIVPLKFSFQSPEKLYFVLAFINGGELFYHLQKEGRFDLSRARFYTAELLCALDNLHKLDVVYRDLKPENILLDYQGHIALCDFGLCKLNMKDDDKTDTFCGTPEYLAPELLLGLGYTKAVDWWTLGVLLYEMLTGLPPYYDEDVPKMYKKILQEPLVFPDGFDRDAKDLLIGLLSRDPTRRLGYNGADEIRNHPFFSQLSWKRLLMKGYIPPYKPAVSNSMDTSNFDEEFTREKPIDSVVDEYLSESVQKQFGGWTYVGNEQLGSSMVQGRSIR", "text": "FUNCTION: Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. Downstream kinase in the sphingolipid-mediated signaling pathway. Its phosphorylation is regulated by the intracellular sphingolipid concentration. Cooperates with SLI1 in mediating resistance to the sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Its kinase activity is essential for the resistance. Required for both receptor- mediated and fluid-phase endocytosis, but is not necessary for receptor phosphorylation or ubiquitination. Necessary for the internalization of plasma membrane proteins carrying different types of internalization signals. Acts downstream of the PKH kinases to control endocytosis by phosphorylating components of the endocytic machinery. Phosphorylation of residue Thr-504 in the activation loop is essential for activity. phosphorylates and down-regulates flippase activator FPK1. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Intracellular localization is regulated by the intracellular sphingolipid levels. During the yeast cell cycle, distributed both on the plasma membrane and in the cytosol. Greater accumulation was detected on the plasma membrane, such as in the budding area, a daughter cell and the neck region of the mother cell in the S phase, and the septum between a mother cell and a daughter cell in the G2 phase. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily."}
{"protein": "HQRVTLNDGHSIPVLGFITYAPDEVIKPGEEMFPTDEHGKSIGVSNFNHKRVXNQVEXHPYLNQSKDIVLVAYSALGSSRDPWKQSPALIALRYQLQRGVVVLAKSFIEREIKVFGFQLSSEDMK", "text": "FUNCTION: Catalyzes the dehydrogenation of morphine to morphinone. Uses both NAD and NADP, but the activity is much greater with NAD than with NADP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE", "text": "FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. SIMILARITY: Belongs to the troponin C family."}
{"protein": "MKVAILFLSILVLAVASESIEESRDDFAVEELGRATCAGQDQTCKVTCDCCGERGECVCGGPCICRQGNFLIAWYKLASCKK", "text": "FUNCTION: Reversible inhibitor of voltage-gated sodium channels (Nav). Delays the fast inactivation kinetics of neuronal-type sodium channels. In vivo, it induces rat penile erection (PubMed:15246765). This effect may be due to the neuronal nitric oxide synthase (NOS1), since one of its selective inhibitor completely abolishes all the toxic effects of the toxin (PubMed:15246765). This toxin also causes scratching, lacrimation, hypersalivation, sweating and agitation followed by spastic paralysis of the anterior and posterior extremities and death at dose levels of 0.24 mg/mouse (PubMed:1397265, PubMed:16278100, PubMed:15246765). It is also insecticidal to the larval and adult forms of the house fly (PubMed:1397265). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 06 subfamily."}
{"protein": "MSQKLVLILNCGSSSLKFAILDPVSGAEKLSGLAEAFYLPDARIKWKLNGEKGNADLGAGAAHSEALNFIVSTILTEDLKNSIAAIGHRVVHGGEKYTKSVVITDEVIQGIKDAAEFAPLHNPAHLIGIEEAFKAFPHLKDNNVAVFDTAFHQTMPEEAFLYALPYSLYKEHGVRRYGMHGTSHYFVSREAAKRLNIAEDKINVITCHLGNGASVAAIRQGKCIDTSMGFTPLEGLVMGTRSGDLDPAIIFYMHNTLGMSVAQIEETLVKKSGLLGLTEVTSDCRYSEDNYEKESAAKRALDVFCYRLAKYIGSYMAIIGENLDAIVFTGGIGENAALVRQITLNHLKLFGYKIDDEKNSAARFGNEGVITADNTPIAIVIPTNEELVIAQDTARLSF", "text": "FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetokinase family."}
{"protein": "MSNGIVIIGSGFAARQLVKNIRKQDASIPLTLIAADSMDEYNKPDLSHVISQGQRADDLTRQTAGEFAEQFNLLLFPQTWVTDIDAEARVVKSQNNQWQYDKLVLATGASAFVPPVPGRELMLTLNSQQEYRACETQLRDARRVLIVGGGLIGSELAMDFCRAGKMVTLIDNAASILASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGILATLDHQRSIEVDAVIAATGLRPETALARRAGLTINRGVCVDSYLQTSNADIYALGDCAEINGQVLPFLQPIQLSAMVLAKNLLGNNTPLKLPAMLVKIKTPELPLHLAGETQRQDLRWQINTERQGMVARGVDDADQLRAFVVSEDRMKEAFGLLKTLPV", "text": "FUNCTION: One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAD-dependent oxidoreductase family."}
{"protein": "MTTAPPPLSVLLELTHRCPLACPYCSNPIALAALREEMDTAGWRSLLEQAAEMGVLQAHFSGGEPMLRKDLPELVAHARTLGLYSNLITSGVAGGEPMLDQLQAAGLEHVQLSVQDVDPAGADRIAGYRNSLPKKRDFAAAVRARGLPLTINAVLHRHNAERVPGMIALALEWQAERIEVAHTQYYGWGLRNRAALMPSREQLMATIDAVDTARRELGDSLAIDFVTPDYYARQPKPCMGGWGQRFVNISPRGDVLPCHAAETIEGMRFDNLRERALADIWNNGEAFVRFRGTAWMPEVCQGCPKREIDWGGCRCQALALSGNAATLDPVCERSPAHAQVRATAEREAAAPAPEFIYRRPERPAPATADTLE", "text": "FUNCTION: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ). SIMILARITY: Belongs to the radical SAM superfamily. PqqE family."}
{"protein": "MMGASTGQGYEIARKSREIVRELISEDISSLGPAEVAIVERIVHSTADPEYARITEFSQGFVDEALRSLRSSGGILTDIEMVRAGISHPSRCYIREPAVRELAEKRDITRAAASMEYAASQGFRGIVVIGNAPTALMKVIELTLEGLMDARAVIGVPVGFVGAAESKEALRGTEIPHMITRGPKGGTPVAVAAANALIALSKDKEV", "text": "FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate. SIMILARITY: Belongs to the CobH/CbiC family."}
{"protein": "MPLLDIRNLTIEFKTSEGWVKAVDRVSMTLSEGEIRGLVGESGSGKSLIAKAICGVAKDNWRVTADRMRFDDIDLLRLSSRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRLGWRKRRAIELLHRVGIKDHKDAMRSFPYELTDGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKDLVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIITPRLTGAKNHLYACHFPLNMERE", "text": "FUNCTION: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "AICVSQAITYTDCTESGQNLCLCEGSNVCGKGNKCILGSNGKGNQCVTGEGTPNPESHNNGDFEEIPEEYLQ", "text": "FUNCTION: Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I14 (hirudin) family."}
{"protein": "MKVIFVVLAIVLVTLWAMPSEAGKDPKITNKVFFDIEIDNKPAGRIVFGLYGKTVPKTVENFRALCTGEKGLGTSGKPLHYKDSKFHRIIPNFMIQGGDFTRGDGTGGESIYGKKFNDENFKIKHSKPGLLSMANAGPNTNGSQFFITTVVTSWLDGRHTVFGEVIEGMDIVKLLESIGSQSGTPSKIAKISNSGEL", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Microsome. SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
{"protein": "MLRQIGEFYHQGEKDDTSRVWMTCWHHGGRILASCGDDKAVRVWSLVGEPDSKMRLECRTTLDDSHTRAVRSVAFSNDGKCLVSASFDASVVVYQQEDGEFAEVNKLEGHESEVKCAVFSKSDEFLATCSRDKSVWFWQQDEDEDFSVSSILQPHTQDVKQVAWHPTEDLLVSCSYDSSIRFYRFDGEDWVTQQKIDGCHVGTVWSIAFDTEGHRLVTVGEDHCIQLFVRENIGSKSADQDTWKSVARYDVENTRWPLYSVAWNSTNDVIATGGGDCKIRLFKISSTPESPVIEHLGVVGRHELDVNHVAWNPNPKFSNLLTSASDDGTIRLWELEI", "text": "FUNCTION: Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins. SIMILARITY: Belongs to the WD repeat CIA1 family."}
{"protein": "MNLSLHEARIIGCLLEKEVTTPDQYPLSLNSLTLACNQKSSRDPVMSMTESETQSAIDSLMKKRLVTDQTGFGSRVTKYKHRFCNTEFSDLQFSPAQFALICLLLLRGPQTPGELKSRSGRLHQFADLNEVENALLALAQREPSLVHQLPKEPGRRDSRFEELISDQVKGESVPISEHSRSQREAPSKRQDEMDELTLRVSQLELEVKTLKEALQDLLD", "text": "SIMILARITY: Belongs to the UPF0502 family."}
{"protein": "MSTTVTLTSSDGVDLTVDRDVAERSVLIKNMLEDLGESGEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE", "text": "FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). SIMILARITY: Belongs to the SKP1 family."}
{"protein": "MICFILFVFSFLVSVSATAPYKPDDVFLINCGETDVPFDNHGRTWTQEEKNILPKNSDNASFSSVVSYKEESGIPQVPYMTARIFRSDFTYSFPVSPGWKFLRLYFYPTSYKSGFDAVNSFVSVTVNDFTLLQNFSADLTVKASIPESKSLIKEFIVPVYLTLNLTFRPSNNSLAFVNGIEIVSMPDRFYSKGGFDDLITNVGSLIDFEIDNSTASETVHRLNVGGHMVDEVNDSGMFRRWLSDDYEFLIGGVSPYMPDVNISYTEKTPAYVAPAYVYSTCRMMGNAQDTYLNLNFNLTWLFTVDAGFSYLVRLHFFEKYLNKANQRVFSIFLGNQMAREEMDVIRLSGGPRIPIYLDFRIYVGSESGPRPDLRLDLHPLVKDNPEYYEAILNGVEILKLNNSGNLAIIQDNELKPNPPLSSNLTPNHVTQQIKGKSSHLLVKIFIAVGPGTGLATFVVVLMLWMRQMKRKNRKEERVVMFKKLLNMYTYAELKKITKSFSYIIGKGGFGTVYGGNLSNGRKVAVKVLKDLKGSAEDFINEVASMSQTSHVNIVSLLGFCFEGSKRAIVYEFLENGSLDQFMSRNKSLTQDVTTLYGIALGIARGLEYLHYGCKTRIVHFDIKPQNILLDGNLCPKVSDFGLAKLCEKRESVLSLMDTRGTIGYIAPEVFSRMYGRVSHKSDVYSFGMLVIDMIGARSKEIVETVDSAASSTYFPDWIYKDLEDGEQTWIFGDEITKEEKEIAKKMIVVGLWCIQPCPSDRPSMNRVVEMMEGSLDALEIPPKPSMHISTEVITESSSLSDGGEDV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MEASITVLLFAFTKVASSLYYEGSGHSDGEIQTNEVYVESRPLGPYRAPRWCYDLHISDGEATCYSPLGPRYRSTLGTRCRLSCDQGFKLIGQSSVQCLSSRRWSGNGHCRRIQCHVLPPIFYGSYHCSVGVSEGSRCDYSCAPGYMVEGDRSRICMEDGQWSGGEPVCVDLDPPKIQCPVSRMKVAEPEKLTARIFWGNPQVKDSADGVITRVFLRGPEPGSELPEGEHVIRYTAYDRAHNRASCKFIVKVQVRRCPDLTPPLHGYLTCSAAGNNYGATCEYHCEGGYERQGPAARVCQFSQNWAGTPSTCTPMLINVNVNSAGAFIDQFFEKQRLLFISSPSSSDRYYRMQTTALQSSGCGLEQRHVLIVELIGESPREVGRVRNQQLSKELIEELRQVLRISRSYFNMVLIDKHGVDRDRYRQPTASEDIFLFIDTYLLSPRELSQVESNKENCD", "text": "FUNCTION: May play a role in angiogenesis, synapse formation, cellular migration and adhesion. SUBCELLULAR LOCATION: Secreted Cytoplasm Cell surface Synapse."}
{"protein": "MSKEAYFSGESIQLSDMLRAREERALRQLHLLKEYPEGSLLSVTMNIPGPIKTSPKLLEAFDIVIKAIQTALADDKICYQLRLLPTTGYEYYLITSLPSRDLKLKMIALETELPIGRLMDLDVLVLQNDLPHSISRTVLGGSPRQCFICSKEAKVCGRLRKHSVEEMQTAISKLLHSFFNKDNQSSSSDKTG", "text": "FUNCTION: Transfers 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A on a serine residue to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield holo-acyl carrier protein. SIMILARITY: Belongs to the CitX family."}
{"protein": "MTDKVRLTTMVQAAGUAAKLGPAGLEEAIHDITRSDDPNLIVGVEGAEDAGIYRIGENLALVETTDIITPLVDDPFTFGRIAAANALSDVYAMGGRPVTAMNLAFFPACSLPTSVLAAILAGGSAALKEAGTCLVGGHTVEDDELKFGLAVTGLIDPARVVRNCTARPGDLIVITKPLGTGIISTAIKAEMIEPEVEAEATRWMTTLNAKAADLMVACRATAATDVTGFGFIGHACEMALGAKVSFKIELARVPVIPGVPALIDDGMVPAGCYRNRQHYEQHVSGNSGDPLLPLFDPQTSGGLLITFAPDDARTFLSRAGKEGLFAACIGEVEPAGGTPIVFV", "text": "FUNCTION: Synthesizes selenophosphate from selenide and ATP. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I subfamily."}
{"protein": "MARYRCCRSQSRSRCCRRRRRCRRRRRRRCRARRRAMRCCRRRYRLRCRRY", "text": "FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the protamine P1 family."}
{"protein": "MASPTASSILQYSGTGQKEKGTLDHGDVPSVDIGKGETKEVFQENVDGVEFRTVSWQRATVVFLKINFAMSILAIPAALGALGSIGGSLCIIGYTSLNVYTGLILGDIKHNHTECHTLADMMGLIWGRWGRELVGVQIIIAQTLVTAGGVVAITIGFNALSDHGTCTVAFGLISAIAVTAFSAIRTFSKLGWLTWIGFITFVIGVFIFVVAVTQVDRPAAAPQTGDFDLGWAPIAYPSFVVGMVSVTNIFISTCGSSNFIPVISEMKRPQDYRKACLVAGFIVGAMYLSFSLVIYRYCGVWLSTPAFASAGPIVKKVAYGVSLPGLILGVGIYQHVAAKYAFVRVLRDSKHLQANTFTHWGTWLGINIALGTAAFIVAEAVPILNYLLGLAGAICLAPFSLIFPALLWMHEFKKYKTGTTTQKVKYSFHVLIMMFGFFMMIAGFYSVVVLIKEAFDTGTIAKVFDCADNSGFVQGK", "text": "FUNCTION: Transmembrane transporter; part of the Fusarium detoxification of benzoxazolinone cluster involved in the degradation of benzoxazolinones produced by the host plant (PubMed:25727347, PubMed:26828593). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (By similarity). FPSE_08127 is proposed to shuttle metabolites of benzoxazolinone degradation (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
{"protein": "MSYTIPAQTRTEIGKGSSRRLRREGKVPAVIYGVGKEPVSIVFDHKDIINIQANDDFYTSVLTIVLDGKEVNVRAQAMQRHVFKPMIDHVDFVYA", "text": "FUNCTION: This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family."}
{"protein": "MIIFSGGTGTPKLLDGLRHIVPEDELTVVVNTAEDVWVSGNLITPDIDTILYLLSGRIDRDKWWGVKDDTFQTHREMKELGHDESMMIGDLDRVTHIMRSDLLRQGLSLSESIHELLSVYGIGVNVLPMSDDSVRTIVETPSGHVHFQDFWVKQHGVPEVLSVEQEGIEEASICSLVLEALESDDEVLIGPSNPITSIGPIISLPGMSRILRKKKVVAVSPIIGNEAVSGPAGKFMTARGFDVSSRGIADCYREFLDVLVLDDRDTTSPEQFQKMGVDVVSTNTLMKSLEISKDLSKKIVSIFANI", "text": "FUNCTION: Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5- deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP. SIMILARITY: Belongs to the CofD family."}
{"protein": "MKSLVLGLLVGSAIASGPLQHVLHAPPDPEPKPEPEPQVVKDPFEELRDTFDRLRNKAGDIWDDVMDNIPNIMSNMRPLTIPAKKFTRRPDSEWTHIVRGADLEALWVDDESGYKHRKIDGKLAQYDLRIKAVDPSDLGIDKVKQYSGYLDDNANDKHLFFWFFESRNDPFGDPVVLWLNGGPGCSSLTGMFFELGPASIDENITANYNPYSWNSNSSIIFLDQPVNVGYSYSSQAVSDTVTAAKDVYALLTLFFTQFRQYSAQDFHIAGESYAGHYIPVFASEILHHNNTNINLQSVLIGNGLTDPLSQYPFYRPMACGDGGYPSVLDSQSCQSMDNALPRCLSMIKSCYDIESTFTCLPASIYCNNALIGPYQKTGRNPYDVRTNCTGNDLCYPQLNYITEYLNKPHVMRSLGVEVDSYESCNMDINRNFLFHGDWMKPYHRLVPSLLARIPVLIYAGDADFICNWLGNKAWTEALEYPGHAKFAEAPMENLTMINSQGKNEVFGEVKSHSNLTFMRIFKAGHMTPFDSPQASLEFANSWLSGEWSEV", "text": "FUNCTION: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity). SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MTSKNILNKNNCYDAILVGAGIMSGTLALLITEILPTIKILIIEKLNKPGSESTGAFNNAGTGHAANCELNYTPVDENGDLQIDKALFINRSFENSMSLWASLYSKGKIDIKKFLKFIPHISFVTGTENISFLKKRFKAMSKYPEFADMEFSSSFNQIKSWAPLITTCRDPLDKVAATRIKRGTDINFQALTREYLTYISKNKNVEIFYNTELIDLKKTDKKQWKLKVRSLGKIVSLNTSYVFLGAGGKTINFLQKSKIPEAKIYGGFPVSGKWLICEEKSLTEKHNAKVYGKADIGSPPMSVPHLDTRWIEGKKFLLYGPFAGFTTKFLKKGSYLDLFSSIKKSNLFSMLDVGIKNNELINYLFSQSFKSHNSRVENLRNMMPSAEPSNWYLENAGQRVQIIKKTKDGGSLQFGTEIVNSGDGSLSALLGASPGASTAVSIMIEVLKKSCLFNADKFELEKKLSNLLYESEIKNESDNNFLEIIKKRNNSILGFHP", "text": "SIMILARITY: Belongs to the MQO family."}
{"protein": "MDLLRILDTKPIPTIVDATTLGISGNTSGDYWLPTTMSLYQKELTDQIVSLHYSDILRYFETSHYKEDVILESMKTMCLNGSLVATHPYLLIDHYMPKSLITRDVPAHLAENSGKFSVLRDLINLVQEYETETAIVCRPGRTMDLLEALLLGNKVHIKRYDGHSIKSKQKANDFSCTVHLFSSEGINFTKYPIKSKARFDMLICLDTTVDTSQKDIQYLLQYKRERKGLERYAPIVRLVAINSIDHCRLFFGKKFDKNSREYLENVTAAMVILRDRLGTLPPDLRPIYSQKLHYLVEWLENPTVPWPLPDIYPLKQYTSMDVERSLLTEVHFKKSDDQLEDAFSNCSKKRGRHGANKAASSTVAGIEDNITPSFYSTKRLKNDYYTNPLKQDMTQLTGITTADNSSNVNYHLSSGIITHKLIQSMGEVYMDICVQKQELDDYSCLDDLQNDHLKFFSNEDEKIIKEYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFVKTDNVQDEIEKEERVSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNGLESELKLKFEKSEISTKELNEKIGFLKKELKLENDLNEELVGQLSKTMDNLENLTIPRVRTQNGNTKKKSRAKKPGNV", "text": "FUNCTION: Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HDA2/3 family. HDA3 subfamily."}
{"protein": "MLQENFVSCSKEREVQLAVLSEFIHIPTFIYTALNLVILYFILKRLLFKPVWEFMENRKNSIAESMEKAEKGKAEALELKNKYESELNEAYAKAQKILKEAEEKAKQEYERIIRDAKNEAEALKLKAKEEIEREKNEALKEIRNEVVSLALEAASKVLEANMDTEENRKLVNRFIDEQGVA", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MTYEYILVRYGEMTTKGKNRSKFVSTLKDNVKFKLKKFPNIKIDATHDRMYIQLNGEDHEAVSERLKDVFGIHKFNLAMKVPSELEDIKKGALAAFLQVKGDVKTFKITVHRSYKHFPMRTMELLPEIGGHILENTEDITVDVHNPDVNVRVEIRSGYSYIMCDERMGAGGLPVGVGGKVMVLLSGGIDSPVAAYLTMKRGVSVEAVHFHSPPFTSERAKQKVIDLAQELTKYCKRVTLHLVPFTEVQKTINKEIPSSYSMTVMRRMMMRITERIAEERNALAITTGESLGQVASQTLDSMHTINEVTNYPVIRPLITMDKLEIIKIAEEIGTYDISIRPYEDCCTVFTPASPATKPKREKANRFEAKYDFTPLIDEAVANKETMVLQTVEVVAEEEKFEELF", "text": "FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ThiI family."}
{"protein": "MAASVPEPRLLLLLLLLLPPLPPVTSASDRPRGANPVNPDKLLVITVATAETEGYRRFLQSAEFFNYTVRTLGLGQEWRGGDVARTVGGGQKVRWLKKEMEKYASQEDMIIMFVDSYDVILASSPTELLKKFVQSGSHLLFSAESFCWPDWGLAEQYPEVGVGKRFLNSGGFIGFAPTIHRIVRQWKYKDDDDDQLFYTQLYLDPGLREKLKLSLDHKSRIFQNLNGALDEVVLKFDQNRVRIRNVAYDTLPVVVHGNGPTKLQLNYLGNYVPNGWTPQGGCGFCNLNRRTLPGGQPPPRVLLAVFVEQPTPFLPRFLQRLLLLDYPPDRISLFLHNNEVYHEPHIADAWPQLQDHFSAVKLVGPEEALSSGEARDMAMDSCRQNPECEFYFSLDADAVLTNPETLRILIEQNRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGLWNVPYISQAYVIRGETLRTELPEKEVFSSSDTDPDMAFCRSVRDKGIFLHLSNQHEFGRLLSTSHYDTDHLHPDLWQIFDNPVDWREQYIHENYSRALDGEGLVEQPCPDVYWFPLLTEQMCDELVEEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTEHLFPGYHTKTRAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGVDYEGGGCRFLRYDCRVSSPRKGWALLHPGRLTHYHEGLPTTRGTRYIMVSFVDP", "text": "FUNCTION: Multifunctional enzyme that catalyzes a series of post- translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2- glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens. Essential for normal formation of basement membranes (By similarity). SUBCELLULAR LOCATION: Rough endoplasmic reticulum Endoplasmic reticulum lumen Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side Secreted Secreted, extracellular space Note=The majority of the secreted protein is associated with the extracellular matrix."}
{"protein": "MLGNKLSISDLKDIKNKKVLVRVDFNVPIENGIIKDTNRITATLPTINHLKKEGASKIILISHCGRPDGLRNEKYTLKPVAETLKGLLGEEVLFLNDCVGKEVEDKINAAKENSVILLENLRFHIEEEGKGVDANGNKVKANKEDVEKFQNDLTKLADVFINDAFGTAHRAHSSMVGVKLNVKASGFLMKKELEYFSKALENPQRPLLAILGGAKVSDKIQLIKNLLDKVDRMIIGGGMAYTFKKVLNNMKIGTSLFDEAGSKIVGEIMEKAKAKNVQIFLPVDFKIADNFDNNANTKFVTDEEGIPDNWMGLDAGPKSIENYKDVILTSKTVIWNGPQGVFEMPNFAKGSIECLNLVVEVTKKGAITIVGGGDTASLVEQQNKKNEISHVSTGGGASLELLEGKELPGVLALSNK", "text": "SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MSEKPKVYQGVRVKITVKELLQQRRAHQAASGGTRSGGSSVHLSDPVAPSSAGLYFEPEPISSTPNYLQRGEFSSCVSCEENSSCLDQIFDSYLQTEMHPEPLLNSTQSAPHHFPDSFQATPFCFNQSLIPGSPSNSSILSGSLDYSYSPVQLPSYAPENYNSPASLDTRTCGYPPEDHSYQHLSSHAQYSCFSSATTSICYCASCEAEDLDALQAAEYFYPSTDCVDFAPSAAATSDFYKRETNCDICYS", "text": "FUNCTION: Transcriptional coactivator that specifically associates with POU2F3 (PubMed:35576971). This complex drives the development of tuft cells, a rare a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues (PubMed:35576971). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the POU2AF family."}
{"protein": "MEVQRVQEIASLSKVIDTIPAEYIRSENEQPVISTVHGVVLEVPVIDLSDSDEKKIVGLVSEASKEWGIFQVVNHGIPNEVIRKLQEVGKHFFELPQEEKELIAKPEGSQSIEGYGTRLQKEVDGKKGWVDHLFHKIWPPSAINYQFWPKNPPAYREANEEYAKRLQLVVDNLFKYLSLGLDLEPNSFKDGAGGDDLVYLMKINYYPPCPRPDLALGVAHTDMSAITVLVPNEVPGLQVYKDGHWYDCKYIPNALIVHIGDQVEIMSNGKYKSVYHRTTVNKEKTRMSWPVFLEPPPDHEVGPIPKLVNEENPAKFKTKKYKDYAYCKLNKLPQ", "text": "FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MLLAQRRLFSLGCRAKPIKTIYSSKVLGLSTSAKMALRFKNAKRIEGLDQNVWVEFTKLAADPSVVNLGQGFPDITLPSYVQEELSKAAFIDNLNQYTRGFGHPSLVKALSCLYGKIYQKQIDPNEEILVTVGGYGSLFNAIQGLVDPGDEVIIMVPFYDCYEPMVKMAGAVPVFIPLRSKRTDGMKWTSSDWTFNPQELESKFSSKTKAIILNTPHNPIGKVYTREELQVIADLCIKHDTLCISDEVYEWLVYTGHKHIKVASLPGMWDRTLTIGSAGKTFSVTGWKLGWSIGPGHLIKHLRTVQQTSVYTCATPLQAALAEAFWIDIKRMDDPECYFNSLPKELEVKRDRMACLLNSVGLKPIIPDGGYFIIADVSSLGVDLSDVKSDEPYDYKFVKWMTKNKKLSAIPVSAFCDSESKPHFEKLVRFCFIKKDSTLDAAEEIFRTWNSRKS", "text": "FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others. May catalyze the beta-elimination of S-conjugates and Se- conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond. Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro). SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MDSTRNSASSNSTGCFTDQKKRKALYEVFKKLSGVDCQRNEGNVVEGVTCYYGEMNKEQFHVAIFQTDKNESLFSERVFDLFDTNHDGLLGFEEFARALSVFHPSAPIDDKIDLSFQLYDLKQQGFIERQGVKQLVVATLAASGMSQSDEIVESIIDKTFVQADTKHEGMIDEEEWMDLVFRHPLLLKNMTLQYLKDITTTFPSFVLHSQVEDT", "text": "FUNCTION: Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the calcineurin regulatory subunit family."}
{"protein": "MPASSVRLPLRLLTLAGLLALAGAAALARGAPQGGPPSPQGGPAPTAAPARGPTLFVLVGDGSAGFVFQLGGLGALNDTRIRGHLLGRYLVSYQVVPPPVSAWYFVQRPRERPRLSGPPSGAELVAFDAPGVRRTYTTAAVWPAEVAVLADAEARCPAAVFNVTLGEAFLGLRVALRSFLPLEVIISAERMRMIAPPALGAGLEPPGPPAGRFHVYTLGFLSDGAMHQTMRDVAAYVHESDDYLAQLSAAHAAALAAVVQPGPYYFYRAAVRLGVAAFVFSEAARRDRRASAPALLRVESDARLLSRLLMRAAGCPAGFAGLFDGRAERVPVAPADQLRAAWTFGEDPAPRLDLARATVAEAYRRSVRGKPFDQQALFFAVALLLRAGGPGDARETLLRTTAMCTAERAAAAAELTRAALSPAAAWNEPFSLLDVLSPCAVSLRRDLGGDATLANLGAAARLALAPAGAPGAAAATDEGAEEEEEDPVARAAPEIPAEALLALPLRGGASFVFTRRRPDCGPAYTLGGVDIANPLVLALVSNDSAACDYTDRMPESQHLPATDNPSVCVYCDCVFVRYSSAGTILETVLIESKDMEEQLMAGANSTIPSFNPTLHGGDVKALMLFPNGTVVDLLSFTSTRLAPVSPAYVVASVVGAAITVGILYALFKMLCSFSSEGYSRLINARS", "text": "FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). SIMILARITY: Belongs to the herpesviridae glycoprotein H family."}
{"protein": "MGILVILVDLQCCRCDAKIRKVLGCLEEEYCIEKVEYDVKNNRVIVRGKFDPEKLCKKIWCKAGKIIKEILIVDVWPPPLPQPPPPCKPPPCEKPPEDCKPKPCHCCSCEKPKPKPKPCHCEKPKPCHCEKPKPCEKPPPCKPEEPPKPPPEKPPPKPECKLVPYPYPVPYPYAGQWCCPKPEPPKPPPEPPKEPEPPKPCGCSHAFVCVCKPAPPPPPPCGCSGGHGNCGCGIRPWPPQVWPPPPVCPPPPWCYTEDNANACSIM", "text": "FUNCTION: Involved in defense responses (PubMed:19696351, PubMed:26740780). Contributes to slowing defense responses toward Magnaporthe oryzae (PubMed:19696351)."}
{"protein": "LSAASWRTQSIYFLLTDRFGRTDNSTTATCNTGNEIYCGGSWQGIIDHLDYIEGMGFTAIWISPITEQLPQDTADGEAYHGYWQQKIYDVNSNFGTADNLKSLSDALHARGMYLMVDVVPDHMGYAGNGNDVDYSVFDPFDSSSYFHPYCLITDWDNLTMVEDCWEGDTIVSLPDLDTTETAVRTIWYDWVADLVSNYSVDGLRIDSVLEVQPDFFPGYNKASGVYCVGEIDNGNPASDCPYQKVLDGVLNYPIYWQLLYAFESSSGSISNLYNMIKSVASDCSDPTLLGNFIENHDNPRFAKYTSDYSQAKNVLSYIFLSDGIPIVYAGEEQHYAGGKVPYNREATWLSGYDTSAELYTWIATTNAIRKLAIAADSAYITYANDAFYTDSNTIAMAKGTSGSQVITVLSNKGSSGSSYTLTLSGSGYTSGTKLIEAYTCTSVTVDSSGDIPVPMASGLPRVLLPASVVDSSSLCGGSGRLYVE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
{"protein": "MDQVTKFIEPGRQFAKDSIRLVKRCTKPDRKEFQKIAVATAIGFCIMGFIGFFVKLIHIPINNIIVGS", "text": "FUNCTION: Necessary for protein translocation in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma family."}
{"protein": "MADRLTQLQDTVNQQAEHFCNSIGILQQCSVPSKFAGFERTGSQTPQQQVHQQQQLPQQQQQQQQPQQQEDFPQLFSTLISRCAKDIDTLIESLPSEESSIELQVQSLQRLEAENKESAEKLEEIVRKGELLLEKIQAALSDIAQSQLDMQYSS", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 21 family."}
{"protein": "MDKLLQWSIAQQSGDQEAIEKIGKPDPKMLEQLFGGPDEPALMKQAIMVIDNEEATLENREIAFDNFEMLIENMDNANNIENIKLWQSVIDKMSAETPTSLRVYAASCAGIAVQNNPKSQEDFLKYDGLASLISICNEEDVPTELRLKALFAISSLIRNFEVGYAKFDELDGWSVVKFNENEDHKVKLRILSLVSAILSTPLDKKKEEHVHREKLVANIISILKKDGHIGCIDKALNIISQLASSEFEFSSSEIGDIAQGLEEIEKLKDSISEDDYNSVKQVVN", "text": "FUNCTION: Functions as a nucleotide exchange factor (NEF) for Hsp70 chaperones which accelerates the release of ADP. Required for fully efficient Hsp70-mediated folding of proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FES1 family."}
{"protein": "MAGQSEDPSLERHFKGHRDTVTAVDFNANTKQLASGSMDSCLMVWNMKTQMRAYRFVGHKDAILSVDFSPSGHLIASASRDKTVRLWVPSVKGESTAFKAHTGTVRSVSFSGDGQSLVTASDDKTIKVWTVHRQKFLFSLNQHINWVRCAKFSPDGRLIVSASDDKTIKLWDKTSRECIQSFCEHGGFVNFVDFHPSGTCIAAAATDNTVKVWDIRMNKLIQHYQVHSGVVNSLSFHPSGNYLITASNDSTLKVLDLLEGRLLYTLHGHQGPVTCVKFSREGDFFASGGSDEQVMVWKTNFDAGSYPDLLKYRQNDTFPSGGDYTSIVQPADVHQPARNAHVTQAADLEPHITEMSVKDRSSPLSYTSRSVDQHHPQAEDGNLQTVASTLEHIVGQLDILTRTVGILEQRLSLTEDKLKECIEQQQATVPPSHSGTKKSSF", "text": "FUNCTION: May play an important role in centriole assembly and/or stability and ciliogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Colocalizes with mitochondria in cortical germ plasm islands. The mitochondrial localization may be microtubule-dependent. SIMILARITY: Belongs to the WD repeat POC1 family."}
{"protein": "MTTELEIDDRKEEEAQIPGETSESEEGDEPVKMNRVKRACAMAAESLKEAKRIKNMLMEEECVLQLGNCKKTASYGHRLSKTEACCPSCFSVAFRGKDYENEFTIWKQKAMDGQTHVRSEQFVKRYVNSCFLPYYAKCHQCSKYSKLITSDSLSAQQLSDFKCDCASTIESPKIERVREDSEWCFNEFGHPPLLQNNISYDLLVDHYVTRTTGMDATCQEKAALIDNGGIEFRDTRRIMNMFYVPFTDVIANIVHPEFMETDEKFAFPKFADDPISIYYLQVRNTIIAMWLKHPFVELTVKMIEPQIIVRGHARIFFIEHLIHPILEFLTIKGVVNYGAFDFRIDPLNGMRPKIAIIGAGISGISTARHLKHLGIDAVLFEAKDRFGGRMMDDQSLGVSVGKGAQIIVGNINNPITLLCEQIGIKYRNSNFFCPLIDENGRCFTLERKELDDQVDLHYNNVLDAIRNKYQSDRNFPDVPLEVTNFRHFTEMFSKMSSGLLSAADLDSLYTPEFEKLLDFHLGNLEFSCGTHVSNLSAKDYDHNEKFGNFAGEHAVITDGAQRIIDFLATGLDIRLNCPVKCIDWGRDDRKVKIFFENAEQAAEEFDKVVITTSLSVLKSNHSKMFVPPLPIEKQKAIDDLGAGLIEKIAVKFDRRFWDTVDADGLRTEYFGKVSDCKTDRSLFNIFYDFSGKDPNGEDTFVLMSYVTAEHVNLVNVLTESEVADKFCATLRKMFPSAVINPLGHMMSHWGADRFVGMSYTFVPFGSDGDATYNQLKKSIDEKLYFAGEHTIAAEPQTMAGAYISGLREAGQIVMSLKRDSATFE", "text": "FUNCTION: Histone demethylase that demethylates di-methylated 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor (PubMed:34329293). Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed (By similarity). Plays a role in the mitotic development of the germline (PubMed:34329293). May be involved in H3 demethylation in mitotic cells including gut and embryonic cells (PubMed:34329293). Plays a role in sensitivity upon interstrand cross- link DNA damage, probably by positively regulating the expression of mlh-1 (PubMed:34329293). Plays a role in developmental growth and lifespan regulation in response to ultraviolet-induced damage (PubMed:33046905). No obvious role in larval development, sex chromosome segregation or for regulating meiotic crossover frequency (PubMed:34329293). SUBCELLULAR LOCATION: Nucleus Note=Only localizes to 5% of premeiotic tip and pachytene nuclei. SIMILARITY: Belongs to the flavin monoamine oxidase family."}
{"protein": "MAESKCPFKSQGSRSNVAGGGTRNTDWWPEQLKLNILRQHTTVTNPLGADFDYAAAFNTLDYDALKKDLTALMTDSQEWWPADFGHYGGLFIRMAWHSAGTYRVFDGRGGAGQGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGDKISWADLMILTGNVALESMGFKTFGFAGGRADTWEADESAYWGRETTWLGNDARYEKGFSGSDKQGTVIADEASHKTTHSRELENPLAAAHMGLIYVNPEGPDGNPDPVAAAHDIRVTFGRMAMNDEETVALIAGGHTFGKTHGAAPADNVGKEPEAAGLEAQGLGWQNSHGSGKGPDTITSGLEVTWTKTPTKWSNQFLEYLFKFDWELTKSPAGAHQWVAKNADDIIPDAYDAFKKHKPTMLTTDLSLRFDPAYEKISRRFLENPDQFADAFARAWFKLTHRDMGPRARYLGPEVPGEVLLWQDPIPAVNHALIDTVDTAALKRDVLATGVNPSKFISTAWAAASTFRGSDKRGGANGARIRFAPQRSWEVNNQPWLQESLSALEGVQSRFNASRPDRKQVSLADLIVLAGCAAVEQAAHDAGFPVRVPFTPGRMDASQDETDVESFSHMEPIADGFRNYAKPYVHGRAEHYLVDKAQLLNLSAPEMTVLVGGLRVLNTNYDGSAHGVFTSRPGVLSNDFFVNLLDMNTAWQAGHNGEIFEGADRKSGAKKWTATRADLVFGSHAELRAVAEVYASADGQRKFVNDFVAAWNKVMNLDRFDLQGKQFIYPRL", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
{"protein": "MTKFWIGTSWKMNKTLAEARLFAEALKAADAGRSPDIQRFVIPPFTAVREVKEILSGTSVKVGAQNMHWADQGAWTGEISPLMLKDCNLDIVELGHSERREHFGETNETVGLKVEAAVRHGLIPLICIGETLEDRESGRAAAVLEEEVRGALSKLSEAQKQAEILFAYEPVWAIGENGIPASADYADARQAEIIAVAQSVLARRVPCLYGGSVNPGNCEELIACPHIDGLFIGRSAWNVEGYLDILARCATKVQAN", "text": "FUNCTION: Catalyzes the isomerization of D-erythrulose-4P to L- erythrulose-1P. FUNCTION: Catalyzes the isomerization of D-erythrulose-4P to L- erythrulose-1P. Involved in the degradation pathway of erythritol, that allows B.abortus to grow on this compound as the sole carbon source. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family."}
{"protein": "MTINTKNIVVVGAGVFGVSVANHLYRELGGTYAIKLVTASNYVYFLPSAVRLTVSKDYTKSILPLKNVLDSGIEVIKDTAASFDDKEVVLGSDRAIKFDILVLATGSKWADPIGSTYTFGDNYKEYFEREASRISDADHILFLGGGFVNCELAGELLFKYLEEIRSGKKRISIIHNSDKLLPDSGLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYIDADLIYRGVGISPNVPVNSISDLCDKKGFIQVEKNFRVKAVEAGNVFAIGDVTNFRYHGLVKRDNWVDVLTRNVISSLQEGTEASLVDADCLETGHAPSGVSLGPNAGFGQFPLPLLGTINIPSFLISRAKSKNLFSDKMEPLFKK", "text": "FUNCTION: Putative FAD-dependent oxidoreductase involved in the resistance to cercosporin and other singlet oxygen-generating photosensitizers. Translocates from mitochondria to the nucleus under apoptotic conditions, where it degrades DNA and induces apoptosis. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Nucleus Note=Translocates from mitochondrion to the nucleus upon apoptosis induction. SIMILARITY: Belongs to the FAD-dependent oxidoreductase family."}
{"protein": "MEEKLEQAYLYDFYGELLNEHQRQVYEDFVFNDLSLGEIASEEGISRQGVADLIKRCNKKLLDYEAKLHLVEKFMSIKSDIRRIHELTNDFKKSHNELLMNEIEAISNQILEEL", "text": "FUNCTION: Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. SIMILARITY: Belongs to the UPF0122 family."}
{"protein": "MARAARRSTTELLWDAIRYGWAQPWTARFRGGIVTVVGAVLLLAIATYNATDPSFNAVTGEPASNALGGLGAAISDILMQSLGLSAWGIALLMLVFGVTRVAQADPDADRKDLRQRALVGALGLLALSAVLAAPPPPAIWQLEKGLGGFWGDSLLHMVAAVLSFAHIPGATIIAAILFGIAAIAALGFAIGVREVDPDAIHAAVSNALQPRARPEPEPEPAPAAKPVRARREKAEPAAPRAGRLPPLEADEDETPIAASQPAAAQRAYTPPPAVQDDEDDFEDSLDARPMAIAKPKTPVKESGREAREQQKAFDFEEDAGFQLPELAMLAKSKPRSSEVDAAALRQNARLLESVLAEFGVKGQIDQIRPGPVVTMYELVPAPGVKTARVVALADDIARSMSVISCRVAVAQGRNAIGIEMPNQRRETVYLRDLLSSADYEKASQILPMALGETIGGEPYIADLAKMPHLLIAGTTGSGKSVGVNAMILSILYKLPPEKCRFIMVDPKMLELSVYDGIPHLLAPVVTDPKKAVVALKWTVREMEDRYRRMSKIGVRNIGGYNEKANEAAAKGEHFERTVQTGFDDAGRPIYETEQIRPEPMPYLVVVIDEVADLMMVAGKDIEGAVQRLAQMARAAGIHLIMATQRPSVDVITGTIKANFPTRISFQVTSKIDARTILGEQGAEQLLGQGDMLYMAGGGRITRLHGPFVSDGEVEAVARFLRDQGIPQYLDEVTAGGDEEQEEAIEGAFSGEGGANDLYDHAVAVVTRDRKASTSYIQRRLQIGYNRAASLMERMEKEGVVGAANHAGKREILAPPTPPL", "text": "FUNCTION: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Note=Located at the septum. SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family."}
{"protein": "MLDNIKIKLQYWLPKIWLTRLAGWGANKRAGKLTKLVIDLFVRQYHVNMQEALQPDTASYRTFNEFFVRPLRPGIRPVDPHAHRLVQPADGVLSQFGPITDGKLIQAKNHDYTLEALLAGNYMMADLFRDGLFATIYLSPRDYHRLHMPCDGVLREMIYVPGDLFSVNLLTADNVPNLFARNERVICLFDTEFGPLAQILVGATIVGSIETVWAGVVTPPREGIIKRWTYPQAGEEGAVVLAKGEEMGRFKLGSTVINLFTAGDLQFAAHLNIMSVTRMGEPFAEVRQDEQTPVVFPEGTELEENDAAQPPVAATSEPVQADGQNPAAEVSGQTGHKPDAP", "text": "FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily."}
{"protein": "MAAIEPSGLHPGERDSSCPQEGIPRPSGSLELAQEYLQQFKVTMTQLQQIQASLLCSMEQALKGQDSPAPSVRMLPTYVRSTPHGTEQGDFLVLELGATGASLRVLWVTLTGTKEHSVETRSQEFVIPQEVILGAGQQLFDFAARCLSEFLDAYPVENQGLKLGFNFSFPCHQTGLDKSTLISWTKGFRCSGVEGQDVVQLLRDAIQRQGTYNIDVVAMVNDTVGTMMGCELGTRPCEVGLIVDTGTNACYMEEARHVAALDEDRGRTCVSIEWGSFYDEEALGPVLTTFDDALDHESLVPGAQRFEKMIGGLYLGELVRLVLVHLSQHGVLFGGCASPALLSQNSILLEHVAKMEDPATGIAHVHTVLQGLGLSPQASDAELVQRVCMAVCTRAAQLCASALAAVLSRLQHSREQQTLHVAVATGGRVFEWHPRFLCILKETVMLLAPECDVSFIPSVDGGGRGVAMVTAVAARLATHRRILEETLAPFQLSLEQLTAVQAQMREAMIRGLQGESSSLRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVRVAEGSVQITNQVYSIPEYVAQGSGQKLFDHIVDCIVDFQKRQGLSGQSLPLGFTFSFPCKQLGLDQGILLNWTKGFNASGCEGQDVVYLLREAIRRRQAVELNVVAIVNDTVGTMMSCGYDDPCCEMGLIVGTGTNACYMEELRNVASVPGDSGHMCINMEWGAFGDDGSLSMLGTCFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQKTQCLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLTLTSDDALMVLEVCQAVSRRAAQLCGAGVAAVVEKIRENRGLQELTVSVGVDGTLYKLHPHFSRLVSVTVRKLAPQCTVTFLQSEDGSGKGAALVTRVACRLTQMACV", "text": "FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D- fructose 6-phosphate, respectively) (PubMed:5871820). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:5871820). SIMILARITY: Belongs to the hexokinase family."}
{"protein": "MSIITEVYAREVLDSRGNPTVEVEVYTEAGAFGRALVPSGASTGEYEAVELRDGDKARYLGKGVLKAVENVNDIIADKIIGFDVTDQIGIDKAMIELDGTPNKGKLGANAILGVSLAAARAAADELGVHLYEYLGGVNGKVLPVPMMNILNGGEHADNNVDVQEFMVMPVGAPNFKEALRMGAEILHALKAVLKGKGLNTGVGDEGGFAPNLKSNEEALETIMQAIKDAGYKPGEEVKLAMDAASSEFYNRETGKYELKGEGVTRTSEEMVTWYEEMITKYPIISIEDGLDENDWDGFKLLTERIGDRVQLVGDDLFVTNTTKLKEGIEKGIANSILIKVNQIGTLTETLDAIEMAKRAGYTAVISHRSGETEDSTIADIAVATNAGQIKTGAPTRTDRVAKYNQLLRIEDNLADLAEYHGNDTFYNLKK", "text": "FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds plasminogen when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence. FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. SUBCELLULAR LOCATION: Cytoplasm Secreted Cell surface Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. SUBCELLULAR LOCATION: Cytoplasm Secreted Cell surface Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. SIMILARITY: Belongs to the enolase family."}
{"protein": "MEYFDMRKMSVNLWRNAAGETREICTFPPAKRDFYWRASIASIAANGEFSLFPGMERIVTLLEGGEMLLESADRFNHTLKPLQPFAFTADQVVKAKLTAGQMSMDFNIMTRLDVCKAKVRIAERTFTTFGSRGGVVFVINGAWQLGDKLLTTDQGVCWFDGRHTLRLLQPQGKLLFSEINWLAGHSPDQVQ", "text": "SIMILARITY: Belongs to the Ves family."}
{"protein": "MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGALLCFLAYGILAAMEDEPSNDNLYLGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGQTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILRDHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTTNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY", "text": "FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity). FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily."}
{"protein": "MRMTTEEAFVKVLQRHGIDTAFGIIGSAFMPISDLFPRAGIRFFDCAHEGSGGMMADGFTRASGRMAMIIAQNGPGVTNFVTAVKTAYWNHTPMLVVTPQAANRTIGQGGFQEVEQMALFRDMVCWQEELRDPARIAEVLDRVIRKARRASAPAQINLPRDMFTKIIDIELPQGVDLPRPAPDAQALDRAAALLSSARFPVILNGAGVVLAEAIPDTVALAERLEAPVCTGYQHNDAFPGSHPLFAGPLGYNGSKAAMQLMSQADVVLCLGTRLNPFSTLPGYGIDYWPKAAAVIQVDINPDRIGLTRPVTLGIAADAGAVARGILARLGAQAGDQDRAERAARIATTKSRWAQELASMDHEEDDPGTSWNERARAAKPGWMSPRMAWRAITAALPPEAILSSDIGNNCAIGNAYPSFAAGRKYLAPGLFGPCGYGLPAIIGAKIACPETPVVGFAGDGAFGISVTELTAIGRADWPAITMVVFRNYQWGAEKRNSTLWYDDNFVGTELDLQVSYAGIAQACGLQGVVARTMEELTEALRKALADQAAGKTTLIEALINQELGEPFRRDAMTKPVVVAGIDPADMRPQPR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TPP enzyme family."}
{"protein": "MEPAFGEVNQLGGVFVNGRPLPNAIRLRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPTVVKHIRTYKQRDPGIFAWEIRDRLLADGVCDKYNVPSVSSISRILRNKIGNLAQQAHYDSYKQHQPAPQPALPYNHIYSYPSPITAAAAKVPTPPGVPAIPGSVAMPRTWPSSHSVTDILGIRSITDQVSDSSPYHSPKVEEWSSLGRNNFPAAAPHAVNGLEKGALEQETKYSQAPNGLPAVGSFVSASSMAPYPTPAQVSPYMTYSAAPSGYVAGHGWQHAGSTPLSPHNCDIPASLAFKGMQAAREGSHSVTASAL", "text": "FUNCTION: Transcription factor required for normal development of thymus, parathyroid glands, ultimobranchial bodies, teeth, skeletal elements of skull and larynx as well as distal limbs. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MMAVAAAQKNREMFAIKKSYSIENGYPSRRRSLVDDARFETLVVKQTKQTVLEEARSKANDDSLEDCIVQAQEHIPSEQDVELQDEHANLENLPLEEYVPVEEDVEFESVEQEQSESQSQEPEGNQQPTKNDYGLTEDEILLANAASESSDAEAAMQSAALVVRLKEGISSLGRILKAIETFHGTVQHVESRQSRVEGVDHDVLIKLDMTRGNLLQLIRSLRQSGSFSSMNLMADNNLNVKAPWFPKHASELDNCNHLMTKYEPDLDMNHPGFADKVYRQRRKEIAEIAFAYKYGDPIPFIDYSDVEVKTWRSVFKTVQDLAPKHACAEYRAAFQKLQDEQIFVETRLPQLQEMSDFLRKNTGFSLRPAAGLLTARDFLASLAFRIFQSTQYVRHVNSPYHTPEPDSIHELLGHMPLLADPSFAQFSQEIGLASLGASDEEIEKLSTVYWFTVEFGLCKEHGQIKAYGAGLLSSYGELLHAISDKCEHRAFEPASTAVQPYQDQEYQPIYYVAESFEDAKDKFRRWVSTMSRPFEVRFNPHTERVEVLDSVDKLETLVHQMNTEILHLTNAISKLRRPF", "text": "FUNCTION: Plays an important role in the physiology of adrenergic neurons. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Cell projection, axon Note=Expressed in dopaminergic axons and axon terminals. SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family."}
{"protein": "MARMAVLWRKMRDNFQSKEFREYVSSTHFWGPAFSWGLPLAAFKDMKASPEIISGRMTTALILYSAIFMRFAYRVQPRNLLLMACHCTNVMAQSVQASRYLLYYYGGGGAEAKARDPPATAAAATSPGSQPPKQAS", "text": "FUNCTION: Mediates the uptake of pyruvate into mitochondria. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family."}
{"protein": "MDAFKLLTRSIKLKGSQLGSSSISSHLPSAGEANNPQLFPASEADKTRGTKRKRESGEDTELPNEIPVPDFFGSGSTAAESPKAQRKRVTGKDADAEGQHGEETSMPEEERKSILKSHKIKMTDLRTPPFRAVDTDISGKKSKRKKKKVEEPPPLTRKQLKAAQRLYPEPLTSFDKLRTRYHISRRLSDNIASQGYTVPTEVQLGSLPLLLGNAPAPNERTADDESLRSQSEREPDLLVVAPTGSGKTLSFMIPLINKIMKHHHDNPGLKEILAIVVAPTKELVAQIVNEGRKLTAGTGVKVSAVRKGMRIVEERGQETRSLEEENDGDDSTASSDEEIHSSEGEKSKDIPLTKSDILVCTPLVLANALSDGGKRDVAPLPSVQKLVLDEADVLLDPLFREQTLSIWRACTHPQLRVGLWSATMGSNIEELTKSTIKERQELLGLKDESSLIRLVVGLKDTAIPNISHKLVYAATEQGKLLGLRQLLHPTSTSSSTTHLRPPFLIFTQTIARAIALHSELMYDIPAEAGGSSRIAVLHSELSDSKRSDVMAGFRKGEIWVLITTDLLARGVDFRGINGVVNYDIPNSSASYVHRVGRTGRAGREGGVAVTFYTKEDIPYVKNIANVISASENLRGTEEGERIPKWLLDALPSLSKNDKKDLKKYGVKARRPSTISDKTTSKKTRISTKSGFDRRMDNKRKGAIKGSQRRKAREQLNDEESEDDVWNGIDD", "text": "FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily."}
{"protein": "MSSRGGGVGGRRGGPGGASSVRGGERGRKRGRGALDAVEPRVPLPRGTGSGPGAGRDGAAAPVPALQPAEADVLSGEVETEMAAGMEAREGASSSSSASAPAVGEVEPPSRAVGALPPTSSKAVVLQARPGFGTVGTSCRVRANHFVVQLADKEIYHYDVAIAPELRSRERNRNIINELLRSHKKYLDGRRSPAYDGRKGMFTAGALPFTDREFVVKIANDPERGNQGEKEFKVTIKCAGAANLYMHSLKQFLAGTYPSQDRFSHKHLDIRILIVALNGGEDISATTFYKAQPVIDFALDYLNMNIRDAYSRFDQDGTRVSVVQYFNRQYSYSLKYINWPCLQAGSDSRPTYLPMEVCRIVKGQRYSRKLNECQVTRMLRLARETPEERENSILEIANENNYGNDYHAREFGIGVTNQLALVDARVLPAPMLKYHDSGQEKVCNPSIGQWNMNNKRMLNGGSINYWACLTFASCVRLAEVRTFCKELVRVCNSIGMQITGEPCVRIRQERQDHLDAAVRDIHRQSAEFLSQQGVIGQQLELLVIVLPDANATVFYGRIKRLCETELGVITQCCLARNVQNVGGRNTVLEDALHRRIPLLTDMPTMIFGADVTHPPAGEDSSPSIAAVVASMDWPEVSKYKCSVSSQSHREEIIADLFTEVKDSQNRLVYGGMIRELIESFRKANGSYKPGRIIFYRDGVSEGQFSQVLLSEMDAIRKACASIEEGYLPPVTFVVVQKRHHTRLFPEDHHARDQMDRSRNILPGTVVDTKICHPSEFDFYLCSHSGIQGTSHPTHYYVLFDENNFSADALQTLTYHLCYTYARCTRSVSIVPPVYYAHLAASRARHYLEEGSLPDHGSSSASAAGGSRRNDRGVPVKPLPEIKENVKQFMFYC", "text": "FUNCTION: Probably involved in the RNA silencing pathway. May bind to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them (By similarity). SIMILARITY: Belongs to the argonaute family. Ago subfamily."}
{"protein": "MKGPITFLLQLGAVYTSIASACKLSDLPILSAHGSYGSNQCIAFGGEQAVIDRLIDPQACDIPKLIEATADQLQDGLTKGCFTSVDLVKVRITLQTPYRQGNVLIIVVVQTYVARIAEVNSTVRAVTEINPDALTIAKQMDNERKMGKLRGPLHGLPIVIKNNIFTDDKMSSTAGSYAIFGARTSADATVATKLREAGLVIMGKSGASQWANFRSLNSTNGWSAYGGQVTAAYIKNQDPSGSSSGSGVASDLGLAFATLGTETSGSIVSPADKSNIVGLKPTVGLTSRRFVVPISERQDTVGPMARSVKDAAYLLQVIAGKDSNDNYTSAIPFDTIPDYVKACDINALKGKRIGVPRNVIKIFGSPQTVVDQFNQALAVMKKAGAIIVENTDFTSFAEFAQSPIPDDILYADSLTNLPAFFKQLKVNPHNITDLESLRRFTQHHRLEEYPSRDTARWDIALQKGIKNTDPKFWPMYQKNVKFGNEGGILGALRRHKLDAAVLPTDLSPYIPALIGSPIITVPMGVYPNGTKVNHDRELVTSGPGIPIGIGFMGDLWSEEKLIGLAYAFEQKTHARPKLKRFIQPKKEVKGIL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the amidase family."}
{"protein": "MDTQEEQRLIQQAKEGNDEAFTALFHYHYSFLYKYLLKLSLHPDLSEELVQETFLKGYIHLRSFQGRSKFSTWLISIASRLYLDHQKKRKREWKRNQTVTEETIRKIKWDVSAKGAEWSETLDLFSKLDPKLRTPVLLRHYYGYTYAEIGVMLQIKEGTVKSRVHKGLQQIRKEWDDE", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Positively regulates the expression of the sigY-yxlCDEFG operon upon nitrogen starvation. Also positively regulates ybgB. SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily."}
{"protein": "MANNPGAKKAIRKIARRTEVNTARRSRVRTFLRKFEDAIAKGDVAVAKAAFVEAQSELMRAVSKGVVHPNTGSRKVSRLAARLKKLDKAAA", "text": "FUNCTION: Binds directly to 16S ribosomal RNA. FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family."}
{"protein": "MLSILMQGLRLKKCFLPILVMFFLAGCVNLLGSSFTASLKNDANASSDFYIRKIEQTQNQQDLQTYKLLAARVLVTENKIPQAEAYLAELIDLNDEQKLDKSLIEAHISAIKGKNETAEYQLSLIHLTLLSPSQKSRYYEIVSRIAENRHDNISAIKARIQMDNFLSDIQRKQQNNDRTWALLRNTDSEVLNNTDAEGNITLSGWLTLAQLYNDNLNQPAQLIQTLLTWKNYYPTHTAAHLLPTELQGLANFQQTTLTQVGLILPLSGNTRLIGETIKNGFDDAKVNYNVQVHVFDSMKMSIEQIINQAKKQGINTLVGPLLKQNVDVIVNNPYLVQDLNVLALNSTPNARAIEHLCYYGLSPEDEAESAASKMWNDTVRIPLVLVPQNNLGRRTAAAFTLRWQQLLGTDANIKFYNQTADINFALKSGLSESTDGVYIIANNKQLAEIKAVLDNINPTLKLYASSRSNSPNSGPEHRLFLNNLQFSDIPFFKDRESEQYKKIEKMTNNDYSLMHLYAMGYDAWLLINQFNEFRQIPGFTIDGLTGKLSAGPNCNVERDMTWFQYQNGSIYPLNEQDDSII", "text": "FUNCTION: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the LpoA family."}
{"protein": "MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQLLEIPQAMKALEGVVMELEDCAFPLLAGLEATDDPKVAFKDADYALLVGAAPRKAGMERRDLLQVNGKIFTEQGRALAEVAKKDVKVLVVGNPANTNALIAYKNAPGLNPRNFTAMTRLDHNRAKAQLAKKTGTGVDRIRRMTVWGNHSSTMFPDLFHAEVDGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHIRDWALGTPEGDWVSMAVPSQGEYGIPEGIVYSFPVTAKDGAYRVVEGLEINEFARKRMEITAQELLDEMEQVKALGLI", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MHAGEAVQQLKKAFETVASFDFRDALSKASTPVTVVATNGPFGLAGLTCSAVCSVCDRPPTVLLCINRKSYAAGIIKSNGVLSVNWLAAGQAVISQTFAGVGSVPMEERFADKGWQTIATGAPYRMDAAVSFDCTIANIVDVGSHSVIFAEVVARNHAEECTPLIYHRRQYATTRSLAE", "text": "FUNCTION: Reductase component of a two-component system that degrades 2,4,5-trichlorophenol. TftC provides the FADH(2) required by TftD. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p- benzoquinone, which is chemically reduced to 2,5-dichloro-p- hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2- hydroxy-p-benzoquinone. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family."}
{"protein": "MRTLMIEPLTKEAFAPFGDVIETDGSDHFMINNGSTMRFHKLATVETAKPEDNAIISIFRADALDMPLTVCMLERHPLGSQAFIPLLGNPFLIVVAPLGDAPVSGLVRAFVTNGRQGINYHRGVWHHPVLTIEKRDDFLVVDRSGTGNNCDEHFFEEDERLILAPHQ", "text": "FUNCTION: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source. SIMILARITY: Belongs to the ureidoglycolate lyase family."}
{"protein": "MSETQIAPLTLNIQYTKDLSFEVPGAPAIYTLLRQAPTVNINLDVQVQRLQDDAHVYEVTLTTRAEATHPAPAESGNGAEGGKDLTVFIADLSYAGVFTLTGIPDNQIEPVLLVECPRLLFPFARNILADVTRDGGFPPVMLGPVDFVGLWQARRAQDDGETIANA", "text": "FUNCTION: One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SecB family."}
{"protein": "MLKEPSVRLREAIIEGNLLIVKRLLRRNPDLLTNIDSENGWSSLHYASYHGRYLICVYLIQLGHDKHELIKTFKGNTCVHLALMKGHEQTLHLLLQQFPRFINHRGENGRAPIHIACMNDYYQCLSLLIGVGADLWVMDTNGDTPLHVCLEYGSISCMKMLLNEGEVSLDDNVRDKGNWKPIDVAQTFEVGNIYSKVLKEVKKKGPPLGAGKKPSSFRTPILNAKATFEDGPSPVLSMNSPYSLYSNNSPLPVLPRRISTHTTSGNGGNRRSSITNPVFNPRKPTLSTDSFSSSSNSSSRLRVNSINVKTPVGVSPKKELVSESVRHSATPTSPHNNIALINRYLLPNKSNDNVRGDSQTATINDDGGGGNGGDATIGMGLRKDPDDENENKYKIKVNNGEPRRRVSLLNIPISKLRNSNNTRAED", "text": "FUNCTION: Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Vacuole membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MKTSILFVIFSLALLFALSAATEIEETDRACGQFWWKCGEGKPPCCANFACKIGLYLCIWSP", "text": "FUNCTION: Moderately inhibits voltage-gated sodium channels and weakly inhibits voltage-gated potassium channel (PubMed:17150181, PubMed:17618665, PubMed:23246579, PubMed:26721415). Inhibits the inactivation of rat Nav1.2/SCN2A (IC(50)=870 nM), rat Nav1.3/SCN3A (IC(50)=845 nM), rat Nav1.4/SCN4A (IC(50)=339 nM), human Nav1.5/SCN5A (IC(50)=335 nM) and human Nav1.7/SCN9A sodium channels (IC(50)=348 nM) (PubMed:26721415). The toxin delays the inactivation of sodium channels without affecting the activation and steady-state inactivation kinetics in the physiological range of voltages (PubMed:26721415). Site-directed mutagenesis of the sodium channel indicates that the toxin interacts with site 3 located at the extracellular S3-S4 linker of domain IV (PubMed:26721415). On potassium channels, it inhibits activation of channels with an IC(50) of 8.05 uM through a voltage sensor-trapping mechanism (PubMed:23246579). It increases muscle contraction in several assays (mouse phrenic nerve-diaphragm, toad heart, rat vas deferens) and is suggested to act both presynaptically and postsynaptically (PubMed:17618665). FUNCTION: Moderately inhibits voltage-gated sodium channels and weakly inhibits voltage-gated potassium channel (PubMed:17150181, PubMed:17618665, PubMed:23246579, PubMed:26721415). Inhibits the inactivation of rat Nav1.2/SCN2A (IC(50)=870 nM), rat Nav1.3/SCN3A (IC(50)=845 nM), rat Nav1.4/SCN4A (IC(50)=339 nM), human Nav1.5/SCN5A (IC(50)=335 nM) and human Nav1.7/SCN9A sodium channels (IC(50)=348 nM) (PubMed:26721415). The toxin delays the inactivation of sodium channels without affecting the activation and steady-state inactivation kinetics in the physiological range of voltages (PubMed:26721415). Site-directed mutagenesis of the sodium channel indicates that the toxin interacts with site 3 located at the extracellular S3-S4 linker of domain IV (PubMed:26721415). On potassium channels, it inhibits activation of channels with an IC(50) of 8.05 uM through a voltage sensor-trapping mechanism (PubMed:23246579). It increases muscle contraction in several assays (mouse phrenic nerve-diaphragm, toad heart, rat vas deferens) and is suggested to act both presynaptically and postsynaptically (PubMed:17618665). FUNCTION: Inhibits voltage-gated sodium channels, preferentially subtype Nav1.5/SCN5A (in cardiac myocytes), but also Nav1.6/SCN8A and Nav1.7/SCN9A (TTX-sensitive Nav in rat DRG neurons) and invertebrate Nav (in insect neurons) as well as voltage-gated potassium channels of the subtype Kv2.1/KCNB1. Is suggested to bind to site 3 of the sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. On potassium channels, inhibits activation of channels with an IC(50) of 8.05 uM through a voltage sensor-trapping mechanism (PubMed:23246579). Increases muscle contraction in several assays (mouse phrenic nerve-diaphragm, toad heart, rat vas deferens) and is suggested to act both presynaptically and postsynaptically. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 33 (Jztx-1) subfamily."}
{"protein": "MVSLLRCQSSKPYSSLICSLALGVAFALSGTAYAEETKPTETVPAPVVTPPKVTPPPATKNQVRFTKTGAFDSDYVVKLARKLAAKPYSVLKDPLPVGLAKLTYDEYRDIRFNPTASIWRDQGLPFQMQMFHRGFYFQDLIEIAIVEGNKATHLAYEPKYFTAGEVITQALPNDDIGYSGFRIHNQLNNNGVFDELMVFQGASYFRALGKGNAYGLSARGLALKTADPEGEEFPIFRAFWVERPHYDSNLIVVHALLDSPSVAGAYRFSVRPGDNTQIDVEATLFPRVELSKVGLAPSTSMFLHSLNGRHDTDDFRPEVHDSDGLLMFNGRGEHLWRPLANPRQLQVSAFSDNSPQGFGLIQRERSYAAYQDLEAQYERRPSLWIEPVGNWGQGAVVLTEIPTESEIHDNIVSFWKPRQPIPAGSEYHFAYRMSWGEEPAVKHNYVVVSRTASGRADIAKPTPRRLFVVDYQVNGAMPEELPLAKVEASGGIISNVVIAPNAANNGYRLAFELEPEGKELIELRAELKFPTPRQVETWLYRWTL", "text": "FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the OpgD/OpgG family."}
{"protein": "MSNRSQFVPSWLVPEAAGDLPLTVSRLSLLALAAAFAVGYGAGFAVPLEVQAGVYLLGMVAMNLPHGGYEHFENLRRRAASFQGKYIVAYLVGIAAFGALFFVAPVAGLGLAVTVAVAKGGFGGVQSMDALYGTDHLRTRPQRWLAAVVRGGAVMVVPMLFWTDVFYAFSSVMISIFDPSAVSALGGDIATRRLVLGGGYGALVVAHLGLGYRRAAGTGSFLADAAETLLLIAYFALVPVVIAVGLYFPLWYSARQVARSSAVDDTAMTQADATGMLDALDADDPARATLASWAVLIVGSVATFGLAAVLWLLSPQPLGGGGILVGLVAFWSIFVSIIALPHVVVGGWLDRTRGIWYVP", "text": "FUNCTION: Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal. FUNCTION: Is required for retinal production and bacteriorhodopsin biogenesis. Probably catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans- retinal. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Brp/Blh beta-carotene diooxygenase family."}
{"protein": "MALPCAFLSAAAAANATSFSSSPESRRCRSVHRVPSRPRPPLAPPARVMGKGNSKRKAANTRLWMRLDRRGGCEMILCDKSFVARRSGLPARDLRVLGPLLSRSPSILAREKAMVINLEFVRAIVTADEVLVLEPLAQEVLPFVEKLRKHFPLKSLDVDDVSTHMHTENQDGELAQDVSCYEVEGANHELPFEFQVLDFALEAVCLSYNSTISDLNRSAIAVLDDLMKSVSTRNLERVRSLKSSLTRLLASVQKVRDEVEHILDDNEAMAHLCTARKTKGQKDLLNTILFPETRLCRTHSSIENSTGIRTCVPSDSDAHILDMLLEAYFKQLDGIRNRIFLVRQYIVDTEDYISIQLDNKRNELLGLQLTLIIASFGIAINTFIAAAFAMNIPHRGYHFVIGVPFGQFVGATSFLCMSIVILLFTYAWRNRLLCT", "text": "FUNCTION: Putative magnesium transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35.5) family."}
{"protein": "MAYRDQPLGELALSIPRASALFRQYDMDYCCGGKQTLARAAARHDVDIDIIEAQLAQLAEQPIEKDWRAVPLADIIDHIVVRYHDRHREQLPELILQATKVERVHADKPNVPRGLTKYLTALHEELSSHMMKEEQILFPMIKQGMGRQATGPISVMEIEHDEAGELVDVIKHVTQNVTPPPEACTTWKAMYNGINEMIDDLMEHISLENNVLFPRALAGE", "text": "FUNCTION: Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RIC family. YtfE subfamily."}
{"protein": "MHRSESSYCREETTLCQGVNSTWVPPADTVPEVSLIPSSPPAPDSPAPSPKPGYGFSTCEEKHGDPRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGQSWKNLTSVEKRPFVEEAERLRVQHLQDHPNYKYRPRRKKQAKKLKRMDPSPLLRNEGFTRGQPMVNLSHFRNLHPLGGSGELESYGLPTPEMSPLDVLEPSEPAFFPPHMREDTDPVPFRTYQHGMDFSQEKTMREISLPYSSSPSHMGSFLRTPTPSAFYYKAHGGSPVCTPLGQLSPPPEAPALDAMDHLNQAELWGDFDRNEFDQYLNMSRTQRPGYSFPMSKLGAPRTIPCEENSLISALSDASTAMYYTPCITG", "text": "FUNCTION: Probable transcription factor. Binds to the consensus DNA sequence 5'-AACAAT-3'. Also binds 5'-CACAAT-3' and 5'-AATAAT-3' with similar affinity. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKPSLVLKMGQQLTMTPQLQQAIRLLQLSTLDLQQEIQEALESNPMLERQEDGDDFDNSDPLADGAEQAASAPQESPLQESATPSVESLDDDQWSERIPSELPVDTAWEDIYQTSASSLPSNDDDEWDFTARTSSGESLHSHLLWQVNLAPMSDTDRMIAVTIIDSINNDGYLEESLEEILAAIDPELDVELDEVEVVLRRIQQLEPAGIGARNLRECLLLQLRQLPSTTPWLNEALRLVSDYLDLLGGRDYSQLMRRMKLKEDELRQVIELIQCLHPRPGSQIESSEAEYIVPDVIVRKDNERWLVELNQEAMPRLRVNATYAGMVRRADSSADNTFMRNQLQEARWFIKSLQSRNETLMKVATQIVEHQRGFLDYGEEAMKPLVLHDIAEAVGMHESTISRVTTQKYMHTPRGIFELKYFFSSHVSTAEGGECSSTAIRAIIKKLVAAENAKKPLSDSKIAGLLEAQGIQVARRTVAKYRESLGIAPSSERKRLV", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Plays a role in the regulation of many virulence factors, motility, quorum sensing, mucoidy, a general mechanism for maintaining lytic phage in populations of bacteria, and biofilm formation. Positively controls the T6 secretion system by directly binding to the promoter regions of hcpA and hcpB, leading to their expression (By similarity). Thereby, allows to colonize several hosts efficiently including mammals, insects, nematodes and plants (PubMed:11717271). FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (PubMed:9595661). Plays a role in the regulation of many virulence factors, motility, quorum sensing, mucoidy, a general mechanism for maintaining lytic phage in populations of bacteria, and biofilm formation (PubMed:2152909, PubMed:12644493, PubMed:10792721, PubMed:26633362, PubMed:29760208). Positively controls the T6 secretion system by directly binding to the promoter regions of hcpA and hcpB genes, leading to their expression (PubMed:29760208). Thereby, allows to colonize several hosts efficiently including mammals, insects, nematodes and plants (By similarity) (PubMed:2152909, PubMed:9595661, PubMed:12644493, PubMed:10792721, PubMed:26633362, PubMed:29760208). SIMILARITY: Belongs to the sigma-54 factor family."}
{"protein": "MQRRDFLKYSVALGVASALPLWSRAVFAAERPTLPIPDLLTTDARNRIQLTIGAGQSTFGGKTATTWGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIEDDEILKLMLPKQWGIDDVPVIVQDKKFSADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPVKVSELPVLMGERFEVLVEVNDNKPFDLVTLPVSQMGMAIAPFDKPHPVMRIQPIAISASGALPDTLSSLPALPSLEGLTVRKLQLSMDPMLDMMGMQMLMEKYGDQAMAGMDHSQMMGHMGHGNMNHMNHGGKFDFHHANKINGQAFDMNKPMFAAAKGQYERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPKEHAYMAHCHLLEHEDTGMMLGFTV", "text": "FUNCTION: In vitro, in the presence of excess copper ions, exhibits ferroxidase and phenoloxidase activities (PubMed:11466290, PubMed:11527384, PubMed:11867755, PubMed:15317788, PubMed:15516598, PubMed:17804014, PubMed:25679350). Fe(2+) is an excellent substrate in the presence of excess Cu(2+), but is inactive in the absence of Cu(2+) (PubMed:15516598, PubMed:17804014). Oxidizes the phenolate iron siderophores enterobactin, 2,3-dihydroxybenzoate (2,3-DHB) and 3- hydroxyanthranilate (3-HAA) (PubMed:11466290, PubMed:15317788). Oxidation and thus inactivation of enterobactin could protect cells from the interaction of enterobactin with copper and play a central role as an interface between copper detoxification and iron homeostasis (PubMed:11466290, PubMed:15317788). Also oxidizes a variety of phenolic model substrates, including 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) (ABTS), p-phenylenediamine (pPD), 2,6-dimethoxyphenol (2,6-DMP) and 3,4-dihydroxybenzoic acid (3,4-DHB) (PubMed:11466290, PubMed:11527384, PubMed:17804014, PubMed:25679350). FUNCTION: Multicopper oxidase involved in copper homeostasis and copper tolerance under aerobic conditions (PubMed:11222619, PubMed:11399769, PubMed:11527384, PubMed:15516598). Is responsible for the oxidation of Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing Cu(+) from entering the cytoplasm (PubMed:15516598, PubMed:20088522, PubMed:25679350). Probably primarily functions as a cuprous oxidase in vivo (PubMed:20088522). SUBCELLULAR LOCATION: Periplasm Note=Exported via the Tat pathway (PubMed:10766774, PubMed:17218314, PubMed:27129241). Cytoplasmic CueO does not contain copper, even under copper stress conditions, and is transported as an apo-protein to the periplasm. Periplasmic CueO is readily activated by the addition of copper ions in vitro or under copper stress conditions in vivo (PubMed:27129241). Can also be exported by the Sec system (PubMed:17218314). SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MSGSGSGSGAGHGGGSGGSIREAGGSLGMMGATREEEYFRRQQKDQLDNLKKKLEADMTQSQQEIRDHEKVLEQHQQRLKEIEKGHGT", "text": "FUNCTION: Thought to be a regulatory component of the ATP-synthesizing complex in the mitochondria. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ATPase inhibitor family."}
{"protein": "WASQVSENRPVCKAIIQGKQFEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSTEILHCLGPDNQESTVQPMITSIPLNLWGRDLLQQWGAEITMPAPLYSPTSQKIMTKMGYIPGKGLGKNEDGIKIPFEAKINQKREGIGYPF", "text": "FUNCTION: Retroviral proteases have roles in processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution. This endogenous protein has retained most of the characteristics of retroviral proteases. SIMILARITY: Belongs to the peptidase A2 family. HERV class-II K(HML-2) subfamily."}
{"protein": "MKTRLGCLSNKSDSCSDFSEFLPPAQERTTRCLKLSNDEVTRWADSFDILLSNKYGLAAFRTFLKTEFSDENIEFWLACEDYKKIKSPAKMMSKANKIYKEFIDVHAPREVNIDHRTREETKNRLLEPTPHSLNEVQAKVYSLMEKDSYPRFIRSKIYQDLLNRTQIYCQRKSV", "text": "FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptors and dopamine receptors. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to G protein-coupled receptor signaling. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Membrane; Peripheral membrane protein; Cytoplasmic side Perikaryon Cell projection, dendrite Nucleus Note=Detected in Purkinje cell soma and dendrites. Associated with Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected in the nucleus after heterologous expression. Recruited to the cell membrane in the presence of GNAO1."}
{"protein": "MTEPSLLPAAKMEGLALLPLTSPCPRIPRARISRQPGRWAHLGCSPGLSTGPTNLQQHPQKPRPADCSHSRLSWAESLSMDGFWMEVERIQQRAEVKKEDCGEGRSQLLEGDTESQWLQDTGLSGLAGGLGLDGDHQGLLSTLTQTQVAAVCRRLDIYARSARRRQKAPVRDVRDIFGVFTSRELAPENGVSGMKWTKINSEDSASPLRSAEPGGPQELAGMEEVFNMDSAYSEQAAVLLQRAWPSPGGTTAWGKGPLPRFRIPKGRLGVTRIGDLSSRDMKKIPPLALIELTALYDILGLDLKRCKGGKWKGPDSGLFGVPLHSLLEADHRVFPSTQVPLLLQALLSCLEKRGLDTEGILRVPGSQARVKGLEQKLERDFYAGLVSWDKVHPNDASDLLKRFLRKLPVPLLTAEYLPAFASVPDIPDLKQRLQALHLLVLLLPEPNRNTLKALLEFLRKVAAQEQHNKMTLWNVSTVMVPSLFLPRGRPPKLTKGGKQLAEGAAEVVCMMVQYQDLLWTVASFLVAQVRKLNDSNGRRSQLCDGGLKTWLWRTHVDRDKAGEGLEATPKVAKIQVQATWPSMDLLQVPLNPSTRVTHVLKLFTEHLNPGSQPEEGSENPNSLLSHNTKPVTFLVYEVGGNIGERRLDPDAYLLDLYRANPHGEWVIRQSPT", "text": "FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state."}
{"protein": "MPLSYQHFRRLLLLDNEAGPLEEELPRLADEDLNHRVAEDLNLQLPNVSIPWTHKVGNFTGLYSSTVPVFNPDWLTPSFPDIHLHQDLIQKCEQFVRPLTKNEVRRLKLIMPARFYPKATKYFPLDKGIKPYYPENVVNHYFKTTHYLHTLWKARILYKRESTHSASFCGSPYSWEQELQHGSTSLNGEKGHGTESLCAQSSGILSRPPVGSTIQSKFQQSRLGLQHKQGQLANGKQGRSGRLWSRVHTPTRWPSGVEPSGTGHSDNLATRSTSRFHQSEVRKETNPSLSTSKGHTSTGHAVELNTVPPSTVGSESQGSVFSCWWLQFRNTEPCSDYCLSHIINLLEDWGPCYEHGEHHIRTPRTPSRVTGGVFLVDKNPHNTTESRLVVDFSQFSRGTTRVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHLPLHPAAMPHLLVGSSGLSRYVARVSSTSRIYNHQHGTLQNLHHSCSRNLYVSLLLLYQTFGRKLHLYSHPIILGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDLVLGAKSVQHLESLYTAVTNFLLSVGIHLNTAKTKWWGYSLHFMGYIIGSWGTLPQEHIVQKIKNCFRKLPVNRPIDWKVCQRIVGLLGFAAPFTQCGYPALMPLYACITAKQAFVFSPTYKAFLCKQYMNLYPVARQRPGLCQVFADATPTGWGLAIGHQRMRGTFVAPLPIHTAELLAACFARSRSGADIIGTDNSVVLSRKYTSFPWLLGCAANWILRGTSFVYVPSALNPADDPSRGRLGLCRPLLRLPFRPTTGRTSLYADSPPVPFHQPARVHFGSPLHVAWRPP", "text": "FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA- DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery. SIMILARITY: Belongs to the hepadnaviridae P protein family."}
{"protein": "MTSPDTQTSSLYAKREPVFPKRVSGKFRSLKWWIMGVTLGIYYIAPWLRWDRGPNLPDQAILVDLANRRFFFFMIEIWPHEFYFVAGLLIMAGLGLFLFTSAAGRVWCGYACPQTVWTDLFILVERWVEGDRNARIRLLRQRWDLEKTRKYLTKWTLWLLIGLATGGAWVFYFTDAPTLLVDLLTGNAHPVAYITMATLTATTFAFGGFAREQICIYACPWPRIQAAMMDEETITVAYREWRGEPRGKLKKGEPLSPDQGDCIDCMACVNVCPMGIDIRDGQQLACITCALCIDACDEVMDKIGKPRGLIGYLALTDERAEREGRSPRSAWRHVFRLRTLIYTALWSGVGLALIVALFLRSPIDINVTPLRNPLYVTLSDGSIRNTYDVRLRNKQGEARDYQISVTSEADLALSLEGHPATVVTVPANETMTQRVYIIAGKGTPAAEAERTDLRLWVEDLAAGQRVHHDTIFNGRGN", "text": "FUNCTION: Involved in a membrane generated redox signal; required to maintain repression of photosynthesis gene expression in the presence of oxygen. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MIIDTTEVQAINSFSILESLKEVYGIIWMLIPIFTLVLGITIGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLLFKENLLPSRGDTRLFSIGPSIAVISILLSYLVIPFSYHLVLADLSIGVFLWIAISSIAPVGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSSSTVDIVEAQSKYGFWGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVASYLNLLVSSLFVTVLYLGGWNLSIPYIFVPEVFEITKRGRVFGTIIGIFITLAKTYLFLFIPIATRWTLPRLRMDQLLNLGWKFLLPISLGNLLLTTCSQLISL", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MSRKQLALLEPTLVRQALLDAVKKLSPMVQWRNPVMFIVWVGSLLTTLLAIAMAGGALTGSATFTAAVSIWLWFTVLFANFAEAMAEGRSKAQANSLKGVKKTAFARKLRAPQHDAPVDHVPAEDLRKGDVVLVEAGDIIPCDGEVIEGGASVDESAITGESAPVIRESGGDFASVTGGTRILSDWLVIRCSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTLVFLLATATIWPFSAWSGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQASAFLPARGVEERTLADAAQLSSLADETPEGRSIVVLAKQRFNLRERDLQSLHATFVPFTAQTRMSGINIDQRMIRKGSVDAIRRHVEANGGHFPADVDKQVEEVARQGATPLVVAEGEKVLGIIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRLTAAAIAAEAGVDDFLAEATPEAKLALIRQYQSEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIEVVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAAVYPQLAMLNVMGLHSPSSAILSAVIFNALIIVFLIPLALKGVSYRPLSASAMLRRNLWIYGLGGLLVPFIGIKAIDLLLTLSGLV", "text": "FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily."}
{"protein": "MASLRFSVTFPALFSLLLSLWVVDACTSRKLISNNEQEGQNISHLFKDGEFEDPTMYMFFKISDLKLGTKLPIYFNKNDLRKVPPLLTRQEADLIPFSESNLDFLLNHFSISKDSPQGEAMKETLQRCDFKAIEGEYKFCGTSLESMLDLAKKTIASNADLKVMTTKVMVPDQNRISYALHNYTFAEVPKELDGIKVLGCHRMPYPYVVYYCHGHKSGTKVFEVNLMSDDGIQLVVGPAVCHMDTSMWNADHVAFKVLKIEPRSAPVCHFFPLDNIVWVSK", "text": "SUBCELLULAR LOCATION: Protein storage vacuole."}
{"protein": "MNGTRNWCTLVDVHPEGQTAGSVDVLRLTLQSELTGDELERIAQKAGRKTYAMVSSHSTSHSLASELVESNDGHEEIIKVYLKGRSGDKMIHEKNINQLKSEVQYIQEARNCLQKLREDISSKLDRDPGDSVHKQEIQVVLEKQNGLSEGPLTTYSSPPEVDTHINEDVESLRKTVQDLLVKLQEAEQQHQSDCSAFKVTLSQYQREAKQSQVALQRAEDRAEQKEAEVGELQRRLQGMETEYQAILAKVREGETALEELRSKNVDCQAEQEKAANLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDTTIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQNRAKTENLGSIRISKPPSPKPMPLIRVVET", "text": "FUNCTION: Involved in the mineralization and structural organization of enamel. SUBCELLULAR LOCATION: Secreted Note=Secreted at a very early stage of enamel formation, and tightly bound to the surface of the growing crystallites. SIMILARITY: Belongs to the tuftelin family."}
{"protein": "MSFAEKITGLLARPNQQDPIGPEQPWYLKYGSRLLGIVAAFFAILFGLWNVFSIITLSVSCLVAGIIQMVAGFVVMLLEAPCCFVCFEQVNVIADKVDSKPLYFRAGLYITMAIPPIILCFGLASLFGSGLIFGTGVVYGMMALGKKASAEDMRAAAQQTFGGNTPAQTNDRAGIVNNAQPFSFTGAVGTDSNV", "text": "FUNCTION: A calcium channel that regulates synaptic endocytosis and hence couples exo- with endocytosis. Required in the nervous system and necessary in photoreceptor cells (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Note=Upon fusion of the synaptic vesicle with the presynaptic membrane, protein is present in the periactive zones, where endocytosis is known to occur. SIMILARITY: Belongs to the calcium channel flower family."}
{"protein": "MGRRPARCYRQIKNKPYPKSRYCRGVPDPKIRIYDVGMKKKGVDEFPFCVHLVSWEKENVSSEALEAARIACNKYMTKYAGKDAFHLRVRVHPFHVLRINKMLSCAGADRLQTGMRGAFGKPQGTCARVSIGQVLLSVRCKDGNSHHAQEALRRAKFKFPARQKIIVSRKWGFTKFNRTDYIKWKSQNRILPDGVNAKLLGCHGPLANRQPGKAFINACT", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL16 family."}
{"protein": "MSLGQRLALLAIRLQEPQRVASFQRLCGVEVPLGSPKAGEDAETEVRGAPGDPRRRPRQSGADGSPAKPDCCGAPNGVRNGLAAEPGPTGPRRAGSLRRNSLTGEEGELAKVSNLPLYYLFCFGTELGNELFYIIFFPFWIWNLDPFVGRRLVIIWVLVMYLGQCTKDIIRWPRPASPPVIKLEIFYNSEYSMPSTHAMSGTAIPIAMILLTYGRWQYPLIYGLILIPCWSSLVCLSRIYMGMHSILDVIAGFLYTILILIIFYPLVDLIDNFNQTYKYAPLIIIGLHLILGIFSFTLDTWSTSRGDTAEILGSGAGIACGSHAAYNLGISLDPSLHTLPLAIPPLTVTLFGKAILRVVIGMLLVLFVRDIMKKVTIPLACKLFGIPCHDLRQARQHMEVELPYRYITYGTVGFSITFLIPYIFSFIGIS", "text": "FUNCTION: Specifically dephosphorylates sphingosine 1-phosphate (S1P), dihydro-S1P, and phyto-S1P. Does not act on ceramide 1-phosphate, lysophosphatidic acid or phosphatidic acid. Sphingosine-1-phosphate phosphatase activity is needed for efficient recycling of sphingosine into the sphingolipid synthesis pathway. Regulates the intracellular levels of the bioactive sphingolipid metabolite S1P that regulates diverse biological processes acting both as an extracellular receptor ligand or as an intracellular second messenger (By similarity). Involved in efficient ceramide synthesis from exogenous sphingoid bases. Converts S1P to sphingosine, which is readily metabolized to ceramide via ceramide synthase. In concert with sphingosine kinase 2 (SphK2), recycles sphingosine into ceramide through a phosphorylation/dephosphorylation cycle (By similarity). Regulates endoplasmic-to-Golgi trafficking of ceramides, resulting in the regulation of ceramide levels in the endoplasmic reticulum, preferentially long-chain ceramide species, and influences the anterograde membrane transport of both ceramide and proteins from the endoplasmic reticulum to the Golgi apparatus (By similarity). The modulation of intracellular ceramide levels in turn regulates apoptosis (By similarity). Via S1P levels, modulates resting tone, intracellular Ca(2+) and myogenic vasoconstriction in resistance arteries. Also involved in unfolded protein response (UPR) and ER stress-induced autophagy via regulation of intracellular S1P levels (By similarity). Involved in the regulation of epidermal homeostasis and keratinocyte differentiation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family."}
{"protein": "MGRTLTSVLVVFISMAGWLGGADTGSISGILGMRDFQSRFADRYNPITNSYSYSAWRQALLTGTVNAGCLFGAMLSSPFTEAIGKKYSIAFFSGCYIIGQILLVTAVPSWVQIMVGKLFTGLTIGALSVLSPGYQSEVAPPQIRGAVVSTYQLFQTCGTLIAACINMGTHKLRKTASWRTSFGINILWGIFLMVGVLFLPESPRYLIYKGRDEEALRIMCQTAELDPESEIIQTNFNTIKSDIEMEMAGGKARWPEVFGKEVRYRTVLGFLTMLLRELIGNNYYFYYATQVFKGTGMTDIFLPAVILGAINFGTTFGALYTIDNLGRRNPLIFGAAFQSICFFIYAAVGDRKLIYKNGTSDHRAGAVMIVFSCLFLFSYCCSWGPMGWVIVGETFPIRYRSKCAAVATSGNWLGNFMVSFFTPFISNSIGFKLGYIYACINMTSAFQIFLMAKETKGLTLEEVNELYESDIKPWDSYKYVRQIESRRIHFSKEEEKREREKSKGYRGQEERFIENADGADNDDSSASSESFASAGAHSRSVFPRRSNVSEESHPTWV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQAVAAAAVQQSTSQQATQGTSGQAPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT", "text": "FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473, PubMed:27193682, PubMed:2194289, PubMed:2363050, PubMed:2374612). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, PubMed:27007846). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TBP forms the TFIID-A module together with TAF3 and TAF5 (PubMed:33795473). TBP is a general transcription factor that functions at the core of the TFIID complex (PubMed:33795473, PubMed:27193682, PubMed:2194289, PubMed:2363050, PubMed:2374612, PubMed:9836642). During assembly of the core PIC on the promoter, as part of TFIID, TBP binds to and also bends promoter DNA, irrespective of whether the promoter contains a TATA box (PubMed:33795473). Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III (PubMed:26638071). Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC during RNA polymerase I-dependent transcription (PubMed:15970593). The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter (PubMed:15970593). SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA (PubMed:15970593). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TBP family."}
{"protein": "MASAQWLGLVLALLSSLAASGFPGSPFRLLGKRSLPEGAVNGIEIYSTKINCKVTSRFAHNVVTTRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGHVKEKEVAKKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEELLKRHKGKYEMYLKVQPKQLVKHFEIDAHIFEPQGISMLDAEASFITNDLLGSALTKSFSGKKGHVSFKPSLDQQRSCPTCTDSLLNGDFTITYDVNRESPANIQIVNGYFVHFFAPQGLPVVPKNVVFVIDVSGSMYGRKLEQTKDALLKILEDMREEDHLNFILFSSDVTTWKEHLVQATPENLQEARAFVKSIQDQGSTNLNDGLLRGISMLNTAREEHRVPERSTSIVIMLTDGDANSGESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLESLALENDGFARRIYEDSDANLQLHGFYEEVANPLLTSVEMEYPKNAILDLTQNSYQHFYDGSEIVVAGRLADEDMNSFKADVKGHGALNDLTFTEEVDLKETEAALKEREYIFGNYIERLWAYLTIEQLLEKRKNARGEEKENLTAQALDLSLKYHFVTPLTSMVVTKPEDNEDQTAIADKPGEEQAQAASQTSFSAYRTSYQPPLGSAASYQPPLGTPYYYVDGDPHFIIQVPEQDNAICFNIDEEPGTVLRLIQDPATGLTVNGQIIGDKKSSPDSATRKTYFGKLGIASAHMDLRIEVTTEKISLWNEVGRSTFSWLDTVTVTQDGLSMTINRKKNMVVSFGEGVTFVVILHQVWKNHPIHQDFLGFYVVDSHRMSAWTHGLLGQFFHPFDFKVSDVHPGSEPTKPDATMVVKNRQLTVTRGSQRDYRMDARAGTKVACWFVHNNGEGLIDGVHTDYIVPNLF", "text": "FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ITIH family."}
{"protein": "MGARLGRRARADAPAAPSAGPAPYERRVRWLREIQSTLRERRPERARQLLRLLRQDLGLEGNLLTDILHRNVTFLNLVDPISHDLLVNLARDLQCPKKDHELWKSSDKICRQLIYHLTPHSKRKHHRKTQSSLKSSLQKTLLVGETVDLSGIPLSARDVQHISRYLDTRGVELVVLDLSFTELSDELLHLLLPSLWALPRLTQLLLNGNRLTRAAARELTEAIKDTAKFPVLAWVDLGNNVDVSSLPQPLLVGLRRRLSQHTSLPTIYEGLDLEPGGGMAETTAAVSTWGSAATEAGPEPQGCCAR", "text": "FUNCTION: May suppress myogenic differentiation by modulating MYOG expression and Erk1/2 signaling. SIMILARITY: Belongs to the LRRC75 family."}
{"protein": "MSRRSIIEKKTIKSDPIYRNRLVNMMVNRILKNGKKSLAYRIFYKAMKNIKQKTKKNPLSILRQAIHRVTPNVTIKARRVGGSTYQVPVEIKSAQGKALAICWLLRASKKRLGRNMAFKLSYELIDAARDSGEAIRKKEETHRMAEANRAFAHFR", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "VAFATSFTVCWTPYYVLGIWYWFDPEMLNRVSDPVNHFFFLFAFLNPCFDPLIYGYFSL", "text": "FUNCTION: Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G- proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSNITDPQMWDFDDLNFTGMPPIDEDYSPCRLETETLNKYVVIITYALAFLLSLLGNSLVMLVILYSRGGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMILSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNVSLALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL", "text": "FUNCTION: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSKRPADIIISTPGSKVRRRLNFDSPYSSRAAVPTVRVTKRQSWTNRPINRKPRWYRMYRSPDVPKGCEGPCKVQSFESRHDVVHIGKVMCISDVTRGIGLTHRVGKRFCVKSIYILGKIWMDENIKTKNHTNSVMFFLVRDRRPVDKPQDFGEVFNMFDNEPSTATVKNMHRDRYQVLRKWHATVTGGQYASKEQALVRRFFRVNNYVVYNQQEAGKYENHTENALMLYMACTHASNPVYATLKIRIYFYDSVSN", "text": "FUNCTION: Encapsidates the viral DNA into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. The CP of bipartite geminiviruses is not required for cell-to-cell or systemic movement. SUBCELLULAR LOCATION: Virion Host nucleus Note=It is actively transported into the host cell nucleus. It may be exported out of the nucleus through a nuclear export signal for cell- to-cell movement and spread (By similarity). SIMILARITY: Belongs to the geminiviridae capsid protein family."}
{"protein": "ASINYTYIIYVIGVITILYASFSTLRTIDIKELIAYSSVSHAAVYLIGAFSNTIQGIEGSIALGLAHGFVSSGLFICAGGILYDRSSTRLITYYRGMAQIMPIFSVLFFILALGNSGTPLTLNFIGEFMSLYGVFERMPILGVLASTSIVFSAAYTIFMYNRIVFGGSYSIYFRENIGDVTRREFIMLLVFVILTVLFGIYPAPILDGLHYSVSYLIYNIN", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family."}
{"protein": "MAGNCSWEAHSTNQNKMCPGMSEARELYSRGFLTIEQIATLPPPAVTNYIFLLLCLCGLVGNGLVLWFFGFSIKRTPFSIYFLHLASADGMYLFSKAVIALLNMGTFLGSFPDYIRRVSRIVGLCTFFTGVSLLPAISIERCVSVIFPTWYWRRRPKRLSAGVCALLWMLSFLVTSIHNYFCMFLGHEAPGTVCRNMDIALGILLFFLFCPLMVLPCLALILHVECRARRRQRSAKLNHVVLAIVSVFLVSSIYLGIDWFLFWVFQIPAPFPEYVTDLCICINSSAKPIVYFLAGRDKSQRLWEPLRVVFQRALRDGAEPGDAASSTPNTVTMEMQCPSGNAS", "text": "FUNCTION: Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily."}
{"protein": "MITTGTPTTRRSAAGTAGADLCPVERCGEPARPGGRLERQQPSPLSPGQRPLADANARRPVAVFAETFGLLAGQLDRQTRREGRAMLRLIDSTPIPLGKLCGWAKSNGRIRGMKMHVVYDPDSDCPRLLDITDANVNDAQIGRTIAIESGATYIFDKGYCHYGWWTAIAEAKAFFVTRPKSNMGLKVVRQRRIKVAEGDGFTVIDDATVRLASKGDSKLPIPLRRLTVKRADGDTITLLTNDRKRPAVAIAALYKGRWQIELLFRWIKQHLKIRSFLGNNDNAVRLQLFAAMIAYALLRIAARLNRITMPILRFTDLVIRCLFERRDIAAIERPPPVNPSHRRPRCSPHQMSFAYV", "text": "SIMILARITY: Belongs to the transposase 11 family."}
{"protein": "MSQNSESIRMVLIGPPGAGKGTQAPNLVKQFGAAHLSTGDMLRSQVAKGTPLGVEAKKIMDQGGLVSDEIMVGMIKQELETNPACGKGFILDGFPRTIPQAEKLDQMLAERGTPLEKAVELKVDDELLVARITGRLVHPSSGRSYHKLFNPPKVEMTDDVTGEPLVQRSDDNAEALMKRLNSYHQQTEPIVEFYKKTGIWAGVDASQAPDNVWTSILKVLGKN", "text": "FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. SUBCELLULAR LOCATION: Cytoplasm, cytosol Mitochondrion intermembrane space Note=Predominantly mitochondrial. SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily."}
{"protein": "MTKKEQSIWRKEMLALMNEDADWYRNEDTERFKRIQELAKKIETASTRQFSSHISKERFEAYQRMGLQFKEIAEEFHITTTALQQWRKDNGYPIYNKNNRK", "text": "FUNCTION: Might be involved in the expression of prgA, but is not required for activation of the expression of prgB."}
{"protein": "AKPAAENLSLVVHGPGDLRLENYPIPEPGPNEVLLKMHSVGICGSDVHYWQGRIGDFVVKKPMVLGHEASGTVVKVGSLVRHLQPGDRVAIQPGAPRQTDEFCKIGRYNLSPTIFFCATPPDDGNLCRFYKHNANFCYKLPDNVTFEEGALIEPLSVGIHACRRAGVTLGNKVLVCGAGPIGLVNLLAAKAMGAAQVVVTDLSASRLSKAKEVGADFILEISNESPEEIAKKVEGLLGSKPEVTIECTGVETSIQAGIYATHSGGTLVLVGLGSEMTSVPLVHAATREVDIKGVFRYCNTWPMAISMLASKSVNVKPLVTHRFPLEKALEAFETSKKGLGLKVMIKCDPSDQNP", "text": "FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)- dependent oxidation of various sugar alcohols. Is mostly active with xylitol, L-iditol and D-sorbitol (D-glucitol) as substrates, leading to the C2-oxidized products D-xylulose, L-sorbose and D-fructose, respectively (PubMed:1459146). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism (By similarity). May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane protein Cell projection, cilium, flagellum Note=Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MQPSFTPSGGKWLSIAVILLVIGLVVGFAAGRFTAPIQQSKELNTFAAGSLKYALGNDFNPEFNNLTGIKVGMTFSGSISGAKEVQAGKQYSVFVSASAPVLYQNLINNTHYASWQIVFSANEMAITWTNSKYAINPSWPYWFENITKNSTIVAASNASLDPSGFQAIETMKLAGILYTNWSDPFVQMAFNHNESLFLQYNKAYNTWFEKLGYKANDSLALYHQIFISKYLNHTTKLTTVEIGLDGYLTSGAADYALTYVSQAINQNLSYYKSATGGNGLPIWINLGSLNKTIDQFYEQINESGPAWDNVGNLPGAPILYSVTIINNYTSPYAVQYVYDLITQMGQHYLAMSRFDPLSQPFGINISNMPKQLQAVVTPPPSYLPVSAYE", "text": "SIMILARITY: Belongs to the bacterial solute-binding protein 1 family. WtpA subfamily."}
{"protein": "MSTVQTVLGTITPNLLGRTLTHEHVALDFEHFYRPPPPDFESELKAKISMSTLGYVRLYPYSSKENVRFYDGEALEAAKKDVLLYKKHGGGSIVENSSYGLKRNLEFIVELAKSTGVHFIAGTGHYIHAMQDASHGSLTVEQMSDLYSKDIITGLQVNGKVVKCGFIGEVASVYPIHDFEKNAIKAAGEIQEVLGCGVSMHPHRVTKAPFEIMRLYLEAGGRADKCVMSHLDRTIFDIDELLEFAKLGCYIQYDLFGTECSFYQLNTSVDMISDGQRIDNLIKLIKEGLVDKLLMSHDIHTKHRLTSYGGHGYHHIHTNILPRMFDRGVTLEQVEQITVTNPANWLAFDP", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family."}
{"protein": "MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGKYRPSSDTATHLELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGDAEPLHTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARSINPQLNHIDSFLMNKHFMRKHGPNAYYGQK", "text": "FUNCTION: Catalyzes the isomerization of L-ribulose 5-phosphate to D- xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization. SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily."}
{"protein": "MKAPPPPSPVAKRARVSPFVFLLVLFLLLFSFLYGEDLKELLGSQAQARPSLHFNAAAAGDGIELPAATAATTEGRTTTRRWRGRLPFAANGDGEEEEEECDVFSGRWVRDEAARPLYREADCPYIPAQLACEAHGRPETAYQRWRWQPRGCALPAFDAAAMLDRLRGKRVMFVGDSLGRGQFTSLVCLLLAAVPDPAARSFATSPDQQRSVFTAAAYNATVEFYWAPFLLQSNADNAAVHRISDRMVRRGSIGHHGRHWEGADVIVFNTYLWWCTGLQFRILEDGPFDAGGNSSTTTWVSTEEAYAMAFREMLQWAREHMDFATTRVFFTSMSPTHGKSQDWGGGEPGGNCYGETEMIGDAAYWGSDSRRGVMRAIGEVLDGDGADVPVTFLNVTQLSLYRKDAHTSVYKKQWTPPTPEQLADPKTYADCVHWCLPGLQDTWNELLYTKLFYP", "text": "FUNCTION: Probable xylan acetyltransferase required for 2-O- and 3-O- monoacetylation of xylosyl residues in xylan (PubMed:29569182). Possesses extremely low activity in vitro (PubMed:29569182). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily."}
{"protein": "MEFSVAHPAVKAFMCGSLSGTCSTLLFQPLDLVKTRLQTLQSGVQPGTGRVGMVTVFVNVLRTEKLLGLWRGVSPSFVRCIPGVGIYFSTYFTLKQRYFSSGAPGPLQAVLLGAGARCVAGVFMLPVTVIKTRFESGRYRYSGVFGALRSVCQTEGPKALFSGLMATLLRDAPFSGIYVMIYSQTKHLLPPEISQSSYAPVANFSCGVLAGVLASVLTQPADVVKTHIQVSPDVFSRTSDVVRYIYKEHGLVGFFRGAVPRSLRRTMMAAMAWTVYEQLMAQIGLKS", "text": "FUNCTION: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. Required during erythropoiesis. FUNCTION: May play a role as pro-apoptotic protein that induces caspase-dependent apoptosis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily."}
{"protein": "MATTQAQIQRPIANFSPSLWGDQFIKNDPGAKAAEKHCKAVEELKKEVMNMITAAGSNLVEAMNLIDTLERLGISYHFEKEIDQKLKHFFNLNKDYSDESYDLYTVSLHFRLFRQHGHRISSDIFGRWIDESGKFKEGLKTDGKGLLSLYEASYLRTRGETILDDALEFATATLNSIAPHLESPLSKQVVHALIQPLHYGNPRIEAHNFISIYEENQDKNEFLLRFAKLDYNLLQMLHKEELNEVSRWWKELDLVSKLPYARDRVVECFFWAMGVYHEPQYSRARIMLTKTITMTSIIDDTYDAYGVIEELDIFTEAIERWNMEEMKKLPEYIQPFYKALLELYEQFEEELAEEGRSYAAHYAIESLKELVRSYHVEAKWFIQGYLPPFEEYLKNALITCTYCYHTTTSLLGVESAVEEDFEWLANKPKMLVAGLLICRVIDDIATYEVEKERGQSATGIESYMRDNNATIEEAVAKFFEIATDAWKDINEECLMPSPYSRDVLMRILNLERIIDVTYKGNEDGYTQPEKVLKPHIIALFVDPIKM", "text": "FUNCTION: Sesquiterpene synthase that catalyzes the conversion of farnesyl diphosphate to (-)-5-epi-eremophilene. SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily."}
{"protein": "MQYVMGRTNSMTRGFLNKRRVLEKCRTAKQKIHYCISRYFHYLPPVLAILLPIGSWPFLSEQQWWYGSFLFPVVSSLGWLFAIGRRERQLRAAAGQLLEAKIRKLTEQDEGLKNIRETIEKRQKETDRLKLHNDKLVEQLGQAREVFIQAKGRYDHMEELSRRLKEENQQLQIQLEAAVRERNEKILENQELLQELKETLAYQQELHDEYQATFVEQHSMLDKRQAYIGNLEAKVQDLMCELRNLLQLEMGAKTNLPGKPVASRDVVAQLVLEFRKIVFRVETTEAADSLTALRYTRTDPSAHNYSLACRQLFDGLREENLGMLFIYAPFAQRVLFANALFNDWTGYGLEDFLNRESDVVLEGFAQWERDLLTESRVERSGKIVIKTKAFGATPFYYCVVTLDKGPFAQHILGVLYPAKASFFTNLSYI", "text": "SIMILARITY: Belongs to the UPF0242 family."}
{"protein": "MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTETGEPQLNPIDGPLPEDNEQSGYAQQDCVLEAMAFLEESHPGIFENSCLETMEVVQQTRVDRLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMDKEEMEITTHFQRKRRVRDNMTKKMVTQRTIGKKKQRVNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMMTYITKNQPEWFRNILSIAPIMFSNKMARLGKGYMFESKRMKLRTQIPAEMLASIDLKYFNESTRKKIEKIRPLLRDGTASLSPGMMMGMFNMLSTVLGVSILNLGQKKYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKKKSYINRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGHTQIQTRRSFELKKLWEQTRSKAGLFVSDGGPNLYNIRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDGQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAMVSRARIDARIDFEAGRIKKEEFSEIMKICSTIEELRRQK", "text": "FUNCTION: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs. SUBCELLULAR LOCATION: Host nucleus Host cytoplasm. SIMILARITY: Belongs to the influenza viruses polymerase PB1 family."}
{"protein": "MNREEQFGILESLLFAAGDAGLSTEQLTEVMEITHIEALNLLELLSERYNGNADRGLILLELAGTFQLATKKAHAEYLRKLVEVPSNTVLSQASLETLAIIAYRQPVTRMEVDEVRGVQTDGPIRTLVAKGLVTDKGRVDGAGRAKLYVTTSEFLDAFGLNSLEDLPKLADPEADDPDQNEMDLFFDRFNQSKEQEEE", "text": "FUNCTION: Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with two foci at the outer edges of the nucleoid region in young cells, and at four foci within both cell halves in older cells. SIMILARITY: Belongs to the ScpB family."}
{"protein": "MNDAINHTACETLFTQARTHNGWLDKPVSDAQLQAVWDLMKMGPTSANCSPARIVFVRSAEGKEKLRPTLSSGNLQKTMQAPVTAIVAWDSAFYDRLPTLFPHGDARSWFTSSPQLAEETAFRNSSLQAAYLIFACRARGLDTGPMSGFDREKVDAAFFADNGWKSNLLVNIGYGDPGKLYGRLPRLSFDEACLLA", "text": "FUNCTION: May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily."}
{"protein": "MAILSLRAPGPWQAMQVWADRTLLTPHTGVTSQVLGVAAAVMTPLPGGHAAGRTREARWDAMEYDEKLARFRQAHLNPFNKQSGPRQHEQGPGEEVPDVTPEEALPELPPGEPEFRCPERVMDLGLSEDHFSRPVGLFLASDVQQLRQAIEECKQVILELPEQSEKQKDAVVRLIHLRLKLQELKDPNEDEPNIRVLLEHRFYKEKSKSVKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPCVSSKVSHQAEYELNICPETGLDSQDYRCAECRAPISLRGVPSEARQCDYTGQYYCSHCHWNDLAVIPARVVHNWDFEPRKVSRCSMRYLALMVSRPVLRLREINPLLFSYVEELVEIRKLRQDILLMKPYFITCREAMEARLLLQLQDRQHFVENDEMYSVQDLLDVHAGRLGCSLTEIHTLFAKHIKLDCERCQAKGFVCELCREGDVLFPFDSHTSVCADCSAVFHRDCYYDNSTTCPKCARLSLRKQSLFQEPGPDVEA", "text": "FUNCTION: Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. Involved in bone resorption. SIMILARITY: Belongs to the DEF8 family."}
{"protein": "MAKSARTKTARPATRTETDSFGPIEVPSDRYWGAQTERSRQNFRIGTDRMPISLVHALGIVKLAAAQSNRELGLLDQRRASAIIRAAREVIDGSLDDHFPLVVWQTGSGTQTNMNLNEVIANRANELLGGELGAKKPVHPNDHVNMSQSSNDSFPTAMHIAAASRITADLVPALGELLRALRKKEKEFAKIVKIGRTHTQDATPLTLGQEFSGYAAQVESGIARLKVAVKELYPLAQGGTAVGTGLNAKPRFARLFAKHVAGITKLPFTSAANKFEALASNDAYVLAHGAISSVATGLFKIANDIRLLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVCCQVFGNHTAITVAGSQGHFELNVYKPVLAYNMLHSIRLMADAARSFTEHCVSGIRADEKRISELMQRSLMLVTALAPKIGYDNAAKVAKTAHANGTTLKEEALRLGFVTADEFDRLVQPEKMTKPG", "text": "FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase subfamily."}
{"protein": "MAAAEQKGKKPRTDGAEAEPVDAALLQSIEKLQEIQDEIEKVNEEACDKVLELEQKYNEVRRPVYVRRNKIIKQIPDFWLTAFLSHPMLGELLTEDDQKIFKHLESIDVDDSEDIKSGYSITLTFSPNPYFEDTKLTKTYSFSDDEAVKVKATSIRWKKGMDIANDRAYTKKGDKRILIDESFFTWFNSEKNRSFAHGAMDEVADVIKEDLWPNPLKYFNNEFEEELELLDDDDEVSDDDDEEEDDEDQGEGEEDGEEN", "text": "FUNCTION: Acts as histone H2A/H2B chaperone in nucleosome assembly. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
{"protein": "MGALEAERAANNATALETQSSPEDLGQPSPLRKIISVASIAAGVQFGWALQLSLLTPYIQLLGIPHKWSSYMWLCGPISGMIVQPIVGYHSDRCESRFGRRRPFIAAGVALVAVSVFLIGFAADMGHSFGDKLENKVRTRAIIIFLTGFWFLDVANNTLQGPCRAFLADLAAGDAKKTRVANACFSFFMAVGNVLGYAAGSYTNLHKMFPFTMTKACDIYCANLKTCFFLSITLLLIVTFSSLWYVKDKQWSPPQGDKEEKTSSLFFFGEIFGAVRHMKRPMVMLLIVTVINWIAWFPFILYDTDWMGREVYGGNSDGDERSKKLYDQGVQAGALGLMFNSILLGFVSLGVESIGRKMGGAKRLWGCVNFILAIGLAMTVLVTKSAEHHREIAGPLAGPSSGIKAGVFSLFTVLGIPLAITYSIPFALASIFSTNSGAGQGLSLGVLNIAICIPQMIVSFSSGPLDAQFGGGNLPSFVVGAIAAAVSGVLALTVLPSPPPDAPAMSGAMGFH", "text": "FUNCTION: Responsible in a heterologous system for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport biotin, and probably maltose at a lesser rate. In planta, the role of SUC5 for the transport of sucrose seems to be negligible. Plays a role in the nutrition of the filial tissues during early seed development and is probably involved in the import of biotin into the endosperm and the embryo epidermis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation symporter transporter (TC 2.A.2.4) family."}
{"protein": "PIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAIGRYPIPPPDSKELELMFGCPVEGDSPVTETSPRQRAPGRPMSSYGSDSRPPMAIFELLDYIVNEPPPKLPNGVFGSEFQDFVNKCLIKNPAERADLKQLMIHAFIKRSEAEEVDFAGWLCSTIGLNQPSTPTHAAGV", "text": "FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily."}
{"protein": "MIGKEATIPDIVLELQELVQPTDLHCYEELSEEETEEEPRFIPYKIVVPCCFCDSKLRLIVVATPFGIRSQQDLLLEEVKLVCPGCREKLRHV", "text": "FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). SUBCELLULAR LOCATION: Host cytoplasm Host nucleus Note=Predominantly found in the host nucleus. SIMILARITY: Belongs to the papillomaviridae E7 protein family."}
{"protein": "MPMLRLYARVLQLLGKEAMLGWVLAGANLLLAAAQFAEPVLFGRIVDVLSGNLSTGAMAQPAQSPWPLLLAWAVFGLFTIGCGAAVALHADRLAHRQRQAILTDYFEHVLQLPLTYHTGTHSGRLMKVMLNGTDALWRLWLGFFREHFAALMSLVVLLPLSIYINWRLALLLFALCVVFTVLTTLVVRKTYAMQGEVEESYSDLSARASDALGNIALVQSFVRIDAEVQGLRFVADRLLAMQMPVLSWWALVTVITRASTTITVLAIFTVGIALHEQGLTSVGEIVMFVSFATMLIQKLEQVVGFVNSVFMEAPRLQEFVNVLDAVPAVRDRLDAIDPGRLSGLVEFDNVSFSYDGKRPAIEDLSFTALPGQTIALVGATGAGKSTAIALLHRAFDPQSGVIKIDGMDVRGLTLAGLRRNIGVVFQEALLFDRTIADNLRVGKPDATEEEMRIAASRAQALDFIERSELKFDTNAGERGRMLSGGERQRLSIARALLKDPPILILDEATSALDAVTEAKVNLALDEVMKGRTTFVIAHRLSTIRHATRILVFDNGRVIESGSFDELLARRGYFAELAHAQFMVQDSARSAMPAAQPEGIPEF", "text": "FUNCTION: Involved in Beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Beta- (1-->2)glucan exporter (TC 3.A.1.108.1) family."}
{"protein": "MLVKTLGAHFAAGQNAKKCSCCALLISLLCVLLLSLNPLPVTSHVTSAGSSTALSSDPNLVLVNKCCEKFEIHVDHECQQVNETDYFQPMFTSYGGEQNRPVKFKFVIGIPNCGSMQMWPIYHYAGSSDKLVLLDDGRLRHYTNAENEAEERHGIQSDYEEDIAGSLEPLYHDYDKGLYCIDKATSSTGEENVLFANICLARKEIKWSDSNFLLRKILNPIFHGISLVILLVIAIIYFILPTLRDLVGNIVTTIAMCLMVSQAADLVRIFTELTSHVSFIVADIILCFSLLAAFFWLNSFGFYIWKTFRSRNVFLRVTDGRKYCYYSAYAWGCTATMAALAVFAHFFLDAESYKQEHMVGEQETIGWLGICIFFAPIACTILVNIFFYVTTRKLINRRTVYGRIAHKLKANFIMFSLMLLVMSIAWLFLIMSWLQMEGLLYAHIVVNALQTPLLLYICVLRQRHVTFLLKKTCCYNEPPSANDWGDELHYMNGNDY", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth subfamily."}
{"protein": "MRAIISLLLISTMVFGVIEAVSVQKSLKIFEGERGDCVGESQQCADWSGPYCCKGYYCTCQYFPKCICVNDNGK", "text": "FUNCTION: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insects. Modifies presynaptic voltage- gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neurons (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 03 (aga-4) subfamily. Aga sub-subfamily."}
{"protein": "MITGKITCLHITDVRFPTSLDQHGSDAMHTDPDYSAAYVVIETDAADGLKGHGLTFTLGKGTEVVVCAVRALSRHVIGKALEDIVNNFRDFYRQLTSDGQLRWIGPEKGAVQLATAAVLNAVWDLWAKKEKKPLWKLLVDMDPHQLVSCIDFRYITDALTEEEALKILQNGKQGQRDREEHMLTSGYPAYTTSCAWLGYSDEQLKKLCSDALKEGWTRFKVKVGADLKDDIRRCELIRDMIGPDNIMMLDANQRWDVQEAISWVKDLAKYKPLWIEEPTSPDDILGHATISKELSPVNIGVATGEQCHNRVMFKQFLQAKALQYLQIDSCRLGSVNENLSVLLMAKKFNVPVCPHAGGVGLCELVQHLILFDYICVSGSLDNRMCEYVDHLHEHFTYPVIINRAAYMPPKDPGYSTEMKEESVLQYQFPDGAVWKKLILEKKVEV", "text": "FUNCTION: Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. May down-regulate thymidylate synthase activity, possibly already at the RNA level, by promoting the degradation of TYMS mRNA via an antisense RNA-based mechanism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. ENOSF1 subfamily."}
{"protein": "MEEQQLGAALDKSAAELSVMDVYDIAAALGLELERVIERTGAELLSRLVPRVVRVLELLEVLVSRSSSSPDTDELRLELDRLRLERLERLEKEKKHKKELELVEDVWRGEAQDLLCQISQLQEENKTLLNNLSIRESPLTEEDIQKQEGMTERERQVMKKLKEVVDKQRDEIRAKDRELTLKNDDVEALQQQMSRLMKINQDVRHRVSVVEAQGKSLIQQKVELEAAAQTQQQEVSSLRQEVSRLKEKLKEQSRSNEEEAQEPVGPPSPAQEALCDEDLSTVDLKDPNRPRFTLQELRDVLHERNELKAKVFMLQEEIAYYRSEEQEEENGPPLPDPSETLRTNPRSNFQPESGIKRLFSFFSRDRSVSQRRMMLNVEPVGDAVGSWTGKQEDVYTETAQEALQHM", "text": "FUNCTION: Plays a role in the regulation of cell shape and polarity. Plays a role in cellular protein transport, including protein transport away from primary cilia. Neuroprotective protein (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium. SIMILARITY: Belongs to the RILPL family."}
{"protein": "MASLDRVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRLHEYREGTPEEKTYYIELWDVGGSVGSASSVKSTRAVFYNAVNGIILVHDLTNKKSSQNLYRWSLEALNRDLQPTGVLVTNGDYDREQFADNQIPLLVIGTKLDQIPEAKRSEVLTRTAFLAEDFNAEEINLDCTNTRCLAAGSSNAVKLSRFFDKVIEKRYSREGNLIPGFSDRKRFAGGNFKSLHYD", "text": "FUNCTION: Required for KRAS signaling regulation and modulation of cell proliferation (By similarity). Regulator of KRAS prenylation, and probably prenylation of other small GTPases (By similarity). Required for lymphocyte development and function (By similarity). Not required for myeloid cell development (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MLDMNPQETYTAPEEVNTPSRPIDENALLQRHQVMVKRVVNQLRVHATSHCSIEDMQQIGLIALVEAGRRYGDIDDTHFPAFAVCRVRGAILDELRRLDWRSRKTRQQAHELNDVTRDLTRSLGRMPTDSEIIKALGTDEQDYYNRQNAALAGEMQSLDQLMENSTDSHFGGQYDGMEHEHIRRSLDSALGRLSKRDQLLLTLFYQHELNLHEIALVLDLTPPRICQLHKQALKQLNQLMSS", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This alternative sigma factor is specific for the flagellin gene (fliC) expression. SIMILARITY: Belongs to the sigma-70 factor family."}
{"protein": "MSEEKKLQFVTEGQADVEKQSEREEAIQGAIETERKKRVRKTLRDQLRANAIKKQKKSNRESAEVKKLNQLSKEETRYFKELEKNREQEIQRLTQFHKDKDYEYEKKRQQLLSRSPDKQSGKPDTLSSNQNNGSTERVILKVKNKNRPRLVVKK", "text": "FUNCTION: Involved in telomere length regulation and promotes fully efficient non-homologous end-joining (NHEJ) by a mechanism activated in postdiauxic/stationary phase. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the FYV6 family."}
{"protein": "MKQPATMKWSASISFLLLLNFAEPRVLHTNEFGIESTLDSSQCPTEKNMFNVATIVVAQFVQDATKAEVNKMSSDALAAMKENTGDGCLENQLSVFLDEICHETELSNKYGFSGCCNQSGVERHQCLLARKKTAPDSVPPFHFPETAESCPAYEENRAMSINTFIYDVSKRNPFLYAPTILYLAAQYDKAVPACCKADNMEECFQTKRASMAKELREGSMLNEHVCAVIRKFGSRNLQAVLIIKLSQKFPKANITEIRKLALDVAHIHEQCCHGNAMECLQDGESVMTHMCSQQEILSSKTAECCKLPTIELGYCIIHAENGDKPEGLTLNPSEFLGDRNFAQFSSEEKLLFMASFLHEYSRNHPNLPVSVILKTAKSYQEILEKCSQSETPSKCQDNMEEELQKHIQESQALAKQSCNLYQKLGPYYLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKRSACGEGLADIYIGHLCLRHEANPVNSGINHCCSSSYSNRRLCITSFLRDETYVPPPFSEDKFIFHKDLCQAQGRALQTMKQELLINLVKQKPEMTEEQHAAVTADFSGLLEKCCKDQDQEACFAKEGPKLISKTREALGV", "text": "FUNCTION: Binds estrogens, fatty acids and metals. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family."}
{"protein": "MDSNIDVEILSILSEASAPVGAKIIADSLKDRGYDIGERAVRYHLKVLDENSLTKKLGYSGREITEKGIEELEKANISFRIGSVFSQVIEKLYLSDFPSKVLINTAKFEGDYKTIKEMVLRSFEAGYSVGDYLNIKKKGNTVSVETLCSITFDNFLLKNGIIPTPEYGGIVKFEDYEPVNFEGVIDFKSSSIDPLVAFIMQGKTDVIGVIENGEGLVPANFRVIPKSSEKQFETILKKDMLNSVLAYGTENVLGMNLNPEQIGVVLVGGLTPLCVPHESGYTADISAATQLKDISSMEKKTKGFLEAKKKKGKFKVTPVLSKMLSKMQTINYDIEDKKGNVVVNTAKIPIEYKEEAINALKDSYENKLAISDRLKVECDDKFLNAYTICSLTVDGVFLKNKIPVIPYYGGILEVKADKKRFIEAIDYEGTSLDPHEVFFNKADGKNYILAGIRKVPMSASEKLIELNEKLGWNSIIEIGRPNNDICGVRVEKCMFGITTIGGTNPFANIRKNNIPVEMKTLHKSIDYSELTHYDDI", "text": "FUNCTION: Transcriptional repressor of nitrogen fixation and assimilation genes. Binds to two tandem operators in the glnA and nif promoters, thereby blocking transcription of the genes. SIMILARITY: Belongs to the NrpR family."}
{"protein": "MINKIFALPVIEQLTPVLSRRQLDDLDLIVVDHPQVKASFALQGAHLLSWKPVGEEEVLWLSNNTPFKTGVALRGGVPICWPWFGPAAQQGLPSHGFARNLPWALKAHNEDDNGVMLTFELQSSEATRKYWPHDFTLLARFKVGKTCEIELEAHGEFATTSALHSYFNVGDIANVKVSGLGDRFIDKVNDAKEGVLTDGIQTFPDRTDRVYLNPEACSVIHDATLNRTIDVVHHHHLNVVGWNPGPALSVSMGDMPDDGYKTFVCVETVYATAPQQATEEKPSRLAQTICVAKR", "text": "FUNCTION: Probably functions as a hexose-6-phosphate 1-epimerase. SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family."}
{"protein": "MLFSLRELVQWLGFATFEIFVHLLALLVFSVLLALRVDGLVPGLSWWNVFVPFFAADGLSTYFTTIVSVRLFQDGEKRLAVLRLFWVLTVLSLKFVFEMLLCQKLAEQTRELWFGLITSPLFILLQLLMIRACRVN", "text": "FUNCTION: Involved in the regulation of cellular calcium homeotasis (PubMed:25996873). Required for spermatogenesis (PubMed:25996873). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
{"protein": "MAISVDQTPAGKYPAKVHAKRVAARIQELGHGDSGIIYLEGQKTHMIEDSDGEMPFRQRRNFFYLSGCPLPDSYLTYDIKADKLTIFIPPIDPASVIWSGLPLSVEEALEIYDVDAVLSTAEVNASLAHYCSAQGGKKVFAIADQVSPHITFLPFQEIDFDVLKRAVEESRVVKDSYEIALLRRANEISSKAHVAVFKAATSARNERELEAIFVGACMSSGCREQSYHPIFASGTNAATLHYQKNDEDLVDSVTGQRRLNMLIDAGAEYRNYCADITRVVPLSGKFSPESREIYDIVLEMQNSSLAMIKAGVMWEDVHSTSHRVAIRGLLKLGILRSTEDELFEKGISVAFFPHGLGHYLGMDTHDTGGNPNYADKDPKFKYLRLRGPLASGGVVTVEPGIYFCRFIIDPYLSSPDLGKYINADVLERYWSVGGVRIEDNVVVTDSGYDNLTTAPKLPEEIERLATEK", "text": "FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MRLRNGTVATALVFITTFLSLSWYTAWQNGKEKLMAYQREFHALKERLRIAEHRTLQRSSELHAILDHFRRMIKEANGSRDALNHFSDETQKLIKDLTNRKALQVPNIYYHMPHLLNHDGSLQPAVQVGLGRTGVSVVMGIPTVKRRVKSYLKETLHSLIDKLSPEEKLDCVIIVFVGETDLEYVNSVVASLQKEFATEISSGLVEVISPPATYYPDLNNLKETFGDSKERVRWRTKQNLDYCFLMMYAQRKGIYYIQLEDDIVAKQNYFSTIKNFALQLSSEDWMILEFSQLGFIGKMFQAPDITLIVEFILMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKSNLRIRFRPSLFQHVGLHSSLAGKIQKLTDKDFLKPLLHKIHVNPPAEVSTSLKVYQGHTLEKTYLGEDFFWAITPVAGDYILFKFDKPVNVERYLFRSGNPEHPGDQLWNTTVEVLPYRKDIVELRSDTKDKRLSDGFFRIGKFEDGLAEGPVNSYLNPISALRLSVLQNSAVWVILNEIHIKRNPAD", "text": "FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity). SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N- acetylglucosaminyltransferase A soluble form]: Secreted. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 54 family."}
{"protein": "MSDAYLALETGDVVEATARAPGMARGELVFTTAYTGYEESLTDPSYEAQVLTFAYPLIGNYGVRPERTESDRVHPSAVVARELTDDVADWLRTEGVPAVDGIDTRDLVLDIRDGGAMQVGIAAGPDASPATARAQLADCPRLSARTEIGAHVSVDTAETHGNGDTTVALVDCGAKRSIIDAFVARGATVHRLPYDATPADIAAVDPDLLFISNGPGDPANFDAAEHLVDEYIGTVPIAGICLGQQIVARALGGDTEKMDFGHRGVNQPVLDHDSGRVVMTTQNHGYTVADPGDLTVTQVNVNDGTPEALDSAPLDVLTRQYHPEANPGPHDTRGFFDDVLAMADASYTPATAD", "text": "SIMILARITY: Belongs to the CarA family."}
{"protein": "MLMLSKTAGAIPRPPRSNVRGFIRRFNVQPRALFHHKLVLGIETSCDDTAAAVVDETGNVLGEALHSQTEVHLKTGGIVPPVAQQLHRENIQRIVEEALSASGVSPSDLSAIATTIKPGLALSLGVGLSFSVQLVNQFKKPFIPIHHMEAHALTIRLTHKVGFPFLVLLISGGHCLLALVQSVSDFLLLGKSLDIAPGDMLDKVARRLSLIKHPECSTMSGGKAIEHLAKEGNRFHFTINPPMQNAKNCDFSFTGLQHVTDKLITHKEKEEGIEKGQILSSAADIAAAVQHATACHLAKRTHRAILFCQQKNLLSPANAVLVVSGGVASNLYIRRALEIVANATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGLGILHDVEDIRYEPKCPLGIDISREVAEAAIKVPRLKMTL", "text": "FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the KAE1 / TsaD family."}
{"protein": "MQQKTKLFLQALKYSIPHLGKCMQKQHLNHYNFADHYYNRIKLKKYHLTKCLQNKPKISELARNIPSRSFSCKDLQPVKQENEKPLPENMDAFEKVRTKLETQPQEEYEIINVEVKHGGFVYYQEGCCLVRSKDEEADNDNYEVLFNLEELKLDQPFIDCIRVAPDEKYVAAKIRTEDSEASTCVIIKLSDQPVMEASFPNVSSFEWVKDEEDEDVLFYTFQRNLRCHDVYRATFGDNKRNERFYTEKDPSYFVFLYLTKDSRFLTINIMNKTTSEVWLIDGLSPWDPPVLIQKRIHGVLYYVEHRDDELYILTNVGEPTEFKLMRTAADTPAIMNWDLFFTMKRNTKVIDLDMFKDHCVLFLKHSNLLYVNVIGLADDSVRSLKLPPWACGFIMDTNSDPKNCPFQLCSPIRSPKYYTYKFAEGKLFEETGHEDPITKTSRVLRLEAKSKDGKLVPMTVFHKTDSEDLQKKPLLIHVYGAYGMDLKMNFRPERRVLVDDGWILAYCHVRGGGELGLQWHADGRLTKKLNGLADLEACIKTLHGQGFSQPSLTTLTAFSAGGVLAGALCNCNPELLRAVTLEAPFLDVLNTMMDTTLPLTLEELEEWGNPSSDEKHKNYIKRYCPYQNIKPQHYPSVHITAYENDERVPLKGIVSYTEKLKEAISEHAKDTGEGYQAPNIILDIQPGGNHVIEDSHKKITAQIKFLYEELGLDSTSVFEDLKKYLKF", "text": "FUNCTION: Serine peptidase whose precise substrate specificity remains unclear (By similarity). Does not cleave peptides after a arginine or lysine residue (By similarity). Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex (By similarity). May play a role in the regulation of synaptic vesicle exocytosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus, trans-Golgi network Cytoplasm, cytoskeleton Golgi apparatus Nucleus Note=Co-localizes with AP-1 in the trans-Golgi network (By similarity). Co-localizes with MAP2 and ACTB on the cytoskeleton (By similarity). Co-localizes with STX6 and GOSR2 at the Golgi apparatus (By similarity). SIMILARITY: Belongs to the peptidase S9A family."}
{"protein": "MCRSVSNMLDRISGLSKDASPNSTTTIQEIITLEKCLTSKVSALFLICKMLKIPACPVCDVPCRIEPHFGGIACAACAAFFRRTVSLNIGYMCKREKLCRKARKSCRACRFERCVKSAGLQRDYVRQLLTPRNTPLYILNRQDNTGGEIVRAFASPTMPKPEPTPQLGFSDILKVSNSSLFKFYLNQVEKAVKLRQKNTLTIKTNAELLKIVATQQELALEACRTCPGMDLLDKEDRKVVQKYFVFSNVWIESTWLYSLAKEHLETENNLNFDINLKKFIEQVKSTLLFSFSQFKLNIFELAAFKAICIWKLIYHETSRAMKIIAQEHYDGVASALRNYYETHTSMDHSEIAIRIGEITLLVVSIFQLYHDMAKLYVQIGIPF", "text": "FUNCTION: Orphan nuclear receptor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family."}
{"protein": "MTQLAIGKPAPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPAEGHRFNPAKLLIDPCARQIDGEFKDNPLLHAGHNEPDYRDNAAIAPKCVVVVDHYDWEDDAPPRTPWGSTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALHEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASACLRYWVETCHVDGFRFDLAAVMGRTPEFRQDAPLFTAIQNCPVLSQVKLIAEPWDIAPGGYQVGNFPPLFAEWNDHFRDAARRFWLHYDLPLGAFAGRFAASSDVFKRNGRLPSAAINLVTAHDGFTLRDCVCFNHKHNEANGEENRDGTNNNYSNNHGKEGVGGTLDLVERRRDSIHALLTTLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNQLTWLDWSQASSGLTAFTAALIHLRKRIPALVENRWWEEGDGNVRWLNRYAQPLSTDEWQNGPKQLQILLSDRFLIAINATLEVTEIVLPAGEWHAIPPFAGEDNPVITAVWQGPAHGLCVFQR", "text": "FUNCTION: Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
{"protein": "MATYQVEVIYQGQSQTFTADSDQSVLDSAQAAGVDLPASCLTGVCTTCAARILSGEVDQPDAMGVGPEPAKQGYTLLCVAYPRSDLKIETHKEDELYALQFGQPG", "text": "FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family."}
{"protein": "MNRLPSSASALACSAHALNLIEKRTLDHEEMKALNREVIEYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGFRHVPFGNIEAMRTALNECKKTGDDVAAVILEPIQGEGGVILPPPGYLTAVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDMLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIEQCELVIKAARKALAAMRVSVEEA", "text": "FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline (PubMed:12617754, PubMed:3510672). This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4- aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source (PubMed:3510672, PubMed:22636776). Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:12617754, PubMed:30498244). Is also able to transaminate spermidine, in lower extent, but not ornithine. Alpha-ketobutyrate and pyruvate can also act as amino acceptors, although much less efficiently (PubMed:12617754). FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4- aminobutanal. Also functions as a cadaverine transaminase in a a L- lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily."}
{"protein": "MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSGERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK", "text": "FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed- state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 28 (Jztx-11) subfamily."}
{"protein": "MQARIDATLNEHNRPEGSVRLLPVTKFHPVEDIKILQEFGVTAVGENREQEARAKALELPDMDFHMIGQIQSKKANSIARWAAAVHSVDSEKIAEALGRGVALALDRGDRTSDELPCFIQLSLDGDPSRGGTPLSQVTQLADCISDTTHLRFEGLMCVPPLGWGPEKAFSQARDVLSGLEEHFDRSLEFSAGMSGDLVAAIKHGSTIVRVGTEILGNRPLA", "text": "FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. SIMILARITY: Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family."}
{"protein": "MAAGVPCALVTSCSATFTGDRLVQHILGTEDAVVEATSSDAVRFYPWTIDNKYYSAEINLCVVPSKFLVTAEIAESVQAFVVYFDSTQKSGLDSVSSWLPLAEAWLAEVMILVCDRVCDDGINRQQAQEWCIKHGFELVELNPEELPEEDDDFPESTGVKRIVQALNANVWSNVVMKSDRSQGFSLLNSLAGANRRVASAESCHSEQQEPSPTAERTESLPGHHSGACGSAGAQVDSIVDPMLDLDIQELASLTTGGGDLENFERLFSKLKEMKDKAATLPHEQRKLHAEKVAKAFWMAIGGDRDEIEGLSSDDEH", "text": "FUNCTION: May be involved in endocytic recycling of growth factor receptors such as EGFR. SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
{"protein": "MGTWILFACLLGAAFAMPLPPHPGHPGYINFSYEVLTPLKWYQSIRPPYPSYGYEPMGGWLHHQIIPVLSQQHPPTHTLQPHHHIPVVPAQQPVIPQQPMMPVPGQHSMTPIQHHQPNLPPPAQQPYQPQPVQPQPHQPMQPQPPVHPMQPLPPQPPLPPMFPMQPLPPMLPDLTLEAWPSTDKTKREEVD", "text": "FUNCTION: Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the amelogenin family."}
{"protein": "MDLLGPMEMTEGSLCSFAAADDFYDDPCFNTSDMHFFEDLDPRLVHVGGLLKPEEHPHHHGHHHGHPHEEEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSTNPNQRLPKVEILRNAIRYIESLQALLREQEDAYYPVLEHYSGESDASSPRSNCSDGMMEYSGPPCSSRRRNSYDSSYYTESPNDPKHGKSSVVSSLDCLSSIVERISTDNSTCPILPPAEAVAEGSPCSPQEGASLNDSGAQIPSPTNCTPLPQDSSSSSNPIYQVL", "text": "FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNKSLVAVGVIVALGVVWTGGAWYTGKKIETHLEDMVAQANAQLKLTAPESNLEVSYQNYHRGVFSSQLQLLVKPIAGKENPWIKSGQSVIFNESVDHGPFPLAQLKKLNLIPSMASIQTTLVNNEVSKPLFDMAKGETPFEINSRIGYSGDSSSDISLKPLNYEQKDEKVAFSGGEFQLNADRDGKAISLSGEAQSGRIDAVNEYNQKVQLTFNNLKTDGSSTLASFGERVGNQKLSLEKMTISVEGKELALLEGMEISGKSDLVNDGKTINSQLDYSLNSLKVQNQDLGSGKLTLKVGQIDGEAWHQFSQQYNAQTQALLAQPEIANNPELYQEKVTEAFFSALPLMLKGDPVITIAPLSWKNSQGESALNLSLFLKDPATTKEAPQTLAQEVDRSVKSLDAKLTIPVDMATEFMTQVAKLEGYQEDQAKKLAKQQVEGASAMGQMFRLTTLQDNTITTSLQYANGQITLNGQKMSLEDFVGMFAMPALNVPAVPAIPQQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Periplasmic side Note=Has been isolated in association with the inner membrane, suggesting it may be tethered to the membrane. SIMILARITY: To E.coli YihF and H.influenzae HI_1236."}
{"protein": "MSIKIIIPSLGESVTEATIAKWYKKLGDAVKTDELLLEIETDKVTLEVNAPCNGTIGKISKTDGANVTVGEEVGEINEIADTDTAWINNKKQEVSQHTSEQLVDKPAMASNILAPSVQKLVTENKLDPNNIKGTGRGGRITKYDVLETINTTPITIETHAINKTNEERTQRVRMSRLRKTIAQRLKDSQNTAAILTTFNEIDMSKVIALRNQYKEEFEKKHTVKLGFMSFFVKATIEALKLIPSINAEIDGDDLLYKNYYDIGVAVGTEQGLVVPVIRDADKMSFADIEQAIGNLAKKAREGKLSISDLSGGTFSISNGGVYGSLLSTPIINPPQSGILGLHKTEERAVVIDGKIEIRPMMYIALSYDHRIIDGKEGVSFLVKIKNLIENPEKLLLNL", "text": "FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family."}
{"protein": "MTYKVLHIGAGGFGERWCDTFLPQNVADGTIEVVGLVDIDAKALDIGRKHLGLKAEQCFTAAAQAFQMVDADFCTIVIPPALHEGIVDLALARGMHILSEKPIADTMEASVRIAEKVRKSGLNMGVTMSHRFDQDKSTLRALVGADAIGRVNTVSCRFAGDFRLYDSWGRFRHEMMHPMLIEGAVHHLDIMADLAGAPCTSIYARTWKPEWADYKGDTDAIVLMDFANGAHGVYEGSSAQATGLNDWAFEYVRVEGESGTAILDHREIEVFHRYPMRLRQASRQGKGQQVSLLPGRKWQNALLIEQFCQWLDSGPPMATNVWENLQSVALVFSAIESVRLGQPVKVQEFLQSYRVGASIE", "text": "FUNCTION: Could be a NAD-dependent oxidoreductase."}
{"protein": "MGVIEFLLALAQDMILAAIPAVGFAMVFNVPVQALRWCALLGSIGHGSRMILMTSGLNIEWSTFMASMLVGTIGIQWSRWYLAHPKVFTVAAVIPMFPGISAYTAMISAVKISQLGYSEPLMITLLTNFLTASSIVGALSVDLSIPGLWLYRKRPRV", "text": "FUNCTION: Involved in succinate export with YjjP. Both proteins are required for export. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ThrE exporter (TC 2.A.79) family."}
{"protein": "MLRNGNKYLLMLVSIIMLTACISQSRTSFIPPQDRKSLLAEQPWPHNGFVAISWHNVEDEAADQRFMSVRTSALREQFAWLRENGYQPVSIAQIREAHRGGKPLPEKAVVLTFDDGYQSFYTRVFPILQAFQWPAVWAPVGSWVDTPADKQVKFGDELVDREYFATWQQVREVARSRLVELASHTWNSHYGIQANATGSLLPVYVNRAYFTDHARYETAAEYRERIRLDAVKMTEYLRTKVEVNPHVFIWPYGEANGIAIEELKKLGYDMFFTLESGLANASQLDSIPRVLIANNPSLKEFAQQIITVQEKSPQRIMHIDLDYVYDENLQQMDRNIDVLIQRVKDMQISTVYLQAFADPDGDGLVKEVWFPNRLLPMKADIFSRVAWQLRTRSGVNIYAWMPVLSWDLDPTLTRVKYLPTGEKKAQIHPEQYHRLSPFDDRVRAQVGMLYEDLAGHAAFDGILFHDDALLSDYEDASAPAITAYQQAGFSGSLSEIRQNPEQFKQWARFKSRALTDFTLELSARVKAIRGPHIKTARNIFALPVIQPESEAWFAQNYADFLKSYDWTAIMAMPYLEGVAEKSADQWLIQLTNQIKNIPQAKDKSILELQAQNWQKNGQHQAISSQQLAHWMSLLQLNGVKNYGYYPDNFLHNQPEIDLIRPEFSTAWYPKND", "text": "FUNCTION: Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D- glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation promotes PGA export through the PgaA porin (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the polysaccharide deacetylase family."}
{"protein": "MDGSSPLLAAAGSDGDRSSSEGEYTLAGGPSAGDTEKREGESPMEAAGAGTVGFSISRLDTLSALRLNRTRPAADTELRYLHLLWKPGELLQAGRSTPGKITSSRVRRLARARRNMGPIGKDLHAVKRLREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLARSKLNILQEGDSRSLETLRGEVTQIIQMLREYLNIMGQSEEREKLEHISTQLQNTRTREQVDEVTDLLASFTSLSIQMQNMGDR", "text": "FUNCTION: Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Midbody Note=Shuttles between nucleus and cytoplasm during the cell cycle."}
{"protein": "MEIPPGLETTKRKVAHSDEHGFSDQVRVPNVIVMVGLPARGKTYISKKLCRYLKWTGFTTKVFNVGEYRRSDANAADAIHGANASFFSPNNADALKVRAESARRAMEDMADYLNSGTGGVAIFDATNTTKDRRRIIIDFCKKQRLRCFFIESVCDDPAIIDCNVTDVKVNSPDYKGLMTAEQAKEDFMNRIENYKKQYEPLDESEDESLSFIKVINAGRSFKVHQVRGHVQSRVVYFLMNIHLLPRSIYLTRHGQSEYNAMGRLGGDSPLTEDGQKYASALADFFEEEEVPGLRVWCSQKVRAAQTAQHLKPDFHTEYWKALDELDAGICEGLTYEDILQRYPKQADDRATDKYHYRYPSGESYEDVVSRLEPVIMELERQANVLVVSHQAVLRCVLAYFYDRPLSELPYIDIPLHSLVKLTPRAYHCDSTIYALDLESGEWTETSDQLPLCDSPRD", "text": "FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate mutase family."}
{"protein": "MTSHFSSLPAHRSYIFSLYRDVLRNIHRCCYSVELQNILTSKLNLTMKQQKGTMSSWKAHSKIKELEELNDRLINRDLPYLKELINNLSGNKINSTQPNQYVQDLKEATNLINEYHSNNSQSIETIKKMDILNRYIKTKQSKHLLPKEISNVYKESLLLPFAIHEDSIYKLNKLHNQLIRGPPRVRLTNTKAGKITIWFLRSALNKKDRQSKKLKLRIAKEKQKHQQRIDNIKTCEKYAYWALLEASWESLLNTGKLPTININKTINNLSTLDNEDININRKNNHHIKDIHVKEWIEPITYSIKQLVDKEFERKCHYENYKKIILYGKNNGLIDFFENKTKVMYARRVSRYKTVVNGLPFIIPTIPRRDLRTALLDNKVLLP", "text": "FUNCTION: Essential for respiratory growth and required for mitochondrial protein synthesis. Required for vacuolar acidification (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRG1 family."}
{"protein": "MDYVNILLGLFFTWFLVNGLMSLRRRKISKKLPPGPFPLPIIGNLHLLGNHPHKSLAQLAKIHGPIMNLKLGQLITVVISSSVVAREVLQKQDLTFSNRFVPDVVHVRNHSDFSFVWLPVNSRWRTLRKIMNSSIFSGNKLDGNQHLRSKKVQELIDYCQKCAKNGEAVDIGRATFGTTLNLLSNTIFSKDLTNPFSDSAKEFKELVWNIMVEAWKTQFGGLLSFPLRKFDPQGIKRRMTNYFTKFLGLISGLIDERLKERNLRDNANIDVLDALLNISKRTQKRLTGIKSSSCLVSLFPTPFLPFIIICPFLYLLIFHRCKVSDLNGEGSYVGGRVQLNHTPLQIGCDRLTVSNKPRNYGDSYSSFRTCLQGLILHLNTLEWANGRTTSRIHTLLAKKHKKTISQHICTSKKIKIKKLLEHFLSFGAIVKKNLPIPPGGFSSSLFHVKWRKTLSCLGYIIPKDSQVLVSVWAIGRNSDLWENPLVFKPERFWESEIDIRGRDFELIPFGAGRRICPGLPLAIRMIPVALGSLLNSFNWKLYGGIAPKDLDMEEKFGITLAKAQPLLAIPTPL", "text": "FUNCTION: Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MKHLWFFLLLVAAPRWVLSQVQLQESGPGLVKPSETLSLTCTVSGGSISSYYWSWIRQPPGKGLEWIGYIYYSGSTNYNPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCAR", "text": "FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins- secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170). SUBCELLULAR LOCATION: Secreted Cell membrane."}
{"protein": "MSPWQPLLLVLLALGYSFAAPHQRQPTYVVFPRDLKTSNLTDTQLAEDYLYRYGYTRAAQMMGEKQSLRPALLMLQKQLSLPQTGELDSETLKAIRSPRCGVPDVGKFQTFDGDLKWHHHNITYWIQSYTEDLPRDVIDDSFARAFAVWSAVTPLTFTRVYGLEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGAVVPTYFGNANGAPCHFPFTFEGRSYLSCTTDGRNDGKPWCGTTADYDTDRKYGFCPSENLYTEHGNGDGKPCVFPFIFEGHSYSACTTKGRSDGYRWCATTANYDQDKADGFCPTRADVTVTGGNSAGEMCVFPFVFLGKQYSTCTSEGRSDGRLWCATTSNFDADKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYHYHEDSPLHEDDIKGIHHLYGRGSKPDPRPPATTAAEPQPTAPPTMCSTAPPMAYPTGGPTVAPTGAPSPGPTGPPTAGPSEAPTESSTPDDNPCNVDVFDAIADIQGALHFFKDGRYWKFSNHGGNQLQGPFLIARTWPAFPSKLNSAFEDPQPKKIFFFLWAQMWVYTGQSVLGPRSLDKLGLGSEVTLVTGLLPRRGGKALLISRERIWKFDLKSQKVDPQSVTRLDNEFSGVPWNSHNVFQYQDKAYFCHDKYFWRVSFHNRVNQVDHVAYVTYDLLQCP", "text": "FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the peptidase M10A family."}
{"protein": "MNNDSFSSFKFRRPSSKLHKDPPGYGSRALNSQQSTTSLKRHPSAPVYPRSSAAGSREHLRTRSNAYGSSSSSLDQNSAGASPVLGSSDSGHFHSSHSSRSRPPYSGRFSLNDQSSDELIGAPFDSRGMLSALEEHTAEPDNRSYQPPDPAERYTEKPPNFRSQTTPNPRALRQSASFTTLPPRMEAFPNAAGNDRPTNTKRFSDEATPVRPPGPSRSKKSSFSSFVNSMLGSPRGIKISAPENPVHVTHVGYDNQTGQFTGLPKEWQRLLQESGITQKEQEEHPQTMVDIMRFYEKNARGDDEVWHKFDHAYPQQPTAASPISQPAGSTTYGTQRTSPPTSPRFPQNHEGSFENPRAPPPIPRAAPIAAHAMSPPLGGLVPNRAPPKPPTAAANLVPSRPAPQPPTSSPYSNISTRPSPETQSPQFSTPPIPETEPLPSESQRSRSNSRTNGAQGPWPSVSPSHYQQQQEQAMAVAQQALANKQLERSRSQRQQQQSPRPDQMPIAQPALPQHAPSPEDVALTQASQTARAAPAARPRQRPRQSNAMDVRARLVAICTPGDPTKLYYNLNKIGQGASGGVFTAYEQHTNNCVAIKQMNLDLQPKKDLIINEILVMKDSKHKNIVNFLDSYLHGLDLWVVMEYMEGGSLTDVVTFNIMSEPQIAAVCRETLNGLQHLHSKGVIHRDIKSDNILLSLDGNIKLTDFGFCAQINDSQNKRNTMVGTPYWMAPEVVTRKEYGRKVDIWSLGIMAIEMIEGEPPYLTESPLRALYLIATNGTPKIKDEHNLSPVFKDFLHFALRVDPEKRASAHDLLKHPFMNLCAPLNHLSPLVKAARISRAQEKAQKGGV", "text": "FUNCTION: MAP4K component of the MAPK pathway required for the mating pheromone response and the regulation of cell polarity and cell cycle. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MFAVFWTNLRCLGYNTFTCGVETPTTWGKVGSLDASSSTFTTYRGYPLAMAISAGTPACDSPDDNIRRAINTLRADLSALLRGESVAYSAFLSACTKFDGFAQSCHGMLSDDTLDLLYSFSESLLALSENMALLETKKEAESNKFTAEVMAILSDKTSGLDLSDDKNEPTSPTPAYVEPCARWLKDNWYNPYPSGEVRTQIARQTRTSRKDIDAWFIDARRRIGWNEVRRKHFENKRVDIVRAASIFTGPQSIPAEVDALPDHIELEFAGILSRARSLYEEKFSPSKLAVKLDTAVKDMTPSLKEQLKNDEARRKREASTVGIINQRARHAYPTPERSPASAAELLASPPSFAIDSDKLPSVGRKRRRSLESDETVSSPLCKRPRSQSVFCELSPVKGLPSPSPSTQDELLETSAAPSPQPSLLPKLTPTDSARSTGKRKRRLSDGFQYPAAKRPEIRPQVVSDPFPATSSEHWEQWFREHVLSSPELTLTGDIPPAVTTDAPDSNTPLDIQLFNFPLIPDLPPSVPVVPAPTAELNIIEPLEVPAVTQVNVDPEATALDHTFSWMASDFPPPLQSTNTFPSSSPFSALDGMSLPFPDTRSSAFLPDPSLWSNISDPDLDFSTVFSQPSTNSAMTSSIQVPLQPTWLTSRSLSEQEREAKRKELEELEARAQAIRAEISAP", "text": "FUNCTION: Has a major regulatory role in sexual and asexual development. It may bind DNA itself or it may have a role in preventing DNA-binding of another protein. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/M-ATYP homeobox family."}
{"protein": "MDEPPSDVLAFLRQHPSLRLLPNTRKVRCSLTGHELPCRLPELQEYTRGKKYQRLSSSFSNFDYAAFEPHIVPSTKNRHQLFCKLTLRHINKSPEHVLRHTQGRRYQRALHQYEECQKQGVEYVPACLLHKRKKREDQTNSDELPGQRTGFWEPASSDEEDALSDDSMTDLYPPELFTKRELGKPKNDDTPEDFLTDQQDEKPEHSEEKSFREREEARVGHKRGRKLRKKQLTSLTKKFKSYHHKPKNFSSFKQLGR", "text": "SIMILARITY: Belongs to the SURF2 family."}
{"protein": "MGEEYKKTHTIVFHTSEEHLNSSIALAKFITKHHSSISITIISTAPAESSEVAKIINNPSITYRGLTAVALPENLTSNINKNPVELFFEIPRLQNANLREALLDISRKSDIKALIIDFFCNAAFEVSTSMNIPTYFDVSGGAFLLCTFLHHPTLHQTVRGDIADLNDSVEMPGFPLIHSSDLPMSLFYRKTNVYKHFLDTSLNMRKSSGILVNTFVALEFRAKEALSNGLYGPTPPLYLLSHTIAEPHDTKVLVNQHECLSWLDLQPSKSVIFLCFGRRGAFSAQQLKEIAIGLEKSGCRFLWLARISPEMDLNALLPEGFLSRTKGVGFVTNTWVPQKEVLSHDAVGGFVTHCGWSSVLEALSFGVPMIGWPLYAEQRINRVFMVEEIKVALPLDEEDGFVTAMELEKRVRELMESVKGKEVKRRVAELKISTKAAVSKGGSSLASLEKFINSVTR", "text": "FUNCTION: Glycosyltransferase involved in the biosynthesis of aurones, plant flavonoids that provide yellow coloration to flowers. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MTESERKQIIALIQREVIPAIGCTEPIAVALCVAKATETLGAKPEKIKVLLSANILKNAMGVGIPGTGMIGLPIAVALGALIGKSDYQLEVLKDSTPEAVEEGKKLIDEKRICISLKEDITEKLYIEVTCEAGGEQATAIISGGHTTFVYVAKGDEVLLNKQQTSGEEEKEETLELTLRKVYDFALTAPLDEIRFILETARLNKKAAEQSFQGDYGHALGKMLRGTYEHKIMGDSVFSHILSYTSAACDARMAGAMIPVMSNSGSGNQGISATLPVVVYAEENGKSEEELIRALMMSHLTVIYIKQSLGRLSALCGCVVAATGSSCGITWLMGGSYKQVAFAVQNMIANLTGMICDGAKPSCALKVTTGVSTAVLSAVMAMENRCVTSVEGIIDEDVDQSIRNLTRIGSQGMNETDRVVLDIMTHKGC", "text": "SIMILARITY: Belongs to the UPF0597 family."}
{"protein": "MRLLVLAALLTVGAGQAGLNSRALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDDLDRCCQTHDNCYKQAKKLDSCKVLVDNPYTNNYSYSCSNNEITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDKKNC", "text": "FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (By similarity). Has anti- helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted from pancreatic acinar cells in its inactive form. SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MTTKLKQRFVPQLAAVNHEFEDDFSKMLETVDTSHIKPGTVVKGQVVDINEVVVVDVGLKNEGRIPKSEFLLSPAHKLPEIGDLVDVYIEKTEGHSGKTLSREKAIKEELWGQLELICSKGEFVDGTIFGRVKGGFTVDLSGVVAFLPGSQVDVRPIKDPSSIMNIRQPFKILSMDKKLGNIVVSRRAILEESRSEARDEMLSKIKEGMILEGTVKNITDYGAFIDLGSVDGLLHLTDISWARVNHPSEVLEFNQKVKVMVIKFNEETKRISLGMKQLDYNPWEKIKEEFPVGKKMTGKVTNFADYGVFIELKDGLEGLVHSSEISWLKSNQNPRKTLTIGQEVEFMVLEVDTEKHRVSLSIKQCQQNPLIKFAETNPVGTVIKAPIRNITDFGIFVALSDNLDGMIHEGDITWEDNGNELLKTYKKGDEVECKVLTINIEKEQISLGIKQLTPNPYQGIADEYKKGTVVKAVVTAIKDDGLEVLVNDKAAGFIKKSDLSDEKEEQKPEMFAVDQEIEAKVASIEKSTNKILLSIKAYKIAERQKALKEYGSSDNTTNMGDILANALEDSKK", "text": "FUNCTION: Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (By similarity). SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family."}
{"protein": "MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR", "text": "FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle. Golgi apparatus. Cell junction, focal adhesion. Note=Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activation of the kinase activity. Shuttles between focal adhesions and cell-cell contacts in epithelial cells. Recruited to the lateral cell membrane in polarized epithelial cells by interaction with phosphorylated EZR. Detected at tubular membrane structures in the cytoplasm and at the cell periphery. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily."}
{"protein": "MEKYTNWRDNGTGIAPFLPNTIRKPSKVMTACLLGILGVKTIIMLPLIMLYLLTGQNNLLGLILKFTFSWKEEITVQGIKKRDVRKSKHYPQKGKLYICNCTSPLDAFSVVLLAQGPVTLLVPSNDIVYKVSIREFINFILAGGLDIKLYGHEVAELSQLGNTVNFMFAEGTSCNGKSVLPFSITGKKLKEFIDPSITTMNPAMAKTKKFELQTIQIKTNKTAITTLPISNMEYLSRFLNKGINVKCKINEPQVLSDNLEELRVALNGGDKYKLVSRKLDVESKRNFVKEYISDQRKKRK", "text": "FUNCTION: Acyl-CoA-dependent lysophosphatidic acid acyltransferase with preference for oleoyl-CoA. Involved in triacylglyceride homeostasis and lipid droplet formation. Involved in vacuolar protein sorting. SUBCELLULAR LOCATION: Lipid droplet Endoplasmic reticulum membrane; Single-pass membrane protein Note=Lipid droplets consist of a surface phospholipid monolayer and a hydrophobic interior. The latter makes embedding of proteins containing transmembrane segments difficult, and these may instead adopt a hairpin or monotonic conformation when associated with lipid droplet membranes. Always localizes to lipid droplets, irrespective of whether cells are grown on glucose or oleate. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family."}
{"protein": "MSLVAESNSGTISEQELDKVQLYSDLCLYEEALTKLVDSVDNFKPQLEIGKQLIEADKKLYSTLDLLPQYDSVFTRLRTLDDEISKVDQQTKNILSILNECHDDLNALPLLEEVEFEKKMILKQREKIKSNVLLEYATKLAKFTKIPPTFDKGTIGPNNFIWPAEDALRKGMLAMASLHGKELTKLPGQEDGEEDGSTANEDKNIVKDAEGAEGEIRQDDKKEDDSFVFGANANDAEGDEDKNAGEDEDEAMDSDLDLFNPDEF", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 4 family."}
{"protein": "MPEILEVVDVDGGPYGVTVDETGTLWFTLAARGAVGRLVDGTVETVALEPADGSPTVIMAEGDGAWFTEFRGNRIGRVEANGALSFLTAESPYGLCRAGDGGLWYTELSAGGVVHRAPDGTTTRHAVEGMPSMIAEAADGTVFVTLNQGNAVARITPDGQVRTTALPTAGAGPVGLATAADGAWFVELLAGQLGHVDRDGTVTEHPLPDRDARPHAVVVAPDGTVWFTEWAAARLGRRTADGEITELALPGAEPHGLAVAPDGTLWVAMESGALVHVRP", "text": "FUNCTION: Inactivates the type B streptogramin antibiotics by linearizing the lactone ring at the ester linkage, generating a free phenylglycine carboxylate and converting the threonyl moiety into 2- amino-butenoic acid. SIMILARITY: Belongs to the Vgb family."}
{"protein": "MAFNPNPEKTTSCCSTSKAQDKCTCPKGKCECETCPKSTKTPGSGPCNCGVKEKVSTCGCNGSGAACTCPPGQCACDSCPRKAKSVSTCGCGGSAAACSCPPGKCACDSCPKQAQEKVSSCACNGSGGACTCPPGKCSCSGCPAQAKENPADQPTTCGCQGVGVACTCPPGQCACDGCPAKAK", "text": "FUNCTION: Copper metallothionein that protects the cell against copper toxicity by tightly chelating copper ions (PubMed:21819456, PubMed:23498952). Required for antioxidant-mediated growth rescue in the presence of fluconazole (PubMed:31694529). Acts as a critical factors for lung colonization and virulence (PubMed:23498952). SUBCELLULAR LOCATION: Cytoplasm, cell cortex. SIMILARITY: Belongs to the metallothionein superfamily."}
{"protein": "MSVEEQFKTSAEQVKKLKSSPSDTELLELYSLYKQATIGDVNTDRPGMLYLKEKAKWDAWNGRKGLGKEQAQELYVKKVKELVEKNGLA", "text": "FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. SIMILARITY: Belongs to the ACBP family."}
{"protein": "MEAEELIGSSVTIDSIMSKMRDIKNKINEDCTDELSLSKICADHTETVNQIMRVGNTPENWLNFLLKLEKNSSPLNDDLLNKLIGRYSQAIEVLPPDKYGQNESFARIQVRLAELKAIQEPDDARDYFQMARENCKKFAFVHVSFAQFELSQGNLKKSEQLLHKAVETGAVPLQMLETAMRNLHLQKKQLLPEEDKKSVSASTVLSAQEPFSSSLGNVQNRSISCESRGQAGAARVLYGENLPPQDAEVRHQNPFKQTHAAKRSCPFGRVPVNLLNSPDFYVKTDSSAVTQLTTRLALSSVPLPYVTCLLHLQLLALAGLAKGSGPDRDAILPGSRPRGSDSYELRGLKPIQTIYLKDSLVSNEKSSELMSDLIALKSKTDSSLTKLEETKPEIAERRPMQWQSTRKPECVFQNPAAFAPLRHVPDVTPKADKESPPISVPKWLDPKSACETPSSSSLDDYMKCFKTPVVKNDFPPACPSSTPYSQLARLQQQQQQGLSTPLQSLQISGSSSINECISVNGRIYSILKQIGSGGSSKVFQVLNEKKQINAIKYVNLEDADSQTIESYRNEIAFLNKLQQHSDKIIRLYDYEITEQYIYMVMECGNIDLNSWLKKKKSINPWERKSYWKNMLEAVHIIHQHGIVHSDLKPANFVIVDGMLKLIDFGIANQMQPDTTSIVKDSQVGTVNYMAPEAIRDMSSSRENSKIRTKVSPRSDVWSLGCILYYMTYGRTPFQHIINQVSKLHAIINPAHEIEFPEISEKDLRDVLKCCLVRNPKERISIPELLTHPYVQIQPHPGSQMARGATDEMKYVLGQLVGLNSPNSILKTAKTLYERYNCGEGQDSSSSKTFDKKRERK", "text": "FUNCTION: Phosphorylates proteins on serine, threonine, and tyrosine (By similarity). Probably associated with cell proliferation (By similarity). Phosphorylates MAD1L1 to promote mitotic checkpoint signaling (By similarity). Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MNSASVSGESSLSDMIQTVHFSSGNPRIGETRGVMHLISDNAVSSSSSSSSSNLPIGRNPLVCVLGVPNHMTYADFCQFCGSFIQHILDMRTVRNDDIENRYSILIRFDSQESTDTFFQHFRGKQFNSLDEDVCRLLFALDVQFTGYSGSIDHTQPSAAGPIEQPTCPVCLERLDQDTGGILTTMCNHSFHCSCISNWPDSSCPVCRYCQQQPENSVCCVCQTTENLWMCVICGVVGCGRYKEGHARRHWEETEHCYSLELETQRVWDYAGDNYVHRLIQSKTDGKLVELNSHGSLSKDGCGSCEYSDSGMTDALLNSKVDMIISEYNELLQAQLENQKQYFEKLLQNVKEETEQKISEAASKAISQRLQKLQTRFDRCVKEKQFLEDLNENLVKNKDVWSTKITEMKEREKKAVRAKDEKIQGLEEQLGNLMAQMDGESEVSETKEVQDATVSTTNTSSSGAGNVIHANKKKSNRRKG", "text": "FUNCTION: RING-type ubiquitin E3 ligase that binds ubiquitin and is required for seed germination and post-germination growth."}
{"protein": "MANQVITGIKETAQSITGAARPWGDFLDLSAFSFPSSIADATTRVTQNLTHFRINYSIILSILLGLTLITRPIAILAFIAVGLAWFFLYFAREEPLTIFGFTIDDGIVAVLLIGLSIGSLVTTGVWLRALTTVGFGVLVLILHAALRGTDDLVSDDLESPYGPMLSTSGGGNDGARGDYSGI", "text": "FUNCTION: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRA1 family."}
{"protein": "MLFLNAKFIDLDLGENAVIVNEDDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVQKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEIGEMTKRIAETGDMISWEKNLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELKEDEIKRIVKTTNGCLVWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYSVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIKVECVLTYGGQPLGRAIGPALEAKEAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQNLAWEILESGRALEKFNQIIIEQGGTPKKPEEIELGDYIEEIIAPIDGYVTDINNTGITNVVKEAGAPRDKKAGLLLNSKIGNKVKKGDVLYTIYSGSEERLVSAVNLARRVYPVKVEGMLIERISKF", "text": "FUNCTION: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily."}
{"protein": "MSAAASPASERGWKSEKLDEAQALARSCAARRPDFQPCDGLSICATHSHGKCFKLHWCCHLGWCHCKYMYQPMTPVEQLPSTEIPARPREPTNTIQISVSLTEHFLKFASVFQPPLPPDSPRYCMISDLFIDNYQVKCINGKMCYVQKQPAPHSHRMSPEEVSAHDALISKESNTPKIDHCSSPSSSEDSGINAIGAHYVESCDEDTEEGAELSSEEDYSPESSWEPDECTLLSPSQSDLEVIETIETTV", "text": "FUNCTION: May play a role in neuronal and neurobehavioral development. SIMILARITY: Belongs to the UPF0524 family."}
{"protein": "MHKRNGPQAPPGRGAVTARQLGLLVDFSPDGLMIPEDGINEEELEAEFLALVGGQPQALEKLKGQGPLPMEAIEKMARLCMRDLDEDEEGTDEDDVEADEDLLAELNEVLGEEQKAVEPLMPVAQPKPSGPNPGVEATLQERLTLYQSALESARQAGDSAKMRRYDRGLKTLENLLVSAKKGNIINEADIPPPVASGKGAAAGHSHTQATSQLASVSPPAPESSGTLEAPSTTTPTSAKPQLPPDPCSPLARLQSLQHEYKLAALRAKHQDDTATATRHLRIAKSFDPVLEALSRGELVDLSRLPPPPDQLSPEPPLPAAQPLTSASTLTRPEVPQPPRNLLEALEQRMERYHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPPGFPPMQGLESAEPSQQSLVGVLETAMRLANHDEGSDDEEEETPKKQNTPAASTTQLKSSPSKAPPSGPAPAGKAAPKGTSNRAQQQLAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDIAKVPPAPVNKDDFVLVQRPGPGLSQEAVRRYGELTKLLRQQHEMCLNHSTQFTHLGNIAETIKFEKLAEDCKRSMDTLKQAFARSLPTPAARFEQRTFSVIKVFPDLSNSDMLLFIVKGINLPTPTGLSPSDLDAFVRFDFPYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRGHRGFRRAIQTKGIKFEVVHKGGLFKTDRVLGTAQLKLGTLETACEVHEILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVIDHIPAAMPTVTGPKAKAPLIPASSREAGNRSARPLHSLSVLAFDQERLERKILALRQARRPVPPEVAQQYQDVVQRSQWQRAQLEQGGAALRREYASHLERQLHFYTEAARRLGYDGSREAAKEALYRRNLVESELQRLRR", "text": "FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the CC2D1 family."}
{"protein": "MSGKIQHKAVVPAPSRIPLTLSEIEDLRRKGFNQTEIAELYGVTRQAVSWHKKTYGGRLTTRQIVQQNWPWDTRKPHDKSKAFQRLRDHGEYMRVGSFRTMSEDKKKRLLSWWKMLRDDDLVLEFDPSIEPYEGMAGGGFRYVPRGIEDDDLLIRVNEHTNLTAEGELLWSWPDDIEELLSEP", "text": "FUNCTION: Confers immunity to L5 superinfection, required for maintenance of the lysogenic state. Binds to multiple asymmetric DNA sites. Regulates transcription initiation at an early lytic promoter, Pleft, but also affects downstream gene expression at 'stoperator' sites in the phage genome."}
{"protein": "MATTHLDVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVHALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGGDERADSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSRTGGILAAPVRDTMKRAEPGKNAIAHTVDRNGLWHALTPQFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIHQENT", "text": "FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily. SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily."}
{"protein": "MDEKEFKRLLRVRARLKRKKPRFLRQEWWRYPKFKNDPKWRRPKGIDSKMRLKLKGKPRSPSIGWSSPRLVRGLHPSGYEEVLIHNVKELEKLDPKRQAARIAHTVGKKKRIEILKRAQELGIKVLNPQL", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family."}
{"protein": "MLAVHTSPLAQPGIGDAGGMNVYVLQSALHLARRGIEVEIFTRATASADPPIVWVAPGVLVRNVVAGPFEGLDKYDLPTQLCAFAAGVLRAEAAHEPGYYDIVHSHYWLSGQVGWLARDRWAVPLVHTAHTLAAVKNAALADGDAAEPPLRSVGEQQVVDEADRMIVNTDDEARQLISIHRADPAKIDVAHPGVDLDMFRPGDRRAARAALGLPLDGNVVAFVGRIQPLKAPDIVLRAAAKLPQVRIVVAGGPSGSGLASPDGLVRLADELGITARVTFLPPQSRTNLATVFQAADLVAVPSYSESFGLVAVEAQACGTPVVAAAVGGLPVAVRDGVTGTLVFGHNVGHWADAVDQLLRLSAGPQARAISRAAVVHAAQFSWDNTTDALLASYRRAIGDFTATRQHRVRDLVATRKPRRWISRRGMGA", "text": "FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2- deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway. FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2- deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway. SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA subfamily. SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA subfamily."}
{"protein": "MSKTHLTEQKFSDFSLHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSMFHYLLSHPAIADRKVNKPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYNPDALMTDLPKPLRLTRPRTGNGPRRTGAPRNRRRSG", "text": "FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. RhlB subfamily."}
{"protein": "MALGGWRWARKALAAGRPLFQGRALLLTNTLGCGVLMAAGDGARQVWEVRARPGQRFSARRSASMFAVGCSMGPFLHFWYLWLDRLLPASGLRSLPSVMKKVLVDQTVASPILGVWYFLGLGSLEGQTLEESCQELRAKFWDFYKADWCVWPAAQLVNFLFIPSHFRVTYINGLTLGWDTYLSYLKYWVPEPLQTPGCAD", "text": "FUNCTION: Required for the assembly and stability of the mitochondrial ribosome (By similarity). Is a positive regulator of mitochondrial protein synthesis (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Mitochondrion inner membrane. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family."}
{"protein": "MALDYKLLEIVACPICKGKLNYDKERSELVCRADKLAYPVEDDIPVLLENRARPLKEEELPL", "text": "SIMILARITY: Belongs to the UPF0434 family."}
{"protein": "MAAACPLPRTPDLPTLHDKLQGLLSFLRGALAISSAHTVDFYTKSVWQELVDLPPESVLAALRESAVEAEPREAETGSGFTELPKIFCETSQKLLSVEAFARTAKHYSVQNLGLCTPSEQLLTALQGNKRQRVDENVKAIEFMNTKKSHEVQAMSELICSIADYCGLKQIIDVGSGKGYLSSFLSLKYGLNVYGIDSSNTNTHGAKERNRKLKKHWSLYHPHSRADANGWASERPRELKVPKGVECKGDAESVQRSRLGNPDLSATDGLPDFSGSAISVIRKQQKNVLAQPAEEENLYFEDAFSLIDFLPVDAIEPTSSQVQNTEKSGLRKERRNTASKARDSSIYSPLTSFITADSQLHDIIEDLEDCLMVGLHTCGDLAPSTLRIFTSKAEVKAVCSVGCCYHLLSEEFENQHKDRCANENWGFPMCHYLKEERWCCGRNARMSACLALQRVAVGQGLPTESLFYRAVLQNIIKDYYGISKCEQHVGKIYSKCSSFLEYVRMSLKKLGLDESKVSEEIIMDYYENYKPRMNELEAFNMLKVVLAPCIETLILLDRLCYLKEQDGVAWSALVKLFDPVQSPRCYAVIALKKQCDLG", "text": "FUNCTION: Probable methyltransferase."}
{"protein": "MGRGLMNSLKPYLAMISMQFGYAGMYIITMVSLKHGMNHYVLAVYRHAIATAVIAPFALFHERKIRPKMTFRIFLQIALLGFIEPVLDQNLYYVGMTYTSATFASATANVLPAITFVLAIIFRLESVNFKKVRSIAKVVGTVITVSGALLMTLYKGPIVDFIRFGGGGGGGSDGAGGSHGGAGAAAMDKHWIPGTLMLLGRTFGWAGFFILQSFTLKQYPAELSLTTLICLMGTLEGTAVSLVTVRDLSAWKIGFDSNLFAAAYSGVICSGVAYYVQGVVMRERGPVFVATFNPLCVVITAALGVVVLSESIHLGSVIGTLFIIVGLYTVVWGKGKDKRMTDDDEDCKGLPIKSPVKPVDTGKGLAAELEMKSKEGQEAKATTTTQVEI", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Plant drug/metabolite exporter (P-DME) (TC 2.A.7.4) family."}
{"protein": "MARLMMTVGCLIFIVVLLDMMVPVSNTCPGYFGECGDGPEEGECCGMYNYCCKGRCLMLASCQKRRDAGRLLRSLKKLKLTTH", "text": "FUNCTION: Acts as a neurotoxin by inhibiting voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conopeptide I2-like superfamily."}
{"protein": "FWGAAAKMLGKALPGLISMFQKN", "text": "FUNCTION: Membrane-perturbating peptide with multiple activities (PubMed:34302796). It is insecticidal, since it induces contractile paralysis in insects (L.cuprina) during several hours, and death after 24 hours (PubMed:34302796). It shows antibacterial activity with higher activity against Gram-positive than Gram-negative bacteria (PubMed:34302796). It is also antiparasitic, since it potently inhibits the larval development of the major pathogenic nematode of ruminants (H.contortus, IC(50)=5.1 uM), but fails to reduce the motility of adult males of the other nematode B.malayi (PubMed:34302796). It also shows cytotoxic activity against HEK293 cells (EC(50)=12-14 uM) and induces hemolysis in human erythrocytes (EC(50)=28.6-48.2 uM) (PubMed:34302796). In addition, it causes an important increase in intracellular calcium concentration on neuronal and epithelial cell lines, which supports a non-specific membrane perturbation mechanism of action (PubMed:34302796). In vivo, it induces pain by intraplantar injection into mice, suggesting a defensive function against vertebrate predators (PubMed:34302796). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Adopts an alpha- helical conformation in membrane-mimetic environments. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Medium-length antimicrobial peptide (group 3) family. Ponericin-W subfamily."}
{"protein": "MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGEHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLNDLQKDGKITAEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIVEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFDEAIKLRGRSFMNNWEVYKLLAHVRPPVSKGGLHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKNLEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSIGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQVNVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHISRKRSGEAAV", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 3]: Cell projection, cilium, flagellum Note=Principal piece region of the sperm flagellum. SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum Note=Principal piece region of the sperm flagellum. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily."}
{"protein": "MAGRLLLLLLCAALPDELRAEGGVFIKKESADKFLERTKRANSFLEEMKQGNIERECNEERCSKEEAREAFEDNEKTEEFWNIYVDGDQCSSNPCHYGGQCKDGLGSYTCSCLDGYQGKNCEFVIPKYCKINNGDCEQFCSIKKSVQKDVVCSCTSGYELAEDGKQCVSKVKYPCGKVLMKRIKRSVILPTNSNTNATSDQDVPSTNGSILEEVFTTTTESPTPPPRNGSSITDPNVDTRIVGGDECRPGECPWQAVLINEKGEEFCGGTILNEDFILTAAHCINQSKEIKVVVGEVDREKEEHSETTHTAEKIFVHSKYIAETYDNDIALIKLKEPIQFSEYVVPACLPQADFANEVLMNQKSGMVSGFGREFEAGRLSKRLKVLEVPYVDRSTCKQSTNFAITENMFCAGYETEQKDACQGDSGGPHVTRYKDTYFVTGIVSWGEGCARKGKYGVYTKLSRFLRWVRTVMRQK", "text": "FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. VAP cleaves the fusion proteins of Sendai virus, NDV, and influenza virus a at a specific single arginine- containing site, and plays a key role in the viral spreading in the allantoic sac. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MSEKPKVYQGVRVKMTVKELLQQRRAHQATSGANLSGSSGLHLPDTTMPSSAGLYFEPEPTSSTPSYFQTREFSTCVSCEEIPSCLDQIFESYLQTDTLPEPLLNSAQIAPHYFPESCQVAPFCHNQSLIPGSPSDSSSLSGSFDCSYSPTQLPSYTPENYSSPPSLDSLHSSLPEEGYFCQHWPSHPQYNHSSPATPSSVCYYASCEAEHLDALRTTEFFSYSGMDCADFAPPVATTGDFYKRETSCDACYS", "text": "FUNCTION: Transcriptional coactivator that specifically associates with POU2F3. This complex drives the development of tuft cells, a rare a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the POU2AF family."}
{"protein": "MTQARCPALLIAAPASGQGKTTVTAALARLHARQGRRVRVFKCGPDFLDPMILARASGAPVYQLDLWMVGEAEARRLLARAAGEADLILIEGVMGLFDGNPSAADLARRFGVPVLGVINGAAMAQTFGALAYGLAHFQPDLPFSGVLGNRVGSQRHSDILRDCLPPGMRWFGGLPRSAEFELPSRHLGLVQAEELADLDARLDAAADALRASAETDLPEPVTFEVPAPAPLQRSLEGVRIGVARDASFAFLYQANLDLLRELGAELAFFSPLQDQALPAVDSLYLPGGYPELHLGRLQGNRAMAEAIRAHHAAGKPLLAECGGMLYLLDCLEDADGERGELLGLLPGRARLQKRLTALALQEVELPEGRLRGHTFHHSTLDCAVEPLARGVCPNGRNTAEAVFRLGRLTASYIHFYLPSNPQAAAALLAPARDAD", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L- glutamine or ammonia as the nitrogen source. SIMILARITY: Belongs to the CobB/CbiA family."}
{"protein": "MDHSAHMGMSTHMGMSDMNHSTTMPPSHHHPTSSGSHESMMMPMTFYFGFKKVEVLFAGLVINTAGEMAGAFVAVFLLAMFYEGLKIAREGLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH", "text": "FUNCTION: [Truncated CTR1 form]: Mobilizes copper(1+) out of the endosomal compartment, making copper(1+) available for export out of the cells. FUNCTION: [High affinity copper uptake protein 1]: Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane and delivers directly copper(1+) to specific chaperone such as ATOX1, via a copper(1+)- mediated transient interaction between the C-terminal domain and a copper(1+) chaperone, thus controlling intracellular copper(1+) levels (By similarity). May function in copper(1+) import from the apical membrane thus may drive intestinal copper absorption (By similarity). The copper(1+) transport mechanism is sodium- independent, saturable and of high-affinity. Also mediates the uptake of silver(1+). May function in the influx of the platinum-containing chemotherapeutic agents (By similarity). The platinum-containing chemotherapeutic agents uptake is saturable (By similarity). In vitro, mediates the transport of cadmium(2+) into cells. Also participates in the first step of copper(2+) acquisition by cells through a direct transfer of copper(2+) from copper(2+) carriers in blood, such as ALB to the N-terminal domain of SLC31A1, leading to copper(2+) reduction and probably followed by copper(1+) stabilization. In addition, functions as a redox sensor to promote angiogenesis in endothelial cells, in a copper(1+) transport independent manner, by transmitting the VEGF-induced ROS signal through a sulfenylation at Cys-189 leadin g to a subsequent disulfide bond formation between SLC31A1 and KDR. The SLC31A1-KDR complex is then co-internalized to early endosomes, driving a sustained VEGFR2 signaling (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Note=The localization is controlled by the intra and extra-cellular copper concentration. Under conditions of elevated extracellular copper concentrations, it is rapidly internalized by endocytosis from the plasma membrane by a clathrin- and dynamin- mediated process and degradated in order to prevent intracellular copper accumulation and to reduce the transport of the copper across the membrane. The internalized SLC31A1 is then localized in early endosomes, and, upon a low extracellular copper concentrations, it is transported back to the plasma membrane in a RAB11A-dependent recycling pathway (By similarity). Localizes to the apical membrane in intestinal epithelial cells (PubMed:20699218). Localizes to the neuronal cell body plasma membranes (By similarity). Mainly localized on the basolateral side of renal tubular cells (By similarity). SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily."}
{"protein": "MIIQIEEYFIGMIFKGNQLVRNTIPLRREEIFNFMDGEVVSNPEDEHLKVAEIILKLYFAEIDDKKVRELISYKLEVPEFTKKVLDIVKDIEFGKTLTYGDIAKKLNTSPRAVGMALKRNPLPLIIPCHRVVAKNSLGGYSYGLDKKKFILERERLNMVSFKFNKVY", "text": "FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MGMT family."}
{"protein": "MIEIEKVCVDFTAGRGTPTRAVDDVSLHIAAGEIFGIVGTSGAGKSTLLRTLNALTRPSQGRVNVNGVEISALDGKALRQARQRIGMIFQHFNLMHTRTVAKNVAFSLKAAGWERSKIAPRVAEILTLVGLADKANCFPVQLSGGQKQRVGIARAIANHPDVLLCDEPTSALDLETSATILALLRQINAQLGITIVLITHEMNVIKSICDRVAVMSGGKVVESGEVFDVFAHPQHAFTQQLVSHTLNLTLPERLREHLPGQLLKILFIGDSAEQPVLSEVAIKFGVAVNILHGKIEYIGERALGILVVQLTAPHNPTAVAAAVEHIRQRTAQVEVIRG", "text": "FUNCTION: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family."}
{"protein": "MSFLKKSLFLVLFLGLVSFSICEEEKRETEEEENEDEMNEESEEKRESPERPPGFTPFRVD", "text": "FUNCTION: Induces relaxation of rat smooth muscle from tail artery and contraction of that from ileum, urinary bladder and uterus. Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Bradykinin-related peptide subfamily."}
{"protein": "MEEKKALIIVDVQKAFDDKKWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSLFHPKNEGFAIKEIVKPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFGMRDQNDTYYDAATIHNISLATLHDEFATILTTDQLINDFIKTH", "text": "SIMILARITY: Belongs to the isochorismatase family."}
{"protein": "LMAGHPNYGDILMQSGGAAGTAHLHEYLSPVDVSRFSSPRVTPRLSRKRALSISPLSDASIDLQTMIRTSPNSLVAYINNSRSSSAASGSYGHLSAGTISPAFSFPHPINPVTYQQILTQQRGLSSAFGHTPPLIQPSPTFPPRQHMAVISVNPPPAQISSNSNCISDSSQSKQSSESAVSSTVNPVINKRTKVKTEVEGLPQYPQPRQEHLTDLKEDLDKDECKQEPEVIYETNCHWEGCTKEYDTQEQLVHHINNDHIHGEKKEFVCRWQDCTREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCSKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYVCKIPGCTKRYTDPSSLRKHVKTVHGPDAHVTKKQRNDVHPRPPPLKENGDNEASAKQSSKVSEESPEANSTTRSMEDCLQVKTIKTENSVMCQSSPGGQSSCSSEPSPLGSTNNNDSGVEMNMHGGGSLGDLTGWMTRLPVVDSTVSSGNLTVSLQLRKHMTTMQRLEQLKKEKLKTVKDSCSWVNPAPQGRNTKLPPISGNGSILENSGGSSRTLPNPRIMELSVNEVTMLNQINERRDSTTSTISSAYTVSRRSSGISPYFSSRRSSEASQLGHRPNNTSSADSYDPISTGGREFDIKL", "text": "FUNCTION: Functions as transcription regulator in the hedgehog (Hh) pathway. Functions as transcriptional activator. May also function as transcriptional repressor. Binds to the DNA sequence 5'-GAACCACCCA-3' (By similarity). Is involved in the smoothened (SHH) signaling pathway. Required for normal skeleton development (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, cilium. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
{"protein": "AISGLTPCKESKQFAKREKQ", "text": "FUNCTION: Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the PsaF family."}
{"protein": "MPLATTLGTLVLLLLLPLPRGAEVTGDHSNVALDYGALEGEEGTEQQLHYHDPCKAAVFWGDIALDEDDLKLFHIDKAEDWTKPSIDKPGHDTGGLEETSARWPNDTASNASIQAPRKDGKDATTFLPNPGTSNTTAKTFSARVRRATTSRTERIWPGGVIPYVIGGNFTGTQRAIFKQAMRHWEKHTCVTFVERTDEESFIVFSYRTCGCCSYVGRRGGGPQAISIGKNCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRGVFLDTILPRRDDNGVRPTIGQRVRLSQGDIAQARKLYKCPACGETLQDTTGNFSAPGFPNGYPSYSHCVWRISVTPGEKIILNFTSMDLFKSRLCWYDYVEIRDGYWRKAPLLGRFCGDKIPESLVSSDSRLWVEFRSSSSSLGKGFFAVYEAMCGGDITKDAGQIQSPNYPDDYRPSKECVWRITVPDGFHVGLTFQSFEIERHDSCAYDYLEIRDGPTEDSTLIGHFCGYEKPEAVKSSANRLWVKFVSDGSINKAGFAANFFKEVDECSWPDHGGCEQRCVNTLGSYTCACDPGYELAADKKTCEVACGGFITKLNGTITSPGWPKEYPTNKNCVWQVVAPVQYRISLQFEAFELEGNDVCKYDFVEVRSGLSPDAKLHGKFCGSETPEVITSQSNNMRVEFKSDNTVSKRGFRAHFFSDKDECAKDNGGCQQECVNTFGSYLCRCRNGYRLHENGHDCKEAGCAYKISSAEGTLMSPNWPDKYPSRKECTWNISSTAGHRVKITFSEFEIEQHQECAYDHLELYDGTDSLAPILGRFCGSKKPDPVVATGSSLFLRFYSDASVQRKGFQAVHSTECGGRLKAEVQTKELYSHAQFGDNNYPSQARCDWVIVAEDGYGVELIFRTFEVEEEADCGYDFMEAYDGYDSSAPRLGRFCGSGPLEEIYSAGDSLMIRFHTDDTINKKGFHARYTSTKFQDALHMRK", "text": "FUNCTION: Protease which specifically processes pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MSNLQTRIITAIVLGTITLWLTWVGGVGFTLFSIAIGLAMFYEWTELSATRQTAFSRLFGWAWLIVTGILLILDRGALLTIGFLVAGCAILLVTQWKSGRGWPAAGLFYAGFSALSLSLLRGDEPFGFTTIVFLFAVVWSTDIAAYFNGRALGGPKLAPRFSPNKTWSGAIGGAAAAVTGGLLVASLVAAPGGWGVPVLALLLSIVSQIGDLAESWVKRQFGAKDSGRLLPGHGGVLDRVDGLVAAAALLYLFGAIFAEPDVPSAIFFSF", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDS family."}
{"protein": "MYRSRNRPKRGGENEVKGPNSALTQFLREEGISAENIKQKWYQRQSKKQEDATDEKKGKAEDDSFTAEISRVVEDEEIDEIGTGSGTETERAQVSYDARMKLVPADSDEEEYETSHISDTPVSLSSANDRESLTKKRQNTAKIIQNRRRKRKRAADLLDRRVNKVSSLQSLCITKISENISKWQKEADESSKLVFNKLRDVLGGVSTANLNNLAKALSKNRALNDHTLQLFLKTDLKRLTFSDCSKISFDGYKTLAIFSPHLTELSLQMCGQLNHESLLYIAEKLPNLKSLNLDGPFLINEDTWEKFFVIMKGRLEEFHISNTHRFTDKSLSNLLINCGSTLVSLGLSRLDSISNYALLPQYLVNDEFHSLCIEYPFNEEDVNDEIIINLLGQIGRTLRKLVLNGCIDLTDSMIINGLTAFIPEKCPLEVLSLEESDQITTDSLSYFFSKVELNNLIECSFRRCLQLGDMAIIELLLNGARDSLRSLNLNSLKELTKEAFVALACPNLTYLDLGFVRCVDDSVIQMLGEQNPNLTVIDVFGDNLVTEKATMRPGLTLIGRQSDSI", "text": "FUNCTION: Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. This protein is one of 10 proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. SIMILARITY: To S.pombe SpCC613.14."}
{"protein": "MASFRIRQFQERDYKQVVDVFSRGMEEHIPTAFRHLLTLPRTLLLLAVVPLAIVLVSGSWFLAVVCIFFLFLFLWFLASKPWKNYVSKCLHTDMADITKSYLSVRGSGFWVAESGGQVVGTVAARPVKDPPLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGLLQQGAVTLYYSMGFQKTGESFVDILTWLVDVSLIHFIYPLPSAQKYEL", "text": "FUNCTION: Acetylates the free alpha-amino group of cysteine S- conjugates to form mercapturic acids. This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S-conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6- acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1. May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type II membrane protein Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the camello family."}
{"protein": "MGRSRRTGAHRAHSLARQMKAKRRRPDLDEIHRELRPQGSARPQPDPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERAAGMGSYVPPRRLAVPTEVSTEVPEMDTST", "text": "FUNCTION: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome (PubMed:32669547). Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity (PubMed:9115366). SUBCELLULAR LOCATION: Nucleus, nucleolus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein family."}
{"protein": "MSSGGLLLLLGLLTLWEVLTPVSSTDRPEFCELPEDSGPCKGLFHVFYYNSDQNQCLEFIYGGCYGNANNFKAIEECKRTCAA", "text": "FUNCTION: Serine protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family."}
{"protein": "MIRVAINGYGRIGRSILRALYESGKRQQIQIVAINELAKPEAIIHLTQYDTTHGRFQHKVKLVDNHMLIGDDAIKILHEPDAAKLPWREMDIDIVYEATGVILDRQSCEAHIHAGAKQVLISHPSSADVDGTIVYGVNHDLLRAEHTVVSNASCTTNCIVPVIDVLDKHFGVKSGAITTIHSAMNDQQVIDAYHDDLRRTRAAGQSIIPVDTKLARGIERILPHMKDKFEAISVRVPTINVTAIDLSVTLAKTVDIASVNQVLELAANGRFNGILGYTDEPLVSCDFNHDPRSSIVDGTQTRVSAGQLVKLLLWCDNEWGFANRMLDTSLAMIAAKQS", "text": "FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily."}
{"protein": "MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVVPEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIGLYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEHTFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRDVDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH", "text": "FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols. Isoform 3 lacks transferase activity but acts as a negative regulator of isoform 1 (By similarity). SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MKYIPVYQPSLTGKEKEYVNECLDSTWISSKGNYIQKFENKFAEQNHVQYATTVSNGTVALHLALLALGISEGDEVIVPTLTYIASVNAIKYTGATPIFVDSDNETWQMSVSDIEQKITNKTKAIMCVHLYGHPCDMEQIVELAKSRNLFVIEDCAEAFGSKYKGKYVGTFGDISTFSFFGNKTITTGEGGMVVTNDKTLYDRCLHFKGQGLAVHRQYWHDVIGYNYRMTNICAAIGLAQLEQADDFISRKREIADIYKKNINSLVQVHKESKDVFHTYWMVSILTRTAEEREELRNHLADKLIETRPVFYPVHTMPMYSEKYQKHPIAEDLGWRGINLPSFPSLSNEQVIYICESINEFYSDK", "text": "FUNCTION: Catalyzes the synthesis of GDP-perosamine from GDP-4-keto-6- deoxy-D-mannose and L-glutamate. Can use only L-glutamate as amino donor. SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family."}
{"protein": "MKINKKQIVFFILFSIFLNHVNGIFYLPGMIPHDFAQGEEGAIKVNKITSVHTQIPYKYYQLPGVCQPKEGIIDDTENLGEILLGDRIENSDYTFNFLTDGGKCKVINSESCSPIIKKEDLKVLEDRIQNQYRVHWLLDGLPVRQTGRLASDPGFDLGFMTLAEGQTVATAEKYLNNHLEITIFYHSNPTDNTSRIVGFEIFPTSRQYKKVENWKGDTGDDCPQYGENFEQLSVSVKEGEDQERFVLWTYEVKYTPSPVLWNKRWDIYFESNDNSVHWFSILNSLMIVFILTVMVAMIIIRTLKKDIRRYTSIDTSEDRDSQEETGWKMIHGDVFRPPSHPMLLSVCIGSGVQIFSMTLITMIFAVLGFLSPANIGGLATALIVLFVLSAMFAGYFSTRVFTIFKGRNWKKNTIYTALSMPGIIFGIFFFVNMFLRGAKSSAAVPFGTFASIIAMWFGISVPLVFLGSYFASKKPVPEDPVRTNQIPRQVPDQIWYMNPYLSILMGGILPFGAVFIELHFILTSLWDNQFYYIFGFLFIVLMILIVTSAEISIVMCYFQLCAEDHHWWWRSFLTAGSSSLYMFIYSVSFFRYLGITKFISSLLDFSYSFIMSLAFAALTGTIGFYSCYFLVRKIYSSIHIN", "text": "FUNCTION: Involved in adhesion, phagocytosis of hydrophilic particles and intracellular killing of bacteria (PubMed:10944536, PubMed:12857872, PubMed:16367873). Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface (PubMed:25999474). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family."}
{"protein": "MSQLLTARQAEELHKAMIAYLLSANLPKSAAALREELADSVQLDDSTAKKYEGLLEKKWTSVVRLQKKIMDLESRNNALQSELDSATPTSLARRNQDPVSWLPHAPARHILQSHREPVTCVGFHPVFSSLASGSDDTTIKIWDWELGELERTIKGHTKAVLDVDYGGPRGGTLLASCSSDLTIKLWDPSDGYKNIRTLPGHDHSVSAVRFIPSGAAGSPLSGNLLVSASRDKTLRIWDVTTGYCVKTLRGHVDWVRDVAASPDGRFLFSAGNDQVARLWDVSSGETKSTFLGHEHAVECVAFAPPTSYPHLSALAGLKKAPPSSSSAEYVATGSRDKSIRIWDARGTLIKTLIGHDNWVRALAFHPGGKYLLSVSDDKTLRCWDLTQECKCVRTVKDAHGHFISCIRWAPNIIKDAGVVNGDDTSTAASANGGALAASAINGVVPTGKKEDPGGGPMMGIRCVIATGSVDLKVRVFAS", "text": "FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules at the hyphal tip and the mitotic spindle poles. SIMILARITY: Belongs to the WD repeat LIS1/nudF family."}
{"protein": "MRQTLCDGYLVIFALAQAVILLMLTPLFTGISRQIRARMHSRRGPGIWQDYRDIHKLFKRQEVAPTSSGLMFRLMPWVLISSMLVLAMALPLFITVSPFAGGGDLITLIYLLALFRFFFALSGLDTGSPFAGVGASRELTLGILVEPMLILSLLVLALIAGSTHIEMISNTLAMGWNSPLTTVLALLACGFACFIEMGKIPFDVAEAEQELQEGPLTEYSGAGLALAKWGLGLKQVVMASLFVALFLPFGRAQELSLACLLTSLVVTLLKVLLIFVLASIAENTLARGRFLLIHHVTWLGFSLAALAWVFWLTGL", "text": "FUNCTION: Possible component of hydrogenase 4. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MSKSERLDGGLEALGIQAGTVNLNWNEPRLYQEAVQRGEAEVAEGGALVVKTGAHTGRSAKDKFTVRDSETEDQVWWDNNAAISPEHFDALWTDFQAHMAGKELFVQQLFGGADLDHRLPVRVVNELAWHSLFIRHLLRVPAAEEYAGFAAEFTIINLPSFKADPARHGCRSETVIGVDFARRIVLIGGTSYAGETKKSVFTILNYLLPAKGVMPMHCSVNSNPNGEDATIFFGLSGTGKTTLSADASRTLVGDDEHGWSPNGLFNFEGGCYAKMIRLSAEAEPEIHATTKMWGTVLENVVMDPQTRVLDLDDDSLAENSRGAYPLSAIPNASETGRCGHPKNVIMLTCDAFGIMPPIAKLTPAQAMYHFLSGYTAKVAGTEKGVTEPSATFSTCFGAPFMPRHPAEYGALLRELIAEHQVDCWLVNTGWTGGAYGTGNRMPIKATRALLNAAMDGSLNSAAFREDPNFGFMVPIAVDGVDASILDPRSTWSDKAAYDDRAAKLATMFIENFKTFEAHVAPYVRAAAPKVRELTAAE", "text": "FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP) family."}
{"protein": "MKGWGWLALLLGVLLGTAWARRSQDLHCGACRALVDELEWEIARVDPKKTIQMGSFRINPDGSQSVVEVPYARSEAHLTELLEEVCDRMKEYGEQIDPSTHRKNYVRVVSRNGESSELDLQGIRIDSDISGTLKFACESIVEEYEDELIEFFSREADNVKDKLCSKRTDLCDHALHRSHDEL", "text": "FUNCTION: Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the canopy family."}
{"protein": "MALPLRPLTRGLASAAKGGHGGAGARTWRLLTFVLALPSVALCTFNSYLHSGHRPRPEFRPYQHLRIRTKPYPWGDGNHTLFHNSHVNPLPTGYEHP", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Plays a role in the assembly and stabilization of complex IV (PubMed:31155743). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family."}
{"protein": "MSSDPKISITSFLECLSEIEEEFLRDKEKNPPVLVSKLQELQQKTPNNIANLDHDPETIQKIHQTTHRINVAVKAFICIDQTFVSLRSDAVEDASRALKKANASSPVVGCRELSEDLPAYHMRKHFLHTLENPYPTQEEKETLVRLTNESTARVGQSIVNRPPLEVHQLTLWFINARRRSGWSHILKKFAREDRSRMKHLVRAKLSSSNQSTPPSPTSEYPSNNLDDFLSDNLGRPLTPADKQQFEDDWASMISWIKYGVKEKVGDWVYDLCAASKKTPKPGMPRPVTTVAKRQPARKTKPAAKPKSRTANPRASTTPSIDSTLDSSKLESTPELSMCSTADTSFSTFGSSLSMSHYDPFQYGNDILQSPTFKARGNRKVKALPKRAGKQQPDEVENGKIPFLCLSVAFV", "text": "FUNCTION: The B locus has at least 25 alleles, and any combination of two different B alleles yields a multimeric regulatory protein, that activates genes responsible for the pathogenicity and for the sexual development of the fungus within the corn plant. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/M-ATYP homeobox family."}
{"protein": "MEEPQRARSQTVTTTASSFAENFSTTSSSFSYDREFLRTLPGLLIVAEIVLGLLVWTLIAGTEYFRVPAFGWVMFVAVFYWVLTVFFLIIYLTMTYTRIPQVPWTTVGLWFNGSAFALYLSAAIVDASSVSPERDSHNFNSWAASSFFAFLVTICYAGNTYFSFIAWRSRTIQ", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chemokine-like factor family."}
{"protein": "MKALVLAGGTGTRLRPITHTSAKQLVPVANKPVLFYGLEAIRAAGIIDVGIVVGDTADEIVAAVGDGSRFGLKVSYIPQSKPLGLAHCVLISRDFLGEDDFIMYLGDNFVVGVVEDSVREFRAARPDAHLMLTRVPEPRSFGVAELSDSGQVLGLEEKPAHPKSDLALVGVYLFSPAIHEAVAAITPSWRGELEITDAVQWLIDAGRDVRSTVISGYWKDTGNVTDMLEVNRLVLETTEPRCDGLVDERSDLIGRVLVEEGAEVRNSRVMGPTVIGAGTRVTNSYVGPFTSLAEDCVVEDSEVEFSIVLRGASISGVRRIEASLIGRHVQVTSAPEVPHANRLVLGDHSRAQISS", "text": "FUNCTION: Involved in the biosynthesis of the streptose moiety of streptomycin. Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis (By similarity). SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase family."}
{"protein": "MSYPQFGYPYSSTPQFLMTTNSLSTCCESSGRSLSDSAAAASAQTPVYCPVYESRLLATARHELNSAAALGVYGNPYTSTQGYGNYVTYGADASAFYSLNAFESKDGTGSAHAGIPQTAAYYPYEHTLSQYQYDRYGTMDGSSRRKNATRETTSTLKAWLQEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWPPRNKCSDEKRPYDEEEEEEEEEEDSQKATIKNEKKTVDEEVVREDKALDLSDLEDFDTIESESSECELKQPFHHQPQDGHQLRQRDCVNDHCKDVILKMPLNSTVNQELDRTNICLKSGVDQCEQDVLRGRQRSGESKACFQQQQILDSKPRIWSLAHTATSLNQTEYPSCMLKHQGLSSPSSSSSSSAVSTPVCVIDRRQDSPVTSLRNWVDGVFHDPLFRHSTLNQALTNTTVSWATTKGTLIDSGSLGRSVGNPTNVKGQLPNIPHDTNKEFIAFQKSGSKMFCS", "text": "FUNCTION: Acts partially redundantly with other irx members in neural patterning. Required for formation of the posterior forebrain, midbrain, hindbrain, and to a lesser extent, spinal cord. Patterns the neuroectoderm in both the anterior/posterior and dorsal/ventral axes. Does not appear to play a role in pronephros kidney development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/IRO homeobox family."}
{"protein": "MEPRLLMLGFLSLTIVPSCRAELCLYDPPEVPNATFKALSYKNGTILNCECKRGFRRLKELVYMRCLGNSWSSNCQCTSNSHDKSRKQVTAQLEHQKEQQTTTDMQKPTQSMHQENLTGHCREPPPWKHEDSKRIYHFVEGQSVHYECIPGYKALQRGPAISICKMKCGKTGWTQPQLTCVDEREHHRFLASEESQGSRNSSPESETSCPITTTDFPQPTETTAMTETFVLTMEYKVAVASCLFLLISILLLSGLTWQHRWRKSRRTI", "text": "FUNCTION: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MLELNGVPVDDTYCEAFDGIYSRIIVTAKHKWLLKKAAYSATALPSTVFGEAEGGVEKWLSPQETPDGRLGAICQIWVQKSKKFLDVLMREMGKRIRQGILVVPTTRVFNATESETKFDAEINVGRCGDGYEWEDEMWGRKVIRVPIMFGEFIIERYIGYAEGIAGGNIWYFCESEEAALEAGEAAVEALKQLDGVITSFDICSAGSKPETKYPEMGPSTNHYFCPTLKGKIPDSKVPDGVKSIPEIVINGIKREVVEKAMFVCMDVVSKIDGVVRISAGNYEGKLGQHKIYLKDLIEKYS", "text": "SIMILARITY: Belongs to the FTR family."}
{"protein": "MASEIFGTAALFWVLIPLGLAGGALLLKLQGD", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetM family."}
{"protein": "MRPIILQGHERPLTQIKYNHDGDLLFSCAKDKVINVWFSHNGERLGTYEGHTGAIWTCDINKSSTLMVSGAADNTMRLWDVKTGKQLYKWEFPTAVKRVEFNEDDTRILAVTEERMGYAGTVTVFRVPISESDAAAETPLYVITTRESKATVAGWSYLSKFLFTGHEDGSVSRYDAITGEFVESKQVHNSGSTITDLQFYPDRTYFITSCKDTTAKAIDVDSFEVIKTYLTDTPLNTSSFTPVQDFVILGGGQEARDVTTTAARQGKFEARFYHAILEEELGRVKGHFGPINTIAVHPKGTGYASGGEDGYVRVHFFDKNYFDFKYTL", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eIF-3 subunit I family."}
{"protein": "MWLLQPLLLCVPLSLAVHGQQKPQVPDYPGELHCGLQSLQFAINPSPGKATPALIVWDNRGLPHKLQNNSGCGTWVRESPGGSVLLDASYSSCYVNEWVSTTQSPGTSRPPTPASRVTPQDSHYVMIVGVEGTDAAGRRVTNTKVLRCPRNPPDQALVSSLSPSPLQNVALEAPNADLCDSVPKWDRLPCASSPITQGDCNKLGCCYKSEANSCYYGNTVTSRCTQDGHFSIAVSRNVTSPPLLLNSLRLAFGKDRECNPVKATRAFALFFFPFNSCGTTRWVTGDQAVYENELVAARDVRTWSHGSITRDSIFRLRVSCSYSVRSNAFPLSVQVFTIPPPHLKTQHGPLTLELKIAKDKHYGSYYTIGDYPVVKLLRDPIYVEVSIRHRTDPSLGLLLHNCWATPGKNSQSLSQWPILVKGCPYVGDNYQTQLIPVQKALDTPFPSYYKRFSIFTFSFVDTMAKWALRGPVYLHCNVSICQPAGTSSCRITCPVARRRRHSDLHHHSSTASISSKGPMILLQATMDSAEKLHKNSSSPIDSQALWMAGLSGTLIFGFLLVSYLAIRKRR", "text": "FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor. SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 4]: Zona pellucida. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ZP domain family. ZPB subfamily."}
{"protein": "MAAGNTYSEEVLKATNWLQDNAQKEAFSYVFKTQKVNLNGKEIAWNNYNKDTTDAEMINLQRGAETSWDQATDMEWESEIDSLTKGQVLIFDSLVKKCLFEGILQKNLSPSDCYWFIQHEHGQDTGYHCHVLLGGKGLQQAMGKWFRKQLNNLWSRWLIMQCKVPLTPVERIKLRELAEDGEWVSLLTYTHKQTKKQYTKMTHFGNMIAYYFLNKKRKTTEREHGYYLSSDSGFMTNFLKEGERHLVSHLFTEANKPETVETTVTTAQEAKRGKIQTKKEVSIKCTIRDLVNKRCTSIEDWMMTDPDSYIEMMAQTGGENLIKNTLEITTLTLARTKTAYDLILEKAKPSMLPTFNISNTRTCKIFSMHNWNYIKCCHAITCVLNRQGGKRNTILFHGPASTGKSIIAQHIANLVGNVGCYNAANVNFPFNDCTNKNLIWIEEAGNFSNQVNQFKAICSGQTIRIDQKGKGSKQIEPTPVIMTTNEDITKVRIGCEERPEHTQPIRDRMLNINLTRKLPGDFGLLEETEWPLICAWLVKKGYQATMASYMHHWGNVPDWSEKWEEPKMQTPINTPTDSQISTSVKTSPADNNYAATPIQEDLDLALALEPWSEPTTPTFTTALTQHARFSNTDTSPTWSEIETDIRACFGENCAPTTNLE", "text": "FUNCTION: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). Cooperatively binds Ori with host PIF and probably other host factors, which activate the nickase function of NS1. Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis. The helicase activity unwinds DNA in a 3'-5' direction on the longer strand. Inhibits the host cell cycle during the G1/S transition, the S-phase, and the G2/M transition. These arrests may provide essential cellular factors for viral DNA replication. Promotes apoptosis in host cell. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family."}
{"protein": "MAHPQSPGEFQILAAEGPTAGAAWTRHSNDAYPKYSALSKTHWEMWMLEGIEQTGNAGVTVTFFIDGSQTFHGNDPLHITFHALLPDGAIEKHHLIAAAVRVRETDASIVLEWPSKENGDGTEANSFSRIEVAQDHSSATATFNVPGAVQGSLALTSYTRSPDPTAGALGPAVSHRQIMTGAHAESDLSFPGSGRRLRFAGKGGHDRCWMEAAFPAILSDTTYVRGHAGPYTFASLGVVSRMGESRGRNCQKFRLLRDGVEVFASKSDTVSLTEDYFVLRSSHGGPVKGPFLDTTTGYRLDFVRPRAGKHWAFEIAHEKVWWSMPLGPPPLVREGNSGFVSKVRGGEVGGDADGETFEGAGDIGQIQMPELSTLVELKTLKAKAAAAATAPAPAEQ", "text": "FUNCTION: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities (PubMed:36452919). The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins (PubMed:36452919). Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B (PubMed:36452919). Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner (PubMed:36452919). Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C (PubMed:36452919). SIMILARITY: Belongs to the Diels-Alderase family."}
{"protein": "MSILSSLISISISSPSKNSTVSSNNNYYSAVSMEGITIASSHIKTISYTSPKSSNTRAYSPTGYGYSYSYSYGYSSCGYNF", "text": "SIMILARITY: Belongs to the hssA/B family."}
{"protein": "MSTEETVDEVPCCGSHDEAQCTIQHDLAPQPLIVEEEVNNGEKKAKIAVVGCSHGEMDAIYETMALIEEKKGYKFDLLICCGDYQAVRNHGDLPHMSIPPKYRSLQTFYKYYSGEKKAPVLTLFIGGNHEASGFLCELPNGGWVAPNIFYMGFANCIQFAGLRIAGLSGIYSHGDVEFSHYERPAFAERDVKSAYHVRNVDMFRLRQLKAANNDKLSNPIDIMLSHDWPGGIPDFGDSAWLFKKKDLFEADHKSGKLGNPALMKLIYDCRPRYYLAAHLHIKFAALVPHKGSGSERPQPTRFLSLDKPIPGRQFMQALEINVASDAKMELSYDPEWLAILKNTDLLTTADKTKIVLPDRIGSVPCVYDRKDFRPTAEEMEEITKLGDLTIKTDTFKHTAPPLKEDTSEAKNVPPSAYYRNPQSAEFCQWLGIKDLNYLLVEKSSDYVGIPFYMMPDSGETEFKSNQDEVDFGEDDFIIDRGHGSEEPEAKKSRLEEEKKKKKKKIENLKTL", "text": "FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the lariat debranching enzyme family."}
{"protein": "MKWMVVALLCLPLLEASLLRVPLRKMKSIRETMKEQGVLKDFLKTHKYDPGQKYHFGNFGDYSVLYEPMAYMDASYFGEISIGTPPQNFLVLFDTGSSNLWVSSVYCQSEACTTHARFNPSKSSTYYTEGQTFSLQYGTGSLTGFFGYDTLTVQSIQVPNQEFGLSENEPGTNFVYAQFDGIMGLAYPGLSSGGATTALQGMLGEGALSQPLFGVYLGSQQGSNGGQIVFGGVDKNLYTGEITWVPVTQELYWQITIDDFLIGDQASGWCSSQGCQGIVDTGTSLLVMPAQYLSELLQTIGAQEGEYGEYFVSCDSVSSLPTLSFVLNGVQFPLSPSSYIIQEDNFCMVGLESISLTSESGQPLWILGDVFLRSYYAIFDMGNNKVGLATSV", "text": "FUNCTION: Hydrolyzes a variety of proteins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MGGEGDSSQPQSGEGEAVAVNIRCSNGTKFSVKTSLDSTVESFKELVAQSSDVPANQQRLIYKGRILKDDQTLLSYGLQADHTIHMVRGSAPSSAPPPAPAASQTTAPSVTRGVGSDNSSNLGGASPGESLFPGLGFNPLGGGNAMSGLFGAGLPDLVQTQQQLAQNPNMIRDMMNTPAIQNLMNNPEFMRSMIMNNPQMRELVDRNPELGHVLNDPSILRQTLEAARNPELMREMMRNTDRAMSNIESMPEGFNMLRRMYENVQEPLMNATTMSGNAGNNTGSNPFAALLGNQGVTTQGSDASNNSSTPNAGTGTIPNANPLPNPWGATGGQTTAPGRTNVGGDARSPGLGGLGGLGSLGGLGGLGMLGADSPLGATPDASQLSQLLQNPAISQMMQSVFSNPQYMNQLMSLNPQLRSMLDSNPQLREMMQNPDFLRQFSSPEMMQQMMTLQQSLSQNRNTASQDAGQTGAATGNNGGLDLLMNMFGSLGAGGLSGTNQSNVPPEERYATQLQQLQEMGFYDRAENIRALLATNGNVNAAVERLLGSIGQ", "text": "FUNCTION: Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a ubiquitin receptor that associates with the 26S proteasomal docking subunit RPN10 for the indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MLKNQDLDIERKQEHIEINLTKNIESTLKSGFESIQFIHNALPEINYDNIDTTTTFLGKALQAPILISSMTGGTARARDINYRLAEAAQKAGIAMGLGSMRVLLAAADTIKTFAVRHIAPDILLLANIGAVQLNYGVTPKECQYLVDATKADALILHLNVLQELTQPEGNRNWANLLPKIREVINYLSVPVIVKEVGYGLSKQVAKSLIDVGVKTLDIAGSGGTSWSQVEAYRAKNSLQNRIASSFINWGIPTLDSLKMVREISKNVSIIASGGLKSGIDGAKAIRMGANIFGLAGQLLKAVDNSEYLVSEEIQLIIKQLKITMLCTGSRTLKDLTKAEIKL", "text": "FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IPP isomerase type 2 family."}
{"protein": "MPPKPAEKKPSSTAGKAPASSAGKAPAEAAKKTSKAPAKSGEKKKATKVRKETYSTYIYRVLKQVHPDTGISNKAMAILNSFVQDIFERIATEASKLASYNKKSTISSREIQTAVRLILPGELSKHAISEGTKSVTKFSSSK", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H2B family."}
{"protein": "MERSVQENTLHYTIGHVLIIARIFGVLPLAGINPNGKPENVRFRWFSPYILFFVVAFTFVIADFMLSTKIVLNDGLQLYTMGSLSFSVICIFCFGSFIKLSRRWPHIIRETALCERIFLKPCYANQEGLNFTRFLRRWALILLVAALCEHLTYVGSAAWSNYVQIRDCNLKVGFVENYFLRERQELFSVFEYRAWMVFFIEWNTMAMTFVWNFGDIFLFLMCRGLKIRFQQLHWRIRQNLGKPMAKEFWQEIRSDFLDLDSLLKLYDKELSGLILVCCAHNMYFICVQVYHSFQVKGAFMDELYFWFCLLYVISRLMNMMLAASSIPQEIKDISNTLYEVRSSPWCDELGRLSEMLRNETFALSGMGYFYVTRRLIFAMAGALMGYELVLFRQMQGAVVQKSICSRGPGSSMSIFFS", "text": "FUNCTION: One of the few identified sugar gustatory receptors identified so far and which promotes the starvation-induced increase of feeding motivation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Gustatory receptor (GR) family. Gr5a subfamily."}
{"protein": "MGAAVTLNRIKIETGIADIRDKYMVLDFNYPEYNRAVRFAEESYMYYYETSPGEIKPKFCLIDGMSIDHCSSFIVPEFAKQYVLIHGEPCSSFKFRPGSLIYYQNEVTPEYIKDLKYATDYIASGQRCHFIKKDYLLGDSDSVAKCCSKTNTKHCPKIFNNNYKTEHCDDFMTGFCRNDPGNPNCLEWLRVKRKPAMSTYSDICSKHMDARYCSEFIRIIRPDYFTFGDTALYVFCNDHKGNRNCWCANYPKSNSGDKYLGPRVCWLHECTDESRDRKWLYYNQDVQRTRCKYVGCTINVNSLALKNSQAELTSNCTRTTSAVGDVHPGEPVVNDKIKLPTWLGASITLVVISVIFYFISIYSRPKIKTNDINVRRR", "text": "FUNCTION: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the mature virion (MV) membrane. The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. SIMILARITY: Belongs to the orthopoxvirus OPG143 family."}
{"protein": "MMIKVASITKLENGSIVTPKGFSAIGTVNGLKKEKKDLGAIVCDVPASCAAVYTTNQIQAAPLQVTKDSITAEGKLQAIIVNSGNANACTGMQGLQDAYEMRVLGAEHFGMKENYVAVASTGVIGVPLPMDIIRKGVATLIPTKEESEAYSFSEAILTTDLITKETCYEMIIDGKKVVIAGVAKGSGMIHPNMATMLSFITTDAHIEHNVLQTALSQITNHTFNQITVDGDTSTNDMVIVMASGLSETRPINMEHTDWETFVGALQKVCEDLAKKIAQDGEGATKLIEVNVLGAQTNEEAKKIAKQIVGSSLVKTAIHGEDPNWGRIISSIGQSEVAINPNTIDITLQSISVLKNSEPQTFSEEKMKERLQEDEIVINVYLHLGEETGSAWGCDLSYEYVKINACYRT", "text": "FUNCTION: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArgJ family."}
{"protein": "MNRVGAVFLFVYERNFFLSIVPDRHRTEIRMSSSERSEVKFDKHFNWWSLLGIAFSLSCSWVGISASMAVGIASGGPLLIIYGLIIAAFFSLMCGISLGDFAAILPNSSGGSFWVLKMLEQESVTLKTPEYEDPSDDDEEVFLENYCQTFNVEVSSKFQKVSSMVVGLLNYFGAIFTTASICSSLSMSCIGIHKLLHPDYELKHWHVFVGYECINAVLTLFNIYSTPLPYISQFGLYTSLLSFAMTFIICIVSRSDNTVDPWPKASNIFGSFDNQTGWNSSGMAFVVGLVNPIWAFVGIDSATHMIDEVGYSKSRFLVPKVIITTIIVGFVTSFIYCVGLFFCITDQTAVVESILPIVEIFYQATGNRNLSVFLQCMCITTGFVSGIASGTWQSRILQSFGKSYAPFYKEGSLGNKSLKKLAVLTPGFKSPLYAHFLSQICVTIIGCIFMGSSTAFNAIITACITLLLMSYAVPSFIFLFVIKKEKFIHRIESDVNCVSRPNRRRMSMIPHIICILWTLFCLVFLSFPYTLPVTAGNMNYTSVVYAVVFCIISIVVFPTCI", "text": "FUNCTION: Transport into the cell of 7-keto 8-aminopelargonic acid. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily."}
{"protein": "MNTSIPYQQSPYSPRGGSNVIQCYRCGDTCKGEVVRVHNNHFHIRCFTCQVCGCGLAQSGFFFKNQEYICTQDYQQLYGTRCDSCRDFITGEVISALGRTYHPKCFVCSLCRKPFPIGDKVTFSGKECVCQTCSQSMTSSKPIKIRGPSHCAGCKEEIKHGQSLLALDKQWHVSCFKCQTCSVILTGEYISKDGVPYCESDYHSQFGIKCETCDRYISGRVLEAGGKHYHPTCARCVRCHQMFTEGEEMYLTGSEVWHPICKQAARAEKKLKHRRTSETSISPPGSSIGSPNRVICAKVDNEILNYKDLAALPKVKSIYEVQRPDLISYEPHSRYTSDEMLERCGYGESLGTLSPYSQDIYENLDLRQRRASSPGYIDSPTYSRQGMSPTFSRSPHYYRSGPESGRSSPYHSQLDVRSSTPTSYQAPKHFHIPAGESNIYRKPPIYKRHGDLSTATKSKTSEDISQASKYSPAYSPDPYYASESEYWTYHGSPKVPRARRFSSGGEEEDFDRSMHKLQSGIGRLILKEEMKARSSSYADPWTPPRSSTSSREALHTTGYEMSFNGSPRSHYLADSDPLISKSASLPAYRRNGLHRTPSADLFHYDSMNAVNWGMREYKIYPYELLLVTTRGRNRLPKDVDRTRLERHLSQEEFYQVFGMTISEFERLALWKRNELKKQARLF", "text": "FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MTEMSFLNSEVLAGDLMSPFDQSGLGAEESLGLLDDYLEVAKHLKPHGFSSDKAGSSEWPAMDDGLASASDTGKEDAFSGTDWMLEKMDLKEFDFDALFRMDDLETMPDELLTTLDDTCDLFAPLVQETNKEPPQTVNPIGHLPESLIKVDQVAPFTFLQPFPCSPGVLSSTPEHSFSLELGSEVDISEGDRKPDSAAYITLIPPCVKEEDTPSDNDSGICMSPESYLGSPQHSPSTSRAPPDNLPSPGGSRGSPRPKPYDPPGVSLTAKVKTEKLDKKLKKMEQNKTAATRYRQKKRAEQEALTGECKELEKKNEALKEKADSLAKEIQYLKDLIEEVRKARGKKRVP", "text": "FUNCTION: Transcription factor that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') and displays two biological functions, as regulator of metabolic and redox processes under normal cellular conditions, and as master transcription factor during integrated stress response (ISR) (PubMed:8506317, PubMed:11106749, PubMed:12667446, PubMed:23624402). Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (PubMed:8506317, PubMed:23624402). Core effector of the ISR, which is required for adaptation to various stress such as endoplasmic reticulum (ER) stress, amino acid starvation, mitochondrial stress or oxidative stress (PubMed:11106749, PubMed:12667446). During ISR, ATF4 translation is induced via an alternative ribosome translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced ATF4 acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (PubMed:11106749, PubMed:12667446). Promotes the transcription of genes linked to amino acid sufficiency and resistance to oxidative stress to protect cells against metabolic consequences of ER oxidation (PubMed:12667446). Activates the transcription of NLRP1, possibly in concert with other factors in response to ER stress (By similarity). Activates the transcription of asparagine synthetase (ASNS) in response to amino acid deprivation or ER stress (PubMed:15775988, PubMed:21159964). However, when associated with DDIT3/CHOP, the transcriptional activation of the ASNS gene is inhibited in response to amino acid deprivation (By similarity). Together with DDIT3/CHOP, mediates programmed cell death by promoting the expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the terminal unfolded protein response (terminal UPR), a cellular response that elicits programmed cell death when ER stress is prolonged and unresolved (PubMed:23624402). Together with DDIT3/CHOP, activates the transcription of the IRS-regulator TRIB3 and promotes ER stress-induced neuronal cell death by regulating the expression of BBC3/PUMA in response to ER stress (PubMed:15775988, PubMed:17369260, PubMed:21159964). May cooperate with the UPR transcriptional regulator QRICH1 to regulate ER protein homeostasis which is critical for cell viability in response to ER stress (By similarity). In the absence of stress, ATF4 translation is at low levels and it is required for normal metabolic processes such as embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (PubMed:10096021, PubMed:10885750, PubMed:11806972, PubMed:12925279, PubMed:15109498, PubMed:22298775). Acts as a regulator of osteoblast differentiation in response to phosphorylation by RPS6KA3/RSK2: phosphorylation in osteoblasts enhances transactivation activity and promotes expression of osteoblast-specific genes and post-transcriptionally regulates the synthesis of Type I collagen, the main constituent of the bone matrix (PubMed:15109498). Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (PubMed:22298775). Activates transcription of SIRT4 (PubMed:23663782). Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4 (PubMed:21768648, PubMed:22572884). Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes (PubMed:21768648, PubMed:22572884). Mainly acts as a transcriptional activator in cellular stress adaptation, but it can also act as a transcriptional repressor: acts as a regulator of synaptic plasticity by repressing transcription, thereby inhibiting induction and maintenance of long-term memory (PubMed:12925279). Regulates synaptic functions via interaction with DISC1 in neurons, which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (PubMed:31444471). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with GABBR1 in hippocampal neuron dendritic membranes. Colocalizes with NEK6 in the centrosome (By similarity). Recruited to nuclear speckles following interaction with EP300/p300 (By similarity). SIMILARITY: Belongs to the bZIP family."}
{"protein": "MFPTIRSCARGTSTPADNYMLARRRTLQVVVSSLLTEAGFDSAEKAAVESLTEMLQSYLSEIGRSAKSYCEHTARTQPTLPDIVVTLIEMGFNVDSLPAYAKRSQRMVITAPPVTNNPVVPKALSAGDNKPHPAHIPSHFPEFPDPHTYIKTPTYREPVCDYQVLREKAASQRRDVERALTRFMAKTGETQSLFKDDTSTFPLIAARPLSIPYLNALLPSELELQQVDETDSSEQDDQTDTENLSLHLQGDEVGMEKENASVLQQNSMKGGEETLIDNPYLRPVKKPKLRRKK", "text": "FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit tbp, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of tbp and TBP-associated factors (TAFs). Mediates both basal and activator-dependent transcription. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the TAF8 family."}
{"protein": "MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPEKNECCPNYACSSKHKWCKSI", "text": "FUNCTION: Lethal neurotoxin. Selectively blocks tetrodotoxin-sensitive voltage-gated sodium channels (Nav). Does not affect tetrodotoxin- resistant voltage-gated sodium channels or calcium channels (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 51 (Hntx-8) subfamily."}
{"protein": "MICPHQGTCGGCALALPYEEQWKLKESEFRELLPLSKDTPTDLYPSAPHSFRARAEFRLYRNESGRLSYAMSQKGSKQPLPIQSCPILLPSIQALMPSLLEALESDEILTQKLFGVEFLSGLSQEVLVSLLYHKRLDHAWEERALGLLSSLPTLSSLIGRSKGQKIVLGESFITETLTIDSKPWRFLHYEGSFTQPNPKVNEKMIEWIISAPPQGDLLELYCGAGNFTLPLSSRYAKILATEVSKTSIHAAKQNCELNSVRHISFVRLNAQETQSALEGEREFYRLRELDLPSYDFQAVFVDPPRAGLGAEVASFLRRFDQILYISCNPKTLQSDLEVLQLSHDVERFALFDQFPYTPHLESGVILRQRR", "text": "FUNCTION: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. TrmA subfamily."}
{"protein": "MTENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEASNEREFGYAQVEVVNDSALVRGIEDALTADGKPLLDVWMSHGDKVTAIPSDFITVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLLRLNEAEQVLDMFGDHFGLNIVHVPAEDRFLSALAGENDPEAKRKIIGRVFVEVFDEEALKLEDVKWLAQGTIYPDVIESAASATGKAHVIKSHHNVGGLPKEMKMGLVEPLKELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE", "text": "FUNCTION: Catalyzes the synthesis of GMP from XMP. FUNCTION: Catalyzes the synthesis of GMP from XMP."}
{"protein": "MAHTEQYRFPKDFWWGSSASATQMEGAADRDGKGQNIWDYWFEKEPHRFFDHVGPADTSQFYDNYKEDIRLMKELGHNSFRMSISWSRLIPNGTGEINDKAADFYNNVIDELIANGIEPFVNLFHFDMPMALQKIGGWVNRETVDAYENYARTCFRLFGGRVKKWFTHNEPIVPVEGGYLYDFHYPNKVDFKEAVQVGFHTMLSSARAIQAYREMKQDGKIGIILNLTPSYPRSSHPADVKAGEIADAFFNRSFLDPSVKGEFPKELVDILKHEGFMPDYNAEDLDIIKKNTVDLLGVNYYQPRRVKAKEHLPNPDAPFLPDRYFDPYVMPGRKMNPHRGWEIYEKGVYDILINLKENYGNIECFISENGMGVEGEERFRDEQGIIQDDYRIEFIKEHLKWIHRAIQEGSNVKGYHLWTFMDNWSWTNAYKNRYGFVSVNLEKDGERTVKKSGKWFKEVAEHSGF", "text": "FUNCTION: Phospho-beta-D-glucosidase that seems to be involved in the degradation of glucomannan. Is also capable of hydrolyzing aryl- phospho-beta-D-glucosides, although very weakly, and plays only a minor role, if any, in the degradation of these substrates in vivo. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MAENGLNIVWHSRSLTKADYYDRNGHRPLVVWFTGLSGSGKSTLAHAAEEALFKKGCYTYILDGDNMRHGLNSDLGFSEADRRENIRRIGEVAKLFVDAGIVVLAAFISPYQEDRDRVRALFEPAEFIEIYVKCDLDTCESRDPKGLYRKARAGQLPQFTGIDSPYEEPQAPELVIDTCRLGVEESVAAIIRFVERRSADGGRLTADG", "text": "FUNCTION: Catalyzes the synthesis of activated sulfate. SIMILARITY: Belongs to the APS kinase family."}
{"protein": "MGLLALGTPLQWFESRTYNEHIRDEGIEQLLYIFQAAGKRDNDPLFWGDELEYMVVDFDDKERNSMLDVCHDKILTELNMEDSSLCEANDVSFHPEYGRYMLEATPASPYLNYVGSYVEVNMQKRRAIAEYKLSEYARQDSKNNLHVGSRSVPLTLTVFPRMGCPDFINIKDPWNHKNAASRSLFLPDEVINRHVRFPNLTASIRTRRGEKVCMNVPMYKDIATPETDDSIYDRDWFLPEDKEAKLASKPGFIYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAPAFKGWLADQDVRWNVISGAVDDRTPKERGVAPLLPKYNKNGFGGIAKDVQDKVLEIPKSRYSSVDLFLGGSKFFNRTYNDTNVPINEKVLGRLLENDKAPLDYDLAKHFAHLYIRDPVSTFEELLNQDNKTSSNHFENIQSTNWQTLRFKPPTQQATPDKKDSPGWRVEFRPFEVQLLDFENAAYSVLIYLIVDSILTFSDNINAYIHMSKVWENMKIAHHRDAILFEKFHWKKSFRNDTDVETEDYSISEIFHNPENGIFPQFVTPILCQKGFVTKDWKELKHSSKHERLYYYLKLISDRASGELPTTAKFFRNFVLQHPDYKHDSKISKSINYDLLSTCDRLTHLDDSKGELTSFLGAEIAEYVKKNKPSIESKC", "text": "FUNCTION: Catalyzes the ATP-dependent condensation of cysteine and glutamate to form the dipeptide gamma-glutamylcysteine (gamma-GC), the first and rate-limiting step in the production of glutathione (GSH). SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family."}
{"protein": "MVLLHWCLLWLLFPLSSRTQKLPTRDEELFQMQIRDKAFFHDSSVIPDGAEISSYLFRDTPKRYFFVVEEDNTPLSVTVTPCDAPLEWKLSLQELPEDRSGEGSGDLEPLEQQKQQIINEEGTELFSYKGNDVEYFISSSSPSGLYQLDLLSTEKDTHFKVYATTTPESDQPYPELPYDPRVDVTSLGRTTVTLAWKPSPTASLLKQPIQYCVVINKEHNFKSLCAVEAKLSADDAFMMAPKPGLDFSPFDFAHFGFPSDNSGKERSFQAKPSPKLGRHVYSRPKVDIQKICIGNKNIFTVSDLKPDTQYYFDVFVVNINSNMSTAYVGTFARTKEEAKQKTVELKDGKITDVFVKRKGAKFLRFAPVSSHQKVTFFIHSCLDAVQIQVRRDGKLLLSQNVEGIQQFQLRGKPKAKYLVRLKGNKKGASMLKILATTRPTKQSFPSLPEDTRIKAFDKLRTCSSATVAWLGTQERNKFCIYKKEVDDNYNEDQKKREQNQCLGPDIRKKSEKVLCKYFHSQNLQKAVTTETIKGLQPGKSYLLDVYVIGHGGHSVKYQSKVVKTRKFC", "text": "FUNCTION: Secretory protein that plays a role in various cellular processes (PubMed:20969804, PubMed:24706764, PubMed:31883645). Acts as a chemorepellent acting on gonadotropin-releasing hormone (GnRH) expressing neurons regulating their migration to the hypothalamus (PubMed:31883645). Also promotes neuron migration, growth and survival as well as neurite outgrowth and is involved in the development of the olfactory system (PubMed:20969804, PubMed:31883645). May also act through the regulation of growth factors activity and downstream signaling (PubMed:31883645). Also regulates extracellular matrix assembly and cell adhesiveness (By similarity). Promotes endothelial cell survival, vessel formation and plays an important role in the process of revascularization through NOS3-dependent mechanisms (PubMed:24706764). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MRSAFILALGLITASADALVTRGAIEACLSAAGVPIDIPGTADYERDVEPFNIRLPYIPTAIAQTQTTAHIQSAVQCAKKLNLKVSAKSGGHSYASFGFGGENGHLMVQLDRMIDVISYNDKTGIAHVEPGARLGHLATVLNDKYGRAISHGTCPGVGISGHFAHGGFGFSSHMHGLAVDSVVGVTVVLADGRIVEASATENADLFWGIKGAGSNFGIVAVWKLATFPAPKVLTRFGVTLNWKNKTSALKGIEAVEDYARWVAPREVNFRIGDYGAGNPGIEGLYYGTPEQWRAAFQPLLDTLPAGYVVNPTTSLNWIESVLSYSNFDHVDFITPQPVENFYAKSLTLKSIKGDAVKNFVDYYFDVSNKVKDRFWFYQLDVHGGKNSQVTKVTNAETAYPHRDKLWLIQFYDRYDNNQTYPETSFKFLDGWVNSVTKALPKSDWGMYINYADPRMDRDYATKVYYGENLARLQKLKAKFDPTDRFYYPQAVRPVK", "text": "FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on mono-, oligo- and polysaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Carbohydrate oxidase is able to oxidize a variety of substrates including D-glucose, D-galactose, D-xylose, D-maltose, D- cellobiose, and lactose. In addition, among various oligosaccharides, the enzyme preferred tetrameric dextrins, indicating a favorable interaction of four linked glucose units with the substrate binding pocket. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MVQAKAQQQLYTHAAEPKAVQQRRAKYREDETTQTLPTANIMFDRRVVRGNTYAARILPADATQTQTKGPSPASTKKRTTRTLPPRTPEAVDGRRHIDIQTDVYLEELTDTVPEADTSTQTDAFLDRPPTPLFVPQKTGTDAITQIENGDLFDFDFEVEPILEVLVGKVLEQGLMEVLEEEELAAMRAHQEHFEQIRNAELVATQRMEAAERRKLEEKERRMQQERERVERERVVRQKVAASAFARGYLSGIVNTVFDRLVSSGYIYDPVMREVETAFMPWLKEQAIGYLARGVVARRVVDKLVEDAAAALAANRSTLADKAASTAATVDAWAERQAKMEAELQGKELEAVRRRPTFVLRELKPAVASADAVEAAAAELTAQAEEAANAKWEADKAEAAEKARAEAEAAAEEQKALLEELAATAAAEAEERGEEPPAEPPSLPDGVEPVDVEAEVAKAVEAVPKPPVKEVTDIDILSYMMDKGAITKDAIIQALAVHALGDKAYTNHPAFAEAEGA", "text": "FUNCTION: Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. FUNCTION: Protein 3 may attach the radial spoke to the outer doublet microtubule or is required to form a stable spoke structure. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme Note=Radial spoke. SIMILARITY: Belongs to the flagellar radial spoke RSP3 family."}
{"protein": "MAKVAKDLNPGVKKMSLGQLQSARGVACLGCKGTCSGFEPHSWRKICKSCKCSQEDHCLTSDLEDDRKIGRLLMDSKYSTLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALGVGEVALPGQGGLPKEEGKQQEKPEGAETTAATTNGSLSDPSKEVEYVCELCKGAAPPDSPVVYSDRAGYNKQWHPTCFVCAKCSEPLVDLIYFWKDGAPWCGRHYCESLRPRCSGCDEIIFAEDYQRVEDLAWHRKHFVCEGCEQLLSGRAYIVTKGQLLCPTCSKSKRS", "text": "FUNCTION: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6- mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC promoter (By similarity). Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=May shuttle between the cytoplasm and the nucleus."}
{"protein": "MNIALVAHDQMKNTMVGFCIGYESILKKYGLYATGTTGKRIMDETELNINRLASGPLGGDQQIGSLIVTQEIDLVIFLRDPLTSQAHETDIQALIRLCDVYHVPIATNLASAEIFIKALDRGELSWREVRKSKSQRI", "text": "FUNCTION: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. SIMILARITY: Belongs to the methylglyoxal synthase family."}
{"protein": "MSASASLPVTRAAAAPRITVLFSTEKPNANTNPYLTQLYDALPDAVQPRFFSMREALLSRYDVLHLHWPEYLLRHPSKMGTLAKQACAALLLMKLQLTGTPVVRTLHNLAPHEDRGWRERALLRWIDQLTRRWIRINATTPVRPPFTDTILHGHYRDWFATMEQGTTVPGRLLHFGLIRPYKGVEVLLDVMRDVQDPRLSLRIVGNPATPQMRTLVETACAQDARISALLAYVEEPVLAREVSACELVVLPYKQMHNSGTLLLALSLARPVLAPWSESNAAIAEEVGPGWVFLYEGEFDAALLSGMLDQVRAAPRGPAPDLSQRDWPRIGQLHYRTYLEALGKDGDAAL", "text": "FUNCTION: Nonprocessive beta-mannosyltransferase that catalyzes the transfer of a mannose residue from GDP-mannose to glucuronic acid-beta- 1,2-mannose-alpha-1,3-glucose-beta-1,4-glucose-PP-polyisoprenyl to form the lipid-linked pentasaccharide repeating unit of xanthan, Man-GlcA- Man-Glc(2)-PP-Pol. Is involved in the biosynthesis of the exopolysaccharide xanthan (By similarity). SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the glycosyltransferase 94 family."}
{"protein": "MQRGALRGASPTARRRLVDRPGLTEDEIEEIREAFNLFDTDGSGMIDPKELKAAMQSLGFETKNPTIYQMIADLDRDSGGPIDFEEFLDAITAKLGDKESREGIQKIFSLFDDDRTGTITLKNLKRVAKELGETMSEDELREMLERADSNGDGEISFEDFYAIMTKKTFP", "text": "FUNCTION: In tachyzoites, plays an essential role in microneme secretion that ensures parasite motility and attachment to, invasion of and egress from host cells (PubMed:31182647, PubMed:31206964). Also involved in the architecture of the peripheral annuli where it appears to regulate the localization of PAP2 (PubMed:31206964). In association with the myosin motor MyoJ, involved in the constriction of the basal complex at the end of daughter cell division in an actin-dependent manner; the basal complex is a cytoskeletal structure formed at the tachyzoite basal pole during daughter cell formation (PubMed:28593938). May be involved in parasite replication (PubMed:31182647). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=In tachyzoites, localizes to preconoidal rings, peripheral annuli, centrioles and basal complex (PubMed:18208326, PubMed:31206964, PubMed:31182647, PubMed:28593938). Recruitment to the daughter basal complex occurs at a late stage of daughter cell assembly (PubMed:18208326, PubMed:31182647). SIMILARITY: Belongs to the centrin family."}
{"protein": "MAHVNNYLLVTLLLISIYGYMGKNFVTVFYGIPAWKNASIPLFCATRNRDTWGTVQCLPDNDDYTEIQLNITEAFDAWDNTVTDQATKDVWSLFETSIKPCVKLTPLCVTMKCNKTWSSASKETTTSSASLRSSTQTLLNEDSKCIQNDSCAGIGLEEMIDCQFKMTGLKRDESKQYKDTWYKQDLVCEKGTRSNESKCYIKTCNTSIIQESCDKHYWDSLRFRYCAPPGFALLRCNDTKYSGFMPNCSKVVVSLYRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNSYYNLTMHCKRPGNKMVVPIRTVSGILFHSQPINKRPKQAWCWFKGNWTEAIQEVKETIKNHPRYSGTTNISQIRLAEHARSSDPEVRYMWTNCRGEFLYCNMTFFLNWVENRTGLKRNYASCHIRQIVNTWHKIGRNVYLPPREGELSCNSTVTSLIANIDWIDKNLTNITVSAEVSELYKLELGDYKLVEITPIGFAPTSIKRYSSVTPRNKRGVLVLGFLGFLATAGSAMGAASLTLSAQSRTLLAGIVQQQQQLVDVVKRQQELLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWVNESLKPDWNNMTWQQWERQVRFLDANITKLLEEAQIQQEKNMYELQKLNQWDIFSNWFDFTSWMAYIRLGLYIVIGIVVLRIAIYIIQMLARLRKGYRPVFSSPPSYTQQIPIRKDRGQPANEETEEGGGNNEGYRSWPWQIEYIHFPIRQLRDLLIWLYSGCRTLLSKTFQTLQPVLQPLRLPPAYLRYGISWFQEAIQAAARAAGETLASAARTSWGVLRRAAGEIIAIPRRIRQGAELALL", "text": "FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. Since CD4 also displays a binding site for the disulfide-isomerase P4HB/PDI, a P4HB/PDI-CD4-CXCR4-gp120 complex may form. In that complex, P4HB/PDI could reach and reduce gp120 disulfide bonds, causing major conformational changes in gp120. TXN, another PDI family member could also be involved in disulfide rearrangements in Env during fusion. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl- ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). FUNCTION: The gp120-gp41 heterodimer seems to contribute to T-cell depletion during HIV-1 infection. The envelope glycoproteins expressed on the surface of infected cells induce apoptosis through an interaction with uninfected cells expressing the receptor (CD4) and the coreceptors CXCR4 or CCR5. This type of bystander killing may be obtained by at least three distinct mechanisms. First, the interaction between the 2 cells can induce cellular fusion followed by nuclear fusion within the syncytium. Syncytia are condemned to die from apoptosis. Second, the 2 interacting cells may not fuse entirely and simply exchange plasma membrane lipids, after a sort of hemifusion process, followed by rapid death. Third, it is possible that virus- infected cells, on the point of undergoing apoptosis, fuse with CD4- expressing cells, in which case apoptosis is rapidly transmitted from one cell to the other and thus occurs in a sort of contagious fashion (By similarity). FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of HIV-specific CD4+ cells (By similarity). SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Host endosome membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag."}
{"protein": "MKKLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHYILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIEIDALSARLGCPVIPLVSTRGRGIEALKLAIDRYKANENVELVHYAQPLLNEADSLAKVMPSDIPLKQRRWLGLQMLEGDIYSRAYAGEASQHLDAALARLRNEMDDPALHIADARYQCIAAICDVVSNTLTAEPSRFTTAVDKIVLNRFLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVALFVHGIQWIGYTLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYMLGIVMAVLTGLMLKYTIMRGEATPFVMELPVYHVPHVKSLIIQTWQRLKGFVLRAGKVIIIVSIFLSAFNSFSLSGKIVDNINDSALASVSRVITPVFKPIGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEFNPAEFNLGEELFSAVDETWQSLKDTFSLSVLMNPIEASKGDGEMGTGAMGVMDQKFGSAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQVASYSQHPTYSLVCILAVILFNIVVIGLLRRARSRVDIELLATRKSVSSCCAASTTGDCH", "text": "FUNCTION: Probable transporter of a GTP-driven Fe(2+) uptake system. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family."}
{"protein": "MSQIPKELEKVIELTREQNRWRRTEVINLIASENVMSPLAETVYMSDFMSRYAEGKPYKRYYQGTKYVDEVETLAMQLMNEITNTKFCDLRATSGTIANAAVFRVLANPGEKALIAPVQAGAHVSHTKFGTLGALGIEHIELPYDADKMNVDVDKAIKMIEQIKPKFIVMGGSLYLFPHPVKELAPHAHAVGAKVVYDAAHVYGLITGKAWHNPLEEGADIMTSSTHKTFPGPQGGAVFSNEEEIFKKVADTIFPWFVSNHHLHRLPATAVTALEMKYFGEDYAKQITKNAKAFAEALAAEGFKVIGEHLGYTQSHQVVLDVRNLGGGAKIAKLFEDANIITNKNLLPYDPPSAVKDPSGIRLGVQEMTRFGMKEEEMREIAKLMREVAIDGKDPNEVKKKVIEFRKNYLEVKYTFSVDLSKYSNGKMLPLLI", "text": "FUNCTION: Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta- hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family."}
{"protein": "MGAFTEKQEALVNSSWEAFKGNIPQYSVVFYTSILEKAPAAKNLFSFLANGVDPTNPKLTAHAESLFGLVRDSAAQLRANGAVVADAALGSIHSQKGVSNDQFLVVKEALLKTLKQAVGDKWTDQLSTALELAYDELAAAIKKAYA", "text": "FUNCTION: Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. SIMILARITY: Belongs to the plant globin family."}
{"protein": "MFNPHALDSPAVIFDNGSGFCKAGLSGEFGPRHMVSSIVGHLKFQAPSAEANQKKYFVGEEALYKQEALQLHSPFERGLITGWDDVERLWKHLFEWELGVKPSDQPLLATEPSLNPRENREKMAEVMFENFGVPAFYLSDQAVLALYASACVTGLVVDSGDAVTCTVPIFEGYSLPHAVTKLHVAGRDITELLMQLLLASGHTFPCQLDKGLVDDIKKKLCYVALEPEKELSRRPEEVLREYKLPDGNIISLGDPLHQAPEALFVPQQLGSQSPGLSNMVSSSITKCDTDIQKILFGEIVLSGGTTLFHGLDDRLLKELEQLASKDTPIKITAPPDRWFSTWIGASIVTSLSSFKQMWVTAADFKEFGTSVVQRRCF", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
{"protein": "MSGRDNRGAGGGGGGGHHHQPLSSAMGKLKEKLTRAGEELGYHRVESNLSASNTGTSLDTILPEDPFPFPQAAPQRHPQQQFPHLHPLRLLHDVDDEPPLSFRPLLEDDDINEPPQQIQQQRSALRSSGSLELTPLPPPPTSLEPHRDRQQRSIVTGGEELQRSKQSLKGSRVSFEKPQQQGNNKAAESSDEDSFEDKRIGFQQQKATSVDHKGILKDLRHILANDNRRQFQAKKHVSLDIKGTRFLQDLLKDSSSEEEFHKTRREFQGRKHQSLDPRVTFKLDKVLQGSSTDSDEEGDDAEHKRLIHRPKDITKPVIIDLKDLESESDEDFLTSRQNFQQQRSISTDSRKSRRLYEMDEMGNKRGDNIRHAVPFVRQITEDGKPKLEVYRPTTNPIYIWTQVLAALSVSLGSLVVGFASAYTSPALVSMTNTNLTSFVVTPQAASWVGGIMPLAGLAGGIAGGPFIEYLGRRNTILATAVPFIISWLLIACAVNVVMVLCGRFLAGFCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILLCFVAGTYMDWSMLAFLGGTLPVPFLILMFLIPETPRWYVSRGREERARKALVWLRGKEADVEPELKGLMRSQADADRQATQNTMLELLKRSNLKPLSISLGLMFFQQLSGINAVIFYTVQIFQDAGSTIDGNVCTIIVGVVNFMATFIATVLIDRAGRKILLYVSNVAMILTLFVLGGFFYCKSTGMDTSNVGWLPLSCFVVYILGFSLGFGPIPWLMMGEILPAKIRGSAASVATAFNWSCTFVVTKSFQDMIDVMGAHGAFWMFGAICFVGLFFVIFYVPETQGKTLEDIERKMMGRVRRMSSVANIKPLSFNM", "text": "FUNCTION: Low-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Trehalose transporter subfamily."}
{"protein": "MATTMMTSSASPPESGELDVASAVASAAAALISPMVMPTSMTNGKDMTKTSQILNEYFNMMVGKRVQLMGDTTSPFSLDTPNPKLMFTPLDLPTTAELMQRCLAVNPFEAKFREANQKISSGSMQPNTSGANQSLEALEANGGSQFSGSNAGTMSDLLLKIPQASLQHSPGIFSNMLLNAGDSEGTTRENLKTADISKLLSVAGDFSAQAPRTADVLNAVLDMHSDRLHTINYLNNKPDFSALLRSPSSSAPNSASVLTNAMAIPSTSGAPFPGTTLLVPPKTVSSYHSPLGASSQPPSTQKSPADGSWDHINGEKQIKKEIPYFNDDAMMLMERSNMSSSGSDQDQSADMSNAGSTASTSTGNPVGRPQNGTPGRGRGRGRSTTADMQPDERRNTILERNKAAAVRYRKRKKEEHDDMMGRVQAMEAEKNQLLAIQTQNQVLRRELERVTALLTERESRCVCLKGVPMSDEQHADHHHRNTNGMYSGSDMLNGLGQINGMQLKLPKLQ", "text": "FUNCTION: Transcription factor which regulates the transcription of various genes, including those involved in innate immunity and oxidative stress responses (PubMed:20369020, PubMed:28632756, PubMed:30789901). Binds to promoter regions of genes, probably at 5'- [GACGTCA]-3' consensus sequences (PubMed:30789901). Together with transcription factor daf-19, involved in regulation of the serotonergic response of ADF neurons to pathogenic food (PubMed:23505381). Modulates response to infection by the Gram-negative bacterium P.aeruginosa, acting downstream of the p38 signal transduction pathway effector serine/threonine kinase pmk-1 (PubMed:20369020, PubMed:30789901). May act with transcription factor elt-2 to control p38 gene induction in response to bacterial infection (PubMed:26016853). May be phosphorylated by pmk-1 (PubMed:20369020). Regulates transcription of the metallothionein gene, mtl-1, perhaps acting downstream of pmk-1 (PubMed:28632756). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MVPNYSTEETVKRIHVDCPVSGRHSYIYIMVPTVYSIIFIIGIFGNSLVVIVIYCYMKLKTVASIFLLNLALADLCFLITLPLWAAYTAMEYQWPFGNCLCKLASAGISFNLYASVFLLTCLSIDRYLAIVHPVKSRIRRTMFVARVTCIVIWLLAGVASLPVIIHRNIFFAENLNMTVCGFRYDNNNTTLRVGLGLSKNLLGFLIPFLIILTSYTLIWKTLKKAYQIQRNKTRNDDIFKMIVAIVFFFFFSWIPHQVFTFLDVLIQLHVITDCKITDIVDTAMPFTICIAYFNNCLNPFFYVFFGKNFKKYFLQLIKYIPPNVSTHPSLTTKMSSLSYRPPENIRLPTKKTAGSFDTE", "text": "FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MGTPGSGRKRTPVKDRFSAEDEALSNIDREAEARLAAKRAARAEARDIRMRELERQQKELDEKSDKQYAENYTRPSSRNSASATTPLSGNSSRRVSGDTSSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKHGLVIIPDGTPNGDVHQEPAVGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSGRDGTAGDLAELQNGSDLQLIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYRTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ", "text": "FUNCTION: May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity). SIMILARITY: Belongs to the LRRFIP family."}
{"protein": "SLVHAQSILAIWACQVVLMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLAEDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWSYATNFVPGK", "text": "FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family."}
{"protein": "MAARLCCQLDPARDVLCLRPVGAESCGRPVSGSLGGLSSPSPSAVPADHGAHLSLRGLPVCAFSSAGPCALRFTSARRMETTVNAHQILPKVLHKRTLGLSAMSTTDLEAYFKDCLFKDWEELGEEIRLKVFVLGGCRHKLVCVPAPCNFFTSA", "text": "FUNCTION: Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus Host mitochondrion Note=Mainly cytoplasmic as only a fraction is detected in the nucleus. In cytoplasm, a minor fraction associates with mitochondria or proteasomes. SIMILARITY: Belongs to the orthohepadnavirus protein X family."}
{"protein": "MFHNTFQSGLLSVLYSIGSKPLQIWDTQIKNGHVKRITDEEIQSLVLEIMGNNISTAFISCPVDPDKTLGIKLPFFVMVVKNMNKYFSFEVQIIDDKKIKRRFRASNYQSATRVKPFICTMPMRMDEGWNQIQFNLSDFVKRAYGTNYVETLRIQIHANCRIRRVYFADRLYTEDELPAEFKLYLPIRGQLSTQSPAFAMTSE", "text": "FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, cilium axoneme Note=Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme. SIMILARITY: Belongs to the CFAP20 family."}
{"protein": "MHGFHDVFIQILLLLAISVSVIAIAKLLKEPDSIALVLVGLVLGLTELPIIEDAERYITQSEVFQATIISLFLPILLGDATLKLPFHHLFSQKKTVLGLAFVGTFVSSICIGTAAYFLLDLPLAVAFTFAALMSATDPISVLSIFKSLGVPQKMSTVMEGESLFNDGIAVVLFKIASIYLLTYMEMGWAGLGSGVFLFLKFAIGGALVGLVLGYFFSQVIRVFDDYPLEVAFSALLFFGSYFIAEHFHTSGVIAVVVGGFVFGDYGAKIGMSKETKTNINTFWDSVTLIANALIFLMVGLEIRNIDLAGNWGVIVGAILIVLVGRTIAVYLGTGWVQELSSKERLLINWGGLRGSLSVALALSLPMDFAGRDQVLLLTFSVVLFSLIVQGLTLKPLIKKLGMI", "text": "FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Can also transport lithium. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family."}
{"protein": "MQIDEQPGNAIGAAVEGFDHATASDADIDALKSTIYTKKIAVLKGQDLSPQQFLALGKRLGRPEAYYEPMYQHPEVTEIFVSSNVPENGKQIGVPKTGKFWHADYQFMPDPFGITLIYPQVIPEKNRGTYFIDMGRAYDRLPEDLKKEISGTYCRHSVRKYFKIRPHDVYRPISEIIEEVERKTPAVVQPTTFTHPMTGETVLYISEGFTVGIEDQDGKPLDEELLKRLFDATGQLDESFEHDNIHLQSFEQGDLLVWDNRSLIHRARHTTTPEPTVSYRVTVHDERKLHDGIQAA", "text": "FUNCTION: Involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs) (PubMed:28634299). Catalyzes the conversion of (3R)-3-[(carboxymethyl)amino]fatty acids such as (3R)-3- [(carboxymethyl)amino]butanoate (CABA) to (3R)-3-isocyanylbutanoate (INBA) through an oxidative decarboxylation mechanism, thereby generating the isonitrile group of INLPs (PubMed:29906336, PubMed:32074393, PubMed:33361191). SIMILARITY: Belongs to the TfdA dioxygenase family."}
{"protein": "MQAEILLTLKLQQKLFADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTRYGQRLIQLYDLLAQIQQKAFDVLSDDDALPLNSLLAAISRFSLQTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKVAITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEATSLQQGQNVTAYFNADSVIIATLC", "text": "FUNCTION: Functions as an intracellular molybdate sensor. The ModE-Mo complex acts as a repressor of the modABC operon, which is involved in the transport of molybdate (PubMed:8550508). Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity (PubMed:9210473, PubMed:9044285). Binds the promoter of moaA activating its transcription; binding is not enhanced by molybdate (PubMed:9044285). The protein dimer binds the consensus palindrome sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3' (PubMed:9210473, PubMed:9044285, PubMed:16205910). Acts as a regulator of the expression of 67 genes, many of which encode molybdoenzymes, acts both directly and indirectly (PubMed:9466267, PubMed:10206709, PubMed:16205910). ModE also binds tungstate (PubMed:9210473, PubMed:11259434). FUNCTION: The ModE-Mo complex acts as a repressor of the modABC operon, involved in the transport of molybdate. Upon binding molybdate, the conformation of the protein changes, promoting dimerization of ModE-Mo. The protein dimer is then competent to bind a DNA region, upstream of the modABC operon. Acts also as an enhancer of the expression of genes coding for molybdoenzymes, both directly and indirectly (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ModE family."}
{"protein": "MSGEDDFYLFQNISSVGPWDGPQYHLAPVWAFRLQAAFMGFVFFVGTPLNAIVLVATLHYKKLRQPLNYILVNVSLGGFLFCIFSVFTVFIASCHGYFLFGRHVCALEAFLGSVAGLVTGWSLAFLAFERYVVICKPFGSIRFNSKHALMVVLATWIIGIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSEYYTWFLFIFCFIIPLSLICFSYSQLLRTLRAVAAQQQESATTQKAEREVSHMVVVMVGSFCLCYVPYAALAMYMVNNRNHGLDLRLVTIPAFFSKSSCVYNPIIYCFMNKQFRACILEMVCRKPMADESDVSGSQKTEVSTVSSSKVGPH", "text": "FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (PubMed:21219924, PubMed:25416279). Involved in ensuring correct abundance and localization of retinal membrane proteins (PubMed:25416279). May increase spectral sensitivity in dim light (PubMed:11055434). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Cytoplasm, perinuclear region. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MVPGPNTLFVLKNSVSSGMKGGYLAACGVFIGDAVLMFLAWAGVATLIKTTPILFNIVRYLGAFYLLYLESKILYATLKGKNNEAKSDEPQYGAIFKRALILSLTNPKAILFYVSFFVQFIDVNAPHTGISFFILATTLELVSFCYLSFLIISGAFVTQYIRTKKKLAKVGNSLIGLMFVGFAARLATLQS", "text": "FUNCTION: Exporter of leucine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Rht family."}
{"protein": "MAEEIDDNEFYRENFSADSDWEVFNAQLGEILQKWDVSSDSETRNLKSEEIFSCNWKVEREKLDMLRNGIEVEYHQAILEDEELVRAEAKEITCLQRTSCHHDLMSTGNSFGPPIRSSQELHILARIYGLRRFIVLHPVNPTLNYMRSTSEFNFFLSAVAVVSAEVQSLVPIFVQIYDPKWNYYTGVALAPALRTNFRLIGLEKAPPECRFLMGLLTLFREKVPTSYTQAAMISVCTTYALDTMRIRMPMYVPFDHGLSSEDIVVDGEVSHLEVQQFCALPHGYKPESRTEIYLVYTWPELSEHVAFDSEQRSDFVPAKAPLGKIYLSVEASSYLSCCLRDYQSVAEVTRSLESFVGRNFSGTSSGAEAASNPLDRITEHKLTKRRERSFELPSQAGLTKRLPGPMTESELSELLAYLFPDMHPEMALFPYAKKNFTDKFDPMRIKSAVPDSLVCRLSCLLATCHAHLGSVEGMAQVWAAFTRQLRLLWDNSLMVPGISAGFPDTRTCLLHQKLQMLNVCVERRVQREANSKRKSEGMVGKASSEEEEDEDDDEGEFFDCDDLTAGAGSPTKAVLSLKPEGRLRRLNNERLLEEPDEYLYIPDTQEPVPKTEDQLQDDAEVMLKLGPGSGLTTQMMCTSLLSDMEAFKAANPRGIMEDFIRWYSPKDWEEVTDELGQVKHQLSIRMTTEGNTWQKVWEQAQAVPVSRQKRLFDDTNEALKVLHYLETRKMHEIYNLTVIPLLHSAILKLADILSNAELEDLFSSQIEKLLSDLCRLSRSHSDELPSIKPLLDDLAELERRFYQFKCFERLSGYPKRSSLQQVKLQFEEILRNDNCCTIVNRRLTAAGDGTLYDILIPKLEEDMADRLISKDYIIRLDGDTKTTEKGLYLGPQFMRAIVTGEKLRLCGAFTESTAFV", "text": "FUNCTION: Catalytic subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of Rab3-GAP and Rab3GAP1, which has both GTPase- activating protein (GAP) activity towards Rab3, and guanine nucleotide exchange factor (GEF) activity towards Rab18 (Probable). As part of the Rab3GAP complex, required for the rapid induction and sustained expression of synaptic homeostasis at the neuromuscular junction (NMJ) (Probable). Also participates in the regulation of autophagy in tissues such as larval fat cells and adult muscles (Probable). The Rab3GAP complex, acts as a GAP for Rab3 by converting active Rab3-GTP to the inactive form Rab3-GDP (By similarity). At the neuromuscular junction (NMJ), forms a presynaptic signaling mechanism with Rab3 that regulates progression of synaptic homeostasis at a late stage of vesicle release (Probable). Within this mechanism Rab3-GTP acts, directly or indirectly, to inhibit the progression of synaptic homeostasis, and Rab3-GAP functions to inactivate this action of Rab3-GTP (Probable). The Rab3GAP complex, acts as a GEF for Rab18 by promoting the conversion of inactive Rab18-GDP to the active form Rab18-GTP (By similarity). Regulates autophagy as part of a Rab3GAP-Rab18 module (PubMed:32248620). Once Rab18 is activated by the GEF Rab3GAP complex, the Rab3GAP-Rab18 module localizes to autophagosomes, and regulates autolysosome formation and maturation together with the Rab18 interacting effector, the PI3K/Vps34 Complex I (PubMed:32248620). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family."}
{"protein": "MYKKVRVVLENGDVFEGVMLPPTQFSDSDIVVLKLKNGYNVGFKKGRIKEIVELGEVQTAPLSAKPMPKIEGEKVWLLATGGTILSRVDYVTGGVYPTLSVDYLFEVLGGLEAPIEAEEVTAKFSEDMTPALWGVIAERVAEAFKKGARGVVVLHGTDTMQYTAAALAFAFKSAPGPIALVGAQRSSDRPSTDAVLNLKAAIAVTARAPFAESVVVMHKTSGDTVVAVHRGTRVRKMHTSRRDTFQSINTTPIAEYYPEKELLQVLTDVYKERGGLDYTAKFEEAVALVKFYPGMHPRLLEALLEVGMKGVVIEGTGFGHVGEGVLPAVKKLIDAGVIVAMTSQTLYGRVNLYVYRRGRELLSMGVIPLEDMLPETAYAKMSWALANFKREEVPRVLTTPIAYEMSPRSDPLVFGGL", "text": "FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily."}
{"protein": "MLNNLLKKVFGSRNDRLIKQYSQNVTAINALEAKIGALSDAELRGKTEEFRQRIGEGADLDMLLPEAFAVVREAGKRVLGMRHFDVQLIGGMVLHDGKIAEMRTGEGKTLMATLPAYLNALAGKGVHLVTVNDYLAKRDAEWMGRIYRFLGISVGVILSQMDHGDKQAAYAADITYGTNNEYGFDYLRDNMVTHPLERVQRVLNFAIVDEVDSILIDEARTPLIISGQAEGNTDVYVRMNALIPKLVRQENEDSPGDFSVDEKAQQVLLSEAGFEHAEKLLVQSGLLPSGTSLYDPANINLVHHLYAGLRAHALFHRDQHYVIQNGEVVIVDEFTGRLMAGRRWSEGLHQAVEAKEGVTIQKENQTLASITFQNYFRMYEKLAGMTGTADTEAYEFQQIYGLETVIIPTHRPMIRVDRMDQVFRTMDEKYQAIIADIKDCQERGQPVLVGTTSIENNELLSSLLTREKLPHQVLNAKQHAREAEIVAQAGRPKMITIATNMAGRGTDIVLGGNPEPEFERIRSDESLSESEKTERIAELQQQWQTLHDEVLEKGGLHIIGTERHESRRVDNQLRGRSGRQGDPGSSRFYLSLEDALLRIFASDRVASIMQRLNMPQGEAIEHPWVTRAIENAQRKVEARNFDIRKQLLEYDDVANDQRKVIYQQRNELLESEDITETTTAMRADMLRNLIALHVPPQSVEEEWDISGLEKALAAEYHLTLPLREWLEKEPDLHEDSLHQRIIEAANALYSGKVEQVGAPIMHQYERAVMLQSLDMHWREHLASLDHLRQGIHLRGYAQKNPKQEYKREAFELFTSMLEEIKAEVSKTLMAVQIRSEQQVEAVAETHHAPVNVQYHHAAFEEALGEEKSPESIGEDIEGREHPQKHQPFVRQGEKIGRNDPCPCGSGKKYKQCHGKLN", "text": "FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Note=Distribution is 50- 50. SIMILARITY: Belongs to the SecA family."}
{"protein": "MLKGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKVIRADGIQIATLLEAITPLFEYDQYVERPLAMMQAVHGDSLDLAVEERYLAAIAKINGKAPLVERVERFAFYDRAKIAYAVVITGELAKYGNIILKKGVTPVLTD", "text": "FUNCTION: Involved in the anomeric conversion of L-fucose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase subfamily."}
{"protein": "MGNGDWSSKWPNDHLFIDDFGKLVWFDVLTDIVKISHFVSQVPTDLSPIPSSYISFIDGRIPMCINHLGWVYIRVKFESEEVFYQKFGEVDVSRFGESELPPDFEVTFSKVTTLVNKSLVRKSELLEKMNNELKQELTNKLDSLEKVNVQLKKELSQAQQSNFTELRDGLILNFSKVGGRIHRMVVRSIQNQLKLVSEINNDGDRWATMGATVILKEGAQYLGFVVVKNDGKIGVKFDLTRLNSLDNQTLLASVV", "text": "FUNCTION: May function by interacting with a small, flexible domain located at the C-terminus of the CP, forming a bridge between the virus particle and the internal surface of the vector nematode feeding apparatus. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the tobravirus protein 2b family."}
{"protein": "MPLPLYLLAVAVCAMGTSEFMLAGLVPDIASDLGVTVGTAGTLTSAFATGMIVGAPLVAALARTWPRRSSLLGFILAFAAAHAVGAGTTSFPVLVACRVVAALANAGFLAVALTTAAALVPADKQGRALAVLLSGTTVATVAGVPGGSLLGTWLGWRATFWAVAVCCLPAAFGVLKAIPAGRATAAATGGPPLRVELAALKTPRLLLAMLLGALVNAATFASFTFLAPVVTDTAGLGDLWISVALVLFGAGSFAGVTVAGRLSDRRPAQVLAVAGPLLLVGWPALAMLADRPVALLTLVFVQGALSFALGSTLITRVLYEAAGAPTMAGSYATAALNVGAAAGPLVAATTLGHTTGNLGPLWASGLLVAVALLVAFPFRTVITTAAPADATR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MARFNLATLLVTLFLAVCTFSFVSAEGRGPVITDKIYFDIKQGDESLGRIVLGLYGKTVPKTAENFKQLATGENGYGYKGSTFHRVIKKFMIQGGDFTNHDGTGGKSIYGNRFADENFKLRHSTPGLLSMANAGRDTNGSQFFITTVVTPWLDGKHVVFGRVLEGMDVVTKIENTPTGSRSKPSVDVVIADCGLLPDEPAKEAAEHAEL", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B subfamily."}
{"protein": "MLTDMDISSRASLKNITEIGADLGLLPEEMMLFGHTKAKVELSVLQRLAGQRKGKLIIVTAVTPTPHGEGKTVTSIGLTQSLNAIGQKACACIRQPSMGPVFGVKGGAAGGGYAQVVPMQEMNLHLTGDIHAVSSAHNLGAAAIAARLFHETRLGKTEFEAQSEQAFLDIDPNEIRWHRVVDHNDRCLRQIHVGLGDNNGPEYESSFDITAASELMAILALSHDLADMRARIGRLVLALNTQGQVITAEDLGVAGAMTAIMADAIKPTLMQTLNGSPCLIHSGPFANIAHGNSSIIADDIALRLADFVVTEGGFGSDMGFEKFCNIKVRQSGQAPAAAVLVTTLKALKANSGLATEVDSNVSNIHVPNISATNINAPDQARLEAGFANLNWHINNVARYGIPVVVAINRFATDSDAELQWLIEAVNASAAFGCEISDAFIQGEAGAIALAQTVVRAAETESQFKLLYPDEASLEAKLSTLAEVGYGATGVSLSIEAKQQAQQLTALGYGHLPLCMAKTPLSISHDPSLKGVPKDFVVPVRELVLHAGAGFITALVGNVMTMPGLGLKPGYLKIDIDAKGEIVGLG", "text": "SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family."}
{"protein": "MKICIFIFFYIFSSIFYVLAKNNQVDNITAIVNDEIILNSDVNEILVFLKKSKKKFIIPLKSDFLKEKVLEKLIVDSLILQEANSKNINITKEQIDTVIKNIALKKHISVDHFKKQILLRNIKNPSYYDNFIKKIEILLKMKTIQDYELHKRINISEQEVNTIFKKLIKDNEKFKKINLSYILLPSLKQDSDNAVRNRTKIAENIVYKLKKGYDFEKLLIECEKNKSTFIVKKMFWKPLLDIQNSFFKTLNIFKKGQILGPIVGDKGLYILKVNDIHHKKENIVTEFYMQHCLIKPSVILTNTEAKKKIFNIYENIKKGIYTFDDAVKNLSDDYYSSNKKGDLGWISKESLGFDLNKKFLILDKNEISEPVKSNWGWHIFKILDRRQVDAFYKLKKNQAFNIVLNQKIISEKNHWIEDLKNTAYIEIIRS", "text": "FUNCTION: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation (By similarity). SUBCELLULAR LOCATION: Periplasm Note=Is capable of associating with the outer membrane."}
{"protein": "MTLQTFTSTDFEVFTVDGLEERMSAIKTNIHPKLEALGEQFAEYLSQQTDESFFYHVAKHARRKVNPPNDTWVAFSTNKRGYKMLPHFQIGLWGTHAFIYFGLIYECPQKVETAHAFLEHLNDLKTNIPNDFVWSIDHTKPGVKLHKTLETEDLQKMIERLATVKKAELLVGIHISPEEFSAMTNEQFLAKIESTMQPLLPLYALCNR", "text": "SIMILARITY: Belongs to the UPF0637 family."}
{"protein": "MAMQAHYEAEATEEEHFGPQAISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELLNIKGISEAKAEKILAEAAKLVPMGFTTATEFHQRRSEIIQISTGSKELDKLLQGGVETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMAESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD", "text": "FUNCTION: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Also involved in interstrand cross-link repair. SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome Note=Accumulated at sites of DNA damage. Recruited to stalled replication forks during replication stress. SIMILARITY: Belongs to the RecA family. RAD51 subfamily."}
{"protein": "MARFPTSPAPNRLLRLFSSNKRSSSPTAALLTGDFQLIRHFSAGTAARVAKDEKEPWWKESMDKLRNIGISAHIDSGKTTLTERVLFYTGRIHEIHEVRGRDGVGAKMDSMDLEREKGITIQSAATYCTWKDYKVNIIDTPGHVDFTIEVERALRVLDGAILVLCSVGGVQSQSITVDRQMRRYEVPRVAFINKLDRMGADPWKVLNQARAKLRHHSAAVQVPIGLEENFQGLIDLIHVKAYFFHGSSGENVVAGDIPADMEGLVAEKRRELIETVSEVDDVLAEKFLNDEPVSASELEEAIRRATIAQTFVPVFMGSAFKNKGVQPLLDGVVSFLPSPNEVNNYALDQNNNEERVTLTGSPDGPLVALAFKLEEGRFGQLTYLRVYEGVIKKGDFIINVNTGKRIKVPRLVRMHSNDMEDIQEAHAGQIVAVFGIECASGDTFTDGSVKYTMTSMNVPEPVMSLAVQPVSKDSGGQFSKALNRFQKEDPTFRVGLDPESGQTIISGMGELHLDIYVERMRREYKVDATVGKPRVNFRETITQRAEFDYLHKKQSGGAGQYGRVTGYVEPLPPGSKEKFEFENMIVGQAIPSGFIPAIEKGFKEAANSGSLIGHPVENLRIVLTDGASHAVDSSELAFKMAAIYAFRLCYTAARPVILEPVMLVELKVPTEFQGTVAGDINKRKGIIVGNDQEGDDSVITANVPLNNMFGYSTSLRSMTQGKGEFTMEYKEHSAVSNEVQAQLVNAYSASKATE", "text": "FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MKTILLFALSLLLSLSVSDVCAQERVYDISQFGLKANSKKNASPVVRKAIAKIKAECRDGEKVILRFPAGRYNFHEAGSTVREYYISNHDQDNPKKVGIALEDMKNLTIDGQGSEFVFYGRMIPVSLLRSENCVLKNFSIDFEQPHIAQVQVVENDPEKGITFEPAPWVDYRISKDSVFEGLGEGWVMRYSWGIAFDGKTKHVVYNTSDIGCPTKGAFEVAPRRICSPKWKDARLVPGTVVAMRGWGRPTPGIFMSHDVNTSLLDVKVHYAEGMGLLAQLCEDITLDGFGVCLKGDNDPRYFTTQADATHFSGCKGKIVSKNGLYEGMMDDAINVHGTYLKVIKRVDDHTLIGRYMHDQSWGFEWGRPGDDVQFVRSETMELIGKQNQITAIRPYDKGEIRGAREFSITFKEAIDPAINEKSGFGIENLTWTPEVLFAGNTIRNNRARGTLFSTPKKTVVEDNLFDHTSGTAILLCGDCNGWFETGACRDVTIRRNRFINALTNMFQFTNAVISIYPEIPNLKDQQKYFHGGKDGGIVIEDNEFDTFDAPILYAKSVDGLIFRNNVIKTNTEFKPFHWNKDRFLLERVTNVKISE", "text": "FUNCTION: Alpha-galactosidase. Removes both branched alpha-1,3-linked galactose residues of blood group B antigens and linear alpha-1,3- linked galactose structures. SIMILARITY: Belongs to the glycosyl hydrolase 110 family. B subfamily."}
{"protein": "MLHVNKCQLCETRRPSICESCLKKQLYDFYHKRDEFSRDIESELEKVAKLKSESFSLKGKITQKEELTYRLQNLAASLNEKKSLSCDLHSRKQLIEDDLSNRKKSINIASQKLAGLSHSTSDYFSKEYLTAYRRSELLQNKLHEYQKKLITRVLDMYQLHWQRDLVLNTQGCTQKSAQMGSEFNPDSIDSSLAYRLSKLSMGNSKSDLSHSDNETGHFYSNFFSQVMELNASVTISGIPVCIRSKEKMFLNPDCALTLSFICIFLAQYTSIPLPCPLQLPSPDQKPMTSFSSEQMLYIMYNIVWISWNCGIFSFPRGITQSQLFELMQYTGFWLVQLRTKPLTSQKPDWHYKMGMDFDLFHRLYLARLPIPINYSSLRSRSSSKPYQLIS", "text": "FUNCTION: Required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific vps34 PI3-kinase complex I. This complex is essential to recruit the atg8-phosphatidylinositol conjugate and the atg12-atg5 conjugate to the preautophagosomal structure. Atg14 mediates the specific binding of the vps34 PI3-kinase complex I to the preautophagosomal structure (PAS) (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG14 family."}
{"protein": "MSLCQFVSSISDCRITQALIYGVLFVGVYKITTFTLSVGSLLVDLFVLPAVDFKKYGAKQGKWAVVTGASDGIGKEYAYQLASRGLNVVLISRTLSKLELIATEIETKYKVSTEVIAFDASTDNDANYAKILHTVSNLPVTVLVNNVGQSHSIPVPFLETEDKELRDIITINNTVTLKITQAVAPVIADTVAKENKKVKGLILTMGSFGGLLPTPYLATYSGSKSFLQAWSSALAGELKPQGIDVQLVISYLVTSAMSKIRRSSASIPNPKNFVTSVLNTAGRRCGAQERFATTTPYWTHALMHFGIENTVGVYSKFANSLNFSMHKSIRVRALKKAARANATKTD", "text": "FUNCTION: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MADVDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNASRPVTPPRGIITKQAKK", "text": "FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (By similarity). Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cleavage furrow Nucleus, nucleolus Nucleus, nucleoplasm Chromosome, centromere, kinetochore Nucleus speckle Midbody Mitochondrion. SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily."}
{"protein": "MRLFLLLITFIALFGAINAFSGVDISQGSSVGDFQCMLNQGFEFAIIRGYMETGQVDPEVVNSIACAREAGVEYVDTYLFPCFNCGNPQDQGPALVNYLSGYNANYGMVWLDIESSDWSGDQSANVAFFEGLISGLQSVGAHIGVYTSASQWIPIMGGYTGGSEFPLWYANWDGVQSFDDFSAFGGWSTPAIKQYNDGGSNCGVGYDFNWYPN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 25 family."}
{"protein": "MEIYSPVVPAVKDVKRLDEIRKSAKFHPSIWGDFFLSYNSDNTQISEAEEEEVAKQKEAVRELLAQVPEGSTYKMELIDLIQRLGVNYHFEKEIHDSLNYIHENSQHNDDEVRTTALRFRLLRQQGYRVPCDVFRKFTDGEGNFATALTNDVEGLLELYEASHLATRGEEILDRAMEFSSSHLQALLNQHLVGSVSLSKRVDEALKMPIRKTLTRLGARKFISLYQEDESRNELLLNFAKLDFNMVQKMHQRELSDATRWWKKLEVAKRMPYARDRVVECFFWIVGVYFEPCYATARRILSKAINMASIVDDTYEYATLDELQILTDAIQRWDVNETLEDSPPHVQMCYKALIQAYAEIEDEVVENFGGEELYRVQYAIEHVKQSAVAFFEEAKWIYNNSIPTVEEYMKVAFVTCGYMMLSTTSLVGVGSDRVSKADFDWIVNEPLIVRASCVICRLMDDLVGDEYEEKPSSVLCYMKQYVVSKDEARARLEQQVKDAWKDMNEECIEPRPASMQILTRVLNLGRVIHLLYREGDSYTDPNRSKEWVKMVFVDPI", "text": "FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)- farnesyl diphosphate (FPP) to alloaromadendrene and bicyclo-germacrene. The product formation is dependent on the metal ions present and in presence of manganese, bicyclo-germacrene is greatly favored while both alloaromadendrene and bicyclo-germacrene are produced in equivalent amounts in the presence of magnesium. Can also convert geranyl diphosphate (GPP) to terpinolene, limonene and geraniol, and this conversion is not affected by the presence of magnesium or manganese. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MTPDEFLSALTEFDIQLSDKQIKQFERYFELLVEWNEKINLTAITEKNEVYLKHFYDSIAPILYGLITDQPVSILDIGAGAGFPSLPMKIIFPELKVTIIDSLNKRINFLSLLTEELGLENVTLLHGRAEDFGQDANYRGTFDFVTARAVARLSVLTEFTIPFLKKNGILLSLKAAQFEEELNDAKKAIATLGGKFIKEVAYELPNGDERHIALIEKKKETPKKYPRKAGTPAKNPIK", "text": "FUNCTION: Specifically methylates the N7 position of a guanine in 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family."}
{"protein": "MSAIGSLIFCSECGNLLESTTAQWTTCDQCQSVYPSEQFANLVVETKSSASAFPSALKLKHSIVQVESQKEEAATIEEKCPKCGNDHMTFHTLQLRSADEGSTVFYECPRCAYKFSTNN", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Required for growth at higher temperatures. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family."}
{"protein": "MAIENCLQLSTSASVGTVAVKSHVHHLQPSSKVNVPTFRGLKRSFPALSSSVSSSSPRQFRYSSVVCKASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP", "text": "FUNCTION: Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily."}
{"protein": "MTIDRTFPIFTVRWLAVHGLAVPTVSFLGSISAMQFIQR", "text": "FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbE/PsbF family."}
{"protein": "MIHTLLRWVFQRLYRIRIEGDSSQFQQSKLLITPNHVSFLDGILLALFLPIKPVFAVYSSISDRWFMRWLKPYIDFVPLDPTKPLAIKGLIKVIERGQPVVVFPEGRISVTGSLMKIYSGAAFVAAKSGATIIPVRIDGAEFTPFGRLAGVFKRRCFPQITITYLPPTTLPMPEADSARTRRALAGEHLHQIMMKARMETRPQHTLYEAFLAARTRYGRRSPSIADISFNEDSYQGLLKKSLGVSRILQRFTRADEHVGMLLPNATITAASILGASLRNRIPAMLNYTAGAKGLQSAMKAAGIKTIVTSRQFLEKGKLTDLPKQVSEANWVYLEDLKDTVTLADKLWILFHLLFPARAMLPQKPDDAAIVLFTSGSEGNPKGVVHSHDSLLANVEQIRTVADFTPRDRFMSALPLFHAFGLTVGLLTPLMTGARIFLYPSPLHYRIVPELVYDQNCTVLFGTSTFLGNYARFAHPYDFARLRYVVAGAEKLSETTRQVWQDKFGIRILEGYGVTECAPVVAINVPMATKIHSVGLLLPEIESRLITVPGITRGGRLQLRGPNIMKGYLRVENPGVLEAPAAENAEGELQQGWYDTGDIVELDEKGFCTIIGRVKRFAKLAGEMVSLESVEQLAVKVSPEAQHAASAKSDSSKGEALVLFTTDSQITRDVLLAQARSSGVPELAVPRDIRYVKALPLLGSGKPDFVTLRHMAEEPVTNASEQSA", "text": "FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. SIMILARITY: In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MDGEEHQIDGDEVNNHENKLNEKKKSWGKLYRPDSFIIEAGQTPTNTGRRSLMSWRTTMSLAFQSLGVVYGDIGTSPLYVYASTFTDGINDKDDVVGVLSLIIYTITLVALLKYVFIVLQANDNGEGGTFALYSLICRYAKMGLIPNQEPEDVELSNYTLELPTTQLRRAHMIKEKLENSKFAKIILFLVTIMGTSMVIGDGILTPSISVLSAVSGIKSLGQNTVVGVSVAILIVLFAFQRFGTDKVGFSFAPIILVWFTFLIGIGLFNLFKHDITVLKALNPLYIIYYFRRTGRQGWISLGGVFLCITGTEAMFADLGHFSVRAVQISFSCVAYPALVTIYCGQAAYLTKHTYNVSNTFYDSIPDPLYWPTFVVAVAASIIASQAMISGAFSVISQSLRMGCFPRVKVVHTSAKYEGQVYIPEINYLLMLACIAVTLAFRTTEKIGHAYGIAVVTVMVITTLMVTLIMLVIWKTNIVWIAIFLVVFGSIEMLYLSSVMYKFTSGGYLPLTITVVLMAMMAIWQYVHVLKYRYELREKISRENAIQMATSPDVNRVPGIGLFYTELVNGITPLFSHYISNLSSVHSVFVLISIKTLPVNRVTSSERFFFRYVGPKDSGMFRCVVRYGYKEDIEEPDEFERHFVYYLKEFIHHEHFMSGGGGEVDETDKEEEPNAETTVVPSSNYVPSSGRIGSAHSSSSDKIRSGRVVQVQSVEDQTELVEKAREKGMVYLMGETEITAEKESSLFKKFIVNHAYNFLKKNCREGDKALAIPRSKLLKVGMTYEL", "text": "FUNCTION: High-affinity potassium transporter. Can also transport rubidium and cesium (Ref.1). Is essential with AKT1 for high-affinity potassium uptake in roots during seedling establishment and postgermination growth under low potassium conditions (PubMed:20413648). Mediates potassium uptake by plant roots in response to low potassium conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by the calcium sensors calcineurin B-like genes CBL1, CBL8, CBL9 and CBL10, and by phosphorylation by CIPK23 (PubMed:26474642). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72.3) family."}
{"protein": "MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF", "text": "FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine (PubMed:34748729). Activity towards 2-iodophenol is weak (PubMed:34748729). SIMILARITY: Belongs to the nitroreductase family."}
{"protein": "MLEQNKFKTKKQQQAWNKTLAGRYYNAMVKRPFLFFGLPFLTTIYAASVYFAEFTAYRYEIQDGKVKALSEEEALKLDKGRRKVDMKEEFYRLQQLGKQDDWEQVRVPRMKGESDNVF", "text": "FUNCTION: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the COX16 family."}
{"protein": "MEPSATPGAQMGVPPGSREPSPVPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFVVALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGHALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAIMVPQAAVMECSSVLPELANRTRLFSVCDERWADDLYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSDQLGDLEQGLSGEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVLKRVFGMFRQASDREAVYACFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSCCLPGLGPCGSLKAPSPRSSASHKSLSLQSRCSISKISEHVVLTSVTTVLP", "text": "FUNCTION: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide (PubMed:9491897, PubMed:26950369). Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding (PubMed:9491897, PubMed:26950369). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRLSVRKVLLAAGCALALVLAVQLGQQVLECRAVLGGTRNPRRMRPEQEELVMLGADHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWTKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLARLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGRDKCLPVYYEQLVLHPRRSLKRILDFLGIAWSDTVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPRDVVRDMAQIAPMLARLGYDPYANPPNYGNPDPIVINNTHRVLKGDYKTPANLKGYFQVNQNSTSPHLGSS", "text": "FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the protein sulfotransferase family."}
{"protein": "MITLNTEEKIFIYSWLKNILSHELTEQQLQQYQQGVFTPLFDFLSEQDLAKQINTVRNSLMQLSNLPLAHLELAADFAQLFLLNGENSALPYASAYLSEKELNQHIAFIDHLLFKYQLKFDHNLREPSDHLAVYLELLITLEKSGQKEKSFNFIQHYLLAWLIPFNKKVQKIKTETSFYQAITEILITLLNKNVKLS", "text": "FUNCTION: Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily."}
{"protein": "MTRRRSTSGTSSRSSTDSGLSVDTAYLEDNKHNNFANGTSGLTDETKYRDVEDAEADVDEPFLPTSSKKLGSGSRTRQIFWALVILCLGGWVLALVLFLTHGRASSQTASETLQQQESDSGSTSAGRPVTLQQVLTGSWNPRAHAISWIAGPDGEDGLLVQRAEVDKEGYMRVDDIRSQEGDDVDSQSGRILIDKAAVRVNGETLMPTFTWPSPDLNKVLLMSNHEKNWRYSFTGRYWIFDVATQTAQPLDPSVPDGRVQLALWSPSSDAVVFVRDNNMYLRKLSSESVVSITKDGGEDLFYGIPDWVYEEEVITDKSVTWWSNDGKYVAFLRTNESAVPEFPVQYFVSRPSGKRPPPGLENYPEVRQIKYPKAGSPNPVVNLLFYDVEKDEVFPVDVPDDFPDDDRIIIEVLWASEGKVIVRATNRESDRVKVFLIDTKSRTGKLVRFEDIANLDGGWVEPSHYTKFIPADPSNGRPDDGYIDTVIHDGYDHLAYFTPLDNPDPIMLTTGEWEVVEAPSAVDLRRGIVYFVATKESPTQRHVYRVHLDGSNLQALTDTSKPGFYDVSFSDGAGYALLSYNGPSVPWQAIINTGGDEITFEKTIEKNPRLASMVETYALPTEIYQNVTIDGFTLQLVERRPPHFNPAKKYPVVFQLYNGPTSQRVDRKFTIDFQSYIASNLGYIVVTLDARGTGYSGRKVRCAVRGNLGHYEAHDQITTAKMWAKKPYVDETRMAIWGWSYGGFMTLKVLEQDAGETFQYGMAVAPVTDWRFYDSVYTERYMHTPEHNPSGYENSTITNVSALSKATRFLLIHGASDDNVHIQNTLTFVDKLDLLNVQNYDMHFYPDSDHNIYFHNAHFMIYERLSNWLINAFNGEWHQIANPVPEDSIWDSVKRSVPAFAH", "text": "FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. SUBCELLULAR LOCATION: Vacuole membrane; Single-pass type II membrane protein Note=Lysosome-like vacuoles. SIMILARITY: Belongs to the peptidase S9B family."}
{"protein": "METKSDYEDAVFYFVDDDEICSRDSIIDLIDEYITWRNHVIVFNKDITSCGRLYKELIKFDDVAIRYYGIDKINEIVEAMSEGDHYINLTEVHDQESLFATIGICAKITEHWGYKKISESKFQSLGNITDLMTDDNINILILFLEKKMN", "text": "FUNCTION: Virulence factor that affects the acute immune response to infection. Bcl-2-like protein which, through its interaction with the DEAD box RNA helicase DDX3X/DDX3, prevents TBK1/IKKepsilon-mediated IRF3 activation. Contributes to virulence by binding to the host TRAF6 and IRAK2 and preventing host NF-kappa-B activation. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the orthopoxvirus OPG044 family."}
{"protein": "MATPQSVFVFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDAHRRKEYDTVGHTAFTNGKGQRGSGSPFEQSFNFNFDDLFKDFNLFGQNQNTRSKKHFENHFQTHQDGSNRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDTTNRHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ", "text": "FUNCTION: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:29198525). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (PubMed:29198525). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (PubMed:29198525). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins (By similarity). Required for survival of B-cell progenitors and normal antibody production (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "MSLYSNIRTFSTRSIVLNRIKPLKFEDLTKIKLREPVVPRVANFEVSPDHPLWQFFPQGNKTKVAIRESEELDLDSREWSSAELRQKSFEDLHKIWYLTLKERNILSREVRLGESLGMGDFRQFNNVDRKLIKTQKRIKQVLLERQVAVERAQATMQDDIQKYLDDFKTRYVNCEADEVEDYHEKLVRLQYAIFGINPNLSLELLQDEETIDVNFVKGLSYIANLKVERHLKLNPQTEFELPLNGPVEELPFFLNDVEVAISQVKQLRDSGKSRMLHKIEVIPFLKQAIESHMQQEENIGGYEEEQNKN", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "AYSWDNRVKYVVRYMYDIDNNGFLDKNDFECLALRNTLIEGRGEFNEAAYANNQKIMSNLWNEIAELADFNKDGEVTIDEFKKAVQNVCVGKAFATFPAAFKVFIANQFKTVDVNGDGLVGVDEYRLDCISRSAFANIKEIDDAYNKLATDADKKAGGISLARYQELYAQFISNPDESANAVYLFGPLKEVQ", "text": "FUNCTION: Like parvalbumins, SCPs seem to be more abundant in fast contracting muscles, but no functional relationship can be established from this distribution."}
{"protein": "MDIVAHIQGDPGSSLTPLILIHAISGLALPYFALRPLSTDSDDGDSDKSRPVYGLSSPIFESVSAFRRHGKSLPSLALEYVRIIRREIQPRGPYLLGGWSMGGMLAIEMAAIFVAQGETVKHVVMIDSLNPEVYPPFQDSQEHQVLSTIMYNAIAWRVEGLEEACMPTLSDDASTTTSSDNSRASTDHGADSEVESEADLDDFMQQLREHVHQGMRMLASYHTLHRHIYLPDTAVTLIKCTMLGNLSPLLRASRKVFAKKNLLDPHNGWRTEQFRSFRSVPFASTHDACFDAEASEELTTILRGVLKDID", "text": "FUNCTION: Thioesterase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA (PubMed:32077283). The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA (PubMed:32077283). A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively (PubMed:32077283). The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo- methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AMT4 thioesterase family."}
{"protein": "MTQQQDELDQIKSQIQEHLISSGNYDIINKQLKLQLYESGWFDKVTQLANRELQENSAHDTAVSFDQLFSFVKPKAEEMVPSNIKEDVLERLKDYLDDVIQ", "text": "FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export- competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. May also be involved in cytoplasmic mRNA decay by interaction with components of P-bodies (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Cytoplasm, P-body. SIMILARITY: Belongs to the ENY2 family."}
{"protein": "MEWIRKYHIAIAWMIATSAMLISLFFSEWMKLPPCDLCWYQRMAMYPLVLILGIGMYRKDPRVSMYAFPFTCIGLILSVYQITIQAFPINEMKICSVGVSCTEDYLNLFGFISIPMLSFIGFLVIIILIYIESDRETKE", "text": "FUNCTION: Required for disulfide bond formation in some proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. BdbC subfamily."}
{"protein": "MNTSISSQPPCIRIFDTTLRDGEQSPGCSMPAQQKLVMARALDALGVDIIETGFPASSQSDYEAMTLIARELRRPTLAVLSRCLQADIETSARALESATKPRLHVFLSTSPLHREHKLRMSKEQVLESVHKHVSLSRTLIDDVEFSAEDATRTEEDFLIEVTRVAIAAGATTINLPDTVGFSTPEEIRNMFTRVIANVEGANKVIFSAHCHDDLGLAVANSLAAIEGGARQIECTINGIGERAGNCALEELTMVLKVRNAFYNIDTSIHTSRIVSTSQLLQRLVGMPVQRNKAVVGANAFAHESGIHQHGMLRHRGTYEIMRPQEVGWVCSHMVLGRHSGRAAVEQRLRALGYLLEEEDLKLVFEEFKQLCEKQRLVTDVDLQVLMQDTTVQHGYRLASMTISDVGNRANALVELSDPQGQRVAETAQGNGPVDALFGALAAATGVKLELDSYQVHSVGIGADARGEANLSVRHNDTQYEGTGTSKDIIEASALAWLEVANRLLRNPENMQNKQNTALA", "text": "FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily."}
{"protein": "MDHKSRMLLDTIFKDMLNTKDVYALIKYIFKKDPVETIFSKKDDDIFIDFVYNDNVLASDYLGMKTTKVEDCCSCRKVVAVEYMNTSIIDNDLEGYIKQSDKLKRFIKLYNKNNAIKKARNIKSRQKMLKDAGIDDIGYEFIKDAIGLISRK", "text": "FUNCTION: Contributes to the formation of crescents and immature virions (IV). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Note=Probably transitorily part of the membrane of crescents during immature virions formation. Not incorporated into virions. Probably synthesized, but not retained in viral factories (By similarity). SIMILARITY: Belongs to the chordopoxvirinae H7 family."}
{"protein": "MDLLAASVESTLKNLQDKRNFLSEQREHYIDIRSRLVRFINDNDDGEEEGEGQGMVFGDIIISTSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNLNHMEDGNGIEEDEANNDEDFLPSMEIREELDDEGNVISSSVTPTTKQPSQSNSKKEQTPAVGPKEKGLAKEKKSKSFEENLKGKLLKRNDEVKKKVQPSKVDTENVYTFADLVQQMDQQDELEDGYIETDEINYDYDAFENSNFKVNDNYEEDDEDEDEEEYLNHSIIPGFEAQSSFLQQIQRLRAQKQSQDHEREEGDVNKSLKPILKKSSFAENSDKKQKKKQVGFASSLEIHEVENLKEENKRQMQSFAVPMYETQESTGIANKMTSDEFDGDLFAKMLGVQEADEVHEKYKEELINQERLEGEASRSNRRTRVSRFRKDRASKKENTLSTFKQETTRSVENEVVEKEPVVGDIIEKEPVVGDVIEKEPVVGDVIEKEPAVTDIVEREPAVNDIVERKPVVGDIIEKEPTINDIVEKEPEINSKSEFETPFKKKKLKSLQKPRSSKSMKKKFDPKILENISDDDYDDDDDGNKKLLSNKSKNNTDEQDKFPSKIQEVSRSMAKTGATVGSEPVRITNVDYHALGGNLDDMVKAYSLGLYDDDLEEDPGTIVEKLEDFKEYNKQVELLRDEIRDFQLENKPVTMEEEENDGNVMNDIIEHEFPESYTNDEDEVALHPGRLQEEVAIEYRRLKEATASKWQSSSPAAHTEGELEPIDKFGNPVKTSRFRSQRLHMDSKP", "text": "FUNCTION: Involved in gene expression controlled by TOR kinase and nutrient signaling. May also be involved in positioning the proximal bud pole signal. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin subunit alpha family."}
{"protein": "MDEIVNIVRDSMWFIPNVFMDNGENDGHVSVNNVCHMYFAFFDVDTSSHLFKLVIKHCDLNKQLKCGMSPLHCYVMNTRFKPSVLKILLHNGVNNFDNKDNKGHIPLHHYLIYSLSIDNKVFDILTDPIDDFSKSSDLLLCYLRYKFNGRLNYYVLYKLLTKGSDPNCVDEDGLTSLHYYCKHISAFHESNYYKSKSYTKMRAEKRFIYTIINHGANINAVTKIGNTPLHTYLQQYTKHSPRVVYALLSRGADTRIRNNFDCTPIMEYIKNDCVTGHILIMLLNWHEQKYGKLQKEEGHHLLYLFIKHNQGYGSHAFNILRYLLDRFDIQKDEYYNTMTPLHTAFQNCNNNVASYLVYIGYDINLPTKDDKTVFDLVFENRNILFNAGVIHNIIHHRLKVSLPMIKSLFYKMLEFSPYDDYYVKKIIAYCILRDESFTELHSKFCLNEDYKSVFMKNISFDKIDSIIKKCNWDISRLKDIQISDTNLYTVLRTEDIRYRTYLKAIHLDSHISFPMYDDLIEQCHLSMERKSKLVDKVLNKLKSTIDGQSRLSYLPPEIIRNIITKLSDYHLNSMLYGKNHYKYYT", "text": "FUNCTION: May be involved in virus-host protein interaction through the ankyrin repeats and PRANC regions. SIMILARITY: Belongs to the orthopoxvirus OPG003 family."}
{"protein": "MKITGISGSPRKGQNCEKIIGAALEVAKERGFETDTVFISNEEVAPCKACGACRDQDFCVIDDDMDEIYEKMRAADGIIVAAPVYMGNYPAQLKALFDRSVLLRRKNFALKNKVGAALSVGGSRNGGQEKTIQSIHDWMHIHGMIVVGDNSHFGGITWNPAEEDTVGMQTVSETAKKLCDVLELIQKNRDK", "text": "FUNCTION: Redox-active protein probably involved in electron transport during fermentation of acetate to methane. SIMILARITY: Belongs to the SsuE family. Isf subfamily."}
{"protein": "MITGIQITKAANDDLLNSFWLLDSEKGEARCIVAKSGFAEDEVVAVSKLGEIEYREIPMEVKPEVRVEGGQHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSLTPEQQRDVIARTFTESL", "text": "FUNCTION: Acts as a radical domain for damaged PFL and possibly other radical proteins."}
{"protein": "MEATIKVVLLGDSSVGKTSIVTRLKSGKFLAKHAATIGAAFITKTIEVPSNDSSTEKRIHMEIWDTAGQERYKSLVPMYYRDANIALIVFELGDVSSLQCAKTWFQDLQDRAQGTQVIIVGNKYDLVCEEHSGEVTIPAELQGLPYVAVSAKTGYNFDTLNKIIISLVPESQFKTLSKNNEQGNILEINKKKSGSGCIC", "text": "FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). Specifically binds guanine nucleotides. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MVASRAIGSLSRFSAFRILRSRGCICHSFTTSSALLSRTHINYGVKGDVAVIRINSPNSKVNTLNKEVQSEFVEVMNEIWANDQIRSAVLISSKPGCFVAGADINMLASCTTPQEAARISQEGQKMFEKLEKSPKPVVAAISGSCLGGGLELAIACQYRIATKDRKTVLGVPEVLLGILPGAGGTQRLPKMVGVPAAFDMMLTGRNIRADRAKKMGLVDQLVDPLGPGIKSPEERTIEYLEEVAVNFAKGLADRKVSAKQSKGLMEKLTSYAMTIPFVRQQVYKTVEEKVKKQTKGLYPAPLKIIDAVKTGLEQGNDAGYLAESEKFGELALTKESKALMGLYNGQVLCKKNKFGAPQKTVQQLAILGAGLMGAGIAQVSVDKGLKTLLKDTTVTGLGRGQQQVFKGLNDKVKKKALTSFERDSIFSNLIGQLDYKGFEKADMVIEAVFEDLAVKHKVLKEVESVTPEHCIFASNTSALPINQIAAVSQRPEKVIGMHYFSPVDKMQLLEIITTDKTSKDTTASAVAVGLKQGKVIIVVKDGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDALTTGFGFPVGAATLADEVGIDVAQHVAEDLGKAFGERFGGGSVELLKLMVSKGFLGRKSGKGFYIYQSGSKNKNLNSEIDNILVNLRLPAKPEVSSDEDIQYRVITRFVNEAVLCLQEGILATPEEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKVVDRLRKYESAYGTQFTPCQLLRDLANNSSKKFYQ", "text": "FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA described here carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the trifunctional enzyme subunit beta/HADHB bears the 3-ketoacyl-CoA thiolase activity. Independently of the subunit beta, the trifunctional enzyme subunit alpha/HADHA also has a monolysocardiolipin acyltransferase activity. It acylates monolysocardiolipin into cardiolipin, a major mitochondrial membrane phospholipid which plays a key role in apoptosis and supports mitochondrial respiratory chain complexes in the generation of ATP. Allows the acylation of monolysocardiolipin with different acyl-CoA substrates including oleoyl-CoA for which it displays the highest activity. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane Note=Protein stability and association with mitochondrion inner membrane do not require HADHB. SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family."}
{"protein": "MNENIAEKFRADGVARPNWSAVFAVAFCVACLITVEFLPVSLLTPMAQDLGISEGVAGQSVTVTAFVAMFSSLFITQIIQATDRRYIVILFAVLLTASCLMVSFANSFTLLLLGRACLGLALGGFWAISASLTMRLVPARTVPKALSVIFGAVSIALVIAAPLGSFLGGIIGWRNVFNAAAVMGVLCVIWVVKSLPSLPGEPSHQKQNMFSLLQRPGVMAGMIAIFMSFAGQFAFFTYIRPVYMNLAGFDVDGLTLVLLSFGIASFVGTSFSSYVLKRSVKLALAGAPLLLALSALTLIVWGSDKTVAAAIAIIWGLAFALVPVGWSTWITRSLADQAEKAGSIQVAVIQLANTCGAAVGGYALDNFGLLSPLALSGGLMLLTALVVAAKVRITPMS", "text": "FUNCTION: Involved in the efflux of purine ribonucleosides, such as inosine and guanosine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. NepI (TC 2.A.1.2.26) subfamily."}
{"protein": "MRLFLSLPVLVVVLSIVLEGPAPAQGTPDVSSALDKLKEFGNTLEDKARELISRIKQSELSAKMREWFSETFQKVKEKLKIDS", "text": "FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C1 family."}
{"protein": "MFTSVAQANAAVIEQIRRARPHWLDVQPASSLISELNEGKTLLHAGPPMRWQEMTGPMKGACVGACLFEGWAKDEAQALAILEQGEVNFIPCHHVNAVGPMGGITSASMPMLVVENVTDGNRAYCNLNEGIGKVMRFGAYGEDVLTRHRWMRDVLMPVLSAALGRMERGIDLTAMMAQGITMGDEFHQRNIASSALLMRALAPQIARLDHDKQHIAEVMDFLSVTDQFFLNLAMAYCKAAMDAGAMIRAGSIVTAMTRNGNMFGIRVSGLGERWFTAPVNTPQGLFFTGFSQEQANPDMGDSAITETFGIGGAAMIAAPGVTRFVGAGGMEAARAVSEEMAEIYLERNMQLQIPSWDFQGACLGLDIRRVVETGITPLINTGIAHKEAGIGQIGAGTVRAPLACFEQALEALAESMGIG", "text": "SIMILARITY: To E.coli YahG."}
{"protein": "MKGTFLICLILIAGFYFRSIQGFYFKRIQGNICSEPKKVGRCRGSFPRFYFDSETGKCTPFIYGGCGGNGNNFETLHACRAICRA", "text": "FUNCTION: Serine protease inhibitor that also shows protective effect in a cytotoxicity model (PubMed:32144281). It binds to all proteases tested (trypsin (Ki=52 nM), alpha-chymotrypsin, cathepsin G, kallikrein, and human neutrophil elastase) (PubMed:32144281). It significantly increases neuroblastoma cell viability in an in vitro neurotoxicity model, being a consequence of an effective decrease of reactive oxygen species (ROS) level in the cells (PubMed:32144281, PubMed:35563513). It also seems to protect cells by inhibiting ATP- induced purinoceptor (P2RX7) activation (PubMed:35563513). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily."}
{"protein": "MAERVSLTLNGTLLSPPPTTTTTTMSSSLRSTTAASLLLRSSSSSSRSTLTLSASSSLSFVRSLVSSPRLSSSSSLSQKKYRIASVNRSFNSTTAATKSSSSDPDQLKNAREDIKELLSTKFCHPILVRLGWHDAGTYNKNIKEWPQRGGANGSLRFDIELKHAANAGLVNALNLIKDIKEKYSGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDCPEEGRLPDAGPPSPATHLREVFYRMGLDDKDIVALSGAHTLGRSRPERSGWGKPETKYTKEGPGAPGGQSWTPEWLKFDNSYFKEIKEKRDEDLLVLPTDAAIFEDSSFKVYAEKYAADQDAFFKDYAVAHAKLSNLGAEFNPPEGIVI", "text": "FUNCTION: Plays a key role in hydrogen peroxide removal. SUBCELLULAR LOCATION: Mitochondrion Plastid, chloroplast stroma. SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase subfamily."}
{"protein": "MATMASTSNCSPVATSPLMMLLFKALQEGGDSEDEARRRREQLNRRPSYRMILKDLETADKVMKKEPEETPPSSVDASPLQFQSVMRPPPTAPPTSAATPNRILPSSNAASPYGSPLGSSILSNQPLVLPFAPINGDFDFSAAIAAASQPKVFPGGPQQNGLGGGGGGGGVPGPSSGIAGMSVQPPTSSTPSQQQSVQSLEGTSGLIGSAMKPMLGIDAVSFPEFGTTDWQSPMLSGGYSSSPSPTMTGGSMRMGGGPLHGEDESNRKRQVRLLKNREAAKECRRKKKEYVKCLENRVSVLENQNKALIEELKTLKELYCRKEKDGM", "text": "FUNCTION: [Isoform c]: Plays a role in associative long-term memory (LTM) and learning. FUNCTION: Transcription factor (PubMed:12231504, PubMed:21331044). Transcriptional activity probably positively regulated by phosphorylation (PubMed:12231504, PubMed:27720609). Modulates expression of target genes, acting by binding to regulatory cAMP response elements (CRE) (PubMed:27720609, PubMed:12231504, PubMed:34260587). Acts downstream of the calcium-triggered CaMKK-CaMK1 signaling cascade, consisting of the protein kinase kinase ckk-1 and the protein kinase cmk-1 (PubMed:12231504, PubMed:27720609). Plays a role in learning and memory, feeding behavior, stress response, entry into the dauer stage and modulation of lifespan (PubMed:31413073, PubMed:21331044, PubMed:19035344, PubMed:27720609, PubMed:23013276, PubMed:34260587). Involved in commitment to the developmentally arrested larval state known as dauer, acting by positively regulating the expression of dauer-inhibiting TGF-beta-like daf-7 in the ASI neurons (PubMed:34260587). Plays a role in both associative and non- associative long-term memory (LTM) (PubMed:23013276, PubMed:31413073). Involved in modulating feeding behavior, acting by regulating transcription of tryptophan hydroxylase tph-1 in serotonergic ADF neurons (PubMed:19035344). Regulates transcription of genes involved in endoplasmic reticulum (ER) stress (PubMed:21331044). Involved in modulation of lifespan, in response to raised temperature, but independently of the heat-shock response pathway, acting by regulating transcription of FMRFamide-like neuropeptides flp-6 in the AFD neuron (PubMed:27720609, PubMed:21331044). FUNCTION: [Isoform e]: Plays a role in associative long-term memory (LTM) and learning; perhaps required at the time of acquisition and/or the consolidation phase of memory formation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MFTTKKSMLLFFFLGTISLSLCEQERGADEDDGVEMTEEEVKRGIMDTVKNVAKNLAGQLLDKLKCKITAC", "text": "FUNCTION: May have antimicrobial activity against the Gram-negative bacterium E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ranatuerin subfamily."}
{"protein": "MMLPRNSPHRTESTLAYNNNNSNNNNNNNGSSLFQRKPLAPINSEFKISKPQHIKPTTHSHTFTTPTPKTRNTATTTTNNNNRNNHQYRNPNLNTSLVFTPTKNSSSSSSSHSSSLLSSSPFVEEPENQPESNHTRATSHYRTTSTSQYKSSANKDASHSLITSSKRKTSTKQTSESTNPKRRTTTTATQNTNNNKILNPSLSSSTIRFSTVSSSTSSSTTSSSSSSHTSPKPQQQLTLDDFEFGKILGKGKLGRVYCVKHKQSGLIFALKVMSKSEIMNLKLEKSLRREIEIQSNLYHINITRLYSWFHDSINIYLLLEYSIEGELYTHLKKLKRFDNIMASNYIFQITQALIFLHQRGIIHRDLKPENIMVSLDNQLKLSDFGWSVQINQNQNQNQIHNQTQTQKTPHQKKQKQKRLTICGTLDYLPPEMIESKSHDFSVDIWALGILCYELLVGKPPFEAINRNITYEKIAKVDIKYPSNLDVDAIDLISKLVVKDPNKRLSLKEVLNHNWIIKNKPKWPKNIYK", "text": "FUNCTION: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule attachments that are not under tension. Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Note=Associates with the mitotic spindle and on elongated and disassembling spindles. Also associated with the kinetochore (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily."}
{"protein": "MAAPRPPPGRLSGVMMPAPIQDLEALRALTALFKEQRNRDTAPRTIFQRVLDILKKSSHAVELACRDPSQVEHLASSLQLITECFRCLRNACIECSVNQNSIRNLGTIGVAVDLILLFRELRVEQDSLLTAFRCGLQFLGNIASRNEDSQSVVWMHAFPELFLSCLNHPDRKIVAYSSMILFTSLNSERMKELEENLNIAIDVVEAHQKQPESEWPFLIITDHFLKSPELVKAMYAKMSNQERVTLLDLMIAKIVGDEPLTKDDAPVFLSHAELIASTFVDQCKIVLKLTSEQHTDDEEALATIRLLDVLCEKTANTDLLGYLQVFPGLLERVIDLLRLIHVAGNDSTNIFSACASIKADGDVSSVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPLILDSCGLDDSNPFLTQWVVYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKMGFEVEKRGDKLILKSTSDTPQL", "text": "FUNCTION: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. SIMILARITY: Belongs to the ataxin-10 family."}
{"protein": "MVFCGLFSELIKGHSSSNNNGTNVSLAKTIQTNIRSQYSSDLSSYASACKKYSSLKSFDSLLHERTNSIISSLAAQAKTRSLNIESLMEVYGYLLELNQDTVRVIIESKEDVLKNNDLKALVDVYFKSTSKTLDFCNTVEKCVKKAEISQLIIRFAVKQFETETVDTDLGESKKKKYVKTLEEMNKFKAMGDPFDGEFVTQYKSVYDEQVLLLDELRKLKVKLGKKLRNIKTWRILSNVVFATAFVTVFVLSVVAAAMMAPPVLSAVASGLTTPIEVVGMWCNKMWKEYEKAVKRQRGLVLTMELGVQANNVTMVNIKFEVENLSIRISSILKTVNFAVDREENEMATRFAMQEIKKKVEGFTEKIEEVGERAANCSKLIALGRLVVLGHILGLHIVEGGAANIISSV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0496 family."}
{"protein": "MNQLDALRQYTTVVADTGDFHQLAQFQPRDATTNPSLILKAVQKPEYAPLMRATVAQYKGRSLDEVMDRMLVRFGCEILNTIPGRVSTEVDARLSFNTSATVARAERLIELYQAEGVHIDRVLIKIASTWEGIEAARQLELRGIHTNLTLLFSFCQAVACGQAKVQLISPFVGRIYDWYKKQAGAQWDEAAMAGANDPGVRSVRAIYEHYKHFGIATEVMGASFRNTGQIVALAGCDLLTIAPELLAQLGASDAPLSRALDPEAARTLELDPVHYDEAGFRLALNEDAMGTEKLAEGIRAFAADTRKLEALMQQAAD", "text": "FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily."}
{"protein": "MILVTLEQTLQDDKASVLDKMVEHEQILFCHDKATGLQAIIAVHDTTMGPALGGCRMAPYKTMDLALKDVLRLSKGMTYKCAAADVDFGGGKSVIIGDPLKDKTPEKFRAFGQFIESLNGRFYTGTDMGTTLEDFVHAMKETNYIVGKPVEYGGGGDSSIPTALGVFYGIKATNQNLFGDDKVEGRKYSIQGLGKVGYKVAEHIINEGGNVIVTDINEQAIADIQKLGGSAVRVVSSEEIYSQQADVFVPCAFGGVINDDTLKVLKVRGISGSANNQLAESRHGELLREKGILYAPDYIVNGGGLIQVADELYGTNPARVLAKTENIYTSLLEVFHQAEQDHMTTATAADRMCEKRIADAKNRNSFFTQSNRPKWNFHQ", "text": "FUNCTION: Catalyzes the reversible NAD(+)-dependent oxidative deamination of L-phenylalanine to phenylpyruvate. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
{"protein": "MACGEFSLIARYFDRVRSSRLDVELGIGDDCALLNIPEKQTLAISTDTLVAGNHFLPDIDPADLAYKALAVNLSDLAAMGADPAWLTLALTLPDVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGPLSMTLGIHGFVPMGRALTRSGAKPGDWIYVTGTPGDSAAGLAILQNRLQVADAKDADYLIKRHLRPSPRILQGQALRDLANSAIDLSDGLISDLGHIVKASDCGARIDLALLPFSDALSRHVVPEQALRWALSGGEDYELCFTVPELNRGALDVALGHLGVPFTCIGQMTADIEGLCFIRDGEPVTLDWKGYDHFATP", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. SIMILARITY: Belongs to the thiamine-monophosphate kinase family."}
{"protein": "MKILFCDVLLLSLLSSVFSSCPRDCLTCQEKLHPAPDSFNLKTCILQCEEKVFPRPLWTVCTKVMASGSGQLSPADPELVSAALYQPKASEMQHLKRMPRVRSLVQVRDAEPGADAEPGADAEPGADDAEEVEQKQLQKRFGGFTGARKSARKLANQKRFSEFMRQYLVLSMQSSQRRRTLHQNGNV", "text": "FUNCTION: [Nociceptin]: Ligand of the opioid receptor-like receptor OPRL1. It may act as a transmitter in the brain by modulating nociceptive and locomotor behavior. May be involved in neuronal differentiation and development. When administered intracerebroventricularly, nociceptin induces hyperalgesia and decreases locomotor activity. FUNCTION: [Orphanin FQ2]: Has potent analgesic activity. FUNCTION: [Nocistatin]: Blocks nociceptin action in pain transmission by inhibiting nociceptin-induced hyperalgesia and allodynia. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the opioid neuropeptide precursor family."}
{"protein": "MAATIKKGALVRVVTGNLENSLEALASDRRLPSYMFNSTAEVLDVKDDYALIKFYVPTPSVWLKLEQLEPV", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I NdhO subunit family."}
{"protein": "MAARPGAITNADSASGGGEEEGKHVKPFTPEKAKEIIMCLQQPAVFYNMVFDWPAQHWTAKHLSEVLHGKQIRFRMGTKSTDTAPQFETACNYVEATLEEFLSWNSDQSSISGAFRDYDHSKFWAYADYKYFVSLFEDKTDIFQDVIWSDFGFPGRNGQESTLWIGSLGAHTPCHLDTYGCNLVFQVQGRKRWHLFPPEDTPFLYPTRIPYEESSVFSKINVVNPDLKRFPQFRKARRHMVTLSPGQVLFVPRHWWHYVESIDPVTVSINSWIELEEDHQTRVEEAITRMLVCALKTAENPHNTRAWLNPTELEETSHEINCHYLNGAISAFFNHYGTSEVVETQALRTNREYTIKEELNMHSHVGVEQAGGHNLSSETVKQEAASPFGLDLVPVTPSSEEPSSERGGIFENDGEDFVSKNGKSFGKRQRMMSESENAVVEQIASDRTVAVSQTFVSTDDLLDCLVNPQVTRIVAQLLIQGRST", "text": "FUNCTION: May play a role in cellular stress response. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "GWRDWLKKAGGWLKKKGPGILKAALGAATQ", "text": "FUNCTION: May have antimicrobial properties, like most ant linear peptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ponericin-G family."}
{"protein": "AHDGNPLEECFREDDEEFFLEIAKNGLTATSNPKRVVIV", "text": "FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:19944711). Shows activity on L-Leu (PubMed:19944711). Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions (By similarity). In addition, this protein inhibits dose-dependently the growth of Gram-positive, Gram- negative bacteria and yeast, probably by the generation of hydrogen peroxide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
{"protein": "MENIMTLPKIKQVRAWFTGGATAEKGAGGGDYHDQGANHWIDDHIATPMSKYRDYEQSRQSFGINVLGTLIVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLNATLYYSGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYAIKLAHACAPYNLKWIEECLPPQQYEGYRELKHNAPAGMMVTSGEHHGTLQSFRTLSENGIDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMRPQFDPILLNEPVPVNGRIHKSVLDKPGFGVELNRDCNLKRPYSH", "text": "FUNCTION: Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily."}
{"protein": "MNGQTPARHYYKKLVPSLILILNCIQFLSHPTKADPILLAFVFAVYLAFIWIIPYVASTAVSLSIFIGLWLLTDFFWAVSGQEQGAAYFLIVFLMIYAAFRLPSRLSLIFTACLIGGNILLLSSQGGSLNTIISNISIMLGLYVLFSSMRFRREARREAERNHAELAKMHVQLEHAHKELQKAHAELQEASVLSLRYAVLEERTRIARDIHDSIGHELTSVIVQLQSLPYILKSSKEDSEKVIQNVLSVARECLQEVRSVVHQMGRSESMVGLTALRGLIHQVEERSGLHVSLDTAGLSEESWPPNVSETIYRILQEALTNIIRHADASHAAAVISNDKSHLYVTITDDGQFTGSLTYGFGLTGMKERAEKAGGSLTFSAVQPSGLKIELSLPLMTTNKEQKDEQR", "text": "FUNCTION: Probable member of the two-component regulatory system YxjM/YxjL. May activate YxjL by phosphorylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MTEKANGVKSSPANNHNHHAPPAIKASGKDDHRASSRPQSAAADDTSSELQQLAEMDAPQQRRGGFRRIARLVGVLREWAYRNFREEEPRPDSFLERFRGPELHTVTTQQGDGKGDKDGEGKGTKKKFELFVLDPAGDWYYRWLFLIALPVLYNWCLLVARACFSDLQKGYYIVWLVLDYVSDVVYIADLFIRLRTGFLEQGLLVKDTKKLRDNYIHTMQFKLDVASIIPTDLIYFAVGIHNPEVRFNRLLHFARMFEFFDRTETRTSYPNIFRISNLILYILIIIHWNACIYYAISKSIGFGVDTWVYPNITDPEYGYLSREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKEMEAKVIRWFDYLWTNKKSVDEREVLKNLPAKLRAEIAINVHLSTLKKVRIFQDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKRVLEERGREILMKEGLLDENEVAASMEVDVQEKLEQLETNMDTLYTRFARLLAEYTGAQQKLKQRITVLETKMKQNNEDDSLSDGMNSPEPPAEKP", "text": "FUNCTION: Odorant signal transduction is probably mediated by a G- protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGA2 subfamily."}
{"protein": "MKLTVKTLKGSHFEIRVLPTDTIMAVKKNIEDSQSKDNYPCGQQLLIHNGKVLKDETTLVENKVTEEGFLVVMLSKSKTASSAGPSSTQPTSTTTSTISSTTLAAPSTTQSIAVPASNSTPVQEQPTAQSDTYGQAASTLVSGSSIEQMVQQIMEMGGGSWDKETVTRALRAAYNNPERAVDYLYSGIPETVTIPATNLSGVGSGRELTAPPPSGGPNSSPLDLFPQEAVSDAAGGDLGTLEFLRGNDQFQQLRSMVNSNPQILQPMLQELGKQNPQLLRLIQENQAEFLQLLNEPYEGSDGDVDIFDQPDQEMPHSVNVTPEEQESIERLEAMGFDRAIVIEAFLSCDRNEELAANYLLEHSADFED", "text": "FUNCTION: May be involved in nucleotide excision repair (By similarity). Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a ubiquitin receptor that associates with the 26S proteasomal docking subunit RPN10 for the indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP) (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RAD23 family."}
{"protein": "MAFEALLEEQREETRLIIEELLEDGSDPDALYTIEHHLSCNNFDSLEKAAVDAFKLGYEVTEPEELELEDGTTVMCVDILSEGALKAELIDAQVEQLVNLVAKYNVDYDGWGTYFEDPNAQDDDEDDGEAIDEDDNGIRH", "text": "FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RraB family."}
{"protein": "MAATMIFGSFTHDLLGKAMSTIHSAVTAEKDIFSSIKERLERKRHGKICRMKNGSIYIKAASSTKVEKINAAAKKLADDKAAFLKAQPTIVDKIIVNEKIQVVEAEEVHKREDVQTVFFKKTKKRAPKLRATCSSSGLDNLYNAVANIAKASSLRVEVIHKKRVCGEFKQTRFGRALFIDVAHAKGHRRRIDCRMHRREQRTMHMFMRKTTKTEVRSKHLRKGDSGIVLLTQKIKGHLSGVRDEFFIVRGTCDDSLLEARARFSQSITLRATHFSTGDIFWKGFNASFQEQKAIGLDHTCTSDLPVEACGHVAALMCQSLFPCGKITCKRCIANLSNLDFDTFSELQGDRAMRILDVMRARFPSFTHTIRFLHDLFTQRRVTNPNTAAFREILRLIGDRNEAPFAHVNRLNEILLLGSKANPDSLAKASDSLLELARYLNNRTENIRNGSLKHFRNKISSKAHSNLALSCDNQLDQNGNFLWGLAGIAAKRFLNNYFETIDPEQGYDKYVIRKNPNGERKLAIGNFIISTNLEKLRDQLEGESIARVGITEECVSRKDGNYRYPCCCVTLEDGSPMYSELKMPTKNHLVIGNSGDPKYLDLPGEISNLMYIAKEGYCYINIFLAMLVNVDEANAKDFTKRVRDESVQKLGKWPSLIDVATECALLSTYYPAAASAELPRLLVDHAQKTIHVVDSYGSLNTGYHILKANTVSQLEKFASNTLESPMAQYKVGGLVYSENNDASAVKALTQAIFRPDVLSELIEKEPYLMVFALVSPGILMAMSNSGALEFGISKWISSDHSLVRMASILKTLASKVSVADTLALQKHIMRQNANFLCGELINGFQKKKSYTHATRFLLMISEENEMDDPVLNAGYRVLEASSHEIMEKNLSRTVRDILVRLKLVWKIQVNLVYAKALWKIQSRIVPKRADRLARTLQQLVAVSLPEYAQALEKQGESVSRKIFGKHFKCKTQDNMCSF", "text": "FUNCTION: [Movement protein P3N-PIPO]: Allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (By similarity). FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma. SIMILARITY: Belongs to the potyviridae P3N-PIPO polyprotein family."}
{"protein": "MAMTSAATGFILTANVPAAIGGGSSKSTTIVSFLPMRSFGSRLVVRAAEDTPPATASSDSSSTTAAAAPAKVPAAKAKPPPIGPKRGSKVKILRKESYWYKNVGSVVAVDQDPKTRYPVVVRFAKVNYANISTNNYALDEVEEVK", "text": "FUNCTION: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the PsaE family."}
{"protein": "MKSLLPISSLLVLLGSASAFAADLNIPMSFEYLALDGKKVESSVFNHKSSLELTPGTHKIAIRYHEMVEDDFSDSQTFVKSAPFIVTLDVDGDYQYYLQAAEGKVVKKPKVYAQNPQIKLTRGDKGDVNFQVVNTNLEEESFVSRLFSGNQAVDVSGTAAAATGAAGAVVAVAPAPVATSATVSATSLTAPVDTSKATAANPQQMLQYWWLQADEKTRKEFMSWAISQL", "text": "SIMILARITY: Belongs to the UPF0319 family."}
{"protein": "MRSNTVILAALPLVASAASTSGNWGGGVNYSKIFGGGLSANASIHYPGQPDYNTTTVQRWSTWAEPTFAVTIKPATDEDVQYIIRTANKYNLTFLATGGGHGGETGFATVKHAVNIDLSNFKENVLDLEANTLTVGPGNSFSAFETNLYNAGKMVPVGNAFCVNMIGATIGAGVGPYQGLHGLVIDALRSVRLVTASGDIVTASDEENPDLFWAVRGAGANFGIITSATYEIFDAPNNGNVVLAEFAYPGSVNGSLWQLLESWGETYPKEMGLTMSASYSQTTGTTSSSASLTYFGTQEAAQPWIDQLLALNPTQWRNATLPWSEVSQNSGFGTGASVCATGKYNNHPSVGAKQTSVSTYIEVFNQYVEIMKARPWLTSALVVQRFNTTATLAVPESKRGVYPGRDFSSLIILENYYDGPRHDADVYRFSKKLRSQLVATSGFDSLQTYINYAHGDEGPEVWYGKDNLPRLVQLKRQWDPEGKFGPGNPIPLA", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities (PubMed:35398258). The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MLSLILTIFFVHVAIYLVNTVGATTIDTLLWILYLKLPTSTSKNAREQSRLKREVVQLKREMNNTSSQDEFAKWAKLRRKHDKAMDEYEAMNKKLTAQKTSFDWSVKIARWLSTNGLKIFLQFYYSKTPVFALPAGWFPSYVEWVLSFPRAPRGSVSVQVWNSVCATAIAVMAEIVTSMLLQLRSRSASPASTAKAQKAQ", "text": "FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble get3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WRB/GET1 family."}
{"protein": "MSRIIALIISFLLVGCATPPMPAQRIVGEVRMSRPLSRTAHIDVSIFGLYEGKVREVQRTRFETGNLPLFFSIKLNPAQRGEGELYLRSTLSFPERGVQAVAQQKLIGKNKVVLQMIPKTCYPNCQSPNTR", "text": "FUNCTION: Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:9427408, PubMed:15292137). Pilot protein that is required for the proper localization of the secretin YscC/SctC in the outer membrane (PubMed:9427408, PubMed:15292137). Also required for efficient oligomerization of YscC/SctC and stabilization of the oligomers (PubMed:15292137). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Note=Association with the outer membrane is a prerequisite for function in the biogenesis of YscC/SctC. SIMILARITY: Belongs to the ExsB/YscW family."}
{"protein": "MKIIEVDEELYQYIASQTRSIGESASDILRRLLSLPVHTSIVNDLIITSAETDQKPKQAINVKEVNIKTTKKQSITAINQIVEKVQTLLNSTEFQEESKAVVRFLAILRVLYRTNPESFAQATESLQGRTRVYFARDEATLLMAGNHTKPKQIPDTPYWVITNTNSGRKMLMLEGAMQSMELPETLIDEVRSYFTVN", "text": "FUNCTION: Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re- initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SeqA family."}
{"protein": "MVLSQKLHEAFKGTVERITGPRTISAFKEKGVLSVSEFVLAGDNLVSKCPTWSWESGDASKRKPYLPSDKQFLITRNVPCLRRAASVAEDYEAAGGEVLVDDEDNDGWLATHGKPKDKGKEEDNLPSMDALDINEKNTIQSIPTYFGGEEDDDIPDMEEFDEADNVVENDPATLQSTYLVAHEPDDDNILRTRTYDLSITYDKYYQTPRVWLTGYDESRMLLQPELVMEDVSQDHARKTVTIEDHPHLPGKHASVHPCRHGAVMKKIIDVLMSRGVEPEVDKYLFLFLKFMASVIPTIEYDYTMDFDLGSSST", "text": "FUNCTION: E2 conjugating enzyme responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATG3 family."}
{"protein": "MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYIWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDDKKEDEKKEMDTDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRTPFDLFENQKKRNNIKLYVRRVFIMDNCEDLIPEYLNFIKGVVDSEDLPLNISREMLQQNKVLKVIRKNLVKKTMELIEELTEDKENYKKFYDQFSKNLKLGVHEDSNNRAKLADFLRFHTSASGDDFCSLSDYVSRMKENQKHVYFITGESKDQVSNSAFVERVKARGFEVVYMTEPIDEYVIQHLKEYKGKQLVSVTKEGLELPEDDAEKKKREEDKAKFESLCKLMNAILDNKVEKVVVSNRLVDSPCCIVTSQFGWSANMERIMKAQALRDTATMGYMAGKKQLEINPDHPIVETLRQKADADKNDKAVKDLVILLFETSLLSSGFSLDSPQVHASRIYRMIKLGLGIDEDEPMTTEDAQSAGDAPSLVEDTEDASHMEEVD", "text": "FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family."}
{"protein": "MSFFKTAVRRFSSTSITRGMAKAIAYSEYGNPKEVLRAVSYNVPKCSKNQVNVRFLASPINPSDINQIQGVYPSKPPFTNDVCSSKPSAVAGNEGLVEVVDVGDQFKGTFSPGQWAILGSVNLGSWRTEMNIDGRSLVPVDKSAFPSIAEAATLSVNPCTAYCLLQHVVQLNKGDWFIQDGANSMVGIATIQLAKHFGYKSINVVRNRPDIEKLKEQLKSLGATIVITDEELMDRKTMKQKVPEWIQGGEVKLGIDCVSGRVAAEMAKYMSKGATMATFGGMSRQPLPVPVSLLIFKNLKFHGFWVTKWKSEHPEEFLKIIHKVEDFYRNGTLKTVNTELVSLKEDADEKTFLDTFLNAIEGHGKKIIKFEH", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
{"protein": "MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY", "text": "FUNCTION: Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids (PubMed:19218247). Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH (PubMed:14672942). Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens (PubMed:10998348). Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3- alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha- androstane-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:15929998, PubMed:17034817, PubMed:17442338, PubMed:8573067). Also specifically able to produce 17beta-hydroxy-5alpha-androstan-3-one/5alphaDHT (PubMed:10998348). May also reduce conjugated steroids such as 5alpha- dihydrotestosterone sulfate (PubMed:19218247). Displays affinity for bile acids (PubMed:8486699). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MAGVILLLLSLCVGYIAYYFFRTESMNKESVRGKRVLITGSSTGLGEQIAYEFARMGAHIMITARRLQQLQEVASQCMKLGAASAHYVASDMGNLESAQSVAQEAVVKLGGLDYLVLNHIGGSGGFGFFKGDMDPVVGSTTVNFLSYVQLTSSALSALQESQGSIVVISSMSGRIGAPFTTSYCASKFALEGFYSSLRREFALQNSKMSVTVAVLGYIDTENAVKKVGNKVSMTASSKEDCAREVVKAAVLQQPEIFYPYWGIKPFVLLRDWFPGLVAKILDKCYILENIQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSPRVVSNSSVLASQSVGITNVRTVFSNVFNNTTAFPILRGSNCHKITAPGLGKGQLVNLLPPENLPWCGGSQGPRMLRTCYVLCSQAGPPSRGWQSLSFDGGAFHLKGTGELTRALLVLRLCAWPPLVTHGLLLQAWSRRLLGSRLSGAFLRASVYGQFVAGETAEEVKGCVQQLRTLSLRPLLAVPTEEEPDSAAKSGEAWYEGNLGAMLRCVDLSRGLLEPPSLAEASLMQLKVTALTSTRLCKELASWVRRPGASLELSPERLAEAMDSGQNLQVSCLNAEQNQHLRASLSRLHRVAQYARAQHVRLLVDAEYTSLNPALSLLVAALAVRWNSPGEGGPWVWNTYQACLKDTFERLGRDAEAAHRAGLAFGVKLVRGAYLDKERAVAQLHGMEDPTQPDYEATSQSYSRCLELMLTHVARHGPMCHLMVASHNEESVRQATKRMWELGIPLDGTVCFGQLLGMCDHVSLALGQAGYVVYKSIPYGSLEEVIPYLIRRAQENRSVLQGARREQELLSQELWRRLLPGCRRIPH", "text": "FUNCTION: Dehydrogenase that converts trans-4-L-hydroxyproline to delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using ubiquinone-10 as the terminal electron acceptor. Can also use proline as a substrate but with a very much lower efficiency. Does not react with other diastereomers of Hyp: trans-4-D-hydroxyproline and cis-4-L- hydroxyproline. Ubiquininone analogs such as menadione, duroquinone and ubiquinone-1 react more efficiently than oxygen as the terminal electron acceptor during catalysis. SIMILARITY: Belongs to the proline oxidase family."}
{"protein": "MTFRNCVAVDLGASSGRVMLARYERECRSLTLREIHRFKNGLHSQNGYVTWNVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDFVLLDQQGQRVGLPVAYRDSRTNGLMAQAQQQLGKRDIYQRSGIQFLPFNTLYQLRALTEQQPELIPHIAHALLMPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGANKAWFGRPTHPGNVIGHWICPQGNEIPVVAVASHDTASAVIASPLNGSRAAYLSSGTWSLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRVLQERQINDLPALIAATQALPACRFIINPNDDRFINPEAMCSEIQAACRETAQPIPESDAELARCIFDSLALLYADVLHELAQLRGEDFSQLHIVGGGCQNTLLNQLCADACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTTANLTTFTPNPDSEIAHYVAQIHSTRQTKELCA", "text": "FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1- hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. SIMILARITY: Belongs to the rhamnulokinase family."}
{"protein": "MTISTTSSSTSSKTSSEKGDDLKGFSSSSSPASSRSSSATTPEPSSPTVLAAKTIESIDPFQPRKDYNENVLPAIPATEAVQPLTSDANTPDHWIARDERMIRLTGKHPFNSEAPLSELFSKGFLTPQNLFYVRSHGDTPRVTREQAENWKLKVHGLVEQEVELSIKDLKEKFPTVTLPITLVCAGNRRKEQNMVAKGLGFNWGAAGVSTGLFTGVYLADILDYCKPKNPLLSSFPSYDVAVPGRARHVVFEGADELPKGKYGTSQRLNWALDRCKGMLIAWGLNGEDLSPDHGYPLRLVVPGQIGGRMVKWLERIEVSDRESQHHLHFHDNKVLPTEVTADQARSEMHWWYDPKYIINDLNVNAAICSPDHDQVVNVAEPSTSSPQMLPLEGYAYTGGGRRIHRVEISLDDGHSWKCASIHYPEDLYRMYPIQGHEYFGTLDLSATEMSFSWCFWRLDVDVQADIIAKDVKVISVRALDEGLATMPRDMYWNATSMMNSWWFRVAVHREGENGNQIRFEHPTLAGNAPGGWMQRMNEAGLNPRYPQFGEAKAVESCKTDANTLAAAKEAKVDPKAIMIDPSKADTIITAADLAAHGDGEGPEPWFVVHGHVYDGTGFLKDHPGGDQSIRLVAGEDATEDFMAIHSMDAKKMLRDFHLGRLEKQDAAPPAATTEGEVLDLSKPFLDPKKWRATRLVSKQIISPDARIFRFALGSEDQELGLPVGQHVFVRVRSKNARTGETEMVQRAYTPYSGNTQRGFLDILIKVYFPSDAAATSAPAFEGGKMTMLLEKIDVSSPSDDLTIELKGPLGSFTYLGQQQIRWKPASAVRRVRKLAMIAGGSGITPIWSTLKAIADEVLDASNPSSPALDPIQIWIVYGNRTEQDILIREELERLRVALKGNLKVWHVLSNCTPENEANWSMGRGHITANVLRTHLPPPPAKPASEDELEDTLALVCGPPPMEKAVSDGLKQLGWDLQRCVVFF", "text": "FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. SIMILARITY: Belongs to the nitrate reductase family."}
{"protein": "MASLGFLFFFLLPLILLELSSSRSVMAAKTRHFKWDVEYIHWSPDGEESVVMGINGQFPGPTIRAKAGDTVAVHLTNKLHTEGVVIHWHGIRQIGTPWADGTAAISQCAINPGETFLYRFKVDKAGTYFYHGHYGMQRSAGLYGSLIVEVGEGEKEPFHYDGEFNLLLSDWWHKGSHEQEVDLSSNPLRWIGEPQTLLLNGRGQYNCSLAARFSKPPLPQCKLRGGEQYAPQILRVRPNKIYRLRVASTTALGSLSLAIGGHKMVVVEADGNYVQPFSVQDMDIYSGESYSVLFKTDQDPTKNYWISINVRGREPKTPQGLTLLNYLPNSASKFPTLPPPIAPLWNDYNHSKSFSNKIFALMGSPKPPPQNHRRIILLNTQNKIDGYTKWAINNVSLVLPTQLYLGSIRYGINAFDTKPPPDNFPKDYDVLKQAPNSNSTYGNGVYMLKFNTTIDIILQNANALAKDVSEIHPWHLHGHDFWVLGYGEGKFSEKDVKKFNLKNPPLRNTAVIFPFGWTALRFVTDNPGVWAFHCHIEPHLHMGMGVIFAEGVHLVKKIPKEALACGLTGKMLMSNKHN", "text": "FUNCTION: May be involved in a redox system involving ascorbic acid. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYFYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVSNAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQELLTQYTKFAQMVKKMGGIKGLFKGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM", "text": "FUNCTION: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (By similarity). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (By similarity). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (By similarity). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (By similarity). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (By similarity). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (By similarity). SUBCELLULAR LOCATION: Nucleus speckle Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily."}
{"protein": "MPVLSNPSFYLPLVDITPFLENPHGAAAQDVIESVRTACKSTGFFQIKGHQVPLRLQKSVFEASARFFALPLKNKLELDSRKTVGFRGYDVMETQSYELEFGAVQEADALRDIKEGFFIATDLPPDHPHVANGRFLQGPNVWPKPEQLAPEDFQSVLEEYYTEMQRLSHVVLSLLAATLPYGPHVFDELETCDPMSLLRLLHYPRGLEKQDGKKLQLGAGEHTDFGTFTLLLQDEHPGLEVQDSVTGEWHGVPPQEDVYIVNVADILSTMTEGDYKSSVHRVWNIKSNDRYSVVFFYDGNLDYKVKPLRSSGQDENEEIDAPTIEEHVRSRLTASYAI", "text": "FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the cla gene cluster that produces clavatol and ortho-quinone methide (PubMed:30811183). The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones (PubMed:30811183). The non-reducing PKS claF is responsible for the formation of clavatol from successive condensations of 3 malonyl-CoA units, presumably with a simple acetyl- CoA starter unit, and 2 methylation steps (PubMed:30811183). The esterase claE probably collaborates with claF by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (By similarity). The clavatol oxidase claD then converts clavatol to hydroxyclavatol (PubMed:30811183). Spontaneous dehydration of hydroxyclavatol leads to the accumulation of the highly active ortho-quinone methide (PubMed:30811183, PubMed:31860310). On the other hand, the PKS-NRPS hybrid traA is involved in the formation of crustosic acid, with the help of traB and traD (PubMed:30811183). The polyketide synthase module (PKS) of traA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl- CoA starter unit with 3 malonyl-CoA units (PubMed:30811183). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with L-malic acid (PubMed:30811183). Because traA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase traG (By similarity). Crustosic acid undergoes decarboxylation and isomerization to the terrestric acid, catalyzed by the 2-oxoglutarate-dependent dioxygenase traH (PubMed:30811183). Both acids are further converted to the 2 gamma-butyrolactones (R)-5-methyltetronic acid and (S)-5- carboxylmethyltetronic acid, with involvement of the cytochrome P450 monooxygenase claJ (PubMed:30811183). Spontaneous addition of the methide to these gamma-butyrolactones leads to peniphenone D and penilactone D, which undergo again stereospecific attacking by methide to give penilactones A and B (PubMed:30811183, PubMed:31860310). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MLRGIFHICLLASFLLLPFSSAVHDSGFTGGTDAPPPWDHNVSPPPETAPSPTPTSSPSTTSPPSPGPVAAPSPINNGSVSGDMTWWCNKTPHAETCNYYFRKSSQNNINLRPPRFRSEFLRMLVKVALDQAVITHSQTVKFGPSCTNNQRKAAWSDCVNLFQNTVAQLNRTLKGLNPAASSDVKCTDFDAQTWLSTAQTNIETCRSGSEDLNVSDFVMPVISNKNLSDLIGNCLAVNGVLMKQHDHTTTANHKEYFPSWVSRHERRLLVSASLAKSSPHLVVAQDRSGHFRSIQAAINFAARRRFKSRFVIYVKKGVYRENIDVGNDNHNIMLVGDGERKTIITSGRSVQHGYTTYNSATGGFGGQRFVAKDMTFINTAGPLRGQAVAVRSSSDLSVFYRVGIHGFQDTLYIHSQRQFFRECYISGTIDFIFGNAAVVFQNCMILVRRPLHGQANIITAQGRGDPFQNTGITIHSSRIIAASDLKPVIRAYKTYLGRPWQAYSRVTIMKTYIDNSISPLGWSPWLRGSNFALNTVFYGEYKNFGPGSSTRWRVRWKGFHAITSTAVASRFTVGSLIAGGSWLPATGVPFKSGL", "text": "FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: In the C-terminal section; belongs to the pectinesterase family. SIMILARITY: In the N-terminal section; belongs to the PMEI family."}
{"protein": "MATVLTTAIDVCFNPQNSDTKKHSLFLKPSLFRQSRSRKLNISCSSLKQPKTLEEEPITTKTPSLSEQLKPLSATTLRQEQTQILSKPKSVWVNPTRPKRSVLSLQRQKRSAYSYNPQIKDLRAFALKLNSSIFTEKSEFLSLLDEIPHPPNRDNALLVLNSLREWQKTHTFFNWVKSKSLFPMETIFYNVTMKSLRFGRQFQLIEEMALEMVKDGVELDNITYSTIITCAKRCNLYNKAIEWFERMYKTGLMPDEVTYSAILDVYSKSGKVEEVLSLYERAVATGWKPDAIAFSVLGKMFGEAGDYDGIRYVLQEMKSMDVKPNVVVYNTLLEAMGRAGKPGLARSLFNEMLEAGLTPNEKTLTALVKIYGKARWARDALQLWEEMKAKKWPMDFILYNTLLNMCADIGLEEEAERLFNDMKESVQCRPDNFSYTAMLNIYGSGGKAEKAMELFEEMLKAGVQVNVMGCTCLVQCLGKAKRIDDVVYVFDLSIKRGVKPDDRLCGCLLSVMALCESSEDAEKVMACLERANKKLVTFVNLIVDEKTEYETVKEEFKLVINATQVEARRPFCNCLIDICRGNNRHERAHELLYLGTLFGLYPGLHNKTIKEWSLDVRSLSVGAAETALEEWMRTLANIIKRQEELPELFLAQTGTGTHRFSQGLANSFALHLQQLSAPFRQSDRPGIFVATKEDLVSWLESKFPPLVTSQA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. P subfamily."}
{"protein": "MSQVKLNLIAAACDNMGIGVNGALPWRLKKEMAYFTTMTSKVSEPTKVNAVIMGRRTWDCIPDKYRPLQDRVNIVLTHNVDSVKENVPEGVMVFPGLDEAIKYIEGREDIESTWVIGGSSIYRAAMTHPNCGKIYLTEIQKSFDCDTFFPNIDKQQFHLVDEEQIPGEKQVEGNISYYFRVYKKL", "text": "FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). SIMILARITY: Belongs to the dihydrofolate reductase family."}
{"protein": "MARKVIALAFLLLLTISLSKSNAARVIKYNGGESGGGGGGGGGGGGGGNGSGSGSGYGYNYGKGGGQSGGGQGSGGGGGGGGGGSNGSGSGSGYGYGYGQGNGGAQGQGSGGGGGGGGGGGGGGSGQGSGSGYGYGYGKGGGGGGGGGGDGGGGGGGGSAYVGRHE", "text": "FUNCTION: Responsible for plasticity of the cell wall. SUBCELLULAR LOCATION: Secreted, cell wall."}
{"protein": "MEWPINKPIYDINKSWEDNLENGPFIEGYKKVDRNDNKDPSKYIDFLGQKLASPIGVPAGPLLNSQWVKFALEAGFDLPTYKTIRSHEHFGHPVPNVMYLDLESEDKQFTKSDSGSTLHATQTIPTTMDQLAITNSFGMPSMGKEYLYKDIALAHSYLGSGQSMIVSITGTASSAHDFLQDFVDTVRIACDAGAKMVEVNYSCPNVVTGEGQIYHNPDAVYEISSTLVKELSSKNIPLIIKVGVMDDLEKMERLFQQAERAGVAAIAGINTLSMKVTDKITGEPSLGASRLTSGVCGAPIRSAALDWVSTASSIIKKQNSKLKLLGCGGIVKPEHFDDFLNSGADIAMSATGLMWDPYIAMKWHNNNKNN", "text": "FUNCTION: Catalyzes the conversion of dihydroorotate to orotate (PubMed:2996629). Participates in the pyrimidine biosynthetic pathway (PubMed:2996629). SIMILARITY: Belongs to the dihydroorotate dehydrogenase family."}
{"protein": "MSRRKTREPKEENVLGPTVREGEFVFGVAHIFASFNDTFIHVTDLSGRETLVRITGGMKVKADRDESSPYAAMLAAQDVAQRCKELGITALHIKLRATGGNKTKTPGPGAQSALRALARSGMKIGRIEDVTPVPTDSTRRKGGRRGRRL", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "MYGRIDSSSDFHYTQSASKQMDAETQEFADTFARMHLDRSNGGSSSAARYTLDHEPPVVPIDLETFRREIRKFHGKEITDIANNPQEYSDFVSAKARRTADVAQQYGIRRDSENARYFSYQLGNQCVGLMRTEGGFSMEEEFESKSWRDQFPGHQEITSTVDLQVAHPLVENAGDILLEHQLRRDGERPLLNWRAENPEAKARAAMMGFVEVDDCDMVLDPKQHPDKWTQTSAAEWRRKDKPPLYLRKFEDAETAQCSTSCSYETYEDDFM", "text": "SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion system (TTSS). SIMILARITY: Belongs to the NopP family."}
{"protein": "MITMTNWESLYEKALDKVEASIRKVRGVLLAYNTNIDAIKYLKREDLEKRIEKVGKEEVLRYSEELPKEIETIPQLLGSILWSIKRGKAAELLVVSREVREYMRKWGWDELRMGGQVGIMANLLGGVYGIPVIAHVPQLSELQASLFLDGPIYVPTFERGELRLIHPREFRKGEEDCIHYIYEFPRNFKVLDFEAPRENRFIGAADDYNPILYVREEWIERFEEIAKRSELAIISGLHPLTQENHGKPIKLVREHLKILNDLGIRAHLEFAFTPDEVVRLEIVKLLKHFYSVGLNEVELASVVSVMGEKELAERIISKDPADPIAVIEGLLKLIKETGVKRIHFHTYGYYLALTREKGEHVRDALLFSALAAATKAMKGNIEKLSDIREGLAVPIGEQGLEVEKILEKEFSLRDGIGSIEDYQLTFIPTKVVKKPKSTVGIGDTISSSAFVSEFSLH", "text": "FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ADP-dependent glucokinase family."}
{"protein": "MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVVLTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNMSLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDLDFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQREVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH", "text": "FUNCTION: [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:15472229, PubMed:18674515, PubMed:18719240, PubMed:23756265, PubMed:23288867, PubMed:24641623). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:23756265). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol and estrone (PubMed:15472229, PubMed:18719240, PubMed:23288867). Contributes to bile acid (BA) detoxification by catalyzing the glucuronidation of BA substrates, which are natural detergents for dietary lipids absorption (PubMed:23756265). Involved in the glucuronidation of calcidiol, which is the major circulating form of vitamin D3, essential for the regulation of calcium and phosphate homeostasis (PubMed:24641623). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonists losartan, candesartan and zolarsartan, which can inhibit the effect of angiotensin II (PubMed:18674515). FUNCTION: [Isoform 2]: Lacks UDP-glucuronosyltransferase (UGT) activity but acts as a negative regulator of isoform 1. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MAMKAPDPGGSGEILPSTPSLSETTSGGAAAASKSAQLPSSSSDIDNIHVPSYSSWFSWTDINDCEVRSLPEFFDSRSSSKNPKFYLYLRNSIIKQYRDDHPRKISFTDVRRTLVSDVVSIRRVFDFLDSWGLINYNSSASAKPLKWEEKEAGKSAGDAASEPATTVKETAKRNCNGCKAICSIACFACDKYDLTLCARCYVRSNYRVGINSSEFKRVEISEESKPEWSDKEILLLLEAVMHYGDDWKKVASHVIGRTEKDCVSQFVKLPFGEQFVKESDSEDGLEMFDQIKDSDIPESEGIDKDGSSPNKRIKLTPLADASNPIMAQAAFLSALAGTNVAEAAARAAVRALSDVDYEADKNASRDPNRQDANAASSGETTRNESERAWADAKSLIEKEEHEVEGAIKETVEVEMKKIRDRIVHFEKLDLEMERSRKQLEEVRNLLFVDQLNIFFHTRKARKTEDRIEC", "text": "FUNCTION: Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. May play an essential role in the transition from the vegetative to the reproductive phase of development. May be a positive regulator of ABA signaling. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKPKVFITRQIPENGIKMIEKFYEIELWKDPKAPPRGVLLEKVREVDALVTLVTDKVDKELLENAPKLKIIAQYAVGYDNIDIEEATKRGIYVTNTPGVLTDATADLAFALLLAVARRIVEADAFVRSGEWKKSEVGWHPLMFLGYGLKGKTLGIVGFGRIGQALAKRAKGFGMKIIYYSRTRKPEAEEEIGAEYVDFETLLKESDFISLHVPLTKETYHMIGEKELKLMKPNAILINTSRGAVVDTNALIKALKEGWIAGAGLDVFEEEPYYNEELFKLKNVVLAPHIGSATHEAREGMAELVAKNLIAFAKGEIPPNLVNKDVLTSSPP", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GyaR subfamily."}
{"protein": "MSGGDRFVQTLQKLNYPKGAQLDGEDFDWLFEAVDLKPFLDWFCSAASEQNVVPDEKLQAFNTLKESGKPVLDEKALDEVLKTFSISKVPAIEEVAIEKLEEEVKALQKQKNLHIRRRNKLQMVESGNRQMCLKSKDKEEETGRAFQEVLHLLRVTNKKLNHELQSIVNGVQTLMSFFSTPETACELSSQPIFLSQLLLDKYLSLEEQSTAALTSFTKEHFFEGMSKFVEGSDENFQLVQLNVNSFGEDGTTEDKCKEMMRLQLAYICAKHKLIQMKAKSASLKVGLQWAENNASVVQDKASQKEENLKVRITSLKNETLQIENHTNSISNEKLPGLVRDNAQLLNMPIVKGDYDLQMAHQTSCSSRQDLVCDHLMKQKASFELLQLGYELELRKHRDVYRELGSIVQELKESGDKLEERLTMLSDVNLLSASKPRSNIDSKDLTSHRLYQLLDGDNTQKLFRTYDGLESVAQKLSQDIASMRDQLEVSEQEHSLLLSKLDSHLKELRDFMYPEGNTLMLTTPELSGEFHQLGSQLEKLNHITVEILGDLQLKRKMLESNKLQQIEKQLYVYFFQNEEQLKSIVGKLEAQTGGGSSA", "text": "FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. SIMILARITY: Belongs to the HAUS3 family."}
{"protein": "MKLIAASLRRLSLAVLTVLLVVSSFAVFTPSASAETYTVKLGSDKGLLVFEPAKLTIKPGDTVEFLNNKVPPHNVVFDAALNPAKSADLAKSLSHKQLLMSPGQSTSTTFPADAPAGEYTFYCEPHRGAGMVGKITVAG", "text": "FUNCTION: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. FUNCTION: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Loosely bound to the thylakoid inner membrane surface. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Loosely bound to the thylakoid inner membrane surface. SIMILARITY: Belongs to the plastocyanin family."}
{"protein": "MDLRRIMETVNMIDNENLDLRTTTMGISLLDCIDSDSDRACQKIYDKITTKAENLVKVARELETEYGIPIANKRITVTPISLIAAASGDSDYVKYAVTLDKAAKAVGVDLIGGFSALVHKGYQNGDRVLIKSIPQALKETERVCSSVNVGSTRSGINMDAVKEMGQIVIENEKINPLNNGNLVIFCNAVEDNPFMAGGFHGVGESDVALNVGVSGPGVVKTALEKVKGESMDVVAETIKQTAFKVTRMGQLVGQEASKRLGVDFGIVDLSLAPTPAQGDSVANILEEIGLESVGTHGTTAALAMLNDAVKKGGIMACSHVGGLSGAFIPESEDAGMIAAAEKGILTVDKLEAMTAVCSVGLDMIAVPGDTPAETISAMIADEAAIGMINNKTTAVRVIPVPGKEVGDSIEFGGLFGYAPIMPVHKESSAAMINRGGRIPAPVHSFKN", "text": "SIMILARITY: Belongs to the UPF0210 family."}
{"protein": "MFGLGAPELILILILALIIFGPGKLPEVGRALGKGIREFKNATNSVTEEIKEAAKIDDGNNNSDKEKATRQAS", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatA/E family."}
{"protein": "MTAFHSLNVSASALTAQRVRMDVVSSNLANMDTTRAKQVNGEWVPYRRKMVSLQSKGESFSSILNSQMSGSGNAGNGVKVSKITEDDSDFNLVYDPTDPDANAEGYVQKPNVDPLKEMVDLVSSTRSYEANVTAMNATKGMLMKALEIGK", "text": "SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the flagella basal body rod proteins family."}
{"protein": "MPNNQLSNATISNTINMSAWQGRTDPEDGELGMRWHQKVLPADQANEEGIMLLGFACDAGVARNKGRTGAYGAPIAIRRALANLAWHHQEPVYDGGDISCDDGNLELAQHRLGEDVCLALRQKHKVIVFGGGHEMAWGTFQGIGAYLLQKQEATESIKAPLNLSEEKTAEPNVKGTAIPTPRVGIINFDAHFDLRNPPSGPQASAGSSGTPFHQIARFCELQHWPFNYACLGLNRGSNTQALYEKADRLGVLYRDDTELTHRTIEQTQAALNTFIAECDYLYLTIDLDVFPACVAPGVSAPAARGVSLEIIEQLMEPILTAKTEQGDSKLLVADLAEYNPRFDIDNQTARLAARLTWTIARAIR", "text": "FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L- glutamate and formamide. SIMILARITY: Belongs to the arginase family."}
{"protein": "MSLSDWHLAVKLADQPLTPKSILRLPETELGEYSLGGYSISFLKQLIAGKLQESVPDPELIDLIYCGRKLKDDQTLDFYGIQPGSTVHVLRKSWPEPDQKPEPVDKVAAMREFRVLHTALHSSSSYREAVFKMLSNKESLDQIIVATPGLSSDPIALGVLQDKDLFSVFADPNMLDTLVPAHPALVNAIVLVLHSVAGSAPMPGTDSSSRSMPSSSYRDMPGGFLFEGLSDDEDDFHPNTRSTPSSSTPSSRPASLGYSGAAGPRPITQSELATALALASTPESSSHTPTPGTQGHSSGTSPMSSGVQSGTPITNDLFSQALQHALQASGQPSLQSQWQPQLQQLRDMGIQDDELSLRALQATGGDIQAALELIFAGGAP", "text": "FUNCTION: Interferon-stimulated protein that positively regulates RNA virus-triggered innate immune signaling. Mechanistically, promotes 'Lys-27'-linked polyubiquitination of MAVS through TRIM21 leading to enhanced the IFN signaling pathway."}
{"protein": "MDPARKAGAQAMIWTAGWLLLLLLRGGAQALECYSCVQKADDGCSPNKMKTVKCAPGVDVCTEAVGAVETIHGQFSLAVRGCGSGLPGKNDRGLDLHGLLAFIQLQQCAQDRCNAKLNLTSRALDPAGNESAYPPNGVECYSCVGLSREACQGTSPPVVSCYNASDHVYKGCFDGNVTLTAANVTVSLPVRGCVQDEFCTRDGVTGPGFTLSGSCCQGSRCNSDLRNKTYFSPRIPPLVRLPPPEPTTVASTTSVTTSTSAPVRPTSTTKPMPAPTSQTPRQGVEHEASRDEEPRLTGGAAGHQDRSNSGQYPAKGGPQQPHNKGCVAPTAGLAALLLAVAAGVLL", "text": "FUNCTION: Supports cell migration. May be involved in urothelial cell- matrix interactions. May be involved in tumor progression. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor."}
{"protein": "MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPSLRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPMTSTVHYPKIYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGTRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVKREEEVLTGNLQTLKIRVHEGYEEFTMVGKRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEHIDNVMGMIGILPDMTPSTEMSMRGVRVSKMGVDEYSSAERVVVSIDRFLRVRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLVPKAIRGQYSGFVRTLFQQMRDVLGTFDTTQIIKLLPFAAAPPKQSRMQFSSLTVNVRGSGMRILVRGNSPVFNYNKTTKRLTVLGKDAGTLTEDPDEGTAGVESAVLRGFLILGKEDRRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN", "text": "FUNCTION: Plays an essential role in transcription initiation and cap- stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7- methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS. SUBCELLULAR LOCATION: Virion Host nucleus Host mitochondrion. SIMILARITY: Belongs to the influenza viruses PB2 family."}
{"protein": "MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS", "text": "FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP- dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin- independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MGMQMKNFKKMMTLMALCLSVAITTSGYATTLPDIPEPLKNGTGAIDNNGVIYVGLGTAGTSWYKIDLKKQHKDWERIKSFPGGAREQSVSVFLNDKLYVFGGVGKKNSESPLQVYSDVYKYSPVKNTWQKVDTISPVGLTGHTGVKLNETMVLITGGVNEHIFDKYFIDIAAADESEKNKVIYNYFNKPAKDYFFNKIVFIYNAKENTWKNAGELPGAGTAGSSSVMENNFLMLINGELKPGLRTDVIYRAMWDNDKLTWLKNSQLPPSPGEQQQEGLAGAFSGYSHGVLLVGGGANFPGAKQNYTNGKFYSHEGINKKWRDEVYGLINGHWQYMGKMKQPLGYGVSVSYGDEVFLIGGENAKGKPVSSVTSFTMRDGNLLIK", "text": "FUNCTION: Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta- anomer, accelerating the equilibrium between the alpha- and beta- anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the NanM family."}
{"protein": "MEFRLLILALFSVLMSTSNGAEILALFPIHGISNYNVAEALLKTLANRGHNVTVVTSFPQKKPVPNLYEIDVSGAKGLATNSIHFERLQTIIQDVKSNFKNMVRLSRTYCEIMFSDPRVLNIRDKKFDLVINAVFGSDCDAGFAWKSQAPLISILNARHTPWALHRMGNPSNPAYMPVIHSRFPVKMNFFQRMINTGWHLYFLYMYFYYGNGEDANKMARKFFGNDMPDINEMVFNTSLLFVNTHFSVDMPYPLVPNCIEIGGIHVKEPQPLPLEIQKFMDEAEHGVIFFTLGSMVRTSTFPNQTIQAFKEAFAELPQRVLWKFENENEDMPSNVLIRKWFPQNDIFGHKNIKAFISHGGNSGALEAVHFGVPIIGIPLFYDQYRNILSFVKEGVAVLLDVNDLTKDNILSSVRTVVNDKSYSERMKALSQLFRDRPMSPLDTAVYWTEYVIRHRGAHHLKTAGAFLHWYQYLLLDVITFLLVTFCAFCFIVKYICKALIHHYWSSSKSEKLKKN", "text": "FUNCTION: Membrane-bound UDP-glucosyltransferase (UGT) which catalyzes the C-glucosylation of kermesate and flavokermesate to produce carminate and flavokermesate 7-C-beta-D-glucoside (dcll) respectively (PubMed:29215010). Carminate is used as a deterrent against insect predators (PubMed:29215010). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=Localization to the endoplasmic reticulum membrane is critical for its activity. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MATKEYFPGIGKIKFEGKDSKNPMAFRYYDAEKMINGRSMKDWLKFAMAWWHTLCAEGGDQFGGGTKQFPWNGDPDPVQAAKNKMDAGFEFMQKMGIGYYCFHDVDLVTEADSIEAYEANLKELVAYAKQKQAETGIKLLWGTANVFSHARYMNGAATNPDFDVVARAAVQIKNAIDATIELGGTNYVFWGGREGYMSLLNTDQKREKEHLAQMLTIARDYGRARGFKGTFLIEPKPMEPTKHQYDVDTETVIGFLKAHGLDQDFKVNIEVNHATLAGHTFEHELAVAVDNGMLGSIDANRGDYQNGWDTDQFPIDNFELTQAMMQIIRNDGLGNGGTNFDAKTRRNSTDPEDIFIAHIAGMDAMARALESAANLLNESPYQKMLSDRYASFDAGKGKEFEEGKLSLEELVAYAKANGEPKQTSGQQELYEALVNIYSL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the xylose isomerase family."}
{"protein": "MSWQTYVDDHLMCDIEGNHLSSAAILGHDGTVWAQSPSFPQLKPEEVSAIMKDFNEPGSLAPTGLHLGGTKYMVIQGEPGDVIRGKKGPGGVTIKKTNQALIIGIYGEPMTPGQCNMVVERIGDYLVEQGM", "text": "FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family."}
{"protein": "MNPTIAKITCPLCGNDEATVHRQKDRKKKLYYRCTGATFADGCGTIQCTGASGQAFISKNMKPLNGVESEDAAIEAAEDAKAEQVKPNKKRSFLDFLVDDE", "text": "FUNCTION: May regulate the expression of phage structural components with protein P13."}
{"protein": "MKHIILCIHFLLMVVGLGQAQDCSVAPNMRVNCGYPTVTEADCRAVGCCFDSSILNTKWCFYNATAGPIKKLECSGDPTKRIDCGFPRITEKQCILRGCCFDSSISGVKWCYARTVITTPAPDTTTASTTAETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTVPTTPETTTASTTAETTTVPTTPETTTEPTTTPTTDTTPPTLPPTPETTTETTTETTTETTTETTTETTTETTTAPPPECAADRVDCGYSGITQADCEGKGCIFDSTIPETKWCFYTEAEAPARKAECTVDPSVRTDCGYPGITDKECREKGCCYDECIPDVIWCFEKAVPVVNS", "text": "FUNCTION: Could be involved in defense against microbial infections. Protects the epithelia from external environment. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MANKLIGEMGLHTKISNIFAARNIITAKDALSMTEFELMELLDVGMKEIRSAISFISEATSPPCQSARSLLEKKVENEHLSGHLPTHLKGLDDTLCGGIPFGVLTELVGPPGIGKSQFCMKLALSASFPVAYGGLDGRVIYIDVESKFSSRRVIEMGLESFPEVFHLKGMAQEMAGRILVLRPTSLANFTESIQELKNSILQNQVKLLVIDSMTALLSGENKPGAQRQPQLGWHISFLKSLAEFSRIPIVVTNQVRSQNRDETSQYSFQAKVKDEFKDNTKTYDSHLVAALGINWAHAVTIRLVLEAKSGQRIIKVAKSPMSPPLAFPFHITSAGISLLSDNGTELKGPGINTIHARGHSDMINFHGDCS", "text": "FUNCTION: May be involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RecA family. RAD51 subfamily."}
{"protein": "LFHYCQCQCPPGFKGKFCQFKLRPP", "text": "FUNCTION: Peptide with nanomolar affinity for human melanocortin receptors. The natural disulfide pairing being unknown, the activity of all three possible peptides (with the cysteine pairings 'bead (I-II, III-IV), 'globular' (I-III, II-IV), and 'ribbon' (I-IV, II-III)) have been tested. All three isomers show similar affinities on each human melanocortin subtype (MC1R (~500 nM), MC3R (~100 nM), MC4R (~50 nM), and MC5R (~50 nM)). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MVAFVWLPRNGVSWTVVLPLKNLTRAKTRLDRPDRSRLALAMALDTVMAVLESETDLVGAVMIVTNDRTADHALSTLLNSHYIGADQPNLSPAARSARLVVIPDEPDRGLNPALVHGAALASARWPTRAVAALSADLPALRPPELHQALSEASQHRRAVLADATGTGTVLLTASAGATLQPAFGPHSHATHRRSGAVDLTGTLGGSVPGLRRDVDTLADLAQARDLGVGRATRAALTAGYHSPLVAEDSGGSGGESGTSAESGLSVPPGIVGGTQRRIVSDASGPGRAKKYP", "text": "FUNCTION: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor. SIMILARITY: Belongs to the CofC family."}
{"protein": "MLHTRTIALLLVGLVVLVNAQTFQYSRGWTNGKRSPLSSSSSSPSSSAAMEPLTANQLLASALSSGGLNSLKPSEKALLRRFLRNPCDLRVASLLAAAHPTKELFPLAGNSFDSAESAGAAFVLPPFLMDPDESNGGIGGSNLANGRSMEDELRFKRGTATGFSDHRQKIA", "text": "FUNCTION: Cardioactive peptide. Corazonin is probably involved in the physiological regulation of the heart beat (By similarity). SUBCELLULAR LOCATION: [Corazonin]: Secreted. SUBCELLULAR LOCATION: [Corazonin precursor-related peptide]: Secreted. SIMILARITY: Belongs to the corazonin family."}
{"protein": "NGWNDNKNFVLFGAAAWIGLVLLVGTLYYFVV", "text": "FUNCTION: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbZ family."}
{"protein": "MAAAAAEEGMEPRALQYEQTLMYGRYTQDLGAFAKEEAARIRLGGPEPWKGPPSSRAAPELLEYGRSRCARCRVCSVRCHKFLVSRVGEDWIFLVLLGLLMALVSWVMDYAIAACLQAQQWMSRGLNTSILLQYLAWVTYPVVLITFSAGFTQILAPQAVGSGIPEMKTILRGVVLKEYLTLKTFIAKVIGLTCALGSGMPLGKEGPFVHIASMCAALLSKFLSLFGGIYENESRNTEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRKIVQVMRKQKTINRFLMRKRLLFPALVTLLISTLTFPPGFGQFMAGQLSQKETLVTLFDNRTWVRQGLVEELEPPSTSQAWNPPRANVFLTLVIFILMKFWMSALATTIPVPCGAFMPVFVIGAAFGRLVGESMAAWFPDGIHTDSSTYRIVPGGYAVVGAAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRMLALVESPESMILLGSIERSQVVALLGAQLSPARRRQHMQERRATQTSPLSDQEGPPTPEASVCFQVNTEDSAFPAARGETHKPLKPALKRGPSVTRNLGESPTGSAESAGIALRSLFCGSPPPEAASEKLESCEKRKLKRVRISLASDADLEGEMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPHSRHGLPREGSPSDSDDKCQ", "text": "FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume, membrane potential stabilization, signal transduction and transepithelial transport. Involved in the regulation of aldosterone production. The opening of CLCN2 channels at hyperpolarized membrane potentials in the glomerulosa causes cell membrane depolarization, activation of voltage- gated Ca2+ channels and increased expression of aldosterone synthase, the rate-limiting enzyme for aldosterone biosynthesis (PubMed:29403011, PubMed:29403012). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC- 2/CLCN2 subfamily."}
{"protein": "MFDCMEALGMGPRQLYDVTNRGACMLRKASPFYAGLDPFAWTGTASVRSVETQSTSSEEMVPSSPSPPPPPRVYKPCFVCQDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKNCQINKVTRNRCQYCRLQKCFEVGMSKEAVRNDRNKKKKDVKDEVIPPESYELSGELEELVNKVSKAHQETFPSLCQLGKYTTNSSSDHRIQLDLGLWDKFSELSTKCIIKIVEFAKRLPGFTTLTIADQITLLKSACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFAGQLLPLEMDDTETGLLSAICLICGDRMDLEEPERVDRLQEPLLEALKIYARRRRPNKPHMFPRMLMKITDLRGISTKGAERAITLKMEIPGPMPPLIREMLENPEAFEDQSESTEKKPEPEPPAPPPPALLTMKKEQEDEDDSWATENGSEPSPEEEDDDDEDGEEERGTDSDGEAWGGQEPNADVSRKSHGGRAQ", "text": "FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain development and for the development of pharyngeal arches. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "ALFAAAGLAAAAPFETRQDYASCPVSTQGDYVWKISEFSGRKPEGTYYNSLSFNIKATNEGTLDFTCSAQADKLEDDKFYPCGENSSMSFAFQSDRNGLLFRQDVSNDITYVATATLPNYCRAGGDGPKDVICQGAS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALTA1 family."}
{"protein": "MQIFVDADACPAVIKDMLFRVARRTGICVTLVANQFLRTPPSPHIKALQVPAGFDEADARIVELAQPGDLVVTADIPLAAALLDKGAHPLDPRGNWFSRENIDERLSTRAMMEQLRSAGIDTGGPAPFSARDANAFASQLDRFVARHGKP", "text": "SIMILARITY: Belongs to the UPF0178 family."}
{"protein": "MGSSSNGGVPPGFRFHPTDEELLHYYLKKKISYQKFEMEVIREVDLNKLEPWDLQERCKIGSTPQNEWYFFSHKDRKYPTGSRTNRATHAGFWKATGRDKCIRNSYKKIGMRKTLVFYKGRAPHGQKTDWIMHEYRLEDADDPQANPSEDGWVVCRVFMKKNLFKVVNEGSSSINSLDQHNHDASNNNHALQARSFMHRDSPYQLVRNHGAMTFELNKPDLALHQYPPIFHKPPSLGFDYSSGLARDSESAASEGLQYQQACEPGLDVGTCETVASHNHQQGLGEWAMMDRLVTCHMGNEDSSRGITYEDGNNNSSSVVQPVPATNQLTLRSEMDFWGYSK", "text": "FUNCTION: Transcription activator. Together with BRN1 and SMB, regulates cellular maturation of root cap. Promotes the expression of genes involved in secondary cell walls (SCW) biosynthesis. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MYIDGVFSGGGVKGIALAGAYEVLEEKGFRFKRVAGTSAGAIIAAFIASGYTSKEIHALIEEVDGEKLLDQRYSFLPLKMLQWVSIYWRLGLYKGDTIEKWIADLLRAKGIRVFGDLQKGSLRLIASDLTNGTMIVLPDDLARYGLNPDMFPVARAVRMSCSIPYFFEPIKLKTDTGTATVVDGGVLSNFPIWLFSKERKRPVIGVTLAPRERERPKKNIRNAFELFGALFETMKDAHDARHIASRYEQNIIFLPVDDVMATDFHLTQQKKLALIELGKRRTELFLKQWTY", "text": "FUNCTION: Probable lipid hydrolase. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MSKDVIEYSKLFAKLVNTNDDTKLDDTIASFLYYMFPRELFIRAISLLESSDMFIYILDRVHNKEGNEHTSLIDVLVDEFYKGSSNSLLEYRLIVKDTNDGAPPILVDIAHWFCSCEEFCKYFHEALEKTDEKEELHDVLINEVDDHLQFSDDRFAQLDPHSLSKQWYFKFDKVCCSHLLAFSILLRSSINVLKFFTVNSNKVFVIAIDNIDEWLNLHINIVE", "text": "FUNCTION: Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase. Required for error-free repair of spontaneous and induced DNA lesions to protect the genome from mutation. FUNCTION: Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase. Required for error-free repair of spontaneous and induced DNA lesions to protect the genome from mutation (By similarity). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SHU2 family."}
{"protein": "MASGKVRCTRKLRSWIVEQVESGHFPGVCWDDAAKTMFRIPWKHAGKQDFREDQDAAIFKAWALFKEKHKDGDIGHPAVWKTRLRCALNKSSEFEEVPERGRMDVAEPYKVYRILPAGTLPNQPRNQKSPCKRSISCVSPEREENMENGRTNGVVNHSDSGSNIGGGGNGSNRSDSNSNCNSELEEGAGTTEATIREDPVFLEHQLPLNSDYSLLLTFIYGGRVVGKTQVHSLDCRLVAERSDSESSMEQVEFPKPDPLEPTQHLLNQLDRGVLVASNSRGLFVQRLCPIPISWNAPEAPPGPGPHLLPSNKCVELFKTTYFCRDLAQYFQGQGPPPKFQATLHFWEESPGSSHSQENLITVQMEQAFARHLLEKIPEEEKAALFLLQHTEQSPSALGH", "text": "FUNCTION: Transcription factor that plays an essential role in anti- viral immunity. It mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IRF family."}
{"protein": "MSQQRPARKLPSLLLDPTEETVRRRCRDPINVEGLLPSKIRINLEDNVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIDLVEKKSKNHIRWIGSDLSNFGAVPQQKKLQEELSDLSAMEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPREDSITVHIRSTNGPIDVYLCEVEQGQTSNKRSEGVGTSSSESTHPEGPEEEENPQQSEELLEVSN", "text": "FUNCTION: Inhibitor of E2F-dependent transcription (PubMed:9689056, PubMed:9704927, PubMed:9501179). Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' (PubMed:9501179). Has a preference for the 5'-TTTCCCGC-3' E2F recognition site (PubMed:9501179). E2F6 lacks the transcriptional activation and pocket protein binding domains (PubMed:9704927, PubMed:9501179). Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression (PubMed:9689056, PubMed:9501179). Represses expression of some meiosis-specific genes, including SLC25A31/ANT4 (By similarity). May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase (PubMed:9501179). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the E2F/DP family."}
{"protein": "MPPTAFALNDFITRFQLQLPPSLRPVHQQRQAAVLVPIICHPTPTLLLTRRSADLRKHAGQVAFPGGAADKTDRSIIETALREAQEEVAIPPENVQVLGVLPPLDSVSGFQVTPVVGLIAAQTRFHPNEDEVAELFEMPLDEAFALTRYYPLDIERKQQRHRVYLSWYQQQFVWGLTAAIIHQLALQISDRP", "text": "FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily."}
{"protein": "MGERRRANASRGDKKVANGEKPHVGQWGRAWEVDYFSLAAVLFLLAFAPLIVYYFVMSCDQYQCALTAPVLDLYWGKAQLSDIWDKTPALTWGAAKIYIVWVSFQVFLYMLVPDILHKFVPGYEGGVQEGARTPAGLINKYQVNGLQAWTITHLLWFANAYHFHWFSPTIIIDNWVPLLWCANLLGYSVATFALLKAYFFPTNAHDCKFTGNFFYDYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSYAAKQQELYGQVTNSMILVNVLQAIYVVDFFWNESWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYNPVELSTATAVGVLLLGLIGYYIFRMTNHQKDLFRRTNGNCKIWGKKPKSIECSYTSADGKRHYSKLMISGFWGVARHLNYTGDLMGSLAYCLACGFDHLLPYFYFTYMTILLVHRCIRDEHRCSSKYGKDWKLYTDAVPYRLLPGLF", "text": "FUNCTION: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7- dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien- 3beta-ol, two intermediates in that pathway. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERG4/ERG24 family."}
{"protein": "MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISELKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGEFNHERGERKVCRFKLEWLGNCSGLNDETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPGMKYNANVLPVQCTGKRDEDKEKIGNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS", "text": "FUNCTION: Involved in cell adhesion and establishing epithelial cell polarity. FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Apical cell membrane; Single-pass type II membrane protein Cell membrane, sarcolemma Note=Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. Localizes in long striations at the level of Z and M lines. SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family."}
{"protein": "MIDTTLPLTDIHRHLDGNIRPQTILELGRQYNILLPAQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIEDAARNGLHYVELHFSPGYMAMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQITALDLAGDKLGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIESCLTSNIQTSTVADLAAHPLKTFLEHGIRASINTDDPGVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKRALREKVAAK", "text": "FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenosine deaminase subfamily."}
{"protein": "MKTLLLTLVVVTIVCLDLGYTTKCYVTPDATSQTCPDGENICYTKSWCDVFCSSRGKRIDLGCAATCPKVKPGVDIKCCSTDNCNPFTPWKRH", "text": "FUNCTION: Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily."}
{"protein": "MKLFIIIVVTSLTISKVFDKTLVTIEARNLRKMDRHEHFNANEDFVEAKMLKKIDNKNNLNNRCINDFAPTNPGHNSGIGHPKVINNKFTKDFAPTNPGHSPGIGHLRVVNNKFTNDFAPTNPGNSPGIRHP", "text": "FUNCTION: Extracellular signaling peptide that may regulate primary root growth rate and systemic nitrogen (N)-demand signaling. SUBCELLULAR LOCATION: [C-terminally encoded peptide 10.3]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap. SUBCELLULAR LOCATION: [C-terminally encoded peptide 10.2]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap. SUBCELLULAR LOCATION: [C-terminally encoded peptide 10.1]: Secreted, extracellular space, apoplast Note=Accumulates in xylem sap. SIMILARITY: Belongs to the C-terminally encoded plant signaling peptide (CEP) family."}
{"protein": "MVVRSLLRVSRLTSASCRHASLAVSSTPKPYIPSVTGVQKSMPFDNLLEQYSRVHWDDSVTYDDPNVQKLFKSLMSGSRAALASAITLVESRHPTKRAQGNMLLKMVLDEEREKYKKFGRDSMIFRVGISGSPGVGKSSFIEALGAELTENRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTRGIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKAKAKMTQAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKHPKIAHLAPKLENEIRSGKITPGLAAETMIRTFFGV", "text": "FUNCTION: May have GTPase activity. May also bind and hydrolyze ATP. May function as chaperone (By similarity). Likely to have a role in propionyl-CoA and adenosylcobalamin metabolism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB subfamily."}
{"protein": "MKRYLILLIVTGVLLWNVVEVLRFRVEFSGGTFVLKNVQDIFVPLEVRGAKVECSKNFVLEENGVLIKQVRPGETVTLHFESGGIFRVKKELKIEARASEEDSDGDGYPDSLELDSEDSERFRNWFVWIALSAFKNDPLLWPKEERDCSGFVRYCAREALKKHTGSWFSLSGYNGPVWEDVEKYNYPNLPLVGTKMFRIEKGAYRGVEDFSNFAVARILVECSMEFVTKSVSEALPGDIAVFFHPEDVEMPYHLMIFVGNLNLADHEGWFVYHTGPIGENPGELRFVRYSELVNYDPSWAPLEINPYFLGFYRFRFLK", "text": "SIMILARITY: To E.coli YfaT and P.aeruginosa PA4490."}
{"protein": "MEDEEEEARALLPGGSDEAGRETRAPPAASGALQALCDPSHLAHRLVVLLLMCFLGFGSYFCYDNPAALQIQVKRDMQVNTTKFMLLYAWYSWPNVVLCFFGGFLIDRVFGIRWGTIIFSCFVCIGQVVFALGGIFNAFWLMELGRFVFGIGGESLAVAQNTYAVSWFKGKELNLVFGLQLSMARIGSTVNMNLMGWLYSKVEASLGSAGHTTLGVTLMIGGITCILSLVCALALAYLDQRAERILHKEQGKTGEVIKLTDVKDFSLPLWLIFIICVCYYVAIFPFIGLVKVFFTEKFGFSSQAASAINSVVYVISAPMSPIFGLLVDKTGKNIIWVLCAVVTTLASHIMLAFTLWNPWIAMCLLGLSYSLLACALWPMVAFVVPEHQLGTAYGFMQSIQNLGLAVISIIAGMILDTRGYLFLEVFFIACVSLSLLSVVLLYMVNHAQGGNLNYSAKKREEMKLSHEE", "text": "FUNCTION: Lysosomal transporter which is essential for liver homeostasis. Required to maintain stability and lysosomal localization of GLMP. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MIPEKRVIRRIQSGGYAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQALFKAGDELKSLYAIRSGTIKSYTITEEGDEQITGFHLAGDLVGFDAISNLQHPSFAQALETSMVCEIPFDTLDDLSGKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERLAAFIYNLSHRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSNILSVKGKYITIENNEALAQLAGNPKPRL", "text": "FUNCTION: Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MLHHEDESSPESDSDFDASELTDKELQEAFSQGKLKPGLNVVLEGKKKPFNDASGLKQSLKDLKNELPWVERLDVTVDPVVDTTGQNGQTDPNTSDINAEDDFQREMCFYRQAQAAVLYSLPRLRKLKVATKRPDDYFAEMAKTDQHMQKIRHKLQLKQASMEKSEKAKQLRALRKYGKKVQVEVLQKRQKEKSAMVTQIKKYQKGLSDKLDFLEGDQTPKKTPNKTGGSAAAQKAKNTPSAKRRYKDQKFGFGGKKKGSKGNTKGSYNDVSGFRGSVAHGKGPHRPGKKGGKNANKRPGKNVRQKMKSKRR", "text": "FUNCTION: Required for the processing of the 27S pre-rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the EBP2 family."}
{"protein": "MADMNQHPTVFQKAANQLDLRSSLSQDVHARYGGVQPAIYQRHFAYGNYSNAGLQRGQATQDLSLITSNASPVFVQAPQEKGFAAFATDFLMGGVSAAVSKTAAAPIERVKLLIQNQDEMLKAGRLSEPYKGIGECFGRTIKEEGFGSLWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKDRDGYWKWFAGNLASGGAAGASSLFFVYSLDYARTRLANDRKASKKGGERQFNGLVDVYKKTLKSDGIAGLYRGFNISCVGIIVYRGLYFGMYDSLKPVLLTGNLQDSFFASFGLGWLITNGAGLASYPIDTVRRRMMMTSGEAVKYKSSLDAFSQIVKNEGPKSLFKGAGANILRAVAGAGVLAGYDKLQVLVLGKKFGSGGA", "text": "FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c- state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MKRFLGILVFVVMVLSVFAGPNHLVIFHMNDTHGHVWGTEDGGGFARAATLINQAREEVAKEGGAVLFLHAGDVNTGIPESDQLDAVPDFLALHYMGLDAMSLGNHEFDKPFEVLEKQYEVAQFPFLGANFVNEKRGGPVFEPYIIKDYGDFSVGIIGLVTEQTKVLEPIYLGENTIVDAEETLNMYLPIVQEKADVVIVLAHLGYHADGGRPNLSVEFTTSDELAENVSGVDIIIDGHSHTLLETPVVINNVIVAQAGDNAENIGRIDLWIDDGRIVDWRGEVIPLTSDIPEDPFIKMFTDAFYQLGSEALNEVVGVTKVYLDGERAHVRSDETNLSNLIADGMIWKTGADVALMNGGGIRASIEAGEITYRDILTVLPFGNTLYVLELTGKDIMDVLNYAATIPDGQGAKLHVAGLTAEIKGGKATNVKINGKPIDLNKTYKVVTNNYVAAGGDGYTMLAGKPGYDTYFRDADSLREYIAHLGTIEDYTSQERLIELDQVK", "text": "FUNCTION: Involved in the biosynthesis of the compatible solute mannosylglucosylglycerate through a phosphorylating pathway. Catalyzes the dephosphorylation of mannosylglucosyl-3-phosphoglycerate (MGPG) to mannosylglucosylglycerate (MGG). Can also dephosphorylate UDP-glucose, ADP-glucose, GDP-mannose, glucosyl-3-phosphoglycerate (GPG), mannosyl- 3-phosphoglycerate (MPG), ADP, GDP and UDP. SIMILARITY: Belongs to the 5'-nucleotidase family."}
{"protein": "MASPDAEDASPSPEYRSDLDDDMAAEQKTDDGSPSQKSSNGQKPASNAKDPLRPRRKKARRACFACQRAHLTCGDERPCTRCIKRGLQDHCMDGVRKKAKYLHDAPDGALMPGVGGHYPYMNGNRPTPLPSQDTHNVPMAPQGNMYTQAPSGTFYQPPSAQIPLPQAQHGRSFSDQQSPLSPPFSQAHHGPNVNPPSSISQGQPGQMQQFGPLFDPSDPALFNFDISSLNFGNHYGALEFGMLGHMSSAVDAPNDNTMMNAMNQTANMYGPQMAGAYGPNNPNAAMPFAQNSLPAGEWQESQSRQNSMHIHTPTSSATALDHGGHRHDSLNGPHAFAIGQGPSSHSTASPASTDASAFENDNPLSTATFFANTNRGQPQRSPTTNRHHQGNRPPSTALQPIHSNGVRKRHRDTKSIYQGIKKPFDYVKGYHRLFQICHKKFSKSLLAQAQQYLNLYRPVLLSVREEMDTDDLIHQEMGLQRNLMTLQDHFTEVGTPFLICRRSGEIVSCNKEFTILTGWRQDVLLGREPNLNVNLGNSREADESEMSTQTNTTPNLTGQEAETGTPAVNAIQLMDAKSALEYLQNFSELCWQDPHGHAKQRANMLRYQTKADFDRIQEMKANADHKSDAFVKMEGGAVHQGESAMQRLGAKNGMVDCMIWWHIKRDIFEMPVLVCMSVMPVLDKGLQ", "text": "FUNCTION: Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ERT1/acuK family."}
{"protein": "MALAPELSRQTKLKEVAGIPLQAPTVDNWSQIQTFKAKPDDLLICTYPKSGTTWIQEIVDMIEQNGDVEKCQRTIIQHRHPFIEWARPPQPSGVDKANAMPAPRILRTHLPTQLLPPSFWTNNCKFLYVARNAKDCMVSYYHFYRMSQVLPDPGTWNEYFETFINGKVSWGSWFDHVKGWWEIRDRYQILFLFYEDMKRDPKREIQKVMQFMGKNLDEEVVDKIVLETSFEKMKENPMTNRSTVPKSVLDQSISPFMRKGTVGDWKNHFTVAQNDRFDEIYKQKMGGTSLNFCMEL", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Sulfonates p-nitrophenol, a small phenolic compond. Does not sulfonate steroids, dopamine, acetaminophen, or alpha-naphthol. SUBCELLULAR LOCATION: Cytoplasm Lysosome. SIMILARITY: Belongs to the sulfotransferase 1 family."}
{"protein": "MKSVKIMGTMPPSISLAKAHERISQHWQNPVGELNIGGKRYRIIDNQVLRLNPHSGFSLFREGVGKIFSGKMFNFSIARNLTDTLHAAQKTTSQELRSDIPNALSNLFGAKPQTELPLGWKGEPLSGAPDLEGMRVAETDKFAEGESHISIIETKDKQRLVAKIERSIAEGHLFAELEAYKHIYKTAGKHPNLANVHGMAVVPYGNRKEEALLMDEVDGWRCSDTLRTLADSWKQGKINSEAYWGTIKFIAHRLLDVTNHLAKAGVVHNDIKPGNVVFDRASGEPVVIDLGLHSRSGEQPKGFTESFKAPELGVGNLGASEKSDVFLVVSTLLHCIEGFEKNPEIKPNQGLRFITSEPAHVMDENGYPIHRPGIAGVETAYTRFITDILGVSADSRPDSNEARLHEFLSDGTIDEESAKQILKDTLTGEMSPLSTDVRRITPKKLRELSDLLRTHLSSAATKQLDMGGVLSDLDTMLVALDKAEREGGVDKDQLKSFNSLILKTYRVIEDYVKGREGDTKNSSTEVSPYHRSNFMLSIVEPSLQRIQKHLDQTHSFSDIGSLVRAHKHLETLLEVLVTLSQQGQPVSSETYGFLNRLTEAKITLSQQLNTLQQQQESAKAQLSILINRSGSWADVARQSLQRFDSTRPVVKFGTEQYTAIHRQMMAAHAAITLQEVSEFTDDMRNFTVDSIPLLIQLGRSSLMDEHLVEQREKLRELTTIAERLNRLEREWM", "text": "FUNCTION: Acts as a virulence determinant. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "NSANPCCDPVTCKPRRGEHCVSGPCCRNCKFLNAGTICRYARGDDMNDYCTGVTSDCPRNPYKS", "text": "FUNCTION: Poor inhibitor of platelet aggregation. The disintegrin inhibits the adhesion of cells expressing the RGD-dependent integrin alpha-5/beta-1 (ITGA5/ITGB1) to immobilized fibronectin. Inhibition on alpha-IIb/beta-3 (ITGA2B/ITGB3) is low, and there is no inhibition on alpha-1/beta-1 (ITGA1/ITGB1), alpha-2/beta-1 (ITGA2/ITGB1) and alpha- 6/beta-1 (ITGA6/ITGB1). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IId sub-subfamily."}
{"protein": "MMEESGIETTPPGTPPLHPAGLAAVPSTEAHSAATSSFSSPNVSGMESLPPHVYSTPQPSLPPVQPSAPPPFVSMSPAPSVPLSGTSVPPSVSPSPATAFSGPPMSHFPPATSASGALLSAPPSGPPISGFSVGTTYDITRGHAGRAPQTPLMPSFSAPPVTGILPAPITQQASMTSLAQGPGTTSAITFPEEQEDPRINRGQDDAPAGGIWGFIKGVAGNPMVKSVLDKTKHSVESMITTLDPGMAPYIKSGGELDIVVTSNKEVKVAAVRDAFQEVFGLAVVVGEAGQSNIAPQPVGYAAGLKGAQERIDSLRRSGAIHEKQTAVSVENFIAELLPDKWFDIGCLVVEDPVHGIRLEAFTQATPVPLEFVQQAQSLTPQDYNLRWSGLLVTVGEVLEKSLLNVSRTDWHLAFTGMSRRQMIYSAAKAVAGMYKQRLPPRPM", "text": "SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the PRRC1 family."}
{"protein": "MLRQETAPLVCKFGGTSVGTAQSIRRVCEIIQEERPSFVVVSAVAGVTDWLEEFCRLPKGKRAALTEKIRERHESIAKELGIEVSLAIFWEILEHFEDVEELFSEDQARILAIGEDLSSTLICSYCCTYVLPLKRLEARQVILTDSQFLRAVPDLALMQTAWGELALQEDTIYLMQGFLGATSSGKTTVLGRGGSDFSASLIGELCKARELRIYTDVCGVHTADPKILKDTQLIDSLTFEEMQELASSGAKVLHQDMLKPCVRAKVPIFVTSTFNVTKEGTWICASLNESTEGPVIKALSLKSNQALWFVEYNSPLVRLEDVLGCVRSLGFVPGVVMAQSLGVYFTIDWEEYPQTITKALEAFGTVSCEGPLSLVALVGAKLASWSMSRVFEALHRTPVLCWSQTDTVINLIINKDFGVAVTELLHDCLFK", "text": "SIMILARITY: Belongs to the aspartokinase family."}
{"protein": "MTQAADTDIRVGQPEMVTLTIDGVEISVPKGTLVIRAAELMGIQIPRFCDHPLLEPVGACRQCLVEVEGQRKPLASCTTVATDDMVVRTQLTSEIADKAQHGVMELLLINHPLDCPMCDKGGECPLQNQAMSNGRTDSRFTEAKRTFAKPINISAQVLLDRERCILCARCTRFSDQIAGDPFIDMQERGALQQVGIYADEPFESYFSGNTVQICPVGALTGTAYRFRARPFDLVSSPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDVITTPLIRDGGDPKGALVPTSWSHAMAVAAQGLAAARGRTGVLVGGRVTWEDAYAYAKFARITLGTNDIDFRARPHSAEEADFLAARIAGRHMAVSYADLESAPVVLLVGFEPEDESPIVFLRLRKAARRHRVPVYTIAPFATGGLHKMSGRLIKTVPGGEPAALDDLATGAVGDLLATPGAVIIVGERLATVPGGLSAAARLADTTGARLAWVPRRAGERGALEAGALPTLLPGGRPLADEVARAQVCAAWHIAELPAAAGRDADGILAAAADETLAALLVGGIEPADFADPDAVLAALDATGFVVSLELRHSTVTERADVVFPVAPTTQKAGAFVNWEGRYRTFEPALRGSTLQAGQSDHRVLDALADDMGVHLGVPTVEAAREELAALGIWDGKHAAGPHIAATGPTQPEAGEAILTGWRMLLDEGRLQDGEPYLAGTARTPVVRLSPDTAAEIGAADGEAVTVSTSRGSITLPCSVTDMPDRVVWLPLNSAGSTVHRQLRVTIGSIVKIGAGS", "text": "FUNCTION: Plays a critical role in M.tuberculosis ability to inhibit apoptosis of infected macrophages; thus helps the bacterium in its struggle to resist the host immune response (PubMed:17658950). In fact, via a NuoG-dependent mechanism, M.tuberculosis can neutralize NOX2- derived reactive oxygen species (ROS) in order to inhibit TNF-alpha- mediated host cell apoptosis (PubMed:20421951). Also mediates inhibition of neutrophil apoptosis, leading to delayed activation of naive CD4 T cells (PubMed:22264515). FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
{"protein": "MTGSVDRPDQNRGERLMKSPGLDLVRRTLDEARAAARARGQDAGRGRVASVASGRVAGRRRSWSGPGPDIRDPQPLGKAARELAKKRGWSVRVAEGMVLGQWSAVVGHQIAEHARPTALNDGVLSVIAESTAWATQLRIMQAQLLAKIAAAVGNDVVRSLKITGPAAPSWRKGPRHIAGRGPRDTYG", "text": "SIMILARITY: Belongs to the UPF0232 family."}
{"protein": "MNQILFIVGARGAGKTTVGKLLANELSYTFIDTDHHIQQTSNMTIADIVNQQGWQQFRQLESQALQQVTQINRVISTGGGIILSAENRQYMRQNGTVIYLQASASILAERLMQQPESTQRPSLTGKSIVEEMEEVLAARENLYCECANHIINAHLSPEKITTYVKEIMFSGIVS", "text": "FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily."}
{"protein": "MKMNITKSYVILFLVVVMTNSLSNSEVLVAPVIETAQNDVCFVPCTSRYGHYECAFDCMHKRYKDGGCVHGRCCCKT", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
{"protein": "MDYEFLRDVTGQVIVRFSMGHEVIGHWINEELKGDFNLLDRIEAGAAEVKGSERQWQLEGHEYTLLMDGEEVMIRANLLEFEGEEMEEGMNYYDEESLSFCGVEDFLQVLKAYRSFMLKY", "text": "SIMILARITY: Belongs to the UPF0231 family."}
{"protein": "MTTLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAQVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKSQILDKEGRLPDAVIACVGGGSNAIGMFADFINDASVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAHLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALKMMREHPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI", "text": "FUNCTION: The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. SIMILARITY: Belongs to the TrpB family."}
{"protein": "MIEVAEFIAREVKKGKVIEVGIGFYTRIAKRLKELGFDVLAIDINKDAVVNAKNSGLNAEVDDIFNPNISLYMGAKAIYSIRPTPEMMNYILKISKAVKVPAYIVPLTGDPVPQGMKLITYRGIPIYKWEP", "text": "SIMILARITY: Belongs to the UPF0146 family."}
{"protein": "ALPSFSRADRYGXRQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scolopendra toxin 2 family."}
{"protein": "MKLCERLRELRQERGLRLKDIAGAAQISVPYLSDLERGRTNPSLETLQSLASTYGITVHDLLEGVEFYGDQTAGALPQGLADLIADPALGAQLTPDWIRTLARIELRGKRPRDKQDWFEIYLHLKRILD", "text": "FUNCTION: Repressor specific for genes preceded by a radiation/desiccation response motif (RDRM) site, which is present upstream of several radiation-induced genes."}
{"protein": "MTFSKQLFPFVFFLLFLVSLRHASNPNNCSSSSSRPLRCGPLEVPIRFPFCNHARFNLHCTDLNKTVLELPMSGTFLVRDIDYRRQKIYINDPNCLAKRLLTFNISGSPFSPHFDILYTFLSCPNEVVLPSWYPSIPCLSNSTSSFFATSNYSLAQSMLPSCQIVKRLHVPATSPFGETRFSSDLNNQSLLLEWALPDCRAKCLGATKKTGTIYNSNIFSCSFSFLYDSRELFINGNLSSGVLVLVISLSAVTVFVFPTCIAIRLYDSERFDSAIAAATVMQQPREVMARRGLDQSTIETFKKMELGESRRLSGTNGIVCPICLSEYASKETVRFIPECDHCFHVECIDVWLKIHGSCPLCRNSCA", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily."}
{"protein": "MTEPTGDQTPEIIGVRRGMFGAKGSGDTSGYGRLVRPVALPGGSPRPYGGYFDEVVDRLAEAVGDDAFTESIERVVIHRDELTLEVHRDRLVEVAQALRDDPALRFELCLGVSGVHYPDDTGRELHAAYPLMSITHNRRIRLEVAVPDDDPHIPSLFGVYPTVDWHERETYDFFGIIFDGHPSLTRIEMPDDWVGHPQRKDYPLGGIPVEYHGAEIPPPDQRRAYN", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 30 kDa subunit family."}
{"protein": "MGGVDFEGFRKLQRADGFASILAIGTANPPNAVDQSTYPDFYFRITGNEHNTELKDKFKRICERSAIKQRYMYLTEEILKKNPDVCAFVEVPSLDARQAMLAMEVPRLAKEAAEKAIQEWGQSKSGITHLIFCSTTTPDLPGADFEVAKLLGLHPSVKRVGVFQHGCFAGGTVLRMAKDLAENNRGARVLVICSETTAVTFRGPSETHLDSLVGQALFGDGASALIVGADPIPQVEKACFEIVWTAQTVVPNSEGAIGGKVREVGLTFQLKGAVPDLISANIENCMVEAFSQFKISDWNKLFWVVHPGGRAILDRVEAKLNLDPTKLIPTRHVMSEYGNMSSACVHFILDQTRKASLQNGCSTTGEGLEMGVLFGFGPGLTIETVVLKSVPIQ", "text": "FUNCTION: Catalyzes the production of pinosylvin from cinnamoyl-CoA and malonyl-CoA, and dihydropinosylvin from dihydrocinnamoyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family."}
{"protein": "MGSSILTNRSAMTALQTLRNIDNNLDKSKDRISTGLRIGSASDNTAYWSISSMMKHDSNTMSAVVDAINLGREQVNVAATAVNLTKESLDDIQKSMVSAREKSDDDIMKIQDSIKGNMQNISNAIQSAAFGGKNILSNGGEKVGIAAGYRREGSAVYVDMIEVGGAELNFGVMGPDGTIDMTQGILKGVFGKSDKDIDAGIKTFTEAADKQKGLEDALAKAEAAVAANPNDEAAKTALEEAKKAVEDNKEDWTKAQSDFKVVADSMTLNDFVQMQGVGGLPSVAQSIILNSVQKTVRHAVDVTLTAGSKIGSAVNQVDSQLNFVKRLLDNIEAGIGALVDADMNAESAKLSALQVQQQLGIPRLFLLQIRAARIF", "text": "FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Flagella are an important component in the invasiveness of B.bacilliformis. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the bacterial flagellin family."}
{"protein": "MGQCGITSSKTVLVFLNLIFWGAAGILCYVGAYVFITYDDYDHFFEDVYTLFPAVVIIAVGALLFIIGLIGCCATIRESRCGLATFVFILLLVFVTEVVVVVLGYVYRAKVENEVDRSIQKVYKTYNGTNSDAASRAIDYVQRQLHCCGIHNYSDWENTDWFKETKNQSVPLSCCRETAKSCNGSLANPSDLYAEGCEALVVKKLQEILMHVIWAALAFAAIQLLGMLCACIVLCRRSRDPAYELLITGGTYA", "text": "FUNCTION: Regulates the proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
{"protein": "MIDKTAVIHPSSIVEEGAVIGAGVHIGPFCFVGSQVEIGAGTELKSHVVVNGITKIGCDNQIYQFASIGEANQDLKYAGEPTRVEIGDRNRIRESVSIHRGTVQGGGLSKVGSDNLLMINAHIAHDCIIGDRCILANNATLGGHVEIDDFAIIGGMTAIHQFCVIGAHVMVGGCSGVAQDVPPFVIAQGNHATPFGINIEGLKRRGFDKESLHAIRNAYKLLYRSGRTLDEVKPEIAELADQHPAVQAFIDFFARSTRGIIR", "text": "FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA subfamily."}
{"protein": "MSATLINVDDGDAMEPTLQSILDQRSLRWIFVGGKGGVGKTTTSCSLAIQLAKVRRSVLLISTDPAHNLSDAFSQKFGKEARLIDGFENLSAMEIDPNGSIQDLLAGQGEGDAGADMGGMGGMMQDLAFAIPGIDEAMSFAEVLKQVKSLSYETIIFDTAPTGHTLRFLQFPSVLEKALAKVSQLSNQYGPLLNGFLGSNGTLPNGQNLNEMMEKLETLRATISEVNTQFKDERLTTFVCVCIPEFLSLYETERMIQELASYGIDTHSIVVNQLLFPKPGSDCEQCTARRRMQKKYLEQIEELYDEFNVVKMPLLVEEVRGKERLERFSEMLVTPFVPPS", "text": "FUNCTION: ATPase required for the post-translational delivery of tail- anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the arsA ATPase family."}
{"protein": "MKCLILALICLQLSEGLVVRQILHKGKSIRERMEENGVLEDFLRYNKKADPAAKFLFNKDAVAYEPITNYLDSFYFGEISIGTPPQNFLVLFDTGSSNLWVPSTYCQSQACSNHNRFSPSQSSTFTNGGQTYTLSYGSGSLTVVLGYDTVTVQNIVVSNQEFGLSESEPTSPFYYSDFDGILGMAYPAMAVGNSPTVMQGMLQQGQLSEPIFSFYFSRQPTHQYGGELILGGVDPQLYSGQITWTPVTQEVYWQIGIEEFAIGNQATGWCSQGCQAIVDTGTFLLAVPQQYMSAFLQATGAQQAQNGDFMVNCNYIQDMPTITFVINGSQFPLPPSAYVFNNNGYCRLGIEATYLPSPNGQPLWILGDVFLKEYYSVYDMANNRVGFAYSA", "text": "FUNCTION: Hydrolyzes various peptides including beta-endorphin, insulin B chain, dynorphin A, and neurokinin A, with high specificity for the cleavage of the Phe-Xaa bonds. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MGTVNVVRVVSLHKLSWYEKFYFYSIGKGLWITLKHFIKAAILRRTVTIEYPEKKRKYSTRFRGMHTMKRDEQGRERCTSCFCCMWICPADAIYIEAGEVVPEIQHLHPEDKYAKKFEIDLLRCIFCGMCEEACPKGAIYLDGPGEMATDSREDLILTKERMMQIVGGPIIGERQ", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family."}
{"protein": "MAFRNWIGAFGKANALDVNSDLDRGYEAALLIQSLELEYYGDRPIRPDLELSVPKSVQATVLRKFRVAINVCRASLDQLEYQRSQLDPQELRQLQLIESVVNRYSPKRVSTAPTMTRDPDPLPRSLLGVFDKVRRQLNPAGEATLVAGFRRRRDSTLISLKVLLLLILVPLLVQQVSRTYIISPAVDRFAPDLPFLSYPKPQLEEQAVEKLRVYKAEIEFDALLRGDTIPSQEELQQQLGKKASELKEEADAESTHAVKNVLADISATIAFVVVCLFSREELRVLRGFFDEAVYGLSDSAKAFAIILFTDIFVGFHSPEGWTVLLDGIANHFGFPARENFILLFIATFPVILATIFKYWIFRYLNRVSPSSVATLRGMNGGG", "text": "FUNCTION: Involved in light-induced Na(+)-dependent proton extrusion. Also seems to be involved in CO(2) transport. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Cema family."}
{"protein": "MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAASSQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPRNEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPTKGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNLPRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDTDTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI", "text": "FUNCTION: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (PubMed:28793216). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.3/KCNQ3 sub-subfamily."}
{"protein": "MLFDQIASNKRKTWILLLVFFLLLALVGYAVGYLFIRSGLGGLVIALIIGFIYALSMIFQSTEIVMSMNGAREVDEQTAPDLYHVVEDMALVAQIPMPRVFIIDDPALNAFATGSNPQNAAVAATSGLLAIMNREELEAVMGHEVSHIRNYDIRISTIAVALVSAITMLSGMAGRMMWWGGAGRRRSDDDRDGNGLEIIMLVVSLLAIVLAPLAATLVQLAISRQREFLADASSVELTRNPQGMINALDKLDNSKPMSRHVDDASSALYINDPKKGGGFQKLFYTHPPISERIERLKQM", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family."}
{"protein": "MAKQYDSVECPFCDEVTKYEKLAKIGQGTFGEVFKAKHRQTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDKYELFEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF", "text": "FUNCTION: Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR and the negative elongation factors DSIF and NELFE. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co- transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement. RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription. AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect. The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation. Catalyzes phosphorylation of KAT5, promoting KAT5 recruitment to chromatin and histone acetyltransferase activity. SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus, PML body Note=Accumulates on chromatin in response to replication stress. Complexed with CCNT1 in nuclear speckles, but uncomplexed form in the cytoplasm. The translocation from nucleus to cytoplasm is XPO1/CRM1-dependent. Associates with PML body when acetylated (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus, PML body Note=Accumulates on chromatin in response to replication stress. Complexed with CCNT1 in nuclear speckles, but uncomplexed form in the cytoplasm. The translocation from nucleus to cytoplasm is XPO1/CRM1-dependent. Associates with PML body when acetylated (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MERSQDGGNLSGVQHIILVLSGKGGVGKSTISTEIALALRHAGKKVGILDVDLCGPSIPRMLNAQSKDVHQCDSGWVPVYVDQEKSISLMSIGFLLEHPDDAVVWRGPKKNALIKQFASDVAWGDLDFLIVDTPPGTSDEHIATVDALRPFNPMGALLVTTPQAVSVGDVRRELTFCKKTGLRVIGIVENMSGYVCPHCTECTNIFSKGGGEELARLSGVPFLGCVPLDPLLSQSLEQGKDFVQEFPNSAAYPAISSIARQILDMASPRS", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nubp1-nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily."}
{"protein": "MALAVLRVLDPFPAETPPLAVLLPPGGPWPATGLGLVLALRPASESPAGPALLVAALEGPGSQNGQRGPGPPQLLVSRALLRLLALGPGARVRARPVRRPPALGWALLGSAPGPGPGPRVGPLLVRRGESLPVPGSRVLETRPALQGLLGPGTRLAVTELRGRAKLGPESTQHSRLPPPPVASSFAVSHAVRQLKGVLGGTGDALGVTRSCLRGLGLFQGEWVWVARVGEFPNTSQPHLAKVQLLEPRWDLSERLGPSSGQLGEPLADGLVFVPATLAFNLGCDPLEVGELRIQRYLEGSIIPEDRGSCSLMSGPPFARELHIEIVSSPHYSANGDYDHVLYRHFHTPRVVQEGDVLCVPTVGQVEILEGSPEKLPRWREVFFKVKKAVGEAPDGPASAFLADTTHTSLYMAGSALSRVPLLPSGRSTPWDSLSPPGLEALVNELCAILKPHLQPGGTLLTGTSCVLLQGPPGSGKTTAVTAACSRLGLHLLKVPCYSLCADSSGAVETKLQAAFSRARRCRPAVLLLTAIDLLGRDRDGLDEDARVVATLRHLLLDEDPVSNCPPLMVVATTSRAQDLPTDVHTAFPHELEVPVLSEEQRLSVLQALTAHLPLGQEVNLLQLARRCAGFVVGDLYALLTHTSRVACARIRASGLAGGLSEEDEGELCAAGFPLLAEDFGQALDQLQTAHSQAVGAPKIPSVSWHDVGGLQDVKKEILETIQLPLEHPELLSLGLRRSGLLLHGPPGTGKTLLAKAVATECSLTFLSVKGPELINMYVGQSEENVREVFARARAAAPCIIFFDELDSLAPSRGRSGDSGGVMDRVVSQLLAELDGLHSTQDVFVIGATNRPDLLDPALLRPGRFDKLVFVGASEDRASQLRVLSAITRKFKLEASVSLVNVLDRCPPQLTGADLYSLCSDAMTTALKRRVRDLEEGLEMGSSALLLTMEDLLQAAARLQPSVSEQELLRYKRIQRKFAAC", "text": "FUNCTION: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling (PubMed:23929341, PubMed:9539740). Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (By similarity). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome membrane Cell projection, cilium, photoreceptor outer segment Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes. Localized at the base of the outer segment of photoreceptor cells. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MFATKILRNAQSIKNELPHREVVKMAYDLHKPRSTAIRNLNENHEEPILFMHGIFGSKKSYVQDSKLISSATHTPVYTIDLRNHGESAHAQPFDYATLAADVKEFCDSHKLDKVKLVGYSLGAKVSMLTALQYPELVKSAVIIDNAPIPQPQIQLFMKQYIKAMKTVLNEANISADDKDWKNKASAAMKRFLPNGVIRKNLLANLVNKPPKDFDSPVIDFGDGQIHFLNPIEQMEEMAVEDVTDWPTELTKDLVFEGPVKFIRGLKSPFITDEGYEAIQKHFPNNEFHDLNSSHDILDQRPTEYVKIINDFFNIHRYESAPDSTILGHKDHPQTQARRSHL", "text": "FUNCTION: Probable alcohol acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols (Probable). Not involved in the synthesis of ethyl acetate (PubMed:28356220). SIMILARITY: Belongs to the AB hydrolase superfamily."}
{"protein": "MASLVSLELGLLLAVLVVTATASPPAGLLSLLTSGQGALDQEALGGLLNTLADRVHCANGPCGKCLSVEDALGLGEPEGSGLPPGPVLEARYVARLSAAAVLYLSNPEGTCEDARAGLWASHADHLLALLESPKALTPGLSWLLQRMQARAAGQTPKMACVDIPQLLEEAVGAGAPGSAGGVLAALLDHVRSGSCFHALPSPQYFVDFVFQQHSSEVPMTLAELSALMQRLGVGREAHSDHSHRHRGASSRDPVPLISSSNSSSVWDTVCLSARDVMAAYGLSEQAGVTPEAWAQLSPALLQQQLSGACTSQSRPPVQDQLSQSERYLYGSLATLLICLCAVFGLLLLTCTGCRGVTHYILQTFLSLAVGAVTGDAVLHLTPKVLGLHTHSEEGLSPQPTWRLLAMLAGLYAFFLFENLFNLLLPRDPEDLEDGPCGHSSHSHGGHSHGVSLQLAPSELRQPKPPHEGSRADLVAEESPELLNPEPRRLSPELRLLPYMITLGDAVHNFADGLAVGAAFASSWKTGLATSLAVFCHELPHELGDFAALLHAGLSVRQALLLNLASALTAFAGLYVALAVGVSEESEAWILAVATGLFLYVALCDMLPAMLKVRDPRPWLLFLLHNVGLLGGWTVLLLLSLYEDDITF", "text": "FUNCTION: Selective transporter that mediates the uptake of Zn(2+) (PubMed:17202136, PubMed:22242765, PubMed:27321477, PubMed:28875161, PubMed:31164399, PubMed:31914589, PubMed:31979155, PubMed:33837739, PubMed:36473915). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability (PubMed:32348750, PubMed:17202136). Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher concentrations (PubMed:22242765, PubMed:31914589). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Note=Colocalized with TFRC in the recycling endosomes. Cycles between endosomal compartments and the plasma membrane in response to Zn(2+) availability. Zn(2+) deficiency promotes accumulation of SLC39A4 on the surface membrane, whereas high extracellular Zn(2+) levels induce internalization of SLC39A4, but also trigger drastic removal of cellular SLC39A4 via proteasomal and lysosomal degradation pathways. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MTTEGGPPPAPLRRACSPVPGALQAALMSPPPAAAAAAAAAPETTSSSSSSSSASCASSSSSSNSASAPSAACKSAGGGGAGAGSGGAKKASSGLRRPEKPPYSYIALIVMAIQSSPSKRLTLSEIYQFLQARFPFFRGAYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPMYHRVVSGLGFGASLLPQGFDFQAPPSAPLGCHSQGGYGGLDMMPAGYDAGAGAPSHAHPHHHHHHHVPHMSPNPGSTYMASCPVPAGPGGVGAAGGGGGGDYGPDSSSSPVPSSPAMASAIECHSPYTSPAAHWSSPGASPYLKQPPALTPSSNPAASAGLHSSMSSYSLEQSYLHQNAREDLSVGLPRYQHHSTPVCDRKDFVLNFNGISSFHPSASGSYYHHHHQSVCQDIKPCVM", "text": "FUNCTION: Probable transcription activator for a number of lung- specific genes (PubMed:8626802). Mediates up-regulation of the E3 ligase IRF2BPL and drives ubiquitination and degradation of CTNNB1 (PubMed:29374064). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLQLMKQLYEKPAVKWTCHTGFYLMILLVLFFMYGFHTANTGSYIYNDF", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MKLNSNINNNINNSSNSNNNFDAKNIIVDTITPPDPSVEFERKLAKSIFCLVHFIVYCVIIFRKGTILDQAFKDKDYFYLIWTHCVFFFAIGTYFLISSKRPGFVSLSNQNLNNNNNNNGSSNKFILEDSMGCIPQLNINPTPNYSKISNIKRKLKNSSGDITKNQENEDLVPLMEISKNIDEDSINDDTITTTTTTTTTTSTSTIPEISNDDDDNNNENNNDNVNNRNNNNSNGEKEDNDIDKLKNHYFCKKCLVDIPLRTKHCVKCNRCVLKYDHHCVFIGGCVGLNNHKNFLLFLLAESLLLLLGLRIIVTGFVRENSIKEWIFSNIAIIPPTLLIFGGLCMPFALFCFHSFLILTNQSSWEFNKYQRITYLKPFSKRGINPFNKGPWNNLKKFLKGDENPSDWILLSKYEVDQMKKKEENTFNIWNNKYYSCCG", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MTVAYFDCPAGVAGDMCLGALLDLGVPLDYLQSQLAKLGIANEFELTTETVQRRGQRGLKAQVHLRDRHGHHHRHWPEIADQICAAHLPDRARDWSLKVFEALAIAEGAVHGIEPEKVHFHEVGAVDALVDIVGTCLGLDYLDVRQVYCSALPTGGGTVKAAHGQLPVPVPAVLELCQRYRVPLYSNGIEKELVTPTGAALVCALSAGFGAPPAMTLQRVGLGAGTQELPLPNLLRLWLGTVPAPPETGTAKTIVELQTQLDDMPPQALSYACEQLYAAGALEVFCQPITMKKSRLGVLVTVLCPPSAEAACVQTLFRETTTLGLRRQVQERYILERQMREIPTPFGTVRVKVAEHQGQRLNVQPEYEDCAALARQHQQPWQVVYQEALAVALKLWPLG", "text": "SIMILARITY: Belongs to the LarC family."}
{"protein": "MPPRRYNPDTRRDELLERINLDIPGAVAQALREDLGGTVDANNDITAKLLPENSRSHATVITRENGVFCGKRWVEEVFIQLAGDDVTIIWHVDDGDVINANQSLFELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQAVEKASWLHPDAPVEVEVENLEELDEALKAGADIIMLDNFETEQMREAVKRTNGKALLEVSGNVTDKTLREFAETGVDFISVGALTKHVQALDLSMRFR", "text": "FUNCTION: Involved in the catabolism of quinolinic acid (QA). SIMILARITY: Belongs to the NadC/ModD family."}
{"protein": "MAINQGKYKPSICAIDEVDDRSFKLHNSQDEIGGKQQLQQIEGSETAPLTTNQQKLHMDDGSHLTPKDLEAARQDALNEVAAGGAGGRTPAAITPNSTHPSANGLRALLLPGRRSFDALMSLSRKRRILYVTTACLCALLLLIIILLLAFWPEVPFYLRAPLCLDKECVESSRQLLLWANTSKSPCHETYEWACGNFASDYANHEYFVIKRGEWNYETYNEYQELNELNRFIAMLPNSQEGSVESTVSSLYRSCRETDVLDKSQSDLLLKRAINAVYGWQAFRDSNRLQSWEYKRVLVVLQAKHGIFPYYRVTVENGFSNPHDYVITLDEGELGLPDKYFYGNDADEEVVRGYKLLLRDFAINMGIVSREADLFADDIFHYERRIVNHIEDAKADANRPINKLMRLADLKIKAPSLPILESLQAIFPKTKITEDTEVLVRDPEVMHALSVLLSTSDKKPINNFIVWSLARKMLPHLSKEYRTLAETFDHALYGRTASYPRWLICSKVVRDWLPFAVDALQQQPPRQQFETMTSKSRGLNKTQGNEELLKLMFFSLRNQLKDSLEQAKWLEPAARQFIQKKLNEMRLQFGIPDEVLQQPTYLAQYYNELILNNVFFVEHLEWIWTFRRSQMEKKLGPLAILDVIVSEMYTRDNPQAIAYSNKLNMLLVSKVLISSNYYDYRYPVAVNFARIGTDILEALIDNFSTFLLQFNTQSTDISDAAPEIRYAQPDVNCLAAGQPPRLVHELNELSSNALKSFHVTLSAARTAARALSNFVNAIDAGSAIQGSGIDQANTYEALGLTRRLRIPGLRSFNENELFTLSYMQQHCSTTIADKDYARIKPLVESQLAESYLFNATWQHIQFLPRSTNCAAAEATCSNLL", "text": "FUNCTION: Plays a role in the ovary in limiting the number of primordial germ cells (PGCs) that develop directly into gametes, allowing them instead to enter the developmental pathway that produces germline stem cells (GSCs) from PGCs and ensuring lifelong production of gametes from these GSCs. Negatively regulates epidermal growth factor receptor (Egfr) signaling. Probably down-regulates EGFR signaling on intermingled cells, a type of somatic stromal cell which contacts PGCs, and the resultant low level of signaling limits the proportion of PGCs which start gametogenesis, maintaining them in an undifferentiated proliferative state. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Note=Not uniformly present at the cell membrane but is concentrated at the interface between germ cells. SIMILARITY: Belongs to the peptidase M13 family."}
{"protein": "MDLTQFNTAGIVWPTVAAIAISYILLSSFLSWYRLRHIPGPFLASISSLWNVLNIVTGRTSPVLEKLPGKYGPLVRTGPNYVLTDDAEILRHVNGARSTYPRNGWYEGFKVDEHDHMGSHIDTSVHDAIKSKVIGGYNGKDGIDLEGAIGSQVKTLVSEIRRRHLGQPVDFSRLMRQMALDAITAVAFGEALGFLTAEDGDVFGYVSAVDKMLTYLTLASDLPVVRSVVRSRRMAPAVRCVLAYTGIGRMLNHTRRVVAERYAADDPGKGDMTASFIRKGLTQIECEGESHLQLIAGADTAVTVLRSTLLYIMTTPRVYTRLKAEIKAAVDAGEVVEVITMAQAQRLPYLQAVVLEGFRMRPAVVYGHFKSVPAGGDTLPNGVRLPAGTAIAPNYIALTRRADVYGADVDLFRPERFLDAEPAKRHEMERAMDLNFGLGRWQCAGRNIALMEMNKVFFELLRHFDLQILYPGKAWDEYTGVVYSQHNMWVQITESS", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 (PubMed:15654104). Lolines are structurally differentiated by the various modifications of the L-amino group and include norloline, loline, N-methylloline, N-acetylloline, N- acetylnorloline, and N-formylloline (PubMed:15861432, PubMed:25531527). The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP (PubMed:15861432, PubMed:16755627). Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo- acetamidopyrrolizidine (AcAP)(PubMed:24374065). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo- acetamidopyrrolizidine (AcAP) (PubMed:29537853). In sequential 2- oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines (PubMed:24374065, PubMed:29537853). The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation (PubMed:15654104). Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines (PubMed:25531527, PubMed:18655839). LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N- methyllonine (NML) by lolM (PubMed:25531527). LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) (PubMed:18655839). A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) (PubMed:25531527). LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate (PubMed:15654104). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MTATQKHNLFTPEPHYIPGYAGFYPQLRYQVGNTYGRTTAQLLTDPSVQKSPCSVLSPMTKPKFIEDFSKSKPPWIPCRDLREPYIPHYTSLKPYKNFEILGQLPRQDVDTQGPPQVENRQGPLTAGFMPYPPYPACPPGRKGEARDLGHPGLLLAYGEEAWKDAAPLQDTPGKNNQLYHCRRDEYLPPHPPQETLDVGRFQRLPQLDHPNLIQRKAISGYAGFVPRFAWVMGMNYRDGVTQAMDDFDKNQFVFRHPVCALGERLPRTHWPNTTIYRSQGLIPFYMGFIPSMQDNYALTFGNSTRRAYQKELDRRSHTL", "text": "SIMILARITY: Belongs to the UPF0605 family."}
{"protein": "MTLALAPTDRPYLPRGVRLVTDRVRGGIVLLAPEKAVALDAVGEAILSRVDGQTSLAALVDQLVEAYDAPREQIEQDVQAFLQGLRARMFLMVAP", "text": "FUNCTION: Functions as a PqqA binding protein and presents PqqA to PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway. SIMILARITY: Belongs to the PqqD family."}
{"protein": "MSSGKKPVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI", "text": "FUNCTION: A highly abundant probable chromatin protein, it binds double-strand DNA without sequence specificity; there is approximately 1 Cren7 molecule for 12 bp of DNA. Constrains negative DNA supercoils, increases DNA stability against thermal denaturation. Binding does not require protein methylation. Binds single-strand DNA weakly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cren7 family."}
{"protein": "MIARILAALADSMEMPVAAGGGSVLGTIKIAVMPIAKVFTMCFLGLLMASKYVNILPPSGRKLLNGLVFSLLLPCLIFSQLGQAVTLQKMLQWWFIPVNVVLGTISGSIIGFIVASIVRPPYPYFKFTIIQIGVGNIGNVPLVLLAALCRDTSNPFGDSEKCSIDGTAYISFGQWVGAIILYTYVYQMFAPPPEGFDAEEENLALKTLPVDAAPEQVPLLTQNFPKDFSPTQDLLPVQSTEPRGRGVSRKGKIAQIFVFLYEKLKLKQIVQPAIVASILAMILGAIPFTKKLIFTNGAPLFFFTDSCMILGDAMIPCILLALGGNLINGPGSSKLGFKTTAAIIIGRLVLVPPVGLGIVTVADKLGFLPADDKMFRFVLLLQHTMPTSVLSGAVANLRGCGRESAAVLFWVHIFAIFSMAGWMVLYINILF", "text": "FUNCTION: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.2) family."}
{"protein": "MDDLVFAGNKALYLVLILSGWPTIVATIIGLLVGLFQTVTQLQEQTLPFGIKLLGVCLCLFLLSGWYGEVLLSYGRQVIFLALAKG", "text": "FUNCTION: Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FliQ/MopD/SpaQ family."}
{"protein": "MSDLGAVVALLLWGQLFAVDSGNDVTDIADDGCPKPPMIANGYVEHLVRYQCKNYYRLRTEGDGVYTLNNEKQWTNKAVGDKLPECEAVCGKPKNPADAVQRILGGHLDAKGSFPWQAKMVSRHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLYPNYSQIDIGLIKLKQKVPVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFNFTDHLKYVMLPVADQYDCIKHYEGSTVPEKKTPKSPVGEQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEKDTWYAAGILSFDKSCGVAEYGVYVKATSIQDWVQKTIAEN", "text": "FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MKKKDTCEIFCYDEEKVNRIQGDLQTVDISGVSQILKAIADENRAKITYALCQDEELCVCDIANILGVTIANASHHLRTLYKQGVVNFRKEGKLALYSLGDEHIRQIMMIALAHKKEVKVNV", "text": "FUNCTION: Metal-binding repressor for the cad operon. Involved in resistance to heavy metals, such as cadmium, bismuth, zinc or lead. Binds 2 metal ions per subunit. Metal binding to the N-terminal regulatory site causes the repressor to dissociate from the DNA."}
{"protein": "MKLVFRWYGEKHDTVTLEQIRQIPGVEGVVGALFDIPVGEVWPLEEIMKLKETVEKAGLKLEVIESVNVHEDIKLGLPTRDRYIENYKETIRNLAKAGVKVVCYNFMPVFDWMRTDLHKKLPDGSETMEYDHRLIEGVTPDELIKRVKEGSQGFVLPGWEWDRLEKLRETFELYKNVDEEKLFENLVYFLERVIPVCEECDVKLAIHPDDPPWSIFGLPRIITNKENIERMLKAVDSPYNGITFCMGSLGANPENNIPEMIRYFGKMGRIHFAHVRNLKFTGEKSFYETAHPSFCGSHDLFEVMKAFHDIGYEGYIRPDHGRLIWGEKARPGYGLYDRALGATYILGLWEAIDKMKKRYC", "text": "FUNCTION: Catalyzes the dehydration of D-mannonate. SIMILARITY: Belongs to the mannonate dehydratase family."}
{"protein": "MASLGQIIFWSIINIIIILAGAIALIIGFGISGKHFITVTTFTSAGNIGEDGTLSCTFEPDIKLNGIVIQWLKEGIKGLVHEFKEGKDDLSQQHEMFRGRTAVFADQVVVGNASLRLKNVQLTDAGTYTCYIRTSKGKGNANLEYKTGAFSMPEINVDYNASSESLRCEAPRWFPQPTVAWASQVDQGANFSEVSNTSFELNSENVTMKVVSVLYNVTINNTYSCMIENDIAKATGDIKVTDSEVKRRSQLQLLNSGPSPCVFSSAFVAGWALLSLSCCLMLR", "text": "FUNCTION: Negatively regulates T-cell-mediated immune response by inhibiting T-cell activation, proliferation, cytokine production and development of cytotoxicity. When expressed on the cell surface of tumor macrophages, plays an important role, together with regulatory T- cells (Treg), in the suppression of tumor-associated antigen-specific T-cell immunity. Involved in promoting epithelial cell transformation. SUBCELLULAR LOCATION: Cell membrane; Lipid- anchor, GPI-anchor Note=Expressed at the cell surface. A soluble form has also been detected. SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family."}
{"protein": "MLGLLVALLALGLAVFALLDVWYLVRLPCAVLRARLLQPRVRDLLAEQRFPGRVLPSDLDLLLHMNNARYLREADFARVAHLTRCGVLGALRELRAHTVLAASCARHRRSLRLLEPFEVRTRLLGWDDRAFYLEARFVSLRDGFVCALLRFRQHLLGTSPERVVQHLCQRRVEPPELPADLQHWISYNEASSQLLRMESGLSDVTKDQ", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the THEM6 family."}
{"protein": "MEKTQSVFIRFIVNGSLVKQILIGLVAGIVLALVSTPAAIAVGLLGSLFVGALKAVAPVLVLMLVIASIANHKKGQKTSIRPILFLYVLGAFSAALVAVVVSFIYPSTLILVAESADITPPSGIVEVLHGLLNSIIANPIHALLNANYIGILAWAVGLGIALRHAADTTKALINDMSDAVTLVVRVVIRFAPLGIFGLVASTIAATGFGALQLYVQLLVVLIGCMLLVALVVNPLIVYWKIRRNPYPLVFACLRESGVTAFFTRSSAANIPVNMEMCKKMNLNEDTYSISIPLGATINMAGAAITITVLTLAAVHTLGITVDLPTALLLSVVAAVCACGASGVAGGSLLLIPLACSMFGIPNDVAMQVVGVGFIIGVLQDSAETALNSSTDVLFTAAVCQAEDAKLANPDALAAGKSV", "text": "FUNCTION: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family."}
{"protein": "MFENILTKIFGSKNERDLKRLQPLVAHIGSLESELETLSEEQLAGKTVEFRQRLAEGASLDSLLPEAFAVVREAGKRVLGMRHFDVQLIGGMVLHKGKIAEMKTGEGKTLVATLAAYLNALPAKGVHVITVNDYLASRDAEWMGRIHRYLGLTVGCIVHGLDDRQRKEAYACDITYGTNNEFGFDYLRDNMKFSLDDYVQRPLSYAIVDEVDSILIDEARTPLIISGPSESSSELYYSVNRIIPMLEKGETIESRDGRVGQTVREYTGDFTIDEKAKTASLTEDGVAKVERLLGVENLYDPGNIELLHHVNQALKAHALFKRDVDYVVKDGEVMIVDEFTGRLMPGRRWSDGLHQAVEAKEGVKIESENQTLATITFQNYFRMYDKLAGMTGTADTEATEFNQIYSLDVMVIPTNRPLARKDEGDVIYKTNREKFLAVVEDIIERHAGGQPILVGTISIENSEVLSSMLRKRGVPHNVLNAKHHEREAEIVAQAGRKGAVTIATNMAGRGTDIILGGNPDLLAQRESAGAENPEAALAQALVKYQEVCAQEKQDVLAAGGLYILGTERHESRRIDNQLRGRAGRQGDPGASRFYLSLEDDLLRIFGSHRVAYIMDRLKIPEGEPIEHRFISKAIANAQKKVEAHNFDIRKHLIEYDDVMNTQRNVIYAQRREVLGGEQLPETFAAIIDEMVEDIVATFCPEKSAPEDWGWASLNEDFFSQFNMPPAPLEVPASDLTPTVMLEHLKQQVDARLQEREAEFTPPVMLHLMKVLLLQTIDAQWKDHLLSIDHLKEGIGLRGYAQRNPKEEYKREAYELFLQMMGRIRQEVVQKLFRIQLAKEQDVERMEQRQRRHRISLNRAGGEAEAAKPVVRDEKKVGRNDPCPCGSGLKYKKCCGQ", "text": "FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Note=Distribution is 50- 50. SIMILARITY: Belongs to the SecA family."}
{"protein": "MGFRLPGIRKTLSARNEASSKVLDAPKGYLAVYVGENMKRFVIPVSHLNQPLFQDLLSQAEEEFGYDHPMGGLTIPCSEDLFQHITSCLSAQ", "text": "SIMILARITY: Belongs to the ARG7 family."}
{"protein": "MALGWYELKLAKDGQFMFNLKAANSQVILTSELYRSRSAAENGIASVQKNGLDEKNFEVRVAKNDKPYFVLKAKNHQEIGRSQYYSSSVSAKKGIVSVTKNAASTVIKDLTNEA", "text": "SIMILARITY: Belongs to the UPF0339 family. Duplicated subfamily."}
{"protein": "MAIEQTAITRATFDEVILPIYAPAEFIPVKGQGSRIWDQQGKEYVDFAGGIAVTALGHCHPALVNALKTQGETLWHISNVFTNEPALRLGRKLIEATFAERVVFMNSGTEANETAFKLARHYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPSDIIHVPFNDLHAVKAVMDDHTCAVVVEPIQGEGGVTAATPEFLQGLRELCDQHQALLVFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKALGGGFPISAMLTTAEIASAFHPGSHGSTYGGNPLACAVAGAAFDIINTPEVLEGIQAKRQRFVDHLQKIDQQYDVFSDIRGMGLLIGAELKPQYKGQARDFLYAGAEAGVMVLNAGPDVMRFAPSLVVEDADIDEGMQRFAHAVAKVVGA", "text": "FUNCTION: Involved in both the arginine and lysine biosynthetic pathways. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily."}
{"protein": "MLRFNLIVAVCENFGIGIRGDLPWRIKSELKYFSRTTKRTSDPTKQNAVVMGRKTYFGVPESKRPLPDRLNIVLSTTLQESDLPKGVLLCPNLETAMKILEEQNEVENIWIVGGSGVYEEAMASPRCHRLYITKIMQKFDCDTFFPAIPDSFREVAPDSDMPLGVQEENGIKFEYKILEKHS", "text": "FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). FUNCTION: By interacting with vestigial (vg), may control genes involved in DNA replication. SIMILARITY: Belongs to the dihydrofolate reductase family."}
{"protein": "MSGMEVWSDPPRSCRMEQPATQQVATCSFPQNIKEENAYCLYDSEKCPKSAAATDLSTFPRLTSESCSNNDTTTSGGVPVPGYFRLSQAYPTSKQTLYSNTGQVGASPFVPQSQIRFGTPPSSASTPTELGRKGSEGTSPGHLTCSSEREEAEAAASSANEESSPVPSESNKNSPEKETKGEVKAENGANWLTAKSGRKKRCPYTKHQTLELEKEFLFNMYLTRERRLEISRSVHLTDRQVKIWFQNRRMKLKKMNRENRIRELTANFSFS", "text": "FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Abd-B homeobox family."}
{"protein": "MSRRRTAKKRIVMPDPVYKNSLLELIVRQVMRNGKKLLAYRIMYNSMIKIAEMTQKDPLDVLEKAIRNVTPLIEVKARRVGGSTYQVPLEVLPERGTTLAIRWILAACRKNRGKPMYIKLTNELIDASNKSGSAIKKKDEIHRMAEANKAFAKQRF", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MDGFSGGIDINIFDSNSTENGSGDFEDFSEPCFMHDNSDFNRIFLPTIYSFIFLLGIIGNGLVVVVMGYQKKSRTMTDKYRLHLSVADLLFVFTLPFWSVDAAIGWYFKEFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQGSRKMLADKVVYAGVWLPALLLTVPDLVFARVSDENGQFVCDRIYPIDNRETWTVGFRFLHITVGLILPGLIILICYCVIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYVCLTTDTFMLLGLLKADCIWENTLHKAISITEALAFFHCCLNPILYAFLGAKFKTSAQNAFTSVSRGSSLKILSKKRAGLSSVSTESESSSFHSS", "text": "FUNCTION: Receptor for the C-X-C chemokine cxcl12/sdf-1. Transduces a signal by increasing the intracellular calcium ion level. Signaling with cxcl12/sdf-1 mediates the directional movement of mesodermal cells during gastrulation. May play a role in the migration of embryonic presumptive primordial germ cells (pPGCs). May also be involved in regulating migration of hematopoietic stem cells into the larval liver (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm Nucleus Early endosome Late endosome Lysosome Note=Expressed in the cytoplasm of a small number of embryonic pPGCs from stage 24. Expressed in the nucleus of 3 lateral pPGCs (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSYIDYLAYTGNTTFYDRFDGDLTSEHRIKCIINGCLINIMFSIRTIKEFPEEIKICQAAVSKFLTCGYVNDYLIEKYPPFYLWHKRFCDYDIYKMLMEKHPKLNYTVAKAAIMQRYNDLYFSFDFQPEEELIMTAALTENTEIYEDQINKAKKLGYCYSYLDYDNYCIKEEPGIEEIPDIEPKFNPFYVYVESGSKMEDVEYAVVNLVEEFKYLQMVYDMSKI", "text": "FUNCTION: The presence of the two linear plasmids, termed pGKL1 and pGKL2, in strains of Kluyveromyces lactis confers the killer phenotype to the host cell, by promoting the secretion of a toxin able to inhibit the growth of sensitive strains."}
{"protein": "MEMKIDALAGTLESSDVMVRIGPAAQPGIQLEIDSIVKQQFGAAIEQVVRETLAQLGVKQANVVVDDKGALECVLRARVQAAALRAAQQTQLQWSQL", "text": "FUNCTION: Covalent carrier of the coenzyme of citrate lyase. FUNCTION: Covalent carrier of the coenzyme of citrate lyase. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CitD family. SIMILARITY: Belongs to the CitD family."}
{"protein": "MIRNLTLLSKSSLDPKCLILKHSNKNLNNYFKQITFRYYSKTNPIIKQQNHNNINNYNNTTPETQERINELLKLFPPIKYGFAYGSGVISQKGYNRNGDGSTSTENPSKKEEQSPMIDLIFAVENSTKWHSLNLVNNQSHYSFLGLMGAHIVAKVQYMNAKIYFNTLLEHNGIKFKYGVIEYKDLIDDLKNWKTLYLSGRMQKPIFNLPTSSTEGLKEIQEINSEYNLKNAVITSLLMLPETFTEYDLYHTISKLSYSGDIRMKGAENPMKTHNIVINNIDGFRSLYFPIINDHLTQYLNVILENGDEVNSSLILSQNNNNKNNNKNETTTTAAPKMVTFKSKQDPMNYLNLLMMLPGSIKSTMLKEVRNNMKLMKSDEKIDPTILHNLIFMIVSKSSFAQTVKGVFTAGISKSLNYMKLKLKKNKK", "text": "FUNCTION: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. Required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the TAM41 family."}
{"protein": "MKVPVSGDVKEETEEENVEQEENQEAKVSLKPVIEDLSMELARKCTELISDIHYKEEYKKSKDKCTFVTDTPMLNHVKNIGAFISEAKYKGTIKADLSNCLYKDMPATIDSVFAREVSQLQSEVAYKQKHEAEKGFSDYTHMKEPPEVRRAMEVNRHQSNISYRKDMQGTHTYTAELDRPDIKKATQISKIISDAEYKKGQGIVNKEPSVIGRPDFEHAVGASKLSSQVKYKEKFDNEMKEKSHHYNPLGSAFFRQHQFAAVLASDWEYKRDFEENKGLYHFDAEAPEHLHHKGNATLQSQVKYREEYEKNKGKSMLEFVETPSYQSSKEAQKMQSEKVYKEDFEKEIKGRSSLDLDKTPAFLHVKHITNLMREKEYKKDLENEIKGKGMELSSEVLDIQRAKRASEMASEKDYKRDLETEIKGKGMQVSTDTLDVQRAKRASEMASQVRMV", "text": "FUNCTION: Binds to actin and plays an important role in the assembly of the Z-disk. May functionally link sarcomeric actin to the desmin intermediate filaments in the heart muscle sarcomeres. Isoform 2 might play a role in the assembly of focal adhesion (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAEPVGKRGRWSGGSGAGRGGRGGWGGRGRRPRAQRSPSRGTLDVVSVDLVTDSDEEILEVATARGAADEVEVEPPEPPGPVASRDNSNSDSEGEDRRPAGPPREPVRRRRRLVLDPGEAPLVPVYSGKVKSSLRLIPDDLSLLKLYPPGDEEEAELADSSGLYHEGSPSPGSPWKTKLRTKDKEEKKKTEFLDLDNSPLSPPSPRTKSRTHTRALKKLSEVNKRLQDLRSCLSPKPPQGQEQQGQEDEVVLVEGPTLPETPRLFPLKIRCRADLVRLPLRMSEPLQSVVDHMATHLGVSPSRILLLFGETELSPTATPRTLKLGVADIIDCVVLTSSPEATETSQQLQLRVQGKEKHQTLEVSLSRDSPLKTLMSHYEEAMGLSGRKLSFFFDGTKLSGRELPADLGMESGDLIEVWG", "text": "FUNCTION: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT- driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity). Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus."}
{"protein": "MGSTKHWGEWLLNLKLAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAARFVAEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLARRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIRKRVVACAAVFYGFAVHMKIYPVTYILPITLHLLPDRDNDKSLRQSRYTFQAHLYELLKRLCDRAVLLFVAVAGLTFFALSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQFILLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMTWKRAVVLLMLWFIGQALWLAPAYVLEFQGKNTFLFIWLAGLFFLLINSSILIQIISHYKEEPLTERIKYD", "text": "FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN- acyl-PI during GPI precursor assembly (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGM family."}
{"protein": "MASWLKAAEDLFEVVDRRAKSVVEDLSEEQNDLQLPASGRKGSQGKRTSSKKKKLVKEESSNKRDSSGDQSGPGVSQSEVPPSKSSVSTDETSSSGPVLLTREIHPTDADVQSVLSLPLSVADTKSDDAAVVAQESIVDGDRSESKHADGDIPNDSLVQPSPSLPDKEIEVVVSENLMDAPKNGTQRELDDSSKRDVENLDSVVHAPSVNEGNVAQSTGDEVKVGTSINLEKEQEPKVPVTSTNLKREQDRRADTTSMKIQDQLEEAQGLLKATVSTGQSKEARLARVCAGLSSRLQEIKAENAQLEELLTAEQELTKSYEASIRHLQKDLSAAKSEVTKVESSMVEALAAKNSEIETLVSAMDALKNQAALNEGKLSSLQGDMESIMRNRELAETRMMQALREELATTERRAEEERSAHNATKMAAMERERELEHRAVDASTALVRIQRIADERTAKVADFEQKVALLEAECTSLNQELQDMEVRARRGQKKAPDEANQVIQIQAWQDEVDRARQGQRDAEEKLSLMEAEMQKLRVEMAAMKRDAEHYSRQEHTELEKRYRELTDLLYYKQTQLETMASEKAAAEFQLEKEVKRLHEAQVEVEKSRVSRRASATWEEDSEIKTLEPLPLYHRHMATASTQLQNAVKLLDSGAVRATRFLWRYPIARMFLLFYLVFVHLFLMYLIHRLQEQAEAQEVAAMTNNVFRL", "text": "FUNCTION: Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Note=Probably located to cisternal rims of cis or medial Golgi."}
{"protein": "MDELGIPIYKRGFPEHLLHGYEFTIDSSTKIQSVGGRHDVTKLPEMNAYDIKSEGMRTALWYNPVRNDGFVLPRVLDITLRGYDGKRAVIDSSRHKSFHTDERWVQWMMKDSMDAQPLKVGLDDQTQKIAHSLHNCVVKIDSKKADTMSYHIEPIEDSLKGCLHTRTMLWNHLVRVEMSHAAQEIAYALKPTYDIVVHAERRDRSQPFRPGDQTLINFSRGQKVQMNHNSYEKMVEGLAHLVIRGKTPELIRDEITKLDEICNRWIRSRYDPGEIKAYELCKVLSTVGRKMLDQEKEPADEANLSIRFQEAIDNKFRQHDSERLKIFEHRNQRRDEDRFYILLMIAASDTFNTRVWWSNPYPCLRGTLIASETKLGDVYSMMRLWYDWSVRPTYIPYEKSREQEKYIYGRVNLFDYVAEPGTKIIHWEYKLNQQIKDITYEQGNPCDLFPDDDEAIVTKFDDVAYGQMVNDLINGGWDQERFKMHKILKSQGNVLTIDFEKDAKLTSNEGVAMPEYFDKWIIAPMFNAKLRIKHGEIAQRRNDDPMVKRTLSPIAFAPIVLQRLTLARFYDIRPAIMGQALSRQQGQSTYDEEISKIEGYAEILQRRGIVQIPKKPCPTVTAQYTLERYALFLINILEQHIIQSTDEDVMYSHPRVDYKLEVHGENIIDISQIVIFVFDFLFERRRTVRGVYESRYMVTRIRDAQGQNRINVITEFFPTFGYHLSRVKEATIIQEIMYLNFLPLFFLVSDNIIYTHKQWSVPLFLYAHELKVIPLEVGSYNDRCSLVSYIEYMVFFPSKAFRTSKLDEVQPKIAREMLKYYINTKIFEGGINLNVVTTKQLLYETYLASICGGLSDGIVWYLPITHPNKCLVAIEVSDERVPASIRASHIKLRFPLSVKHLKGIVIIQVDEEGKFTVYSEGIVSHRVCKKNLLKYMCDIVLLKFSGHVFGNDEMLTKLLNV", "text": "FUNCTION: The VP2 protein is one of the two proteins (with VP5) which constitute the virus particle outer capsid. It is the major target of the host immunogenic response. Responsible for viral attachment to target host cell, probably by binding to sialic acid. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the orbivirus VP2 family."}
{"protein": "MAESLRSPRRSLYKLVGSPPWKEAFRQRCLERMRNSRDRLLNRYRQAGSSGPGNSQNSFLVQEVMEEEWNALQSVENCPEDLAQLEELIDMAVLEEIQQELINQEQSIISEYEKSLQFDEKCLSIMLAEWEANPLICPVCTKYNLRITSGVVVCQCGLSIPSHSSELTEQKLRACLEGSINEHSAHCPHTPEFSVTGGTEEKSSLLMSCLACDTWAVIL", "text": "FUNCTION: Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Isoform 2 is sumoylated and mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, PML body. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus."}
{"protein": "MPTQRDSSTMSHTVACGGGGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCSEVRDMCSFDNEQPFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPPEPMMPMDQSSMHPDHTQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV", "text": "FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine- protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity (By similarity). Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (PubMed:27498875). SUBCELLULAR LOCATION: Cytoplasm Membrane Endosome Nucleus Note=Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily."}
{"protein": "MSAATVILILLMLLGILGRSNVIAAAAAFLLLLQFTSLQRFYPILERRALEAGLIFLVVSVLVPFASGRVAPRDMLQSFVSLPGLIAIASGIIATHMNCQGLELLQRFPQMMIGMVIGSIIGVAFFGGIPVGPLMAGGIAALLVHLMAWLR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0756 family."}
{"protein": "MSDDRINYLKNKLVQYPDFPKKGILFEDIMPIFQDPRAFGILIDLLLEAVETEFNNIDVIVGLEARGFLFGPTLALRANCAFVPVRKPNKLPGDLVVVSYNKEYSTDSFAIQKGTIKPGQRVLIVDDILATGGTALAADELVTRLGGELVGHLFLLELTFLQGRKRLMAPTYTLLTGQDEAPDGSEFA", "text": "FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MEFSEWYSDILEKAGIYDLRYPIKGCGVYLPYGFKIRRYSFEILRKLLDETGHDETLFPMLIPENLLAKEGEHIKGFEDEVFWVTHGGKTPLEVKLALRPTSETTMYYMMKQWIKVHTDLPLKLYQVVNTFRYETKHTRPLIRLREIMSFKEAHTAHATKEDCDAQIKEALNLYGEFFDEICVPYIISKRPEWDKFPGADYTMAFDTIYPDGKTMQIGTVHNLGQNFAKTFELEFETPDGEKDFVYQTCYGISDRAIASLISVHGDEKGLVIPVDVAPIQIVLIPLLFKGKEEIVMEKIKELNSTLKSEFRVHLDDRDIRPGRKYNDWEIKGVPLRIELGPRDIENGQALIVRRDTGEKITVEYSNILEEVEKIVSMYKENLKIKADEKIKNFLTVVDFESDVNALSEKVKAALLENKGIILIPFDESVYNEEFEELIDASVLGQTTYEGKDYISVARTY", "text": "FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily."}
{"protein": "MEEQQAAAAGGGGGGGGASMCANGCGFFGSEATKKLCSKCYRDQLKAAPSSPPAAPDLVANEEEEASTAAAAAADEQLALCSSGCGFFGSKETNNMCSKCYRDHLKATSPLFSSSSSPATASTTDITVPIAPATTAPTPSLKGKEEEATAAASSSAAAAAKPNRCVACRKKVGLLGFECRCGGTFCSTHRHADKHACTFDFKKSDREKIAKENPLIVAPKITKF", "text": "FUNCTION: May be involved in environmental stress response."}
{"protein": "MPYGKIEDIKTSGASDVTAAQDGLKEGGWKSSHRMAEIDSNRMENYRTIINEAGRQCDVDPAVIAGIISRESRAGNQLINGWGDHGKAFGLMQIDVTPPPNGGGHTPVGTWDSLEHLIQATEILVEFIERIKTKFPRWNADQHLKGALAAYNKGEKNVESYASVDAKTTGKDYSNDVVARAQWYKSNMGF", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 23 family."}
{"protein": "MKLMYKIAVIGDKDSVLAFKILGVDVFITLDAQEARKTIDRIAKENYGIIFVTEQLAKDIPETIKRYNSEIIPAVILIPSNKGSLNIGLTNIDKNVEKAIGSKIM", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase F subunit family."}
{"protein": "MYIVIMGAGRIGTLVARMLESEGHDVAIIEMNRERAREISEYISGLVIEGDATDQKVLENANIKNANAFAALTGKDDANILACILAKHLNPNIMTILRITDPGKKKIFEDVKELKTYFDIVVSPEDIAANYIFRTLVTPGFNRVLLPREGAEIIQFQIDEDCEVAGKPVKELNLPKDSLIIAVYDEKGNLTIPSGDTIIPKKGQVIIFAKNSALQEVKKIMEKKKKEQ", "text": "FUNCTION: Part of a potassium transport system."}
{"protein": "MIGNSSKDNFGQQQKLSRGLKNRHIQLMAIGGAIGTGLFLGSGKSIHFAGPSILFAYLITGVFCFFIMRSLGELLLSNAGYHSFVDFVRDYLGNMAAFITGWTYWFCWISLAMADLTAVGIYTQYWLPDVPQWLPGLLALIILLIMNLATVKLFGELEFWFALIKVIAILALIVTGILLIAKGFSAASGPASLNNLWSHGGMFPNGWHGFILSFQMVVFAFVGIELVGLTAGETENPQKVIPKAINQIPVRILLFYVGALFVIMCIYPWNVLNPNESPFVQVFSAVGIVVAASLINFVVLTSAASAANSALFSTSRMVYSLAKDHHAPGLLKKLTSSNVPSNALFFSSIAILIGVSLNYLMPEQVFTLITSVSTICFIFIWGITVICHLKYRKTRQHEAKANKFKMPFYPLSNYLTLAFLAFILVILALANDTRIALFVTPVWFVLLIILYKVQTRRGHKVK", "text": "FUNCTION: Probable amino-acid or metabolite transport protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily."}
{"protein": "MSISSKIRPTPRKPSRMATDHSFKMKNFYADPFAISSISLAIVSWVIAIGGSISSASTNESFPRFTWWGIVYQFLIICSLMLFYCFDLVDHYRIFITTSIAVAFVYNTNSATNLVYADGPKKAAASAGVILLSIINLIWILYYGGDNASPTNRWIDSFSIKGIRPSPLENSLHRARRRGNRNTTPYQNNVYNDAIRDSGYATQFDGYPQQQPSHTNYVSSTALAGFENTQPNTSEAVNLHLNTLQQRINSASNAKETNDNSNNQTNTNIGNTFDTDFSNGNTETTMGDTLGLYSDIGDDNFIYKAKALYPYDADDDDAYEISFEQNEILQVSDIEGRWWKARRANGETGIIPSNYVQLIDGPEEMHR", "text": "FUNCTION: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Detects changes in external osmolarity and activates PBS2 through the stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2 activation leads to changes in glycerol production that helps to balance the intracellular and external osmotic pressures. Activates also HOG1 in response to heat stress and mediates resistance to oxidative stress. Involved in the regulation of the mating pathway. May be a receptor that feeds into the pseudohyphal growth pathway (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Bud Bud neck Cell projection Note=Localizes at the tip of the mating projection during conjugation. SIMILARITY: Belongs to the SHO1 family."}
{"protein": "MLFHVRMDVNIPDDMPVEVADEIKAREKAYSQALQKSGKWPHIWRLVGEYANYSIFDVESNAELHGILTGLPLFSYMKIEVTPLCRHPSSIRDDES", "text": "SIMILARITY: Belongs to the muconolactone Delta-isomerase family."}
{"protein": "MLQGTCSVLLLWGILGAIQAQQQEVISPDTTERNNNCPEKTDCPIHVYFVLDTSESVTMQSPTDILLFHMKQFVPQFISQLQNEFYLDQVALSWRYGGLHFSDQVEVFSPPGSDRASFIKNLQGISSFRRGTFTDCALANMTEQIRQDRSKGTVHFAVVITDGHVTGSPCGGIKLQAERAREEGIRLFAVAPNQNLKEQGLRDIASTPHELYRNDYATMLPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPSGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGADGRKGAPGLAGKNGTDGQKGKLGRIGPPGCKGDPGNRGPDGYPGEAGSPGERGDQGGKGDPGRPGRRGPPGEIGAKGSKGYQGNSGAPGSPGVKGAKGGPGPRGPKGEPGRRGDPGTKGSPGSDGPKGEKGDPGPEGPRGLAGEVGNKGAKGDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGAPGEKGEPGPRGPEGGRGDFGLKGEPGRKGEKGEPADPGPPGEPGPRGPRGVPGPEGEPGPPGDPGLTECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAKDPKSETGTRVGVVQYSHEGTFEAIQLDDERIDSLSSFKEAVKNLEWIAGGTWTPSALKFAYDRLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHEKHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPDLPCQTELSVAQCTQRPVDIVFLLDGSERLGEQNFHKARRFVEQVARRLTLARRDDDPLNARVALLQFGGPGEQQVAFPLSHNLTAIHEALETTQYLNSFSHVGAGVVHAINAIVRSPRGGARRHAELSFVFLTDGVTGNDSLHESAHSMRKQNVVPTVLALGSDVDMDVLTTLSLGDRAAVFHEKDYDSLAQPGFFDRFIRWIC", "text": "FUNCTION: Collagen VI acts as a cell-binding protein. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Membrane; Peripheral membrane protein Note=Recruited on membranes by CSPG4. SIMILARITY: Belongs to the type VI collagen family."}
{"protein": "MEIRRQGLIVWLHSLKQAKMLRKFGNVHYVSKRLKYVVVYCNMEDAERIIAKIRSYSFVKQVDLSYKPFLKMEFESKQDKAKEYDYKAGL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0298 family."}
{"protein": "MELDDLDLSGSWPLDQITFASNFKSPVIFSSSEQPFSPLWSFSETSGDVGGELYSAAVAPTRFTDYSVLLASSESETTTKENNQVPSPSWGIMPLENPDSYCAIKAKMTQALRYFKESTGQQHVLAQVWAPVKNRGRYVLTTSGQPFVLGPNSNGLNQYRMVSLTYMFSLDGERDGELGLPGRVFRKKLPEWTPNVQYYSSKEFSRLGHALHYNVQGTLALPVFEPSRQLCVGVVELIMTSPKINYAPEVEKVCKALEAVNLKTSEILNHETTQICNEGRQNALAEILEILTVVCETYKLPLAQTWVPCRHRSVLAFGGGFKKSCSSFDGSCMGKVCMSTSDLAVYVVDAHVWGFRDACAEHHLQKGQGVAGRAFQSGNLCFCRDVTRFCKTDYPLVHYARMFKLTSCFAVCLKSTYTGDDEYVLEFFLPPAITDKSEQDCLLGSLLQTMKQHYSSLKVVSETELCENNMSLEVVEASEDGMVYSKLEPIRIHHPAQISKDYLELNAPEQKVSLNSDFMENNEVDDGVERFQTLDPIPEAKTVKKSERKRGKTEKTISLEVLQQYFAGSLKDAAKSLGVCPTTMKRICRQHGISRWPSRKINKVNRSLTRLKHVIDSVQGADGSLNLTSLSPRPWPHQIPPIDIQLAKNCPPTSTSPLSNLQDVKIENRDAEDSAGSSTSRASCKVNPICETRFRLPTHNQEPSRQVALDDSDSSSKNMTNFWAHLTCQDTASPTILQHKLVSIKATYREDIIRFKISPESVSITELKQQVAKRLKLETAAFELKYLDDDREWVSVSCDADLSECLDTSAAKANTLRLSVHDVTFNFGSSCESSEETMMCL", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKDYLVKALAFDGEVRAYSVRTTNTVSEAQRRHDTWRTASAALGRSLTAGTMMGAMLKGEQKLTIKVEGNGPIGPILVDAHANGDVRGYVTNPHVDFEGTEQGKLRVYQAVGTEGFVTVIKDIGMREPFIGQSPIVSGELGEDFTYYFAVSEQTPSSVGVGVLVNGDDSILAAGGFILQIMPGAQDETISFIEDRLQKIPPVSTLIEQGLSPEELLYAVLGEDKVKVLETMDVQFNCTCSRERIESVLISLGKTELEQVREEEEETEVHCHFCNERYKFSKEDITNLIENL", "text": "FUNCTION: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HSP33 family."}
{"protein": "MVHINELPENILLELFIHIPAPQLLRNCRLVCRLWRDLIDVVSLWKRKSLREGFFTKDRCEPVEDWKVFYILCSLQRNLLRNPCAEENLSSWRIDSNGGDRWKVETLPGSCGTSFPDNKVKKYFVTSFEMCLKSQMVDLKAEGYCEELMDTFRPDIVVKDWVAPRADCGCTYQLRVQLASADYIVLASFEPPPVTFQQWNDAKWQEISHTFSDYPPGVRHILFQHGGQDTQFWKGWYGPRVTNSSIIISHRTAKNPPPARTLPEETVVIGRRRRASDSNTHEGFFWQGLWQRLRR", "text": "FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to ensure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication (By similarity). Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MKAVTVIPGIPESLRLMDVSKPNPNKGQVLLKPIRVGVCGTDKEIIEGRYGKAPEGNQYLILGHEAVAEVVEIGDGVDNAGVGDIVVPTVRRPLNCDLPVDFCPVGHYLEHGIWGLHGHAAEYSVTDAKYLVKVPKEIVDVAVLTEPLSVVEKGIDMAMRIGQARFDWKPRTALVLGAGPVGLLATMVLRLMGLSTVTTATRPPDSLKAKLVKELGGTYVDSAVGQISGEFDIVVEATGSPQVINEGLGHIAPNGVYVLLGVYPSGGSLNNLGELMTSVVLNNKVIVGSVNAGIKHFEMALEHLRRAKDEFNNWPAKLITKRANLSNYQEAYTWTHDDIKTVLEIIQS", "text": "FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily."}
{"protein": "MIVQRVVLNSRPGKNGNPVAENFRMEEVYLPDNINEGQVQVRTLYLSVDPYMRCRMNEDTGTDYITPWQLSQVVDGGGIGIIEESKHTNLTKGDFVTSFYWPWQTKVILDGNSLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGIQEKGHITAGSNKTMVVSGAAGACGSVAGQIGHLLGCSRVVGICGTHEKCVLLTSELGFDAAINYKKDNVAEQLRESCPAGVDVYFDNVGGNISDTVISQMNENSHIILCGQISQYNKDVPYPPPLSPAIEAIQKERNITRERFLVLNYRDKFEPGILQLSQWFKEGKLKIKETVINGLENMGAAFQSMMTGGNIGKQIVCISEEISL", "text": "FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family."}
{"protein": "MESPSYKNLIKAEDAQKKAGKRLLSSEWYPGFHVTPLTGWMNDPNGLIFFKGEYHLFYQYYPFAPVWGPMHWGHAKSRDLVHWETLPVALAPGDSFDRDGCFSGCAVDNNGVLTLIYTGHIVLSNDSLDAIREVQCMATSIDGIHFQKEGIVLEKAPMPQVAHFRDPRVWKENNHWFMVVGYRTDDEKHQGIGHVALYRSENLKDWIFVKTLLGDNSQLPLGKRAFMWECPDFFSLGNRSVLMFSPQGLKASGYKNRNLFQNGYILGKWQAPQFTPETSFQELDYGHDFYAAQRFEAKDGRQILIAWFDMWENQKPSQRDGWAGCMTLPRKLDLIDNKIVMTPVREMEILRQSEKIESVVTLSDAEHPFTMDSPLQEIELIFDLEKSSAYQAGLALRCNGKGQETLLYIDRSQNRIILDRNRSGQNVKGIRSCPLPNTSKVRLHIFLDRSSIEIFVGDDQTQGLYSISSRIFPDKDSLKGRLFAIEGYAVFDSFKRWTLQDANLAAFSSDAC", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 32 family."}
{"protein": "MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVHNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVKEMEQFVKKYKSEALGVGDVKLPCEMDAQGPKQMYIPGGDRSTPPAAGAMEDKSAEHKSTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSICHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAEKQSWHLKHFCCFACDGILAGDIYVMVNDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKMMS", "text": "FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion Note=Detected along actin stress fibers. SIMILARITY: Belongs to the prickle / espinas / testin family."}
{"protein": "MRFECSHFPLFLIILTCHISPLKSSQNYQWSYDSDVFGGPHFWGLVEKDWWMCKKGRLQSPIDIQPDRLLFDASVKPVSYAELNFFLIIYLTISLKLMRYIFTCAHLFACNKKLGTWNRIFGANIAKFRAWVVYIIIFHAQVPQLQVVSEFVNTGQMVRVRIGYSSKKPSVNITSGPLYGYRYRVQRIDFHMGRKNENGSEHTINGRRFPMEVQLVAYNTDLYPNFTSASKSPHGIAILSVLVDFGPETNQELIKLTIATASISYKDQRVQLADFEPWRLLPFTRDIITYEGSLTSPGCHETVTWIILNQPIFIKKEHFEEWSHLYLSMEGAEKVPVAPNFRKIQETNNRLVRTNIQHKVWIFLS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
{"protein": "MAHRLLVNVIFTGASVFGRAFTEAYRQAAKASAAGAAGRPAKASSAGGIPVEEAMKILDLEKSELSLDKVEEKYEYLFNVNSKEQGNSFYLQSKVYYAMDTLKKELEYLEKLQNEKGAASN", "text": "FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TIM16/PAM16 family."}
{"protein": "MLLELSEEHKEHLAFLPQVDSAVVAEFGRIAVEFLRRGANPKIYEGAARKLNVSSDTVQHGVEGLTYLLTESSKLMISELDFQDSVFVLGFSEELNKLLLQLYLDNRKEIRTILSELAPSLPSYHNLEWRLDVQLASRSLRQQIKPAVTIKLHLNQNGDHNTKVLQTDPATLLHLVQQLEQALEEMKTNHCRRVVRNIK", "text": "FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF- kappa-B (PubMed:15799966). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MKGMIFLAAAILSEVFGSTMLKLSEGFSAPLPAAGVIIGFAASFTFLSFSLKTLPLSAAYATWAGTGTALTAAIGHFIFQEPFNLKTLIGLTLIIGGVFLLNSKRTEAADQKAQLTIEI", "text": "FUNCTION: Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. EbrA/EbrB subfamily."}
{"protein": "MGVEIETISPGDGRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLSLE", "text": "FUNCTION: Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Cytoplasm Sarcoplasmic reticulum. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily."}
{"protein": "MNYLVMISFALLLMTGVESVRDAYIAKPHNCVYECARNEYCNDLCTKNGAKSGYCQWVGKYGNGCWCKELPDNVPIRVPGKCHR", "text": "FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "DCPSDWSSYEGHCYRVFKPPKDWADAERFCSQQAKGGHLVSIERFGREDFVSNLITKNLQRG", "text": "FUNCTION: Snaclec that binds to von Willebrand factor (VWF) and induces its interaction with GPIbalpha (GP1BA) (via the vWF A1 domain), resulting in platelet aggregation. Intramuscular and intravenous injections in mice induce a dose-dependent drop in platelet count (thrombocytopenia). Pretreatment by intravenous injection by this protein in mice potentiates the hemorrhagic lesion in the skin provoked by the metalloproteinase BaP1 intradermally injected. This result is not observed when both BaP1 and this protein are injected simultaneously. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
{"protein": "QKLCERPSGTXSGVCGNNNACKNQCIR", "text": "FUNCTION: Possesses some antifungal activity sensitive to inorganic cations and antibacterial activity against B.megaterium. SIMILARITY: Belongs to the DEFL family."}
{"protein": "MVLFYRAHWRDYKNDQVRIMMNLTTLTHRDALCLNARFTSREEAIHALTQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEGVDGPEAVDLVVLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDKGGTQPSASFSNAPTIVCVTACPAGIAHTYMAAEYLEKAGRKLGVNVYVEKQGANGIEGRLTADQLNSATACIFAAEVAIKESERFNGIPALSVPVAEPIRHAEALIQQALTLKRSDETRTVQQDTQPVKSVKTELKQALLSGISFAVPLIVAGGTVLAVAVLLSQIFGLQDLFNEENSWLWMYRKLGGGLLGILMVPVLAAYTAYSLADKPALAPGFAAGLAANMIGSGFLGAVVGGLIAGYLMRWVKNHLRLSSKFNGFLTFYLYPVLGTLGAGSLMLFVVGEPVAWINNSLTAWLNGLSGSNALLLGAILGFMCSFDLGGPVNKAAYAFCLGAMANGVYGPYAIFASVKMVSAFTVTASTMLAPRLFKEFEIETGKSTWLLGLAGITEGAIPMAIEDPLRVIGSFVLGSMVTGAIVGAMNIGLSTPGAGIFSLFLLHDNGAGGVMAAIGWFGAALVGAAISTAILLMWRRHAVKHGNYLTDGVMP", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:14645248, PubMed:9063979). This system is involved in mannosyl- D-glycerate transport (PubMed:14645248). Also involved in thermoinduction of ompC (PubMed:9063979). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MPTAAAPIISSVQKLVLYETRARYFLVGSNHAETKYRVLKIDRTEPKDLVVIDDRHVYTQQEVRELLGRLDLGNRTKMSQKGSSGLFRAVSAFGVVGFVRFLEGYYIVLITKRRKMADIGGHAIYKIEDTSMIYIPNDSVRISHPDEARYLRIFQNVDLSSNFYFSYSYDLSHSLQYNLTVLRMPLEMLKSETSKACQESFDIFEDEGLITQGGSGVFGISSEPYMKYVWNGELLDIIKNTVHRDWLLYIIHGFCGQSKLLIYGRPVYVTLIARRSSRFAGTRFLKRGANCEGDVANEVETEQILCDASVMSFTAGSYSSYVQVRGSVPLFWSQDISTMMPKPPITLDQADPFAHVAALHFDQMLQRFGSPIIILNLVKEREKRKHERILSEELVAAVTYLNQFLPPEHTIVYIPWDMAKYTKSKLCNVLDRLNVIAESVVKKTGFFVNRPDSYCSILRPDEKWNELGGHVIPTGRLQTGILRTNCVDCLDRTNTAQFMVGKCALAYQLYSLGLIDKPNLQFDTDAVRLFEELYEDHGDTLSLQYGGSQLVHRVKTYRKIAPWTQHSKDIMQTLSRYYSNAFSDADRQDSINLFLGVFHPTEGKPHLWELPTDFYLHHKNTMSLLPPRRSYTYWWTPEVVKHLPLPYDEVICAANLKKLMVKKFHRWEEEIDIHNEFFRPYELSSFDDTFCLAMTSSARDFMPKTVGIDPSPFTVRKPDETGKSVLGNKNTREEAVLQRKTAASAPPPPSEEAVSSSSEDDSGTDREDEGSISQRSTPVKMTDTGDSAKATENVVQPMKEVYGVSLSSSLSEEDHSIYARFVQLGQSQHKQDRGNQQLCSRCSDGVIKLTPISAFSQDNIYEVQPPRVDRKSTEIFQAHIQASQGIMQPLGKEDTAMYREYIRNRYL", "text": "FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). In vitro, hydrolyzes all three D5-phosphorylated polyphosphoinositide substrates in the order PtdIns(4,5)P2 > PtdIns(3,5)P2 > PtdIns(3,4,5)P3. Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. FUNCTION: Dual specificity phosphatase component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the dephosphorylation of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) to form phosphatidylinositol 3-phosphate. Has serine- protein phosphatase activity acting on PIKfyve to stimulate its lipid kinase activity, its catalytically activity being required for maximal PI(3,5)P2 production. In vitro, hydrolyzes all three D5-phosphorylated polyphosphoinositide and although displaying preferences for PtdIns(3,5)P2, it is capable of hydrolyzing PtdIns(3,4,5)P3 and PtdIns(4,5)P2, at least in vitro. SUBCELLULAR LOCATION: Endosome membrane Note=Localization requires VAC14 and PIKFYVE."}
{"protein": "MIIGVVSGQEPEEATPSLSARSTVRWRTFVRTETSSAVFLLAAVAAALVWANVGPHSYEAVWQARFTVGFDTRRLSLTVHEWINSGLMSLFFFVVGLEARRDFDMGELRDRRWLLLSAIAGLGSMIVPALIFVLVNAGRESVHGWGTAMSTDTAFALGVLAVFGSRLPASLRAFLLSVSVVDDLVALLVIAVFYSDEIRLPALLVAVCALLAIALLRLAGVRGALYCAVLSVVVWVALHEAGVDPVVAGLAVGVLVAAYPAPRGDLEQASRLFRLFREQPTPELHRSAVQGLDAAISPNERLEQRFLPWVSFGIVPLFALANAGIELSGPALADAFTSPVTLGIVLGCVVGKVIGTVGSMAAARLLSGGRLRPNVGWGSVTVGGAIAGSAFTVSLLIASLAFDGAELEEARIGILVTLVGAFLTSWAVTAVIGLLPERRRARALLGDVDPLTDLAVPVDRRHDRIRGPESAVVTVVEYGDFECPYCGQAEPVVRDLLGQESDVRYVWRHLPLRDVHPRAQLAAEASEAAARQDRFWEMHDLLLERQNALAAPDLLRYAGELGLDVERFRQDLRDHLGARRVAEDVDSADLSRVSGTPTFFINGRRHHGAYDIAALTRAVELARQRALTG", "text": "FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family."}
{"protein": "MSCHLIQQIENQQRKEPAETFRVGDTVRVHFKIVEGKTERIQAYEGLVLCFKNSGVRRTFTVRKNSYGVGVERIFPLHSPRIERVDVVRAGKVRRAKLYYIREKIGKAARIKARIVKKPSPSA", "text": "FUNCTION: This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. FUNCTION: This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family."}
{"protein": "MRSDDLYITTVPCFFKCPISLDVMKSPVSLSTGVTYDRVSIQRWLDDGNNTCPATMQILQNKEFVPNLTLHRLIDHWSDSINRRADSESPESDTPTRDEINAAIERFRIENDARSKILRFARESDENREFLAGKDDFVAMLVDLISDSRNFSDSQLLLVGEAVKILSMIRRKIFDRRRLSNLILTNGGDCLTSFFLLIKRGNPKLKIDCSAVLEFIAVDAESKLIIAKGEGLVTEIIKLISSDSDSSLIEANLSLLIAIASSKRVKLALIREKLVTKLTSLLTDPTTSVSVTEKCLKLLEAISSCKEGRSEICDGVCVETVVNKLMKVSTAATEHAVTVLWSVCYLFKEKKAQDAVIRINGVTKILLLLQSNCSLTVRHMLTDLLKVFKVNSRSCLSVYETKTTHIMPF", "text": "FUNCTION: Functions as an E3 ubiquitin ligase."}
{"protein": "MDIYAVAVGRVGVELDAAQLERVRATHLRVQGWGMEKYPMYGVNTGFGELINVIIPPQFKSDLQHNLLRSHAAGGGEPFPDEVVRAIMTVRINCLMKGYSGISPEALQLLATMLNRGIHPVIPMQGSLGASGDLAPLSHMALPLIGDGHVRKNGVTRPTMEVFQEEGLTPLKLGFKEGLALVNGTSAMTGAASLALYRARHLLRLSLLASADIVQAMNASTRPFSHTGNAVKNHPGQVVIARLMRDLTEGTGLMRDHQDIMRAISERTSHSNDVEETEIYLQNAYSLRCMPQVLGVVLETLQMCQRFIEEEANSVNDNPVILDTPAETYHGANFHGQYVAMACDYLSIAVAEMGVLAERQLNRLLDPHINKPLPGFLAHAKTGLFCGFEGGQYLATSIASENLDLAAPSSIKSIPSNGQNQDIVSMGLIAARKTLALCENVGTILSVLMAALNQASHFTEAAKYSAPIRSIHEKLGKVAPRYEDERPMSTVIAQVRGVLLQEQGLALAQSLVNLDLTPDLSLEPRA", "text": "FUNCTION: Has aminomutase and, to a much lesser extent, ammonia-lyase activity. Primarily, catalyzes the rearrangement of L-tyrosine to S- beta-tyrosine, which is probably incorporated into secondary metabolite myxovalargin. The aminomutase activity exclusively produces S-beta- tyrosine. SIMILARITY: Belongs to the TAL/TAM family."}
{"protein": "MAVPTTAVEGVRSRGAPGEVIHLNVGGKRFSTSRQTLTWIPDSFFSSLLSGRISTLKDETGAIFIDRDPTVFAPILNFLRTKELDPRGVHGSSLLHEAQFYGLTPLVRRLQVREELDRSSCGNVLFNGYLPPPVFPVKRRNRHSLVGPQQIGGRPAPVRRSNTMPPNLGNAGLLGRMLDDRAPPSPSGQPEEPGMVRLVCGHHNWIAVAYTHFLVCYRLKEASGWQLAFSSPRLDWPIERLALTARVLGGAPGEHDKMVAAATGSEILLWALQAQGGGSEIGVFHLGVPVEALFFVGNQLIATSHTGRIGVWNAVTKHWQVQEVQPITSYDAAGSFLLLGCSNGSIYYVDVQKFPLRMKDNDLLVSELYRDPAEDGVTALSVYLTPKTSDSGNWIEIAYGTSSGVVRVIVQHPETVGSGPQLFQTFSVHRSPVTKIMLSEKHLISVCADNNHVRTWSVTRFRGMISTQPGSTPLASFKILALESADGLGGCSAGNDIGPYGERDDQQVFIQKVVPNASQLFVRLSSTGQRVCSVRSVDGSATTAFTVLECEGSRRLGSRPRRYLLTGQANGSLAMWDLTTAMDGLGQTPAGGLTEEELMDQLEQCELSPLTSSRASFPSPSPRTSLTSLHSASSNTSLCGHRGSPSPPQAGARSRGAGSFVDRFKELARGAPELRGPPTPAPRPSTSLGNPLILPKNTLNETSF", "text": "FUNCTION: Inhibits CBL-SH3KBP1 complex mediated down-regulation of EGFR signaling by sequestration of SH3KBP1. Binds to SH3KBP1 and prevents its interaction with CBL and inhibits translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the KCTD3 family."}
{"protein": "SEGGQDFWL", "text": "FUNCTION: May control digestion processes in crustaceans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family."}
{"protein": "MALLRLVATECRNVLQRGYSTASVPTTKMFIDGKFVESKTNDWIDLHDPATNEVVTRVPKCTQDEMQTAVESSKKAYKTWRQSSILSRQQVMLKLQHIIRNNMSELAKNITKEQGKTLIDAEGDVLRGLQVVEHCCSITSLQMGETVPNIAKDMDTYSYHLPLGVTAGIAPFNFPAMIPLWMFPVAITCGNTSIIKPSERVPGATMLLMEMLNEAGCPPGVVNVIHGAHDAVNFVCDNPDIRAVSFVGSDQAGKYIYERAGRNGKRVQCNMGAKNHGVIMADANKENTLNQLAGAAFGAAGQRCMALSTAVFVGEARNWIPDLVERARKLKVNAGHLPGTDLGPVISPQSKQRINELVESGAKEGAKIVLDGRNIKVEGFEKGNFVGPTIISDVTPNMKCYTEEIFGPVLVCLSVDTIDEAIELINNNPYGNGTAIFTTNGATARKFVNDIDVGQVGVNVPIPVPLPMFSFTGSRGSFLGDCHFYGKQGIKFYTQTKTVTQLWREGDVSHTKAAVAMPTMK", "text": "FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MPNRKASRNAYYFFVQEKIPELRRRGLPVARVADAIPYCSSDWALLREEEKEKYAEMAREWRAAQGKDPGPSEKQKPVFTPLRRPGMLVPKQNVSPPDMSALSLKGDQALLGGIFYFLNIFSHGELPPHCEQRFLPCEIGCVKYSLQEGIMADFHSFINPGEIPRGFRFHCQAASDSSHKIPISNFERGHNQATVLQNLYRFIHPNPGNWPPIYCKSDDRTRVNWCLKHMAKASEIRQDLQLLTVEDLVVGIYQQKFLKEPSKTWIRSLLDVAMWDYSSNTRCKWHEENDILFCALAVCKKIAYCISNSLATLFGIQLTEAHVPLQDYEASNSVTPKMVVLDAGRYQKLRVGSSGFSHFNSSNEEQRSNTPIGDYPSRAKISGQNSSVRGRGITRLLESISNSSSNIHKFSNCDTSLSPYMSQKDGYKSFSSLS", "text": "FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with piP-bodies suggests a participation in the secondary piRNAs metabolic process. Required for the localization of germ-cell factors to the meiotic nuage (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs (By similarity). SIMILARITY: Belongs to the maelstrom family."}
{"protein": "MDNAILNSELIAIQAGNIIVYNYDGGNREYISASTEYLAVGVGIPANSCLDAPGSHKAGYAILRSEDLSSWEYVPDHRGETVYSIDTGNPEEITVLGDYPENTTTIAPLTPYDKWDGEKWVVDTEAQHSAAVEAAETKRQSLIDTAMDSISLIQLKLRAGRKLTQAETTQLNSVLDYIDELNAMDLTTAPDLNWPEKQLSTAS", "text": "SIMILARITY: Belongs to the tfa family."}
{"protein": "MVAKALAQLITCIILFCHVVASVEDLTIRQVTADNRRIRPNLLGTHTESKFRLFMSDYGKNYSTREEYIHRLGIFAKNVLKAAEHQMMDPSAVHGVTQFSDLTEEEFKRMYTGVADVGGSRGGTVGAEAPMVEVDGLPEDFDWREKGGVTEVKNQGACGSCWAFSTTGAAEGAHFVSTGKLLSLSEQQLVDCDQACDPKDKKACDNGCGGGLMTNAYEYLMEAGGLEEERSYPYTGKRGHCKFDPEKVAVRVLNFTTIPLDENQIAANLVRHGPLAVGLNAVFMQTYIGGVSCPLICSKRNVNHGVLLVGYGSKGFSILRLSNKPYWIIKNSWGKKWGENGYYKLCRGHDICGINSMVSAVATQVSS", "text": "FUNCTION: Probable thiol protease. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MIYKVFYQETKDQSPRRESTKALYLNIDATDELDGRIKARRLVEDNTYYNVEFIELLSDKHLDYEKETGVFELTEF", "text": "FUNCTION: A non-essential component of RNA polymerase (RNAP). SIMILARITY: Belongs to the RNA polymerase subunit epsilon family."}
{"protein": "MGSLKPWARYLLLLMAHLLAMGLGAVVLQALEGPPARHLQAQVQAELASFQAEHRACLPPEALEELLGAVLRAQAHGVSSLGNSSETSNWDLPSALLFTASILTTTGYGHMAPLSSGGKAFCVVYAALGLPASLALVAALRHCLLPVFSRPGDWVAIRWQLAPAQAALLQAAGLGLLVACVFMLLPALVLWGVQGDCSLLEAIYFCFGSLSTIGLGDLLPAHGRGLHPAIYHLGQFALLGYLLLGLLAMLLAVETFSELPQVRAMVKFFGPSGSRTDEDQDGILGQDELALSTVLPDAPVLGPTTPA", "text": "FUNCTION: Probable potassium channel subunit. No channel activity observed in vitro as protein remains in the endoplasmic reticulum. May need to associate with an as yet unknown partner in order to reach the plasma membrane. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the two pore domain potassium channel (TC 1.A.1.8) family."}
{"protein": "MTKLLEMKNITKKFGDVVALNNISISLETGEILSLCGENGSGKSTLMKVLCGIYPSGDYEGEIYFSGEKLTAKNIKDTEEKGISIIHQELTLVKNMSVLENMFLGNEITQAGITNDNKMYLRCKTLLEQVQLDIDPNTKVSALGLGQQQLVEIAKALNKQVRLLILDEPTASLTEKETDILLNLIKGLQAHNIACIYISHKLNEVKAISDKICVIRDGEHIGTQLAQGISEDDIITMMVGREITSLYPHEPHDIGKEILRVENLTAWHPTNTHIKRVDNANFILRKGEILGVAGLVGSGRTEMAQCIFGSYVGKYQGNIFLNNQKVKINKCAEAIANHIVMVPEDRKKHGIIPIMSVGKNITLSSLSQFCFGKKVINEPLEETIINQSIAKLKVKTSSPELAIGRLSGGNQQKAILAKCLLLHPNILILDEPTRGIDVGAKYEIYKLINQLAQEGMSIIVISSELPEVLGISDRVLVMHQGKVKADLINHHLTQEQVMEAALKE", "text": "FUNCTION: Part of the ABC transporter complex XylFGH involved in xylose import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Xylose importer (TC 3.A.1.2.4) family."}
{"protein": "MAKGIREKIRLVSSAGTGHFYTTDKNKRNMPGKFEIKKYDPVVRQHVVYKEAKIK", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MAGEDHPWHGSILYNLLMSAKQKHGSREEREVRLGAQCWGCACGTQPVLGGEGLPGGQALSLLYRCCFCGENHPRQGGILYSMLTNARQPSGATEAPRARFRTPCWGCACSNAKPLVGRXGLPAGQVPSLLYRCCFCGKKHPRQGSILYSLLTNAQQTHVSREVPEAHRGGEWWQLSYCTHNVGGPEGLQSTQAMAFLYRSYVCCEEQPQQSSVASDTPVRADQTPAAPQEQPRAPWWDTSSGVQRPIALKDPQVVCEAASAGLLKTLRFVKYLPCFQILPLDQQLVLVRSCWAPLLMLELAQDHLHFEMMEISEPNLMHEMLTTRRQETEGPEPADPQATEQPQTVSAEAGHVLSVAAVQAIKSFFFKCWSLNIDTKEYAYLKGTVLFNPDLPGLQCVKYIESLQWRTQQILTEHIRLMQREYQIRSAELNSALFLLRFINTDVVTELFFRPIIGAVSMDDMMLEMLCAKL", "text": "FUNCTION: Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the cytoplasm and nucleus. Homodimers exits in the cytoplasm and in the nucleus (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family. NR0 subfamily."}
{"protein": "MEVRVAGVRKEFARFPALHNVSLTIQSGELIALLGPSGSGKTTLLRLIAGLETPTEGMIFFGDEDASQKSVQERNVGFVFQHYALFRHMTVADNIGFGLKVRPGGTRPSTAEIRRRALELLDLVQLSGLEKRYPAQLSGGQRQRVALARAMAIEPRVLLLDEPFGALDAQVRKELRRWLREIHDKTGHTTVFVTHDQDEALELADRVVVMSQGRIEQVGTPDEVYDKPNSPFVYGFIGESSTLPVRVENGEVWLADRNIGLGAENMPDGDAQLYFRPHDVELLDGCGGCIAGTVIASRRSGGKRRVELEVGGARERIEIEIPAEHPAAEKSRIAFRPRYWTLFRAGDSELPAPKAAATT", "text": "FUNCTION: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family."}
{"protein": "MSSEMAAKSVKAFGLALKDSSGLFSPFNFSRRATGEHDVQLKVLYCGVCNFDNLMRRNKYGRTKFPYVFGHEIVGVVTEVGSNVKKFKIGNKVGVSFIVDTCRECERCKIGQQIACKKAVSSDGFFETPGYGGCSNIFVADENYVILWPENLPMDSGAPLLCIGITCYNPLRRFGLDKPGVRVGIVGLGAVGHLAIKFAKAFGARVTLISSSPGKKDEAFQKFGVDSFLVSSNAEEMQAAAETLDGILDTVPVVHPLEPLFALLKPLGKLIIIGEPHKPFEVSAMSLMEGGKIISASTGGSIKDTQEIVDFAAEHNVVADVEVIPVDYVNTAMERLDKADVKYRFVIDIGNTFKSP", "text": "FUNCTION: Converts the unstable imine alcohols produced by CYP71D1V2/T3O into 3-hydroxy-16-methoxy-2,3-dihydrotabersonine or 3- hydroxy-2,3-dihydrotabersonine. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MATVKVIDFIQTPFDFLIVGGGTAGLVLAARLSEEPGIQVGVIEAGSLRLGDPKVDLPTGPGQMLGDPGYDWNFESIPQAGANAKAYHIPRGRMLGGSSGINFMSYNRPSAEDIDDWANKLGVKGWTWSELLPYFKRSENLEPIEPSASCPVSPKVHGTGGPIHTSIGPWQAPIEESLLAAFDEAARLQRPAEPYSGAHLGFYRSLFTLDRTSTPVRSYAVSGYYAPVMGRPNLKVLENAQVCRILLSDASDGIPVAEGVELHHAGARYAVSARREVILSAGSVQSPQLLELSGIGDPSVLEGAGIACRVANTDVGSNLQEHTMSAVSYECADGIMSVDSLFKDPALLEEHQSLYAKNHSGALSGSVSLMGFTPYSSLSTETQVDATMARIFDAPSVSGRLSQQNASYQRRQQEAVAARMQNRWSADIQFIGTPAYFNTAAGYASCAKIMSGPPVGYSACYSIVVSNMYPLSRGSVHVRTSNPMDAPAIDPGFLSHPVDVDVLAAGIVFADRVFRSTLLNGKVRRRVSPPAGLDLSNMDEARQFVRNHIVPYHHALGTCAMGQVVDEKLRVKGVRRLRVVDASVMPMQVSAAIMATVYAIAERASDIIKKDCGFGRRLRAHI", "text": "FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato- nephrotoxic compound to humans due to inhibition of respiration complex III (Ref.1). The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT also named citS) from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (Ref.1). Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain (Ref.1). CitA collaborates with citS by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (PubMed:29189834). CitB then catalyzes the oxidation of the C-12 methyl of the ketone intermediate to an alcohol intermediate which is further oxidized by the oxidoreductase citC to produce a bisaldehyde intermediate (Ref.1). The fourth catalytic step is catalyzed by the citD aldehyde dehydrogenase (Ref.1). The final transformation is the reduction of C-3 by citE to provide the chemically stable citrinin nucleus (Ref.1). CitE appears highly selective for its substrate as its presence in any context other than a full complement of citS and citA-D does not result in observable new compounds (Ref.1). FUNCTION: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III (PubMed:27913218, PubMed:19012408, PubMed:19111642, PubMed:28238725). The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensations of 4 malonyl- CoA units, presumably with a simple acetyl-CoA starter unit (PubMed:28238725). Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain (PubMed:28238725). Mp11 collaborates with pksCT by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (By similarity). Mpl2 then catalyzes the oxidation of the C-12 methyl of the ketone intermediate to an alcohol intermediate which is further oxidized by the oxidoreductase mpl7 to produce a bisaldehyde intermediate (PubMed:27913218). The fourth catalytic step is catalyzed by the mpl4 aldehyde dehydrogenase (PubMed:27913218). The final transformation is the reduction of C-3 by mpl6 to provide the chemically stable citrinin nucleus (PubMed:27913218). SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MAAATPLLKDELDIVIPTIRNLDFLEMWRPFFQPYHLIIVQDGDPSKIIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPSGKDINALEQHIKNLLCPSTPHFFNTLYDPYRDGADFVRGYPFSMREGAPTAVSHGLWLNIPDYDAPTQLVKPHERNTRYVDAVMTIPKGTLFPMCGMNLAFDRDLIGPAMYFGLMGDGQPIGRYDDMWAGWCTKVICDHLGLGIKTGLPYIWHSKASNPFVNLKKEYNGIFWQEEIIPFFQAATLPKECTTVQQCYLELSKQVKKKLSSIDPYFTKLGEAMVTWIEAWDELNLLGTTWLSCLSPMVQQRLKSRCY", "text": "FUNCTION: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides (By similarity). Was initially shown to possess an autoglycosylating activity which is dependent on the presence of UDP-glucose and manganese (Probable) (PubMed:10580281). SUBCELLULAR LOCATION: Secreted, cell wall Cell junction, plasmodesma Golgi apparatus Note=Cell wall-associated, with highest concentrations on plasmodesmata. Also located in the Golgi apparatus (By similarity). SIMILARITY: Belongs to the RGP family."}
{"protein": "MALTKDNEDLVRVGRGTPMGGLMREYWIPALKSTELEAGGSPVRLLLLGEKLVAFREPSGAVGVMDSRCPHRGVSLFMGRVEEGGLRCVYHGWKFSAEGKCVDMPSVRPEDEFKNSVRVARYPVKEMAGVVWVYMGTRKVLPELPRLEVLNLPENEVDVICLQRKSNWLQNLEGEIDTSHFNFLHVGGLHADEVPDDHPLKYTAQVAPQYLVKETALGTCYAAQVPAEEDHTYTRFAHFLFPFWALIPQADIAQNILARAWVPMDDEHTMMFFFRWTGSKAKRLDTPLKSGSPMPGVTLTDMKYKENTTDWYGRWQPLGDESNDWLIDRDLQKVGRVFSGIYGIHAQDQAMTDSMGPIIDHGLEQLAPTDLMIVRTRRRILKALRAHEANGTLPPGVDEADQYFTPRSGYYLTPKSVDWETAYEQRIEGLVR", "text": "SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family."}
{"protein": "MGKLTLGHRGEASEPDFFRGVLGELVLTFLFVFIGVGAAMTDGATTKGSTAGGDLTAVALGQALVVAVIATAGFHISGGHVNPAVTLSLAVGGHVTLFRSSLYIAAQMLASSAACFLLRWLTGGLATPVHALAEGVGPLQGVVAEAVFTFSLLFVIYATILDPRKLLPGAGPLLTGLLVGANSVAGAALSGASMNPARSFGPAVASGVWTHHWVYWVGPLAGGPLAVLVYECCFMAAAPTHDLLPQQDP", "text": "FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP (TC 1.A.8.10) subfamily."}
{"protein": "MHLTKEKFIKLSMISSIIILCIAIVSVILFGVQQFKIGSQLASVNQVSNLSHLLIRQQANLLSMLLVNNASTEQLTESLDAFAKEEFVLDASIYSNRGELLAHTSHFQNLRLTLGLNSPTQPDEENTQQIVEPIYSLNGIEGFLRVTFDSKYGKTTQSKIDHLFHQLYGELIIIFLAGVLLASSIHYFLSHYRRTYRKVTENKAVKVLKTKQNVGNYHRRRRRLNK", "text": "FUNCTION: When anaerobically expressed in wild-type E.coli K12 confers a hemolytic phenotype, but not in an sheA mutant. Suggests it affects the expression of the latent E.coli K12 hemolysin sheA under anaerobic conditions. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Smp family."}
{"protein": "MTKRERIIQSVLVKVPKDAINQFLSHGSTPISVLFLAALVGVLAGLVGTYFEIAVHFVSETRTEWLKSEIGHLLPLWLAAILISAALAFVGYFLVHRFAPEAAGSGIPEIEGAMDNIRPVRWWRVIPVKFFGGMGALGSGMVLGREGPTVQMGGAVGRMVTDIFRVKDDDTRHSLLASGAAGGLAAAFNAPLAGIMFVVEEMRPQFRYSLISIRAVIISAVMANIVFRAINGQDAVITMPQYQPPELKALWLFLLLGGLFGVFGVLFNKLVTVAQDAFVALHKNDRKRYLITGTCLGGIFGLLLLYVPELTGGGIHLIPDVTNGNYSVSLLVMLFVGRVLTTLICFGSGAPGGIFAPMLALGTLFGYAFGATAKILLPDLPIEPGMFAIAGMGALFAATVRAPITGILLVIEMTNNYYLILPLIITSLGAVICAQICGGKPIYSQLLHRTIKNDKLRQQDLPEQQNS", "text": "FUNCTION: Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcA subfamily."}
{"protein": "MTQLENEVPDKDHLRFFSLGGSNEVGRSCHILQYKGKTLMLDAGIHPAHQGLASLPYYDEFDLSTIDLLLISHFHLDHAASLPYVMQRTNFRGRVFMTHPTKAIYRWLLNDFVKVTSIGDSPGQDSSNDNLYSDEDLAESFDRIETIDYHSTMEVNGIKFTAFHAGHVLGAAMFQIEIAGVRVLFTGDYSREVDRHLNSAEVPPQSSDVIIVESTFGTATHEPRQNRERKLTQLIHTVVSKGGRVLLPVFALGRAQEIMLILDEYWQNHKEELGNGQVPIFYASNLAKKCMSVFQTYVNMMNDDIRKKFKDSQTNPFIFKNISYLKNLDEFEDFGPSVMLASPGMLQNGLSRDILEKWCPEEKNLVLVTGYSVEGTMAKYLLLEPEAIPSVHNPEITIPRRCQVDEITFAAHVDFRENLEFIELIGASNIILVHGESNPMGRLKSALLSNFSSLKDTENEVHVFNPRNCVFVDIEFKDVKVARAVGKIIEDLDEFITEEDALKNEKRITEIHEEDPETEESKTEIVKEENEKIVSGILVSDEKNFDLSLVSLSDLREHYQQLSTTVLTERQTVHLDCKSELVYWHICQMFGDVDVYIDEENVSLKNINPEFKTRKIKKGELEIKIMGDVILNIVDNVATLQWTQNVISDSVADSVMAILLSVESAPASIKMSSKSCGHHHGHDDHTTKIKNISRVFKEQFGDTFTLFLNEEDSKEEIKGTINLGKTTACINFSKMVVEECNSNPLKGRIESLLKIGSDLVAPLC", "text": "FUNCTION: Component of the cleavage factor I (CF I) involved in pre- mRNA 3'-end processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily."}
{"protein": "NNYCKIKCLKGGVHTACKYGSLKPNCGNKIVVSYGLTKEEKQDILKEHNDFRQKIARGLETRGNPGPQPPAKNMKNLVWNDELAYVAQVWANQCQYGHDTCRDVAKYPVGQNVALTGSTADKYDNPVKLVKMWEDEVKDYNPKKKFSENNFNKIGHYTQMVWANTKEIGCGSIKYIQNEWHKHYLVCNYGPSGNFGNEELYQTK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family. Venom allergen 5-like subfamily."}
{"protein": "MAASQTSQTVASHVPFADLCSTLERIQKSKGRAEKIRHFREFLDSWRKFHDALHKNHKDVTDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPRDGKDALKLLNYRTPTGTHGDAGDFAMIAYFVLKPRCLQKGSLTIQQVNDLLDSIASNNSAKRKDLIKKSLLQLITQSSALEQKWLIRMIIKDLKLGVSQQTIFSVFHNDAAELHNVTTDLEKVCRQLHDPSVGLSDISITLFSAFKPMLAAIADIEHIEKDMKHQSFYIETKLDGERMQMHKDGDVYKYFSRNGYNYTDQFGASPTEGSLTPFIHNAFKADIQICILDGEMMAYNPNTQTFMQKGTKFDIKRMVEDSDLQTCYCVFDVLMVNNKKLGHETLRKRYEILSSIFTPIPGRIEIVQKTQAHTKNEVIDALNEAIDKREEGIMVKQPLSIYKPDKRGEGWLKIKPEYVSGLMDELDILIVGGYWGKGSRGGMMSHFLCAVAEKPPPGEKPSVFHTLSRVGSGCTMKELYDLGLKLAKYWKPFHRKAPPSSILCGTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGCTLRFPRIEKIRDDKEWHECMTLDDLEQLRGKASGKLASKHLYIGGDDEPQEKKRKAAPKMKKVIGIIEHLKAPNLTNVNKISNIFEDVEFCVMSGTDSQPKPDLENRIAEFGGYIVQNPGPDTYCVIAGSENIRVKNIILSNKHDVVKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFIDTDLNQLKEVFSGIKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYAVINDLSTKNEGTRLAIKALELRFHGAKVVSCLAEGVSHVIIGEDHSRVADFKAFRRTFKRKFKILKESWVTDSIDKCELQEENQYLI", "text": "FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination (PubMed:8798671, PubMed:9242410, PubMed:9809069, PubMed:12517771, PubMed:17290226). Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed (PubMed:9242410, PubMed:9809069, PubMed:12517771, PubMed:17290226). Joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction (PubMed:9242410, PubMed:9809069, PubMed:12517771, PubMed:17290226). LIG4 is mechanistically flexible: it can ligate nicks as well as compatible DNA overhangs alone, while in the presence of XRCC4, it can ligate ends with 2-nucleotides (nt) microhomology and 1-nt gaps (PubMed:17290226). Forms a subcomplex with XRCC4; the LIG4-XRCC4 subcomplex is responsible for the NHEJ ligation step and XRCC4 enhances the joining activity of LIG4 (PubMed:9242410, PubMed:9809069). Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends (PubMed:10854421). LIG4 regulates nuclear localization of XRCC4 (PubMed:24984242). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
{"protein": "MRVVFSSMASKSHLFGLVPLAWAFRAAGHEVRVVASPALTEDITAAGLTAVPVGTDVDLVDFMTHAGHDIIDYVRSLDFSERDPATLTWEHLLGMQTVLTPTFYALMSPDTLIEGMVSFCRKWRPDLVIWEPLTFAAPIAAAVTGTPHARLLWGPDITTRARQNFLGLLPDQPEEHREDPLAEWLTWTLEKYGGPAFDEEVVVGQWTIDPAPAAIRLDTGLKTVGMRYVDYNGPSVVPEWLHDEPERRRVCLTLGISSRENSIGQVSIEELLGAVGDVDAEIIATFDAQQLEGVANIPDNVRTVGFVPMHALLPTCAATVHHGGPGSWHTAAIHGVPQVILPDGWDTGVRAQRTQEFGAGIALPVPELTPDQLRESVKRVLDDPAHRAGAARMRDDMLAEPSPAEVVGICEELAAGRREPR", "text": "FUNCTION: Catalyzes the conversion of alpha-L-mycarosylerythronolide B into erythromycin D in the erythromycin biosynthesis pathway. SIMILARITY: Belongs to the glycosyltransferase 28 family."}
{"protein": "MAIKRRKVSVIGAGFTGATTALMVAQKELGDVVLVDIPQMEGPTKGKALDMLESTPVQGVDVNITGTSSYEYTKDSDVVVITAGIARKPGMSRDDLVSTNAGIMKAVTKEVVKHSPNAYIIVLTNPADAMTYTVYKESGFPKNRVIGQSGVLDTARFRTFVAQELNLSVEDITGFVLGGHGDDMVPLIRYSYAGGIPLEKLLPQERIDAIVERTRKGGGEIVGLLGNGSAYYAPAASLAEMVEAILKDKKRVLPTIAYLEGEYGYEDIYVGVPTILGGDGIEKVIELDLTDEEKATFAKSIESVRNVMSALPKE", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family."}
{"protein": "MDLMQMDKRLDSTEQVVEEIMRIHRSLPARPGIDEVEAAKGLIDNVEKEDQACLEAIARQRKSSEVPGELFMVLQEMKKGYVQFRSKEQIREALKLLDLESVHSLFDDFIQRASNCIASPSSNGSVSSRPPLPPATTTAARSDSQSSLNFSERAPVRPKDMVSRDDSFVTKSKPSSLYSDGFAAPPRRPQILDSTLTTGNDGEKLSLIKLASLIEVSAKKATQEINLQNKLTEQLEWLPDSLGKLSSLTSLDLSENHIVVLPNTIGGLSSLTKLDLHSNRIGQLPESIGELLNLVYLNLGSNQLSSLPSAFSRLVRLEELDLSCNNLPILPESIGSLVSLKKLDVETNDIEEIPYSIGGCSSLIELRADYNKLKALPEAIGKITTLEILSVRYNNIRQLPTTMSSLASLKELDVSFNELESVPESLCFATTLVKLNIGNNFADMVSLPRSIGNLEMLEELDISNNQIRVLPDSFKMLTKLRVFRAQENPLHIPPRDIAEKGPQAVVQYMNDLVETRNAKSLMVKPKKSWVQMCFFSKSNKRKQSSMEIV", "text": "FUNCTION: Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction. SIMILARITY: Belongs to the SHOC2 family."}
{"protein": "MSMSTPQKAILPPFNADILPLGLYVAATVLLIGILLLAAWWLGDKKRSAAKEIAYESGVIPTGTARLAYPVPFYLVAIFFIVFDVEAVFIFTWAVAWDELGFPGLIHITAFIIVLLLGLVWLWLKGGLEWGPSKQVRRSKFEVRS", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family."}
{"protein": "MDKFADLNYTLSVITLMNDTLHSIIQDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVIKCCIVTIINTLLKLAGYKEQVTTKDEIEQQMDRIVKEMRRQLEMIDKLTTREIEQVELLKRIHDNLIIKPVDVIDMSKEFNQKNIKTLDEWESGKNPYEPLEVTASM", "text": "FUNCTION: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly. FUNCTION: The secreted form acts as an enterotoxin that causes phospholipase C-dependent elevation of the intracellular calcium concentration in host intestinal mucosa cells. Increased concentration of intracellular calcium disrupts the cytoskeleton and the tight junctions, raising the paracellular permeability. Potentiates chloride ion secretion through a calcium ion-dependent signaling pathway, inducing age-dependent diarrhea. To perform this enterotoxigenic role in vivo, NSP4 is released from infected enterocytes in a soluble form capable of diffusing within the intestinal lumen and interacting with host plasma membrane receptors on neighboring epithelial cells such as integrins ITGA1/ITGB1 and ITGA2/ITGB1. SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane; Single-pass type III membrane protein Host membrane, host caveola; Single-pass type III membrane protein Secreted Note=NSP4 localizes also in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus- infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. SIMILARITY: Belongs to the rotavirus NSP4 family."}
{"protein": "MGANQLVVLNVYDMYWMNEYTSSIGIGVFHSGIEVYGREFAYGGHPYPFSGIFEISPGNASELGETFKFKEAVVLGSTDFLEDDIEKIVEELGKEYKGNAYHLMHKNCNHFSSALSEILCGKEIPRWINRLAYFSSCIPFLQSCLPKEWLTPAALQSSVSQELQDELEEAEDAAASASAASTAAGSRPGRHTKL", "text": "FUNCTION: Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'- linked polyubiquitin chains. Deubiquitinates 'Lys-48'-linked polyubiquitination of RPS7 leading to its stabilization. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DeSI family."}
{"protein": "MAETQNLLLFRKWDLSDIEVVDPGLKTAISLRKMTLPYTYGRSALKRFNKADANIVERLANKMMHFGKKYAKNTGRMAGKKMGSINTVKTAFEIINLKTGRNPVEVLVRAVENSAPNEDTTRIVYGGTVYHVSVDVSPLRRVDLALRFIADGVKEAAFRKPKSLEEFLAEHLILAANNTTDAPSVKKKNELERIAQASR", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center. SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MEEVRDCRLEEGLSVEGLVECYRDIHGFMAGHLAEAVEVLREGLEASSVRVLTFTGNLVATGLRGVLAQLIDGGLFNVVFTTAGALDHDIARFMGGKYLKGRFEADDTELHRRGVHRLGNVFIPVESYGPLVERFVRTLAEQAAGVRGEWGVYELLRLAGSLMEGDRDSILAAAARRGVDVFVPGWPDGAFGTSLFMERQRGTSITVDYFRDMARLADIFFPQEGEAAALIVGGGISKHHAIWWSQFRGGLDYAVYVTTAVEYDGSLSGAHPREAVSWGKIKESSRRVVVYGDATITLPVIAYCLLHGCG", "text": "FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. SIMILARITY: Belongs to the deoxyhypusine synthase family."}
{"protein": "MSSNKNQSDLNIPTNSASLKQKQRQQLGIKSEIGASTSDVYDPQVASYLSAGDSPSQFANTALHHSNSVGYSASAAAAAAELQHRAELQRRQQQLQQQELQHQQEQLQQYRQAQAQAQAQAQAQREHQQLQHAYQQQQQLHQLGQLSQQLAQPHLSQHEHVRDALTTDEFDTNEDLRSRYIENEIVKTFNSKAELVHFVKNELGPEERCKIVINSSKPKAVYFQCERSGSFRTTVKDATKRQRIAYTKRNKCAYRLVANLYPNEKDQKRKNKPDEPGHNEENSRISEMWVLRMINPQHNHAPDPINKKKRQKTSRTLVEKPINKPHHHHLLQQEQQQQQQQQQQQQQQQQQQQHNANSQAQQQAAQLQQQMQQQLQASGLPTTPNYSELLGQLGQLSQQQSQQQQLHHIPQQRQRTQSQQSQQQPQQTAHGLDQPDAAVIAAIEASAAAAVASQGSPNVTAAAVAALQHTQGNEHDAQQQQDRGGNNGGAIDSNVDPSLDPNVDPNVQAHDHSHGLRNSYGKRSGFL", "text": "FUNCTION: Transcriptional activator that binds to the RPG box and to telomeres. Involved in the regulation of the transition between yeast and filamentous forms and plays a role in virulence. Induces expression of HWP1, a major hyphal cell protein and virulence factor. SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. SIMILARITY: Belongs to the RBF1 family."}
{"protein": "MAEIKNYTLNFGPQHPAAHGVLRLVLELDGEVIQRADPHIGLLHRATEKLAESKTFIQSVPYMDRLDYVSMMVNEHGYVLAIEKLLGIEVPERAQYIRVLFDEITRVLNHLMWIGAHALDVGAMAVFLYAFREREDLMDVYEAVSGARMHAAYYRPGGVYRDLPEAMPQYKASKIRNERALAKMNEARSGSVLDFIDDFFTRFPKCVDEYETLLTDNRIWKQRLVGIGVVSPERALQLGLTGPMIRGSGIAWDLRKKQPYEVYDRIDFDIPVGVNGDCYDRYLVRVEEMRQSTRIAKQCIEWLRENPGPVITDNHKVAPPSRVGMKTNMEDLIHHFKLFTEGFHVPEGEAYAAVEHPKGEFGIYLVSDGANKPYRLKIRAPGYAHLSALDEMARGHMIADAVTIIGTQDIVFGEIDR", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 49 kDa subunit family."}
{"protein": "LTEEQKQDIREAFDLFDTDGSGTIDAKELKVAMRALGFEPKKEEIKKMIADIDKDGSGTIDFEEFLQMMTAKMGERDSREEIMKAFRLFDDDETGKISFKNLKRVAKELGENMTDEELQEMIDEADRDGDGEVNEEEFFRIMKKTSLF", "text": "FUNCTION: This calcium-binding protein is found in the basal body complexes (the functional homolog of the centrosome in animal cell). In mitotic cells it is specifically associated with the poles of the mitotic spindles at the sites of the duplicated basal body complexes. SIMILARITY: Belongs to the centrin family."}
{"protein": "MVSSFSVPMPVKRIFDTFPLQTYAAQTDKDEAVALEIQRRSYTFTERGGGSSELTVEGTYKLGVYNVFLEANTGAALATDPWCLFVQLALCQKNGLVLPTHSQEQTPSHTCNHEMLVLSRLSNPDEALPILVEGYKKRIIRSTVAISEIMRSRILDDAEQLMYYTLLDTVLYDCWITQIIFCASDAQFMELYSCQKLSGSIVTPLDVENSLLQKLSAKSLKISLTKRNKFQFRHREIVKSMQGVYHNHHNSVNQEQVLNVLFENSKQVLLGLKDMLKSDGQPTYLHLKIASYILCITNVKEPIKLKTFVENECKELVQFAQDTLKNFVQ", "text": "FUNCTION: Essential component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex. SUBCELLULAR LOCATION: Mitochondrion outer membrane."}
{"protein": "MKKLVLCVSILAVILSGVALTQLSTDSPSNIQVAERPVGG", "text": "FUNCTION: Signaling molecule involved in the regulation of genetic competence development (PubMed:16816200). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates expression of the genes controlled by ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:16816200). Acts by inhibiting RapK, which regulates the activity of ComA (PubMed:16816200). SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Produced through an export-import maturation process. SIMILARITY: Belongs to the Phr family."}
{"protein": "MNKHASQPRAIYYVVALQIWEYFSFYGMRALLILYLTNQLKYNDTHAYELFSAYCSLVYVTPILGGFLADKVLGNRMAVMLGALLMAIGHVVLGASEIHPSFLYLSLAIIVCGYGLFKSNVSCLLGELYEPTDPRRDGGFSLMYAAGNVGSIIAPIACGYAQEEYSWAMGFGLAAVGMIAGLVIFLCGNRHFTHTRGVNKKVLRATNFLLPNWGWLLVLLVATPALITILFWKEWSVYALIVATIIGLGVLAKIYRKAENQKQRKELGLIVTLTFFSMLFWAFAQQGGSSISLYIDRFVNRDMFGYTVPTAMFQSINAFAVMLCGVFLAWVVKESVAGNRTVRIWGKFALGLGLMSAGFCILTLSARWSAMYGHSSLPLMVLGLAVMGFAELFIDPVAMSQITRIEIPGVTGVLTGIYMLLSGAIANYLAGVIADQTSQASFDASGAINYSINAYIEVFDQITWGALACVGLVLMIWLYQALKFRNRALALES", "text": "FUNCTION: Probable proton-dependent permease that transports dipeptides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpD subfamily."}
{"protein": "MEDFVRQCFNPMIVELAEKAMKEYGEDPKIETNKFAAICTHLEVCFMYSDFHFIDERGESIIVESGDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGVEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFVSPREAKRQLKKDLKSQEPCAGLPTKVSHRTSPALKTLEPMWMDSNRTAALRASFLKCQKK", "text": "FUNCTION: May play a role in the modulation of host immune response. SIMILARITY: Belongs to the influenza viruses PA-X family."}
{"protein": "MARYDLVDRLNTTFRQMEQELAAFAAELEQHKLLVARVFSLPEVKKEDEHNPLNRIEVKQHLGNDAQSLALRHFRHLFIQQQSENRSSKAAVRLPGVLCYQVDNFSQAALVSHIQHINKLKTTFEHIVTVESELPSAARFEWVHRHLPGLITLNAYRTLTVLHAPATLRFGWANKHIIKNLHRDEVLAQLEKSLKSPRSVAPWTREEWQRKLEREYQDIAALPQNAKLKIKRPVKVQPIARVWYKGDQKQVQHACPTPLIALINRDNGAGVPDVGELLNYDADNVQHRYKPQAQPLRLIIPRLHLYVAD", "text": "FUNCTION: Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Tus family."}
{"protein": "MAALYACTKCHQRFPFEALSQGQQLCKECRIAHPVVKCTYCRTEYQQESKTNTICKKCAQNVQLYGTPKPCQYCNIIAAFIGNKCQRCTNSEKKYGPPYSCEQCKQQCAFDRKDDRKKVDGKLLCWLCTLSYKRVLQKTKEQRKHLSSSSRASHHEKEQYSRLSGGSHYNSQKTLSTSSIQNEIPKKKSKFESITTNGDSFSPDLALDSPGTDHFVIIAQLKEEVATLKKMLHQKDQMILEKEKKITELKADFQYQESQMRAKMNQMEKTHKEVTEQLQAKNRELLKQAAALSKSKKSEKSGAITSP", "text": "SIMILARITY: Belongs to the FAM76 family."}
{"protein": "MAAPAPSLWTLLLLLLLLPPPPGAHGELCRPFGEDNSIPVFCPDFCCGSCSNQYCCSDVLRKIQWNEEMCPEPESRFSTPAEETPEHLGSALKFRSSFDSDPMSGFGATVAIGVTIFVVFIATIIICFTCSCCCLYKMCCPQRPVVTNTTTTTVVHAPYPQPQPQPVAPSYPGPTYQGYHPMPPQPGMPAAPYPTQYPPPYLAQPTGPPPYHESLAGASQPPYNPTYMDSLKTIP", "text": "FUNCTION: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Nucleus membrane. SIMILARITY: Belongs to the shisa family."}
{"protein": "MMPRAQLTTFLIVTSFLSTVPYLRAPVHGGVLTSYDVSSLDIMSKIHTDHDATTKASSDFGHIVHATPNGVFRPTFPADIAALIRLSLSQPTPFTVAPRGKGHSSRGQAFAPGGIVVDMSALGDHGHHTSHRIDVSVDRMYVDAGGEQLWIDVLHTALKHGLTPRVWTDYLRITVGGTLSNAGIGGQAFRHGPQISNVHELDVVTGMGEMITCSPEVNSALFFAVLGGLGQFGVITRARIRLEPAPKRVKWVRIAYSDVHPFTTDQELLISKWASGSGFDYVEGQVQLNRTLTQGRRSSSFFSATDLARLTGLAIDTGSVAIYYIEGAMYYDDNTAASVDQKLDALLEELSFVRGFVFVRDASYVEFLDRVGREEQNLRSAGAWDVPHPWLNLFVPRSRILHFDAAVFKGILRNANPVGLILMYPMNKDMWDDRMTAMTPDEDVFYAVGLLRSAVAGGSGGDVEQLERENAAVLELCDLAGGGIGCRQYLPHHASRDGWRRHFGAKWGRVADLKARYDPRAILSPGQGIFPPPPPPSPPPPAAGEPITAS", "text": "FUNCTION: Catalyzes the oxidation of cytokinins, a family of N(6)- substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MIPEKKSIAIMKELSIGNTKQMLMINGVDVKNPLLLFLHGGPGTPQIGYVRHYQKELEQYFTVVHWDQRGSGLSYSKRISHHSMTINHFIKDTIQVTQWLLAHFSKSKLYLAGHSWGSILALHVLQQRPDLFYTYYGISQVVNPQDEESTAYQHIREISESKKASILSFLTRFIGAPPWKQDIQHLIYRFCVELTRGGFTHRHRQSLAVLFQMLTGNEYGVRNMHSFLNGLRFSKKHLTDELYRFNAFTSVPSIKVPCVFISGKHDLIVPAEISKQYYQELEAPEKRWFQFENSAHTPHIEEPSLFANTLSRHARHHL", "text": "FUNCTION: Probable aminopeptidase. SIMILARITY: Belongs to the peptidase S33 family."}
{"protein": "MGHDIKGFSCAFAVGLLFNILACIVSHSGYPIIVVASYFLAPFPNILCRNRDSFSSEKGTFEDIGLFLTGLFITSGFAIPMILAHSDIISGKALAFSMAGGVTVYATIITFLWFFNRHNDEDNNW", "text": "FUNCTION: Involved in endosomal protein transport. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OB-RGRP/VPS55 family."}
{"protein": "MTESPLSAPAPTSNQSPAPEQTFGTAGIAPMDRPSAMTRFFMSIVAWAESLNLKYAKLGNPPVYDTATFPWAAEIEKDYPAIRAELEKVLLRQSELPTFQDISTDVKTISTDTRWKTFFLLGFGVKSEQNIKACPNTWAAVQKIPGLTTAMFSIFEPGKHLPAHRGPYNGVLRLHLGLIVPEPNDKLAIRVDNQVCHWQEGKALIFDDAYEHEAWNHTDKTRVVLFVDFVKPLKSPARFVNWALMNLAIFTPFIKEGLDNHKEWEKKFYAEAEAFRNRPKP", "text": "FUNCTION: Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids (PubMed:16353552, PubMed:21205018). Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL (PubMed:21205018). Contributes to symbiotic performance and acid tolerance (PubMed:16353552, PubMed:21205018). SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase family."}
{"protein": "MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYFAYFLIIVPVISTIENVLFYIGRVNK", "text": "FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome b is a catalytic core subunit containing 2 b-type hemes BL and BH topographically segregated in the quinone reduction (Qi) and quinol oxidation (Q0) sites on opposite sides of the membrane (PubMed:18390544). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family."}
{"protein": "MASIIFTAKDIFDQDFKREVRGYSKSEVDEFLDDIIKDYETYAALVKELREENRRLKEELAAKPVEKAPVQPTQPVQSTQATQSTVESFSQMTSATNFDILKRLNRLEKEVFGKQILDRE", "text": "FUNCTION: Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation. SUBCELLULAR LOCATION: Cytoplasm Note=Shuttles between the lateral wall and the division site in a cell cycle-dependent manner. SIMILARITY: Belongs to the GpsB family."}
{"protein": "MNKKLKLFSMPGAQTSQIVIMLFQSLLHLLEAIASREPTRYIITYSIGNTHTPEIFSYSDLLQSARKAAGALRFKYHVVPGSVVLLHFNDHWNSMLWFWATLIADCIPAMSTPFSNNPETRLRHLKHLSTTLRSPKCLTTASLAAEFAGQEYITPICVQSLDYENLVHLPIKEGGDIAVLMFTSGSSGHCKVVPLTHEQILASLSGKAWTFPLPDNTAQLNWVGMNHVASLVEVHLFSIYTHSDQVHIPTVEVLSHVTLFLDLIHRHRVSRTFAPNFFLAKLRAALSADDTLAKYTGSLSNLRYIVSGGEANVTQTINDLAQMLKKCGAVSNVIVPAFGMTETCAGAIYNTSFPQYDVEHGLPFASVGSCMPGIQVRIVQLNGNGNSVPPGTVGNLEICGPVVLKGYFNDPAATKSTFTNDNWFKTGDLAFVDDNGMLVLAGREKDSIIVNGANYSPHDIESAIDEANIPGLISGFTCCFSTFPPSADTEEVIIVYLPNYTPADTVRRSETAAAIRKVAMMSVGVRATVLPLDRTMLEKSTLGKLARGKIKAAYERGDYKSYQEANEQMMALHHKVSHHQPRSGLEQSLLGVFTRTIPENLTEDFDVLTSIFDLGITSIELLKLKRGIEDLIGHGQIPLITLMTNPTIRTLSDALKQHAQQRDCSIYNPVVVLQSQGKKPPIWLVHPVGGEVMIFMNLAKFIIDRPVYGLRARGFNDGEDPFHTFEEIVSTYHASIKEKQPSGPYAIAGYSYGAKVAFDIAKALEHNGDEVRFLGLLDLPPSLNGTQMRAVAWKEMLLHICRMVGVIREEGIKKIYPRLEPENISPRHAIETVMGEADVTRLAELGLTASALERWANLTHALQRCIVDHKTNGSVAGADAFYCDPMASMAISNEQWACDYIGKWSDHTRSPPRFHHIAGTHYTILDAENIFSFQKTFLRALNDRGI", "text": "FUNCTION: Nonribosomal peptide synthetase that mediates the biosynthesis of phenguignardic acid (PubMed:26851300, PubMed:29305695). PngA alone is sufficient for phenguignardic acid synthesis (PubMed:26851300, PubMed:29305695). PngA first activates phenylpyruvic acid (PPA) through its A domain to AMP-PPA (PubMed:26851300, PubMed:29305695). The PPA unit is then loaded to the T domain and eventually transferred to the TE domain (PubMed:26851300, PubMed:29305695). Another PPA unit is then loaded onto the T domain (PubMed:26851300, PubMed:29305695). The TE domain likely promotes the enolate formation on the attached unit, followed by a nucleophilic attack on the carbonyl to yield an ether linkage between the two units (PubMed:26851300, PubMed:29305695). Finally, the TE domain probably catalyzes a similar reaction to give the cyclized dioxolanone core and releases phenguignardic acid (PubMed:26851300, PubMed:29305695). SIMILARITY: Belongs to the NRP synthetase family."}
{"protein": "MSGELPPNINIKEPRWDQSTFVGRANHFFTVTDPRNILLTNEQLENARKVVHDYRQGIVPPGLTENELWRAKYIYDSAFHPDTGEKMILIGRMSAQVPMNMTITGCMMTFYRTTPAVLFWQWINQSFNAVVNYTNRSGDAPLTVNELGTAYVSATTGAVATALGLNALTKHVSPLIGRFVPFAAVAAANCINIPLMRQRELRAGIPVTDENGNRLGESANAAKQAITQVVISRILMAAPGMAIPPFIMNTLEKKAFLKRFPWMSAPIQVGLVGFCLVFATPLCCALFPQKSSMSVTSLEAELQAKIRETSPELRRVYFNKGL", "text": "FUNCTION: Amino acid transporter importing serine, an essential substrate of the mitochondrial branch of the one-carbon pathway, into mitochondria. Mitochondrial serine is then converted to glycine and formate, which exits to the cytosol where it is used to generate the charged folates that serve as one-carbon donors. May also transport other amino acids including alanine and cysteine. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sideroflexin family."}
{"protein": "MSILFYVIFLAYLRGIQGNNMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPERGGPAKSAFQPVIAMDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGSPVVANRTSRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT", "text": "FUNCTION: Seems to promote the survival of visceral and proprioceptive sensory neurons. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NGF-beta family."}
{"protein": "MFSKVIDPEMLEDCFYIRKKVFVEEQGVPEESEIDEYESESIHLIGYDNGQPVATARIRPINETTVKIERVAVIKSHRGQGMGKMLMQAVESLAKDEGFYVATMNAQCHAIPFYESLNFKMRGNIFLEEGIEHIEMTKKLTSLN", "text": "FUNCTION: Could catalyze the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. SIMILARITY: Belongs to the UPF0039 (ElaA) family."}
{"protein": "MTSQIRQNYSTEVEAAVNRLVNLHLRASYTYLSLGFFFDRDDVALEGVGHFFRELAEEKREGAERLLKLQNERGGRALFQDVQKPSQDEWGKTLEAMEAALALEKNLNQALLDLHALGSARTDPHLCDFLESHFLDKEVKLIKKMGNHLTNLRRVAGPQPAQTGVAQASLGEYLFERLTLKHD", "text": "FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). SIMILARITY: Belongs to the ferritin family."}
{"protein": "MADVSTSMRLKLPVVCFILEIILIILFGALVQYDYETDAKEWHNQSHNDYENDFYFRYPSFQDVHVMIFIGFGFLMTFLQKYGFGSVGFNFLIAAFSLQWATLMQGFFHGMHGGKIHVGVESMINADFCTGSVLISFGAVLGKTSPIQLLTMAMFEVTLFAVNEFILLSLLGTRDAGGSMTIHTFGAYFGLMVTRILYRPHLDKSKHRNSSVYHSDLFAMIGTIYLWMFWPSFNSAITAHGDDQHRTALNTYYSLAACTLATYGMSAVTSHDGKLDMVHIQNAALAGGVAVGTAGEMMLTPFGSMIVGFLAGIISVLGFKFLSPILESKLKIQDTCGVHNLHGMPGVLGAIVGAVTAALATMDVYGKGMEDVFPAVADGSIDASKQGGVQALSLAITLGIALLGGLIVVFGTPPDTLCFEDGVYWEVPESEAPHEAQLTTVRTEETEKLSS", "text": "FUNCTION: Functions as an ammonia transporter. May play a role in the elimination of ammonia in the gill (By similarity). SUBCELLULAR LOCATION: Basolateral cell membrane; Multi- pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily."}
{"protein": "MPLWLPDDETFASFWPGDNPSLLAALQTMLRHDRSGYIYFWSREGGGRSHLLHAACAELSQRGDAVGYVPLDKRTWFVPEVLEGMEQLSLVCIDNIECIAGDEPWEMAIFNLYNRILESGNTRLLITGDRPPRQLNLKLPDLASRLDWGQIYRLQPLSDDDKLQALQLRARMRGFELPEDVGRFLLKRLDREMRTLFLTLDQLDRASISAQRKLTIPFVKDTLGL", "text": "FUNCTION: Mediates the interaction of DNA replication initiator protein DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for reinitiation, a process called regulatory inhibition of DnaA or RIDA (By similarity). SIMILARITY: Belongs to the DnaA family. HdA subfamily."}
{"protein": "MGSNGADNAHNNAFGGGKNPGIGNTSGAGSNGSASSNRGNSNGWSWSNKPHKNDGFHSDGSYHITFHGDNNSKPKPGGNSGNRGNNGDGASAKVGEITITPDNSKPGRYISSNPEYSLLAKLIDAESIKGTEVYTFHTRKGQYVKVTVPDSNIDKMRVDYVNWKGPKYNNKLVKRFVSQFLLFRKEEKEKNEKEALLKASELVSGMGDKLGEYLGVKYKNVAKEVANDIKNFHGRNIRSYNEAMASLNKVLANPKMKVNKSDKDAIVNAWKQVNAKDMANKIGNLGKAFKVADLAIKVEKIREKSIEGYNTGNWGPLLLEVESWIIGGVVAGVAISLFGAVLSFLPISGLAVTALGVIGIMTISYLSSFIDANRVSNINNIISSVIR", "text": "FUNCTION: Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. FUNCTION: This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the channel forming colicin family."}
{"protein": "MSVYDAAFLNTELSKPTSIFGLRLWVVIGILLGSLIVIALFLLSLCLTSRRKNRKPRADFASAAIATPPISKEIKEIVPAQNQSVPAEIQVDIGKIEHRVVFSDRVSSGESRGTASASETASYSGSGNCGPEVSHLGWGRWYTLRELEAATNGLCEENVIGEGGYGIVYRGILTDGTKVAVKNLLNNRGQAEKEFKVEVEVIGRVRHKNLVRLLGYCVEGAYRMLVYDFVDNGNLEQWIHGDVGDVSPLTWDIRMNIILGMAKGLAYLHEGLEPKVVHRDIKSSNILLDRQWNAKVSDFGLAKLLGSESSYVTTRVMGTFGYVAPEYACTGMLNEKSDIYSFGILIMEIITGRNPVDYSRPQGETNLVDWLKSMVGNRRSEEVVDPKIPEPPSSKALKRVLLVALRCVDPDANKRPKMGHIIHMLEAEDLLYRDERRTTRDHGSRERQETAVVAAGSESGESGSRHHQQKQR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MKKYKILLVIGDGLGDRQVASLNGRTPLENADKPTIASLLRSSLVGLMDPIGPGIVPGSDTSHLAIFGLDPKKYYKGRGSFEALGAGAILTEGDIAFRGNFATVDSNLVVIDRRAGRKIEEAEDLVKELNDKIQEIDGVKVRFYHGTEHRVSVVLSGDNLSDKVSDTDPHEVGKRILNSEPTDDALSSKRTANIINALTRRIYEVLSNSQLNDKRVREGLPPANIVLLRGASIHTELPKLKDYTGLSGAAVSATALIKGVCKSLGMEVVTPPGATGGIDTDYMAKAEAAAKLLEDHDLVFLHIKATDAASHDGKVSEKVKAIEMIDRSIGRVLDRYGSELVVLFTGDHATPVELREHSGDPVPLMLYVPTNIIPDNVGDFNERQARKGSLKITGLNIIDLLLNFSNRATKYGA", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily."}
{"protein": "MIDTTLPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIEDAARHGLHYVELRFSPGYMAMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQITALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPGVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKRALREKVAAK", "text": "FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenosine deaminase subfamily."}
{"protein": "MTIKLRFVASLALVFGLAAASVPAQASGGDTPHLQSWSFAGPFGQYDKAQLRRGFQVFQNVCVSCHTLENGGFRNLPSRAAPNWPLDEVRQLAASWPVQVKDINDKGDPMQRAPKLPDRIPSQYANEAAARIIHNGAVPPDLSVIAKARTFQRGFPWWVTDIFTQYNENGVDYIVALLNGYEDPPERFKVPDGSFYNKYFPGHIIGMTPPIADGLVTYGDGTPETQLQYSKDVAAFLMWAAEPTLDVRKRIGWWVLGFLVIFTGLLVATKIVVWRPVKKGLA", "text": "FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. c1 functions as an electron donor to cytochrome c. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MEECKLDINKGKDAEILYEEYKYHEIKEMSFSSCARTSPELLKKFGCDAHVITSVEGAPKKENKKIWEFFKGSNKIKNLFTMFTCCFANDEEEIWGEETNESVVYKEYTYNSRWKIEIPSYPVREIPYVVADTPYNKLLCPLSSLEWVSKLILMDNANSIGMKNNRYSTNPFIYGMCYIIRNNANRILLESCYCENSTGMSTCPRILEFMPYEPLLKYNSYRLLSTYENSYKELSEMLTNNNAPLEVLIHHVMLYHYYPSFLQSALWTAVSSYLEERCNNGLYSKLLVKAAKQHFGDIRLYFVTPDDIYTFDHCNNWIAIVTRNFMAYIETKRKLEFDSIPFNCPLITQLFPLISSPKEMAWLLLIVCTDSNESWFPVHAYINTKTRILRPRSPKLDFFLKESDLLYFQDKQSISEFDIIRKDLLEDLIQCDSYVNTREQLRRRRETLNRKRITIAKLQNNHSQITFPYKRHNIHKSVDSIQFCKPASNLLTLKDNSYTQIPLEPLLLAEISV", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Golgi apparatus Vacuole membrane. SIMILARITY: Belongs to the UPF0300 family."}
{"protein": "MADTVRKKQKLVVVGAGPVGSLAALYAAARGDEVEIYELRGDLRDPSTVPLNFTKSINLALSERGITAMKHSNREDLVNNVLRDTIPMHGRMIHGRDRGKLWEAAQAYDVHGRAINAVDRSTLNNALLDELECTPNVKLFFNHKLTGADFNARKAWFERRVPGEAPLPNSANRVPEIEVDFDFMIGADGAHSAARYHMMKFARVDYQQEYIDTLWCEFRIPPTEDGDFRISPNHLHIWPGREFMFIALPSADKSFTCTLFAPAAHYKHLGSSPQNLVESFKDHFPGVCPELISPEDLQEQFTTNPHLPLISLKCKPHHYNSSIVIVGDAAHAVLPFYGQGLNAGLEDIRVLFECLDKHGSYNLDASPDARREARAKAFQAYTDQRCADTHAINDLSKQNYLEMRWGVKTPLYKLRKSVEEALDRYVPSLGWQTQYSRVSFSNQRYSDVIRSARWQGRILALGLATTLISTVGVIAYVFWKKPRQYSPLSLLRYSWRRLSSIWVTMFRTIAYA", "text": "FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid. SUBCELLULAR LOCATION: Mitochondrion outer membrane. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO subfamily."}
{"protein": "MPEDQAGAAMEEASPYSLLDICLNFLTTHLEKFCSARQDGTLCLQEPGVFPQEVADRLLRTMAFHGLLNDGTVGIFRGNQMRLKRACIRKAKISAVAFRKAFCHHKLVELDATGVNADITITDIISGLGSNKWIQQNLQCLVLNSLTLSLEDPYERCFSRLSGLRALSITNVLFYNEDLAEVASLPRLESLDISNTSITDITALLACKDRLKSLTMHHLKCLKMTTTQILDVVRELKHLNHLDISDDKQFTSDIALRLLEQKDILPNLVSLDVSGRKHVTDKAVEAFIQQRPSMQFVGLLATDAGYSEFLTGEGHLKVSGEANETQIAEALKRYSERAFFVREALFHLFSLTHVMEKTKPEILKLVVTGMRNHPMNLPVQLAASACVFNLTKQDLAAGMPVRLLADVTHLLLKAMEHFPNHQQLQKNCLLSLCSDRILQDVPFNRFEAAKLVMQWLCNHEDQNMQRMAVAIISILAAKLSTEQTAQLGTELFIVRQLLQIVKQKTNQNSVDTTLKFTLSALWNLTDESPTTCRHFIENQGLELFMRVLESFPTESSIQQKVLGLLNNIAEVQELHSELMWKDFIDHISSLLHSVEVEVSYFAAGIIAHLISRGEQAWTLSRSQRNSLLDDLHSAILKWPTPECEMVAYRSFNPFFPLLGCFTTPGVQLWAVWAMQHVCSKNPSRYCSMLIEEGGLQHLYNIKDHEHTDPHVQQIAVAILDSLEKHIVRHGRPPPCKKQPQARLN", "text": "FUNCTION: Serves as substrate adapter subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC. Acts redudantly with ZER1 to target substrates bearing N-terminal glycine degrons for proteasomal degradation (PubMed:33093214). Involved in the clearance of proteolytic fragments generated by caspase cleavage during apoptosis since N- terminal glycine degrons are strongly enriched at caspase cleavage sites. Also important in the quality control of protein N- myristoylation in which N-terminal glycine degrons are conditionally exposed after a failure of N-myristoylation (PubMed:31273098). SIMILARITY: Belongs to the zyg-11 family."}
{"protein": "MPALTYLLLAAIGASTVHSLPSQQSCNAPVTPSSFSSTSLDVVIVGGGTAGLVLASRLSESKKLQVGVIEGGYDRTNDPLIDVPNAANALGYQGAVFGNSTYDWEYTSVPQRGLGGRVLSYPSGKVLGGSSAINGLTIQRGSREDYDAWGNAFGNGPEWTFDALLPYFKRYERWHAPTLSATGDLNSDGLSAVHGTDGRISISYNNFFTGVDIPLTQAGIALGLGPTQNPDGGDDSLFPNFGASHSLDPATGNRSYAANGYYGQTERCRSNLHLLTGAVVTRIIWDKKKATKAVGVEYAVGNDKFTVKASKEVVLSAGSLRSPQILELSGVGNKTLLESLNIPVVVDIPQLGENLQEQFIAGTDFLVRDGVVTLDALGNNATFLAEQQNLYRTNKTGAFTYLSNVNAPTPIRSLVTEDQYKTMRAALDTYLASQTLTPLQIVQYNLVKQFLDGGKVATSSLLVVASGGLVSTPAAGQGYISVVSSPAHPLSRGNVHINTTDPLAYPLIDSAFLTNPWDAQATINVMKFVRRWVAKSDIIESPGTPPQAADEWSDDQWIAYLQSVLGTAHHPVGTAAMASQKLGGVVDPRFKVYGLKNVRIVDASVFPMHIGVAPSSTTYMLAEKAADAIKKDLNAY", "text": "FUNCTION: Dehydrogenase, part of the gene cluster that mediates the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols (Probable). The first step in melleolides biosynthesis is performed by the delta(6)-protoilludene synthase PRO1 which catalyzes the cyclization of farnesyl diphosphate to protoilludene (PubMed:21148562). The orsellinic acid synthase armB produces OA by condensing acetyl-CoA with 3 malonyl-CoA units in a three-round chain elongation reaction folowed by a C2-C7 ring closure (By similarity). ArmB further catalyzes the trans-esterification of OA to the various sesquiterpene alcohols resulting from the hydroxylation of protoilludene (By similarity). The melleolides cluster also includes 5 cytochrome P450 monooxygenases, 4 NAD(+)-dependent oxidoreductases, one flavin-dependent oxidoreductase, and one O-methyltransferase (By similarity). The cytochrome P450 monooxygenases may be involved in protoilludene hydroxylation to elaborate melleolides with multiple alcohol groups, such as melleolide D, which carries alcohol functionalities at C-4, C-5, C-10, and C-13 (By similarity). The role of the NAD(+)-dependent enzymes remains unknown (By similarity). Numerous melleolides, including arnamial, show 5'-O-methylation of the aromatic moiety which may be catalyzed by the methyltransferase encoded in the cluster (By similarity). The flavin-dependent oxidoreductase might represent the dehydrogenase yielding the aldehyde in position 1 of arnamial and other melleolides (By similarity). Finally, several halogenase localized outside of the cluster, are able to catalyze the transfer of a single chlorine atom to the melleolide backbone, resulting in a 6'-chloromelleolide product (By similarity). SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MSFSSQSSKSSAESTLQKFLSGIVPVEAVQAGKARSQSKAQSVNNQLKTRALSADEVRRLQKKAKLKQQRKLKKQQEEAKKVNKLAKHQIIKSHKENNELTVEEEKYLNKIVKRNANSLSRLSEIEDYELKSELESLQEEILAAQRKSNKKTKQKSKKDFNEKLKRGKISYPGLTPGLAPVGLDDDDEDSD", "text": "FUNCTION: Involved in ribosome biogenesis, probably through modulation of rDNA transcription. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRT14 family."}
{"protein": "MGECMLKTNICGIEFKNPVFLASGIMGETGSALKRIAKGGAGAVTTKSIGLNPNPGHKNPTIVEVYGGFLNAMGLPNPGVDEYLEEIEKVRDELNRMDVRIIGSIYGKDEEEFAEVAKKMERYVDIIELNISCPHAKGYGATIGQNPDLSYDVCKAVKKAVKIPVFAKLTPNVTDIIEIAQAVVDAGVDGLVAINTVRGMAIDIRAKKPILANKFGGLSGKAIKSIGIKVVWDLYENFDVPIIGVGGIMSGEDAIEYMMAGASAVQIGSGVYYRGYDIFKKVCDEIISFLKEENLTLEEIVGMAHE", "text": "FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily."}
{"protein": "MTVKKLYFIPAGRCMLDHSSVNSALTPGKLLNLPVWCYLLETEEGPILVDTGMPESAVNNEGLFNGTFVEGQILPKMTEEDRIVNILKRVGYEPDDLLYIISSHLHFDHAGGNGAFTNTPIIVQRTEYEAALHREEYMKECILPHLNYKIIEGDYEVVPGVQLLYTPGHSPGHQSLFIETEQSGSVLLTIDASYTKENFEDEVPFAGFDPELALSSIKRLKEVVKKEKPIIFFGHDIEQEKSCRVFPEYI", "text": "FUNCTION: Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL. FUNCTION: Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL (By similarity). FUNCTION: Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily."}
{"protein": "MGISRDHWHKRRATGGKRKPIRKKRKFELGRPAANTKLGPQRIHTVRTRGGNKKYRALRLDTGNFSWGSECTTRKTRIIDVVYNASNNELVRTKTLVKNAIVTIDATPFRQWYEGHYVLPLGRKRGAKLTEAEEEVLNKKRSKKAEAKYKARQRFAKVEPALEEQFATGRVLACISSRPGQCGREDGYILEGKELEFYMRRIKSKKAK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family."}
{"protein": "MSDTETKPSSDGGEKKDGEYIKLKVIGQDNSEIHFKVKMTTHLKKLKESYSQRQGVPVNSLRFLFEGQRITDNLTPKELGMEDEDVIEVYQEQTGGCRND", "text": "FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. SUBCELLULAR LOCATION: Nucleus membrane Nucleus speckle Cytoplasm Nucleus, PML body Cell membrane Nucleus. SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily."}
{"protein": "MEKSWFNLMFSKGELESRGELSKAMDSFAPSEKTTISQDRFIYDMDKNFYGWGERSSYSNNVDLLVSSKDIRNFISDDTFFVRDSNKNSYSIYFDIKKKFFEIDNDFSDLEIFFYNYCSSSYLNNRSKGDNDLHYDPYIKDTKYNCTNHINSCIDSYFRSHICIDSNFLSNSKNSNESYIYNFICSESGKIRESKNYKIRTNRNRSNLISSKDFDITQNYNQLWIQCDNCYGLMYKKVKMNVCEQCGHYLKMSSSERIELSIDPGTWNPMDEDMVSADPIKFHSKEEPYKNRIDSAQKTTGLTDAVQTGTGQLNGIPVALGVMDFQFMGGSMGSVVGEKITRLIEYATNQCLPLILVCSSGGARMQEGSLSLMQMAKISSVLCDYQSSKKLFYISILTSPTTGGVTASFGMLGDIIIAEPYAYIAFAGKRVIEQTLKKAVPDGSQAAESLLRKGLLDAIVPRNLLKGVLRELFQLHAFFPLNKN", "text": "FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the AccD/PCCB family."}
{"protein": "MRLSYVSLTLAIIFVMAIVHAPETEAKAYPEADAVGEASAVGEADAVGVADPGVGSLLAKAALKILKIVAPAAAEVIANKIG", "text": "FUNCTION: Induces paralysis 5 minutes after injection into blowflies (L.caesar) (PubMed:32182430). In most cases is not lethal 24 hours after injection, but paralysis is irreversible (PubMed:32182430). May have antimicrobial properties, like most ant linear peptides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily."}
{"protein": "MAVCIAVIAKENYPLYIRSTPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSSRAFDNMVTSMMIQVC", "text": "FUNCTION: Plays a role in vesicular transport from endoplasmic reticulum to Golgi. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Endoplasmic reticulum Golgi apparatus. SIMILARITY: Belongs to the TRAPP small subunits family. Sedlin subfamily."}
{"protein": "MASSAKRRAVETGQNPQDSDESSDEGLEDSGDDDSENSEEEVNEEVIVDFEAHTISDNDFHGIKTLLQQLFLKCHVNTSDLTDIIIQQNHIGSVIRQAEVPEDSDDEGDPDEVFGFISMVNLTERQGVECLEKLKDMILDQCVKCSTPDGQERMENLLQGNAQSVGLLLSERFVNVPPQIALPLHKQLQKEMAEAQRTNKPSGKCQFCLMISKTCKPLKKKSISAGDQAKDELLFVNDEEECFYEQATVKFSYCVQDEADSCATGKWSYDDEPMKPFRTVMVIPMDRMDTIMQKMTDYLTV", "text": "FUNCTION: During interphase, required for microtubule organizing and anchoring activities. During mitosis, required for the organization and stabilization of the spindle pole. May promote cell cycle arrest and DNA repair. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, spindle pole. SIMILARITY: Belongs to the BCP1 family."}
{"protein": "MRGLVTAVRTLTVLPVPGKEAERFSSALFWFPVVGLFLGLLQAGAGYLAMLSGWPELAASMVLIAGVLLTRGMHADGFADMADGFFGGRDRESRLRIMKDPSVGSFGAIGLILLFLFKSIVLVKLLAFGLYPWIVSGVLLARLVQVALASMLPYARREGGTAAGFVEGAGIQHFVAAFLVALFILLLLMNGEMLPSGIGLSAAIAGAVLMSLLTIKKIGGVTGDVLGASSEFTEVLVWVSGVFLALCS", "text": "FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CobS family."}
{"protein": "MEGKEEDVRLGANRYTERQPIGTAAQGAEEKDYREPPAAPVFEVEELTSWSFYRAGIAEFVATFLFLYISILTVMGVNKSASKCATVGIQGIAWSFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRAVFYMAMQCLGAICGAGVVKGFQRGLYMGSGGGANAVNPGYTKGDGLGAEIVGTFVLVYTVFSATDAKRNARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIVYNRAHAWHDHWIFWVGPFIGAALAAIYHVVVIRAIPFKSRD", "text": "FUNCTION: Water channel required to facilitate the transport of water across cell membrane. Increases the capacity for root water uptake under water deficit. May play a role in drought avoidance in upland rice. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC 1.A.8.11) subfamily."}
{"protein": "MRKGGIQDAEPVEPPQSSRKSGTWFAKRPSEMPERHVERAPVRQKINNVGLYKATLYSNIGSFFFGIAVGWSGTAERSVMEQHSYSFQPTELQWSGVCILLTLGAALWCLPMGLMVRLLGCRRTILIQLLPNFLGWFLTVFARSVPMLYAGRFFLGMCGGAHCVVVPIYNAEISTTKKRGAMGVVFEGACICGVIYSFAMSLFLELRIINFVNLGLLALGPLQILMPESPAYYVDHGNIPRAEDSLRFLRGQKYDTRREIDFLTRDPTESEREVRQGPLLGFKYKKVRRSLARSLAIALLQKLCGALIFIFYGLNMLDCLRIRREFGLILCLGLILGFLACFFLVDRLGRRPLLIFSSAGIVFVSIYLGLHFKVWMTMGLTVMSWIALFCIAIFVGCYTAGVGSLTWVLNAELLVRPMRPLGCSIVCAFNWLTAFFVICWFGSHGVKCQPYLFLLFAIIASLILLFSLIYIPETKKLSSAKIQQRLGGLINRPAVITFTSSSDSSNA", "text": "FUNCTION: Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Perikaryon Cell projection Note=Localized to densely spaced patches along neuronal processes. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily."}
{"protein": "MRTPMSDTQHVQSSLVSIRSSDKIEDAFRKMKVNETGVEELNPYPDRPGERDCQFYLRTGLCGYGSSCRYNHPTHLPQDVAYYKEELPERIGQPDCEYFLKTGACKYGPTCKYHHPKDRNGAQPVMFNVIGLPMRLGEKPCPYYLRTGTCRFGVACKFHHPQPDNGHSTAYGMSSFPAADLRYASGLTMMSTYGTLPRPQVPQSYVPILVSPSQGFLPPQGWAPYMAASNSMYNVKNQPYYSGSSASMAMAVALNRGLSESSDQPECRFFMNTGTCKYGDDCKYSHPGVRISQPPPSLINPFVLPARPGQPACGNFRSYGFCKFGPNCKFDHPMLPYPGLTMATSLPTPFASPVTTHQRISPTPNRSDSKSLSNGKPDVKKESSETEKPDNGEVQDLSEDASSP", "text": "FUNCTION: Possesses RNA-binding and ribonuclease activities in vitro. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSNSKFNVRLLTEIAFMAALAFIISLIPNTVYGWIIVEIACIPILLLSLRRGLTAGLVGGLIWGILSMITGHAYILSLSQAFLEYLVAPVSLGIAGLFRQKTAPLKLAPVLLGTFVAVLLKYFFHFIAGIIFWSQYAWKGWGAVAYSLAVNGISGILTAIAAFVILIIFVKKFPKLFIHSNY", "text": "FUNCTION: Probably a thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Thiamine transporter subfamily."}
{"protein": "QGYGFNEPEQTRNQGGSSWEAP", "text": "FUNCTION: Probable transcriptional activator which may play a role in neuronal differentiation. Able to bind DNA and activate expression in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus matrix. SIMILARITY: Belongs to the AKAP95 family."}
{"protein": "MQPFHTLSRILPFPDATQKAWWDKLAPMLLKAMQAQGYDTEAQYAQLGMVYKCVLPYLGQYPTVENDATRWKSFLCPYGIPIEPSLNISQGILRYAFEPIGPDVGTDKDPQNMNVIQDCLKGLTDHDDRIDTTLYAQFASRLLLTKEESQRVAATGQFTFKPGQGMHGYAVDMKGSQPMVKGYFCVGIKSAVTGIPTGKLMLDAVREVDTEGRITEPLDKLEDYYGNALGNLRLCFMSVDMIDPQDARTKLYGLQQEVSFEGLEDLWTLGGRINTPTNQEGLQLLRELWDLLQIPPGVRDIEVDHCSVGQPPKYLLPSLVNWTFLPGHSDPMPQVYLVPFGLPDAHISDALVTFFERRGWTDLARSYKSNLASYFPDVDFSQSRHVQEAISFSFRKGKPYLSVYMSLF", "text": "FUNCTION: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid (PubMed:35843946). The pathway begins with the biosynthesis of the cyclic dipeptide cyclo-L- Trp-L-Ala (cyclo-TA) by the NRPS criC via condensation of L-alanine and L-tryptophan (PubMed:35843946). The prenyltransferase criA then catalyzes the first prenylation step, a reverse prenylation reaction at C2, to yield preechinulin (By similarity). Preechinulin is the substrate of the cytochrome P450 monooxygenase criE that catalyzes the formation of the double bond between C10 and C11 to produce neoechulin A (By similarity). The unique prenyltransferase criF functions as a competitive enzyme with criE for preechinulin metabolization and uses preechinulin for effective regiospecific prenylations. Preechinulin is prenylated by criF at C5 or C7. C7-prenylation leads to accumulation of tardioxopiperazine B without further modification by criF. In contrast, the C5-prenylated tardioxopiperazine A can be prenylated again by criF, predominantly at C7 to form echinulin or less frequently at C4 to give variecolorin L. CriF accepts also neoechilunin A to produce varlecolorin G (prenylation at C5) or isoechinulin A (prenylation at C7). CriF further converts isoechinulin A into dehydroechinulin. Moreover, a yet unidentified enzyme can also convert neoechilunin A into neoechilunin B by introducing a double bond between positions C14 and C17 and thus provides a further substrate to criF for C5 and C7 prenylation (By similarity). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family."}
{"protein": "MANVALLGCTGMVGSHILTHLLGNSSVARIDTISRRTPQPATAAPQEKLTTFVSDDSSKWASQLSSLTPTPDIFISAFGTTRGAAGGFENQYKIEHGLNVEMARAARDAGTKVYVLISSTGADKNSSFGYPRMKGEIEEEVKAMGFDRTIILRPGLISGERQESRPAEAVMRGFAGLVGKIHSGLKDGWAQDADVIAKAAVNAGVKALNGEVPAGSEKVWVMYGKDIIQYGKGQ", "text": "SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein. SIMILARITY: Belongs to the FMP52 family."}
{"protein": "MKTLLFIYLQLLLLLSIIIGRVVKVEYLHLVVEVEPSTITESCLSDGIDGYSGSFYLNTTFAELMLKEHNNKRKLHQSCPLKWSSELFNYASQFAAEYSCSGILQHSGGKYGENLAFGYSPIGAIEAWYDEGEMYVYGSENVYNHFTAIVWNNTNSLGCAYKSCDTTTNLNALYIVCSYYPPGNVIGYSSQNVFPLNSKMVN", "text": "FUNCTION: Secreted protein that acts as a virulence factor during infections. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MSPKQVTCRYFLHGVCREGSRCLFSHDLATSKPSTVCRFFLRGQCAYGTRCRYDHVKPCNGTVFIPPQEMSPVLSPPPLFPAQEAAVPPTIPAPQRREKKTLVLRDRDLCGASVDPALQPGCITESQGSEGEAKPHSYLEAICTGLDESQDPASYPGAPQQLCPFAQAGECHCGDSCPYLHGDACEICGLQVLHPHDQEQRRDHEKLCMENFELDMERAFAVQASEGRVCSICMERVYEKQSPAQRRFRILSDCNHTYCLTCIRQWRCARQFDNPVIKSCPECRVISEFVIPSAYWVEDQSKKDELIEAFKQGMGKKLCKYFDQGRGTCPFGGKCLYLHSYPDGTRAQPEKPRKQLGSEGSVRFLNSLRLWDFIEDREQRGVPNAEVGKLGELFMHLSGADEELPAPFN", "text": "FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Inhibits neurogenesis and axis formation during embryonic development by modulating the phosphatidylinositol 3-kinase (PI3K) pathway (PubMed:18198183). Acts downstream of PI3K and akt1 to up-regulate gsk3b mRNA expression (PubMed:18198183). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MRIGHGYDVHRLVEDRKLIMGGVDIPWEKGLLGHSDADVLLHAIADALLGALAMGDIGKHFPDTDPAFKGADSMKLLEHVVGLIRTQGYAVGNLDATIIAQRPKMAPHIQAMRENVARACGVEVDRINVKATTEEGLGFTGTGEGISAHAVVLLIPQ", "text": "FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). SIMILARITY: Belongs to the IspF family."}
{"protein": "MTRIKRGYIARRRIKKFRLFASSFLNAHSRLTRTITQQKIRALVSSDRDRNNKKRKFRSLWITRINAVIREEGVSYSYKNFIYAQYKIQLLINRKILAQIAILNRNFFYMIFNEIRKEADLKEYIRIN", "text": "FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity). SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
{"protein": "MAGNQQLRVLHALDIARTQLYHFIAIVIAGMGFFTDAYDLFSISLVADLLGHVYYHGELPRNIHAAVTGIALCGTVPGQLVFGWLGDKMGRKRVYGITLLLMVVSSLASGLSFSKHEGMNIIAVLCFFRFWLGVSIGGDYPLSATIMSEYANKRTRGAFIAAVFAMQGFGNLAAGIIGMIVSAAFKHSSASKIDYAWRIILMFGAIPAALTYHWRMKMPETARYTALISKNAKKAAKDMSAVLNVNITPDDEVINELARQDEYGLFSFEFLHRHGLHLLGTTVCWFVLDVTFYSLNIFMKNIFTEVGLLPRLDSEYHHTLQRMITMTAVHTFISLCGALPGYFFTVAFVDRIGRVKIQLIGFTMMTVFMLCLAIPYDQWLRHKNKYGFAVMYGLTFFFANFGPNTTTFIIPAEIFPARLRSTCHGISGAVGKIGAIVGVFGFLYTEYHIRIFLFVLIGCNLVGFIFTLLLPESKGKSLEDLTGEIEEFQEEDEGSEVALSRPIHTVPL", "text": "FUNCTION: High-affinity transporter for external inorganic phosphate. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. phosphate:H(+) symporter (TC 2.A.1.9) family."}
{"protein": "MSEEKRKQHFVLVHGACHGAWCWYKVKPLLEALGHRVTALDLAASGIDTTRSITDISTCEQYSEPLMQLMTSLPNDEKVVLVGHSFGGLSLALAMDKFPDKISVSVFVTAFMPDTKHSPSFVEEKFASSMTPEGWMGSELETYGSDNSGLSVFFSTDFMKHRLYQLSPVEDLELGLLLKRPSSLFINELSKMENFSEKGYGSVPRAYIVCKEDNIISEDHQRWMIHNYPANLVIEMEETDHMPMFCKPQLLSDHLLAIADNFC", "text": "FUNCTION: Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity, methyl salicylate (MeSA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro. SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase family."}
{"protein": "MAEGLVLKGTMRAHTDMVTAIATPIDNADIIVSASRDKSIILWKLTKDDKAYGVAQRRLTGHSHFVEDVVLSSDGQFALSGSWDGELRLWDLAAGVSTRRFVGHTKDVLSVAFSLDNRQIVSASRDRTIKLWNTLGECKYTISEGGEGHRDWVSCVRFSPNTLQPTIVSASWDKTVKVWNLSNCKLRSTLAGHTGYVSTVAVSPDGSLCASGGKDGVVLLWDLAEGKKLYSLEANSVIHALCFSPNRYWLCAATEHGIKIWDLESKSIVEDLKVDLKAEAEKADNSGPAATKRKVIYCTSLNWSADGSTLFSGYTDGVIRVWGIGRY", "text": "FUNCTION: Major component of the RACK1 regulatory proteins that play a role in multiple signal transduction pathways. Involved in multiple hormone responses and developmental processes (PubMed:16829549, PubMed:18715992, PubMed:18947417). MAPK cascade scaffolding protein involved in the protease IV and ArgC signaling pathway but not the flg22 pathway (PubMed:25731164). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Detected in the cytoplasm and nucleus when interacting with NUDT7. SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily."}
{"protein": "MLVMKLFTCFLQVLAGLAVHSQGALSAGNNSTEVEVVPFNEVWGRSYCRPMEKLVYILDEYPDEVSHIFSPSCVLLSRCSGCCGDEGLHCVPIKTANITMQILKIPPNRDPHFYVEMTFSQDVLCECRPILETTKAERRKTKGKRKRSRNSQTEEPHP", "text": "FUNCTION: Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Also promotes cell tumor growth (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the PDGF/VEGF growth factor family."}
{"protein": "MAAPTAAALSTLSTASVTSGKRFITSSFSLSFSSRPLATGVRAAGARAARRSAASASTVVATIAVGDKLPDATLSYFDPADGELKTVTVAELTAGRKAVLFAVPGAFTPTCSQKHLPGFIEKAGELHAKGVDAIACVSVNDAFVMRAWKESLGLGDADVLLLSDGNLELTRALGVEMDLSDKPMGLGVRSRRYALLADDGVVKVLNLEEGGAFTTSSAEEMLKAL", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides (By similarity). May be involved in chloroplast redox homeostasis (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily."}
{"protein": "YVPKLEEERIVIYSTMDRADLAEHRLEAICAAMIESWGYSELTHQIRRFYSWLLQQQPFASIAQEGKAPYIASMALRKLYMDRAVDEEELRVFTEMMVALDDEFECDSYEVHHQANDTIDTGGNSKKDVKPEQGSIQPSSNKGKEKDVNAGTSGTHTVPRIKAITAKMRMPKSKGAAVLKLDHLLEYAPQQIDISNTRATQSQFDTWYEAVRVAYDIGETEMPTVMNGLMVWCIENGTSPNINGVWVMMDGSEQVEYPLKPIVENAKPTLRQIMAHFSDVAEAYIEMRNKKEPYMPRYGLVRNLRDASLARYAFDFYEVTSRTPVRAREAHIQMKAAALKSAQSRLFGLDGGVSTQEENTERHTTEDVSPSMHTLLGVKNM", "text": "FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to- cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication. SUBCELLULAR LOCATION: [Capsid protein]: Virion. SIMILARITY: Belongs to the potyviridae genome polyprotein family."}
{"protein": "MVDEMVLITQQWLNDTYSGKHGYNPVEESGKTGWDTIYGLTRALQIELGISEPADNFGPTTQRLFKPLKRQAPDSKPSNMNFILQGALWCKGFNPGGFTGVFYEKTENAVKEFQKAAGLTTQDGIVTTLIMKALLDMSAFKLVSGGDSRIRQIQQNLNRDYNDYIGLMPCDGLYGRDTNKALIYALQKEEGMSTSVANGFFGNGTTSLCPTLTPGDSRTGFVLIVQYALYCNGKSFDPGEFDGKYGVGVVSAVKAFQEFMCLPQTGYADMPTIKALLSSSGDTTRTASACDTATIITAEKAQTLRNNGYKTVGRYLTGNVRTSSGLTSKALTSKELAVILDAGLKVFPIYQDGGYESSYFVKDQGTRDAYSAASAARRLGFPSGTTIYFAVDFDAYDYEVTDKIIPYFQEIKSAFTKMQTFSTAPKYEIGVYGPRNICIRTSEAGLTKYSFVANMSTGFSGNLGYPMPNNWAFDQFYEGTIGSGSGSIGIDKDGYSGRDSGASNVNPPSDPVYDARLRTLTDILSTIPALENLTSLANAMFEFDTTETIFTSPELDIILSTSLLATIPSEGSPNTITITNGKPGAYITGLLGDTQTSLTASQIDSYQNLLNSLSLSVRNGYLEVYVNPTAESLNIQIKIYTPDIPVGDNVTTGLTTTITFKIKTYKGVPVTSPESELALDWPSYDQYLFPVVGVAALLLIGNMGSDLTNNKGVKVATALSAMLLAIFAYYTS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FadG family."}
{"protein": "MKLKKKMLTLLLTASMSFGLFGATSSAATDYWQYWTDGGGMVNAVNGPGGNYSVTWQNTGNFVVGKGWTVGSPNRVINYNAGIWEPSGNGYLTLYGWTRNALIEYYVVDSWGTYRPTGNYKGTVNSDGGTYDIYTTMRYNAPSIDGTQTFQQFWSVRQSKRPTGSNVSITFSNHVNAWRSKGMNLGSSWAYQVLATEGYQSSGRSNVTVW", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MAASETVRLRLQFDYPPPATPHCTAFWLLVDLNRCRVVTDLISLIRQRFGFSSGAFLGLYLEGGLLPPAESARLVRDNDCLRVKLEERGVAENSVVISNGDINLSLRKAKKRAFQLEEGEETEPDCKYSKKHWKSRENNNNNEKVLDLEPKAVTDQTVSKKNKRKNKATCGTVGDDNEEAKRKSPKKKEKCEYKKKAKNPKSPKVQAVKDWANQRCSSPKGSARNSLVKAKRKGSVSVCSKESPSSSSESESCDESISDGPSKVTLEARNSSEKLPTELSKEEPSTKNTTADKLAIKLGFSLTPSKGKTSGTTSSSSDSSAESDDQCLMSSSTPECAAGFLKTVGLFAGRGRPGPGLSSQTAGAAGWRRSGSNGGGQAPGASPSVSLPASLGRGWGREENLFSWKGAKGRGMRGRGRGRGHPVSCVVNRSTDNQRQQQLNDVVKNSSTIIQNPVETPKKDYSLLPLLAAAPQVGEKIAFKLLELTSSYSPDVSDYKEGRILSHNPETQQVDIEILSSLPALREPGKFDLVYHNENGAEVVEYAVTQESKITVFWKELIDPRLIIESPSNTSSTEPA", "text": "FUNCTION: Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. SUBCELLULAR LOCATION: Nucleus Nucleus, Cajal body. SIMILARITY: Belongs to the coilin family."}
{"protein": "MAGARRRARCPASAGCAYSARPPPLSTRGRRISAGSGQPRWWPWGSPPPPDTRYRRPGPGRRARSCLHAGPRGRPPHSRTRARRTSPGAGGGGWRGGSCTSQR", "text": "SIMILARITY: Belongs to the epstein-barr virus RPMS1 family."}
{"protein": "MSWSAAQYAKFEDERTRPARDLLAQVPDLPAGPAFDLGCGPGNSTELILARFPGSPLTGIDSDDDMLSAARTRLPDLRFERGDLAAWTPPAESALFFANAVFQWLPEHVTLFERLILALAPGGTLAVQMPDNLDEPTHLLMEETAEESAFAPAFAGRTIRRRSLPSPATYVERLASKEVRVDVWHTVYYHQLANANAIVEWVKGTGLRPYLDALPTTQRAGYLAAYAEKIRKAYPAMKNGRVLLRFPRLFIVATRNL", "text": "FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. Tam family."}
{"protein": "MSDLGESPSSSPPAPPADTAPPPETPSENSALPPVDSSPPSPPADSSSTPPLSEPSTPPPDSQLPPLPSILPPLTDSPPPPSDSSPPVDSTPSPPPPTSNESPSPPEDSETPPAPPNESNDNNPPPSQDLQSPPPSSPSPNVGPTNPESPPLQSPPAPPASDPTNSPPASPLDPTNPPPIQPSGPATSPPANPNAPPSPFPTVPPKTPSSGPVVSPSLTSPSKGTPTPNQGNGDGGGGGGGYQGKTMVGMAVAGFAIMALIGVVFLVRRKKKRNIDSYNHSQYLPHPNFSVKSDGFLYGQDPGKGYSSGPNGSMYNNSQQQQSSMGNSYGTAGGGYPHHQMQSSGTPDSAILGSGQTHFSYEELAEITQGFARKNILGEGGFGCVYKGTLQDGKVVAVKQLKAGSGQGDREFKAEVEIISRVHHRHLVSLVGYCISDQHRLLIYEYVSNQTLEHHLHGKGLPVLEWSKRVRIAIGSAKGLAYLHEDCHPKIIHRDIKSANILLDDEYEAQVADFGLARLNDTTQTHVSTRVMGTFGYLAPEYASSGKLTDRSDVFSFGVVLLELVTGRKPVDQTQPLGEESLVEWARPLLLKAIETGDLSELIDTRLEKRYVEHEVFRMIETAAACVRHSGPKRPRMVQVVRALDCDGDSGDISNGIKIGQSTTYDSGQYNEDIMKFRKMAFGGDNSVESGLYSGNYSAKSSSDFSGNESETRPFNNRRF", "text": "FUNCTION: Regulates the auxin-related MAX (More Axillary Growth) pathway during the shoot branching. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MARELAAVYAQVFDLAAEVSLLGYCDPSSIDKRCVMANSNKVFKLCESLLPCLRLQNDTECSPLSLELQHLLQNTREALGVLTDLLSGDPSRSEYFEALHPSRPLEGPCKRHARVRVPFYGGAEKTVSLSLLNDVEVFFKRLNSVFYCLPAEGALEALGETVAFLGRLRGVSPIPPADAYVSSVPCASCFAEAAMLPNQGESVLSMLAAVNCNHVCRQVPSDPVIGVFENELRHLGADARAAGRAGGGRESERRGREDADDEEDDEEEPRDGQGDAGDGAALRVLTESSLSVLAGHTIFEEEDGRLAEISNLVYWSSAADRGGVGGTARATSSSHMAKLFAHEARMHRSRAWLGRGAPSHFFDAHRPSPLESLFCGGVFNSIDDTIAALQKDCSATFLKKSNYQTLIQQQNELYVRLNEVLNGAGRDEGGAKGAEAIADAEPLKPDGGASCDPRDVLSDARVRRDLYLKKLTRDGLRRLTDCIETHGRVLSDTLSLRVWGSALYASAARLVNHFLFRRQFVGLGWADLTAGGEAAFENSKYIKNALHGQRLNREHLDSIVVHFYRLITGPLSLQNSHFPVPDNVALAYCLDAAGAMPHQKLVITEMIWPGIESKDWIDCNFNSFYSIETGDLNLTQKKTLNYIREAVLSISLYNRVWEKSLSLLSATELRGSCLAESASGELGEGVYLTYEGTAPLVLVFDSKGYVFKDLYTLLYTHLQLSGRRQASV", "text": "FUNCTION: Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes. SUBCELLULAR LOCATION: Host nucleus Note=Found associated with the external surface of the viral capsid during assembly and DNA packaging, but seems absent in extracellular mature virions. SIMILARITY: Belongs to the herpesviridae TRM1 protein family."}
{"protein": "HLLQFNKMLKFETRKNAVPFYAFGCYCGWGGQRRPKDATDRCCFVHDCCYEKVTKCNTKWDFYRYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPDSRCREPSETC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that has anticoagulant activity and inhibits bactericial growth of the Gram-negative bacteria Xanthomonas axonopodis pv. passiflorae (in monomeric form). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3- sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
{"protein": "MAASVLNTVLRRLPMLSLFRGSHRVQVPLQTLCTKAPSEEDSLSSVPISPYKDEPWKYLESEEYQERYGSRPVWADYRRNHKGGVPPQRTRKTCIRRNKVVGNPCPICRDHKLHVDFRNVKLLEQFVCAHTGIIFHAPYTGVCVKQHKRLTQAIQKARDHGLLIYHIPQVEPRDLDFSTSHGAVSATPPAPTLVSGDPWYPWYNWKQPPERELSRLRRLYQGHLREESGPPPESMPKMPPRTPAEASSTGQTGPQSAL", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family. Mitochondrion-specific ribosomal protein mS40 subfamily."}
{"protein": "DAEFRHESGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV", "text": "FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane; Single-pass type I membrane protein Perikaryon Cell projection, growth cone Membrane, clathrin-coated pit Early endosome Cytoplasmic vesicle Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N- glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. SIMILARITY: Belongs to the APP family."}
{"protein": "MRDSVLSVIFALALFLECYTPSMAIPMGKMEDTALEQDTLDSLLNEEVADKNPDSVRSGSSKIIVLADSGMWKNLNRGLPLYKLKAAAAGLDRALTLDRREADQDLSPSISIVRRDTMRCMVGRVYRPCWEV", "text": "FUNCTION: Plays a role in skin pigmentation by antagonizing the action of melanotropin alpha. Induces melanin concentration within the melanophores. May participate in the control of the hypothalamo- pituitary adrenal gland axis by inhibiting the release of ACTH. SIMILARITY: Belongs to the melanin-concentrating hormone family."}
{"protein": "MSDPLHVTFVCTGNICRSPMAEKMFAQQLRHRGLGDAVRVTSAGTGNWHVGSCADERAAGVLRAHGYPTDHRAAQVGTEHLAADLLVALDRNHARLLRQLGVEAARVRMLRSFDPRSGTHALDVEDPYYGDHSDFEEVFAVIESALPGLHDWVDERLARNGPS", "text": "FUNCTION: Key virulence factor required for mycobacterial survival within host macrophages (PubMed:16085396, PubMed:18474358, PubMed:22087003, PubMed:25187516, PubMed:25642820, PubMed:27698396). Exhibits protein tyrosine phosphatase activity (PubMed:10986245, PubMed:12066895, PubMed:17975835, PubMed:23102706, PubMed:25187516, PubMed:32142609). Shows no detectable activity towards substrates containing phosphoserine/threonine residues (PubMed:10986245, PubMed:12066895). FUNCTION: Key virulence factor required for mycobacterial survival within host macrophages (By similarity). Exhibits protein tyrosine phosphatase activity (By similarity). FUNCTION: Supports mycobacteria survival during infection by modulation of the phagosome maturation and modulation of the normal host signaling pathways, including host innate immune responses and cell apoptosis. FUNCTION: Supports mycobacteria survival during infection by modulation of the phagosome maturation and modulation of the normal host signaling pathways, including host innate immune responses and cell apoptosis (PubMed:18474358, PubMed:22087003, PubMed:25187516, PubMed:25642820, PubMed:27698396). Affects the phagocytosis process by preventing phagosome acidification and maturation in the macrophage (PubMed:22087003, PubMed:16085396, PubMed:18474358). This inhibition depends on both PtpA phosphatase activity and its ability to bind to host vacuolar-H(+)-ATPase (V-ATPase) machinery (PubMed:22087003). Enters into the host cytosol and binds to subunit H of the human V- ATPase machinery to block V-ATPase trafficking and phagosome acidification (PubMed:22087003). Dephosphorylates and inactivates host VPS33B protein, which inhibits phagosome maturation, fusion with the lysosome and promotes bacteria survival (PubMed:18474358, PubMed:22087003). Dephosphorylation of VPS33B requires interaction of PtpA with host V-ATPase and ubiquitin (PubMed:22087003, PubMed:25642820). Binding to host ubiquitin also leads to the dephosphorylation of phosphorylated Jnk and MAPK p38, leading to suppression of innate immunity (PubMed:25642820). Dephosphorylates host GSK-3 alpha on Tyr-279, which leads to modulation of GSK-3 alpha anti- apoptotic activity, promoting pathogen survival early during infection (PubMed:25187516). In vitro, dephosphorylates two subunits of the trifunctional enzyme TFP (ECHA/ ECHB), which means that it may also affect pathways involved in cell energy metabolism (PubMed:25743628). Furthermore, blocks innate immune system responses mediated by the host adapter TAB3 and dependent on NF-kappa-B by competitively binding the ubiquitin-interacting domain of TAB3, in a phosphatase activity- independent manner (PubMed:25642820). Antagonizes TRIM27-promoted JNK/p38 MAPK pathway activation and cell apoptosis through competitively binding to the RING domain of TRIM27 (PubMed:27698396). In addition, PtpA enters the nucleus of host cells and regulates the expression of several host genes, some of which are known to be involved in host innate immunity or in cell proliferation and migration, either by directly binding to the promoters of its target genes, or in an indirect manner (PubMed:28811474). In vitro, can bind directly to the promoter region of GADD45A, a gene encoding a protein involved in cell division, cell death and senescence, and DNA-damage repair (PubMed:28811474). SUBCELLULAR LOCATION: Secreted Host cytoplasmic vesicle, host phagosome Host cytoplasm Host nucleus Note=Translocates into the host cytosol by crossing the host phagosomal membrane during human macrophage infection. Colocalizes with host VPS33B in macrophage cytosol and associates with phagosomes. SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase family."}
{"protein": "MLYTSIFAAAMAASGAMAAPTTSHGASNCTTLDSFFKSHGKLYWGTAADKNTLMKPGVADFIAKEFGQVTPENSMKFDATEPSRGQFHFDAADYLVDYAEKHDLLIRGHTFLWWSQMPAWVKAIKDKDTLIDVIQTHISTVAGRYKGKIYAWDVVNEIFEQDGSFRKTVYYNLLGEDYVRIAFEAAHKADPKAKLYINDFNLDDPNAAKLKAMIKYVTKWRAAGWPVHGIGSQSHLFAGMGEKSAAAIKMLGAAADEVAITELDITGAPQADYEAVTKGCIDVKNCVGITSWGARDTDSWLASKSPLLFDGNFKPKAAVKAIMAI", "text": "FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family."}
{"protein": "MSSISNVYHDYSSFSNATTFSQVYQNFNQLDNLNVFEKLWGSYYYYMANDLFATGLLFFLTHEIFYFGRCLPWAIIDRIPYFRKWKIQDEKIPSDKEQWECLKSVLTSHFLVEAFPIWFFHPLCQKIGISYQVPFPKITDMLIQWAVFFVLEDTWHYWFHRGLHYGVFYKYIHKQHHRYAAPFGLAAEYAHPVEVALLGLGTVGIPIVWCLITGNLHLFTVSIWIILRLFQAVDAHSGYEFPWSLHNFLPFWAGADHHDEHHHYFIGGYSSSFRWWDFILDTEAGPKAKKGREDKVKQNVEKLQKKNL", "text": "FUNCTION: C-4 methylsterol oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:10783002). ERG25 is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4- dimethylfecosterol into fecosterol via 4-methylfecosterol (PubMed:10783002). Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols (PubMed:10783002). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4- dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3- beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron- containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C- methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl- methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen- 3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MIIDILNSDSDPAGRNIRAAIDELLKNPPEGGFPLFDGNEVTFHTVSGRIIHAEKSAVNPDADLIIVVSRHSSVNPVPVLTVHPAGNFGIAGLGGNDRELGLTSPAWMKSILQNHAEFVPEGYRVSYEITHHGPTDFPVPFFFVEVGSTEKEWNDPAACIAAAKSVLYARPSPEIVPLIGFGGTHYAVRQTAIGLETKGAFGHMMHTRDVGSVSKEMVSQMIAKSCGVFAAHIDRKALSKQEISHIEGILAEVGLEEITEGDLRKMNAMSFSTWVAYRDLAALQAPGLKIFPHGRIFDGDPAVVELPSDLFSAAFLGYEEIFLAELDKMGNIFHTTGKGGRLMPTLLTSAKNRQKVSGDLIVLSVQQITRTQDSLVEGDQITIARRQFDPVLARTLGVPSGPLYGQLVAGKPVTLPDGRMITPDMVTKVVRTSIKIPGLENYS", "text": "FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. SIMILARITY: Belongs to the DtdA deacylase family."}
{"protein": "MKAARWHNQKDIRIEHIEEPKTEPGKVKIKVKWCGICGSDLHEYLGGPIFIPVDKPHPLTNETAPVTMGHEFSGEVVEVGEGVENYKVGDRVVVEPIFATHGHQGAYNLDEQMGFLGLAGGGGGFSEYVSVDEELLFKLPDELSYEQGALVEPSAVALYAVRSSKLKAGDKAAVFGCGPIGLLVIEALKAAGATDIYAVELSPERQQKAEELGAIIVDPSKTDDVVAEIAERTGGGVDVAFEVTGVPVVLRQAIQSTTIAGETVIVSIWEKGAEIHPNDIVIKERTVKGIIGYRDIFPAVLSLMKEGYFSADKLVTKKIVLDDLIEEGFGALIKEKSQVKILVRPN", "text": "SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MFQRLNKMFVGEVTTSSSQEPEFSEKEDDEWILVDFIDTCPGFSAEEEEEDEDIGEESSAEHTSVFSCLPASLECLTDTSDSCFLQFESCPMEESWFITPPPCFTAGGLTTIKVETSPMENLLIEHPSMSVYAVHNSCPGLSEASCGNDEYNSSGPRMEAQSEMGKHIHCCVAALAAQATFLEQPKSFRPSQWIKGHSERQSLNRNGLRRQNLTRDCHTRQMKHSGWVVHQPCPRQYNY", "text": "FUNCTION: Antiproliferative and proapoptotic protein involved in cell stress response which acts as a dual regulator of transcription and autophagy. Acts as a positive regulator of autophagy. In response to cellular stress or activation of autophagy, relocates to autophagosomes where it interacts with autophagosome-associated proteins GABARAP, GABARAPL1/L2, MAP1LC3A/B/C and regulates autophagy. Acts as an antioxidant and plays a major role in p53/TP53-driven oxidative stress response. Possesses both a p53/TP53-independent intracellular reactive oxygen species (ROS) regulatory function and a p53/TP53-dependent transcription regulatory function. Positively regulates p53/TP53 and p73/TP73 and stimulates their capacity to induce apoptosis and regulate cell cycle. In response to double-strand DNA breaks, promotes p53/TP53 phosphorylation on 'Ser-46' and subsequent apoptosis. Acts as a tumor suppressor by inducing cell death by an autophagy and caspase-dependent mechanism. Can reduce cell migration by regulating the expression of SPARC. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Nucleus, PML body Cytoplasmic vesicle, autophagosome Note=Shuttles between the nucleus and the cytoplasm, depending on cellular stress conditions, and re-localizes to autophagosomes on autophagy activation."}
{"protein": "MGQTAGDLGWRLSLLLLPLLLVQAGVWGFPRPPGRPQLSLQELRREFTVSLHLARKLLSEVRGQAHRFAESHLPGVNLYLLPLGEQLPDVSLTFQAWRRLSDPERLCFISTTLQPFHALLGGLGTQGRWTNMERMQLWAMRLDLRDLQRHLRFQVLAAGFNLPEEEEEEEEEEEEERKGLLPGALGSALQGPAQVSWPQLLSTYRLLHSLELVLSRAVRELLLLSKAGHSVWPLGFPTLSPQP", "text": "FUNCTION: Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN- gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR which appears to be required but not sufficient for IL-27- mediated signal transduction. IL-27 potentiate the early phase of TH1 response and suppress TH2 and TH17 differentiation. It induces the differentiation of TH1 cells via two distinct pathways, p38 MAPK/TBX21- and ICAM1/ITGAL/ERK-dependent pathways. It also induces STAT1, STAT3, STAT4 and STAT5 phosphorylation and activates TBX21/T-Bet via STAT1 with resulting IL12RB2 up-regulation, an event crucial to TH1 cell commitment. It suppresses the expression of GATA3, the inhibitor TH1 cells development. In CD8 T-cells, it activates STATs as well as GZMB. IL-27 reveals to be a potent inhibitor of TH17 cell development and of IL-17 production. Indeed IL27 alone is also able to inhibit the production of IL17 by CD4 and CD8 T-cells. While IL-27 suppressed the development of pro-inflammatory Th17 cells via STAT1, it inhibits the development of anti-inflammatory inducible regulatory T-cells, iTreg, independently of STAT1. IL-27 has also an effect on cytokine production, it suppresses pro-inflammatory cytokine production such as IL2, IL4, IL5 and IL6 and activates suppressors of cytokine signaling such as SOCS1 and SOCS3. Apart from suppression of cytokine production, IL-27 also antagonizes the effects of some cytokines such as IL6 through direct effects on T-cells. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines such as IP- 10/CXCL10 and MIG/CXCL9. In vein endothelial cells, it induces IRF1/interferon regulatory factor 1 and increase the expression of MHC class II transactivator/CIITA with resulting up-regulation of major histocompatibility complex class II. IL-27 also demonstrates antiviral activity with inhibitory properties on HIV-1 replication. SUBCELLULAR LOCATION: Secreted Note=Does not seem to be secreted without coexpression of EBI3. SIMILARITY: Belongs to the IL-6 superfamily."}
{"protein": "MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMKLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQSHFDWVRPGIILYGVSPLEDRSIGADFGCQPVMSLTSSLIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD", "text": "FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. SIMILARITY: Belongs to the alanine racemase family."}
{"protein": "MSEVNLSGMTALSIGRGVTLNNASELEAALRHIGATRYHNHHPFHKLLHSGKLNKGQVQAWALNRYYYQSTIPLKDAMVMTRFRDRATRLEWRHRIEDHDGDVGTEGGIERWIKLTEGLGLDTAYVESTEGILPATRFAVEAYVHFCRDRSPLEAIASSLTELFAPSIHEERISGMLEHYSFVNNDTMSYFKRRLTQAPRDANFALHYVREHATTPEQRAAVCNALIFKTNVLWVQLDALYHAYVEGHIPPGAFVPKEG", "text": "FUNCTION: Ring cyclization and eight-electron oxidation of 3a-(2-amino- 2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9- dicarboxylic-acid to PQQ. SIMILARITY: Belongs to the PqqC family."}
{"protein": "MALSTSAIGFEGYENRLEISFFEAGIFSDPEGRGLRALSKEQLDKVLKPAECTIVSSLSNNEVDSYVLSESSLFVYPYKIIIKTCGTTKLLLSIPPILELADGLSLKVKSVKYTRGSFNFPEVQPYPHRNFSEEVAILDSYFGKLSTGSKAYVMGGAGKQQQWHVYSASAESAENTFPIYTLEMCMTGLDKKSASVFFKTQSSSAAVMTDASGIRKILPGSEICDFDFEPCGYSMNAVEGGAISPIHVTPEDGFSYASFEAMGYDFKDVNLDALIQRVLSCFQPAEFSVALHCDSIGEKLDSVFKLDVKGYACGERSYEGLNKGGSIMYCGFTSTGSCGSPRSTLLCCWSENEDEEGEKKHF", "text": "SIMILARITY: Belongs to the eukaryotic AdoMetDC family."}
{"protein": "MEGLYKEAVTFADRYNLLNVYGISAVIAVGLAIYSASLAIYRLYFHPLAGFPGPRIAAATRWYEFYYDVIKRGQYVYKIEEMHQKYGPIIRINPHEIVINDPDFYNSVYVAGNTRRTAIWPRYRTGIGFDGSHTMTENHELHRRRRKPLEPFFSRMGIDKMEPMIIEEAKLLNDRLTGLKGSGNVIRLDHVFSAFAGDVIGRICSESPPDMMNHPEFGKEWSAQFDREYRETAPFVHARPATGLVSSLSQSTSACPNRDRLARMIPTGFLLRVYPGAAGFNVFRQLAISHIVDAKKDNFSKEKVEKNSKSSVFRYIITSEMPASECETERLSREAMVLFGAGTATTARTMGFMCYYILTNPHMRERLADELRDVMADYPHKLPSWQELERLPYLQAMIKEGLRLSYGVMRRLPRISPDIPLVYKQWSIPAGTPVGMAAYSLHTDPEVYPEPFKFIPERWLGKYDSRMDRNWVPFSRGSRNCLGMK", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of talaronoid C, a fusicoccane diterpenoid with an unprecedented tricyclic 5/8/6 ring system (PubMed:36126322). The first step in the pathway is performed by the fusicoccadiene synthase tndC that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and further converting GGDP into talarodiene, a precursor for talaronoid C (PubMed:36126322). The remaining enzymes from the cluster include the cytochrome P450 monooxygenase tndB, the aldehyde reductase tndE and the alcohol dehydrogenase tndF that are involved in the conversion of talarodiene into talaronoid C (PubMed:36126322). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MVLMILPIIGSVSASEGLVAMVTLCLVYMIMKYMHTEIPEGLKRLPGPKPLPIIGNMLEVHNNPHLSLTAMSERYGSVFQIQIGMRPVVVLSGNETVRQALIKQGEDFAGRSDLYSFKFINDGKSLAFSTDKAGVWRARRKLAMSALRSFATLEGTTPEYSCALEEHVLKEGEYLVKQLTSVMDVSGSFDPFRHIVVSVANVICGMCFGRRYSHDDQELLGLVNMSDEFGQVVGSGNPADFIPILRYLPNRTMKRFMDINDRFNNFVQKIVSEHYESYDKDNIRDITDSLIDHCEDRKLDENANIQVSDEKIVGIVNDLFGAGFDTISTALSWAVVYLVAYPETQERLHQELKEKVGMIRTPRLSDKINLPLLEAFILEIFRHSSFLPFTIPHCTIKDTSLNGYFIPKDTCVFINQWQVNHDPELWKEPSSFNPDRFLSADGTELNKLEGEKVLVFGMGKRRCIGEAIGRNEVYLFLAILLQRLRFQEKPGHPLDMTPEYGLTMKHKRCQLKASMRPWGQEE", "text": "FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MAFPKKKLRGLVAATITPMTENGEINFPVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVNQGRNKLDQVVIHVGALNVKESQELAQHAAEIGADGIAVIAPFFFKSQNKDALISFLREVAAAAPTLPFYYYHMPSMTGVKIRAEELLDGIQDKIPTFQGLKFTDTDLLDFGQCVDQNHQRQFALLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDLASALSYQFRIQRFINYVIKLGFGVSQTKAIMTLVSGIPMGPPRLPLQKATQEFTAKAEAKLKSLDFLSSPSVKEGKPLASA", "text": "FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family. NanA subfamily."}
{"protein": "MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGTMLRLFAEKIPVFQKILLKPSTESDLMPTSFGKIKPLGFERFRICELYAELLHCSNMSLLSDPNGEAMVMQRDHLRDYLFRHNSCARDLVMSDEDDDDSTFSDKNSKDFKETEDMNGAEDMHGRAPQITKDNLNLTTTDSPMSEAEPVSEEEYKDVMETAKALHHGDDDAASDTSYEPLPESVIEDAKKLPVIGDFLKIEFIQNNVIPTILDHFFDYPWNNFLHNVVYDVVQQVLNAPMDKDQNYALAVDMFKQGKITEKIVYGQELNDKKVAKPSGFRAGYMGHLTIIADEVVKFVEHYSSTFDQELLNLINDEKWQNFVNKTLVETRNRDNQLLGGLEPSMVGYLEDMDEGEMLDANNLPEMQFALEQELESNSSDDDVVEVHRELSHNSSSNDEDDGNDEDPLSREMSRRLSFESANDSDQDNRDHFAQYMSQQISDNNANQFSSSDEDDDDDDEVVEWVSRGNENKYPRSNFFINGSDREDFSDSEEEDGNDSSDDDRGFAEEEYSDGLVLNHGK", "text": "FUNCTION: Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. SUBCELLULAR LOCATION: Nucleus Note=Associated with chromatin. SIMILARITY: Belongs to the SAPS family."}
{"protein": "MGDGWLPPDCGPHNRSGGGGATAAPTGSRQVSAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGTWLWGSFLCECWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKEQIRKIDRCEGRFYGSQEQPQPPPLPQHQPILGNGRASKRKTSRVMAMREHKALKTLGIIMGVFTLCWLPFFLVNIVNVFNRDLVPDWLFVFFNWLGYANSAFNPIIYCRSPDFRKAFKRLLCFPRKADRRLHAGGQPAPLPGGFISTLGSPEHSPGGTWSDCNGGTRGGSESSLEERHSKTSRSESKMEREKNILATTRFYCTFLGNGDKAVFCTVLRIVKLFEDATCTCPHTHKLKMKWRFKQHQA", "text": "FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity (PubMed:18594507). In dorsal pons neurons, involved in the regulation of sleep/wake behaviors (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome Note=Colocalizes with RAPGEF2 at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily."}
{"protein": "MENLCPPPPSQMKDFSTPPRNRHRHKRSFAISGDFEFLKQPASAPVLPSAYDSPTFENTPRRVSGMSVTMPDESQNESALLNSPSPRFFISEASTYSSPIKGVPDAIINLDDVLINKPKMCRSHRKTKSVPVKLDEFYSSHKCSSVPELTINEEIDEDDTNPQLLEPVKPLSSTSLSTDMNEDKKMTLKNARSHNSLKIQAQKQRYYNSARYLPLNSEDRATDPQILTKQSSVTSLFSSRSITPVSCNINNAGRINAISGNYLDDVLYDLDTPATTLIQDIDNLQTSINERVRLSPQSSSIKKYFSKDGKSVSSFNFQSQECDMVSFTEDFAHVTSLSSSILDSEKQTDDEEEESIPEEILRGEPLHVYNETSGSDKSVILPTKQKSAPINKDSKHSSTQYEEKSFKKNRKFKIFAKLFCTRK", "text": "FUNCTION: Involved in cell wall composition and integrity and response to osmotic stress. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MLGRELRLRWRMCALRLLAISLGILLCTHFSAELRRRSGPPEKLVVAKVESTARDLNKRAEEMPSRRQVIYVRRSSSSSKAANPATNRRDNNKPIRWHIDLQPWASSSHSLDSEAIRFLRYITTTQIICSHRIKNGQTDQSVDASKPWTVCLDEKFNLAHQIRNKQCRVYSLGLGEDDNNFEVNMASRGCEVHRFDPSIASTQIHEGERLWHHRLSIDWRDPKPAIATHKLHITTKKLGTILNEFGHWKIDVLKADMESAEWKILENLILEGVVEQIGQLIFEIHLHWPGFEVSGNDSSVVRYWYSLFKELERKDFKLFYTYKDLSKPQRFLKKEIYNASSCYILSWVNTRWT", "text": "FUNCTION: Probable methyltransferase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the methyltransferase superfamily."}
{"protein": "MNDVIRDFFKMESAGGILLVIAAAIAMVIANSPLNESYQAVLHTYVFGMSVSHWINDGLMAIFFLLIGLEVKRELLEGALKSRETAIFPAIAAVGGMLAPALIYVAFNGNDPEAIKGWAIPAATDIAFALGIMALLGKRVPVSLKVFLLALAIIDDLGVVVIIALFYSGDLSTLALTVGFAMTGVLFMLNAKNVTKLIWYIVVGFILWVAVLKSGVHATLAGVVIGFSIPLQGKKGEHSPLKHMEHALHPYVAFAILPVFAFANAGISLEGVSLSGLTSMLPLGIALGLLVGKPLGIFTFSWAAVKFGVAKLPEGVNFKHIFAVSVLCGIGFTMSIFISSLAFGGANPDFDTYSRLGILMGSTTAAVLGYFLLHVSLPKTAAESEKAIS", "text": "FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family."}
{"protein": "MIVQFVALLLLNLLQIIAAESSHTNNWAVLISTSRFWFNYRHTANVLGIYRSVKRLGIPDSQIILMIADDYACNSRNLFPGTVFDNADRALDLYGEEIEIDYKGYEVTVEAFIRLLTERVPENTPASKRLLTNERSNILIYMTGHGGDGFIKFQDAEELSSEDLADAIEQIHQHKRYNEILFMVDTCQANSLYTKIYSPNVLAIGSSEVGTSSYSHHADIDIGVAVIDRFTFSNLEFLENRVDSKSKLTMQDLINSYNPYEIHSTPGVQPINLRRSPDDILITDFFGNVRDIELHSEKINWMLPGENTTKPSIKRNSFVFQAQNDMQDDGKGFGISNLKSFLPPTRELKYKKHPISRIISAVVCISFSIGFPYYASKYLK", "text": "FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase C13 family."}
{"protein": "MKISCFLLLILSLYFFQINQAIGPDTKKCVQRKNACHYFECPWLYYSVGTCYKGKGKCCQKRY", "text": "FUNCTION: Synthetic Defb38 kills both Gram-negative (E.coli and P.aeruginosa) and Gram-positive (E.faecium) bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MLVKIVLVVLLTLALVFECFSTISVPITIGLYISEYNGYRFGVFGWCKVDRSVCSPIRIGYSKDDILLFNEQEYLHLPNHAKYALSNLLLVHVLAFVCVTILWVFGMLTCFRCIKTSRRMLIIAVLWSMLTFMVTLLGFLIDILIFSSHVTWCTWLTLASAFFTVLSGTVLCVMRRNLTYDKFLESKPEKHGVYVPLCRLNDVEELEIPWCNTMNHQALTAPTPM", "text": "FUNCTION: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the palI/RIM9 family."}
{"protein": "MSATTSGTASAAELAKFSAMADAWWDPEGDFKPLHKFNPVRIAFLRDHFAAHFGRDIEAPRPFEGLSLLDIGCGGGLLCEPFARLGFAVTGIDAAERNIGTASVHAERAGLPLTYRCAMPEDLVAEGKTFDAVLTMEVVEHVADVRLFLDSVGQLCRPGGAVGAATLNRTLKSLALAKVGAEYVLRWLPRGTHDWRKFMKPSELTAGLREAGLSVDAIAGMTFDPFSGTWSQTTDVSVNYMLFATRAAA", "text": "FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. SIMILARITY: Belongs to the methyltransferase superfamily. UbiG/COQ3 family."}
{"protein": "MELGKSMENQTDVMVLLAKHVIPTVANGSNLVFSPMSINVLLCLIAAGSNCVTKEQILSFIMLPSSDYLNAVLAKTVSVALNDGMERSDLHLSTAYGVWIDKSLSFKPSFKDLLENSYNATCNQVDFATKPAEVINEVNAWAEVHTNGLIKEILSDDSIKTIRESMLILANAVYFKGAWSKKFDAKLTKSYDFHLLDGTMVKVPFMTNYKKQYLEYYDGFKVLRLPYVEDQRQFAMYIYLPNDRDGLPTLLEEISSKPRFLDNHIPRQRILTEAFKIPKFKFSFEFKASDVLKEMGLTLPFTHGSLTEMVESPSIPENLCVAENLFVSNVFHKACIEVDEEGTEAAAVSVASMTKDMLLMGDFVADHPFLFTVREEKSGVILFMGQVLDPSIH", "text": "FUNCTION: Probable serine protease inhibitor. SIMILARITY: Belongs to the serpin family."}
{"protein": "MVFRIASSPYTHNQRQTSRIMLLVLLAAVPGIAAQLWFFGWGTLVQILLASVSALLAEALVLKLRKQSVAATLKDNSALLTGLLLAVSIPPLAPWWMVVLGTVFAVIIAKQLYGGLGQNPFNPAMIGYVVLLISFPVQMTSWLPPHEIAVNIPGFIDAIQVIFSGHITSGGDMNTLRLGIDGISQATPLDTFKTSVRAGHSVEQIMQYPIYSGMLAGVGWQWVNLAWLAGGVWLLWQKAIRWHIPLSFLVTLALCATLGWLFSPETLAAPQIHLLSGATMLGAFFILTDPVTASTTNRGRLIFGALAGLLVWLIRSFGGYPDGVAFAVLLANITVPLIDYYTRPRVYGHRKG", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrB/RnfD family."}
{"protein": "MAELVQGQSAPVGMKAEGFVDALHRVRQIAAKIDSIPHLNNSTPLVDPSVYGYGVQKRPLDDGVGNQLGALVHQRTVITEEFKVPDKMVGFIIGRGGEQISRIQAESGCKIQIASESSGIPERPCVLTGTPESIEQAKRLLGQIVDRCRNGPGFHNDIDSNSTIQEILIPASKVGLVIGRGGETIKQLQERTGVKMVMIQDGPLPTGADKPLRITGDAFKVQQAREMVLEIIREKDQADFRGVRGDFNSRMGGGSIEVSVPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERAAQVMGPPDRCQHAAHIISELILTAQERDGFGGLAAARGRGRGRGDWSVGAPGGVQEITYTVPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNSDPNLRRFTIRGVPQQIEVARQLIDEKVGGTNLGAPGAFGQSPFSQPPAPPHQNTFPPRSSGCFPNMAAKVNGNPHSTPVSGPPAFLTQGWGSTYQAWQQPTQQVPSQQSQPQSSQPNYSKAWEDYYKKQSHAASAAPQASSPPDYTMAWAEYYRQQVAFYGQTLGQAQAHSQEQ", "text": "FUNCTION: May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSSTKTPISLTIKLNQFTDKPTGLDINPYHNSPIMWRNIIKQLSSRTPQKLLFSSKNRTYSFLGFGQDSIFKDNTKFRSLIPISCSNIVMGFQNLGEYLPGDEFLSRPLIKNQVNNNFCCRKSYASVAEAVAVSSTDAEEDVSVVDEVHELLTELKKEEKKQFAFRRRKQRMLTSGMGHRKYQTLKRRQVKVETEAWEQAAKEYKELLFDMCEQKLAPNLPYVKSLFLGWFEPLRDKIAEEQELCSQGKSKAAYAKYFYQLPADMMAVITMHKLMGLLMTGGDHGTARVVQAALVIGDAIEQEVRIHNFLEKTKKQKAEKDKQKEDGEHVTQEQEKLRKKVTNLMKKQKLRAVGQIVRRQDDSKPWGQDARAKVGSRLIDLLLQTAYIQPPANQLAVDPPDIRPAFVHSVRTVAKETKSASRRYGIIQCDELVFKGLERTARHMVIPYMPMLVPPVKWTGYDKGGHLYLPSYVMRTHGARQQREAVKRASRNQLQPVFEALDTLGNTKWRINKRVLSVVDRIWAGGGRLADLVDRDDAPLPEEPDTEDEALRTKWRWKVKSVKKENRERHSQRCDIELKLAVARKMKDEESFFYPHNVDFRGRAYPMHPHLNHLGSDICRGVLEFAEGRPLGESGLRWLKIHLANLFAGGVEKLSLEGRIGFTENHMDDIFDSSDKPLEGRRWWLNAEDPFQCLAVCINLSEAVRSSSPETSVSHIPVHQDGSCNGLQHYAALGRDKLGAAAVNLVAGEKPADVYSGIAARVLDIMKRDAQRDPAEFPDAVRARVLVNQVDRKLVKQTVMTSVYGVTYIGARDQIKRRLKERGAIADDSELFGAACYAAKVTLTALGEMFEAARSIMTWLGECAKIIASENEPVRWTTPLGLPVVQPYRKIGRHLIKTSLQILTLQRETEKVMVKRQRTAFPPNFIHSLDGSHMMMTAVACRRAGLNFAGVHDSYWTHACDVDKLNRILREKFVELYEAPILEKLLESFQTSYPTLLFPPLPERGDFDMRDVLESPYFFN", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion. SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase family."}
{"protein": "MVFTKEEVDYSLYLVTDSTMLPPGTTLCSQVEAGLKNGVTLVQIREKDIETKNFVAEALEVQKICKKYNVPLIINDRIDVAMAIDADGVHVGQDDMPIPMVRKLLGPSKILGWSVGKPSEVETLAKWGPDMVDYIGVGTLFPTSTKKNPKKSPMGPQGAIAILDALEEFKATWCRTVGIGGLHPDNIQRVLCQCVASNGKRSLDGISLVSDIMAAPDACAATKRLRGLLDATRYQFVECELNNTFPTTTSIQNVISQVSNNRPLVQHITNKVHQNFGANVTLALGSSPIMSEIESEVSELARIPNASLLLNTGSVAPIEMLKAAINAYNEVNRPITFDPVGYSATETRLCLNNTLLTYGQFACIKGNCSEILSLAKLNNHKMKGVDSSSGKTNIDTLVRATQIVAFQYRTVAVCTGEFDCVADGTFGGEYKLSSGTEGITAEDLPCVIIEDGPIPIMGDITASGCSLGSTIASFIGGLDSTGKLFDAVVGAVLLYKSAGKLASTRCQGSGSFHVELIDALYQLFHENKPEKWSASLKKFK", "text": "FUNCTION: Essential for thiamine biosynthesis. The kinase activity is involved in the salvage synthesis of TH-P from the thiazole. FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). SIMILARITY: In the N-terminal section; belongs to the thiamine- phosphate synthase family. SIMILARITY: In the C-terminal section; belongs to the Thz kinase family."}
{"protein": "MSEPVLVIDNGSYEIKFGESGWDQPLRALNCLTKDKYSRFHLSNQTKKMRDISQALIRRPHELGQLVSWELESEVWDYCFYNEDDFHWNLTHDNDTKDHHLVVSETLMTIPELSKNMDQVIFEEYDFKSMFKGPVAQYIPFYQGQYQDDAMTAAEDKKTSSYKDFQLVIDSGFNCTWAVPIIKGVPYYKAIKKLDIGGRFLTGLLQETISFRHYNVMEETILVNNIKEQCTFVPPESYFSSFHNKMNTKVEYVLPDFQTSFLGYVKKPGKEKLTDDAQTLLLTDEVFSVPETFFHPEIAQILKPGIVETILECINMCPEVVRPLLVANIVCTGGNFNIPNFHERLQTELQRQCPIDWSCKVHSPQEKDKSLHGWESMKDFANSDQFRSARVTREEYLEHGLDWCTKNRFGYQQWL", "text": "FUNCTION: Component of the SWR1 complex which mediates the ATP- dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Nucleus. SIMILARITY: Belongs to the actin family. ARP6 subfamily."}
{"protein": "MAVRLRRVKRANPYDLYRTCATGDCPQDVKDRFEHNTIADKILKWGSAGVFLGGLGIGSTQARPGLGTYSPLGRGGVTGRIPVRGPGSTRPLGRPFSSGPIDTIGAGVRTSVETSVTVPDVVAVLPESPAVITPDSMPVDPGVGGLDISAEIIEEPSLTFVEPHGPEDVAVLDVNPAEHDRSVYLSSSTTHHNPSFQGQVTVYTDIGETSETENLLISGSNIGSSRGEEIQMQLFSGPKTSTPETDAVTKVRGRANWFSKRYYTQTSVRDPTFIQEPQTYFYGFENPAYEPDPFEDSFDVQLASPSEPVQPELRDITHVSAARTFRGESGRVGISRLGQKSSIQTRSGVTVGGRVHFRYSLSTIEDAIEDAGEIELQVTNGSQGPSGSLQHTAETILSEGHDAYVDVDMDSVGSLYSDIDLIDEHSETPHGILVFHDEAETDVVPVIDVSYVRKPLSTIPGSDLWPTNINIQNGPVDVDLQDSILPGIIITDSGVDGTYFLNTYLHPSLHKRKKRRFS", "text": "FUNCTION: Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus by promoting escape from the endosomal compartments and traffic through the host Golgi network. Mechanistically, the C-terminus of L2 possesses a cell-penetrating peptide that protudes from the host endosome, interacts with host cytoplasmic retromer cargo and thereby mediates the capsid delivery to the host trans-Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of infection. Later on, promotes late gene expression by interacting with the viral E2 protein and by inhibiting its transcriptional activation functions. During virion assembly, encapsidates the genome by direct interaction with the viral DNA. SUBCELLULAR LOCATION: Virion Host nucleus Host early endosome Host Golgi apparatus. SIMILARITY: Belongs to the papillomaviridae L2 protein family."}
{"protein": "MGVDLTGVQKKKRVVRHHTYSTNPYIKLLIKLYKFLGKRTNSPFNKLIHKRLLKSRNNRAPISLSRIAVCMRRRTVWLKKGKKSPIAVIVGDVLDDVRMTRIPALRICALRFSKSARERITGAGGECLTFDQLAMMAPTGKNTMLLRGRKSGRESVKHFGAAGVPGSHAKPHVSSRGKERQRSSKRRHAFRHK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family."}
{"protein": "MYKGIVTPMITPMGQNGEIDYRATEILIDNLADFGVDGLFPMGSTGLFPMFSTDEKKKFLGFVRDHSKKIEVYAGVGSSSTQESVELSKYTEDIGIKVRVLMPTYYIKPDEDWMYRHFSTVISAASNDLFIYNIPQLSGSWISESLIEKLTREFSNVKGIKDSSGDMRFFSRIIRHKNEKFDIFQGQDDLLFLSLSIGASGGVCGLSNISPYITNLYHEFSAGNLEKARKIQIDEVNPLMYAINEATFPAGYYYAFYKMNGIKGGYRAPMVEPTTDQKKKIDQELTKIPKKQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family."}
{"protein": "MGPQRLLLVAAGLSLCGPLLSSRVPVRQPESEMTDATVNPRSFFLRNPGENTFELIPLGDEEEKNESTLPEGRAIYLNKSHSPPAPLAPFISEDASGYLTSPWLRLFIPSVYTFVFVVSLPLNILAIAVFVLKMKVKKPAVVYMLHLAMADVLFVSVLPLKISYYFSGSDWQFGSGMCRFATAAFYCNMYASIMLMTVISIDRFLAVVYPIQSLSWRTLGRANFTCLVIWVMAIMGVVPLLLKEQTTRVPGLNITTCHDVLNETLLQGFYSYYFSAFSAVFFLVPLIISTICYMSIIRCLSSSSVANRSKKSRALFLSAAVFCVFIVCFGPTNVLLIMHYLLLSDSPATEKAYFAYLLCVCVSSVSCCIDPLIYYYASSECQRHLYGILCCKESSDPNSYNSTGQLMPSKMDTCSSHLNNSIYKKLLA", "text": "FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MILTALRGALGFLTRIPVGRDEAAWAAFARSPWTFPVVGYLVGGLVALSLFVPAPAPTVALAFVLAVYAVTGIGHLDGVADIGDAAAVHGDREERRRVLKDSALGVGGTVALALVVLGLATAALGLVEVAATAGDGGPLPPVIGIVVAAEVGAKAATATLVCVGDAPHEGLGSALTGESSPGATLSVFALAAPAALLTWPQVLPGLAALLVALATAALVARWSRRRLGGVSGDVLGATTELARVAALHAGVIAWTRF", "text": "FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CobS family."}
{"protein": "MAGSRVPRQLFLQGVAAVFMFAFASLYTQIPGLYGPEGILPARRTLRPQGKGRWQQLWETPTLLWEAPLLGLDTAQGLELLSLLGTVLALGALLTRQLHHPLVYLLLWAAYLSVCQVGQVFLYFQWDSLLLETGFLAMLVAPLGLPPNHKQAPQGRPGGVSPHEGLPFWLVRWLLFRLMFASGVVKLTSRCPAWWGLTALTYHYETQCLPTPAAWFAHHLPVWLHKLSVVATFLIEIAVPPLFFAPVRRLRLAAFYSQVLLQVLIILTGNYNFFNLLTLVLTTALLDDTHLAAKSSTSRRKRMPSSWPKALLAMLTLLLELAVYGLLACGVVHYFGLEVDWEQHVVRSRTMFTFHQLSQWLKTVTLPTMWLGAASLAWELLTALWRWVQVRGSLRKLCAAVQLSVFGTATVALFLISLVPYSYMEPSSHGRLWTGAHRLFSTVEHLQLANSYGLFRRMTGLGGRPEVVLEGSYDGHQWTEIEFMYKPGNLSRPPPIVVPHQPRLDWQMWFAALGPHTHSPWFTSLVLRLLQGKEPVIRLVQNHVPSYPFHQQPPTYVRAQLYKYWFSHPWEQGQWWRRQWVEEFFPSVSLGDPALDMLLRQFGLQDKSPPRAGGSSNTLSQALHWVRKQLSPLEAPALLWGLLGAVGAIKVMQALLGPQSLPRTKEEKHKPAPQEDSVAASKQASPAPNISSGSQTPRRKKSP", "text": "FUNCTION: Involved in the maturation of specific proteins in the endoplasmic reticulum. May be required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the lipase maturation factor family."}
{"protein": "MASVEEIRNAQRAKGPATILAIGTATPDHCVYQSDYADYYFRVTKSEHMTALKKKFNRICDKSMIKKRYIHLTEEMLEEHPNIGAYMAPSLNIRQEIITAEVPKLGKEAALKALKEWGQPKSKITHLVFCTTSGVEMPGADYKLANLLGLEPSVRRVMLYHQGCYAGGTVLRTAKDLAENNAGARVLVVCSEITVVTFRGPSEDALDSLVGQALFGDGSAAVIVGSDPDISIERPLFQLVSAAQTFIPNSAGAIAGNLREVGLTFHLWPNVPTLISENIEKCLTQAFDPLGISDWNSLFWIAHPGGPAILDAVEAKLNLDKKKLEATRHVLSEYGNMSSACVLFILDEMRKKSLKGERATTGEGLDWGVLFGFGPGLTIETVVLHSIPMVTN", "text": "FUNCTION: Mediates resistance to pathogens which are sensitive to stilbenes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family."}
{"protein": "MFHSRALLLSWLVGFTAAKDIHLDWNITWVWAAPDGFGRPMIGINNEWPCPIVNADLGDRLIVDVHNGLGNQSTGIHWHGFHQYMTGTMDGSNQVTQCALPPGSSMRYEFDVNQTGTYWYHSHEMGQYPDGLRGPFIVRDPSPPFAYDDEFTLTLTDHYHEQMSVLLQQYEADSVGAQAGVNEPLPAAALINEGFDTTTLRVEPNKTYLIHLVCVGNWPGHVIVFDDHEISVVEVDGTWVDAYPARDKKIRLATGQRMSILLKTKDNTDRNYAIWDSMDVNMMFFYQNRAIPEGFNPNTTAWLVYDEAKELPPAPDVHELDPNNDFVDDLVFVPASHEPLLEKVDRQIIFDTGVTQRDGRSVYTINGQTYVDPEEPTLYTALAASPENASNASLYGQVNPFVVQYGEVVEIIINNHHGNLHPWHMHGHQFQVLQRTIPEGGYFDGYFANISSTPVKRDTIMVQNHGHAVLRFRANNPGVWLIHCHIEWHVTKGLTGTLIEAPAQMHKISVPLDHQRICPSYGTPPGGTPSSPPHDAPRPDGASGSPQYPPKPWGEPDASAPEQDDSQPGGTPDSPEDFPQPWGEPEESPQEPPQPWSPSNNAQPPANTYAPEYPSGYVPVAPGPVIIDSELHYGGKSSHVECSGVNAGHTQDTTTGGDGCANAS", "text": "FUNCTION: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:14970241, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN- melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN- melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622). SUBCELLULAR LOCATION: Secreted Cell surface Note=Localized at the surface of stalks and conidiophores, but not in young hyphae (PubMed:24123270). SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MAIHLTRIYTRTGDNGTTGLSDFSRVAKTDLRLVAYADCDETNSAIGVALALGNPDQKITDVLQQIQNDLFDAGADLSTPMQDSVRNPEYPQLRITQTHIDRLEEWCDTYNTPLPTLNSFVLPGGSPLSALLHVARTVARRAERSAWAAVEAHPGVVSMLPAKYLNRLSDLLFILSRVANTGNDVLWRPGG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family."}
{"protein": "MSSSKMNGRSIRINRVPATIFAILLTIVLVYFLNFHQEERPAIYGKLRSDNPNRVNLRKMLIAAIQASQRGGLEVLDVARSRQLKVRSKGQTDEGVNDPFTDADGRSHCVMKQGLQRIFPRVRIFSEEDKEHCKESHSYDLDPTVLHETAQVPDVSVNAQDVTVWVDPLDATKEFTEELYEYVTTMVCVAVAGRPVIGVIHSPFNGQTAWAWVGNSMSEYLAGLHPPHGQENELPIITVSRSHTAGAKDLARGIFGEQVNLLTAAGAGYKVLQVVANNATAYLHTSKIKKWDICAGDAILHALGGTMTTLNDQLIRYGPDESPVNTEGLLATLEKHDKYMDQLVKYRTAHNGQLA", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
{"protein": "MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRCDFQLIGIQDGFLSLLQDSGEVREDLRLPEGELGREIEQKYDCGEEIITIHGARFTTS", "text": "FUNCTION: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. SIMILARITY: Belongs to the eIF-5A family."}
{"protein": "MTSKPTCLIVASAASAGVSARSFQQCFNLCNPVFNLQTATPGGKSIDFTGVDDSTGRWVQEFSIKPYANPAKLESIDGARYQALLIPDCPGAMNDLAHSGSLARILSHFISQQKPVCAVGQGVAALCCATEDQKWIFSRYSMTGPSVFELVRSSEFANLPLIVEDFIKDNGGSYTASIEDAVHVVLDRHLITGQNIQSTTAAVNNLILLCNNR", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C56 family."}
{"protein": "MAVNLYDYANQLEQALRESEEYKAIKEAFANVKANEESKKLFDEFRETQINFQQKQMQGEEIAEEDLQKAQEQAQAIEKDENISALMNAEQKMSQVFQEINQIIVKPLDEIYAD", "text": "SIMILARITY: Belongs to the UPF0342 family. SIMILARITY: Belongs to the UPF0342 family."}
{"protein": "MVKNSFISIISQEQEEKEENKGSVEFQVFSFTNKIRRLTSHLGLHKKDFSSQRGLRIILGKRQRLLAYLSKKNRVRYKKLIGQLDIREPKTR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MDKPVCLIDTGSDGKLCVQQAALQVLQQIQQPVVVVAVVGLYRTGKSFLMNRLAGKRTGFALSSNIKPKTEGIWMWCMPHPTKAGTTLVLLDTEGLEDVEKGDSKRDTYIFSLAVLLSSTLVYNSRGVIDNKAMEELQYVTELIEHIKVTPDEDADDCTAFAKFFPHFIWCLRDFTLELKLDGKDLTEDEYLEFALKLRPGTSKKVMMYNLPRECIRKFFPCRTCFTFPSPTTPEKRSILESLSPAELDPEFLEVTKRFCKFVFDRSEVKQLKGGHTVTGRVLGNLTKMYVDTISSGAVFCLENAVIAMAQIENEAATQEGLEVYQRGMEKLKSSFPLELEQVSSEHQRLSSMATQAFMARSFKDTDGKHLKALEGEMGKLFDAYRSQNKQVGLETHCDLLLYMRCKDPLILHVYFFPVNDARSKEKVEQNERSSLPISHPRPDRPFQVKTPHVLEVPGASVYPEEGISFRTDVEPNFFKVRKLQVDDVQMNLVRQKDKMSVWTTTIWKEEFVHLQQVRDERKLNSEIEKNDFFNAHRVAFIERVTNVKSIADKLHGQRIIHKELYSEITQTNVTRQQIMRKICDSVDSSGRIAKCKFIDILQEEERCLLEDLKQSES", "text": "FUNCTION: GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils (PubMed:27363812). Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2 (PubMed:27363812). SUBCELLULAR LOCATION: Inflammasome. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. GB1 subfamily."}
{"protein": "MFARRLRGAGSLAAASLARWQSSKVTGDVIGIDLGTTYSCVAVMEGDKPRVLENTEGFRATPSVVAFKGQEKLVGLAAKRQAVTNPQSTFFAVKRLIGRRFEDSNIQHDIKNVPYKIGRSSNGDAWVQDANGKQYSPSQVGAFVLEKMKETAENFLGRKVSNAVVTCPAYFNGPQRQATKDAGTIAGLNVIRVVNGPTAAALAYGLDKTKDSMIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLCLSDYILTEFKKSTGIDLSNERMALQRIREAAEKAKCELSTTMETEVNLPFITANQDGAQHVQMTVSRSKFESLAEKLVQRSLGPCKQCIKDAAVDLKEISEVVLVGGMTRMPKVIEAVKQFFGRDPFRGVNPDEAVALGGATLGGVLRRDVKGLVLLDVTPLSLGVETLGGVFTRMIPKNTTIPTKKSQTFFSTAAFNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIEPNGICHVTAKDKATGKTQNITITASGGLSKEQIERMIRDSESHAESDRLKRELVEVRNNAETQANTAERQLTEWKYVSDAEKENVRTLLRACRKSMENPNVTKDELSAATDKLQKAVMECGRTEYQQAAAGNSSSSSGNTDSSQGEQQQQGDQQKQ", "text": "FUNCTION: May participate in eukaryotic mitochondrial DNA replication. SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast. Note=Associated with kinetoplast DNA in the mitochondrion, in the region where kdna replication occurs. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MYVQEHRLWGLMDKPHSAPCLMSLSLSFLICNKGRNAIRVQQSTDERMDAMLLWQCPTQGTRKNHESNSSLHHVPNWIFHSTIIPPNKGSKRCLRKVDWLLPRAGGVGGKRGVTADGDRVSF", "text": "SIMILARITY: Belongs to the FAM223 family."}
{"protein": "MGDQRLQDWLRSPGMDSKPWYCNKRPSKCFAKCKHRRLRFPPMDTQNWVFVKEGMDDFRYGCPSPEDTLVCRRDEFLLPKISLRGPQADPKSGQKKLLKKAALFSKLSPAQLARKAFVEQVEAQLMAKHPLAMYPNLGEDMPPDLLLQVLKHLDPERELEDAWACCETQEKTTEVPTEPGKHPCGEFCLKPPETPVSHLLPEPPETGVSHLSPEPPKTPVSSLRPEPPETGVSHLRPEPPETGVSHIRPGPPITRRRSSLLRQLLKLDSERKLEDARAPCEGREKTTDEPTEPGKYPCGKFCPRPFETPLSHLRQEPPKTPVSSLRPEPPETGESHLRLEHSKTRRGSSLRSEPSETGVSRLRLAPPKTRRGSSLHAEPSKTGVSHLSPEPPKTEVSHLHPVPPKTGVCHLRLEPPDTSQVSNLLLYILKVLDSGRTLKDVWDRCEARVKKTKEPTEPHKSPCGEPCLQPPETQVSHPHPEHPKTRRRSSLHSQPPKTRRTSSLRSEPPKTRRTSSLRSEPPKTRRTSSLGPEPPKTRRVSSLRPELPKSRRVSSLHPEPPKAPESHQFSEPPKIRASYIKELLQEDTPSTKECVSDSLQYRYTSEKLREFFKWAGDLGADEESIRNLFDFTPKYRATHEDQKFKKVKECSSELKYSMELDEKDEDKFFSQEKYWGRKFHTPSNSYTAQRVKMKYGAWYLKPKLWKKLRSDEPLIDPKLLLKKPDEPDVLDDLYGPIAFKDFILSKGYEMPGIIQRLFARRGWTYDSVKTPIQRAMIFYKYKEIVEASEED", "text": "SIMILARITY: Belongs to the FAM47 family."}
{"protein": "MNKFEDIRGVAFDLDGTLVDSAPGLAAAVDMALYALELPVAGEERVITWIGNGADVLMERALTWARQERATQRKTMGKPPVDDDIPAEEQVRILRKLFDRYYGEVAEEGTFLFPHVADTLGALQAKGLPLGLVTNKPTPFVAPLLEALDIAKYFSVVIGGDDVQNKKPHPDPLLLVAERMGIAPQQMLFVGDSRNDIQAAKAAGCPSVGLTYGYNYGEAIDLSQPDVIYQSINDLLPALGLPHSENQESKND", "text": "FUNCTION: Specifically catalyzes the dephosphorylation of 2- phosphoglycolate (2P-Gly). Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'- phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family."}
{"protein": "MKKMFMAVLFALASVNAMAADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND", "text": "FUNCTION: The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the stxB family."}
{"protein": "MSSVNSIPTATSTVYISVLPATATPSGGSGGNVLHEDLNKFYDYGNTSWILACTPLCLIMVPGVAFFYSGLARRKNTLALIMLSMLGLCVSFFQWYFWGYSLAFSQTGTSGYIGNLRHFAFIRTLADYSPGSNNIPELVFANFQGMFAAITVALFTGAAAERGRIGPMLIITFVWLTVVYCPIACWIWNPNGWAFKFGVYDFAGGGPVEVGSGFAALAYTVCLGRRSKFVEEQFRPHSVLNVVLGTSLLWFGWLGFNGGSAYGSNLRAAMAITNTNLAGAVAGLVWVIYDYIFRTRKWSTIGFCSGVVAGLVAATPCAGFVSPHASLAIGAITGLCCNWAIKLKSHMRIDDAMDIFAIHGVAGFVGTFLNGLFAVDYIAAMDGIYVGENKIRGGWFDHHWRQLGLQMAYICAVGAYDFVVTFIILFITDKIPYLQLRVSPDAEEIGVDADQIGEYAFDYIEERREYKHWKISPAGVPEEIIISNGVAQPTGNVAAPGKILESTNPLELGLTI", "text": "FUNCTION: Transporter for ammonium to use as a nitrogen source. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family."}
{"protein": "MIGWGDVYKVVAATVPLYFALFLGYGSVRWWRIFTREQCDAVNRLVAFFALPFFTFEFTLHTDPFQVNYRAVAADVISKAVIVAVIGAWARFMSKGGCAVSWSITSFSLSTLTNSLVVGVPMARAMYGEWAQQLVVQLSVFQAIVWLTLLLFVLEVRKAAIGMYVDGAEAAAAAGKDVEAAGAAAAAGTVVVAAAAGKPSLWALVKVVAHKLARNPNTYASFVGITWACLANRLHIALPSAFEGSVLIMSKSGTGMAMFSMGLFMAQQEKIIACGTSFAALGLVLKFALGPAAMAIGSIAVGLRGDVLRVAIIQAALPQSITSFIFAKEYGLHADVLSTAVIFGMLVSLPLLVGFYIVLELIR", "text": "FUNCTION: May act as a component of the auxin efflux carrier. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family."}
{"protein": "MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHISCVGNDFGFNDIFSRYVEAVGREGDVLLGISTSGNSANVIKAIAAAREKGMKVITLTGKDGGKMAGTADIEIRVPHFGYADRIQEIHIKVIHILIQLIEKEMVK", "text": "FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIS family. GmhA subfamily. SIMILARITY: Belongs to the SIS family. GmhA subfamily."}
{"protein": "MYLIADWRRTHYSEEVIPEMDGQEVILMGWVHSIRALGKLAFVILRDREGTIQAVVPKQKVDEETFEIAKKLGKEDIIAIRGKVVANEKAPKGFEVIPIEIRVLNKADAPLPLDPSEKVPAEIDTRLDKRFLDIRRPKIQAIFKIRSEMLRSIRKTFADEGFVEVNTPKLVASATEGGTELFPISYFEKEAFLGQSPQLYKQMMMAGGFDKVFEIAQIFRAEEHNTRRHLNEAVSIDTEMSFVNEKDAMAMLEKVVYNCYADIEYNRPQEIELLELNWEIPEKTFDKLTYTEAIDIAISKGVEIEWGEDLSRAAERAVGDEMGGLYFITEWPTQTRPFYTLPHENDNKVCKAFDLMYKELEISSGAQRVHKYDLLVENISNMGMNPDSFETYLEAFKFGMPPHAGWGLGADRFAMVLTAQDNIRECVLFPRDRQRLTP", "text": "FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily."}
{"protein": "MAANSSAVSSDGILIGDKLYSGVMISLENCLMAEERCALTPSVVDGIDVNTEIDLRCVGCELVQAAGILLRLPQVAMATGQVLFQRFFYTKSFVKHSMEHVAMACVHLASKIEEAPRRIRDVINVFHRLRQLREKQKSTPLILDQEYVNLKNQIIKAERRVLKELGFCVHVKHPHKIIVMYLQVLECERNKHLVQTSWNYMNDSLRTDVFVRFNPETIACACIFLAARTLEIPLPNRPHWFYLFGASEEDIKEICLQILRLYTRKKADVALLENKVEKRKLFIEEAKAKAKGLLPDGTPRLENAPEFSPSLKNDSPKELKANKPSPLAVHALKNCKRKVDGTKRPTSSSPVNGRVSKGRDSRSGSRSRDQSYSRSQSRSQSPKRRKSQSYSPSSDSKSRSPSRSRSDSPPHKPNHGSYKSTKGHVYGNNSDYKYQGHKRRSRSRSSSPSHSRSRESSDSGKYKKKDHYYRRERSRSYDRVSHRGYDREYHGHSHHRR", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleoplasm. SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily."}
{"protein": "MVVQNSPVSSVHTANFSERGSNTRTMTYKNKLTVCFDDILKVGAEMMMQQQLKNVQLDSYLVNGFSQSQQKLLKEKVKLFHGILDDLETSLSQSSSYLETLTALGKEKEKEREEAEKKRAEQENMRKVREQEELKKRQELEEASQQQQLQQNSKEKNGLGLNFSTTAPANTTDANGSKENYQELGSLQSSSQTQLENANAANNGAAFSPLTTTRIQSQQAQPSDVMFNDLNSMDISMFSGLDSTGFDSTAFNATVDETKGFDDNDSGNNYNDINISSIENNINNNINSTKNGKDNNNESNKNNNGDEKNKNNNEDNENNNNSSEKNNNNNNNNNNNNDDNGNNNNNNSGNDNNNTTNNDSNNKNNSITTGNDNENIVNNDLPTTVVSNPGDNPPPADNGEEYLTLNDFNDLNIDWSTTGDNGELDLSGFNI", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the mediator complex subunit 2 family."}
{"protein": "MAAPRAGRGAGWSLRAWRALGGIRWGRRPRLTPDLRALLTSGTSDPRARVTYGTPSLWARLSVGVTEPRACLTSGTPGPRAQLTAVTPDTRTREASENSGTRSRAWLAVALGAGGAVLLLLWGGGRGPPAVLAAVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGISGSQRRYIGVMMLTLSPSILAELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQLAVQIRRGRETLTLYVTPEVTE", "text": "FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase- independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive. SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Mitochondrion membrane; Single-pass membrane protein Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID. SIMILARITY: Belongs to the peptidase S1C family."}
{"protein": "MALRVTRNRLASTRAEQGGKTCSVSGPTLKPRAALGEIGNVAANKDVTKKNVKMEAAKKTRITAKAEKIEQPKATVVPVKPEPKVQVPAQPEPASPTPMETSGCEPADLCQAFSDVILNTAIRDVDADDYDNPMLCSEYVKDIYKYLRQLEVEQSVKPNYLQGQEVTGNMRAILIDWLVQVNLKFRLLQETMYMTVGIIDRFLQDHPVPKKQLQLVGVTAMFLASKYEEMYPPEISDFAYVTDRAYTTAQIRDMEMTILRVLKFQLGRPLPLQFLRRASKIYEVTAEQHTLAKYLLELSIVDYDMAHFPPSTVASAALGLTLKVLDAGEWDVTLQHYMDYTAHTLTPVMAHIAKNVVKVNDGLTKHMAIKGKYSTSKQMRVATIAQLKSSLVKDLAKQLSQ", "text": "FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily."}
{"protein": "MLFKSLSKLATAAAFFAGVATADDVPAIEVVGNKFFYSNNGSQFYIRGVAYQADTANETSGSTVNDPLANYESCSRDIPYLKKLNTNVIRVYAINTTLDHSECMKALNDADIYVIADLAAPATSINRDDPTWTVDLFNSYKTVVDTFANYTNVLGFFAGNEVTNNYTNTDASAFVKAAIRDVRQYISDKNYRKIPVGYSSNDDEDTRVKMTDYFACGDDDVKADFYGINMYEWCGKSDFKTSGYADRTAEFKNLSIPVFFSEYGCNEVTPRLFTEVEALYGSNMTDVWSGGIVYMYFEETNKYGLVSIDGNDVKTLDDFNNYSSEINKISPTSANTKSYSATTSDVACPATGKYWSAATELPPTPNGGLCSCMNAANSCVVSDDVDSDDYETLFNWICNEVDCSGISANGTAGKYGAYSFCTPKEQLSFVMNLYYEKSGGSKSDCSFSGSATLQTATTQASCSSALKEIGSMGTNSASGSVDLGSGTESSTASSNASGSSSKSNSGSSGSSSSSSSSSASSSSSSKKNAATNVKANLAQVVFTSIISLSIAAGVGFALV", "text": "FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Secreted, cell wall Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. SIMILARITY: Belongs to the glycosyl hydrolase 72 family."}
{"protein": "MTKHPPNRRGISFEVGAQLEARDRLKNWYPAHIEDIDYEEGRVLIHFKRWNHRYDEWFCWDSPYLRPLEKIQLRKEGLHDEDGSSEFQINQQVLACWSDCRFYPARVTAVNKDGTYTVKFYDGVVQTVKHIHVKAFSKDQNIVGNARPKETDHKSLSSSPEKREKFKEQRKVTVNVKKDKVEKALKTEKRPKQPDKEGKLICSEKGKVSEKSLPKNEKEDKENISENEREYSGDAQVEKKPEKDLVKNPQENLKEPKRKRGRPPSITPTAVDSNSQTLQPITLELRRRKISKRSDTPLKRPRLDKNSPQEQSKKRSENSDKDLSRRRSSRLSTNGTREILDPDSIVPDLVHTVDTNPLPDKSPSAKDSAEGQLKSPLEAGQVSSALTCHPIGDGLGAADLELNCKSMGENTMKTEPVSPLAEVQEVSTVEVPNTLKKVDDSVTLNVPAVDLDHKFRCKVLDCLKFFRKAKLLHYHMKYFHGMEKSPEPEEGPGKTHVQTRGSAVPDKTSQESLTRKRVSASSPTAKEKEKTKEKKFKELVRVKPKKKKKKKKKTKPECPCSEDISDTSQEPSPPKTFAVTRCGSSHKPGVHMSPQLHGSDNGNHKGKLKTCEEDNLSESSSESFLWSDEEYGQDVDVTTNPDEELEGDDRYDFEVVRCICEVQEENDFMIQCEECQCWQHGVCMGLLEENVPEKYTCYVCQDPPGQRPGFKYWYDKEWLSRGHMHGLAFLDQNYSHQNARKIVATHQLLGDVQRVIQVLHGLQLKMSILQSREHPDLQLWCQPWKQHSGEGRAHPRHIHITDARSEESPSYRTLNGAVEKPSPLPRSVEESYITSEHCYQKPRAYYPAVEQRLVVETRGSALDAAVSPLCENGDDSLSPRLGWPIDQDRSRGDIDPKPSSPKVREYISKNVLPEETPARKLLDRGGEGLVSSQHQWQFNLLTHVESLQDEVTHRMDSIEKELDVLESWLDYTGELEPPEPLARLPQLKHCIKQLLTDLGKVQQIALCCST", "text": "FUNCTION: Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage (By similarity). Methyllysine- binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDNHNEVPMSMSVPWASAASVTCLSLDAKCHRPCPSSISASASASACASDSAAIATTKLRHIAYTQRCSSRLTMLMTVLLLLLPLSFTPAHSCGPGRGLGRRRERNLYPLVLKQTIPNLSEYQTGASGPLEGEIKRDSPKFKDLVPNYNRDILFRDEEGTGADRLMTKRCKEKLNVLAYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDREPSRYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGITKPLSEISIGDRVLSMGSNGQPVYSEVILFMDRNLEQMQNFVELHTDGGAVLTVTPAHLISVWHPERQQLDYVFADRVEELNYVLVRDPQTGELRPQRVVRVGSVRSKGVVAPLTREGTIVVNSVAASCYAVIDSQSLAHWGLAPMRILAMLQSWMPAKDQLRSSQTEGVVSRAEQQNGIHWYANALYKVKDYVLPKSWRHD", "text": "FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior- posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA- dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane; Lipid-anchor Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. SIMILARITY: Belongs to the hedgehog family."}
{"protein": "MTETHNDPEELARRVASLSAQNERLAQILVEARSKIVGLQQQIDDLAQPPSTYATFIRSYSDGTADVMVQGRKMRLTSLPAAMVSTARPGQQVRLNEAMAIVETMTYDHTGELVTVKELIGTHRAMVVGRGDDERVVNLAGSLIGRDGPTIRTGDSVLVDLKAGYALEKIDKSEVEELVLEEVPRVAYEDIGGLSRQIDTIKDAVELPFLHPDLYREHGLKAPKGILLYGPPGCGKTLIAKAVAHSLAQTVGQGNNTPTDDTRGYFLNIKGPELLNKYVGETERQIRLIFTRARDKAAQGHPVVVFFDEMESLFRTRGTGLSSDVETTIVPQLLAEIDGVERLDNVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAEAALDIFSKYLTPDLPIHPVDLAEHGGNAQDAVTAMGQRVVEHMYATTPDNQFLEVTYASGDKETLYFKDFSSGAMIQNIVDRAKKAAIKGYLSHGTRGLQVEHLLAACDDEFQENEDLPNTTNPDDWARISGKKGERIVFIRTIVQRKGEGKNPTPAKAIETPHNTGPYL", "text": "FUNCTION: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MAMASLARRKAYFLTRNISNSPTDAFRFSFSLTRGFASSGSDDNDVVIIGGGPGGYVAAIKAAQLGLKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHVFANHGVKVSSVEVDLPAMLAQKDTAVKNLTRGVEGLFKKNKVNYVKGYGKFLSPSEVSVDTIDGENVVVKGKHIIVATGSDVKSLPGITIDEKKIVSSTGALSLTEIPKKLIVIGAGYIGLEMGSVWGRLGSEVTVVEFAADIVPAMDGEIRKQFQRSLEKQKMKFMLKTKVVGVDSSGDGVKLIVEPAEGGEQTTLEADVVLVSAGRTPFTSGLDLEKIGVETDKGGRILVNERFSTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEFIAGKHGHVDYDKVPGVVYTYPEVASVGKTEEQLKKEGVSYNVGKFPFMANSRAKAIDTAEGMVKILADKETDKILGVHIMSPNAGELIHEAVLAINYDASSEDIARVCHAHPTMSEAIKEAAMATYDKPIHM", "text": "FUNCTION: Lipoamide dehydrogenase is a component of the glycine decarboxylase (GDC) or glycine cleavage system as well as of the alpha- ketoacid dehydrogenase complexes. LPD1 is probably the protein most often associated with the glycine decarboxylase complex while LPD2 is probably incorporated into alpha-ketoacid dehydrogenase complexes. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MFTLARLLDFQKTKYARFMNDRVPAHKRYQPTEYEHAANCATHAFWIIPSILGSSNLYFLSDDDWETISAWIYGLGLCGLFVVSTIFHTVSWKKSHLRMVEHCLHMIDRMVIYFFIAASYAPWLNLRELGPWASHMRWLVWIMASIGTIYVFFFHERYKLVELLCYVVMGFFPALVILSMPNTDGIWELMTGGAFYCLGMVFFKSDGRIPFAHAIWHLFVAFGAGTHYYAIWRYLYLPSTLQTKVSK", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the ADIPOR family."}
{"protein": "MASTAARRLAWVAVRPGALWSGPRGRRGGDVYTVPGSSGLSQVPSRSVIVTRSGAILPKPVKMSFGLLRVFSIVIPFLYVGTLISKNFAALLEEHDIFVPEDDDDDD", "text": "FUNCTION: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria (PubMed:27001609). Required to bridge the calcium- sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU. Plays a central role in regulating the uniplex complex response to intracellular calcium signaling. Acts by mediating activation of MCU and retention of MICU1 to the MCU pore, in order to ensure tight regulation of the uniplex complex and appropriate responses to intracellular calcium signaling (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein Note=MAIP1 is required to assist sorting of EMRE/SMDT1 into mitochondrion by protecting EMRE/SMDT1 against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB). SIMILARITY: Belongs to the SMDT1/EMRE family."}
{"protein": "MSSFQFEQIGVIRSPYKEKFAVPRQPGLVKSANGELHLIAPYNQADAVRGLEAFSHLWILFVFHQTMEGGWRPTVRPPRLGGNARMGVFATRSTFRPNPIGMSLVELKEVVCHKDSVILKLGSLDLVDGTPVVDIKPYLPFAESLPDASASYAQSAPAAEMAVSFTAEVEKQLLTLEKRYPQLTLFIREVLAQDPRPAYRKGEETGKTYAVWLHDFNVRWRVTDAGFEVFALEPR", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU) that read codons starting with adenosine (PubMed:9537379, PubMed:25063302). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability (PubMed:9537379, PubMed:25063302). SIMILARITY: Belongs to the tRNA methyltransferase O family."}
{"protein": "MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWLFSIVVFGSIVNEGYLNSASEGEEFCIYNRNPNACSYGVAVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFLWFVGFCYLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPTGPDPAGMGGTYQQPANTFDTEPQGYQSQGY", "text": "FUNCTION: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short- term and long-term synaptic plasticity (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the synaptogyrin family."}
{"protein": "MTHRRTKLFMMAAVVSYVMTSCGAVPINDLLDRASQRSDQLHSLSTTLSQELDSHFPPIGRVIMPRPSMCHTSALQTPNDKTQALQVSESELLSLARSLLQAWADPLSALSSSAFSLPHPAQSSIFNKVREMQEHSKNLGDGLDILSGKMGEAAQALSSLPFRGNDVGQDRISKLINFHFLLSCFRRDSHKIDSFLKVLRCRAANTQPEMC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MGETEGKKDEADYKRLQTFPLVRHSDMPEEMRVETMELCVTACEKFSNNNESAAKMIKETMDKKFGSSWHVVIGEGFGFEITHEVKNLLYLYFGGTLAVCVWKCS", "text": "FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the dynein light chain family."}
{"protein": "MTTEKTVVFVSGATGFIALHVVDDLLKTGYKVIGSGRSQEKNDGLLKKFKSNPNLSMEIVEDIAAPNAFDKVFQKHGKEIKVVLHIASPVHFNTTDFEKDLLIPAVNGTKSILEAIKNYAADTVEKVVITSSVAALASPGDMKDTSFVVNEESWNKDTWESCQANAVSAYCGSKKFAEKTAWDFLEENQSSIKFTLSTINPGFVFGPQLFADSLRNGINSSSAIIANLVSYKLGDNFYNYSGPFIDVRDVSKAHLLAFEKPECAGQRLFLCEDMFCSQEALDILNEEFPQLKGKIATGEPGSGSTFLTKNCCKCDNRKTKNLLGFQFNKFRDCIVDTASQLLEVQSKS", "text": "SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily."}
{"protein": "MLSNTITIVPSIETRVVEPLPQFDTSRRLSFPVSLPLDSLAGARKKAANEALVERIAEIIASYRISGPDDRYEVVYKPKLLDTLRYFVSKQEPVNMVVPAYPFKSPNRDEKVLGPDPDVGERMSLEHFNSMGARIQQIYPPGGYVTIVSDGCCYNDLLGVSDEEVFRYAEGLHRIVDRLGLKHIKFSDPFDLIEGRHNVPVTEEEYASRIGELKDYLFRSYHPDGYDFDEELSKDPNAALTYRGYIRFLMSDLALFFKERQMSKNAIKKHCSTVARSMIKRGKAFSALVARASPLHVRLSIHASDNTGKLSVALLPHKRYSTFPVTPWHNTPYLDTTSVSLSLSRKPTDGATPYRLCQDELGLHFLCADVPMYRVIETPDLPALAQQVQFQPLYPFGLRIKVPRGTPIGQFRLERVAELAKVHSPIIFEGLDPMEYTAAIADDFQRVAGGTMSLSILHEGVATTANTARHLGGSAAASYFLQISAATGDDAQPALLPFLAAAAALDDVRYRVLHHWQAGHAVVSDHRVALPVHLSPSSLRVLHGGV", "text": "FUNCTION: Isocyanide synthase involved in the biosynthesis of isocyanides (or isonitriles), a class of microbial secondary metabolites. The presence of an isonitrile moiety within a compound imparts unique biological (cytotoxic, antibacterial, and antiprotozoal) and chemical (transition metal coordination) properties and enables synthetic and biochemical applications. SIMILARITY: Belongs to the isocyanide synthase family."}
{"protein": "MNRGSISSGTPGLFVGSMRNTPFVVKINVIFLKVISNTAVSVFWRDRRIRFESDWLNSYFQK", "text": "SIMILARITY: Belongs to the asfivirus C62L family."}
{"protein": "MNRFGTRLVGATATSSPPPKARSNENLDKIDMSLDDIIKLNRKEGKKQNFPRLNRRLLQQSGAQQFRMRVRWGIQQNSGFGKTSLNRRGRVMPGKRRPNGVITGLAARKTTGIRKGISPMNRPPLSDKNIEQYFPVLKRKANLLRQNEGQRKPVAVLKRPSQLSRKNNIPANFTRSGNKLNHQKDTRQATFLFRRGLKVQAQLNTEQLLDDVVAKRTRQWRTSTTNGGILTVSIDNPGAVQCPVTQKPRLTRTAVPSFLTKREQSDVKKVPKGVPLQFDINSVGKQTGMTLNERFGILKEQRATLTYNKGGSRFVTVG", "text": "FUNCTION: Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus speckle. SIMILARITY: Belongs to the UIF family."}
{"protein": "MKPGPPRRGTAQGQRVDTATHGPGARGLLLPPLLLLLLAGRAAGAQRWRNENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGLETAMRFIPDIALAAPTAPAMLPTTVIQPVDTPFEELLSEHPGPEPVTSPPLVTEVTEVVEEPSQRATTISTTTSTTAATTTGAPTMATAPATAATTAPSTPAAPPATATTADIRTTGIQGLLPLPLTTAATAKATTPAVPSPPTTVTTLDTEAPTPRLVNTATSRPRALPRPVTTQEPEVAERSTLPLGTTAPGPTEVAQTPTPESLLTTTQDEPEVPVSGGPSGDFELQEETTQPDTANEVVAVEGAAAKPSPPLGTLPKGARPGLGLHDNAIDSGSSAAQLPQKSILERKEVLVAVIVGGVVGALFAAFLVTLLIYRMKKKDEGSYTLEEPKQASVTYQKPDKQEEFYA", "text": "FUNCTION: Cell surface proteoglycan that may bear heparan sulfate. May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the syndecan proteoglycan family."}
{"protein": "MKFSFLTVASFLIGQVALAALSAKKFASASDLQFTIDGKTGYFAGSNSYWIGFLTNNADVDLVFDHMKESGLKILRVWGFNDVNTVPGQGTVYYQVHANGKSTINTGADGLQRLDYVVHSAEKRGIKLIINFVNNWDDYGGMNAYVKAYGETDHNAFYSNKNIQNAYRRYVKAVVSRYTNSPAVFAWELANEPRCKGCDTEVLYEWIKSTSEYIKKLDKRHMVCIGDEGFGLDLLSDGSYPYTYVEGSNFTRNLAIPTIDFGTFHLYPDSWGTTHEWGNGWAQSHGAACKAAGKPCLFEEYGVTSNHCALETPWQKTSLNTTGVSGDLYWQYGDTLSTGQSPNDGNTIYYGTDEFKCIVKDHVAAIKAKQGWV", "text": "FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MSIEIITGPMYSGKTTELIRRITRYKLCKKNCVIISHSIDNRCEEDDNILINHDGFKISHDDFIKTNILINKIKIFDKYEIIGIDECQFFDSNDLMIFCDTLANNGKKIIVAGLNSDFNKNPFKSIIKLIPISEKITKLQSICNFCYNDATFTMKKFNKDIIIEIGGSDLYIPVCRICYNENNTIN", "text": "SIMILARITY: Belongs to the thymidine kinase family."}
{"protein": "MAASLSSEVHSLGQLLIDPGKPLPLRFRALFTLRNLGGAEAIDCIGRGFQDESALLKHELAYCLGQMKDRRALPVLKQVLQDRQQEPMVRHEAGEALGAIGDPEVLELLREYAQDPVIEVAETCQLAVSRIEWLQKNPDSPDTNPYLSVDPAPPAEEKDVPTLRATLLDETCPLFHRYRAMFALRNIGGEEAVLALADGLQIGGSLFRHEIGYVLGQMQHKAAVPGLSAALERFEENPMVRHECAEALGSIAHEDCLKALRAHVGDGERVVRESCEVALDMHDYENSGDFQYANGLSQICEQI", "text": "FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L- lysine intermediate produced by deoxyhypusine synthase/DHPS on a critical lysine of the eukaryotic translation initiation factor 5A/eIF- 5A. This is the second step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function. SIMILARITY: Belongs to the deoxyhypusine hydroxylase family."}
{"protein": "MPQPYIFRTVELDNQSIRTAVRPGKPHLTPLLIFNGIGANLELVFPFIEALDPDLEVIAFDVPGVGGSSTPRHPYRFPGLAKLTARMLDYLDYGQVNVIGVSWGGALAQQFAHDYPERCKKLVLAATAAGAVMVPGKPKVLWMMASPRRYVQPSHVIRIAPTIYGGGFRRDPELAMQHASKVRSGGKMGYYWQLFAGLGWTSIHWLHKIQQPTLVLAGDDDPLIPLINMRLLAWRIPNAQLHIIDDGHLFLITRAEAVAPIIMKFLQQERQRAVMHPRPASGG", "text": "FUNCTION: Complements a mutant that does not degrade PHA; might be a lipase. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MVSMLTNVVSGETEPSASATWTMGHKREREEFSLPPQPLITGSAVTKECESSMSLERPKKYRGVRQRPWGKWAAEIRDPHKATRVWLGTFETAEAAARAYDAAALRFRGSKAKLNFPENVGTQTIQRNSHFLQNSMQPSLTYIDQCPTLLSYSRCMEQQQPLVGMLQPTEEENHFFEKPWTEYDQYNYSSFG", "text": "FUNCTION: Transcriptional activator involved in the regulation of plant development and tolerance to abiotic stresses (PubMed:21069430). Binds to the GCC-box pathogenesis-related promoter element and the cis- element CE1 (coupling element 1). Involved in the regulation of gene expression in response to abiotic stresses, possibly through the abscisic acid (ABA) signaling pathway (PubMed:20193749). Involved in resistance to the beet cyst nematode Heterodera schachtii in roots. May promote callose deposition at syncytia which may interfere with nutrient import into syncytia and inhibit the development of nematodes (PubMed:23510309). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
{"protein": "MKLRAEDVLANGTSRHKVQIDMERQVQIAKDLLAQKKFLEAAKRCQQTLDSLPKDGLLPDPELFTIFAQAVYNMEVQNSGNLFGDALLAGDDGSGSESESEPESDVSNGEEGNENGQTEIPNSRMFQFDQEEEDLTGDVDSGDSEDSGEGSEEEEENVEKEEERLALHELANFSPANEHDDEIEDVSQLRKSGFHIYFENDLYENALDLLAQALMLLGRPTADGQSLTENSRLRIGDVYILMGDIEREAEMFSRAIHHYLKALGYYKTLKPAEQVTEKVIQAEFLVCDALRWVDQVPAKDKLKRFKHAKALLEKHMTTRPKDSELQQARLAQIQDDIDEVQENQQHGSKRPLSQPTTSIGFPALEKPLGDFNDLSQLVKKKPRRH", "text": "FUNCTION: Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NASP family."}
{"protein": "MRPKRLGRCCAGSRLGPGDPAALTCAPSPSASPAPEPSAQPQARGTGQRVGSRATSGSQFLSEARTGARPASEAGAKAGARRPSAFSAIQGDVRSMPDNSDAPWTRFVFQGPFGSRATGRGTGKAAGIWKTPAAYVGRRPGVSGPERAAFIRELEEALCPNLPPPVKKITQEDVKVMLYLLEELLPPVWESVTYGMVLQRERDLNTAARIGQSLVKQNSVLMEENSKLEALLGSAKEEILYLRHQVNLRDELLQLYSDSDEEDEDEEEEEEEKEAEEEQEEEEAEEDLQCAHPCDAPKLISQEALLHQHHCPQLEALQEKLRLLEEENHQLREEASQLDTLEDEEQMLILECVEQFSEASQQMAELSEVLVLRLENYERQQQEVARLQAQVLKLQQRCRMYGAETEKLQKQLASEKEIQMQLQEESVWVGSQLQDLREKYMDCGGMLIEMQEEVKTLRQQPPVSTGSATHYPYSVPLETLPGFQETLAEELRTSLRRMISDPVYFMERNYEMPRGDTSSLRYDFRYSEDREQVRGFEAEEGLMLAADIMRGEDFTPAEEFVPQEELGAAKKVPAEEGVMEEAELVSEETEGWEEVELELDEATRMNVVTSALEASGLGPSHLDMNYVLQQLANWQDAHYRRQLRWKMLQKGECPHGALPAASRTSCRSSCR", "text": "FUNCTION: Originally identified as neuronal protein that specifically associates with HTT/huntingtin and the binding is enhanced by an expanded polyglutamine repeat within HTT possibly affecting HAP1 interaction properties. Both HTT and HAP1 are involved in intracellular trafficking and HAP1 is proposed to link HTT to motor proteins and/or transport cargos. Seems to play a role in vesicular transport within neurons and axons such as from early endosomes to late endocytic compartments and to promote neurite outgrowth. The vesicular transport function via association with microtubule-dependent transporters can be attenuated by association with mutant HTT. Involved in the axonal transport of BDNF and its activity-dependent secretion; the function seems to involve HTT, DCTN1 and a complex with SORT1. Involved in APP trafficking and seems to facilitate APP anterograde transport and membrane insertion thereby possibly reducing processing into amyloid beta. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptors to synapses; the function is dependent on kinesin motor protein KIF5 and is disrupted by HTT with expanded polyglutamine repeat. Involved in regulation of autophagosome motility by promoting efficient retrograde axonal transport. Seems to be involved in regulation of membrane receptor recycling and degradation, and respective signal transduction, including GABA(A) receptors, tyrosine kinase receptors, EGFR, IP3 receptor and androgen receptor. Among others suggested to be involved in control of feeding behavior (involving hypothalamic GABA(A) receptors), cerebellar and brainstem development (involving AHI1 and NTRK1/TrkA), postnatal neurogenesis (involving hypothalamic NTRK2/TrkB), and ITPR1/InsP3R1-mediated Ca(2+) release (involving HTT and possibly the effect of mutant HTT). Via association with DCTN1/dynactin p150-glued and HTT/huntingtin involved in cytoplasmic retention of REST in neurons. May be involved in ciliogenesis. Involved in regulation of exocytosis. Seems to be involved in formation of cytoplasmic inclusion bodies (STBs). In case of anomalous expression of TBP, can sequester a subset of TBP into STBs; sequestration is enhanced by an expanded polyglutamine repeat within TBP. HAP1-containing STBs have been proposed to play a protective role against neurodegeneration in Huntigton disease (HD) and spinocerebellar ataxia 17 (SCA17). SUBCELLULAR LOCATION: Cytoplasm Cell projection, axon Presynapse Cytoplasm, cytoskeleton Cell projection, dendritic spine Cell projection, dendrite Lysosome Endoplasmic reticulum Mitochondrion Nucleus Cytoplasmic vesicle, autophagosome Early endosome Cell projection, growth cone Cell projection, neuron projection Cytoplasmic vesicle, secretory vesicle, synaptic vesicle Note=Localizes to large nonmembrane-bound cytoplasmic bodies found in various types of neurons, called stigmoid bodies (STBs). Localization to neuronal processes and neurite tips is decreased by YWHAZ. In the nucleus localizes to nuclear rods."}
{"protein": "MRRREVLLFLTGSRVRHVRTGVDSLIGGYRLNLTPSEPLGLWRIEALHRPVSIGDLVFFCPPMTAVFDEARRRGYVRRGLCAGGVAPLIKTVAALAAQNVEITDHIVIDGRSLPSSVVRKTDGEGRVLLPDPGGVVPPHHLFLHSSFASSYDSRYFGPVPDSGLLGLARPVFTFDP", "text": "FUNCTION: Involved in conjugal transfer of the plasmid. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the peptidase S26C family."}
{"protein": "MDNNPNINECIPYNCLSNPEVEVLGGERIETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWEIFSVLSSDAFLVQIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEADPTNPALREEMRIQFNDMNSALTTAIPLFAVQNYQVPLLSVYVTCNYIISSESVMCGQRSGFDAATINSRYNDLTRLIGNYTDHAVRWYNTGLERVWGPDSRDWIRYNQFRRELTLTVLDIVSLFPNYDSRTYPIRTVSQLTREIYTNPVLENFDGSFRGSAQGIEGSIRSPHLMDILNSITIYTDAHRGEYYWSGHQIMASPVGFSGPEFTFPLYGTMGNSAPQQRIVAQLGQGVYRTLSSTLYRRPFNIGINNQQLSVLDGTEFAYGTSSNLPSAVYRKSGTVDSLDEIPPQNNNVPPRQGFSHRLSHVSMFRSGFSNSSVSIIRAPMFSWIHRSAEFNNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQISTLRVNITAPLSQRYRVRILYASTTNLQFHTSIDGRPINQGNFSATMSSGRNLQSGSLRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVPAEVTFEAEYDLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKKELSEKVKHAKRLSDERNLLQDPNFRGINRQLDRGWRRSTDITTQGGDDFFQENYVTLLGTLMGFPSIYIKKWWFEIKSLYPLPIRGYIEDSQDLEIYLIRYNAKHETVNVPGTVPYGRFQPQVPIGKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHARLGNLEFLEEKPLVGEALARVKRAEKKWRDKREKLEWETNIVYKEAKESVDALFVNSQYDRLQADTNIAMIHAADKRVHSIREA", "text": "FUNCTION: Promotes colloidosmotic lysis by binding to the midgut epithelial cells of both dipteran and lepidopteran larvae. SIMILARITY: Belongs to the delta endotoxin family."}
{"protein": "MSSANIVPSNMGITKFLLLTISTSSVVAGVFALKPFFHINFGLHLLSHYQYWRILLWQFIYWNSTEVFQALFIIYQARDVERLLGSHRFASFCVYMFILGMFVTPIFSFLYSLLFKNLDYIQPGPTFLIFAILYQYYYIVPSTVFVRLFNIKFTDKFQMVIPMIGLAFSHFPSTFINAFLGWTMGMFYHLSLLPGTSWRLPIRFVKPALSPTHVFIRPPYSDMQNASTFNPETLFALPTGLDAERTENENQVENPVSNADANDSPTRQNARATAIASSSNTAASFRNRQQISHPPLGRTSSSSVLPTGPASQLYDMLSGRSERPELGNIREEDINTVQTIMQTSRAQAIQALSQTNDVQRAVELLLEQTADY", "text": "FUNCTION: Component of the DSC E3 ubiquitin ligase complex which is required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. The complex also plays an important role in the multivesicular body (MVB) pathway and functions in a post- endoplasmic reticulum pathway for protein degradation. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein."}
{"protein": "MAGSNDVAKVMKTLDGMREGLIQTAVELGSIEAPTGREGAAGDYVYEWMARNGFGPERVGVFDDRFNVVGRLRGTGGGASLSFNSHLDTIMAREDTARFADANDRIYHEAWHEEGRIYGYSVVNCKGPMACWLIAAKALKEAGAALKGDVVLTAVCGEIDCEPVDEFQGHDYLAEDIGARYAISHGAISDYALVAEATNFKPAWVEAGKVFLKVTVFAGPSRYTPYVPRPVAALDSPNAIVRMAKLVEALEEWADNYEKRYTREYGGGTVVPKVAIGAIRGGVPYKIYRFPELCSIYMDIRLNPDTNPLVVQREVEAVVSKLGLKAEVKPFLFRRGYEAQGIEPLQNALEVAHREVVGRPTERPGSPECSMWRDTNPYNELGIPSLTYGCGGGAGGGNTYFLVDDMLKAAKVYAMTAMDLCNRTP", "text": "FUNCTION: Catalyzes the deamination of 5-nitroanthranilate (5NAA) to 5- nitrosalicylate (5NSA), the first step in biodegradation of 5- nitroanthranilate. SIMILARITY: Belongs to the peptidase M20A family."}
{"protein": "AASYKVTFVTPSGTNTITCPADTYVLDAAEESGLDLPYSCRAGACSSCAGKVTAGAVNQEDGSFLEEEQMEAGWVLTCVAYPTSDVTIETHKEEDLTA", "text": "FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family."}
{"protein": "MATPALISETEAWKDLKAHLEGIKRTHLRELMGDTERCQSMMVEFDNIFLDYSRQQASPDTINKLYKLAEAAHLKQKIDRMYNGDHINSTENRSVLHVALRAPRNSAICSDGKNVVPDVWNVLDKIKDFSERVRNGSWVGATGKELKDVIAVGIGGSFLGPLFVHTALQTDPEASKNARGRELRFLANVDPIDAARNISGLNPETTLVVVVSKTFTTAETMLNARTLREWISSALGVAAVAKHMVAVSTNLPLVEKFGIDPNNAFAFWDWVGGRYSVCSAVGVLPLSLQYGFAVVEKFLQGAHNIDQHFSSAPFEKNIPVLLGLLSVWNVSFLGYPARAILPYSQALEKLAPHIQQVSMESNGKGVSIDGLPLPFESGEIDFGEPGTNGQHSFYQLIHQGRVIPCDFIGVVKSQQPVYLKGEVVNNHDELMSNFFAQPDALAYGKTPEELKKENVSEHLIPHKTFTGNRPCLSILLPTLDAYRIGQLLAIYEHRVAVQGFVWGINSFDQWGVELGKSLATQVRKQLHASRVKGEPVEEGFNFSTKTLLTRYLQATTDVPADPSTLLPNI", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family."}
{"protein": "MLKKKIEEEAAKYRNAWVKKCCYDGAHRNDDETCEERAARIAIGPECIKAFKSCCAIASQFRADEHHKNMQLGR", "text": "FUNCTION: Derived from proteolytic degradation of complement C5, C5a anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MGQCVTKCKNPSSTLGSKNGDRDPSSKSHGRRSASHREEQLPTCGKPGGDILVNGTKKAEAAPEACQLPTSSGDAGREPKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT", "text": "FUNCTION: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage. At the cell membrane, can promote and as well inhibit cullins neddylation. SUBCELLULAR LOCATION: Cell membrane Cytoplasm Nucleus Cytoplasm, perinuclear region Note=After UVC treatment, the protein enters to the nucleus gradually. Cell membrane localization is essential for CUL3 neddylation."}
{"protein": "MGLKNLFEKMEPAFLPGGKYSKLYPIFESIYTLLYTPGTVTHKNTHVRDALDSKRMMITVFLALFPAIFYGMYNVGNQAIPALNQLGNLDQLIANDWHYALASSLGLDLTANATWGSKMALGAIFFLPIYLVVFTVCTIWELLFSVVRGHEVNEGMFVSTILFALIVPPTLPLWQAALGITFGIIVAKEIFGGVGRNFMNPALAGRAFLFFAYPAQISGDTVWTAADGFSGATALSQWSQGGQGALQHTVTGAPITWMDAFVGNLPGSMGEVSTLAILIGGAVIVFTRIAAWRIIAGVMIGMIATSTLFNLIGSETNPMFSMPWHWHFVLGGFALGMVFMATDPVSASFTNTGKWWYGALIGVMAVLIRTVNPAYPEGMMLAILFANLFAPIFDYIVVQANIKRRRARTNG", "text": "FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrB/RnfD family."}
{"protein": "MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFDFGLLGTTLLNLDANYVETARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLRKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPYSASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANTQQFEHIVQLRRVLTTATITLLPDAERFSFPRVINSADGATTWYFNPVILRPNNVEVEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVAALFPNAQPFEHQATVGLTLRIESAVCESVLADASETMLANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLVK", "text": "FUNCTION: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices (PubMed:20122940). This capsid constitutes the middle concentric layer of the viral mature particle (PubMed:20122940). The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus (By similarity). Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes (PubMed:20122940). VP6 is required for the transcription activity of the DLP (By similarity). SUBCELLULAR LOCATION: Virion Note=Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus VP6 family."}
{"protein": "MSTTRTPKVSERVAPKPADPQPAKKKRGEDDDGPDFRTLLHAWLESHRASMADSLRRLGKQPIGSFFTCLVMAVALSMPMGLSLLLKNIEQLGGSWQRAAQISLFLKLDAGSRDGEALRDEIKGMPGVADAQYVSREQALEEFQQQSGLGEALRELPDNPLPGVVVVTPTEVDKPALEALRQRLSELPRVEVAQLDLVWVERLAAILKLGDRFVFGLAVMLISALLLVIGNTIRLHIENRRIEIEVIKLVGGTDAYVRRPFLYMGALYGLGAGLLAWGILAFGLNWLNEAVVGLSGLYGSDFALGGVPASDGLSLLIGAVLLGYIGAWIAVARHLNELAPR", "text": "FUNCTION: Part of the ABC transporter FtsEX involved in cellular division. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-4 integral membrane protein family. FtsX subfamily."}
{"protein": "MMKDYYTWTYPDIPEDVAQKLQQLKNSLVVVGIVGRSKCDQANKMQAFGMEPPIEHTAKDGQVQCYYKPGTSSLLLHFETTYDEAILGQMIDVCMEDVDTPFDFDSFYERMRCRFVRMMLLALHACHIVVYVETGPTFDPTLVTVFQLLKFAREQHLMQFLPQMLRETPAARMSEKTRLCAPRILFLFENFPRDEPKTRECVSAYEFQTEDCIYELLRHHTIVTNSSSTSLVALPNNKQFVFFNAHEQLHEDKLLKAIECLNQAMYKPDAKEEEEDLEILELAPFDGFVKPYNLPVDEKELEKQQYKKDHTVWHFLQRHVQDALLGCFDEGSFKQHSQHGQFQLLNIQEWHDYMATLHKLLVENAKDPNHETSNEEYKLFLKCFDESLNYEKKFWTHLCELGLKKGIAAYKNAAPANYGSATHRQLLADATVAFEEEGRGPQAKAALAKLAAICQKYWQDGRQQCEQLSLRSHPCTLPKNLPHEKHNSAVIHISSCNCGRTQGRREDPFSMRQANYEFYEHIAQMCNLCVKVKHYKFPVFEPSVSDYRAAAFEAAFPLLHTAKSGARQGEEGDDEPEDEVVQEQQQPVEEQRQNTASNGCSQPLSPTFGSDLNMSIAGFGASLNESQASSEQLSNSEQNTSSSGTSSADTENELVVELQEPAKKETREDAGPADALPTSTTEYLPGLVHTVSNFGLLPLFPSWSLACVGPSSIYSHNTGLQEHFQSGFLSGANFLLPWDVQLRLVHAPKQQHHTHHQQQHPGKKQQRWKKQGDRLSLKIFVGMEYECSRGHRFMMCAPDRVLRGGADIERDTCSKVVHNNMPLYYPCPCRSQTSYLAQLMRIHVVTPKAPVNIIVDPKVCVGKEKYTFTLGSIVPPRLSQSAYWIIRLPYIYQGDDVIIAPPEKLEPDDPLAGGYLLPGMFGVAETDATQDLNEPGRMGASAAEDFTRI", "text": "FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing nonC and recruited to stalled ribosomes (By similarity). SIMILARITY: Belongs to the SMG8 family."}
{"protein": "MAEHEQVHEHVRVAVIGSGFGGLGAAVRLRREGITDFVVLERAGSVGGTWRDNSYPGCACDVPSHLYSFSFAPNPEWPRTFSGQEHIRAYLEHVADTFGLRPHLRFDSEVKRMAWDTEQLRWEIETVRGTLTADVVVSATGPLSDPKVPDIPGLDTFPGKVFHSARWDHDYDLAGQRVAMIGTGASAIQIVPSIQPKVDRLTLFQRTPAWVMPRVDRAISGAERALHRALPATTKLRRGLLWGIRELQVQAFTKHPNELGFVEQIAKRNMGAAIKDPALRAKLTPDYRIGCKRILLSSTYYPALAKPNVDVVASGLSEVRGSTLVAADGTEAEADAIVFGTGFHVTDMPIAERVVGADGRTLAETWKGGMEALRGGTAAGFPNFMTVIGPNTGLGNSSMILMIESQLNYLADYLRQLNVLGGRTALDPRPAAVRNWNHRVQERMKRTVWNTGGCTSWYLDASGRNTTVWPGTTAEFRRETRRVDLAEYQVLRPAPAQVGAKAAEADTGADTGADAEVSA", "text": "FUNCTION: Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH and/or NADH as an electron donor. Thus, can convert bicyclo[3.2.0]hept- 2-en-6-one into the oxidative lactone products 2-oxabicyclo[3.3.0]oct- 6-en-3-one and 3-oxabicyclo[3.3.0]oct-6-en-2-one. Is also able to catalyze the sulfoxidation of methyl phenyl sulfide (thioanisole). SIMILARITY: Belongs to the FAD-binding monooxygenase family."}
{"protein": "MVKNIKIFLSLFFVVVLGLLATTANSMVIGIDLGSQTFKVSLIKPGAFETVLNEQSGRKTISSVGWFKDERLFSSDSFSVWARNPKQNYNLIQAFLGIKYKEGLVEEISNGLPLGFKVKNDTVRNTVSIVYDDDTNYSAEELTGMLLRRVKDMASSYAGSSIKDCAITIPPYFTQQQRQALLDAAQLAGLNVLSLIHDVNAAALSFAMDRTFLEKNESVIFYDMGARHTSVSLVEFESHNEQIKGVKKNKTVSSASVKGIEWDEKLGGFDFDMVIVNHLKTLLKKQIPSANVDDIKITIKLLKEVGKMKENLSVNQQAQIFIGSLVDDHDFQATISKQQFEELSQSLIERSLLPLKKLILSTGIKLKDIEYFEVIGGGVRIPFIQQALKDYLKRDTLDKHLNGDEAMSNGAAFYAASLTHYFKVKEIKLKDILLNSVDVEINNNIINSGGAGETLLEETEDNEDNELNNSGNEQQQQQQPTINQGGLKDKKIQLFKVNSKLGIKKTVSFSSENGFSLFLNNPTINNPLATYTVSNVPTPGEKYNFTGKPKIHCSFRLTTSGIVVLEKAEAEITVSLIKPQPQQNKTSSSTSTTKKNTTTIETTDGGSEETTDETTTKQQQQQEKEEEEEVVVVEKVIEYIQKTIRVPLNFTIKYNGCVEPLSKELSQESNDRINKLDQVDRILRELRQERNNLESFIYETKDKLESNEEYLKCSTQQERDQLVEELDKTSAWLSDALDNDNTETEEYRKQLKDIKKKADKIVNRVSQYQLVPVALEELEDTVDKVKPMFEIASKDLNVTAEELKETTDKIQSVSDWVQEKKSEFKLADYSKDLQTSSFDIKFKLYDLERTIKEILKKKKKPVKPSSSKKDKSSKSSKGKSNSTDEKDQKQKEQKEQQQQQKEESQFQNDGAEEQQFEDDHKVHDEL", "text": "FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MQTAYWVMVMMMVWITAPLSEGGKPNDVIRGLVPDDLTPQLILRSLISRRRSDKDVREGYKCVWKTCMPALWRRHDLKGKD", "text": "FUNCTION: Moderately activates human somatostatin receptors (SSTR) with a specific activation of SSTR1 (EC(50)=2.9 uM) and SSTR4 (EC(50)=5.1 uM). In vivo, does not cause behavioral changes in mice within a few minutes of intracranial injection, but causes a progressive loss of movement thereafter. Four to five hours after injection, mice recover, even with the highest dose tested (5.4 mg/kg). Shows antinociception and antihyperalgesia activities in two mouse models of acute pain, most probably by acting outside the central nervous system. FUNCTION: Moderately activates human somatostatin receptors (SSTR) with a preferential activation of SSTR1 and SSTR4. In vivo, does not cause behavioral changes in mice within a few minutes of intracranial injection, but causes a progressive loss of movement thereafter. Four to five hours after injection, mice recover, even with the highest dose tested. Shows antinociception and antihyperalgesia activities in two mouse models of acute pain, most probably by acting outside the central nervous system. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin C superfamily. Consomatin family."}
{"protein": "MADAEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDMKEKLSYIALDYDQEMETAKTSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSFIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF", "text": "FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. FUNCTION: Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family."}
{"protein": "MPGPLRLLCFFALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNILTEVPVRPLSNLPTLQALTLALNNISSIPDFAFTNLSSLVVLHLHNNKIKSLSQHCFDGLDNLETLDLNYNNLDEFPQAIKALPSLKELGFHSNSISVIPDGAFAGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASLVQWFPNLAGTVHLESLTLTGTKISSIPDDLCQNQKMLRTLDLSYNDIRDLPSFNGCRALEEISLQRNQISLIKETTFQGLTSLRILDLSRNLIREIHSGAFAKLGTITNLDVSFNELTSFPTEGLNGLNQLKLVGNFQLKDALAARDFANLRSLSVPYAYQCCAFWGCDSYANLNTEDNSPQDHSVTKEKGATDAANATSTAESEEHSQIIIHCTPSTGAFKPCEYLLGSWMIRLTVWFIFLVALLFNLLVILTVFASCSSLPASKLFIGLISVSNLLMGIYTGILTFLDAVSWGRFAEFGIWWETGSGCKVAGSLAVFSSESAVFLLTLAAVERSVFAKDVMKNGKSSHLRQFQVAALVALLGAAIAGCFPLFHGGQYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAIIYTKLYCNLEKEDPSENSQSSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAISISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKDDWKLLKRRVTRKHGSVSVSISSQGGCGEQDFYYDCGMYSHLQGNLTVCDCCESFLLTKPVSCKHLIKSHSCPVLTVASCQRPEAYWSDCGTQSAHSDYADEEDSFVSDSSDQVQACGRACFYQSRGFPLVRYAYNLPRVRD", "text": "FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however require additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development; required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and pro-inflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP (PubMed:24353284). Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland (PubMed:32493844). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGSGGSGGGSHHHHQSRGACTSHDPQSSRGSRRRRRQRSEKKKAHYRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEDDHGDECSYTDLLPQDEGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLVMALSAGGHGGLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCAKEEKCQGKGDDSETDKNNCSNAKAVETDV", "text": "FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:19912772, PubMed:8495559). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:8495559). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure (PubMed:19912772, PubMed:8495559). Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:17156368). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, axon. SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily."}
{"protein": "MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV", "text": "FUNCTION: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Cytoplasm, cytoskeleton Cell membrane; Single-pass type I membrane protein Cell projection, lamellipodium Cell projection, filopodium. SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted. SIMILARITY: Belongs to the SCF family."}
{"protein": "MVSKPFQRPFSLATRLTFFISLATIAAFFAFAWIMIHSVKVHFAEQDINDLKEISATLERVLNHPDETQARRLMTLEDIVSGYSNVLISLADSHGKTVYHSPGAPDIREFTRDAIPDKDAQGGEVYLLSGPTMMMPGHGHGHMEHSNWRMINLPVGPLVDGKPIYTLYIALSIDFHLHYINDLMNKLIMTASVISILIVFIVLLAVHKGHAPIRSVSRQIQNITSKDLDVRLDPQTVPIELEQLVLSFNHMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLNLADEVGKVFDFFEALAEDRGVELRFVGDECQVAGDPLMLRRALSNLLSNALRYTPTGETIVVRCQTVDHLVQVTVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDVRGTRFVIILPA", "text": "FUNCTION: Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Acts as a copper/silver ion sensor. Activates CusR by phosphorylation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MAKLSKQQKKQMYIEKLSSLIQQYSKILIVHVDNVGSNQMASVRKSLRGKATILMGKNTRIRTALKKNLQAVPQIEKLLPLVKLNMGFVFCKDDLSEIRNIILDNKSSSHPARLGVIAPIDVFIPPGPTGMDPSHTSFLESLGISTKIVKGQIEIQEHVHLIKQGEKVTASSATLLRKFNMNPSYGVDVRTVYDDGVIYDAKVLDITDEDILEKFSKGVSNVAALSRATGVITEASYPHVFVEAFKNIVALIIDSDYTFPLMKILKKWVENPEAFAAVAAPASAAKADEPKKEEAKKVEEEEEEEEDGFMGFGMFD", "text": "FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10. SIMILARITY: Belongs to the universal ribosomal protein uL10 family."}
{"protein": "MEFPASVASLSANTVGSNDVLRRSVAYHPNIWGDFFLAHTSEFMEISIAEKEEHEWLKEEIKKLLVQTEYDSILKLELIDSIQRLGVSYHFEKEIDRILRYVHQTYPIYETENKDLRMLALRFRLLRQHGFHVPCDVFSEFIDAEGNLMESIAYDIQGILSLYEASNYGVLGEEILDKALDSCSSHLESLITDTNDDRLSRQVKEALKIPISKTLTRLGARKFISMYKEDDSHNEKLLKFAMLDFNMVQRLHQNELSHLTSWWKELDFANKLPFARDRLVECYFWIMGVYFEPRHEIARKILTKVIYMASVLDDTYDVYGTLDELILFTSVVRRWDISGIDELPTYMRIYLRALFDVYVEMEEEMGKIGKSYAVEYAKEEMKRLAEVYFQEAQWFFSKYKPTMQEYMKVALLSSGYMMMTINSLAVIEDPITKKEFDWVVSEPPILKSSSIITRLMDDLAGYGSEDKYSAVHLYMNEKGVSEEEAFQELRKQVKNSWKNRNKECLEPRSASVPILTTVVNFTRVVVVLYTDEDAYGNSKNKTKDMIKSILVDPV", "text": "FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)- farnesyl diphosphate (FPP) to (E)-beta-caryophyllene and alpha-humulene (PubMed:20419468, Ref.2). SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MVEMESAKSVLEPLAWLMQMITGLLMILLVTAHFYVTHMTTHDALRYAEVVERVAQPEFKALYALLLLAVSFHAFNGLRAILLDTNAGMRKKGAVSALTTLAFLLAFFYGLYLLFSI", "text": "FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MTPATRNNDSAVAVADAFDDTGDGPPTAARFAALAACWRQPDDDLQAALAAETDTTVDAQSLRAEYTRLFVGPGPSQSPPYESVYRDGERDADLGPVYGSSTQAVARWYSEYGLQPAASESAPPDHLATELEFAAYLREHEGAETLEQFLTEHPRNWVESFARRVRDADPKPFYRTLLNVTVDTLARADTPL", "text": "FUNCTION: May be involved in the biogenesis/assembly of dimethyl sulfoxide (DMSO) reductase. SIMILARITY: Belongs to the TorD/DmsD family."}
{"protein": "MEASAPDRARRGWRRARAAASPLSRAAVVLLLSALVLRAPPSVGYLDRLPRSFHLTQESAKIVGSPNFPVKVYVMLHQKSPHVLCVTQRLRNFELVDPSFQWHGPKGKIVSENSTAQVTSTGSLVFQNFEESMSGVYTCFLEYKPTVEEVVKNLQLKYIIYAYREPRYYYQFTARYHAAPCNSIYNISFEKKLLQILSKLVLDLSCEVSLLKSECHRVKMQRAGLQNELFFTFSVSSLDTEKGPKPCAGHSCESSKRLSKAKNLIERFFNQQVEVLGRRAEPLPEIYYIEGTLQMVWINRCFPGYGMNILKHPKCPECCVICSPGTYNSRDGIHCLQCNSSLVFGAKACL", "text": "FUNCTION: Plays a role in acrosome compaction and sperm morphogenesis. Is implicated in sperm-oocyte interaction during fertilization. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome Secreted Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Peripheral membrane protein Note=First localized in acrosome granule, later migrates to the inner and outer acrosomal membrane. Released after the acrosomal reaction. SIMILARITY: Belongs to the zona pellucida-binding protein Sp38 family."}
{"protein": "VEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAQEMFEHICRHVRYATNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDG", "text": "FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S- nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro- inflammatory mediators such as IL6 and IL8. SUBCELLULAR LOCATION: Cytoplasm, cytosol Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. SIMILARITY: Belongs to the NOS family."}
{"protein": "MSDQKFISIRGAREHNLKNVDLDLPRDKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLEMMQKPDVDQIDGLSPAISIEQKTTSRNPRSTVGTVTEIYDYMRLLFARVGIPYSPATGLPIESQTVSQMVDRVIALEEGTRLYILAPIVRGRKGEYRKELAELQKKGFQRVKVDGTFYEIADVPPLDKKYKHDIDVVVDRVVVRPDLSTRLADSLETCLKLADGLAIAEFADKPLPVGETAEGGSANKSANETHERILFSEKFACPVSGFTIPEIEPRLFSFNNPFGACPTCDGLGTQQAIDPNLIIPDESAALKDGAVAPWARSSSPYYNQTLEALGKAYGFKVSARWSELSEEARQAILYGTKGREITFHYDDGLRSYQTTKPFEGVIPNLERRWKETDSAWSREEIERFMASTPCPACNGYRLKPEALSVKIGKKHIGEITEMSIRKADAWFRDIDGSFNEKQREIAARILKAIRERLQFLNNVGLDYLTLARNSGTLSGGESQRIRLASQIGSGLTGVLYVLDEPSIGLHQRDNARLLDTLRHLRDLGNTVIVVEHDEDAILTADYVVDIGPAAGVHGGKVIAQGSPQDIMANTNSLTGKYLSGAMEVAVPAERRKISKTKRLRVVGARGNNLKNVSADIPLGTFTAVTGVSGGGKSTFLIETLFKAASRRIMGSREHPAEHDRIEGLEFLDKVIDIDQSPIGRTPRSNPATYTGAFTPIRDWFAGLPEAKARGYQPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVTCDVCHGKRYNRETLDVLFKGKSIADVLDMTVEEGAEFFSAVPAVRDKLETLVKVGLGYIKVGQQATTLSGGEAQRVKLAKELSRRATGRTLYILDEPTTGLHFHDVAKLLEVLHELVEQGNTVVVIEHNLEVIKTADWVIDLGPEGGDGGGEIVAVGRPEDIVQEKRSYTGQFLKELLERRPKRSSQAAE", "text": "FUNCTION: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family."}
{"protein": "MAFEDVWKKISWLYYQYILVTALYMLEPWERAIFNSILISVAGMAVYTGYVFMPQHIMAILQYFEMVQ", "text": "FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SPTSS family. SPTSSA subfamily."}
{"protein": "MSLPPLDELQWKSPEWIQTFGLHTDNVLDYFSESPFFDKTSNNQVVKMQQQFSQQSQVPGSMPLGSSSGIGAAAGAGTVSPSDRSLIWERYPVHAMLEKELMKMKGIEYILVLVREPDLWIIRKQQRDGPTKTTTLRDYYVIGSAVYQSPTVYKIIQNRLLSTNYHLSHSLSQLNKLVEFHPAQGASFLRPEDPLCSSVAAATTSGSTASHTVASSVSVPETGPINAETSGATAAATSIDPDRRQDSFNTEIMDKLMATSIKANPVYI", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 6 family."}
{"protein": "MEAIAKYDFKATADDELSFKRGDVLKVLNEECDQNWYKAELNGKDGFIPKNYIEMKAHPWFFGKIPRAKAEEMLGKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQVHGGDRATSLPQQPTYVQALFDFDPQEDGELGFRRGDFIQVVDNSDPNWWKGTCLSQTGMFPRNYVTPVNRNM", "text": "FUNCTION: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway (By similarity). Promotes meiotic reinitiation during oocyte maturation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Endosome Golgi apparatus. SIMILARITY: Belongs to the GRB2/sem-5/DRK family."}
{"protein": "MNNIDLRVYSFIDSLQPQLASYLATSSQGFLPVPGDACLWIEVAPGMAVHRLSDIALKATNVRLGEQVVERAFGSMEIHYRNQSDVLASGEAVLREINHAQEDRLPCRIAWKEIIRAITPDHATLINRQLRKGSMLLPGKSMFILETEPAGYIVQAANEAEKAAHVTLIDVRAFGNFGRLTMMGSEAETEEAMRAAEATIASINARARRAEGF", "text": "FUNCTION: Part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. It may control transport of RuBisCO reactants in and out of the carboxysome (By similarity). In an E.coli expression system not absolutely necessary, its presence leads to fewer defective carboxysomes, suggesting this subunit may play a role in assembly (PubMed:22184212). FUNCTION: Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell. SUBCELLULAR LOCATION: Carboxysome Note=This bacterium makes alpha-type carboxysomes. SIMILARITY: Belongs to the EutL/PduB family."}
{"protein": "MSNFFKKLVKKDGTPKSSRKSKSESPVGKYDMNGNQVVPDTASSYSDDSNSLSDSYDKRGEPNIGEQIDTLDDYNFGNEIGDAESAPEDKKSLWKKVGGLVGKDPMSLVSLPVYFFEPLTVLECQLEPLRFVELIEKASTCSDSIDRLMYLTAFNIAVFSSYTRTAKPFNPLLGETFEYIDKQGRYKSFCEQVSHHPPIGIAQTTSEIFDLQQESWITTKFWGNSLDVFSHGQNHLYLNSTGEHFTWKVPSAICHNIIFGKMWIEHYGDLIVENHNTGEKAIINFQKSGWFEGTQRKVQGEILDSKGNARVHINGKWDKYVKAKKHSEGPSRKSSGEITLWEATIEPPENFNKWKHGKWIQGLNEMSKEYQAVLPSTDSRVRMDRIYLEREENKLANKEKNKIEEREREKRKTRESRKEIWKPNYFSKREDSKYGYRWDFNGKYWDERDKRVDSVVDKFKNDPNFDSNKIPEYDDSKLNISVKSVRKFSRDFTNSSTPTQLKRSFSKLKLEEQPQSQSLPPMIKEELSSSTVDHEETFYSESNEAKLESIKEDANSHTYIYSSPTIGHSGR", "text": "SIMILARITY: Belongs to the OSBP family."}
{"protein": "MRVSLFLQKQIIECSKAFQPHSTRLQWPKSQDKVFVAMSGGVDSSFSAYLLKSQGYNVEGVFMRNWLDEDSAPSGCPAERDWATVQKVCKKLNISCRRFNFEKEYWNLVFEPSLDLYENGLTPNPDVSCNRQVKFGALFDALKKHCENNVKGDWWLASGHYAKSVVNIETNESHMCIPTDKRKDQTLFLCTIRKEALEKTIFPLHNWTKENVKKQASSAGFKEIAEKQESQGLCFVSPNVGRKFRKFLQRYLNFSDRPIKVIAGKNVVGEFSGNHGIWSLTVGERCGLSLPQAQSEYFGRWYVWKKDIKNNALYICRGTNNELLMSKCIYLKDWKWCGTKLQNLEKSALSCFVRVRHQQPLQPAKVTWRNPESVKIHFQDKQRAVTPGQVIAVYVNDVCLGGGMVDTVEPEKDFD", "text": "FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the MnmA/TRMU family."}
{"protein": "MNTLIYISALGILSLLAEIFNARKAIVPITIIGLLAIFGFNISEYNHLGSYYNNMMVVDKFSVAFSSLFIIITVFLVALSHEFYKEQKTKISDYVGIKVFLLSGAVAMVSFGNLSMFFLGIEVLSISLYILAASNRLNLKSNEAGMKYFLMGSFASGIILFGICLIYGATGSFDLNKILILINTQAYPQWYYIGIVFLLIGMLFKIATVPFHFWAPDVYEGSPALTTATMSTLAKIVAMATLYKLVTVLLPIQLYSIQIIIVCVAIASMLLGNIMALRQNNVKRMFAFSGISHAGFMVSTLLLTSNAASTLLYYASAYAIAGIAFFAVVMYVTKDKENETINSFNGLGKTHPLLAGILTAALLSMAGIPVLSGFFAKFFLLNQLVYTDWLIVVFVAIISSIISVGYYFKIIIAMYTKESEQTLPNVPVMYQIVAVVALILNIALGLFPNVVLKLL", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."}
{"protein": "AVMGRNLALNIESRGYTVSVFNRSREKTEEVIAENPGKKLVPYYTVKEFVESLETPRRILLMVKAGAGTDAAIDSLKPYLDKGDIIIDGGNTFFQDTIRRNRELSAEGFNFIGTGVSGGEEGALKGPSIMPGGQKEAYELVAPILTKIAAVAEDGEPCVTYIGADGAGHYVKMVHNGIEYGDMQLIAEAYSLLKGGLNLSNEELAETFTEWNKGELNSYLIDITKDIFTKKDEEGKYLVDVILDEAANKGTGKWTSQSSLDLGEPLSLITESVFARYISSLKEQRVAASKVLSGPKAQLAGDKAEFIEKVRRALYLGKIVSYAQGFSQLRAASDEYNWDLNYGEIAKIFRAGCIIRAQFLQKITDAYAENAGIANLLLAPYFKKIADDYQQALRDVVAYAVQNGIPVPTFSAAVAYYDSYRAAVLPANLIQAQRDYFGAHTYKRT", "text": "FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family."}
{"protein": "MIPPRALLLISVWMVSGGRTLLVTVQDTQRYTMLFSSIILKCDYSTSAQIQDVAVTWRFKSFCKDPIFDYYSAAYQASLSLNQDPANDCNDNQREVRIVIQKRGQNEPVLGVDYRQRKITIQNKADLVISEVMWWDHGVYFCSVEAQGDTSGDPDKEVKLVVLHWLTVLFIILGALFLFLLIGICWCQCCPHCCCCYVRCPCCPTRCCCPEEALARHNYMKQMESMTPWMLDRPYYAGADRNSQHSSYQLNPLLQRDLSLQSSLPMPAPMSFSPPNNKVLDFLETEIKNLNTAQPLMSAPHYGGASHHPSMLSSLSEVGVREVDRRVIQLPPLVEHIVSSHRSSNSSHQRRNMGSWDPLDGERDRRRNRQLDDSLSNETNWRAQERQHSDRSSGHRRDPPNNRRPRRDVSPPRRYGDSYSDESANNDPRGRSNPHSDRARPTERRRSPERGDQGRRGSPDRYSRSQRHRRSYSPPHRRDSWSSEDETRNNQRGRGRRERSYEWPEEKPPSYKSLEICAGKAPTQRPGAVRQSDRASSRSGRSMVI", "text": "FUNCTION: Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (tTJs). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell junction, tight junction. SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7 family."}
{"protein": "MFTTALAQRENTQLGELPLDLFAAIQSLKKELNAVILAHYYQEPDIQDIADFIGDSLQLARAAEKTNADVIVFAGVHFMAETAKILNPDKLVLLPDLNAGCSLADSCPPEAFAAFKAAHPDHLVVSYINCSADIKAMSDIICTSSNAVKIVQQIPKEQPIIFAPDRNLGRYVMEQTGRDLVLWQGSCVVHETFSEKKIVQLKIAHPEAEAIAHPECESSVLRHASFIGSTAALLKYCQNSPTKEFIVATEPGIIHQMQKLAPDKHFIPAPPMNNCACNECPFMRLNTLEKLYWAMKNRTPEITMLEDIRLAALRPMQRMLEMSV", "text": "FUNCTION: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the quinolinate synthase family. Type 2 subfamily."}
{"protein": "MTENHDAIVTDAKSEGSGGCPVAHDRALHPTQGGGNRQWWPERLNLKILAKNPAVANPLDEDFDYAEAFKALDLAAVKRDIAEVLTTSQDWWPADFGNYGPLMIRMAWHSAGTYRISDGRGGAGAGQQRFAPLNSWPDNGNLDKARRLLWPVKKKYGQSISWADLLILTGNVALETMGFKTFGFGGGRADVWEAEEDVYWGPETTWLDDRRYTGDRELENPLGAVQMGLIYVNPEGPNGNPDPIAAARDIRETFRRMAMNDEETVALIAGGHTFGKTHGAGPADHVGADPEAASLEEQGLGWRSTYGTGKGADAITSGLEVTWTSTPTQWSNGFFKNLFEYEYELEQSPAGAHQWVAKNAPEIIPDAHDPSKKHRPRMLTTDLSLRFDPIYEPISRRFYENPEEFADAFARAWYKLTHRDMGPKSLYLGPEVPEETLLWQDPLPEREGELIDDADIAILKTKLLESGLSVSQLVTTAWASASTFRASDKRGGANGARIRLAPQRGWEVNDPDQLAQVLRTLENVQQEFNASSGAKKVSLADLIVLGGAAGVEKAAKEAGFEIQVPFTPGRVDATEEHTDVESFEALEPTADGFRNYLGKGNRLPAEYLLLDKANLLNLSAPEMTVLVGGLRVLGANHQQSQLGVFTKTPGVLTNDFFVNLLDMGTTWKATSEDQTTFEGRDAATGEVKWAGSRADLVFGSNSELRALAEVYASDDAKEKFVKDFVAAWHKVMDADRFDLV", "text": "FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily."}
{"protein": "MNKWLCCALLVLLDIIEWTTQETLPPKYLHYDPETGHQLLCDKCAPGTYLKQHCTVRRKTLCVPCPDHSYTDSWHTSDECVYCSPVCKELQSVKQECNRTHNRVCECEEGRYLEIEFCLKHRSCPPGSGVVQAGTPERNTVCKKCPDGFFSGETSSKAPCIKHTNCSTFGLLLIQKGNATHDNVCSGNREATQKCGIDVTLCEEAFFRFAVPTKIIPNWLSVLVDSLPGTKVNAESVERIKRRHSSQEQTFQLLKLWKHQNRDQEMVKKIIQDIDLCESSVQRHLGHSNLTTEQLLALMESLPGKKISPEEIERTRKTCKSSEQLLKLLSLWRIKNGDQDTLKGLMYALKHLKTSHFPKTVTHSLRKTMRFLHSFTMYRLYQKLFLEMIGNQVQSVKISCL", "text": "FUNCTION: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MRPATRIFIKQRFTDYYDKARISPPSSVKEREFGFIFFDDRYPDDIRMRRHIGFSSGDEMQEYVKSLVPAHAYYSTAYYRTPQAPTMGDKEWLGADLIFDLDADHIMRGSYEAMLERIKGEAEKLLDVLDNELGIDMRTIKLVFSGGRGYHVHVQELAFRDFEPAERRELVDYVCGTGISPSLLLHDWKPGRRGWHDRFRLVLTRYLQDLSTRPIKEVKAELSSLRGVGQVMAERFAGMIPELITLLNTNPSSILLRDQTVRTVFGALTSERESTLLPHIREAAVQADEPVTTDTRRLIRLPGSLHAKSGFKVVPMEVKELHDFDPLIDAVAFGEREVIIESEREYSFSLLGSSYDIPKGRLKVPEAVGVFLCCRGMAEIGGVLDHAS", "text": "FUNCTION: Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair. SIMILARITY: Belongs to the eukaryotic-type primase small subunit family."}
{"protein": "MEQVEILRKFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKIADGVNEINTENMVSSIEPEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDNDRYHPKPVLHMVSSEQHSADLNRNYSKSTELPGKNESTIEQIDKKLERNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASPCIADKISKPQELSSDLNVGDTSQNSCVDCSVTQSNKVSVTPPEESQNSDTPPRPDRLPLDEKGHVTWSFHGPENAIPIPDLSEGNSSDINYQTRKTVSLTPSPTTQVETPDLVDHDNTSPLFRTPLSFTNPLHSDDSDSDERNSDGAVTQNKTNISTASATVSAATSTESISTRKVLPMSIARHNIAGTTHSGAEKDVDVSEDSPPPLPERTPESFVLASEHNTPVRSEWSELQSQERSEQKKSEGLITSENEKCDHPAGGIHYEMCIECPPTFSDKREQISENPTEATDIGFGNRCGKPKGPRDPPSEWT", "text": "FUNCTION: Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:18559503). Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2 (PubMed:17329398, PubMed:27134172). Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (PubMed:27134172). SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion Cell projection, podosome Note=Partial translocation to focal adhesion sites may be mediated by interaction with SORBS2. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class 4 subfamily."}
{"protein": "MKYQTLSGLLALSLLFGCSSSPDVVPDVPPSQLYSEAQTALQSGTWLTAIEKLEALDSRYPFGAYSEQVQLDLIYAYYKNDDLALGLATIERFTRLNPTHEKMDWVLYMRGLTHMAQDRNFMHDLFNIDRRDRDPEPVKAAFADFKKLLQRYPNSPYAEDAQRRMFALKNRLAEYDLATADFYLRREAWIAAINRTQELQKTYPDTEAARKSLEIQLEAYQQLGLTDAIERTKQLMQLNPL", "text": "FUNCTION: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the BamD family."}
{"protein": "MFSPCTVKEKRSTLRSVAPNPESSVIPPIPLPSRRYKTRHIDALCSLMHLCLLRKDYPRASRAFSLLLRSKSVDISKLWNIGLEILNKVNPEASSEYMERLIARYPARPSINNSYPNRNAEHFFPAYIMLLIQRQEYNKAMKLLDEYLLLPPYNQNPALHEYSGMLCFELAKEEASESERTKWIEKAKYNFSNAGIDVEL", "text": "FUNCTION: Subunit of a multiprotein complex essential for the initiation of rDNA transcription by RNA polymerase I. Binding to the DNA template is dependent on the initial binding of other factors. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "DPAFRLPTTTRPRHYQAAIPDFSAGA", "text": "FUNCTION: Binds to the B.thuringiensis toxin, CryIA(A). SIMILARITY: Belongs to the peptidase M1 family."}
{"protein": "MKSPAPSRPQKMALIPACIFLCFAALSVQAEETPVTPQPPDILLGPLFNDVQNVKLFPDQKTFADAVPNSDPLMILADYRMQQNQSGFDLRHFVNVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRSTENTEKWDSLLPLPEPYVVPGGRFREVYYWDNYFTMLGLAESGHWDKVADMVANFAHEINTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMDGVENLQAGQQEKRVVKLQDSTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDLNSLMFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQGWYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRANKMATATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQHTYDREKKLVEKYDVSTTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEQPCDNVPATHPTVKSATTQPSTKEAQPTP", "text": "FUNCTION: Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the glycosyl hydrolase 37 family."}
{"protein": "MAGVCAVKVGIIGGSGLDDPDILEGRLEKYVDTPFGKPSDALVLGKIKNVDCVLLASRHGRQHTIAPTNVNYRANIWALKSEGCTHILVTTACGSLREEIQPGDIVIVDQFIDRTTKREQTFYDGGPSCLPGVCHIPMAEPFCAKTREVLIDIAKRLGIKCHSKGAMITIEGPRFSSKAESQMFRLWGADVINMTTVPEVILAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKATSILLTAIPQIAAMDWTELLQSMKSTVQLSVMLPKH", "text": "FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily."}
{"protein": "MKLERILPFSKTLIKQHITPESIVVDATCGNGNDTLFLAEQVPEGHVYGFDIQDLALENTRDKVKDFNHVSLIKDGHENIEHHINDAHKGHIDAAIFNLGYLPKGDKSIVTKPDTTIQAINSLLSLMSIEGIIVLVIYHGHSEGQIEKHALLDYLSTLDQKHAQVLQYQFLNQRNHAPFICAIEKIS", "text": "FUNCTION: Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA (PubMed:36762482). Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34 (PubMed:36762482). SIMILARITY: Belongs to the methyltransferase superfamily. MnmM family."}
{"protein": "MMMNAFIEPAQHHLASYGLRMSPNTTASNSNAQQQQQQQLEMTQQQQQQQQQQQQQQQQDQESAAATAAAYQNSGYGHFNSYASRDFLLGRREAEYGVAGSAGQASAAADSMLFSGFPAQAAELGSGFGQHPFHSHHHHHQMRMGMADAYAAGHPYNHHGNFPTAAVHHPVVHHPSHHAMSAMHPAGAGAFLRYMRHQPASSASSVKQEMQCLWIDPDQPGLVPPGGRKTCNKVFHSMHEIVTHLTVEHVGGPECTTHACFWVGCSRNGRPFKAKYKLVNHIRVHTGEKPFACPHPGCGKVFARSENLKIHKRTHTGEKPFKCEHEGCDRRFANSSDRKKHSHVHTSDKPYNCRINGCDKSYTHPSSLRKHMKVHGNVDEKSPSHGYDSEGEESSSSSIITGGAQTPPSTRLDGSAGSSSGVSSLSGGSGIKSSPHSIKSEPNPMHSVHLGASSSGSSSTASSSASHLLQHQQHQHQQQQQQQQHQQQAQQQQQLTAHPSDPKSSPALQLMAASASAYLPPPLGPPPSHHHHPHHHQAAPSPGAAAASASMLHHNHHLLYHPAAQHHPPSDWYHTTAPSGSAEAMNPLNHFGHHHHHHHLMHPGAATAY", "text": "FUNCTION: Transcription factor essential for parasegmental subdivision of the embryo. It is involved in the activation of wingless (wg) in odd parasegments. It is also required for the timely activation of wg in the remaining parasegments and for the timely activation of engrailed (en) in all parasegments. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
{"protein": "MHPAAFPLPVVVATVLWGAAPVRGLIRATSEHNASMDFADLPALFGATLSDEGLQGFLVEAHPENACGPIAPPPSAPVNGSVFIALLRRFDCNFDLKVLNAQKAGYGAAVVHNVNSNELLNMVWNSEEIQQQIWIPSVFIGERSAEYLRALFVYEKGARVLLVPDNSFPLGYYLIPFTGIVGLLVLAMGTVLIVRCIQHRKRLQRNRLTKEQLKQIPTHDYQKGDEYDVCAICLDEYEDGDKLRVLPCAHAYHSRCVDPWLTQTRKTCPICKQPVHRGPGDEEQEEETQEQEEGDEGEPRDQPASEWTPLLGSSPTLPTSFGSLAPAPLVFPGPSTDPSPPSSAALA", "text": "FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of the TORC1 signaling pathway. Positively regulates the TORC1 signaling pathway independently of arginine levels: acts by catalyzing 'Lys-29'- polyubiquitination and degradation of CASTOR1, releasing the GATOR2 complex from CASTOR1. Also negatively regulates the TORC1 signaling pathway in response to leucine deprivation: acts by mediating 'Lys-63'- linked polyubiquitination of SESN2, promoting SESN2-interaction with the GATOR2 complex. Also involved in protein trafficking and localization. Acts as a regulator of synaptic transmission by mediating ubiquitination and degradation of AMPAR receptor GluA2/GRIA2. Does not catalyze ubiquitination of GluA1/GRIA1. Also acts as a regulator of the recycling endosome pathway by mediating ubiquitination of VAMP3. Regulates lysosome positioning by catalyzing ubiquitination and degradation of ARL8B. Plays a role in growth regulation involved in G1/S transition by mediating, possibly by mediating ubiquitination of SLC22A18. Acts with a limited set of E2 enzymes, such as UBE2D1 and UBE2N. SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane protein Endosome membrane; Single-pass type I membrane protein Endomembrane system; Single-pass membrane protein Cell membrane; Single-pass type I membrane protein Note=Targeted to cytoplasmic membranes; mainly localizes to lysosomal membrane. A subpopulation localizes to the cell membrane of neurons. SIMILARITY: Belongs to the Godzilla family."}
{"protein": "MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRSLLPGELAKHAVSEGTKAVTKYTSSK", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H2B family."}
{"protein": "MSSERVLSYAPAFKSFLDTSFFQELSRLKLDVLKLDSTCQPLTVNLDLHNIPKSADQVPLFLTNRSFEKHNNKRTNEVPLQGSIFNFNVLDEFKNLDKQLFLHQRALECWEDGIKDINKCVSFVIISFADLKKYRFYYWLGVPCFQRPSSTVLHVRPEPSLKGLFSKCQKWFDVNYSKWVCILDADDEIVNYDKCIIRKTKVLAIRDTSTMENVPSALTKNFLSVLQYDVPDLIDFKLLIIRQNEGSFALNATFASIDPQSSSSNPDMKVSGWERNVQGKLAPRVVDLSSLLDPLKIADQSVDLNLKLMKWRILPDLNLDIIKNTKVLLLGAGTLGCYVSRALIAWGVRKITFVDNGTVSYSNPVRQALYNFEDCGKPKAELAAASLKRIFPLMDATGVKLSIPMIGHKLVNEEAQHKDFDRLRALIKEHDIIFLLVDSRESRWLPSLLSNIENKTVINAALGFDSYLVMRHGNRDEQSSKQLGCYFCHDVVAPTDSLTDRTLDQMCTVTRPGVAMMASSLAVELMTSLLQTKYSGSETTVLGDIPHQIRGFLHNFSILKLETPAYEHCPACSPKVIEAFTDLGWEFVKKALEHPLYLEEISGLSVIKQEVERLGNDVFEWEDDESDEIA", "text": "FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity. SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure. SIMILARITY: Belongs to the ATG7 family."}
{"protein": "MSWNHQSVEIAVRRTTVPSPNLPPGFDFTDPAIYAERLPVAEFAELRSAAPIWWNGQDPGKGGGFHDGGFWAITKLNDVKEISRHSDVFSSYENGVIPRFKNDIAREDIEVQRFVMLNMDAPHHTRLRKIISRGFTPRAVGRLHDELQERAQKIAAEAAAAGSGDFVEQVSCELPLQAIAGLLGVPQEDRGKLFHWSNEMTGNEDPEYAHIDPKASSAELIGYAMKMAEEKAKNPADDIVTQLIQADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITQGMMAFAEHPDQWELYKKVRPETAADEIVRWATPVTAFQRTALRDYELSGVQIKKGQRVVMFYRSANFDEEVFQDPFTFNILRNPNPHVGFGGTGAHYCIGANLARMTINLIFNAVADHMPDLKPISAPERLRSGWLNGIKHWQVDYTGRCPVAH", "text": "FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one. FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one. FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection (PubMed:20843794, PubMed:20545858). Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26- hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4- en-26-oate (PubMed:19846551, PubMed:20843794, PubMed:20545858). Also able to sequentially oxidize cholesterol itself, not only cholest-4-en- 3-one (PubMed:19846551, PubMed:20843794, PubMed:20545858). SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MVQPHVLLVTFPAQGHINPSLQFAKRLIEMGIEVTFTTSVFAHRRMAKIAASTAPKGLNLAAFSDGFDDGFKSNVDDSKRYMSEIRSRGSQTLRDVILKSSDEGRPVTSLVYTLLLPWAAEVARELHIPSALLWIQPATVLDIYYYYFNGYEDEMKCSSSNDPNWSIQLPRLPLLKSQDLPSFLVSSSSKDDKYSFALPTFKEQLDTLDGEENPKVLVNTFDALELEPLKAIEKYNLIGIGPLIPSSFLGGKDSLESSFGGDLFQKSNDDYMEWLNTKPKSSIVYISFGSLLNLSRNQKEEIAKGLIEIQRPFLWVIRDQEEEKEEEKLSCMMELEKQGKIVPWCSQLEVLTHPSLGCFVSHCGWNSTLESLSSGVPVVAFPHWTDQGTNAKLIEDVWKTGVRMRVNEDGVVESDEIKRCIEIVMDGGEKGEEMRKNAQKWKELARAAVKEGGSSEVNLKAFVLQVSKSC", "text": "FUNCTION: Glucosyltransferase acting on both abscisic acid (ABA) and auxin (IAA). Required for ABA-mediated fruit ripening, seed germination, and negative responses to drought. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MSFFIASSPHAHSRKSTPDLMKWVALCALPGLLAQTYFFGWGTLVQLILAITIALSLEALVMLFRKRPPMRALRDHSALVTAWLLAVAIPPMAPWWIITIGLLFAIVIAKHLYGGLGQNPFNPAMIAYVVLLISFPVQMTSWSAPLPLIEAGHEVAKDPVTFGDLLSLIFTGLTIDGSSLQQVRAGIDGITTATPLDAFKTGLHSGATSSEILSQPIFEGFAGVGWQWVNLAYLAGGLILLKQRVIQWHIPVGFLGALLVMSSFFSLFFPGETASPLFHLLSGATMLGAFFIATDPVSASTTIKGRILFGAIIGTLVFIIRSWGGFPDGVAFAVLLANMCVPLIDYYTKPRTYGH", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrB/RnfD family."}
{"protein": "MKSERVNYPVKLLNFILSIMNSYLFVLIVSIGFAESSSPKSSTSCSLMTSCAVEKCLDRGMVGRIITESSRDEVFGNLVEKFDMVCIAAKCGNECSQCKHCHYALEQMSALAQGEKTSGLCPKLETCVFNCLTEDVSKVLSCVATRCNVHCYDGDCPSCKMISRRIFSNICKQHSMTTQPQIKYEGTCPNLFMELADDYVAMKKKKL", "text": "FUNCTION: Acts downstream of daf-16/foxo to suppress tumors induced by disruption of gld-1. Potentially a direct target of daf-15/foxo. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MSIDKSYCGFIAIVGRPNVGKSTLLNKLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRAINRLMNKAASSSIGDVELVIFVVEGTRWTPDDEMVLNKLREGKAPVILAVNKVDNVQEKADLLPHLQFLASQMNFLDIVPISAETGLNVDTIAAIVRKHLPEATHHFPEDYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFVSNERGGYDINGLILVEREGQKKMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGYVDDL", "text": "FUNCTION: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. FUNCTION: An essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring on the order of seconds whereas hydrolysis occurs on the order of minutes. Plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing and 30S ribosomal subunit biogenesis. One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late assembly stage of the 30S ribosomal subunit. Its presence in the 30S subunit may prevent translation initiation. Seems to be critical for maintaining cell growth and cell divison rates; a dramatic reduction in Era protein levels temporarily arrests cell growth just before cytokinesis (at the predivisional two-cell stage) and delays cell division. Era mutant era1 suppresses some temperature-sensitive mutations that affect DNA replication and chromosome partitioning and segregation. The dominant-negative Era-de mutant which is missing residues in a putative effector region, is unable to complement the disruption mutant; upon overproduction it shows a significant decrease in cell viability and a synthetic lethal phenotype in the presence of acetate. Era function probably overlaps RbfA (PubMed:16825789). Binds to the pre-30S ribosomal subunit through several stages of protein assembly (PubMed:20188109). SUBCELLULAR LOCATION: Cytoplasm Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Binding is GDP or GTP-dependent, slightly more protein is bound in the presence of GTP than GDP. SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family."}
{"protein": "MRDAVTTLIKNYDLTGRYLDRNAMDELKAYFESGSARIAAAAMINANSATIVKRAAAQLFEEIPELIRPSGNAYTTRRFSACLRDMDYYLRYASYALIAADNNVLDERVLQGLRETYNSLGVPIGPTVRGIQIMKEMIEAMAEDSSLNSTDFIASPFDHMTRELSELSV", "text": "FUNCTION: A variant beta-allophycocyanin (AP) which forms a complex with ApcE, a phycobilisome terminal emitter that influences energy transfer to photosystem II. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the phycobiliprotein family."}
{"protein": "MAGTFPPKISPTLMTPDPHFIPGYSGFCPQYRYSLGKTYGQLTSQLLTNPDIRRSELLVLQSNPFPPPRDHSFDGGSQELGGRRQHPGDPNLTISMIPGYTGFIPRSQKFFAKTYAETSRDALSDFHSERRGQEAQRQELLLMSKLQEGRLPRTEQEKQLLASRHRTPLPALAKEPAPFMALRGFQPQGSPYYMEEENPNKCFISGYTGYVPRSRFLIGSGYPITTNRAMVEFAHMNQKKGVRFSEGYKEGGSPHTEPGQIYLEELGLLPRYTGYVPGYKFQFGNTFGRLTQNALGHSTLQKQTVN", "text": "FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the UPF0605 family."}
{"protein": "MKVKAPGRINIIGEHTDYNDGYVLPFAVNRYVFLSIEGSERFIFHSENVNETVEMEKIEKLNKWTDYISGVIASFEKRGYRVSPVKISVSSNLPIGAGLSSSAALEVATAYAISEYFGFNVPKLELVKIAREAEVEFVGVRCGIMDQFTAVFGKKDHAIFLDTMTLEYEYVPLKLEGYEINLVDSNVKHELSSSEYNRRRQECEEVLKTLEKKSFREVTKEDLERLSGTLRKRAQHVLEENERVLKSVQALKEGDFETLGKLLFSSHESLRDLYEVSCEETDFIVDYLRGKEGILGARMVGGGFGGGVIVLSKKGAFGKIKEELVESYRKRFGIDLIFHEIESSDGVQKI", "text": "FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily."}
{"protein": "MSPHFPALTPDQKKELADIAQRIVASGKGILAADESVGTMGKRLTQIGLENTDEHRRFYRQLLFTTDPSIKEHIGGIIFFHETMYQKTDGGVPFVKLVKDNGILVGIKVDKGVVPLAGTNGEGTTQGLDGLAERCAQYKKDGADFAKWRCVLKISPNTPSRLSIVENANVLARYATICQQNGLVPIVEPEILPDGDHDLKTCQYITEKVLAATYKALSDHHVYLEGTLLKPNMVTVGTAAPASTRPEQVAMATLTALRRTVPPAVPGITFLSGGQSEEDASIHLNAINKLHLIKPWALTFSYGRALQASVLKAWGGKKENLKAAQDELMRRAKINGQASKGEYKPTGTGAAAGESLFVANHAY", "text": "SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family."}
{"protein": "MASLEDGTYRLRAVTTHNPDPGVGGEYATVEGARQPVKAEPNTPPFFERQYWQVTRNADGQYTIKYQGLNTPFEYGFSYDELEPNAPVIAGDPKEYILQLVPSTTDVYIIRAPIQRVGVDVEVGVQENTLVYKIFPVDGSGGDKAAWRFTRE", "text": "FUNCTION: Binds and inhibits cysteine proteinases. Inhibits most strongly papain and cathepsin L, more weakly bromelain and cathepsin B while it is completely ineffective against cathepsin H. SUBCELLULAR LOCATION: Note=Not secreted. SIMILARITY: Belongs to the protease inhibitor I48 family."}
{"protein": "MANEEQSNTYSTESHQKKSFFQSLFGRFFQGELKNREELVEVIRDSEQNELIDQNTREMIEGVMEIAELRVRDIMIPRSQIVFIHTDQNLDSCLDTIIVSAHSRFPVITDERDNIAGILHAKDLLRFLRSNAEEFDLMPLLRPAVIVPESKRVDRMLKDFRSERFHMAIVVDEFGAVSGLVTIEDILEQIVGDIEDEFDEEEIVNIRQLSRHTYAVRALTDIEDFNQQFNTHFADEEVDTIGGVVMQAFGYLPKRGEEITIENIGFKVTSADSRRLIQLRITVTDEQLAEIEKAEELKED", "text": "FUNCTION: Plays a role in the transport of magnesium and cobalt ions. SIMILARITY: Belongs to the UPF0053 family."}
{"protein": "MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRAAPCFCPGKPDRGDLWIFRGTCPGGYGYTSNCYKWPNICCYPH", "text": "FUNCTION: Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone type 3 (BDS) potassium channel toxin family."}
{"protein": "MKVTDVRMRKLVTDSRMKALASITLDEAFVIHDLRVIDGNNGLFVAMPSKRTSDGEFRDIAHPINSEMRQEIQEAVMKVYDETEAVEPGTIATSEVSSQLEESDSDKTLSEDLKA", "text": "FUNCTION: Could be involved in septation. SIMILARITY: Belongs to the SpoVG family."}
{"protein": "MGKTNKNRIKTGISYRSLHLLISANETVKEKREAEQLPALDNDTQCLMSTGKVHILNADYSRYGVSVYDKLYGYSSSAASTIEEEDKGSGDGFKKRYMSLMQGSSQWKSRKLKQKKNAPKASAKAKAFLVRLHSEKRRHEVDFADINCLPEEIICRIIANLNDADSQRNCLLVSQEWSECAKRIIYKDVKFTSTYRVGQFVTTLRENPQYGKYVESLDLSQLKNGFINDESSTLENDVSQSSYGFEPPDIAYAGWRDWRYRKNSLYGSEMLSSIHRSRTRRSSDASSMNSSVFSHNYNRTRSSSVTSLVSRSTQTAAGSKNVVKRIRKLFSNSFRGKGQQKTHLHQNNGSGLSTLELKDEQFAAGTDSCSLRRSHLPFTNKFFLKYAHLRDLPLGYIIHLLTLCVNLKSINLSNLSLSPDFEIEELEYKRNGYVSFFPEETEEENLNGLNTFNGDRELTPKFFSDSDKPYHYYKDTQYESIIWKLDSSRDNNMFTNRRRSRKKFQLKILTNDDLCEAILSLKHMKHLNVGNVVWLMQRDMKRLIVHSMESCIIEDRCLDKIYMNFEGSGLQTNLPLAGQGLLKAMVLLQVITDMTNNCSDDQILEWFELRWIPTFRRVSQPADLVYLARACDQLHYVIQSEESPTYTRVGEVLITESHTGHYKYEISRNVNNVYLTIQIENGKPDTITDVKLKECSDRLLERVSNLRKNQLLQHTGENFFSTAGLA", "text": "FUNCTION: F-box protein probably involved in ubiquitin conjugation pathway."}
{"protein": "MANLKEIRDRIKSVKNTRKITEAMRLVAAAKVRRAQEQVLRSRPFADRLARILENLQSRMGFEDAASPLMQQRNVETITLVAVTGDRGLCGGYNANIIKRTEQRFAELKGKGFDVKLLLIGTKAIGYFTRRDYPIQATFSGLEQVPTADEANTISTDLLAEFLAESTDRVELIFTKFINLVSCKPVVQTLLPLDPQDIADPEDEIFRLTTKDGLLTVEPGAGPANTEPKIPSDIVFEQTPEQLLNALLPLYLQNQLLRSLQESAASELASRMTAMNNASDNAKELAKTLTLDYNKARQAAITQEILEVAGGAAAVG", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family."}
{"protein": "MADLDDIKDGKDFGIGIPQQNPAFTLKGSGSLDWGMQSRLARIFNPKTNRTVMLAFDHGYFQGPTTGLERIDINIAPLFEYADVLMCTRGILRSVVPAAANRPVVLRASGANSILTYLSNEAVAVAMEDAVRLNACAVAAQVYIGTEHEHQSIKNIIQLIDQGMRYGMPTMAVTGVGKDMVRDQRYFSLASRIAAEMGAQVIKTYYVDSGFERIAAGCPVPIVIAGGKKLPERDALEMCYQAIDQGASGVDMGRNIFQSDAPIAMLKAVHAIVHKNENAAAAYQLFLHEQN", "text": "FUNCTION: Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5- phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DeoC/FbaB aldolase family."}
{"protein": "MAYQDFREFLAALEKEGQLLTVNEEVKPEPDLGASARAASNLGDKSPALLFNNIYGYHNARIAMNVIGSWPNHAMMLGMPKDTPVKEQFFEFAKRYDQFPMPVKREETAPFHENEITEDINLFDILPLFRINQGDGGYYLDKACVISRDLEDPDNFGKQNVGIYRMQVKGKDRLGIQPVPQHDIAIHLRQAEERGINLPVTIALGCEPVITTAASTPLLYDQSEYEMAGAIQGEPYRIVKSKLSDLDVPWGAEVVLEGEIIAGEREYEGPFGEFTGHYSGGRSMPIIKIKRVYHRNNPIFEHLYLGMPWTECDYMIGINTCVPLYQQLKEAYPNEIVAVNAMYTHGLIAIVSTKTRYGGFAKAVGMRALTTPHGLGYCKMVIVVDEDVDPFNLPQVMWALSTKMHPKHDAVIIPDLSVLPLDPGSNPSGITHKMILDATTPVAPETRGHYSQPLDSPLTTKEWEQKLMDLMNK", "text": "FUNCTION: Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions (PubMed:15979273, PubMed:18388975). Phenolic acid decarboxylase that catalyzes the reversible decarboxylation of 4- hydroxybenzoate and vanillate (PubMed:15979273, PubMed:18388975). Could also catalyze the decarboxylation of salicylate (Probable). Is not active on di- and tri-hydroxybenzoate derivatives (PubMed:18388975). SIMILARITY: Belongs to the UbiD family. YclC subfamily."}
{"protein": "MDLIVEDLAAIDNKLSQRHIDLDPNGYFIIYIDKTAGLIYAKHFTNIIDERGLAVDPETGKVIPARGKVERTYTTVFAGRTAKELCVKIFEETQPCPVTMLDHAAYLGREFVRAEVALVAGQEYVQD", "text": "SIMILARITY: Belongs to the ycf91 family."}
{"protein": "MQQDGTQQDRIKQSPAPLNGMSRRGFLGGAGTLALATASGLLLPGTAHAATTITTNQTGTDGMYYSFWTDGGGSVSMTLNGGGSYSTQWTNCGNFVAGKGWSTGGRRTVRYNGYFNPSGNGYGCLYGWTSNPLVEYYIVDNWGSYRPTGTYKGTVSSDGGTYDIYQTTRYNAPSVEGTKTFQQYWSVRQSKVTSGSGTITTGNHFDAWARAGMNMGQFRYYMIMATEGYQSSGSSNITVSG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MAFEKTRQFLPPLHFVLFPFMAQGHMIPMVDIARILAQRGVTITIVTTPHNAARFKDVLNRAIQSGLHIRVEHVKFPFQEAGLQEGQENVDFLDSMELMVHFFKAVNMLENPVMKLMEEMKPKPSCLISDFCLPYTSKIAKRFNIPKIVFHGVSCFCLLSMHILHRNHNILHALKSDKEYFLVPSFPDRVEFTKLQVTVKTNFSGDWKEIMDEQVDADDTSYGVIVNTFQDLESAYVKNYTEARAGKVWSIGPVSLCNKVGEDKAERGNKAAIDQDECIKWLDSKDVESVLYVCLGSICNLPLAQLRELGLGLEATKRPFIWVIRGGGKYHELAEWILESGFEERTKERSLLIKGWSPQMLILSHPAVGGFLTHCGWNSTLEGITSGVPLITWPLFGDQFCNQKLIVQVLKAGVSVGVEEVMKWGEEESIGVLVDKEGVKKAVDEIMGESDEAKERRKRVRELGELAHKAVEEGGSSHSNIIFLLQDIMQQVESKS", "text": "SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MAPKLDIILHPPENGEFYSSDDLISGTIVLDLTKSLSIKQIKVGLKGFTETTTKMDSEYVFPQNGMLGPATENKSYHNLVREERRVFPPDNVWDALEGSSKPFKVKPGHYEYMFQFNKLPSKPMCLKNHTKKTICFVSKSQSTMPPSFNTQWRELNKIDNLDLYFYSFGKIIYVVEVEIEMGRPRTWFKPFDKMLREPKIIEFIPEPKKFASNETVTRSGRNNHGVIDYISKNNSSKSLSAMQESEDGVTAIAPNGPDEKFLARNLDQLDINNDLEYEIEETEENPMKRYKCRYPLGLPDGASMMWVEVRSRDIDTIYRQDFLFRQGSGNFDNVYLIVKGNLSFSDFSNISVKPTRLQLNLLETVSYLSQGIGNENFSSLKLMEIDNLSKSDRPLFDTNELKFISSKNHEIMECEIKLKDNPILKRLQFNEEDYKHRGNRLYSFKTCVITRLFSYQLLIDWNINGQTRQTETIIPVQVFAHKRPPPVNEALPRYVEPPSYDDHV", "text": "FUNCTION: May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ART10 family."}
{"protein": "MLRAVSTSFGTARAASAVAKKNMPNIVLVDAVRTPFVVSGTVFKDLMAVDLQKEAIKALVEKTKLPYEQLDHIICGTVIQECKTSNIAREAALLAGVPDKIPAHTVTLACISSNVAMTTGMGMLATGNANAIIAGGVELLSDVPIRYNRNARKAMLGMNKAKDVPSKLKIGGQIVKNLLSPELPAVAEFSTGETMGHSGDRLAAAFNVSRREQDEFAIRSHTLASEAAKNGKFTDVVPVFLDGKKPKTIKEDNGIRVSTLEKLSSLKPAFVKPHGTVTAANASYLTDGASAALIMTEEYALANGYKPKAYLRDYLYVAQDPKDQLLLSPAYVIPKLLDKAGLTLKDVDVFEIHEAFAGQVLANLNAMDSDYFCKEQMKRSGKFGRVPMDKLNLWGGSLSIGHPFGATGVRLATHSAHRLKEEKGQYAVIAACAAGGHGVGMLIEAYGK", "text": "FUNCTION: Mitochondrial enzyme that catalyzes reactions of the mitochondrial beta-oxidation pathway. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MKVIISGGGTAGHINPGLAIAKYIKKREPDTEILFIGTERGLEARLVPRENFEIKMIKVRGFKRKLSMDTLVAVKELFQGLAEARKIIKDYKPDLVIGTGGYVCGPVLFNASRMKIPTLVHEQNAFPGVTNKILSKFVDRVAISFKEAEKYFKDKSKVVFTGNPIRSEMLEVSRETARKKLGIPKDMPLVVIFGGSRGAENINSTVAELIKRHKSDLGFYLIYATGEAQYDGIMKKIGEVKSPNINILPYIFDMANAMAAADLVVCRAGAITVSELTALGVPSILIPSPYVTANHQEHNARALERQGASVVILEKNLRPDILYEEITTLLKDRNKLSQMAKNAKSIGITNATERIYEIIKDIMKNKAAG", "text": "FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG subfamily."}
{"protein": "MEVAQPKDLKEDFVLAKRRHAELVRQKRIFNARNRIIGGDTTAWDAQVCDQNIKAATEKARDEAFAAEMRQNDKIACLSENRERRDRKNLCKAINDFQQSFQRPETRREFDLSDPLALKKDRPARQSDYDARNTISGMQKFMGEDLNFHLRKKFQEEQNREWSLQQQKEQMIGRENQKCAEDLYLKTRLQFDETAKHLQNLETATRKAVCATVKEFNKNQALESAEKKIQERKQEQEDNLAEISNMLRGDLLSENPQQAASSFGPHRVVPDRWKGMSQEQLEEIRLVQRQQVQEKLRLQEEERQRDMDWDRRRIQKARATLLFEQQQQRLQRGLRRALDCSNLSLAREQLLQKKHMKELCTNHATEDYFTQFNTGSR", "text": "FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the RIB43A family."}
{"protein": "MAKPIPKVGSRRNGRSSARKSARRIPKGVIHVQASFNNTIVTVTDVRGRVISWSSAGTCGFKGTRRGTPFAAQTAAGNAIRAVVDQGMQRAEVMIKGPGLGRDAALRAIRRSGILLSFVRDVTPMPHNGCRPPKKRRV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSGKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLNDSEKQPYITKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEDEEEEEEEEEEEEEEDE", "text": "FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (By similarity). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm. SIMILARITY: Belongs to the HMGB family."}
{"protein": "VIGGDECNINEHRFLVALYTSRTLFCGGTLINQEWVLTAAHCNMEDIQIKLGMHSKKVPNEDEQKRVPKEKFFCLSSKKLYLWDKDIMLIRLDSPVKNSAHIAPLSLPSSPPSVGSVCRTMGWGRISSTKETYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCVGDSGGPLICNGQFQGIASWGDHPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP", "text": "FUNCTION: Snake venom serine protease that may act in the hemostasis system of the prey. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MKNFMDKNFLLQTETAQELYHNHAAKMPIIDYHCHLNPQMVADDYRFKSLTEIWLGGDHYKWRAMRSNGVDECFCTGKETSDWEKFEKWAETVPYTFRNPLYHWTHLELKTAFGIDKVLNPKTAREIYDECNEKLSSQEYSARGMMRRYHVETVCTTDDPIDSLEYHIRTRESGFEIKMLPTWRPDKVMAVEVPSDFRTYIEKLSEISEITISDYNDMILALRKRHDYFAEQGCKLSDHGIEEFYAEDYTEGEIKTIFNKIYGGSELTKEEVLKFKSAMLIVLGEMDWEKGWTQQFHYGAIRNNNSRMFKQLGPDTGFDSIGEFATAKAMSKFLDRLNSKGKLTKTILYNLNPCANEVIATMIGNFQDGSIPGKIQFGSGWWFLDQKDGMERQLNALSLLGLLSRFVGMLTDSRSFLSYPRHEYFRRTLCNLLGCDVENGEIPLSEMERVCQMVEDISYFNAKNFFHF", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family."}
{"protein": "MPQPSVSGMDPPFGDAFRSHTFSEQTLMSTDLLANSSDPDFMYELDREMNYQQNPRDNFLSLEDCKDIENLETFTDVLDNEDALTSNWEQWDTYCEDLTKYTKLTSCDIWGTKEVDYLGLDDFSSPYQDEEVISKTPTLAQLNSEDSQSVSDSLYYPDSLFSVKQNPLPPSSFPSKKITNRAAAPVCSSKTLQAEVPSSDCVQKASKPTSSTQIMVKTNMYHNEKVNFHVECKDYVKKAKVKINPVQQGRPLLSQVHIDAAKENTCYCGAVAKRQERRGVEPHQGRGTPALPFKETQELLLSPLTQDSPGLVATAESGSLSASTSVSDSSQKKEEHNYSLFVSDNMREQPTKYSPEDDEDDEDEFDDEDHDEGFGSEHELSENEEEEEEEEDYEDDRDDDISDTFSEPGYENDSVEDLKEMTSISSRKRGKRRYFWEYSEQLTPSQQERILRPSEWNRDTLPSNMYQKNGLHHGKYAVKKSRRTDVEDLTPNPKKLLQIGNELRKLNKVISDLTPVSELPLTARPRSRKEKNKLASRACRLKKKAQYEANKVKLWGLNTEYDNLLFVINSIKQDIVNRVQNPREEREPSMGQKLEILIKDTLGLPVAGQTSEFVNQVLGKTAEGNPTGGLVGLRIPASKV", "text": "FUNCTION: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with CREB3 in nuclear foci. SIMILARITY: Belongs to the bZIP family. CREBRF subfamily."}
{"protein": "TIIGAPCRKCEHLDRSGNCVRDWSCGQEV", "text": "SUBCELLULAR LOCATION: Secreted Nematocyst."}
{"protein": "MTSNRSTRSSTKREEVSKNGVEKRELDESDVMKNGKKPVKRAKVSSLPKPVRVPGSAKRINKIPELPTERLNVYVFGSGSMNELGMGEEEMDVVYRPRLNPILSTDKVGVVDLAVGGMHSAALSHDGRVYTWGVNDDYALGRLTKDQKDENGDKVDNDLLEGTPSKVEGALSHLRVTKVICSDNLTAAITDNGCCFTWGTFRCSDGVLGYSDSQKRTAEPTQMRLPEICQLATGTDHIIALTTTGKVYTWGNGQQFQLGRRMLERRRLQGLTPQPLALKNIISVGAGSYHSFAIDNKGRVYAWGLNITRQCGIEVEDEEEGAVITKPTLVDALEGYNVKSITGGEHHTLALLEDGRVLAWGRDDRHQLGIPDNALPETVVKDEKGNNYYLSTPTIIPGLTNVIQVVCGTHHNLAVTSDGKVYSWGSAENYEVGQGDNDEDVAVPTLVRSKAIKEVAIRVAGAGGQFSIIAGIPNASEEPVANGIKSEPENEKKLKTEETSKTDDSPVTDAKPDVTSNGEPSTATSESKDSVLEPSSTTA", "text": "FUNCTION: Promotes the exchange of Ran(spi1)-bound GDP by GTP. Involved in the control of mitosis. Regulates a variety of nuclear events, including mitotic check-point, chromosome decondensation and mRNA processing/transport. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAGVAQNGHQEMDFCMKVDPLNWEMAADSLKGSHLDEVKKMVAEFRKPVVKLGGETLTVAQVAAIAAKDNVKTVKVELSEGARAGVKASSDWVMDSMGKGTDSYGVTTGFGATSHRRTKNGGALQKELIRFLNAGVFGNGTESCHTLPQSGTRAAMLVRINTLLQGYSGIRFEILEAITKLLNHNVTPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPNGETLNAEEAFRVAGVNGGFFELQPKEGLALVNGTAVGSGLASMVLFDANVLAVFSEVLSAIFAEVMNGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYVKAAQKLHETDPLQKPKQDRYALRTSPQWLGPQIEVIRSATKMIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNARLALASIGKLMFGQFSELVNDYYNNGLPSNLTAGRNPSLDYGFKGSEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLDLISARKTAEAVDILKLMSSTYLVALCQAIDLRHLEENLRNAVKNTVSQVAKRTLTMGTNGELHPSRFCEKDLLRVVDREYVFAYADDACSANYPLMQKLRQVLVDHALQNGENEKNANSSIFQKILAFEDELKAVLPKEVESARAALESGNPAIANRIKECRSYPLYRFVRGELGAELLTGEKVRSPGEECDKVFTAMCNGQIIDSLLECLKEWNGAPLPIC", "text": "FUNCTION: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAL/histidase family."}
{"protein": "MDVRRRLPPKLRRPLPITESSHHHRKTPFPADVDRSPSPTPKASDALPLPLYLTNGIFFTLFFSVAYYLLHRWRDKIRSSTPLHIVTLSELAAIVSLIASFIYLLGFFGIDFVQSFVSRADVDVDIDVEPDILEADRRPCSKLMDQPPPPPVVMSSEEDEEIVKSVVSGKTPSYSLESKLGDCYRAASIRREAVQRTTGRSLLGLPLDGFDYESILGQCCEMPIGYVQIPVGIAGPLLLNGCEYVVPMATTEGCLVASTNRGCKAIYACGGATGILLKDGMTRAPVVRFSTAKRASDLKFFLEDPLNFDTLAVVFNKSSRFARLQSIQCSMAGKNLYIRFCCSTGDAMGMNMVSKGVQNVLEFLQSDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITDDVVKKVLKTTVPALVELNMLKNLAGSAVAGALGGFNAHAANIVSAVFIATGQDPAQNIESSHCITMMEAINNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGANKESHGSNSRLLATIVAGSVLAGELSLMSAIAAGQLVRSHMKYNRSSRDMSKIGS", "text": "FUNCTION: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:24569845, PubMed:29378087). Promotes triterpenes accumulation in roots (PubMed:24569845). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Plastid, chloroplast membrane; Multi-pass membrane protein Peroxisome membrane; Multi-pass membrane protein Note=Localized in intracellular vesicles. SIMILARITY: Belongs to the HMG-CoA reductase family."}
{"protein": "MTEMKILIVTLTYIEKSIIDEIVNNLSSYGLEVDILFDSRKYLPISAFNWERLQYDAEKVLSFLKSKYDFNYDSIIFLADSDGYIDGYNFVFGLTIDNFAIIFLNRLREEFYNRKPDLELFMKRVVKEVTHEAGHTLGLGHCNTIGCVMNFSNTVEDVDKKQARFCKNCIYKIENLSKYLQRK", "text": "FUNCTION: Probable zinc metalloprotease whose natural substrate is unknown. SIMILARITY: Belongs to the peptidase M54 family."}
{"protein": "MKNKKRLCHILKYIITCFLFGVIFIIPIQAQIVLQTDFTDSENARQNIDYHFNVFNRITPLNGVKIKTPLGKPRVCIVRPLGGIVKNGKPDISKDSYKWDKKSKTFYTDFTVLKNQIDGVINSGYAIHQIVLDNPSWAFQRNKNGELVADSLKVSTYGNAEPPKDYNAWSNYLKDVLKFLVNTYGEESMLKIQFNIGREIGTPSHWSGSKEAFFEFYKISSSAIREVLPTAKVGTHFLWGSSKNAWGTDFIKWSKANNVHYDFIGVSFYPFYNKPDRTLFKEVYAKDFAVIKDIPEWHKNAKLEMHEYALIKSLNKAGNAFENAPKAQQNSFIVGLMKMFYEHNMQNVFQWGQGTNFEAAQEALFSIQGQTYYTSTKNGKPLLETNDVDAIFIKDVSNNIYNIMAYNYNANPNATTDEHLNLKAKLDVPPGTKVKVRFALYNKEKDTMSWSEWKEEATQGNEKSKSVISLNAELPVFSFLKYEVKVQ", "text": "FUNCTION: Alpha-rhamnosidase involved in ulvan degradation (PubMed:31285597). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D- glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). Endo-acting alpha-1,4-L-rhamnosidase cleaves rhamnose sections interspersed between xylose residues within the polymer, degrading larger oligomers with consecutive Xyl-Rha3S units that are resistant to the ulvan lyases and producing dimers Xyl-Rha3S and Xyl2S- Rha3S as the smallest products (PubMed:31285597). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the glycosyl hydrolase 39 family."}
{"protein": "MGFHQIDERNQALLSKIALDDGHGENSPYFDGWKAYDNDPFHPENNPLGVIQMGLAENQLSFDMIVDWIRKHPEASICTPEGLERFKSIANFQDYHGLPEFRNAIANFMGKVRGGRVKFDPSRIVMGGGATGASETVIFCLADPGDAFLVPSPYYAGFDRDLKWRTRAQIIRVHCNGSNNFQVTKAALEIAYKKAQEANMKVKGVIITNPSNPLGTTYDRDTLKTLVTFVNQHDIHLICDEIYSATVFKAPTFTSIAEIVEQMEHCKKELIHILYSLSKDMGLPGFRVGIIYSYNDVVVRRARQMSSFGLVSSQTQHLLAAMLSDEDFVDKFLAENSKRVGERHARFTKELDKMGITCLNSNAGVFVWMDLRRLLKDQTFKAEMELWRVIINEVKLNVSPGSSFHVTEPGWFRVCFANMDDNTVDVALNRIHSFVENIDKKEDNTVAMPSKTRHRDNKLRLSFSFSGRRYDEGNVLNSPHTMSPHSPLVIAKN", "text": "FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MLRHLPSRLPVKMWGRTLEKQSWRDSSQTPPPCLIRRLDHIVMTVKSIKDTTMFYSKILGMEVMTFKEDRKALCFGDQKFNLHEVGKEFEPKAAHPVPGSLDICLITEVPLEEMIQHLKACDVPIEEGPVPRTGAKGPIMSIYFRDPDRNLIEVSNYISS", "text": "SIMILARITY: Belongs to the glyoxalase I family."}
{"protein": "MSRSESPRPLLEMRGISKTFPAVRALDNVSLTVYPGEIHSLMGENGAGKSTLMKILSGAYRADAGGEILIDGQRIEIDGPLAARDAGVAVIYQELCLSPNLTVAENIYVGRELRRGNRRWGTIDRAAMARGCQDVLARLGAPFGPDTLVDTLSIAEQQLVEIARAVHTRARILVMDEPTTPLSSRETEHLFRLIRQLREEGLAIIYISHRMAEIYELSDRVSVLRDGAYVGTLERASLSAERLVAMMVGRDISGFYKKEHAPYDPGHLLLSVRDIADGTRVRGCSLDLHAGEVLGIAGLVGAGRTELARLIFGAEPRVRGDVKLGERTFGAHSPRDAIDAGLVYLTEDRKRQGLFLDMSVRDNINISVCNRDARLGALDLARGAERARDAIASLSIRVPHANVNVGALSGGNQQKVLLSRLLETKPRVLILDEPTRGVDIGAKSEIYRIINELARAGVGVIVISSELPEIIGVADRVLVMREGEIAGELGGHTHTPITQEAIIALATGSQAELADAH", "text": "FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Ribose importer (TC 3.A.1.2.1) family."}
{"protein": "MNSFSAFSEMFGSDYESSVSSGGDYIPTLASSCPKKPAGRKKFRETRHPIYRGVRRRNSGKWVCEVREPNKKTRIWLGTFQTAEMAARAHDVAALALRGRSACLNFADSAWRLRIPESTCAKDIQKAAAEAALAFQDEMCDATTDHGFDMEETLVEAIYTAEQSENAFYMHDEAMFEMPSLLANMAEGMLLPLPSVQWNHNHEVDGDDDDVSLWSY", "text": "FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
{"protein": "MSTSVAERLAIKDEVDKKIELRPNWSEDELQIVFKTAYEQVFGRQGLYASQRFATAEALLRNGKISVKQFIELLAKSEFYKECFFYNNSQVRFIELNYKHLLGRAPYDQSEIAFHVDLYAAAGYDAEIESYIYSPEYDNAFGNFVVPYYRGFQSIPGMKTVGFNRIFELYRGRANSDNAQFGGKSARLRSKISMNLANTIVPPTSPIAASTSSARTLVTSPVMGDARMFIVEAIAGTLNTNVAVRRSRQVYTVPYDRLSATYQEIHKRGGKIVKITPAS", "text": "FUNCTION: Rod linker protein, associated with phycoerythrocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=This protein occurs in the rod, it is associated with phycoerythrocyanin. SIMILARITY: Belongs to the phycobilisome linker protein family."}
{"protein": "MATSQQFLNPTLFKSLASSNKNSCTLCPSPFLQLKSASTIFNYKPLTSSSATIITRVAASSSDSGESITRETFHGLCFVLKDNIDTDQIIPAEYGTLIPSIPEDREKLGSFALNGLPKFYNERFVVPGEMKSKYSVIIGGDNFGCGSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATGEIFPLESEVRICDECKTGDVVTIEHKEDGSSLLINHTTRKEYKLKPLGDAGPVIDAGGIFAYARKAGMIPSA", "text": "FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate (Probable). Functions redundantly with LEUD1 in the methionine chain elongation pathway of aliphatic glucosinolate formation. SUBCELLULAR LOCATION: Plastid, chloroplast stroma Plastid. SIMILARITY: Belongs to the LeuD family."}
{"protein": "MVVKVGINGFGRIGRIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGDIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTTEKAKAHLKGGAKKVVISAPSPDAPMFVMGVNHETYKPDIEALSNASCTTNCLAPLAKVIHDKYTIIEGLMTTIHSYTATQKVVDGPSAKDWRGGRTAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAMRVPTANVSVVDLTVRIEKGASYDEIKQAVKEASEGSLNGILGYTEDDIVSTDLNGDNRSSIFDAKAGISLNKNFVKLVSWYDNEWGYSRRVLDLLVYIAKIDGNA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MAFLHNGNHTAVTEFILLGLTDDPVLRIVLFTIILCIYLVTVSGNLSTILLIRVSSQLHHPMYFFLSHLASADIGYSSSVTPNMLVNFLVKQNTISYIGCSIQFGSAAFFGGLECFLLAVMAYDRFVAICNPLLYSTKMSTQVCVQLVVGSYIGGFLNASFATVSFLFLFFCGPNIINHFFCDFAPLIELSCSDVRISVLVTSFSAGTVTMLTVLVIAISYTYILITILKMRSTEGRHKAFSTCTSHLTAVSLFYGTITFIYVMPKSRYSTDQNKVVSVFYMVVIPMLNPLIYSLRNNEIKGALRRHLGKKIFSQSNILFY", "text": "FUNCTION: Potential odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "DDCLGIFKSCNPDNDKCCESYKCSRRDKWCKYVL", "text": "FUNCTION: Voltage-gated sodium channel Nav1.7/SCN9A inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 14 (Hntx-1) subfamily."}
{"protein": "MAASLWMGDLEPYMDENFISRAFATMGETVMSVKIIRNRLTGIPAGYCFVEFADLATAEKCLHKINGKPLPGATPAKRFKLNYATYGKQPDNSPEYSLFVGDLTPDVDDGMLYEFFVKVYPSCRGGKVVLDQTGVSKGYGFVKFTDELEQKRALTECQGAVGLGCKPVRLSVAIPKASRVKPVEYSQMYSYSYNQYYQQYQNYYAQWGYDQNTGSYSYSYPQYGYTQSTMQTYEEVGDDALEDPAPQLDVTEANKEFMEQSEELYDALMDCHWQPLDTVSSEIPAMM", "text": "FUNCTION: Involved in the early steps of selenocysteine biosynthesis and tRNA(Sec) charging to the later steps resulting in the cotranslational incorporation of selenocysteine into selenoproteins. Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins synthesis (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Abundant in the nucleus. SIMILARITY: Belongs to the RRM TRSPAP family."}
{"protein": "MKVSVIIPTYNERENLEELFSRIDNALQGLNYEIVVVDDDSPDRTWEKAQELSSKYPVKVIRRTKEKGLSSAVIRGFKEASGDVFVVMDADLQHPPEVIPKLIEAIKNGSDIAIGSRYVKGGKVENWPFYRKLISKGAIMVGRIALPKIRDIKDPVSGFFALRKEVVEGVELNPIGFKILMEILIKGKYSKVVEVPFTFGIRARGESKLKGKTIFEYLRHIYRLMKWEGEIDRIVKFSIVGLSGILVNEGFLWLFVNLGIPKEIAVIPAVELSILNNFFWNDIWTFKDIRRGSIFSRLLKFHIAALSGAVVNFIVYWILLFLGIHYLIANLVGIVLSFGVRYVINRHVTWAT", "text": "FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MKHSFSRLFGLGDKEEEAEIAEHDTNKEEIQEIPVGDIIPNRFQPRTIFSEEKIKELAATIHTHGIIQPIVVRKTEREGQYELIAGERRWRAVQTLDWEKVPAIIKDFSDTETASVALIENLQREELSSIEEAHAYARLLELHDLTQEALAQRLGKGQSTIANKLRLLKLPEEVQEAILKKEISERHARALIPLKQPDLQVKLLHEVIEKSLNVKQTEDRVVKMLEQDKRKPKPKRKAYSRDARIAMNTIRQSLSMVEDSGVKLNTEEEEFEEYIQFTIRIPK", "text": "FUNCTION: Effects nucleoid occlusion by binding relatively nonspecifically to DNA and preventing the assembly of the division machinery in the vicinity of the nucleoid, especially under conditions that disturb the cell cycle. It helps to coordinate cell division and chromosome segregation by preventing the formation of the Z ring through the nucleoid, which would cause chromosome breakage. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the ParB family."}
{"protein": "MMKREQRRSVGLRLRAGIRCHNRFYAVLKRDISSTSASGVYTDRLECLLGGSVSAESLKKAKGVYLACEVNLGRRRPDCVCTIQ", "text": "SIMILARITY: Belongs to the herpesviridae UL24 family."}
{"protein": "MTTPAQDAPLVFPSVAFRPVRLFFINVGLAAVAMLVAGVFGHLTVGMFLGLGLLLGLLNALLVRRSAESITAKEHPLKRSMALNSASRLAIITILGLIIAYIFRPAGLGVVFGLAFFQVLLVATTALPVLKKLRTATEEPVATYSSNGQTGGSEGRSASDD", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.leprae ML1138."}
{"protein": "MAHPPRLNDDKPVIWTVSVTRLFELFRDISLEFDHLANITPIQLGFEKAVTYIRKKLANERCDAIIAAGSNGAYLKSRLSVPVILIKPSGYDVLQALAKAGKLTSSIGVVTYQETIPALVAFQKTFNLRLDQRSYITEEDARGQINELKANGTEAVVGAGLITDLAEEAGMTGIFIYSAATVRQAFSDALDMTRMSLRHNTHDATRNALRTRYVLGDMLGQSPQMEQVRQTILLYARSSAAVLIEGETGTGKELAAQAIHREYFARHDARQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCNLEEDMQQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKVSLAALSAPFSAALRQGLQASETVLLHYDWPGNIRELRNMMERLALFLSVEPTPDLTPQFMQLLLPELARESAKTPAPRLLTPQQALEKFNGDKTAAANYLGISRTTFWRRLKS", "text": "FUNCTION: Involved in the transcriptional regulation of the propionate catabolism operon."}
{"protein": "MIYRKWSLLSSTILIWGGAATAGLAGVFLFNAKEKFQKYLSGEGQRLRQQDRAAMGKN", "text": "SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein."}
{"protein": "MASQSKTSVHDFTVKDAKGQDVDLSIYKGKLLLIVNVASQCGLTNSNYTELSQLYDKYKNQGLEILAFPCNQFGAQEPGDNEQIQEFACTRFKAEFPIFDKVDVNGDNAAPLYKHLKSSKGGLFGDSIKWNFSKFLVDKEGNVVERYAPTTSPLSIEKDIKKLLETA", "text": "FUNCTION: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutathione peroxidase family."}
{"protein": "MKIAVYGKGGIGKSTTSCNISVALARRGQKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRITASIREKARTHPLRLAGLVGNRTSRRDLINKYVEACPMPVIEVLPIIEDIRVSRVKGKTLFEMVGFEPSLNYVCNYYLGIADQILSQPEGIVPKEIPDRELFSLLSDLYLNPIGGGGQKKNNKENLLGFTRI", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the NifH/BchL/ChlL family."}
{"protein": "MIVLTRRIDESDTITGTVTLDVDSRIKSRLRVTLDDGREAGLMLERGHLLRGGELLADAAGSQVVRVLAAPEAVSTVRCSDPHLLARAAYHLGNRHVPLQIQPGLLRYQHDHVLDDMLRGLGLAVEAEQAPFEPEAGAYQSAPHSHSHAHDHPFVRLPAHS", "text": "FUNCTION: Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UreE family."}
{"protein": "MAEKEAKHHVVLFPLPGQGHIGSMLKLAQLLSTAGFYITFVHTERNYRRFLLTSTSFNVPKFRFRTIPDGFPDNDPRSPLPFIELQESLDTKCKGYYREVLVAVDEEWPPVTCVVADTALPLALEVPEELGIPVMILAPHSAGSILTGYSIPQLIQGGEFPFPEDADMDELLQGVLGLEGIVRRRDMSVRGFKSIDSPFVRFEVKMNQNLSRGRALILNTTESMDSLALRHIRSICPTTYTLGPFHVLLRNIKDQSHSASLSEEDRSCIAWLDTKPNKSVVYVSFGSLAAMSREAFLEFQQGLLDSGYHFLWVIRPDMVEGGLEECELTASERRYFVKWAPQEEVLAHPAVGCFLTHSGWNSTLESIYAGVPMICWPFFADQLINSRFVSEVWKIALDMKDLCGRSYVERMVKEVMSGEKGKELRKSICEMADMVKKSAEEGGSSYTNFKELIGHIKSLSLPACSSTSGF", "text": "FUNCTION: Glucosyltransferase involved in montbretin A (MbA) biosynthesis (PubMed:29967287, PubMed:31004005). Catalyzes the glucosylation of myricetin 3-O-alpha-L-rhamnoside (MR) to produce myricetin 3-O-[beta-D-glucosyl-(1->2)-alpha-L-rhamnoside] (MRG), a precursor of MbA (PubMed:29967287, PubMed:31004005). MbA is a potent inhibitor of human pancreatic alpha-amylase and is being developed as drug candidate to treat type-2 diabetes (PubMed:29967287, PubMed:31004005). In vitro, is able to transfer UDP-xylose with 50-fold less efficiency compared with UDP-glucose (PubMed:29967287). In vitro, can use myricetin 3-O-glucoside and quercetin 3-O-glucoside as substrates, although these two flavonoids may not be physiological substrates in vivo (PubMed:29967287). SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MGKMAAAVASLATLAAEPREDAFRKLFRFYRQSRPGTADLGAVIDFSEAHLARSPKPGVPQVVRFPLNVSSVTERDAERVGLEPVSKWRAYGLEGYPGFIFIPNPFLPGCQRHWVKQCLKLYSQKPNVCNLDKHMTKEETQGLWEQSKEVLRSKEVTKRRPRSLLERLRWVTLGYHYNWDSKKYSADHYTPFPSDLAFLSEQVATACGFQGFQAEAGILNYYRLDSTLGIHVDRSELDHSKPLLSFSFGQSAIFLLGGLKRDEAPTAMFMHSGDIMVMSGFSRLLNHAVPRVLPHPDGECLPHCLETPLPAVLPSNSLVEPCSVEDWQVCATYLRTARVNMTVRQVLATGQDFPLEPVEETKRDIAADGLCHLHDPNSPVKRKRLNPNS", "text": "FUNCTION: Dioxygenase that acts as on nucleic acids, such as DNA and tRNA (PubMed:27027282, PubMed:27745969). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:27027282). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment (By similarity). Mainly acts as a tRNA demethylase by removing N(1)- methyladenine from various tRNAs, with a preference for N(1)- methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs (PubMed:27745969). Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N(1)-methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation (By similarity). In mitochondrion, specifically interacts with mt- tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c) at this position (By similarity). mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation (By similarity). Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:27027282). N(6)- methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (PubMed:27027282). Demethylates mRNAs containing N(3)-methylcytidine modification (By similarity). Also able to repair alkylated single-stranded DNA by oxidative demethylation, but with low activity (By similarity). Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites (By similarity). DNA lyase activity does not require alpha-ketboglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product (By similarity). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation (PubMed:23825659). May play a role in placental trophoblast lineage differentiation (PubMed:18163532). SUBCELLULAR LOCATION: Nucleus Note=Mainly localizes in euchromatin, largely excluded from heterochromatin and nucleoli."}
{"protein": "MQFDYIIIGAGSAGNVLATRLTEDPNTTVLLLEAGGPDYRFDFRTQMPAALAFPLQGKRYNWAYETEPEPFMNNRRMECGRGKGLGGSSLINGMCYIRGNALDLDNWAQEPSLENWSYLDCLPYYRKAETRDVGENDYHGGDGPVSVTTSKPGVNPLFEAMIEAGMQAGYPRTDDLNGYQQEGFGPMDRTVTPHGRRASTARGYLDQAKSRPNLTIRTHAMTDHIIFDGKRAVGVEWLEGDSTIPTRAAANKEVLLCAGAIASPQILQRSGVGNAELLAEFDIPLVHELPGVGENLQDHLEMYLQYECKEPVSLYPALQWWNQPRIGAEWLFGGTGVGASNHFEAGGFIRSREEFAWPNIQYHFLPVAINYNGSNAVKEHGFQCHVGSMRSPSRGHVRIKSRDPHQHPGILFNYMSHEQDWQEFRDAIRITREIMHQPALDQYRGREISPGVECQTDEQLDEFVRNHAETAFHPCGTCKMGYDEMAVVDGEGRVHGLEGLRVVDASIMPQIITGNLNATTIMIGEKIADMIRGKEALPRSTAGYFVANGMPVRAKK", "text": "FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MGFGKPSSFLAFSILVLCQAGSLQAQPLRSSLESLPDPAALSEKEGRLLLAALVKAYVQRKTNELEQEQEQEMEGSSLTAQKRSCNTATCVTHRLAGLLSRSGGVVKSNFVPTDVGSEAFGRRRRDLQA", "text": "FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calcitonin family."}
{"protein": "MFRPPSIKDAKKIWELIGRCKPLDINSPYCYALIGRDFFDSSIVYEEEGRIKGVVIGYLRPRAPERLFVWQVAIEAKSRGKGIAKRAIEAILKNLERKGHCIQAIEATYTPSNLASKALFHALGREWKVVWIEENFLEGALLSAQEAHEEEWLITLPFSSEALGVQGANHANL", "text": "FUNCTION: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A. SIMILARITY: Belongs to the acetyltransferase family. EctA subfamily."}
{"protein": "MPRSQRNDNFIDKTFTVVADILVKVLPTSNREKQAFTYYRDGMAAQAEGEYAEALQNYYQALRLEIDPYDRSYILYNIGLIYTCNGEHGRALEYYYQALERNPSLPQALNNIAVIYHYRGEQAIERGQSEISKLLFDKAADYWKEAIRLAPTNYLEAQSWLNQYTN", "text": "FUNCTION: Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the Ycf3 family."}
{"protein": "MAKNTSCGVQLRIRGKVQGVGFRPFVWQLAQQLNLHGDVCNDGDGVEVRLREDPETFLVQLYQHCPPLARIDSVEREPFIWSQLPTEFTIRQSTGGTMNTQIVPDAATCPACLAEMNTPGERRYRYPFINCTHCGPRFTIIRAMPYDRPFTVMAAFPLCPACDKEYRDPLDRRFHAQPVACPECGPHLEWVSHGEHAEQEAALQAAIAQLKMGKIVAIKGIGGFHLACDARNSNAVATLRARKHRPAKPLAVMLPVADGLPDAARQLLTTPAAPIVLVDKKYVPELCDDIAPDLNEVGVMLPANPLQHLLLQELQCPLVMTSGNLSGKPPAISNEQALADLQGIADGFLIHNRDIVQRMDDSVVRESGEMLRRSRGYVPDALALPPGFKNVPPVLCLGADLKNTFCLVRGEQAVLSQHLGDLSDDGIQMQWREALRLMQNIYDFTPQYVVHDAHPGYVSSQWAREMNLPTQTVLHHHAHAAACLAEHQWPLDGGDVIALTLDGIGMGENGALWGGECLRVNYRECEHLGGLPAVALPGGDLAAKQPWRNLLAQCLRFVPEWQNYSETASVQQQNWSVLARAIERGINAPLASSCGRFFDAVAAALGCAPATLSYEGEAACALEALAASCHGVTHPVTMPRVDNQLDLATFWQQWLNWQAPVNQRAWAFHDALAQGFAALMREQATMRGITTLVFSGGVIHNRLLRARLAHYLADFTLLFPQSLPAGDGGLSLGQGVIAAARWLAGEVQNG", "text": "FUNCTION: Involved in the maturation of [NiFe] hydrogenases (PubMed:8661925, PubMed:12377778, PubMed:12586941). Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases (PubMed:12586941). HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide (PubMed:12586941, PubMed:15291820). In the absence of any other substrate, displays carbamoyl-phosphate phosphatase activity (PubMed:12377778). SIMILARITY: Belongs to the carbamoyltransferase HypF family."}
{"protein": "MASARTLVLLLIGAVLMCQVSADSELLNEILAAHMEEDMPEKRCIDRYRSNICGSVIRPLDCTRRKSRMGRFARTNCKKLCGFC", "text": "SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone 8 toxin family."}
{"protein": "MEIINGPVLPRYAAPATGALTSDAKISGQLLRRVHLRRRACGLQGDHYRAARRFFGFPSERHARSGWVWPVYCSYGSSSDGDGAAAADYDASGEEFVNSSVMEAVELRSVSDGFVIKMRDGKNLRCVQNNPRVLRLRDSAPHHAIVLKMEDGSDLLLPIIVMETPSIMLLAALRNIRIPRPTIYNVVKEMTERMGYAVRLVRITEMVHDAYYSRLYLAKIGNEEETISLDLKPSDAINIAFRCKVPIQVNRRIAYNNGLKVVQPTPSESYVSSDQFQYTRLDRPDDQPCFEAQEFDLVRNMLVAAVEERYKDAAQYRDQLFMFRAKKKNMI", "text": "FUNCTION: Bifunctional nuclease with both RNase and DNase activities. Involved in basal defense response. Participates in abscisic acid- derived callose deposition following infection by a necrotrophic pathogen. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bifunctional nuclease family."}
{"protein": "MSKRKSKDLCLPVGECISKVHGILRQRLFQHHGKPFGVDSQHKHLVELLKRTVIHGESNSALIIGPRGSGKSMLLKGALEDIFGMKQMKETALQVNLNGLLQTTDKIALKEITRQLHLENVVGDRVFGSFAENLSFLLEALKTGDRKSSCPVLFVLDEFDLFAHHKNQTLLYNLFDIAQSAQTPVAVIGLTCRLDVMELLEKRVKSRFSHRQIHLLNSFSFSQYLQIFQEKLSLPASFPDSQFAEKWNESIKSLVESKLVEDVLQKQYNASKDVRSLHMLMLLAVCRVNVSHPHITAADFLEVFRLRNQDSKANILHGVSVLELCLIIAMKHLQDIYDGEPFNFQMVHNEFQKFIQRKAHSVYNFEKAVVIKAFEHLHQLELIKPMEGLSVRTQKEYRLMKLLLDNTQIVEALQKYPNCPTDVKQWAMSSLS", "text": "FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC4 family."}
{"protein": "MKERFIKKTHYLDYQFDEPTDIKLGFTTRENGLSPYPNHSFNMARYISDSAHHITHHQDILANLIGYPRDEWVFPIQTHDSRIVEVTSEHKGTNIDELTDDLHGIDGMYTFDSHILLTMCYADCVPVYFYSEPHGYIGLAHAGWRGTYGQIVKEMLKKVDFDYEDLKIVIGPATSNSYEINDDIKNKFEELTIDSTLYIETRGKNQHGIDLKKANALLLEEAGVPSKNIYVTEYATSENLDLFFSYRVEKGQTGRMLAFIGRK", "text": "FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl- 5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity. SIMILARITY: Belongs to the purine nucleoside phosphorylase YfiH/LACC1 family."}
{"protein": "MEMMVHGRRDEQYGGLRLGLGLGLSLGVAGGAADDEQPPPRRGAAPPPQQQLCGWNGGGLFSSSSSDHRGRSAMMACHDVIEMPFLRGIDVNRAPAAETTTTTARGPSCSEEDEEPGASSPNSTLSSLSGKRGAPSAATAAAAAASDDEDSGGGSRKKLRLSKDQAAVLEDTFKEHNTLNPKQKAALARQLNLKPRQVEVWFQNRRARTKLKQTEVDCELLKRCCETLTDENRRLHRELQELRALKLATAAAAPHHLYGARVPPPTTLTMCPSCERVASAATTTRNNSGAAPARPVPTRPWPPAAAQRSSA", "text": "FUNCTION: Probable transcription repressor involved leaf development. Binds to the DNA sequence 5'-CAAT[GC]ATTG-3'. May act as a regulatory switch to specify provascular cell fate. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class II subfamily."}
{"protein": "MTKKHYICSNCGNISPKWSGQCFDCGVWGSIVEEIISTNQVIVKVGSKQDFDKLSGHVTEQLRIPTPIGEFNRVLGGGLVLGSAILIGGDPGIGKSTLLLQLAASNFASKMNCLYITGEESLDQIKLRAIRLNLTNYNTDILAATNLENIIASIEANKNNIDLIVIDSIQTITTKELSSPPGTVSQIRTCANELVNYAKQNNIIILLSCHVTKDGQLAGPKILEHLVDTVLYFEGDHNNHFRILRSYKNRFGGVGEIGVFEMSGSGLIEVTNPSELFLMQREQNVIGTSIFAGIEGSRPLLMEVQALMVPSNMVTPRRSAVGWDANRLSMILAVLSSRIGLNLANYEVYLSIAGGLKIADPASDLAVTASLISAATGNPVPEHSVFFGEISLSGEIRKTAKAETRIKEAVKLGFNKIICSKFENLTYDFISSVSHLKDLKEIIK", "text": "FUNCTION: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. SIMILARITY: Belongs to the RecA family. RadA subfamily."}
{"protein": "AGGKATCCPCFMCSYTAGCPWGQCAHHCGCD", "text": "FUNCTION: Binds specifically to voltage-gated sodium channels (Nav), thereby delaying their inactivation during signal transduction. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone short toxin (type III) family."}
{"protein": "MSQFSVLNVGFGNIVLVSKIVSIIHSDSASAKRIRNEAKSNNSLIDATQGKKTRSIIVTDSNHLILSNLRVESLAKRIESSDNSIASEEEDLD", "text": "SIMILARITY: Belongs to the RemA family."}
{"protein": "MFRLLASSGQVSLRPVLLQHVRNNKHGLGFPNASGVPQSPSSMTSSSIVSPSQFTRSNSSAAGLSESPASSVDSKIENFLSKSAKDPLVREALDAETKNKLNYFKEQIDLAHRYRSIHDHDSERAFASTLDNLSRALEDESLRDTFVSRDLFSYAQVLNSGVYNNRTNRLSGAKNRDSDQYQNQNLHDEVLLKQAVLHLGELITNGEFKAILNAPTLSFLFYSMKQFQLYPEMIHLWENGVNDQQTGQVYLDEKILAVILPVTFEQNRFTYEEILHIYELNTEKLDKVGHELLTSMGKIAIAAGDYSRGLDSLESILQLYEKAQQSHYKNKILASLSDLHLSFIGTCKDIKISKHFFDKVVHYDLPYRVKLKVPHIQSLLENCYEQNEPMDNILYFWRASIAHYNTEQQLVLNSRYAILNNALFTIFFKKYPELNEESFSKLREIIAMYAESKPIDEVFLNTIIGNYSWDSKEVLEQIIENYDVYNVKRTPVSYRVCLKKTGSLESYSNEEILQKWNASLKHLDENKFTYIPVADWAALRDATILSHFKDARKEFYLSVLDKYKDYIQDHRSCIRFVRYWIKRKDVAADIARVASPEPQTFDCDIEIQVPQFRHLRKNINYVKEVQNMRFSG", "text": "FUNCTION: Binds the 3'-UTR of mitochondrial mRNAs. Involved in the processing or stability of mitochondrial mRNAs. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the RMD9 family."}
{"protein": "MQRPEAWPRPHPGEGAAAAQAGGPAPPARAGEPSGLRLQEPSLYTIKAVFILDNDGRRLLAKYYDDTFPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELMLMSVLTCLFESLNHMLRKNVEKRWLLENMDGAFLVLDEIVDGGVILESDPQQVIQKVNFRADDGGLTEQSVAQVLQSAKEQIKWSLLK", "text": "FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum- Golgi intermediate compartment membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows a significant preference for ERGIC and cis-Golgi apparatus compared with trans-Golgi network. SIMILARITY: Belongs to the adaptor complexes small subunit family."}
{"protein": "MAEFPEPGTVNPDSDLSNGRAEKPEIDTSAPFESVREAATRFGGFGFWRPSLNKLPDASQENIQEPDIMGLKAQAFELQRELIVKERETLEVLKELEATKATVLKLQQRNEAYEEDTLREEVDSHIKPAGVVLKDLSQAKMNLCKIASIRESVEQLKNKLNEERAALEKTRERLMEKSLKVFSLEEEEVRVRFAKEGQTGEKDLGMLNEVQRLSRQAQEVKKTGENAELEVVKAMAETESTRDKIRTAKIRLVAARKMKEAAREAEAVAIAEIEAVTGSMNVGKAEAVTISAEEYSVLARSARDAEEEARKRVEDAMSRVEEANVSKKDVLKKVDEAAQEIETSKRVLEEAVERVDAANASKIEAEEALRKWRSENGQRRRLSSSVNNTSKFKSRRETTTRLMDVNGLHLTYDVVDGSSSSSTVPVLKPTMSIGQILSKKLLLAEDSDMNVANERRKMSLGQMLAKNSSSDKTVSKRSEGKENEKRTKTRKRKSFGFAKISVLLNKESKNKKKKKKIALNLR", "text": "SIMILARITY: Belongs to the WEB family."}
{"protein": "MVLASSTTSIHTMLLLLLMLFHLGLQASISGRDTHRLTRTLNCSSIVKEIIGKLPEPELKTDDEGPSLRNKSFRRVNLSKFVESQGEVDPEDRYVIKSNLQKLNCCLPTSANDSALPGVFIRDLDDFRKKLRFYMVHLNDLETVLTSRPPQPASGSVSPNRGTVEC", "text": "FUNCTION: Cytokine secreted predominantly by activated T-lymphocytes as well as mast cells and osteoblastic cells that controls the production and differentiation of hematopoietic progenitor cells into lineage- restricted cells. Stimulates also mature basophils, eosinophils, and monocytes to become functionally activated. In addition, plays an important role in neural cell proliferation and survival. Participates as well in bone homeostasis and inhibits osteoclast differentiation by preventing NF-kappa-B nuclear translocation and activation. Mechanistically, exerts its biological effects through a receptor composed of IL3RA subunit and a signal transducing subunit IL3RB (By similarity). Receptor stimulation results in the rapid activation of JAK2 kinase activity leading to STAT5-mediated transcriptional program (PubMed:8378315, PubMed:10376805). Alternatively, contributes to cell survival under oxidative stress in non-hematopoietic systems by activating pathways mediated by PI3K/AKT and ERK (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-3 family."}
{"protein": "MAIVTLAELLEAGVHFGHQARRWNPKMFPYIYTERNGIHIIDLVQTSQLLTEACEFVKQASSDGRKVLFLGTKRQAAGIIAQEAQRCDSYYVNQRWLGGMLTNWVTIKSRVTRLRQLEEQDSSGLIDQLPKKEAAVLRRELDKLRKHLNGIKNMTRLPDIVVVVDQKRETTAIQECLKLGIPTICILDTNCSPEIINIPIPANDDAIRSIKLIIGKIADAIYEGKYGQMEPTELISSAEDK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MSLDNDINTKKRKLQDDEKPRKKRKHKRPTRDDDADLDVEAGLNRAFARMDGQLLADHLAQKTRRFGTELSSVELNDLYISAASIRDSSSFEKDRTLENLPSFLEKFAQEKEKLDEAPKKNGSPHTLIVAAAGLRAADLVRACRKFQKKGSPVAKLFAKHFKLEEQVAFLNKTRTGIAVGTPQRLIDLIEHGALSVENLRRIVVDASHIDQKKRNITDMRETMMPLAKLLARADFKERYTDEKKHIDLLFY", "text": "FUNCTION: May play a role in the regulation of DNA replication and cell cycle control. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CMS1 family."}
{"protein": "MKRTKSIRHASFRKNWSARHLTPVALAVATVFMLAGCEKSDETVSLYQNADDCSAANPGKSAECTTAYNNALKEAERTAPKYATREDCVAEFGEGQCQQAPAQAGMAPENQAQAQQSSGSFWMPLMAGYMMGRLMGGGAGFAQQPLFSSKNPASPAYGKYTDATGKNYGAAQPGRTMTVPKTAMAPKPATTTTVTRGGFGESVAKQSTMQRGATGTSSRSMGG", "text": "SIMILARITY: Belongs to the UPF0441 family."}
{"protein": "MKLLKLLSVAALSAASMMANAAGVDALSGLLKNVETFTANFTQTMRSQSGQVLQEVTGTLKAKRPGLFFWKTRAPLEQTIVTDGQQVWIYDPDLEQVTIQHLSQQLSNTPALLLSGEVGKIDEQYQVEQQPESQPGQVDFLLRPKGVDSLFDTLQLSFVNDQLVSMKLKDSLGQQTSLFFTAVSVNQTISEKAFHFEIPDGVDVIREAP", "text": "FUNCTION: Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the LolA family."}
{"protein": "GLLTNVLGFLKKAGKGVLSGLLPL", "text": "FUNCTION: Has antibacterial and antifungal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family."}
{"protein": "MIIKEFLATEKAVKLIESQNTLTIIVNRNTTKKDIKNEVEKLFSVKVEKINTLITPKGEKKAYVKLKQEYKASDVAHKLGML", "text": "FUNCTION: Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
{"protein": "MGAFRWLSIAAAASTALALTPEQLITAPRRSEAIPDPSGKVAVFSTSQYSFETHKRTSWWSLLDLKTGQTKVLTNDSSVSEIVWLSDDSILYVNSTNADIPGGVELWVTQASSFAKGYKAASLPASFSGLKTAKTKSGDIRFVAYGQSYPNGTAYNEELATAPLSSARIYDSIYVRHWDYWLSTTFNAVFSGTLKKGHGKNGYSLDGELKNLVSPVKNAESPYPPFGGASDYDLSPDGKWVAFKSKAPELPKANFTTSYIYLVPHDASETARPINGPDSPGTPKGIKGDSSSPVFSPNGDKLAYFQMRDETYESDRRVLYVYSLGSKKTIPSVAGDWDRSPDSVKWTPDGKTLIVGSEDLGRTRLFSLPANAKDDYKPKNFTDGGSASAYYFLPDSSLLVTGSALWTNWNVYTAKPEKGVIKKIASANEIDPELKGLGPSDISEFYFQGNFTDIHAWVIYPENFDKSKKYPLIFFIHGGPQGNWADGWSTRWNPKAWADQGYVVVAPNPTGSTGFGQALTDAIQNNWGGAPYDDLVKCWEYVHENLDYVDTDHGVAAGASYGGFMINWIQGSPLGRKFKALVSHDGTFVADAKVSTEELWFMQREFNGTFWDARDNYRRWDPSAPERILQFATPMLVIHSDKDYRLPVAEGLSLFNVLQERGVPSRFLNFPDENHWVVNPENSLVWHQQALGWINKYSGVEKSNPNAVSLEDTVVPVVNYN", "text": "FUNCTION: May be involved in metabolism of dipeptides or may affect host defense mechanisms. Has a substrate specificity limited to the hydrolysis of X-Ala, His-Ser, and Ser-Tyr dipeptides at a neutral pH optimum (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S9C family."}
{"protein": "MSDIILDSKSFQSAVSKISREISDNNKNIREVAIIGIQNKGVFLAKRILAEIAKLAGIGRSLIPFGTLDITLYRDDLDDLGSKIPVIKDTVIPFDTSRKNIILIDDVLYTGRTVRAALDVLMDFGRPKSIQLAVLIDRGFRELPIEAKYIGIRYQSEELIKVECKETDGVDRVTFIK", "text": "FUNCTION: Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. FUNCTION: Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily."}
{"protein": "ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY", "text": "FUNCTION: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). SUBCELLULAR LOCATION: Secreted Nucleus Cytoplasm Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytosol Microsome Endoplasmic reticulum Mitochondrion Mitochondrion membrane Cytoplasm, perinuclear region Cytoplasmic vesicle, secretory vesicle, chromaffin granule Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. SIMILARITY: Belongs to the clusterin family."}
{"protein": "MATRRLGVGETLGALNAALGPGGPVWIKETRTRHLRSRDFLAPHRALQARFDDGQVPEHLLHALACLQGPGVAPVLRCAPTPAGLSLQLQRSAVFERVLSAVAAYATPASPASLGQRVLLHCPALRSSPCALRLSQLRTVLVADHLARALRAHGVCVRLVPAVRDPHMLTFLQQLRVDWPAASERASSHTLRSHALEELTSANDGRTLSPGILGRLCLKELVEEQGRTAGYDPNLDNCLVTEDLLSVLAELQEALWHWPEDSHPGLAGASDTGTGGCLVVHVVSCEEEFQQQKLDLLWQKLVDKAPLRQKHLICGPVKVAGAPGTLMTAPEYYEFRHTQVCKASALKHGGDLAQDPAWTEIFGVLSVATIKFEMLSTAPQSQLFLALADSSISTKGTKSGTFVMYNCARLATLFESYKCSMEQGLYPTFPPVSSLDFSLLHDEGEWLLLFNSILPFPDLLSRTAVLDCTAPGLHIAVRTEMICKFLVQLSMDFSSYYNRVHILGEPRPHLFGQMFVRLQLLRAVREVLHTGLAMLGLPPLSHI", "text": "FUNCTION: Involved in tRNA methylation. Facilitates the recognition and targeting of tRNA(Arg)(CCU) and tRNA(Arg)(UCU) substrates for N(3)- methylcytidine modification by METTL2A and METTL2B."}
{"protein": "MALVRGAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQATVALDEVFGAGRAQHTQWYKLHSKPGKKEKERGEIEVTIQFTRNNLSASMFDLSMKDKPRSPFSKIRDKMKGKKKYDLESASAILPSSAIEDPDLGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSASGSLAYQGPGAELLTRSPSRSSWLSTEGGRDSAQSPKLFTHKRTYSDEANQMRVAPPRALLDLQGHLDAASRSSLCVNGSHIYNEEPQGPVRHRSSISGSLPSSGSLQAVSSRFSEEGPRSTDDTWPRGSRSNSSSEAVLGQEELSAQAKVLAPGASHPGEEEGARLPEGKPVQVATPIVASSEAVAEKEGARKEERKPRMGLFHHHHQGLSRSELGRRSSLGEKGGPILGASPHHSSSGEEKAKSSWFGLREAKDPTQKPSPHPVKPLSAAPVEGSPDRKQSRSSLSIALSSGLEKLKTVTSGSIQPVTQAPQAGQMVDTKRLKDSAVLDQSAKYYHLTHDELISLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQIPPGPPK", "text": "FUNCTION: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. SUBCELLULAR LOCATION: Cytoplasm. Recycling endosome membrane; Peripheral membrane protein. Early endosome membrane; Peripheral membrane protein Golgi apparatus membrane; Peripheral membrane protein Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein Mitochondrion membrane; Peripheral membrane protein."}
{"protein": "MNPVNYLYLAALLFAIGASGVLVRRNAIVVFMCVELMLNACNLALVTFSRMHGNLDGQIVAFFTMVVAAAEVVVGLAIIVSLFRSRHSASVDDASLMKL", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
{"protein": "MDLVSELNETQPWLTTPFDLNGSVGAANISNQTEPYYDLASNVVLTFIYFVVCIIGLCGNTLVIYVILRYAKMKTITNIYILNLAIADELFMLGLPFLAMQVALVHWPFGKAICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRRPRTAKMINVAVWGVSLLVILPIMIYAGLRSNQWGRSSCTINWPGESGAWYTGFIIYAFILGFLVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKVTRMVSIVVAVFIFCWLPFYIFNVSSVSVAISPTPALKGMFDFVVVLTYANSCANPILYAFLSDNFKKSFQNVLCLVKVSGTDDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI", "text": "FUNCTION: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasm Note=Located mainly at the cell surface under basal conditions. Agonist stimulation results in internalization to the cytoplasm (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MGQKINPLGFRLGTTQDHHSLWFSQPKNYSESLQEDKKIRDFIKNYVQNNMIKASGAEGIARIYIQKRIDLIQVVIFMGFPKLLIETRPQGIKELQRTLQKEFNFGNQKLNITITRIEKPYGNPNILAEFIAVQLKNRVSFRKAMKKAIELAEQADTKGIQVQIAGRVDGKEIARVEWIREGRVPRQTIRANLDYCSYPVRTIYGVLGVKIWIFLDQAK", "text": "SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
{"protein": "MAVNVYSTSVTSDNLSRHDMLAWINESLQLTLTKIEQLCSGAAYCQFMDMLFPGSVALKKVKFQAKLEHEYIQNFKVLQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPVAARQGQETVAPNLVAPVMNKPKKPLGTGSAAPQRPIVAQRTPATPKGGTGMVKKAAGDDESAGLIEQINVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVEILYATDEGFVIPDEGAPQEEQEEY", "text": "FUNCTION: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection between astral microtubules and the cortex during mitotic chromosome segregation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Golgi apparatus Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole. SIMILARITY: Belongs to the MAPRE family."}
{"protein": "MSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGPLGSIRNLAMEKVANSVLFPCKYASSGCEITLPHTEKADHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595, PubMed:28546513, PubMed:32430360, PubMed:33591310). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP (PubMed:10747903, PubMed:11146551, PubMed:11389839, PubMed:11389840, PubMed:11483517, PubMed:11483518, PubMed:11752454, PubMed:12072443). Confers constitutive instability to HIPK2 through proteasomal degradation (PubMed:18536714, PubMed:33591310). It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Has some overlapping function with SIAH2 (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Induces apoptosis in cooperation with PEG3 (By similarity). Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus (By similarity). GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins (By similarity). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin- mediated proteasomal degradation of AXIN1 (PubMed:28546513, PubMed:32430360). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic. Partially nuclear. SIMILARITY: Belongs to the SINA (Seven in absentia) family."}
{"protein": "MSNTTEKKMPQQQQVERPTALAPADAEIERVFTRFDADGDGRISPSELAAVTRAIAPPPSESAGGREVAAMMNELDTDRDGFVDLGEFAAFHGRGRGDAEHEAELRAAFDVYDVDGDGRITAAELGKVLGRIGEGCSAEECERMIASVDVDGDGCVGFEEFKKMMCRDAAATGGADKAKTE", "text": "FUNCTION: Potential calcium sensor."}
{"protein": "MEQAPEDQGPQREPYNEWALELLEDLKNEALRHFPRPWLHGLGQYFYNTYGDTWEGVEAIIRTLQQLLFIHYRIGCQHSRIGITPQRRRNGASRS", "text": "FUNCTION: During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions. FUNCTION: During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the VPR carried into the virion. Additionally, VPR induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Detected in the serum and cerebrospinal fluid of AIDS patient, VPR may also induce cell death to bystander cells. SUBCELLULAR LOCATION: Virion Host nucleus Host extracellular space Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient. SIMILARITY: Belongs to the HIV-1 VPR protein family."}
{"protein": "MGEIVFTEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKDMFSFLRDTDEVPHNNPKLKAHAVKVFKMTCETAIQLREKGKVVVADTTLQYLGSVHFKSGVLDPHFEVVKEALVRTLKEGLGEKYNEEVEGAWSKAYDHLALAIKAEMKQEDSQKP", "text": "FUNCTION: May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule. SIMILARITY: Belongs to the plant globin family."}
{"protein": "MSTPARRRLMRDFKRMKEDAPPGVSASPLPDNVMVWNAMIIGPADTPYEDGTFRLLLEFDEEYPNKPPHVKFLSEMFHPNVYANGEICLDILQNRWTPTYDVASILTSIQSLFNDPNPASPANVEAATLFKDHKSQYVKRVKETVEKSWEDDLKDMDDGDDDDDDDDDDD", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MVRRLARGCWSAFWDYETPKVIVVRNRRLGFVHRMVQLLILLYFVWYVFIVQKSYQDSETGPESSIITKVKGITMSEDKVWDVEEYVKPPEGGSVVSIITRIEVTPSQTLGTCPESMRVHSSTCHSDDDCIAGQLDMQGNGIRTGHCVPYYHGDSKTCEVSAWCPVEDGTSDNHFLGKMAPNFTILIKNSIHYPKFKFSKGNIASQKSDYLKHCTFDQDSDPYCPIFRLGFIVEKAGENFTELAHKGGVIGVIINWNCDLDLSESECNPKYSFRRLDPKYDPASSGYNFRFAKYYKINGTTTTRTLIKAYGIRIDVIVHGQAGKFSLIPTIINLATALTSIGVGSFLCDWILLTFMNKNKLYSHKKFDKVRTPKHPSSRWPVTLALVLGQIPPPPSHYSQDQPPSPPSGEGPTLGEGAELPLAVQSPRPCSISALTEQVVDTLGQHMGQRPPVPEPSQQDSTSTDPKGLAQL", "text": "FUNCTION: Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the P2X receptor family."}
{"protein": "MTQLSSNDVPSMGRRQFMNLLTFGTATGVALGALYPVANYFMPLRAGGGGGGTSAKDELGNPITKTGWLATHQAGDRSLVQGLKGDPTYLIVNEVGEIGEFGLNAICTHLGCVVPWDSGANKFICPCHGSQYDTNGKVVRGPAPLSLALAHVDIEDDAVLVKQWSETDFRTNENPWWA", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer. SIMILARITY: Belongs to the Rieske iron-sulfur protein family."}
{"protein": "MIEPLLCGIVLGLIPVTLAGLFFAAYQQYKRGSQLEL", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetG family."}
{"protein": "MAARVLLARGGLLRPAAQSAFLPGLRTVTSSSHRAREDSWLKSLFVRKVDPRKDAHSNLLAKKETSSLYKLQFHNVKPECLDAYNKICQEVLPKIHEGKQYPCTLVGTWNTWYGEQDQAVHLWRYEGGYPALTEVMNKLKENQEFVNFRKARSDMLLSRKNQLLLEFSFWNEPVPRPGPNIYELRSYQLRPGTMIEWGNYWARAIRFRQDSNEAIGGFFSQIGQLYMVDHLWAYRDLQTREDIRNAAWHKHGWEELVYYTVPLIQEMESRIMIPLKTSPLQ", "text": "FUNCTION: May act as a positive regulator of L-type calcium channels. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion outer membrane. SIMILARITY: Belongs to the NipSnap family."}
{"protein": "MSKVSSAVLRQGVATILKEKKERKFVETVELQIALKNYDPDKDKRFAGSVKLPNITKANYKVCVLGDAQACEAAQKENIPFMDVDALKALNKDKKLVKKLARKYNAFLASDSVLRQLQKILGPGLNKAGKFPTLLGKNEDLKVKINELQCQVKFQLKKVLCMGVAVGNVKLTEDQLVANIERSISFLVSLLKKGWQNIKCLYIKSSMGAPIKIY", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL1 family."}
{"protein": "MKTIEQKIEQCRKWQKAARERAIARQREKLADPVWRESQYQKMRDTLDRRIAKQKERPPASKTRKSAVKIKSRGLKGRTPTAEERRIANALGALPCIACYMHGVISNEVSLHHIAGRTAPGCHKKQLPLCRWHHQHAAPAEVREKYPWLVPVHADGVVGGKKEFTLLNKSEMELLADAYEMANIMH", "text": "FUNCTION: Stimulates microhomologous recombination. Enhances the recA- dependent precise excision of an IS1 element inserted within the E.coli galT gene."}
{"protein": "MRASPLLSLSIFITFVSIFSLLTYLPSFFAQISRIERQLEEELDEFLNIEHEFRKEFDIYPKNYERRQKKHVYSYCECEYINTCPPGRIGITGPDGQPGKDGLPGMPGSPGIPGELPNILYQQVFGCRICPYGPKGKSGYKGIDGPPGIPGWPGEPGVRGMNGERGSTGLDGAPGEPGSPGLPGFAGLPGSIGITGIKGVMGEVGEPGAPGIPGEEGLSGPTGQPGSPGSIGAMGYEGAYGDRGEPGPPGPIGRRGGPGLDSHYCPCPSRKMFLSILREKTKKQL", "text": "FUNCTION: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment (By similarity). SIMILARITY: Belongs to the cuticular collagen family."}
{"protein": "MAVTDIFARRATLARSVRLLSQFRYERSEPARFYGALAADTAAMVDDLWRAGHGESAAGRTLLDVGGGPGYFAAAFTDAGVRYLGVEPDPGEMHAAGPVVAADTGTFVRASGMALPFADDSVDICLSSNVAEHVPRPWQLGAEMLRVTRPGGLAVLSYTVWLGPFGGHEMGLTHYLGGARAAERYARKHGHPAKNNYGSSLFEVSVADGLAWAASTGAALAAFPRYHPRWAWSLTSVPVLREFLVSNLVLVLQPQ", "text": "SIMILARITY: Belongs to the methyltransferase superfamily."}
{"protein": "MSKLTHVREDGSAHMVDVTGKNETSRTAVAEGFVKMRGDVVKQLFSAGLPKGDALPVARIAGIMGAKKTPDIIPLCHPLPLGKITVDFFELADGVRIEASVKTRGVTGVEMEALTAVSTAALTVYDMIKAVDKMAVIDGIRVLSKTGGKSGDWSVQ", "text": "FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). SIMILARITY: Belongs to the MoaC family."}
{"protein": "MASPNGGDDFESSLLSFEKLDRASPDLWPEQLPGVVEFAASCKNPITDSPPKWMAELESEDYEMLKELGSLTTANLMEKVRGLQNLAYQLGLEESREMTRGKFLNILESFKK", "text": "SIMILARITY: Belongs to the lin-52 family."}
{"protein": "VRDGYIALPHNCAYGCLNNEYCNNLCTKDGAKIGYCNIVGKYGNACWCIQLPDNVPIRVPGRCHPA", "text": "FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active on both mammals and insects. It can be considered as a cardiotoxin, as it can bind to human cardiac sodium channel and modify its normal properties. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MAVSGFEGFEKRLELRFFDDDKPITKNPMGLRLIDFESLDQVLNEVQCTVVSAVANRSFDAYVLSESSLFVYPTKIIIKTCGTTQLLKSIRPLIHLARNLGLTLRACRYSRGSFIFPKAQPFPYTSFKDEVIVVEESLPKSLCYRKASVMTPSNNPSRAWHVFTASADVESDEHVVVVEVCMTELDRVNARSFFKRKGDEKNNSDSAGKEMTRLSGIDNINANAYICDFAFDPCGYSMNGVDGDRYSTIHVTPEDGFSYASFECGLSLYDNGHEDISEVLSRAIDVFRPSDVSIATTYGGEDYNHEVTKRVERVLAKKLDLKCRSRLMDEFPGSGTVVYQSFTPRRK", "text": "FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Essential for polyamine homeostasis, and normal plant embryogenesis, growth and development. SIMILARITY: Belongs to the eukaryotic AdoMetDC family."}
{"protein": "MRCFRWWLYSGWWWLTFGCARTVTVGFVAPTVRAQSTVVRSEPAPPSETRRDNNDTSYFSSTSFHSSVSPATSVDRQFRRTTYDRWDGRRWLRTRYGNASACVTGTQWSTNFFFSQCEHYPSFVKLNGVQRWTPVRRPMGEVAYYGGCCMVGGGNRAYVILVSGYGTASYGNALRVNFGRGNCTAPKRTYPRRLELHDGRTDPSRCDPYQVYFYGLQCPEQLVITAHGGVGMRRCPTGSRPTPSRPHRHDLENELHGLCVDLLVCVLLLALLLLELVPMEAVRHPLLFWRRVALSPSTSKVDRAVKLCLRRMFGLPPPPSVAPPGEKKELPAQAALSPPLTTWSLPPFPSTRIPDSPPPPYQLRHATSLVTVPTLLLYTSSDIGDTASETTCVAHATYGEPPEPARSTATVQECTVLTAPNCGIVNNDGAVSEGQDHGDAVHHSLDVVSQCAADTGVVDTSE", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HHV-5 US29 protein family."}
{"protein": "MSSKSTKRAKIEDPKDNVFMVEKVLDKRTGKAGRDEFLIQWQGFPESDSSWEPRENLQCVEMLDEFEREFSKREKPIRKRHSQKPEPSEDQADPEEDKDEKKETNQNDKFSLEGKQLKCIVGLTKGPGELHFLCKFSDDTARLLPAKEVNSRYPSQVIRYYESKLTIQDPKADEL", "text": "FUNCTION: Seems to be involved in transcriptional silencing in heterochromatin-like complexes (PubMed:11850401). Probably does not act as global transcriptional repressor, instead targeting a subset of genes (PubMed:23028351, PubMed:19064713, PubMed:22185090, PubMed:25467431). Involved in RNA processing mediated by Tar DNA- binding protein homolog tdp-1 (PubMed:29760282). Plays a role in linking epigenetic regulation with the innate immune response (PubMed:22083954). Involved in the endoplasmic reticulum (ER) stress response via modulation of the unfolded protein response (UPR), acting mainly through the IRE1-XBP1 pathway and perhaps, to a lesser extent, through the autophagy pathway (PubMed:24715729). May act in a common pathway with retinoblastoma-like protein homolog lin-35 and zinc finger protein lin-13 to influence the ER stress response in the intestine (PubMed:24715729). Plays a role in the formation of the vulva and in fertility, acting together with a CoREST-like complex, and chromobox protein homolog hpl-1 (PubMed:26476455, PubMed:16905130, PubMed:16890929, PubMed:11850401). Acting in concert with hpl-1 and histone H1 protein his-24, involved in reproduction, somatic gonad development, male tail development and vulval cell fate specification; perhaps as a result of modulating expression of Hox genes mab-5 and egl-5 (PubMed:23028351, PubMed:16905130, PubMed:16890929, PubMed:11850401, PubMed:19064713). In vulval cell fate specification may act by repressing transcription, of EGF family gene lin-3 in hypodermal hyp7, and of homeobox lin-39 in vulval precursor cells (VPC) (PubMed:19064713). Role in growth and somatic gonad development is antagonized by histone-lysine N-methyltransferase set-2/SET1 (PubMed:17967446). Required for larval development, acting redundantly with hpl-1 (PubMed:16905130). Plays a role in regulation of the developmentally arrested larval state known as dauer, longevity, and lipid metabolism (PubMed:22185090). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to distinct nuclear foci, not overlapping significantly with hpl-1, in embryonic cells (PubMed:26476455, PubMed:16905130). Localization to nuclear foci overlaps partially with zinc finger protein lin-13 (PubMed:16890929). Localizes to foci in a lin-13- dependent manner (PubMed:16890929). Localization along chromosomal arms correlates with localization of histone H3 methylated at 'Lys-9' (H3K9me), however, hpl-2 can associate with chromatin in an H3K9me- independent manner (PubMed:25467431). Localization on chromosome correlates with sequences enriched in repetitive elements, or in well- expressed genes (PubMed:25467431). Localized to gene bodies (PubMed:29760282)."}
{"protein": "MPLHKVPVGLWKRLRLREGIYSRLPAHYLRSLEEARTPTPVHFRPHGAKFKINPKNGQRERVEDVPIPVHYPPESQLGLWGGEGWLKGHRYVNNDKFSKRVKKVWKPQLFQRELYSEILDTRFTVTVTMRTLDLIDEAYGFDFYILKTPKEDLCSKFGMDLKRGMLLRLARQDPQLHPDDPERRAAIYDKYKAFVIPEAEAEWVGLTLDEAVEKQRLLEEKDPVPLFKVYVEELVEQLQQQALSEPAVVQKRANRT", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family."}
{"protein": "MFQGQRGWFCGSVSQDLRQFWVAEGGTISDPRAADFLFSCDASHPDTLRIYQSLDYIEDNATVFHAYYLSAVANAKIKNSVALGHFILPPACLQKEIRRKIGSFIWEQDQHFLIEKHDEVTPNEIKTLRENSELATEHKKELSKSPEKHFIRTPVVEKQMYFPLQNYPVNNMVTGYISIDAMKKFLGELHDFIPGTSGYLAYHVQNEINMSAIKNKLKRK", "text": "FUNCTION: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. SUBCELLULAR LOCATION: Chromosome, telomere Nucleus inner membrane Note=Localizes to telomeres throughout meiotic prophase I and disappears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. SIMILARITY: Belongs to the TERB2 family."}
{"protein": "MSINLHSAPEYDPSYKLIQLTPELLDIIQDPVQNHQLRFKSLDKDKSEVVLCSHDKTWVLKQRKHSNTVLLMREFVPEQPITFDETLLFGLSKPYMDVVGFAKTESEFETRETHGELNLNSVPIYNGELDFSDKIMKRSSTKVIGTLEELLENSPCSALEGISKWHKIGGSVKDGVLCILSQDFLFKALHVLLMSAMAESLDLQHLNVEDTHHAVGKDIEDEFNPYTREIIETVLNKFAVQEQEAENNTWRLRIPFIAQWYGIQALRKYVSGISMPIDEFLIKWKSLFPPFFPCDIDIDMLRGYHFKPTDKTVQYIAKSTLPMDPKERFKVLFRLQSQWDLEDIKPLIEELNSRGMKIDSFIMKYARRKRLGKKTVVTSR", "text": "FUNCTION: Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double- stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. SIMILARITY: Belongs to the DCC1 family."}
{"protein": "MARIIVLIVAFMALIAGVFATEEKLAKLQIGILKKISPEECTQKARKGDTVSVHYTGKLEDGTVFDSSVERGQPIQFPLGTGRVIPGWDQGILGMCVGEKRKLTIPPHLAYGKQGAGRVIPPDSTLIFTTELVSIDNDGDRDEL", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily."}
{"protein": "MLSARSFLSSARTIARSSLMSARSLSDKPKGHVIGIDLGTTNSCVSIMEGKTPKVIENAEGVRTTPSTVAFTADGERLVGAPAKRQAVTNSANTLFATKRLIGRRYEDPEVQKDLKVVPYKIVKASNGDAWVEAQGKVYSPSQVGAFVLMKMKETAESYLGTTVNNAVVTVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKDAGDKIIAVYDLGGGTFDVSILEIQKGVFEVKSTNGDTFLGGEDFDHALVHHLVGEFKKEQGVDLTKDPQAMQRLREAAEKAKCELSSTTQTDINLPYITMDQSGPKHLNLKLTRAKFEQIVGDLIKRTIEPCRKALHDAEVKSSQIADVLLVGGMSRMPKVQATVQEIFGKVPSKAVNPDEAVAMGAAIQGAVLAGDVTDVLLLDVTPLSLGIETLGGIMTKLITRNTTIPTKKSQVFSTAADGQTQVQIKVFQGEREMATSNKLLGQFSLVGIPPAPRGVPQVEVTFDIDANGIVNVSARDRGTGKEQQIVIQSSGGLSKDQIENMIKEAEKNAAEDAKRKELVEVINQAEGIIHDTEAKMTEFADQLPKDECEALRTKIADTKKILDNKDNETPEAIKEACNTLQQQSLKLFEAAYKNMAAKNSGGDAQEAKTAEEPKKEQN", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "EEGGSPPPVVI", "text": "FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-potentiating peptide family."}
{"protein": "MTYLAETVTLNNGEKMPLVGLGCWKMPNDVCADQIYEAIKIGYRLFDGAQDYANEKEVGQGVNRAIKEGLVKREDLVVVSKLWNSFHHPDNVPRALERTLSDLQLDYVDIFYIHFPLAFKPVPFDEKYPPGFYTGKEDEAKGHIEEEQVPLLDTWRALEKLVDQGKIKSLGISNFSGALIQDLLRGARIKPVALQIEHHPYLTQERLIKYVKNAGIQVVAYSSFGPVSFLELENKKALNTPTLFEHDTIKSIASKHKVTPQQVLLRWATQNGIAIIPKSSKKERLLDNLRINDALTLTDDELKQISGLNQNIRFNDPWEWLDNEFPTFI", "text": "FUNCTION: Reduces D-xylose into xylitol. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MKALSFLFIPVLGLLVCGQSLCPIDKAISEKIQEVTTSLVPGAVRIIGLDCRSVTSRGSLVTCPSGFAVTGCTCGSACGSWDVRAETTCHCQCAGMDWTGARCCRLHIQ", "text": "FUNCTION: Hormone that seems to suppress insulin ability to stimulate glucose uptake into adipose cells. Potentially links obesity to diabetes (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the resistin/FIZZ family."}
{"protein": "MSKHGVEQLPAARALTWPQRLGQYWKLVRGDRPIGSLLLLWPTWWALWLAADGLPPLWTLLVFTAGVWLTRSAGCVINDYADRWLDPHVERTKSRPLATGAVSGREALWVFVVLMLVAFALVLTLNWLTVALSVPGVFLAASYPYLKRHTHLPQVYLGMAFGWGIPMAFAAVQGRVPLLGWLLYAANILWATAYDTWYAMVDRDDDIRMGSKSTAILFGRFDLIAQGILYALMAATLVLVGLRADLGVAYWAGLAVAALLVAYEFRIARHRERGPCFRAFLHNNWVGLAIFVGIAVAVAGR", "text": "FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
{"protein": "MAEKSSKKLWGGRFSGATDPLMAEFNKSIYSGKEMCEEDVIGSMAYAKALCQKNVISEEELNSILKGLEQIQREWNSGQFVLEPSDEDVHTANERRLTEIIGDVAGKLHTGRSRNDQVTTDLRLWLCRKIKEVEVYVINLLKVFTNRAEMEIDVIMSGYTHLQRAQPVRWSHFLMSHALPLLGDLGRLRQLYTRVSQLPLGAGALAGNPFNVDREFLRKELGFEGIIMNSMNAVGDRDFVIEFMFWAGMVMLHISRFAEDLIIYSSSEFGFVTLSDAYSTGSSIMPQKKNPDSLELLRGKSGRVLGDMIGLMITVKGTPTTYNKDLQEDKEPLFDAFKTVSDSLQILTGVVSTLTINPTKIAESLTPDLLATDLAEYLVRKGLPFRQTHHISGSAVRMAEERNTTLDKLSVSDLQSLHPLFDEDVSKVFNYEESVEKRCSIGGTAKHCVQEQIEHIRSAIL", "text": "SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily."}
{"protein": "MDDIFNFELPLHDRIKAIVKFGDETTIKRLISLLTISNSSIIKNTLYHLCKFCSDISCVLRLEIALALIDYEKEETEPSEIIGFEALDYVCFSMHKSKEIPFSCKLNAYLILNSGLPNLKRVYLYLYDMLTDSSTTFQFKYKTVKFLVSEREENNITSLMVEYCISVLLSNFHDSSYPKINNETYEDYLQIFILTCQLSLSYVPKLKCSCIAENKLLEICKNQNLSVNIRADASDMLLSYGSSENKEEAKIILDSLSFDNHTIKTIYNNKENVHTSTINKTAINTITIIIEDVNKMFQREDIWILTENILQNLIEKYPPNFKPQIKSQIDNAIKAYNRIMYLDNALYTAYNFNLKNIMNYVWTFINNSNKVSNKVELEKRLIEEMREMNNTCSSGYLTRFANIFSGFLENGGVFIGWDEQILSIFYGKVNSAITSSLNKDLILENLIETENENDKQEFQKLLRTILPNIIESIKIEFKDHISESDIDLYIRRALSVFEGHEFI", "text": "SIMILARITY: Belongs to the IIV-6 467R family."}
{"protein": "MNFLAHLHLAHLAESSLSGNLLADFVRGNPEESFPPDVVAGIHMHRRIDVLTDNLPEVREAREWFRRETRRVAPITLDVMWDHFLSRHWSQLSPDFPLQEFICYARKQVMTILPDSPPRFINLNNYLWSEQWLVRYRDMDFIQNVLNGMASRRPRLDALRDSWYDLNAHYTALETRFWQFYPRMMAQASHKAL", "text": "FUNCTION: Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP. SIMILARITY: Belongs to the AcpH family."}
{"protein": "MDLRLIFGPTCTGKTSTAVALAQQTGLPVLSLDRVQCCPQLSTGSGRPTVEELKGTSRLYLDDRPLVKGIIAAKQAHERLMGEVYNYEAHGGLILEGGSISLLKCMAQSSYWSADFRWHIIRHELADEETFMNVAKARVKQMLRPAAGLSIIQELVDLWKEPRLRPILKEIDGYRYAMLFASQNQITSDMLLQLDADMEDKLIHGIAQEYLIHARRQEQKFPRVNAAAYDGFEGHPFGMY", "text": "FUNCTION: Transfers dimethylallyl groups to AMP as part of the biosynthesis of cytokinin phytohormones. FUNCTION: Transfers dimethylallyl groups to AMP as part of the biosynthesis of cytokinin phytohormones. SIMILARITY: Belongs to the isopentenyl transferase family."}
{"protein": "MPPKRNKKAEAPIAERDAGEELDPNAPVLYVEHCRSURVFRRRAEELHSALRERGLQQLQLQLNALGAPRRGAFELSLSAGGMGKQEQVALWSGLKRGPPRARKFPTVEEVYDQIVGILGDQQESKEQTNTQKSSKIDLPGSEAIASPKKSESTEEAQENKAPTSTSTSRKSKKEQKSEEEPTQVDSKEAKQSKELVKTKRQPKAQKKQAKASESQEEVAEDKPPSSQKRKRTTRSSTDEATAGAKRRR", "text": "FUNCTION: May be involved in a redox-related process. Required for survival and specifically for salivary gland morphogenesis. SUBCELLULAR LOCATION: Cytoplasm Secreted Note=Secreted into the salivary gland lumen."}
{"protein": "MAKVPDLFEDLKNCYSENEEYSSAIDHLSLNQKSFYDASYGSLHENCTDKFVSLRTSETSKMSTFTFKESRVVVSATSNKGKILKKRRLSFNQPFTEDDLEAIAHDLEETIQPRSAPHSFQNNLRYKLIRIVKQEFIMNDSLNQNIYVDMDRIHLKAASLNDLQLEVKFDMYAYSSGGDDSKYPVTLKVSNTQLFVSAQGEDKPVLLKEIPETPKLITGSETDLIFFWEKINSKNYFTSAAFPELLIATKEQSQVHLARGLPSMIDFQIS", "text": "FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity. SUBCELLULAR LOCATION: Nucleus Cytoplasm Secreted Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. Recruited to DNA damage sites and secreted after genotoxic stress. SIMILARITY: Belongs to the IL-1 family."}
{"protein": "MNPNCARCGKIVYPTEKVNCLDKYWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGVEPERREAQDSSSYRRPTEQQQPQPHHIPTSAPVYQQPQQQQMTSSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI", "text": "FUNCTION: Plays an important role in the regulation of dynamic actin- based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cell cortex Cytoplasm, cytoskeleton Note=Associated with the F-actin rich cortical cytoskeleton."}
{"protein": "MIQKNWQELIKPNKVEFASSGRTKATLVAEPLERGFGLTLGNALRRVLLSSLRGAAVTAVQIDGVLHEFSSIPGVREDVTDIVLNIKEIAIKMDGDDAKRMVVRKQGPGVVTAGDIQTVGDIEILNPNHVICTLDEGAEIRMEFTVNNGKGYVPADRNRSEDAPIGLIPVDSLYSPVKKVSYKVENTREGQVLDYDKLTMSIETDGSVTGEDAIAFAARILQDQLSVFVNFDEPQKETEEEAVTELAFNPALLKKVDELELSVRSANCLKNDNIVYIGDLIQKTEAEMLRTPNFGRKSLNEIKEVLASMGLHLGMEVPSWPPENIEDLAKRYEDQY", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the RNA polymerase alpha chain family. SIMILARITY: Belongs to the RNA polymerase alpha chain family."}
{"protein": "MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDLAFEATVKKQVQKLKEPSIKCVDMVVSELTATIRKCSEKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKASGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPTGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSQPIGSGKSIPS", "text": "FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Note=Microtubule-associated. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MTAGTVVITGGILATVILLCIIAVLCYCRLQYYCCKKSGTEVADEEEEREHDLPTHPRGPTCNACSSQALDGRGSLAPLTSEPCSQPCGVAASHCTTCSPYSSPFYIRTADMVPNGGGGERLSFAPTYYKEGGPPSLKLAAPQSYPVTWPGSGREAFTNPRAISTDV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FAM163 family."}
{"protein": "MEVIRDGEGESVKYKPGGRLDMSHGFLRHIRRNQIARDDYDREVKQAKEKQRRRHTNTPRRPRRPDRQVYNPRIRNGSEPGVNAEAEDWNESSSGTEMENTGTELFWLDYQADNGKITSFIVHKEDKPEVIVQRVAEKNVLDSSMRAALLARVGQEMNKRCDKR", "text": "SIMILARITY: Belongs to the UPF0561 family."}
{"protein": "MGFKGVGTYEIVPYQAPSLNLNAWEGKLEPGAVVRTYTRGDKPSDNAKWQVALVAGSGDSAEYLIINVHSGYFLTATKENHIVSTPQISPTDPSARWTIKPATTHQYEVFTINNKVSELGQLTVKDYSTHSGADVLSASAKTADNQKWYFDAK", "text": "FUNCTION: Lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha- over the beta-anomer. Can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. Strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. Strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans (By similarity). FUNCTION: Lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha- over the beta-anomer. Can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. Strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. Strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans."}
{"protein": "MAAYQTYTMAGIKEDFADWVSNISPEYTPLISMIRKFPVHNTMFQWQWDVLKDVDTENQHNEASDAKDVELTPTTVVQNYVQIMRKVVFVSDSANAVSSHGREKELFYQLKKAAKELKRDNEGIFLLKDRAGDAGSATKPRLTASFGSLIDASMKKTADLDEATLFEMTAKLYTEGADPTLIMYHPSNANFFASLQEKSGTRMRIFENDKRFVKQVEYIVDPLGQELKCIPNRWCPEDATYIFNPSDLGMAVLRAPKKVALAKSGSAEKYMIEQEVGFRLNNPKAAALIIGKYKEGGNGGGESVKS", "text": "SUBCELLULAR LOCATION: Virion."}
{"protein": "MSSSRPVFRSRWLPYLLVAPQLIITVIFFIWPAGEALWYSLQSVDPFGFSSQFVGLDNFVTLFHDSYYLDSFWTTIKFSTFVTVSGLLVSLFFAALVEYIVRGSRFYQTLMLLPYAVAPAVAAVLWIFLFNPGRGLITHFLAEFGYDWNHAQNSGQAMFLVVFASVWKQISYNFLFFYAALQSIPRSLIEAAAIDGAGPIRRFFKIALPLIAPVSFFLLVVNLVYAFFDTFPVIDAATSGGPVQATTTLIYKIYREGFTGLDLASSAAQSMVLMFLVIVLTVVQFRYVESKVRYQ", "text": "FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn- glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. UgpAE subfamily."}
{"protein": "MKTVAFLAVVVLFAAFACASCSSSYAAPAPAAAPASSYSSVPAPPCPKNYLFSCQPNLVPAPCAQQAAPAAYGSAGAYTEQVPSYIGFAPYQQLQQYHQRIGNAALIDELRSLGQGIQGQQY", "text": "FUNCTION: Major early eggshell protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the vitelline membrane family."}
{"protein": "MPIPNNPGAGENAFDPVFVNDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYDIKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVETSKPLFGEHYVRVKSYCNDQSTGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPLWNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL", "text": "FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to the N(9) of hypoxanthine, guanine or xanthine, leading to IMP, GMP and XMP, respectively. Plays a central role in the generation of purine nucleotides through the purine salvage pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MDPGTTGIVGGVSEAKPATPEIQEVADKVKRQLEEKTNEKYEKFKVVEYKSQVVAGQILFMKVDVGNGRFLHMKVLRGLSGDDDLKLLDYQTNKTKNDELTDF", "text": "FUNCTION: This is an intracellular thiol proteinase inhibitor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cystatin family."}
{"protein": "MDPPFNEIYNNLLYNQITKKDNDVSEIPFSFSVTAVVEEVELPVIDVSRLIDGAEEEREKCKEAIARASREWGFFQVINHGISMDVLEKMRQEQIRVFREPFDKKSKSEKFSAGSYRWGTPSATSIRQLSWSEAFHVPMTDISDNKDFTTLSSTMEKFASESEALAYMLAEVLAEKSGQNSSFFKENCVRNTCYLRMNRYPPCPKPSEVYGLMPHTDSDFLTILYQDQVGGLQLIKDNRWIAVKPNPKALIINIGDLFQAWSNGMYKSVEHRVMTNPKVERFSTAYFMCPSYDAVIECSSDRPAYRNFSFREFRQQVQEDVKKFGFKVGLPRFLNHVY", "text": "FUNCTION: Catalyzes the 2-beta-hydroxylation of gibberellins (GA) precursors, rendering them unable to be converted to active GAs. Hydroxylates the C20-GA GA12 and GA53, but is not active on C19-GAs, like GA1, GA4, GA9 and GA20. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family. GA2OX subfamily."}
{"protein": "MLLLLHLLPAVLPASALGSCTGAGADRQLVLAKVRARVLEHLSPPAMQEPQKDVRRVHRRDVLEEVEVPPEEQEDTSQVILFPSTDVPCEPTQPDKLLEEEGIFTYLFQPSAHALSRTLTSAQLWFYSGPSAAPNHSAPAVLTLSPQGRVPVVATASRTPEHWTVFDFGPDALPQLAQPLFVLLVRCPGCPCLADGDKMPFLVATTRAKAAGRARRSAVPWSPAALSLLQRPSEDVAAHTNCRRASLNISFEELGWDNWIVHPSSFVFHYCHGNCAEGHGLSHRLGVQLCCAALPGTMRSLRVRTTSDGGYSFKYETVPNILAQDCTCV", "text": "FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MTVNDKKRLAIIGGGPGGLAAARVFSQSLPNFEIEIFVKDYDIGGVWHYPEQKSDGRVMYDHLETNISKKLMQFSGFPFEENVPLYPSRRNIWEYLKAYYKTFIANKDAISIHFSTEVTYLKKKNSQWEITSKDELRTTKSDFDFVIVASGHYSVPKLPTNIAGLDLWFDNKGAFHSKDFKNCEFAREKVVIVVGNGSSGQDIANQLTTVAKKVYNSIKEPASNQLKAKLIETVQTIDSADWKNRSVTLSDGRVLQNIDYIIFATGYYYSFPFIEPSVRLEVLGEGVTGDKHSSVNLHNLWEHMIYVKDPTLSFILTPQLVIPFPLSELQAAIMVEVFCKSLPITTTFDSNACGTHNFPKGKDLEYYAELQELLNSIPRRVGHFEPVVWDDRLIDLRNSSYTDKEERNVLLAEHAQALKKKKAPYFLPAPHT", "text": "FUNCTION: Flavin-dependent oxidation of thiol-containing compounds. Probably required for the correct folding of disulfide-bonded proteins. SIMILARITY: Belongs to the FMO family."}
{"protein": "MNEYIKGLPKAELHLHIEGTLEPEMMIDIGKRNGVPLPYPDAEAAREAYAFKDLQSFLDIYYQAASVLLCEQDFYDLTMAYLKKARSQNVRHAEIFFDPQTHTSRGIAFDTVITGINNALRDGEQNLGITSKLIMCILRHLSQDEGLKTLEQALEYKGVIAGIGLDSSELGNPPDKFRSLYERAHKEGFLTVAHAGEEGHADYIWQALNTLHVARIDHGVHCMEDETLIHTLVERQIPLTVCPLSNVRLGVFSSMEEHNLKKMLDRELSVTVNSDDPAYFGGYVNENYLAVQQALTLERKDLVRLAVNSFTASFLTQEKKQQHIAAIHTFDKNIT", "text": "FUNCTION: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily."}
{"protein": "MTDFGHDVWWLVVAKAIAIFVFLMLTVLVAILAERKLLGRMQLRPGPNRVGPKGSLQSLADGIKLALKESITPGGIDRFVYFVAPIISVIPAFTAFAFIPFGPVVSVFGHRTPLQLTDLPVAVLFILGLSAIGVYGIVLGGWASGSTYPLLGGVRSTAQVISYEVAMGLSFAAVFLYAGSMSTSQIIAAQDRVWYIFLLLPSFVIYLISMVGETNRAPFDLPEAEGELVAGFHTEYSSLKFAMFMLAEYVNMTTVSALAATLFLGGWHAPWPLNLWHGANAGWWPVLWFTAKVWGFLFMYFWLRATLPRLRYDQFMALGWKLLIPVSLVWVLIAAVIRTLRNQGYQYWTPALVVSSIVVAAILVMSLRKPFSTPNAVTKARRRGKQPAAGPDEQGALEPLFPTPPLPMKPLAQPVGASKENARG", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MANSSPVYDWFQERLEIQDIADDVTSKYVPPHVNIFYCLGGITLVCFLIQFATGFAMTFYYKPTVTEAYNSVSYLMTDVSFGWLIRSVHRWSASMMVLMLILHVFRVYLTGGFKRPRELTWVTGVVMAVITVAFGVTGYSLPWDQVGYWAVKIVSGVPAAIPVVGDFMVELLRGGESVGQTTLTRFYSLHTFVLPWTLAIFMLMHFLMIRKQGISGPL", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family. PetB subfamily."}
{"protein": "MLHISRLGLFLALFAIVMHSVNLIKYTSDPLEAFKTVNRHNWSDEQREHFYDLRNLYTTFCQRNLSLDCFTQILTNVFSWNIRDLQCKSAVNLSPLQNLPRAETKIVLSSTAANKSIVASSFSLFYLLFATLSTYTADPPCVELLPFKILGTQLFDIKLTDESLQMAISKFSNSNLTRSLTPFTPEIFFNYTSFVYFLLYNTTSCIRSNDQYFEHSPKPINVTTSFGRAIVNFHSILTTTPSSTPSSTSASITSPHIPSTNTPTPEPSPVTKNFTELQTDTIKVTPNTPTITAQTTESIKKVVKRSDFPRPMYTPTDIPTLTIRRNATIKTEQNTENPTENPKSPPKPTNFENTTIRIPETFESTTVATNTTQKLESTTFATTIGIEEISDNIYSSPKNSIYLKSKSQQSTTKFTDTEHTTPILKFTTWQDAARTYMSHNTEVQNMTENFIKISLGETMGITPKEPTNPTQLLNVKNQTEYANETHSTEVQTVKTFKEDRFQRTTLKSSSEPPTVQTLSVTPKKKLPSNVTAKTEVQVTNNALPSSNSSHSITKVTEEPKQNRMSASTHGEINHTEIPRMTPILNAHTWEKSTTPQWPFTAETSLTTSSKSAILTWSNLLTTPKEPLTNTSLRSTNHITTQLTTSNRTQSAKLTKAHVSSQTTNIYPQTITERSTDVKKKSSTESREANKTLPGNDYRVTDKNSHNHPDNLTTKAYSTQNATHYTYNERHDLNNTDST", "text": "SUBCELLULAR LOCATION: [80 kDa Glycoprotein O]: Virion Host cell membrane. SIMILARITY: Belongs to the herpesviridae U47 family."}
{"protein": "MAAAGGGATRGARMLAERIRAERKVLEGAARETSRKNAPTIVYLRELKSQVVREDPELVLVNKPHGLPVHGGPTVERSVASLLPALAKHHFGWKAEPLKLCHRLDRDTTGALILARTTEAAERVQQALREREVHRVYWALCLGTPSPREGILDIPIMEKETSGPQKHYKMALSPRFRVSEEGAVERVRVPRSAHEAVTRYRTLGAASGASLVELHPITGVKHQLRVHLALGLNCPILGDHKYSHWGRLAPQKPPDSVLRALGLTVPQARTLSLHLHAVQLTLPSSDGSTPIVLQCPLPYTFRKTLRKLRIPPPDLESLQPPPTD", "text": "FUNCTION: Catalyzes uridine to pseudouridine isomerization (pseudouridylation) of different mitochondrial RNA substrates. Acts on position 1397 in 16S mitochondrial ribosomal RNA (16S mt-rRNA). This modification is required for the assembly of 16S mt-rRNA into a functional mitochondrial ribosome. Acts on position 39 in mitochondrial tRNA(Phe). Also catalyzes pseudouridylation of mRNAs in nucleus: acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions. Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing. SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Cytoplasm Note=Mainly localizes to mitochondrion. Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. Also found in nucleus and cytoplasm. SIMILARITY: Belongs to the pseudouridine synthase RluA family."}
{"protein": "MATSYGFFSPSVPSSLNNKISPSLGINGSGFCSHLGISKRVFCSSIEASEKHAAAGVSSSESRVSRLVNRGCKLVGCGSAVPKLQISNDDLSKFVETSDEWIATRTGIRQRHVLSGKDSLVDLAAEAARNALQMANVNPDDIDLILMCTSTPEDLFGSAPQVQRALGCSRTPLSYDITAACSGFMLGLVSAACHVRGGGFKNVLVIGADALSRFVDWTDRGTCILFGDAAGAVVVQACDSEEDGMFAFDLHSDGGGGRHLNASLLNDETDAAIGNNGAVTGFPPKRPSYSCINMNGKEVFRFAVRCVPQSIEAALQKAGLTSSNIDWLLLHQANQRIIDAVATRLEVPSERVLSNLANYGNTSAASIPLALDEAVRSGKVKPGNIIATSGFGAGLTWGSSIIRWG", "text": "FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. KAS III catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the thiolase-like superfamily. FabH family."}
{"protein": "MISSHPEIELAGFIEQTCLKPTATADDVRQMCWEAQRYRFAAVCVAPVYAPLAVELLHKQKPQVFTVVGFPLGLATAPCKLFEAQEAAARGVTGLEVMVNLGAIKSGHYNAIYEELGQIVDAVGCEVRAILELNLLDATERRHVAEVCLDVGVTALKTSAGWSGPVRPEDILGLRRILRNQLGIKVAGGIHTLNQALELLAAGANRLGTGRGVEILREQHALGKTA", "text": "FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily."}
{"protein": "MEVCLPNGHQIVDWINNAFEGRVSIYSAQQGWDKTISAQPDMMVCGGAVVCMHCLGVVGSLQRKLKHLPHHKCNQQLRQQDYVDVQFADRVTAHWKRGMLSFVSQMHAIMNDVTPEELERVRTDGGSLAELNWLQVDPGSMFRSIHSSWTDPLQVVEDLDTQLDRYWTALNLMIDSSDLVPNFMMRDPSHAFNGVKLEGEARQTQFSRTFDSRSNLEWGVMIYDYSELERDPLKGRAYRKEVVTPARDFGHFGLSHYSRATTPILGKMPAVFSGMLTGNCKMYPFIKGTAKLRTVKKLVDAVNHTWGSEKIRYALGPGGMTGWYNRTMQQAPIVLTPAALTMFPDMTKFGDLQYPIMIGDPAVLG", "text": "FUNCTION: The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3. FUNCTION: Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2/PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding (By similarity). SUBCELLULAR LOCATION: Virion Note=Found in the outer capsid. Each subunit is positioned with the small lobe anchoring it to the protein mu1 on the surface of the virion, and the large lobe, the site of initial cleavages during entry-related proteolytic disassembly, protruding outwards (By similarity). SIMILARITY: Belongs to the orthoreovirus sigma-3 protein family."}
{"protein": "MSVENLKNSLPEYAKDLKLNLSSIARTTVLNEQQLWGTLLATAAATKSASTLKEIASEAADNLSAEAYNAALGAASIMGMNNVFYRTKGYLDGKYDDLRAGLRMNIIGNPGVDKADFELWSLAVSAINGCNHCLEAHENTLRQEGVDREVIFEAIRAGSIVAGVAQAVEANEILSAAQV", "text": "FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity. SIMILARITY: Belongs to the AhpD family."}
{"protein": "MVLGLLAFIWLMRAWRQSLKIWVDVPSIGKDGILGQWITALQWQQKARSLIQEGYEKHGHYAFKIATPSRWEIFICNEKMIKEYKNLMDDKFSANAVTADMFQTKWTAPGAAEGVHKIPIPLLAKALTWQRNRSSVTGDTYFKEFVTEFLHAWEVETKITSEGPYEFCCFETGTRIVAHLTAKSLVGHPLCRDPEIIDLFAGYGNAVPSSGFLIAMFPGILKPLVAKFCEAPKMSDRLDRIFLSEMKERQLQTGSDASDIMSWLWHWTQENEPGKYSEVDIVRSITSAVFGAIHTTTQVLVHCLFELATRPEYVEPLRQEVQQAVENHGGWEKEGIESMLKLDSFIKECQRFNPLDSGSLARCATNDFTFSNGLKVAKGTYVFAPNAPVLFDERFYPNPHQFDGYRFYRLGQQTGKPQGFRFVATNSNYLQFGDGRHTCPGRYMAADEIRLMLGHILLHYDITTKENEGRPKNWFFKKILFPDMKGVIVLKKRAEVRAVNK", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes janthitremanes such as shearinine K or shearinine A (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in janthitremane biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:26213965). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3-geranylgeranylindole (3-GGI) (PubMed:26213965). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline (PubMed:26213965). Paspaline is subsequently converted to 13- desoxypaspaline by the cytochrome P450 monooxygenase janP, via beta-PC- M6 in a series of alpha-face oxidations (Probable). The cytochrome P450 monooxygenase janQ is proposed to carry out sequential beta-face oxidation steps at C-7 and C-13 of 13-desoxypaspaline to form paspalicine and paspalinine respectively (Probable). The indole diterpene prenyltransferase janD may then convert paspalinine into shearinine K which is substrate of janO and/or additional enzymes for oxidation and cyclization to generate shearinine A (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MPKNKKRNAPHRGGGGGGGSGAATSAATAGGPHRTVQPFSDEDASIETMSHCSGYSDPSSFAEDGPEVLDEEGTQEDLEYKLKGLIDLTLDKSAKTRQAALEGLKNALSSKVLYEFVLERRMTLTDSIERCLKKGKSDEQRAAAAVASVLCIQLGPGFESEEILKTLGPILKKIICDGAASIQARQTCATCFGVCCFIATDDITELYSTLECFENIFTKSYLKEKDTNVTCSTPNTVLHISSLLAWTLLLTICPINEVKKKLELHFHKLPSLLSCDDVNMRIAAGESLALLFELARGMESDFFYEDMDSLTQMLRALATDGNKHRAKVDKRKQRSVFRDVLRAVEERDFPTETVKFGPERMYIDSWVKKHTYDTFKEVLGSGMQYHLQTNEFLRNVFELGPPVMLDAATLKTMKISRFERHLYNSAAFKARTKARSKCRDKRADVGEFL", "text": "FUNCTION: Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand- induced signal. SIMILARITY: Belongs to the IFRD family."}
{"protein": "MTYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKENNIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPIDVLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGIDLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWFFISGSV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase family."}
{"protein": "MKTLLILTILAMAITIGTANMQVDPSSQVQWPQQQPVPQPHQPFSQQPQQTFPQPQQTFPHQPQQQFPQPQQPQQQFLQPQQPFPQQPQQPYPQQPQQPFPQTQQPQQLFPQSQQPQQQFSQPQQQFPQPQQPQQSFPQQQPPFIQPSLQQQVNPCKNFLLQQCKPVSLVSSLWSMIWPQSDCQVMRQQCCQQLAQIPQQLQCAAIHTIIHSIIMQQEQQEQQQGMHILLPLYQQQQVGQGTLVQGQGIIQ", "text": "FUNCTION: Gliadin is the major seed storage protein in wheat. SIMILARITY: Belongs to the gliadin/glutenin family."}
{"protein": "MKFVLLFGVLLVALFSYSSAEMLDDFGQADEDELLSLIEKEEARAKECTPRFYDCSHDRHSCCRSELFKDVCTCFYPEGGDNEVCTCQQPKHLKYMEKAAGKAKKFGGKIKKWFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 01 subfamily."}
{"protein": "MACLRKLKEDIQVLEKLFPKNHNRFQILSASVDELSMKFINAENKGIIVTANIQENYPRQPPIWFSESDDVPVIGMSLQRLTETEESTNILHQVHRLVSDLCSFYNLQMPCELPQIAPPVRDDIDEGRGSDISDTTSEPIDDDMAGDGEVDDDDEEEEDDEDADGDIEIVEMAEEDPTSQHDVGVSKEGLDMLDKVSKINRQQHLDGKVQGSITATDRLMKEIRDIHRSEHFKNGIYTFELEKEENLYQWWIKLHKVDEDSPLFEDMKKLKKDHNQDHLLFSFTFNEKFPCDPPFVRVVAPHINQGFVLGGGAICMELLTKQGWSSAYSIESCILQIAATLVKGRARISFDAKHTSTYSMARAQQSFKSLQQIHAKSGWYTPPKTEG", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (Potential). Required for the maintenance of neuromuscular function (PubMed:12763049). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MTGCCTVLGAFLFEYDTPRIVLIRSRKVGLMNRTVQLLILAYVIGWVFVWEKGYQETDSVVSSVTVKAKGVTMTNTSKLGFRIWDVADYVIPAQEENSVFIMTNMVITMNQTQGLCPEIPGKTTVCETDANCTAGSAGTHSSGVATGRCVSFNGTLKTCEVAAWCPVEDDTEVPKPAFLKAAENFTLLVKNNIWYPKFNFSKRNILPNITTAYLKTCIYDAKTDPFCPIFRLGKIVESAGHSFQDIAIEGGIMGIQIKWNCNLDRAASFCLPRYSFRRLDTRDLAHNVSPGYNFRFAKYYSDLKGAEHRTLIKAYGIRFDIIVFGKAGKFDIIPTMINIGSGLALLGVATVLCDVIVLYCMKKRYYYREKKYKYVEDYEQGLGNQMEQ", "text": "FUNCTION: ATP-gated nonselective transmembrane cation channel permeable to potassium, sodium and calcium. Activated by extracellularly released ATP, it plays multiple role in immunity and central nervous system physiology (By similarity). Could also function as an ATP-gated cation channel of lysosomal membranes (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the P2X receptor family."}
{"protein": "MNVIFSLASFVKNMYNASLNQRNLISLPFNFMLNFAPVFIWLSIFKRAGLIPIRLRPDIHSKFAFFADQFLFGDYWHELTVQLPDNTSKLFFWSFISSSAFLLVFLICIPFAIWYYIYYIKHVNYNLLEWFANIFHYPCKRKQRPIQKRFRTIFIPFALPLFTFVILNIDHFFAYQSDANFTKTKDLLAWFSYVILHLTAPILTAVYLYVFQPPGTLKCFSFALGLQNIAGVLTHLLVPMASPWFTHLYGIDDTEHVNYTQEGFAAGLIRVDSHLGTHLNTKGFHMSPIVFGAVPSLHSAIAFQCFLFLVSRSTSLKHRFSNAGGFTMHNNDSSTFKLSEEDSEDEGDNSIPPTIGPNDLEMEPLGTVEPVDISNERSSSPSSSFTVSSNERSTGGGDGSIINSNGNKKPLQFVHLYDEDTNFTNKWIFKIVNDGFIPKFWAILYIILQWWATMYLDHHYRFDLFVGVLYAMTSFIIINWFVLQPKVLKKWIHIRLGDKVDTRNEARTFGMRVFCGTKMEWFFDPLA", "text": "FUNCTION: Catalyzes the addition of a phosphorylinositol group onto mannosyl phosphorylinositol ceramide (MIPC) to form mannosyl diphosphorylinositol ceramide (M(IP)2C), the major sphingolipid in membranes of S.cerevisiae. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein."}
{"protein": "MHLFINMIFLINIVFIISIIFIERRNPQTTWAWILILTFLPILGFIIYILFGQNITREKNFKRKILDDKTKQKYLNSFKSHYKLDNISLKYKDLIMMNFNNDNSTYTQRNDIDLYFDANSLFEEMIDEINKAEKFIHMEFYIFKSDEIGKKILQALTKKAKEGVEVKLLVDSIGNSIHKKDIDKLKAAGGDFKIFFPGFCKYINLRINYRNHRKILIIDSKVAFLGGFNIGDEYLGKDKNIGHWRDTHTKIKGLAINDLEGRFLLDWSYANESDLDIDLKKYFINPHSTDLPKKIIGAQIVSSGPDHTEQQIKNGYFKIINSAKKNLFIQTPYFVPDEPMLEALRLAALSGVDVKIMLPGNPDHKFMGWIANSYFESLLNAGAKIYLYEKGFLHAKTIVADSSICSVGTANMDIRSFSLNFESNIFIYNEAISKSMEEQFFKDLKVCTKVTLESFEKRSIISRIGESITRLVSPLM", "text": "FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase subfamily."}
{"protein": "MKKIAVYTSGGDAPGMNACIRAAVRAGHYHNLEVYGIVRGYDGMINGNFIELDNRAVSNIIQKGGTILKSARSEEFRSPEGRRKAFDQIQKFGIDGLVAIGGNGTFTGAELFYNEYQIPCVGAPGTIDNDLYGSDFTIGYDTAVNTCLAAIDKIRDTADAHERVFFIEVMGRDTGYIAVRSAISGGAEMAIIPEFPYDKNVVINRLKHGTSDTKASHIIIVAEGHQEGRASMIARDIKEALPQLDCRVTTLGHVQRGGGPSAADRVLASRLGLATVEGLLEGRANVMAGIIDHKVVYTPFIDTITKRKPINEDLLSLAEKLNGRSYKV", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub- subfamily."}
{"protein": "MSTPNSYDDEELEELLRRKAAQEQKRIEEERKRKAELESQKESILRVILTPEARQRLTNIKLVKPEFAESLENQLIALAQSGRIKIPITDEELKQILEQISQQNRRDFKIQIRERGWK", "text": "SIMILARITY: Belongs to the PDCD5 family."}
{"protein": "MTLAVKCPILGFEETKNMEFSTIDEVFVRLKSLDGKDFSFVLINPYLIRPDYEFDIPTYYQELLSLTPESNMKIFNIVAIAKSIEESTVNFLAPVVINLDNNTMVQVILDTVNYPDFFQADQIANYIKK", "text": "FUNCTION: Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. FUNCTION: Overexpression leads to increased levels of FlaA and FlaB, but levels of FlaC remain stable (PubMed:27353476). Involved in post- transcriptional regulation of flagellin biosynthesis (PubMed:27353476). FUNCTION: Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum (Probable). Antagonizes CsrA-mediated translational repression of flaA in a promoter-independent manner, leading to expression of FlaA and probably other flagellar genes. Binds to FlaA, which releases CsrA to repress translation of flaA mRNA. Also has a negative effect on flaA transcription, and influences the localization of flaA mRNA to the poles of short, probably elongating, cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FliW family."}
{"protein": "MKWLKHFQSLHTKLVIVYVLLIIIGMQIIGLYFTNSLEKELTQTFKNNISQYAKQIEINIEKVYDEDNAINAQKEVQNLLNEYANRQEIEEIRFIDKDQIIMATSKQSTRSLINQKANDNSIQKALSLGEINSHTVLKDYGNGKQRVWVYNLPVKTSNDGTIGDVYIEADINDVYNQLSNINQIFIVGTGISLLITVILGFFIARTITKPITDMRNQTVEMSKGNYTQRVKIYGNDEIGELALAFNNLSKRVQEAQANTESEKRRLDSVITHMSDGIIATDRRGRVRIVNDMALTMMGTMKEDIIGDHMLKVLKLEEDFSLDEIQENNDSFLLDINENEGIIARVNFSTIVQETGFVTGYIAVLHDVTEQQQVERERREFVANVSHELRTPLTSMNSYIEALESGAWKDGELAPQFLSVTREETERMIRLVNDLLQLSKMDNESEQITKEIVDFNMFINKIINRHEMSAKDTTFVREVPTETIFTEIDPDKMTQVFDNVITNAMKYSRGDKRVEFHVKQNALYNRMTIRVKDNGIGIPINKVDKIFDRFYRVDKARTRKMGGTGLGLAISKEIVEAHNGRIWANSVEGQGTSIFITLPCEVLEDGDWDAE", "text": "FUNCTION: Member of the two-component regulatory system WalK/WalR. WalK functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to WalR. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MDTNTLLLILANIIVIIGLARLIGLLFARFQQPPVIGEIIAGIMLGPSLLGLLSPALEKSFFPATTQPFLYLLSEIGLIFYMFLVGLELNPQYLRQKLKVAILTSNVSIFFPFVLGIVLSFFVLYSLNQPNKTSFIPFALFIGAAMSITAFPVLARILKDTGLDKTPLGTLGLTCASVDDISAWCLLAIAIAVTRTDNIFGAFPTLLGIIVYTVFMVTLGRKFFKYILRNYGQKNYLSQGLLTFIYIMVILSAMLTEWIGIDVIFGGFILGAILPKNTNLSTELATKTEDFVSTFLLPIFFAYSGLSTDLGLLNKPYLWAVCALVVAAAIAGKYCGVYVTTRALGVEKQEAKALGWLMNTRGLTELIILNVGLKLGVISPVIFTMFVIMAIITTIITSPLVVKIYPAPAH", "text": "FUNCTION: Na(+)/H(+) antiporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family."}
{"protein": "MYNIFQLKNNHLFRINEKDKISFLNNIIWIDIIDSCGDGHNYIPNILLHQKIKFFELKDINKTTRFFKDKNGLHIHSFFFSYNSQEQIDNSSVFFTIHNGCLYTSRKKEFPVFCMYQKYLHNHLLINGNAYELLLNLFEVKLDDLTNKIEHIYATLETLSSVIMNGQQIDEYDHALSDLAILENIGWKIRVNLLDTERAIKFLIRKVKLPVSQQKYANDILNEITLLLPHNEYVFHQISSLTQSAMGFINIEQNRIIKIFSVIFLPPTLIASSYGMNFKFMPELQWSFGYPSAIILMILSGLAPYIYFKYKNWL", "text": "FUNCTION: Mediates influx of magnesium ions (By similarity). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family."}
{"protein": "MHALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVLFTEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH", "text": "FUNCTION: TRAPP plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network Endoplasmic reticulum Cytoplasm Nucleus. SIMILARITY: Belongs to the TRAPP small subunits family. TRAPPC4 subfamily."}
{"protein": "METLFNGTLTVGGRDQESTGFAWWAGNARLINLSGKLLGAHVAHAGLIVYWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGYGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGVYHSLIGPETLEESFPFFGYVWKDKNKMTNILGYHLIMLGIGAWLLVWKAMYFGGVYDTWAPGGGDVRIITNPTTNAAVVFGYLLKSPFGGDGWIVSVDNMEDIIGGHIWIGTLCILGGLWHIYTTPWPWARRAFVWSGEAYLSYSLGAISLMGFIACCMSWFNNTAYPSEFYGPTGPEASQSQAFTFLVRDQRLGANVASAQGPTGLGKYLMRSPTGEIIFGGETMRFWDFRGPWLEPLRGPNGLDLNKLKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINAVNFVSPRSWLATSHFVLGFFFFVGHLWHAGRARAAAAGFEKGIDRLDEPVLSMRPLD", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily."}
{"protein": "MAALDSLSLFTGLGLSEQKARETLKNTVLSAQLREAATQAQQTLGSSIDKATGTLLYGLASRLRDPRRLSFLVSYITSRKIHTETQLSAALEYVRSHPLDPINTEDFEQECGVGVVVTPEQIEEAVEAAINRHRAKLLVERYHFSMGLLMGEARAALKWADGKMIKHEVDMQVLHLLGPKTETDLEKKPKVAKARPEETDQRTAKDVVENGEVVVQTLSLMEQLRGEALKFHKPGENYKTPGYVTTPHTMDLLKQHLDITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRDQAYVCHQRGEELKGHNPLPSPWRDRPIEESLLLFEAMRKGKFAEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDTWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLEPLQVVITNFPATKALDIQVPNFPADETKGFHQVPFGSTVFIERMDFKEEPEPGYKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLKVTCRRADAGEKPKAFIHWVSQPLTCEIRLYERLFQHKNPEDPAEVPGGFLSDLNPASLQVVEAALVDCSVALAKPFDKFQFERLGYFSVDPDSNQGQLVFNRTVTLKEDPGKV", "text": "FUNCTION: Glutamine--tRNA ligase. Plays a critical role in brain development. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MRQSIKGRALRHFTLSTGKSAGRNSSGRITVFHRGGGSKRLQRKIDLKRSTSSIGIVERIEYDPNRSSRIALVRWIEGVLPGRQRKFKTIEEFALPRKILESTTATIFCLFSFSSLSSPLAQGETASLSFGSSLGFPRIAVAGAKPAFFAERMREKKIGKKTFSLCEIRKWRTHCVLWAHRIKRKAALSWQSLRQQKTLELVGAAEHNESKLKADQGSLLPRQVLAYALCSGRPSYLHASRSFYKALLPVEASRFGSLPAKPPIGEGPKDGAYKVDRAPVTYILASHQLEAGNMVINCDCSKPSKSGFLRPAQNAHTYLRFQELGRTVNKGRVEGGSQLAASWPRPPAYRHEILDLNSKVGNSIPLADIRMGTWVHDIECHPGQGAKLARAAGTYAKIIKEPASQCLVRLPSGVEKLIDSRCRATIGIVSNPNHGARKLRKAGQSRWSGRRPIVRGVAMNPVDHPHGGGEGRTKGGRPSVSPWGKPTKAGFRAGVGVGKRRI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
{"protein": "NTVSSFQVDCFLWHVRKRFADLELGDAPFLDRLCRDQKSLRGRSSTLGLDIETATRAGKQIVERILEEESDETLKMTIASAPAFRYPTDMTLEEMSRDWFMLMPKQKVAGSLCIRMDQAIMDKNIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTNEDVKNAIGDLIGGLEWNDNTVRVSETLQRFAWRSSNEGGRPPLPPKQKRKMARTIESEV", "text": "FUNCTION: Inhibits post-transcriptional processing of cellular pre- mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in the host nucleus and are no longer exported to the cytoplasm. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism. Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated RIGI ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Also binds poly(A) and U6 snRNA. Inhibits the integrated stress response (ISR) in the infected cell by blocking dsRNA binding by EIF2AK2/PKR and further phosphorylation of EIF2S1/EIF-2ALPHA. Stress granule formation is thus inhibited, which allows protein synthesis and viral replication. SUBCELLULAR LOCATION: Host nucleus Host cytoplasm Note=In uninfected, transfected cells, NS1 is localized in the nucleus. Only in virus infected cells, the nuclear export signal is unveiled, presumably by a viral protein, and a fraction of NS1 is exported in the cytoplasm. SIMILARITY: Belongs to the influenza A viruses NS1 family."}
{"protein": "MASGGGGCSASERLPPPFPGLEPESEGAAGGSEPEAGDSDTEGEDIFTGAAVVSKHQSPKRATSLLPINNGSKENGIHEEQDQEPQDLFADATVELSLDSTQNNQKKMPAKTLISLPPQEATNSSKPQPTYEELEEEEQEDQFDLTVGITDPEKIGDGMNAYVAYKVTTQTSLPLFRSKQFAVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKVGKEDSSSAEFLEKRRAALERYIQRIVNHPTMLQDPDVREFLEKEELPRAVGTQTLSGAGLPKMFNKATDAVSKMTIKMNESDIWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTAQFAKSLAMLGSSEDNTALSRALSQLAEVEEKIEQLHQEQANNDFFLLAELLSDYIRLLAIVRAAFDQRMKTWQRWQDAQATLQKKREAEARLLWANKPDKLQQAKDEILEWESRVTQYERDFERISTVVRKEVIRFEKEKSKDFKNHVIKYLETLLYSQQQLAKYWEAFLPEAKAIS", "text": "FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Can sense membrane curvature and has in vitro vesicle- to-membrane remodeling activity. Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1). Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN. Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (By similarity). SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans- Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium Note=Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles. Colocalized with F-actin at the leading edge of lamellipodia in a KALRN-dependent manner. SIMILARITY: Belongs to the sorting nexin family."}
{"protein": "MNVTLVEINIKPERVDEFLEVFRANHEGALREPGNLRFDVLQDPEVKTRFFIYEAYKDDEAVLAHKKTPHYLACVEKLEEMMSQPRQKRSFIGLLPQV", "text": "FUNCTION: Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5- phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5- phosphonooxypentane-2,4-dione (P-HPD). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LsrG family."}
{"protein": "MTKAVLTSISQLALKALLYEVSLSPKPGLVDRFDNGAHDDMSFMTFIDSMIALSPFFQAYIETGFAYAKEEPLLLFNRLRQLGQKAEETMFCATQGINTHKGLNFSMALLLGATGAYLARTPHLMTDLGCFSKEDTLAICRLVKPMTAHLIQTDLGHLNTKKEFTYGEQLFVTYGIKGPRGEASEGFTTLTDHALPYFRQMISQNDPETSQLRLLVYLMSIVEDGNLIHRGGIEAWKGVKADMRLLLQQDLSTTDLRLALSSYNQCLINQHLSPGGAADLLALTFYFAFLEKLL", "text": "SIMILARITY: Belongs to the CitG/MdcB family."}
{"protein": "MLLCDTNIWLALALSGHVHHRASRAWLDTINAPGVIHFCRATQQSLLRLLTNRTVLGAYGSPPLTNREAWAAYAAFLDDDRIVLAGAEPDGLEAQWRAFAVRQSPAPKVWMDAYLAAFALTGGFELVTTDTAFTQYGGIELRLLAK", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB41 (By similarity). FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB41. SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient starvation. SIMILARITY: Belongs to the PINc/VapC protein family."}
{"protein": "MAKFGSRNKSPKWISNGCCFLLGAFTALLLLWGLCSFIIPIPNTDPKLNSVATSLRSLNFPKNPAATLPPNLQHDPPDTTFYDDPETSYTMDKPMKNWDEKRKEWLLHHPSFGAAARDKILLVTGSQPKRCHNPIGDHLLLRFFKNKVDYCRLHNYDIIYNNALLHPKMNSYWAKYPVIRAAMMAHPEVEWVWWVDSDAVFTDMEFKLPLKRYKNHNLVVHGWEGLVRLNHSWTGLNAGVFLIRNCQWSLEFMDVWVSMGPQTPEYEKWGERLRETFKDKVLPDSDDQTALAYLIATDNKDTWREKIFLESEYYFEGYWLEIVKTYENISERYDEVERKVEGLRRRHAEKVSEKYGAMREEYLKDNKRRPFITHFTGCQPCNGHHNPAYNANDCWNGMERALNFADNQILRTYGYHRQNLLDKSVSPLPFGYPAA", "text": "FUNCTION: Galactomannan galactosyltransferase (GMGT) involved in galactomannan biosynthesis in seed endosperm. GMGT specificity is an important factor regulating the distribution and amount of alpha-1,6- galactose (Gal) substitution of the beta-1,4-linked mannan backbone. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 34 family."}
{"protein": "MDTERHATLLLDLVWPEVDEKAQGFIYAKDFPLVVSRMEEILNRGKLERDRAQLVSETGREILRKFGSDQEFFKVYKEDFRELFDGLVGTSFKSAVKSCAGDGVLDRLQDSQAVDGIQDEKTSSHALQEEVMRLREQVRVLSSKNDEKDREITARDEIIADLQGKDASPAGSPRSLQRMRTLQARVTSLEDELSFRDEVIREKDRELLNLTKRVGEFKDKYQFLEREFQFYKGHREQKSPDSIKEATRHEFIISELRRKITEQSEIIGQMRMQVEAKPGALHPQGIGSTAGLPLNLPLRLVLRLIIGAILAYLAFDIGIRSLKAVGGLFGSSSPATLTPKSELSWWEQNTLLSKLLWFFKDLFDTYNLDAGRDEVVSANYDKLFGV", "text": "FUNCTION: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. SUBCELLULAR LOCATION: Nucleus membrane; Single-pass membrane protein Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. SIMILARITY: Belongs to the MPS2 family."}
{"protein": "MTISYEAVRDFLYREARYLDDKQWESWLEMYAPDATFWMPAWDDRDQLTEDPQSQISLIWYGNRSGLEDRVFRIKTERSSATIPDTRTSHNISNLELLEQSDGVCKLRYNWHTMNYRYKTVDHFFGTNFCTLDTCGETPLITAKKVVLKNDYIRQVIDVYHV", "text": "SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family."}
{"protein": "MAAHELKEALETLKETGVRITPQRHAILEYLVNSMAHPTADDIYKALEGKFPNMSVATVYNNLRVFRESGLVKELTYGDASSRFDFVTSDHYHAICENCGKIVDFHYPGLDEVEQLAAHVTGFKVSHHRLEIYGVCQECSKKENH", "text": "FUNCTION: Hydrogen and organic peroxide sensor. Represses the expression of a regulon of peroxide-inducible genes such as katA, ahpC, ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and mrgA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Fur family."}
{"protein": "MKPDIIKKRRPLPSDDEDEYNEEDEMYEDDNNNYEEDEDDDDDDDEDDEDDDENEEELIKQQLSNVSFSSLLKYKKNGPTDKLNLNTITKNLQQQKSFKKEEQQEKEEMNSKNKYKIKRESSDAPVEMTAMKPVSRFRQVVVNKTKMNVRDPRFDSLSGGKYNEDLYRKRYGFLDDVIKRDVERMESTWKQMDDCRERDQLYKKIQSKKSQLKTQQLKDQKRETKNKLWSNEIESVKKGKTPYHISNKTVKQFELQEKFKQLKASNKLDKFMETKRKRISSKEKTFLPQRRSFDQDEN", "text": "FUNCTION: Involved in the early processing steps of the pre-rRNA in the maturation pathway leading to the 18S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRP36 family."}
{"protein": "MAHLSLNQYKCTHIIMHGTCLSGLYPVPFTHKAHDYPHFNIYISFGGPKYCITALNTYVIPLFHHLLSTQFIYTYVNITKKSPLKSPKHKNILSFNDNT", "text": "SIMILARITY: Belongs to the UPF0320 family."}
{"protein": "MSSSNYVTTGQARNLRACMICSIVMTSQRFQNEGCPNCEEFLHLQHSPDQIESCTSQVFEGVITLANPTKSWIAKYQRLDSYVPGMYAIKVSGQLPDDVRSTLEDEYRIQYIPRDGTEVENDA", "text": "FUNCTION: The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Centromere and heterochromatin. SIMILARITY: Belongs to the SPT4 family."}
{"protein": "MPSNMFIQADKKKRLSLDVIGQLEDDLEADPLDYNKWNKLIQQVLAKDKEEQVKSVFNKYLNIFNFDQWCNYINYQLNRGEFQEVEQLFSKCLPITDHVELCRLYVSYVRRTNDVITGGEKARGIVVQAFEFAVTKVGIDISSGDLWNDYLDFLKAWTPAATWEQQQKTDLIRRVYKRFLVIPTEKIEQVWSTYTKWENEVNASSANKFIAEKSSEFMDARSWNTEWHNATERSLRREVIPIGIHNDNNNLVHTQLQLWYKWIALERENKLNLKDDSSVQQRIEYVYKQAIMALPFVPELWFKFNKFWLRSNEEANSNKCIELLNEALVLNPRSYLLTFQLSEMYEKDNTINKATETYDNLITFLTNDYNNINNQIESITNRELNNKKQEENTGEENNNENDDSDNDDNDDDDSFKNPTFQLSEEDALLLSKLQEKKDELNKAITLVYTKLMMACKRSRGIKEARGVFKQARNNFEAIGYEFYVENALMEYHSDNLKTASKIFELGMKHFKKQGEFLLAYLDFLIMINKGESIKVLFEQGLTALLQDVNIENENSNGDITSGANMRLQESKSKENIKKKNCIKKLIKKFSRYQSVYGDLDLIKSLDSRYEEYFPDDDSIELFSDRYRGHSIDVIKHFDLGKEDTSHEEIDTTAQETKRRKIQNPTVDEFTPEVSNNNNQHTNNKDAVQNQQQPQNFVGNTIYNLLRVLPNSSYFGPPSDHLFNNTKLVELFGNLPNVPTE", "text": "FUNCTION: Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation- dependent pre-mRNA 3'-end formation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nucleus and/or cytoplasm."}
{"protein": "MTNVFTIDAFREEVKKKYEPVTIGISEDVTVELKPLLKLGQKAREAVVEAVKEVEDIPDIDEDDEEAEELVDEYSLRICEIVAKVFRLIATKPKKLIAALDEEEDPRIRAELYATVLRTWMVETQLGESRALAELIDKFGGAILSDLSEYHGVDLRDLFRDEDPLSPRYVLNLVIHLPKTGAFYAERRGGQQYRGWDEDRYALADIYDAVQAGNHILLMANRDPKKPKPKAPKAYPRPDDFEKTTPKPGSFAAMVVAAKKAAREKREREEANAE", "text": "FUNCTION: Promotes tail assembly by creating a scaffold for the tail tube proteins. The tail assembly proteins Gp24 and Gp25 would wrap the linear tape measure protein to create a tail assembly scaffold. It would allow polymerization of tail tube protein during which Gp24 and Gp25 are released and therefore are absent from the mature virion. The tail assembly protein Gp25 is produced by a rare -1 ribosomal frameshift. The ratio Gp24/Gp25 is important for proper tail assembly. SIMILARITY: Belongs to the L5likevirus tail assembly protein family."}
{"protein": "MATGLIKAKEYDWKDSNLALFGSDTEKQVKKDSAATEPAWKGAGQKEGLKIWRIVNFKVTEWPQNQHGKFYNGDSYIILNTYKPDPKSNELAYDVHFWIGSQSSQDEYGTAAYKTVELDTFLDDKPVQHREVQGYESELFRNYFKQGLTILEGGAETGFHHVKPTEYKPRLLHFSGQKQQIYVHEVPLVKERLDHKDVFILDLGLTLYQWNGKESSKEEGFKAMQYLGLMRSERPKAEAETLEDESTPESHKFYTSLTGTDEPNLVKPLVKEENQLLKVSDAGGHLKTTEVKRGAVNSKDFSSNDVFILDTGDQCFVWVGKGRFAVGEAEWTRISHAHLMKTCHPLAPIHVIKEGQLCKAFNVAIAA", "text": "FUNCTION: Calcium-regulated protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end- blocking or capping). Can promote the assembly of monomers into filaments (nucleation) as well as sever existing filaments. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the villin/gelsolin family."}
{"protein": "MREALNTGLIDFLKASPTPFHATASLALRLEAAGYQRLDERDSWATVPGGRYYVTRNDSSIIAINLGKQAPLQGGIRMVGAHTDSPCLRVKPQPELQRQGFLQLGVEVYGGALLAPWFDRDLSLAGRVTFRRDGKVESQLIDFKLPIAIIPNLAIHLNRTANEGWQINPQNELPPILAQVAGDERIDFRALLTEQLAREHQLNADVVLDYELSFYDTQDAALIGLNSDFIAGARLDNLLSCYAGLQALLAADSDETCVLVCNDHEEVGSCSACGADGPMLEQTLQRLLPDGDTYVRTIQRSLMVSADNAHGVHPNYADKHDGNHGPKLNAGPVIKVNNNQRYATNSETAGFFRHLCMAEEVPVQSFVVRSDMGCGSTIGPITASHLGVRTVDIGLPTFAMHSIRELCGSHDLAHLVKVLTAFYRSRELP", "text": "SIMILARITY: Belongs to the peptidase M18 family."}
{"protein": "MDTADIVWVEESVSAITLYAVWLPPRAREYFHALVYFVCRNAAGEGRARFAEVSVTATELRDFYGSADVSVQAVVAAARAATTPAASPLEPLENPTLWRALYACVLAALERQTGPVALFAPLRIGSDPRTGLVVKVERASWGPPAAPRAALLVAEANIDIDPMALAARVAEHPDARLAWARLAAIRDTPQCASAASLTVNITTGTALFAREYQTLAFPPIKKEGAFGDLVEVCEVGLRPRGHPQRVTARVLLPRDYDYFVSAGEKFSAPALVALFRQWHTTVHAAPGALAPVFAFLGPEFEVRGGPVPYFAVLGFPGWPTFTVPATAESARDLVRGAAAAYAALLGAWPAVGARVVLPPRAWPGVASAAAGCLLPAVREAVARWHPATKIIQLLDPPAAVGPVWTARFCFPGLRAQLLAALADLGGSGLADPHGRTGLARLDALVVAAPSEPWAGAVLERLVPDTCNACPALRQLLGGVMAAVCLQIEETASSVKFAVCGGDGGAFWGVFNVDPQDADAASGVIEDARRAIETAVGAVLRANAVRLRHPLCLALEGVYTHAVAWSQAGVWFWNSRDNTDHLGGFPLRGPAYTTAAGVVRDTLRRVLGLTTACVPEEDALTARGLMEDACDRLILDAFNKRLDAEYWSVRVSPFEASDPLPPTAFRGGALLDAEHYWRRVVRVCPGGGESVGVPVDLYPRPLVLPPVDCAHHLREILREIELVFTGVLAGVWGEGGKFVYPFDDKMSFLFA", "text": "FUNCTION: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae HEPA family."}
{"protein": "MENQPKLNSSKEVIAFLAERFPQCFSAEGEARPLKIGIFQDLVERVGGEMNLSKTQLRAALRLYTSSWRYLYGVKAGAIRVDLDGNPCGELEEQHIAHARQQLEEAKARVQTQRAAQQAKKREAAAAAGQQDEGVRRERKPRPQQPRRKEGAEQRKPRPVAAKAPREERHTPVSDVSVLTVGQALKVKAGNNAMDATVLEITKDGVRVQLTSGMSMIVRAEHLVF", "text": "FUNCTION: RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ProQ family."}
{"protein": "MSMQIHAKTLTEKTITIDVVSSDTINNVKAKIQDIEGIPLDQQRLIFSGKLLDDGRTLADYSIQKDSILHLALRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGVPPDQQRLIFAGKQLDDGRTLADYNIQKESTLHLVLRLRGGMQIFVRTLTRKTIALEVESSDTTDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLCGGMQIFVNTLTGKTITLEVESSDTIDNVKAKIQDKERIQPDQQRLIFAGEQLEDGYYTLADYNIQKESTLHLVLRLRGGECFGFIFLFLLCFNS", "text": "FUNCTION: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin family."}
{"protein": "MVNDNYNTAEGIDSYYLVNSKHKYSITSPSPLDNLLVLYGLEPIAKSLARTNADGSKGVKLRKSYKNHIQDLPGKHQIVGGQKPIPAGLLDPMVAQAPDIIKELDPELLSRGLRFEKTPINGIPGFNTADLAINDQHTLMRGDDMSENDEFGARRSKRKKKAQNGTDSKRQHI", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 19 family."}
{"protein": "MAGPSTLWETLQALLPHTKEELKLELGEKVEGSVLMLLQEAAELFLGGQRRECLQTCEVLLDYSWEKLNTGPWQHVDKDWRRVYAFGCLLKAVCLCEPPGDAASVAAALKACDMGLLMGAAILGDILLKVAAVLQKYLLSGKRPAPGPSQEPPGTKKARNDHVPIPDVTTERTVPRLHCPSLQYFKKHFLVPGRPVILEGVANHWPCMKKWSLEYIQEVAGCRTVPVEVGSRYTDEEWSQTLMTVNEFISKYIREEPKDIGYLAQHQLFDQIPELKQDISIPDYCCLGDGEEEEITINAWFGPQGTVSPLHQDPQQNFLAQVMGRKYIRLYSPQESEALYPHDTHLLHNTSQVDVENPDLEKFPRFAEAPFLSCVLSPGEVLFIPVKHWHYVRALDLSFSVSFWWS", "text": "FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage. Additionnally, acts as Fe(2+) and 2- oxoglutarate-dependent monooxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established. Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation. Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition. Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation. Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition (By similarity). Regulates the circadian gene expression in the liver (By similarity). Represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a catalytically-independent manner (By similarity). Negatively regulates the protein stability and function of CRY1; required for AMPK-FBXL3-induced CRY1 degradation (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3)."}
{"protein": "MIKKIVTTCFGLVLGLCVFGVGLVAIAILVTYPKLPSLDSLQHYQPKMPLTIYSADGEVIGIYGEQRREFTKIGDFPEVLRNAVIAAEDKRFYQHWGVDVWGVARAVVGNIVAGGVQSGASTITQQVAKNFYLSSEKTFTRKFNEALLAYKIEQSLSKDKILELYFNQIYLGQRAYGFASAAQIYFNKDVRELTLAEVAMLAGLPKAPSAYNPIVNPERAKLRQKYILNNMLEEKMITLQQRDQALNEELHYERFVQKIDQSALYVAEMVRQELYEKYGEDAYTQGFKVYTTVRTDHQKVATEALRKALRNFDRGSSYRGAESYIDLSKGEDVEETVSQYLSGLYTVDKMVPAIVLDVTKRKNVVIQLPSGKRVTLDGRSLGFAARAVNNEKMGESRIRRGSVIRVRNNGGRWVVVQEPLLQATLVSLDAKTGAVRALVGGYDFHSKTFNRAAQAMRQPGSTFKPFIYSAALSKGMTASTMVNDAPISLPGKGANGSVWTPKNSDGRYSGYITLRQALTASKNMVSIRILMSIGVGYAHEYIQRFGFKPSELPASLSMALGTGETTPLKIAEAYSVFANGGYRVSSHVIDKIYGSDGRLRAQMQPLVAGQNAPQAIDPRNAYIMYKIMQDVVRVGTARGAAALGRSDIAGKTGTTNDNKDAWFVGFNPDVVTAVYIGFDKPKSMGRAGYGGTIAVPVWVDYMRFALKGGQGKGMKVPEGVVSSNGEYYMKERMVTDPGLVVDNSGIAAQPSRRIREDKEAGAEDVERGAADEVRQEVQETPVLPSNTGSKQPQLDSLF", "text": "FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family."}
{"protein": "MNLFEKMTDQLHETLDSALALALHHKNAEVTPMHMLFAMLNNSQGILIQALQKMPVDIQALRLSVQSELNKFAKVSQISKQNIQLNQALIQSLENAQGLMAKRGDSFIATDVYLLANMGLFESVLKPYLDAKELQKTLESLRKGRTIQDKNDDSNLESLEKFGIDLTQKALENKLDPVIGRDEEIIRMMQILIRKTKNNPILLGEPGVGKTAVVEGLAQRIMNKEVPKTLLNKRVIALDLSLLVAGAKYRGEFEERLKKVIEEVKKSANVILFIDEIHTIVGAGASEGGMDAANILKPALARGELHTIGATTLKEYRKYFEKDMALQRRFQPILLNEPSINEALQILRGLKETLETHHNITINDSALIASAKLSSRYITDRFLPDKAIDLIDEGAAQLKMQMESEPAKLSSVKRSIQRLEMEKQALEMEKKESNAKRMQEILKELSDLKEEKIQLEAQFENEKEVFKEISRLKMEMESLKKEAERFKRNGDYQQAGEIEYSKIPENKKKEEELQRKWEAMQQNGALLQNALTENNIAEIVSQWTHIPVQKMLQSEKNRVLNIESELQKRVVGQEKAIKAIAKAIKRNKAGLSDSNKPIGSFLFLGPTGVGKTESAKALAQFLFDSDKNLIRIDMSEYLEKHAMSRLIGAAPGYVGYEEGGQLTEAVRRKPYSVVLLDEVEKAHPDVFNLLLQVLDEGHLTDSKGVRVDFKNTILILTSNVASGALLEENLSEAEKQKAIKESLRQFFKPEFLNRLDEIISFNALDSHAVINIVGILFENIQKKALERGINITLDEEAKELIAEAGFDRFYGARPLKRALYEMVEDKLAELILEDKVKENDSVAFVVENNEIVPKIK", "text": "FUNCTION: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary for surviving high-temperature stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ClpA/ClpB family."}
{"protein": "MKGTLLLLALLVTGELGFQRTEACIPFFGVYLGILSGNRIGLHTELAPFDPTVEEKEAFEKIQDCYEEEGLKAKTEDMKLMTTILFSSECRSYYTKEVLKNILVKFSKKLTHGS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secretoglobin family."}
{"protein": "MKYCLLCLALALGGCQTNDKLASCKGPIFPLNVGRWQPTPSDLQLSNVGGRHEGV", "text": "FUNCTION: Is essential for the biogenesis of the T-pilus, which is required for virulence and T-DNA transfer to plant cells. When is associated with virB9, might function as a nucleation center for recruitment of VirB proteins during assembly of the T-DNA transfer machine (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. Note=Also associated with the T-pilus when is a homodimer, possibly at the pilus base."}
{"protein": "MAFGDYPAEYNPKVHGPYDPARFYGKADVPFGQVKLGEIGAWLGRRNKTPNAVAGAVSRAWWRWQHKYVFPKRAGIAPFFQLTVASMTFFYLINYTKLKHHRNYKYH", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane. SIMILARITY: Belongs to the ATPase F chain family."}
{"protein": "MSEADPVGEKGPAEDDGEESVPFNPFLHEFEPKGLWQNARFYILGPILFPLRFLLAAVFLFLMWPIAALRVAGLTDKELSCSIRHRRTILHHLIYLLSRTMFFMCGFHWITIRGRRAPASEAPILVVAPHSTFFDPIVTVVCDLPSVVSRVENLNIPVIGALLRFNQSILVSRQDPSSRKKVVEEVKRRATSNGEWPQVLFFPEGTNGNGKVLLKFKPGAFVAGVPVQPVLMRYPNKLPATIWTWKGNGVFKVLWLTMSQFYINLEIEFLPVYHPTAEERADPTLYAFKVQKIMADALAKPATEFELIGDTPVSPLGHLKVALDPKIWELGNILKKAGFSLDSVQGLIDLCLEGVCSRVGLDELAEKLGVTQHDVISRVFNYFNKDAAGMIDFREVSLVLAAQDATRSAEELAKLAFDLFSTCDADGRSLLSADGFASVLRSLLGSPPAESGKVFTELYTYTELQGLTQDGFVRFAIRHPCYRHLFLFYLRPPSSGRRKPPQIQQNGGCSGKNNPGKQSKMD", "text": "FUNCTION: Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates. Prefers long chain acyl-CoAs (C16, C18) as acyl donors (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family."}
{"protein": "MSPAFHPLRTRVGEAIEQSLFRRTDPVPPPRPSGAVTLRADGIAVTRGGRPVLDDVSVDVRIGEVLVLVGPNGAGKSTLLAALSGDQDVHTGTVHLDDRDLGEWTALEMAQRRAVLPQQNTVGFSFTARQVITMGRSPWARTPRSDDDAVAIAEAMRICDVVAFADRPFTALSGGERARVALARVLAQRTETILLDEPTAALDLGHQETVMRLARSRAEQGTAVVVVLHDLALAAAYADRIVVLEQGRVAANGPPADVLSEELLTRVYGHPVEVIEHPVTGATLVLPRRDQR", "text": "FUNCTION: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Heme (hemin) importer (TC 3.A.1.14.5) family."}
{"protein": "MSADYSSEKFKATHLFDEILWHFRSNLSLKTNRRGLATAENSFSGKEAVDFLMIEMPRIIPNNVPERDKMQKFLEFMMDMNVISEAFPKKVKQRRPFSESRIYLFMKTLDELKHPKPRSRRSASFSGARKSAKVAQPASPAATMHRPPKARLPRRLSRSNGNIDKAGIDNSSGGVENHGFDDHKDDEIPKKQRTPKILNRSLESICTEEYTEKREVSEMKEKVYDWLPFFKSRRNHTKVNQPTRRSASLDRNHCVLEQEKAEAALRSQKVTTPPIREAPKDVVFMHPQGPLPAVPSRYQNHRTSIAGSNPALLSRGRMYESIMRRSSVVPVADSVQANNECSFWKTELLGRLEQIYDRTLPCEWASKVDGYDIQWNMIEIDHADGIVKSRCQGLQPDYPQTVIQFMDYLVRYPFVTHKKMDTGLEYNVNRIFITLVNRLEDLNAPLQFDECSLIVNLLCKIDSFAAMLDNGPARRWSKVMISSSASSIEEAGLMVDGFSRDLPACGIRASKYRRRALSPFDNRVNLEIQDEKSYEIREQWLIEAIQLVLLSLPTSRRRKLHKFVTFIQSIETNAVFDLADPSNGSSNNREAAIIGLWTGVCSKCRKQQGMLITAVLLANFQSLFAVPVEFIEQVKRLECEEKDRYSGPRYAKITRSRNDWQPPVPDKPQASPAVFKKPLREVACEKTKKGLFTRLLRK", "text": "FUNCTION: Required for the proper orientation of spindles after the establishment of polarity (PubMed:9477332, PubMed:14534135). May play a role in interactions between the astral microtubules and the cortical cytoskeleton (PubMed:9477332). Required for asymmetric forces on nuclei and spindles (PubMed:9477332). Acts downstream of the PAR signaling as an intermediate that transduces polarity information to the machinery that positions the mitotic spindle, possibly by regulating force generation (PubMed:12223405). Regulates gpr-1/2 asymmetric cortical localization during the first embryonic cell divisions (PubMed:14534135). Acts antagonistically to the gpr-1/2 signaling pathway (PubMed:14534135). Regulates mes-1 expression and/or localization pattern during early embryogenesis (PubMed:11003841). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cell cortex Note=Enriched at the cell cortex during both meiosis and mitosis (PubMed:12223405). Enriched asymmetrically at the cell cortex in 1-cell embryos (PubMed:14534135). Localizes at the contact site between EMS and P2 in interphase and is excluded from the contact site during prophase (PubMed:14534135)."}
{"protein": "MGLRIHFVVDPHGWCCMGLIVFVWLYNIVLIPKIVLFPHYEEGHIPGILIIIFYGISIFCLVALVRASITDPGRLPENPKIPHGEREFWELCNKCNLMRPKRSHHCSRCGHCVRRMDHHCPWINNCVGEDNHWLFLQLCFYTELLTCYALMFSFCHYYYFLPLKKRNLDLFVFRHELAIMRLAAFMGITMLVGITGLFYTQLIGIITDTTSIEKMSNCCEDISRPRKPWQQTFSEVFGTRWKILWFIPFRQRQPLRVPYHFANHV", "text": "FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:22031296). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane (PubMed:22031296). This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (PubMed:22031296). Palmitoylates FYN, regulates its localization in hair follicles and plays a key role in epidermal homeostasis and hair follicle differentiation. Through the palmitoylation of PLCB1 and the regulation of PLCB1 downstream signaling may indirectly regulate the function of the endothelial barrier and the adhesion of leukocytes to the endothelium. Has also a palmitoyltransferase activity toward ADRA1D, positively regulating its activity and expression and may thereby play a role in vascular contraction. May also palmitoylate eNOS and LCK (By similarity). FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (By similarity). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity). Palmitoylates FYN, regulates its localization in hair follicles and plays a key role in epidermal homeostasis and hair follicle differentiation. Through the palmitoylation of PLCB1 and the regulation of PLCB1 downstream signaling may indirectly regulate the function of the endothelial barrier and the adhesion of leukocytes to the endothelium. Has also a palmitoyltransferase activity toward ADRA1D, positively regulating its activity and expression and may thereby play a role in vascular contraction. May also palmitoylate eNOS and LCK (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MHYLYLFISIATEIIGTSFLKTSEGFTKLWPTLGTLLSFGICFYFLSLTIKFLPLNITYATWAGLGLVLTTIISVIVFKENVNLISIISIGLIVIGVVLLNVFGESH", "text": "FUNCTION: Multidrug exporter. Is implicated for the resistance to bacteriocidal quaternary ammonium compounds. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family."}
{"protein": "MDSRPQKVWMTPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAPDDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHTEGRQTQSRPTQNVPGPHRTIHHASAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNRTPTVAPPAPVYRDHSEKRELPQDEQQDQDHTQEARNQDSDNTQPEHSFEEMYRHILRSQGPFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQFYWPVMNHKNKFMAILQHHQ", "text": "FUNCTION: Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response. VP35 binds to and stabilizes monomeric NP, keeping it soluble. Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm. Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid. Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription. Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1. SUBCELLULAR LOCATION: Virion Host cytoplasm. SIMILARITY: Belongs to the filoviruses nucleoprotein family."}
{"protein": "MGQTLSEPVLDKHSSSGGDRWLHFGVSHMQGWRISMEDAHCALLNFTDSNSSNPPTSFFGVFDGHGGDRVAKYCRQHLPDIIKSQPSFWKGNYDEALKSGFLAADNALMQDRDMQEDPSGCTATTALIVDHQVIYCANAGDSRTVLGRKGTAEPLSFDHKPNNDVEKARITAAGGFIDFGRVNGSLALSRAIGDFEYKKDSSLPPEKQIVTAFPDVVIHNIDPDDEFLILACDGIWDCKSSQQVVEFVRRGIVARQSLEVICENLMDRCIASNSESCGIGCDNMTICIVAFLHGRGLEDWYNWITQRVNSGEGPCAPPSYAELRGPNTIADARNLQLEYDHIASHEYGSGDTYDSDSDDETIAYDRYYLH", "text": "FUNCTION: Has an important role in osmotic stability and cell shape control. It may negatively regulate the osmosensing signal transmitted through wis1 map kinase. SIMILARITY: Belongs to the PP2C family."}
{"protein": "MTQEVLEAVKEAKEQSKPRNFTQSVDMIVNIRDLDVKKPENRFNEEVTLPNGRGKEVKIGVIADGELIVQAKDAGVALVINKADLEELGKDRKAAKKAANSVDFFIAQADMMPLVGRFLGPILGPRNKMPKPVPASIKLDPLLERLQSTVKVGIKQQPAIQIIVGSQDMSDEDLAENIETVLTVLDRHLDKGRNQIKSMFIKTTMGPIVRVI", "text": "FUNCTION: Binds directly to 23S rRNA. Probably involved in E site tRNA release. FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA. SIMILARITY: Belongs to the universal ribosomal protein uL1 family."}
{"protein": "MAIASNVVEAGNAVRAEKGRKYFYFRKMIGDYIDTSIRIVATVFLADLLLRLYRCVVEYGSNGRYYLPEDRLWIILRRSCTYNNRSIYLIVGFLLVAFFRISVTGNYRNVMPTTLFLFQMPLYWIWSFTDMDQSTLSYSHWIRDSHGLDYAAGMASNYFHGYLKLSLPERKDDGLKHRLAMYEDKNNVTFGIKRLVILIPDEMFVNGVLESHLLDKAEPLETQFINRAGVYRPFKHDVYRMNKKVNGRTYYFAVEGATPMISFFDATYSNLSGTWQMQELKREIWIKFYKHLKELITTWPETRDLVELIIYNSHDSKGNLVDVGELLVAHMQNKTKTIDEISN", "text": "FUNCTION: Facilitator of innate immune signaling that binds cyclic dinucleotides produced in response to infection by bacteria and/or viruses, and promotes the activation of the NF-kappa-B transcription factor Rel (Relish) (PubMed:29934091, PubMed:29924997, PubMed:30119996, PubMed:33262294, PubMed:34261127, PubMed:34261128). Recognizes and binds cyclic di-GMP (c-di-GMP), a cyclic dinucleotide messenger produced by bacteria such as L.monocytogenes, leading to activation of the peptidoglycan recognition protein (IMD) signaling pathway and activation of Rel (Relish) (PubMed:29924997). Innate immune response is triggered in response to double-stranded RNA from viruses delivered to the cytoplasm: Sting acts by specifically binding cyclic dinucleotides 3',2'-cGAMP and 2',3'-cGAMP produced by cGlr1 and cGlr2 in response to RNA virus in the cytosol (PubMed:34261127, PubMed:34261128). Has a strong preference for 3',2'-cGAMP compared to other cyclic dinucleotides such as 2',3'-cGAMP or 3'3'-c-di-GMP (PubMed:34261127). Upon binding to 3',2'-cGAMP, activates an antiviral immune response, leading to the activation of Rel (Relish) (PubMed:34261127, PubMed:34261128). Activated in brain in response to Zika virus infection, leading to autophagy (PubMed:29934091). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the STING family."}
{"protein": "MKRRSIFMYYCFCFLLKYVAFSNVPNPNTTIGHFEICEVNTSSGDAEECVLENEFGKMFLFICDIDYNEMSKNIVLPSECAKKTYIDHVNPNGTSPEVNTYDIFPDLIAANESQFRDKFYFYGTPYSSKDIDFICLCFSETKPDIKHVMKMSFKKMTKKIKGCDFGDNIPTKKDLTNGKALYENSSCHIYAYPGDVIGINCYKKDINNIYNNNLELQPNNCFHNVYYEDDILLSSKNLIPNSRVIPDPSNDVKLSKMHSYMSYIILPDEINENVKISCACKRDEYIGTMFLYVNTSKNILTSPDNNVEEIAPLNDHYISIGDMWDMGLHENPEQIQGIISNHANKKYYEHMKIYKSNKMDSSDDDESNETESSENESNERTHNGNRANKDANNSEKMTGNRRKKNNSINNTNYYSNYEDDNGINISTHDKYYEDQHFGNNGPLRKKRTFWQNMFGTSSSYYEVFNYFSIAFILIIHMLLL", "text": "FUNCTION: Involved in sporozoite infection of hepatocytes and replication therein. SUBCELLULAR LOCATION: Cell surface Cell membrane; Lipid-anchor, GPI-anchor Note=Present on the surface of sporozoites."}
{"protein": "MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIICPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVSNINILQDNDFGDFGMDDREMMREGSAFEDDMLTTNASNLKLEPEQSTSQLNEKSNHLEYDDQYKDDNFGEGNEGGILDDKLLSNDAGGIFDDPPAMPEEGVAMPEQPVHDDLDDDDNVSMGAPDSPDSVDPVEPLPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNTRLLKLFTRCLTPLVLDDLRKRRKGGEADNLDEFLKEFENPEVPREELRPQDVIDQPILEEASHLQESLMEGSRTHLDDTIMPPPPPKQGVKRDSLQMEPEPMPMMQEAEPQIEMPPPPLPPPLELPPEEPQSISDLIPELNLLPEKEKEKDEEEEEEEEDTTGTEQDQEERRWNKRTQQMLHGLQRVLAKTGAESISLLDLCRNTNRKQAAAKFYSFLVLKKQQAIELTQREPYSDIVATPGPRFHTV", "text": "FUNCTION: [64-kDa C-terminal product]: May promote apoptosis. FUNCTION: [Double-strand-break repair protein rad21 homolog]: As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the prevention of inappropriate recombination between repetitive regions. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity). In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (By similarity). May play a role in embryonic gut development, possibly through the regulation of enteric neuron development (By similarity). SUBCELLULAR LOCATION: [64-kDa C-terminal product]: Cytoplasm, cytosol Nucleus. SUBCELLULAR LOCATION: [Double-strand-break repair protein rad21 homolog]: Nucleus Nucleus matrix Chromosome Chromosome, centromere Cytoplasm, cytoskeleton, spindle pole Note=Associates with chromatin. Before prophase, scattered along chromosome arms. During prophase and prometaphase, most cohesins dissociate from the arms of condensing chromosome, possibly through Polo-like kinase PLK1/PLX1-catalyzed phosphorylation (PubMed:11931760). A small amount of cohesin remains in centromeric regions and is removed from chromosomes only at the onset of anaphase. At anaphase, cleavage by separase/ESPL1 leads to the dissociation of cohesin from chromosomes and chromosome separation (By similarity). SIMILARITY: Belongs to the rad21 family."}
{"protein": "MIWLTLVFASLLSVAGQLCQKQATCFVAINKRRKHIALWLGLALACLGLAMVLWLLVLQNVPVGIAYPMLSLNFVWVTLAAVKLWHEPVSPRHWCGVAFIIGGIVILGSTV", "text": "FUNCTION: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ArnE family."}
{"protein": "MTEHGIKWACEYCTYENWPSAIKCTMCRAPRPSGAIITEEPFKNSTPDVGSMERESGSPLICPDSSARPRVKSSYSMETSTKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSSLRAIPSPIDPCEEYNDRNKLNIKGQHWTCSACTYENCAKAKKCVVCDHPTPNNMDAIELANTDEASSIINEQDRARWRGGCSSSNSQRRSPPTSKRDSDMDFQRIELAGAVGSKEEFELDLKKLKQIKNRMRKTDWLFLNACVGVVEGDLSAVEAYKTSGGDIARQLSADEVRLLNRPSAFDVGYTLVHLSIRFQRQDMLAILLTEFSQHAAKCIPAMVCPELTEQIRREIAASVHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELGTRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYSRWKEWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGFDNRGAGANLNTDDDVTVTFLPLVDSERKLLHIHFLSAQELGNEDQQEKLLREWMDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDGYRQIRPCTALSDGEEDEDDEDE", "text": "FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys- 29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates apc protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of pik3c3/vps34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Enriched in punctate localization in the cytoplasm. SIMILARITY: Belongs to the peptidase C64 family."}
{"protein": "MAWWKAWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPALALQDAQDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP", "text": "SIMILARITY: Belongs to the annexin family."}
{"protein": "MWTQRNAVGNWLLVLTAVIGFITFIWIPQTSAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKNLHTNGCQLHLIPIAVAVSWLMGQLLSR", "text": "FUNCTION: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the quiver family."}
{"protein": "MVETQMDKLGFLLNHIGKQVTTKVLSNAHITQTMKEIILENHSVDGGAAKNASKGKSSPKEKKHWTEFESWEQLSKSKRSFKEYWTERNEIVNTLLLNWDNVRAAIKKFLNDDREWCGRINMVNGVPEIVEIIPSPYRAGENIYFGSEAMMPAEIYSRVANKPAMFVFHTHPNLGSCCGGMPSICDISTTLRYLLMGWTAGHLIISSNQVGMLTVDKRIIVDLWANENPRWLMAQKILDIFMMLTSRRSLVNPWTLRDLKKILQDYGIEYIIFPSNDFFIYEDARLLMFSKKWTNFFTLHELLNDLETIETKATSST", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the asfivirus F317L family."}
{"protein": "MVLYIIGLGLGDEKDVTIKGFEAIKKSSKIYLEAYTSLLGGSTSIEALEKFYEKKIIIADREMVESGCEEMLKESTENDVSFLVVGDPFGATTHTDLVIRAKELSIPVKVIHNASIMNAIGCCGLQLYSYGQTISMVFFTETTKPDSWYDRVKINRVNGMHTLCLLDIKVKEQSIENMCRGRLIYEPPRFMTVNQCIEQLLEIEEIRKEKVYDQDTLCIGLSRVGQDDQQIISGTMKELLDVDFGAPLHSFIICGDMHFIEKEYFETFRVKKN", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis. SIMILARITY: Belongs to the diphthine synthase family."}
{"protein": "MGRRAPRGSPEAAPGADVAPGARAAWWVWCVQVATFIVSAICVVGLLVLASVFRDRFPCLYAPATSYAKANATVEVRGGVAVPLRLDTQSLLATYAITSTLLLAAAVYAAVGAVTSRYERALDAARRLAAARMAMPHATLIAGNVCAWLLQITVLLLAHRISQLAHLIYVLHFACLVYLAAHFCTRGVLSGTYLRQVHGLIDPAPTHHRIVGPVRAVMTNALLLGTLLCTAAAAVSLNTIAALNFNFSAPSMLICLTTLFALLVVSLLLVVEGVLCHYVRVLVGPHLGAIAATGIVGLACEHYHTGGYYVVEQQWPGAQTGVRVALALVAAFALAMAVLRCTRAYLYHRRHHTKFFVRMRDTRHRAHSALRRVRSSMRGSRRGGPPGDPGYAETPYASVSHHAEIDRYGDSDGDPIYDEVAPDHEAELYARVQRPGPVPDAEPIYDTVEGYAPRSAGEPVYSTVRRW", "text": "FUNCTION: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Host Golgi apparatus, host trans-Golgi network Host endosome membrane; Multi-pass membrane protein Host nucleus inner membrane; Multi-pass membrane protein Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. SIMILARITY: Belongs to the herpesviridae glycoprotein M family."}
{"protein": "MPLSAAIKSSLSVSVRADAKGLVGFANTGYNGITVLKQTYWTSFYMKGEYSGTVLLRLTGTDSGTVYGSRNLSVKSTGGKWTQYETTFEANESYVAENEWQLLFDAATAKGHPLHFGLVQLFPPTYKNRTNGLRNDIARPIADLKPKFLRFPGGNNIQADRPGDWHYPNTDALGLDEYLWWCEDMDMVPVLSVWDGKSYGGIVSGEELQPYLDDIKDELEVTLPLTLLSHPLRAYLTPNTNEQYLLGPPSTPFGALRARNGHPDPWPIQYIEIGNEDDYSGGCDTYPDRLVQIYDTIHASYPNLTLIANNMDENCLPEIPLPGLWHDYHYYRSADDLVAMFNYWDNHDRGDRVLVGEYGCRNDSNPDGVFWSFMQGSCAEAVHMIGLERNSDVVMMAAYAPLLQHFGYTQWSVCTPSASLAYLGIHPADRGEEQPTLFGFESRPNSLTLSTSYYVNRMFSTNQGSTVHKVHSTAGFGPLYWVATSNETAYQVKLANYGAANQTVNIRVPGVGRGVLEMISGPKDASNLPGDIKIVPVSRNIRAGKEGYTVHMPPWGVAVLVVVFK", "text": "FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 51 family."}
{"protein": "MMNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATADPLRYNLAAMVARFNETGRSQVLAKRMKGDLSEYSVIQTKEPLDNEGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEQLLHE", "text": "FUNCTION: May play a role in stationary phase survival. FUNCTION: May play a role in stationary phase survival. SIMILARITY: Belongs to the UDPGP type 2 family."}
{"protein": "MKYSLCTISFRHQLISFTDIVQFAYENGFEGIELWGTHAQNLYMQEYETTERELNCLKDKTLEITMISDYLDISLSADFEKTIEKCEQLAILANWFKTNKIRTFAGQKGSADFSQQERQEYVNRIRMICELFAQHNMYVLLETHPNTLTDTLPSTLELLGEVDHPNLKINLDFLHIWESGADPVDSFQQLRPWIQHYHFKNISSADYLHVFEPNNVYAAAGNRTGMVPLFEGIVNYDEIIQEVRDTDHFASLEWFGHNAKDILKAEMKVLTNRNLEVVTS", "text": "FUNCTION: Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence (PubMed:17189355, PubMed:18955706). Catalyzes the conversion of 3- dehydroshikimate to 3,4-dihydroxybenzoate (3,4-DHBA) (PubMed:18955706)."}
{"protein": "MNSIHIKKKSNRSFRRRKVFGNEKEFDLEELDDNDIRLRQALEATKRRKIRNSIIGINAEKLLNQETKKEKQLNTANEPHEANDQTSAQSSKLIEAQLPTVEDRFAKQTNEVDINTHLLNFVEKKLKQERLAQNYSENGETNALNTKNESTVQNIKNSLHPNEHSFIRDAAALGAIREVDLGIISTDVDNLKNGRKRQKKRARMKEKLDSKALRTSEDAARDEFIEKMLKPISQDEESKGIYRRFRVYKDGTQD", "text": "FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of introns featuring long spacing between the branchpoint and 3'-splice site (PubMed:36095128). Assists the splicing of several components involved in chromatin organization, such as several shelterin complex subunits (PubMed:25245948, PubMed:36095128). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TLS1 family."}
{"protein": "RPSFNSWG", "text": "FUNCTION: Mediates visceral muscle contractile activity (myotropic activity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kinin family."}
{"protein": "MAAIRNLLILTMLLIVCVSWNADAAPGAAPSIALDKRANENFSLREQEQPICEHCWKQPPPRRCPKFCLE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-04 family."}
{"protein": "MASADHTRDPCPYVILNDFGAAFSMGTIGGAIWHSIKGWRNSPPGEKRISAIAAAKTRAPVLGGNFGVWGGLFSTFDCAVKGVRRKEDPWNAIIAGFFTGGALAVRGGWRATRNGAIGCACILAVFEGLGIALGRMNAEYNRPVAPVIPDAPASGSTSAAPAAV", "text": "FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family."}
{"protein": "MSTPDNRSVNFFSLFRRGQHYSKTWPLEKRLAPVFVENRVIKMTRYAIRFMPPIAVFTLCWQIALGGQLGPAVATALFALSLPMQGLWWLGKRSVTPLPPAILNWFYEVRGKLQESGQVLAPVEGKPDYQALADTLKRAFKQLDKTFLDDL", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0208 family. SIMILARITY: Belongs to the UPF0208 family."}
{"protein": "MSKTMIEKVDEVLETEVCAADQKMINLFGRLNNRKHELMREKKAKQEDLEKATDSQDDLFIADDDSKFKYSMGEAFLEVNKEDAESLIEKYINKLEEDIKKIDSDINDINEKHKELKVILYAKFKNSINLEE", "text": "FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). SIMILARITY: Belongs to the prefoldin subunit beta family."}
{"protein": "MKYKFRNVVLGGTFDTLHSGHVKLLATATLIGDRILIGLTSDSFASTYKQYKVRPFSVRLANLRNLMSLIAPEREVAYVEIHDPYGPAVFDPRLEAIVASIETAPRALQINDERAKRGLRPMEVFIISTVRDGYGHTLSSTYIRRVLERPESKQS", "text": "FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic CoaD family."}
{"protein": "MAEGLVLKGTMCAHTDMVTAIATPVDNSDVIVTSSRDKSIILWKLTKEDKSYGVAQRRMTGHSHFVQDVVLSSDGQFALSGSWDGELRLWDLATGESTRRFVGHTKDVLSVAFSTDNRQIVSASRDRTIKLWNTLGECKYTISEADGHKEWVSCVRFSPNTLVPTIVSASWDKTVKVWNLQNCKLRNTLAGHSGYLNTVAVSPDGSLCASGGKDGVILLWDLAEGKKLYSLEAGSIIHSLCFSPNRYWLCAATENSIRIWDLESKSVVEDLKVDLKAEAEKTDGSTGIGNKTKVIYCTSLNWSADGNTLFSGYTDGVIRVWGIGRY", "text": "FUNCTION: Minor component of the RACK1 regulatory proteins that play a role in multiple signal transduction pathways. Involved in multiple hormone responses and developmental processes (PubMed:18947417). MAPK cascade scaffolding protein involved in the protease IV and ArgC signaling pathway but not the flg22 pathway (PubMed:25731164). SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily."}
{"protein": "MMDIFLAILPAIFWGSIVLFNVKLGGGPYSQTLGTTFGALIFSIVVYIFMKPVLTPTVIGVGVVSGLFWALGQANQLKSIDLMGVSRTMPISTGLQLVATTLFGVIVFHEWSTTISVVLGILALVCIIIGVILTSLQSEEEKNAEQAANFKRGIVILLISTVGYLVYVVVIRLFNVDGWSALLPQAVGMVLGGILLTFKHHPFNKYAIRNIIPGLIWAAGNMFLFISQPRVGVATSFSLSQMGIIISTLGGILILGEKKTKRQLTGIVVGIVFIIAAGIMLGIAKS", "text": "FUNCTION: Involved in the uptake of glucose. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GRP transporter (TC 2.A.7.5) family."}
{"protein": "MSRLFMILLVICVITLGTDASQAEDSGTEKRSWPVPDAFLKAFQSWPLTDPDLKAGFKVNSAQRVAHGYGK", "text": "FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin NSf-1 superfamily."}
{"protein": "MLSPKKTKYRKQHRGRLKGACSRGNRISFGKFAIQALEPAWITSGQIEAGRRAITRTTRRGIKIWIRIFPDKPITKKPADTRMGSGKGDPKFWVAVVKPGRMLYEMGRISESVARKAAQNVAYKMCLHTRFVKI", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL16 family."}
{"protein": "MSSYFVNPLYSKYKAAAAAAAAAAAAAAGEAINPTYYDCHFAPEVSGRHAAALQLYGNSAAGFPHAHPHPHPHPSPPPGCGGGGGPGPGQDYFHAGAGSPTAAYQAAPPPPHPPPPPPPPPCGGIACHGEPAKFYGYDNLQRQPIFTTQQEAELVQYPDCKSSSGNIGEDPDHLNQSSSPSQMFPWMRPQAAPGRRRGRQTYSRFQTLELEKEFLFNPYLTRKRRIEVSHTLALTERQVKIWFQNRRMKWKKENNKDKFPASRPEAKDGDPKKEVSGLEEDGAEGCPTN", "text": "FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family."}
{"protein": "MASLNSDVIMGESSSISVPSSSSKNSKRFELKKWSAVALWAWDIVVDNCAICRNHIMDLCIECLANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDVCEWEFQKYGH", "text": "FUNCTION: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The SCF complex plays a crucial role in regulating response to auxin and is essential for growth and development. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, to the complex and brings it into close proximity to the substrate (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the RING-box family."}
{"protein": "MAVRASEISRVYEAYPEKKATLYFLVLGFLALIVGSLFGPFQALNYGNVDAYPLLKRLLPFVQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPARELNMRPNMGLMWLSWWMAFIGLVVAALPLLANEATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWRRWKAANPGKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEFAGRLRGGRGLFGWIRALPWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAQRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIAQVPDAYPHAAVPMVFNVLAGIVLLVALLLFIYGLFSVLLSRERKPELAEAPLPFAEVISGPEDRRLVLAMDRIGFWFAVAAILVVLAYGPTLVQLFGHLNPVPGWRLW", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the heme-copper respiratory oxidase family."}
{"protein": "MVPLRLVLLLHIIHFSCENEVGSAANNGSAQLYNYRKIHLPDDHIPYYLHSNRHVAALCLQDLHCPYKQHLQNLNSCWGYEKTCAEGHRFGYPVCDQVDFGWAKTIEESQQVFWRQADFGYVKERLAETQILCRPQEQGDSMLACSQNLQHCRATNLYLDLRHPRRGQENFKEDFLQEGEIGGHCDLDKQALLSQGAWKSPLQSWFAELQSYSSFKFKPIEDAHCDIIIEKPTYFMKLDAGVNMYHHFCDFVNLYITQHVNNSFSTDINIVMWTTSVYGYGDLFSDTWKAFTDYEITHLKAYDNKRVCFKDAVFALLPRMRYGLFYNTPLISHCHGSGLFRAFSQHVLHRLNITQHPATEAKIRVTILVRSTEFRKILNLDELVQALEAVPTFQVKVVDYKYRVLGFLEQLSITHNSDIFIGMHGAGLTHLLFLPDWAVVFELYNCEDARCYLDLARLRGIQYMTWEKGDKVFPQDKGHHPNLGEHPKFTNYAFDVEEFLRLVQQGATYVSRHSKWPLRRTRDEL", "text": "FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the glycosyltransferase 61 family."}
{"protein": "MAQAIIGAIAASAAGSALGAGIQAGAEAALQSQRYQQDLALQRNTFEHDKDMLSYQVQASNALLAKNLNTRYSMLIAGGLSSADASRAVAGAPVTRLIDWNGTRVAAPRSSATTLRSGGFMAVPMPVQPKSKTPQSSGFSNPAYDMSTVSSRTSSWVQSQNSLRSVSPFHRQALQTVWVTPPGSTSSSSVSSTPYGVFNTDRMPLFANLRR", "text": "FUNCTION: Minor structural protein present in one or two copies per virion. Stabilizes capsid protein VP1 by protecting it from disassembly and degradation. May play a role in RNA genome packaging (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the norovirus VP2 family."}
{"protein": "MHQSLTQQRSSDMSLPDSMGAFNRRKRNSIYVTVTLLIVSVLILTVGLAATTRTQNVTVGGYYPGVILGFGSFLGIIGSNLIENKRQMLVASIVFISFGVIAAFCCAIVDGVFAARHIDLKPLYANRCHYVPKTSQKEAEEVISSSTKNSPSTRVMRNLTQAAREVNCPHLSREFCTPRIRGNTCFCCDLYNCGNRVEITGGYYEYIDVSSCQDIIHLYHLLWSATILNIVGLFLGIITAAVLGGFKDMNPTLPAMNCSVENTHPTVSYYAHPQVTSYNTYYHSPPHLPPYSAYDFQHSSVFPSSPPSGLSDEPQSASPSPSYMWSSSAPPRYSPPYYPPFEKPPPYSP", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM255 family."}
{"protein": "MASRQPEVPPALAPSGPLSKMSLPIGMCRRAFSYDDALEDPAPMTPPPSDMGSIPWKPVIPERKYQHLDKTEEGAASVSSLAVTPSTATDSSDKAPVVKAKATHIIMNSLITKQTQESIQRFEQQAGLRDAGYTPHKGLTTEETKYLRVAEALHKLKLQSGETTREEKHPASAQSSPSSTPHSSPKQKSRGWFPSGSSTALPAPNPHSMDPGGGNDRNSADKWSLFGPRPLQKSDSGFAIQAYKGAPKPSPMEVMRAQATRAGEDPAVFKPPKMDVPVVEGKKQPPRTHNLKPRDLNVLTPTGF", "text": "FUNCTION: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the P33MONOX family."}
{"protein": "MSPRPLRALLGAAAAALVSAAALAFPSQAAANDSPFYVNPNMSSAEWVRNNPNDPRTPVIRDRIASVPQGTWFAHHNPGQITGQVDALMSAAQAAGKIPILVVYNAPGRDCGNHSSGGAPSHSAYRSWIDEFAAGLKNRPAYIIVEPDLISLMSSCMQHVQQEVLETMAYAGKALKAGSSQARIYFDAGHSAWHSPAQMASWLQQADISNSAHGIATNTSNYRWTADEVAYAKAVLSAIGNPSLRAVIDTSRNGNGPAGNEWCDPSGRAIGTPSTTNTGDPMIDAFLWIKLPGEADGCIAGAGQFVPQAAYEMAIAAGGTNPNPNPNPTPTPTPTPTPPPGSSGACTATYTIANEWNDGFQATVTVTANQNITGWTVTWTFTDGQTITNAWNADVSTSGSSVTARNVGHNGTLSQGASTEFGFVGSKGNSNSVPTLTCAAS", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family."}
{"protein": "MDTELLKTFLEVSRTRHFGRAAESLYLTQSAVSFRIRQLENQLGVNLFTRHRNNIRLTAAGEKLLPYAEMLMSTWQAARKEVAHTSRHNEFSIGASASLWECMLNQWLGRLYQNQDAHTGLQFEARIAQRQSLVKQLHERQLDLLITTEAPKMDEFSSQLLGYFTLALYTSAPSKLKGDLNYLRLEWGPDFQQHEAGLIGADEVPILTTSSAELAQQQIAMLNGCTWLPVSWARKKGGLHTVVDSTTLSRPLYAIWLQNSDKNALIRDLLKINVLDEVY", "text": "FUNCTION: Negatively regulates the transcription of the flagellar master operon flhDC by binding to the upstream region of the operon. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MSKSRSLVRLLQLASPMLPVGAYSYSQGLEWGIESGEVHDLESAQAWIGDVLQVYQGGFELPVLSRCYRAWQRGDVEALNEWNAFYLAGRDNAEALAESRQMGYSLKRLLLEFEELSGAWATMLEALPNASFPALYAGISQAWEIEEQDALQAYAWSWLENQASAAMKAVPLGQVAGQKILLGVAGKIPVLVEAAIQMQDHEISNFCPALTIAGCRHETQYSRLFRS", "text": "FUNCTION: Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UreF family."}
{"protein": "MTVQIDELDDKDLDEIIANGTLDGAKQGAVDSETMIQYYRHLFPWKYLFQWLNHGPVVTNDFAHREFAFTLPNDAYIRYLSFSNWEELKKEALNLCPSRFEVGPVYSANPRDRKTIRKSTFHPLKKELVFDIDMTDYDDVRTCCSKTNICEKCWPFITIAVQVLDICFHEDFGFKHILWVYSGRRGIHAWICDEIACSLDDRSRRMIASYLQVVVGNPQGGVRLINNLKRPLHPHLTRSLNILKSAFVKIVLEDQDPWASKEGAENLLKLLPDKDLASALRKKWEVDPERSSKNKWSDIDTVLASGSIASISPSVIAIAKQDIVLTYLYPRLDVEVSRHLNHLLKSPFCVHPGTSRVCVPIDIERMDSFNPLKVPTVNDLLQELDKNSQNDNGHGPTMETNTTENQKDNARGQSNKGHGFSTSLNPYTLYFKSFSSQLFKETVGNKRKHENLEF", "text": "FUNCTION: Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12 and two primase subunits, the catalytic subunit spp1/pri1 and the regulatory subunit spp2/pri2) is recruited to DNA at the replicative forks (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic-type primase small subunit family."}
{"protein": "MPKFYCDYCDTYLTHDSPSVRKTHCSGRKHKENVRDYYQKWMEEQAQSLIDKTTTAFQQGRIPPNLFSAPPLGGPMIPPPHPSMMGPPPPGMMPVGPPPGMRMPMGGHMPMMPGPPMMRPLPHPMMVPTRPVMPRPDR", "text": "FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family."}
{"protein": "MYRALWLLARSRRLVRPPASALASAPGLSGAAVPSFWPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAVTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK", "text": "FUNCTION: [Isoform Mitochondrial]: Catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH. FUNCTION: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (By similarity). Experiments in other species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable). FUNCTION: [Isoform Cytoplasmic]: Catalyzes the dehydration of L-malate to fumarate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism (By similarity). Also plays a role in DNA repair by promoting non-homologous end-joining (NHEJ). In response to DNA damage and phosphorylation by PRKDC, translocates to the nucleus and accumulates at DNA double-strand breaks (DSBs): acts by catalyzing formation of fumarate, an inhibitor of KDM2B histone demethylase activity, resulting in enhanced dimethylation of histone H3 'Lys-36' (H3K36me2) (By similarity). SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol Nucleus Chromosome Note=Translocates to the nucleus in response to DNA damage: localizes to DNA double-strand breaks (DSBs) following phosphorylation by PRKDC. SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase subfamily."}
{"protein": "MSFVIAVPEALTMAASDLANIGSTINAANAAAALPTTGVVAAAADEVSAAVAALFGSYAQSYQAFGAQLSAFHAQFVQSLTNGARSYVVAEATSAAPLQDLLGVVNAPAQALLGRPLIGNGANGADGTGAPGGPGGLLLGNGGNGGSGAPGQPGGAGGDAGLIGNGGTGGKGGDGLVGSGAAGGVGGRGGWLLGNGGTGGAGGAAGATLVGGTGGVGGATGLIGSGGFGGAGGAAAGVGTTGGVGGSGGVGGVFGNGGFGGAGGLGAAGGVGGAASYFGTGGGGGVGGDGAPGGDGGAGPLLIGNGGVGGLGGAGAAGGNGGAGGMLLGDGGAGGQGGPAVAGVLGGMPGAGGNGGNANWFGSGGAGGQGGTGLAGTNGVNPGSIANPNTGANGTDNSGNGNQTGGNGGPGPAGGVGEAGGVGGQGGLGESLDGNDGTGGKGGAGGTAGTDGGAGGAGGAGGIGETDGSAGGVATGGEGGDGATGGVDGGVGGAGGKGGQGHNTGVGDAFGGDGGIGGDGNGALGAAGGNGGTGGAGGNGGRGGMLIGNGGAGGAGGTGGTGGGGAAGFAGGVGGAGGEGLTDGAGTAEGGTGGLGGLGGVGGTGGMGGSGGVGGNGGAAGSLIGLGGGGGAGGVGGTGGIGGIGGAGGNGGAGGAGTTTGGGATIGGGGGTGGVGGAGGTGGTGGAGGTTGGSGGAGGLIGWAGAAGGTGAGGTGGQGGLGGQGGNGGNGGTGATGGQGGDFALGGNGGAGGAGGSPGGSSGIQGNMGPPGTQGADG", "text": "SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily."}
{"protein": "MYRFIIFFSLLALTASKVSEPEKDDEIAVKIPTKRSVSEPPKDDDIAVKIPMRKKRGIAIHPWQWESHLWPNAEVPYDIASHYTATERGIILSAMEAFRDVTCVRFRPRRSTDKHYLQINKHYQLERCFSYIGRQSSRWLFGTRDGKVETRMKLDPSCLLYNGRGTVMHELMHILGFYHEHQRDDRDRRIGGSASHYNFKIYQRAKSYYMGGYDANSIMHYNFGSVPWQKRDYFSPSDIRNINTLYKCNNRVVSKFPSTIPSTSTTTTKAPQFELFEKKQIESNSLFRRRRS", "text": "FUNCTION: Metalloprotease. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MEAEESSSSVVPLPQDVQSVVRGGFRCLLCGVNIPNRPSLTDHLSGRRHVRLHEERDKRNQQQERSVYVSNFPRETSEEQLRDVFQKISPVRNIVMDKDRGLYAIVEFESKDGMCAALEEPQIKLSGKRLRVKPREKKEFQRKKGGSPRTLQPPDPEALSKELLNCADVEQQIKKLVSLCSPSHHESHLRELLLSLLQETFTEFFPGCQLLPFGSSVNGFEISGCDLDLYLDLGDDEAENVEGKAEKEIQNREESSTDMEVSMEDPETERKEEEMEIGNSKNDEDEDVTPGLSLKGLSSEEILEVVGKVLRHCVPGVHGVQSVPTARRPVIHFQHKTSGLRGDVTLNNRLALRNSSFLRLCSDLDARVPQLVYTVRYWARVNQLAGNPFGGGPLLNNYALTLLVFFFLQTRNPPVLPTLVHLREETANEVPQVIDGWDCSFPSDPAQVKESGNQQSLSSLLSEFFSFYASLDLHLLILCPCNGLTIPLPFSSPPPAWSEGFRLGPLNIQDPFELSHNVCGNVSSRAARRFISHCAAAARICRTPNYNLHSTSHPWGITPILLPPPTERECVGRGGTEISIPLGGVSPEKTYAAVSKVFVDVLLCTLEEGREDSCQEGKALELSTKHAKAQCKVEKNEVGGELGEQEVPCKAEQNNTKEASKQKSIFKTEEGMTESARRKREMTEPCMSDMTNGKKRRLEFTRGIWDHHLATSAMEEEMCGEAHKDSKTKIDYSNNGTAQWELLVWHRVWEGRRKERRRKQKGEADGVELEIAVSQALALEKEDKCDGPLMKLILTAQLTVKESLQLYLTPKFDPQGLSSTFFHFLESYLPRMVAQIQGCGDPV", "text": "FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus speckle. SIMILARITY: Belongs to the DNA polymerase type-B-like family."}
{"protein": "MKNGIAFRTIGEEFDGFLLIKESTRGTTSNGKPFLTLILRDASGEIEAKLWDATKDDEETLIPEQIIQVTGEINQFRGKHQLKILSIRLSQPMDNVQVTDFLGKAPMEKEELAEKLTEAIFEMENPKIQRLVRAFIKKYQEELLTYPAATKNHHEFASGLAYHVVSMLAIGKELHKLYPEINRDLLYAGIILHDIGKIKELSGVVSTTYTLEGKMLGHIPMMVEEIGLMANELQIEGEEVLILKHLVLSHHGKAEWGSPTPPLVREAELLHLIDLIDAKMNMLGRALEKIQPGEFTERLFAMDNRAFYKPNFEENEG", "text": "FUNCTION: Shows a 3'-5' exoribonuclease activity. SIMILARITY: Belongs to the YhaM family."}
{"protein": "MMSPTPEDDRDLVVVRGRLRMMDNGAEHDRERRSYTAWPHLCCGCTIGIILTMFVIATTLLLASLFAFSYMSLESGTCPKEWIGLGYSCMRVAGNNATELEALDMCAQHNSKLVDFTNAKTLVEAIVPFGSTNASFGNIFRLRDSRSTCILPTIGGPISVDCPRTCSVVCQRPRPLSTAASIIRDARIYLRLERRDYYEVYSSILSNAIMK", "text": "SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the herpesviridae HHV-1 UL45 family."}
{"protein": "MNSKYLFVFLILNVIFIDLCQGFLFNVIPHAINATASLIKKGTRRRELGSQYDYLQDFRKRELDLDDLLSKFPDY", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
{"protein": "MAERDHYHTIDDPNVPCNFYDTVNLTGHTVFPNGSYDYYGTIVPAELVGTYDYIHSSLTERIEVREHVRGCVCKFKSCLNICCPWRQVFNSEVDGCIIDHSDNRTWPDPPMLNITFRNDSTILVNMFAQFAIQSFRPCPKMFSLQPETSHWDDYLLFENGSMLRVDDQQLIRKNEFCMVPTYVNESDMFYTIHPANCDMQDDNSTVKIINAYAMMFSIPFMMLTIAVYLLIPELRNQHGKSLVCYLVGLTVGYTSLCYVQLYQVDATGDACKVFGYTAYFFFMGAYMWLSVISFDLWHNFRGTRGINRFQEKKRFLFYSLYSWGIAVVFLAFTYIAQELTNLPAYLKPGIGDGVYCWLDMSNWAAMIYFYGPILVIVVANTIMFIMTAIKIHGVQREMARIIASENSTKNLRTEKDKFGLFLRLFLIMGITWLTELISYFVGSDKGWSKLFYISDLANAMQGFLIFMLFVMKKKVKHLITNRCSSVRDGSNQRQSQYSTKTTSSSVANLSLHEKPSVEKPLVISSSVDPQKTTIFR", "text": "FUNCTION: Involved in biological aging and stress response. Essential for adult survival (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth subfamily."}
{"protein": "MARGLKKHLKRLNAPRHWMLDKLGGAFAPKPSSGPHKSRECLPLILILRNRLKYALTYREVIAILMQRHVMVDGKVRTDKTYPAGFMDVVSIPKTNEDFRLLYDTKGRFCLHAITGDETKFKLCKVRSVQFGQKGIPYLNTYDGRTIRYPDPLIKANDTIKLDLESNKIVDFIKFDVGNVVMVTGGRNRGRVGVIKNREKHKGSFETIHVQDAAGHEFATRLGNVFTIGKGTKPWVSLPKRKGIKLSIIEEARKRLAAQNAA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family."}
{"protein": "MSDVPGEDSPTHFYPVNFENYLRPKQSIKCQPLQRFKKPNERATNLYRNLKRLKILRWYNRVSKRFEEFPLPKFLGFLQARNDDGLCKRKTGFEIYCEMASIHGFHIFVGAKTWQRILWWLLICNAVLLSFTLVIMSLSMSKETPTIRFIDTMMKPTAEVPFPAVTICGFNTKEWMNSSQIVNQRNASWLELLEDLALPICPQIKICQWDNRMVNCLDQLQPIWTLDQRLCCSFNYNKQLFSSYLGVSFVLRSNDEILQSSKSAGFEVLIHESHEIPNGATPRVFVPGESDAHIMLRPYINRFTKNLKGLSLQKRGCYFSTERRLILSDVYNQINCLAECRTESILKSCGCIPPKSPIEKSWLICDLKQMQCVIDFDHDEIISGEQKNCDCLPPCEFNRYEFQSDIRFIKGMINNSIVNTSNQETTNEVRVRVYYDSAIAEELLLDVYENWLTFIGTFGGITGLFMGCSFVSVFELIFFSCVRPTCNWLTRQQILWRRRRNQRVGITESRSLGPAN", "text": "FUNCTION: Part of a complex that plays a role in tracheal liquid clearance. In both larvae and adults, contributes to the behavioral response to salt. Probable role in sodium transport. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family."}
{"protein": "MLDKVKNVIVVLSGKGGVGKSTVSTQLALALRATGHKVGLLDIDLCGPSVPHLLGLEGRDIYQCDDGWVPIYTDESKTLAVMSIGFLLKNRNDPVIWRGPKKTMMIKQFLTDVKWEDLDYLIIDTPPGTSDEHITVMECMREVPCNGAIIVTTPQGVALDDVRKELTFCKKTGIKVLGIVENMSGFVCPHCSDCTNIFSSFGGAELAQLAQVPLLGTLPIDPRVGVLAGSTASVLNELADSSTAQVLRSIVQHLDGLTALPTSA", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily."}
{"protein": "MSIPQSNTSLSAVIAVDQFDPSSGGQGVYDTPLGITNPPIDELLDRVSSKYALVIYAAKRARQINDHYNQLGEGILEYVGPLVEPGLQEKPLSIAMREIHADLLEHTEGE", "text": "FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. SIMILARITY: Belongs to the RNA polymerase subunit omega family. SIMILARITY: Belongs to the RNA polymerase subunit omega family."}
{"protein": "MSESDETKSISSLISSSSSSRPKKYICTYEGCDKAYNRPSLLEQHLRTHSNDRPYKCTVEDCDKAFFRKSHLETHIVSHSEKKPFHCSVCGKGVNSRQHLKRHEITHTKSFKCTFENCQEAFYKHQSLRHHILSVHEKTLTCKQCNKVFTRPSKLAQHKLKHHGGSPAYQCDHPGCFKNFQTWSVLQFHIKQSHPKLKCPKCGKGCVGKKGLSSHMLSHDDSTMIKIWTCDYCDVGKFAKKNELVEHYNIFHDGNIPDDLLKETEVKKLENLLDQGSKLNNLHELETEKLKVEEDEEDEEDSLDEKRSDVRSDSMSAQRSIKSFTASLEGSKSVSKLISNSGKKINCPKNNCDRMFSREYDLRRHLKWHDDNLQRIESFLNSIEKEETPEGEPLVKKARMDLLPNETSVISR", "text": "FUNCTION: Transcription factor required for transcription of 5S rRNA by RNA polymerase III. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTTLNSTPRADGFHMPAEWAPQTQVWMVWPERPDNWRLGGKPAQAAHVAIAKAIARFEPVTVAVSAAQYDNARARLDMPNIRVVEMSSNDAWVRDSGPTFVINDRGELRGVNWEFNAWGGFDGGLYAPWNLDSQVGSKVLEIERCPRYATQGFVLEGGSIHVDGEGTLITTEECLLNRNRNPHLTREQIEAVLSDYLAVDKIIWLPDGLFNDETDGHVDNFCCYIRPGEVLLAWTDDPEDPNYPRCHAALSILENTRDAQGRAFIVHKMPIPGPLFATEEECAGVDQVHGSQERNPSVRLAGSYVNFLIVNGGIIAPSFDDPMDEKAREILQKLFPEHEVVMAPGRELLLGGGNIHCLTQQQPAPFKA", "text": "FUNCTION: Mediates the hydrolysis of agmatine into N- carbamoylputrescine in the arginine decarboxylase (ADC) pathway of putrescine biosynthesis, a basic polyamine. SIMILARITY: Belongs to the agmatine deiminase family."}
{"protein": "MKSIRYYLAFAAFIALYYVIPVNSRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSLGQWLFGATNFGVRAGAILTTLLAAALVAWLTFRLWRDKRTALLASVIFLSLFAVYSIGTYAVLDPMIALWLTAGMCCFWQGMQATTRTGKIGMFLLLGATCGLGVLTKGFLALAVPVVSVLPWVIVQKRWKDFLLYGWLAVLSCFVVVLPWAIAIARREADFWHYFFWVEHIQRFAMSDAQHKAPFWYYLPVLLAGSLPWLGLLPGALKLGWRERNGAFYLLGWTIMPLLFFSIAKGKLPTYVLSCFAPIAILMARFVLHNVKEGVAALRVNGGINLVFGIIGIVAAFVVSSWGPLKSPVWTHIETYKVFCVWGVFTVWAFVGWYSLCHSPKYLLPAFCPLGLALLFGFSVPDRVMESKQPQFFVEMTQAPLASSRYILADSVGVAAGLAWSLKRDDIMLYGHAGELRYGLSYPDVQNKFVKADDFNAWLNQHRQEGIITLVLSIDKDEDISALSLPPADNVDYQGRLVLIQYRPK", "text": "FUNCTION: Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 83 family."}
{"protein": "MAAEKKTEVLEKKISIKPRYKMTRGIQVETLMKCADNSGAKILRCIGVKRYRGRLNRLPAAAPGDICVVSVKKGKPELRKKVHYAILIRQKKIWRRTDGSHIMFEDNAAVLINNKGELRGAQIAGPVPREVADMWPKISSQASSIN", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
{"protein": "RKVAVMGAAGGIGQPLSLLLKLSPQVTELSKY", "text": "SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family."}
{"protein": "MVLTGPPQRESVSMVKRVSMLDQHKKSSCARVRVAVRLRPYMEEKEEDKVPTACVRGLDSHSLEIVNWRNQLETMQYQFDAFYGDSASQREIYMGSVCHILPHLLIGQNASVFAYGPTGAGKTHTMLGNPDQPGVIPRAVRELLQMTRMAASAPENENWTYTITMSYVEIYQEKVMDLLEPKNKDLPIREDKDHNILIPGVTLKTINSFGDFDEHFIPASQNRTVASTKLNDRSSRSHAVLLIKVQKSQQVAPFRQLIGKLYLIDLAGSEDNRRTGNQGIRLKESGAINSSLFTLSKVVDALNQGLPRIPYRDSKLTRLLQDSLGGSAHSVMITNIAPEQTYYFDTLTALNFAAKSKQIINKPFSRETTQTVAQPAMKRPREEAEATTSSRQRKKSKTDSTESSPNSSMESTGKRKLNLASLDSAVVERLLKLDKILTEKGKKEAQLLSTPKRERMALLKKWEESQMEIERLKEKQKELEQKAMEAEARLEKSNNSDLSDSSVSENTFRAPLRGRNTSTAKVKKVLRVLPMQGNSQLQSTIEEGIPVFEKKKKKQVTCDGHENQPTWEMNMRTDLLESGKERILKLLNTGSVKELKSLQRIGDKKAKLIIGWREVNGLFKNVEELECLEGISAKQVSSFIKANILSSISS", "text": "FUNCTION: Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family."}
{"protein": "MAEKGDCIASVYGYDLGGRFIDFQPLGFGVNGLVLSATDSRACRKVAVKKIVLSDARSMKHALREIKIIRRLDHDNIVKVYEVLGPKGSDLQGELFKFSVAYIVQEYMETDLACLLEQGTLTEDHAKLFMYQLLRGLKYIHSANVLHRDLKPANIFISTEDLVLKIGDFGLARIVDQHYSHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCILAEMLTGKMLFAGAHELEQMQLILDTIPVVREEDKEELLRVMPSFVSSTWEVKRPLRKLLPDVNSEAIDFLEKILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDDIVLMAASQSQLSNWDRYPVSLSSDLEWRPDRCQDASEVQRDPRAGSTPLAEDVQVDPRKDSQSSSERFLEQSHSSMERAFEADYGRSCDYKVGSPSYLDKLLWRDNKPHHYSEPKLILDLSHWKQAASAPPRAAVAADPVSREDEPASLFLEIAQWVKSTQSGSERASPPPDAPEPRLSASPPGHPTPIDGGASPQFDLDVFISRALKLCTKPEDLPENKLGDLNGACISEHPGDLVQTEAFSKERW", "text": "FUNCTION: Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the cytoplasm following interaction with MAPKAPK5. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
{"protein": "MPHSTNREMILGIVVGTAGISLLLLWYHKVRKPRTAMSLPKFLSLGNSLDLMTLQDEMPSGQGTTAIFQGRQLQILEKLNELLTHMEELKEEIRVLKEAIPKLEEYIQGELGGKVTVHKISPQHRARKRRLATVQSSATSNSSEEAESEGGYVTANTDTEEQSFPVPKEFNTHVEELNLDALIQRADNLRVNESRKVESFELLCDHKEKFRDEIEFIWRFARAYGDMYELSTNIQEKKHYANIGKTLGEKAIMRAPKNGYCHLWYAVLCGYVSEFEGLQNKINYGYRFKEHLDKAIEFLPEEPFLYYLKGRYCYAVSKLSWIERKMAATLFGNIPSSTVQEALQNFLKVEELQPGFSKSNYMFMAKCYADLNQIDSAMKFCNLAVLLPCITKEDKDAQKEVKKISTSLKR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Cytoplasm. Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. Also detected as large dots in the perinuclear region (By similarity). SIMILARITY: Belongs to the RMDN family."}
{"protein": "MRRAALRLCTLSKGLLAPSRGLTQESQNPENVFHIREVRDKLREIVGASTNWRDHVKAMEERKLLHSFLAKSQKGLPPRTMKDSYIEVFLPLGSQPELREKYLTVQNTVRFGRILEDLDSLGVLICYMHNKIHSAKMSPLSIVTALVDKIDMCKKNLSPEQDIKFSGHVSWVGKTSMEVKMHMFQLHGNDFSPVLDATFVMVARDSENKGPAFVNPLILESPEEEELFQQGELNKGRRVAFSSTSLLKMAPTAEERTTIHEMFLNTLDPKTISFRSRVLPANSVWMENSKLKSLDICHPQERNIFNRIFGGFLMRKAYELGWATACNFGGSRPFIVAVDDIMFQKPVEVGSLLFLSAQVCFTQGNYIQVRVHSEVASLQDKEHMTTNVFHFTFMSEKEVPLVFPRTYGESMLYLDGQRHFKSMSAPVTLKRNYVVEP", "text": "FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acyl coenzyme A hydrolase family."}
{"protein": "MKLRVGQTLGTIPRQCEVLLLLLLLGLVDGVHHILSPSSAERSRAVGPGASVGSNRPSLWALPGRLLFQIIPRGAGPRCSPHRLPSKPQFWYVFGGGTQLTILGQPKSDPLVTLFLPSLKNLQANKATLVCLVSEFYPGTLVVDWKVDGVPVTQGVETTQPSKQTNNKYMVSSYLTLISDQWMPHSRYSCRVTHEGNTVEKSVSPAECS", "text": "FUNCTION: Critical for B-cell development. SUBCELLULAR LOCATION: Endoplasmic reticulum Secreted Note=In pre-B cells, localizes predominantly to the endoplasmic reticulum."}
{"protein": "MFKKLFGQLQRIGKALMLPVAILPAAGILLAFGNAMHNEQLVEIAPWLKNDIIVMISSVMEAAGQVVFDNLPLLFAVGTALGLAGGDGVAALAALVGYLIMNATMGKVLHITIDDIFSYAKGAKELSQAAKEPAHALVLGIPTLQTGVFGGIIMGALAAWCYNKFYNITLPPFLGFFAGKRFVPIVTSVVAIATGVLLSFAWPPIQDGLNSLSNFLLNKNLTLTTFIFGIIERSLIPFGLHHIFYSPFWFEFGSYTNHAGELVRGDQRIWMAQLKDGVPFTAGAFTTGKYPFMMFGLPAAAFAIYKNARPERKKVVGGLMLSAGLTAFLTGITEPLEFSFLFVAPVLYGIHVLLAGTSFLVMHLLGVKIGMTFSGGFIDYILYGLLNWDRSHALLVIPVGIVYAIVYYFLFDFAIRKFKLKTPGREDEETEIRNSSVAKLPFDVLDAMGGKENIKHLDACITRLRVEVVDKSKVDVAGIKALGASGVLEVGNNMQAIFGPKSDQIKHDMAKIMSGEITKPSETTVTEEMSDEPVHVEALGTTDIYAPGVGQIIPLSEVPDQVFAGKMMGDGIGFIPEKGEIVAPFDGTVKTIFPTKHAIGLESESGVEVLIHIGIDTVKLNGEGFESLINVDEKVTQGQPLMKVNLAYLKAHAPSIVTPMIITNLENKELVIEDVQDADPGKLIMTVK", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in alpha- and beta-glucoside transport (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MAASASTAAGEEDWVLPSEVEVLESIYLDELQVMKGNGRSPWEIFITLHPATAEVQDSQFVCFTLVLRIPVQYPHEVPQISIRNPRGLSDEQIHKISQALGHVAKEGLGTAMLYELIEKGKEILTDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELTTQEQEQERQHVVTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEELKLLYQRQQEKGGIIDLEAERNRYFISLQQPPAALEPESAVDVSREPQPPNALSAEQSTSLADQSTLPTSLPMTTQYTYEKTSGAGPNQQRPGETQKSVLDPPRHGRGSWRQYDRRHPKGGECCTPKGTSEIHELPPPEKPLKETVDLKAEPRNKGLTGHPQEKGPGSWQGPSARRTRDCARWERSKNRTPGSCYPHLPRGQGAYRSGTRREPLGLESEEGS", "text": "FUNCTION: E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (By similarity). Catalyzes ubiquitination of RPS27A in response to ribosome collisions, promoting activation of RNF14 (By similarity). RNF25 catalyzes ubiquitination of other ribosomal proteins on stalled ribosomes, such as RPL0, RPL1, RPL12, RPS13 and RPS17 (By similarity). Also involved in ubiquitination and degradation of stalled ETF1/eRF1 (By similarity). Independently of its function in the response to stalled ribosomes, mediates ubiquitination and subsequent proteasomal degradation of NKD2 (PubMed:10500182, PubMed:18757723). May also stimulate transcription mediated by NF-kappa-B via its interaction with RELA/p65 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNF25 family."}
{"protein": "MATRIPFTESQWEELENQALVFKYLAANMPVPPHLLFLIKRPFLFSSSSSSSSSSSFFSPTLSPHFGWNVYEMGMGRKIDAEPGRCRRTDGKKWRCSKEAYPDSKYCERHMHRGKNRSSSRKPPPTQFTPNLFLDSSSRRRRSGYMDDFFSIEPSGSIKSCSGSAMEDNDDGSCRGINNEEKQPDRHCFILGTDLRTRERPLMLEEKLKQRDHDNEEEQGSKRFYRFLDEWPSSKSSVSTSLFI", "text": "FUNCTION: Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRF family."}
{"protein": "MARGCLCCLKYAMFLFNLIFWLCGCGLLGVGIWLSVSQGNFATFSPSFPSLSAANLVIAIGTIVMVTGFLGCLGAIKENRCLLLSFFIVLLIILLAELILIILFFVYMDKVNENAKKDLKEGLLLYNSENNVGLKNAWNIIQAEMHCCGVTDYRDWFLVLGENTVPDRCCMENSQGCGQNNTTLLWRTGCYEKVKQWFADNKHVLGTVGMCLLITQILGMAFSMTLFQHIHRTGKKYDA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Note=Colocalizes with GP6 in tetraspanin microdomains on the platelet surface. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
{"protein": "MTADSALYIPPYKADDQDIVVELNSRFGAETFTVQPTRTGMPVLWVPRERLIEVLTFLRQVPKPYVMLYDLHGVDERLRTHRRGLPSADFSVFYHLMSLERNSDVMIKVALSERDLNLPTATRIWPNANWYEREVWDMYGITFTGHPHLTRMLMPPTWQGHPLRKDYPARATEFDPYSLSAAKQDLEQEALRFKPEDWGMKRHGENEDYMFLNLGPNHPSAHGAFRIILQLDGEEIIDCVPEIGYHHRGAEKMAERQSWHSFIPYTDRIDYLGGVMNNLPYVLSVEKLAGIKVPQRVDVIRIMMAEFFRILNHLLYLGTYIQDVGAMTPVFFTFTDRQRAYKVVEAITGFRLHPAWYRIGGVAHDLPRGWDKLVREFLDWMPKRLDEYETAALKNSILRGRTIGVAQYNTKEALEWGTTGAGLRATGCDFDLRKARPYSGYENFEFEVPLAHNGDAYDRCMVKMGEMRQSLRIIEQCLKNMPEGPYKADHPLTTPPPKERTLQHIETLITHFLQVSWGPVMPANEAFQMIEATKGINSYYLTSDGSTMSYRTRIRTPSFAHLQQIPSVINGSMIADLIAYLGSIDFVMADVDR", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa subunit family. SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa subunit family."}
{"protein": "MEKALKIKQIVVVLIAIAAVAIGYYMFQSITSPAKAVAKQENVVQLASEQPKVEMNKTAPSRFNGKERKVAYLTFDDGPGKYTAELLNTLKQHDAKATFFLIGANVKEFPDLVKRENAEGHYVGMHSMTHNFAKLYKNGEYVNEMKEDQGLIANIIGKSPKLTRPPYGSMPGLNEGLRNKVVEGGFKVWDWTIDSLDWRYNKMPVDAAAAQIAQNVLTNATKPQEVILMHDIHPQSVAAVPAILKGLKEKGYEFEAYHEESHFPVNFWHDNRM", "text": "FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the polysaccharide deacetylase family."}
{"protein": "AVCVSLLGAANIPPHPLNLINFMEMIRYTIPCEKTWGEYADYGCYCGAGGSGRPIDALDRCCYVHDNCYGDAANIRDCNPKTQSYSYKLTKRTIICYGAAGTCARVVCDCDRTAALCFGDSEYIEGHKNIDTARFCQ", "text": "FUNCTION: Beta bungarotoxin is a presynaptic neurotoxin. The A chain has phospholipase activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
{"protein": "MAVKISLVDLAQNIGAELHGDKNILITHVSSIKNAQVGHITFLKNSRFREQLKSCAASAVILSQDNLSFCRVSALVVKNPYLAYVKVAQLLDSSPKLNANIKSQSVIHSNSILGKDVGIGYNVIIESGVIISDNVKIESGCIIGKNVKIGIGTYLWSNVTVYHGVEIGEYCIIQSGSIIGSDGFGYIKNDGVWIKIPQLGKVSIGNNVEIGSCTTIDRGTLDDTCIGDGVIIDNQCQIAHNVAIGSHTAIAGGVIIAGSVVIGKSCMIGGASVINGHIRICDKVTITGMSMVMKSITTSGIYSSGIPVQPNFAWRRTAALVMRIHSIDKRIKDIEQKVNCFFYIVIVGFFIVLGLTGLFPLIYFFVKQG", "text": "FUNCTION: Catalyzes the N-acylation of UDP-3-O- (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD subfamily."}
{"protein": "MMDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNAAYSAGILLAPPLVLFLLGLVMNNNVSMLAEEWKRPLGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVSALGNGSLAPGLPAPELARLLARVPCPEIYDGDWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQAAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGTLATAPASAAAPTTPDGAEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQEEPPLMGNGWAGGGPRPPRKEVATYFSKV", "text": "FUNCTION: Pore-forming subunit of a voltage-gated ion channel required for sensory perception of sweet, bitter and umami tastes (By similarity). Specifically present in type II taste bud cells, where it plays a central role in sweet, bitter and umami taste perception by inducing ATP release from the cell, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways (By similarity). Together with CALHM3, forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells (TBCs) (By similarity). Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to changes in extracellular Ca(2+) concentration (PubMed:22711817, PubMed:23300080). Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of Ca(2+), Na(+) and K(+), as well as permeation of monovalent anions (PubMed:22711817). Acts as an activator of the ERK1 and ERK2 cascade (PubMed:23345406). Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum (PubMed:21574960). May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner (PubMed:18585350). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein Note=Colocalizes with HSPA5 at the endoplasmic reticulum (PubMed:18585350). Localizes to the basolateral membrane of epithelial cells including taste cells (By similarity). SIMILARITY: Belongs to the CALHM family."}
{"protein": "MVVFLFILYRQSDLKFKSMNGVIIVNTLKKRLFVATTMIWGLSVTLPVLAEYKPIEQPVEPANPSLKIESRNDLFKEKYPKQYQTWADTSKSTDLDSVNYEDPRVIVLWAGYAFAKDYKKPRGHFYAVTDVREILRTAAPMTPDAGPMPMACWSCKSPDVPRLIAERGEAGYFGATWASGGSEVVNPIGCADCHDTTSKDFAEGKPALRIARPYVLRALEKIDHKFDTSDRTDQRAALCANCHVEYYFAGDLKQVTFPWDNGITVDAMEKYYDDIGFVDWTHAVSKAPMLKAQHPDYETWMLGVHGKNGVTCIDCHMPKVQGADGKVYTDHQIGNPFNAFEHTCANCHDQSKEKLQAMVKSRKTEIKDVMLRLEDQLVAAHFEAKAAWEAGATKEEMKEALQDIRHAQWRWDYAAAGHGGHIHAPDVLLKVIGTGLDKSSDARTKLVRVLAKHGITDPVQLPDISTAENAWKATGVDIEKERKAKAEFLKTVVPQWDKEAREKGLLPAEK", "text": "FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the cytochrome c-552 family."}
{"protein": "MIRLAAIDVDGTLTDRDRLISTKAIESIRSAEKKGLTVSLLSGNVIPVVYALKIFLGINGPVFGENGGIMFDNDGSIKKFFSNEGTNKFLEEMSKRTSMRSILTNRWREASTGFDIDPEDVDYVRKEAESRGFVIFYSGYSWHLMNRGEDKAFAVNKLKEMYSLEYDEILVIGDSNNDMPMFQLPVRKACPANATDNIKAVSDFVSDYSYGEEIGQIFKHFELM", "text": "FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate. Also has significant, but less efficient, pyrophosphatase activity, since it is able to catalyze the release of phosphate from inorganic pyrophosphate (PPi). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Archaeal SPP-like hydrolase family."}
{"protein": "MGFLRETVFGELVEYVSHNSNDNDLEKLRVWKDISKVDSNDSCSSESGDLKIHEVNSEGHIIVRWDDANDPENPLNWPLWAKLVVTFDICFLTFAVYVGSAIFTPGISEMQETMHVGTVPVVLGLTLFVLGYAIGPLILSPLSEIPQVGRQKIYVLSLLVFVCLQIPTALGSSLGVLLPMRFLAGFFGSPALATGGATLADIWQPWLLPYFMCFWAIGAIGGPVLGPLLGGAMVVAESWRWQFWLLMMISGFALIVIFFFMPETSEWHILYKRAKRFRKITGNENYRTEAELASSHLSVAQLAKETIIRPIILSISEPIVLSLNIYIGLIYSILYLWFEAFPILFTSVYHFTIIENGLVYLGILVGALITLACYFVFLYKVMIPAFMASGGDFAPEGVLVISFPATFFIPICLFWFGWSGRESVHWIVPIVSTLFYASGAFLMFQSMFQYLAASYPKYVASVFAGNDLFRSAMAASFPLFARAMFNNTGPSYAPVAWGSTILGIVACLMIPIPFVLHKWGLKLRSRSKYAS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family."}
{"protein": "MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH", "text": "FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells. FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells. SUBCELLULAR LOCATION: Host cytoplasm Host cell membrane; Peripheral membrane protein; Cytoplasmic side Virion Note=In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor. Incorporated in virions at a ratio of approximately 7 to 20 molecules per virion. SIMILARITY: Belongs to the primate lentivirus group Vif protein family. SIMILARITY: Belongs to the primate lentivirus group Vif protein family."}
{"protein": "MNKQASGKDTGNRGAVTGGKQMDGFADMLTNLLSKVGISNHEVFTSEKPHLPGYFRATKKWDFLVVKTNDRGEKYLLAAVELKSHVGPSFGNNLNNRVEESLGSATDIWIAFREKAFKNSRAPWLGYLMLLEDCPQSTKPVKVDEPHFEVFPEFKNASYAKRYELFCRKIVLERKYTSSCLLMSDKQGGLQGIYKEPANDLKIYPFLYSLLTHVATEAALISSS", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-CTCGAG-3' and cleaves after C-1. SIMILARITY: Belongs to the XhoI type II restriction endonuclease family."}
{"protein": "MKIIRKIVKSCKDDEMQKPNPVSAPPDDDDLWLPPPEYVPLSEMTGKKNMRNFCINGEVKVCSPNGYSFRIIRHILSSFEGVYSGNRRMIGLVKVVIGLALSGAPVPDGMNWVYKIRRTLIFQWAESSGPLDGEELEYSQEITWDDDSEFVGLQMRVSARQCHIQGRLWCINMNSRACQLWSDMSLKTQQSDEDKNTSLLLE", "text": "FUNCTION: Plays a major role in assembly and budding of virion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication. Plays a major role in early induction of TRAIL-mediated apoptosis in infected neurons (By similarity). SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. SIMILARITY: Belongs to the lyssavirus matrix protein family."}
{"protein": "MAVDPRCLLSLCSTISKASSAKGTNDFVKIGMELWQTAQPYLVQALGLQPPPPKVDVDAAVANAGDAHGEQPWVATPLPGQTVRALFIGINYYGTSAALSGCCNDVKQMLATLQKKGLPINEAVILVDEDNFPGRTDQPTRDNIVRYMAWLVKDAKPGDVLFFHYSGHGTQCKSRGDSDEKYDQCIAPVDFQKSGCIVDDDIHKLLFSRLPEKVRLTAVFDCCHSGSIMDLPFTYVCSGGEQASGTPHMKRIREGNDVLGDVMMISGCADEQTSADVKNTATFGTGSTGAGGAATQCITCMLMNNQSLSYGKLLIETRDMLKRKRFKQVPQLSASKAIDLDQTFSLTEMFSVDRSVQ", "text": "FUNCTION: Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:21949125). In the bloodstream form, may cleave inactive metacaspase-4 MCA4 prior to MCA4 secretion (PubMed:21949125). SUBCELLULAR LOCATION: Recycling endosome. SIMILARITY: Belongs to the peptidase C14B family."}
{"protein": "MSLAVEYISDKTPCQRCSTKDAVLLARRENYCGDCFIRFIRGKQRRSMQDEAYKVKYKTVENPHRVLLALSGGSSSLVLLDAVASLLQEQAGQHGGRQGFALTVVNVDERERLKLDKSFQDIISELKSRYLPVDIDFVSLDYDMYVDGRLLHHIKVASDFSSYSIPLNKGTNINDILKGCNSKSSEEDLLSIILNELLLKTAITHQCGTLLYGHSMTRLADEVLALTIKGRGSTIHSSVLDHTEEISGQTINVKYPLRDVLMGEIEAYCKLAKLDSVVMSSTIPDPVINKNKTVRGLTAQYFRQLDATGYSSTASTVVRTAAKLAAPTVGTKSGTCKVCGVEIRQDPHQWLRRITVAENEKVENNSEESGEIGADKKEDVGEQIDLCYGCTVTIGDAPSFRWPLSDKDIIAEYTLDSDED", "text": "FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CTU2/NCS2 family."}
{"protein": "MKLSILFLFAIAVQAAFLGIDYGQQSIKAMVVSPKAMMEIVLTPEAKRKDTSGICIRNVNGVLERHYGNSIGSLVTRFPQNTAMHLRSLLGKSMNDKDTIESYLRENPGANLTSTTRNTIAITIDGVEYPVEQLVAMNLQEIIDRANQHIKETDTTGIDFVEQVGIAIPEQFNQAQRQALLDALALTSVKDEAVLVSDGLSVAIDYALKRPDLEINVPQYYIVFDVGTSAAKATLFSLTQPEDLSSPIKIEIGAFDSEATVGGSKFIAAIADIVEDKFLEKNTKITRKSLVENPRARAKIIQAAEKAKLVLSANNEAIISIESLVDDIDFRTTIARSEFQDIFEDNKHTVVKAIKGAIGNQLWDDNISLEDISGVILSGGSSRVPMVQEEIAKLVGEEKILKNVNADETVINGATLKGLKYFGSFKTKPLDITERSLFDYSVEMSGESSSKTVFEKGTKFPNESSILYKAPKKFGKELKFDLFESDTRILSNIVDTTVSSKNWTSACKKGQLYLNVTFDLDSNRVFKIKDITVLCDSDGNAKEEEFEFIDVINDVTKATDVMPLSNAEIRQLSNAITSWNRKDRERKRVQESLNVLEAELYDCRSFIEEFEEKLGEEEFETLKSFTAFVKEKLEYLEDNSADMSKKDIEKLVRETRSQRDTLSRFYNSLDAALGSKDFQKLVDTASKSIKKYKEIESKNLADLENKAEKFNVIGLNVTEKYNSILSKMSFSSIRRSSEENIKTLAGLIDEVNESIKSKAIDDESLENLIKTKLAFEELINTLDLENRQWTYQHQLVMKELKKMYNKKMKAIKKQEKQNENEENGDDEGDDEDETKTKKYLKEATSSGDSSTIKEEDSTGSNEAGNKGDEEDEEEEEDDSSAGNVFDDEL", "text": "FUNCTION: Chaperone required for protein translocation and folding in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MTLSPYLQEVAKRRTFAIISHPDAGKTTITEKVLLFGQAIQTAGTVKGRGSSQHAKSDWMEMEKQRGISITTSVMQFPYHDCLVNLLDTPGHEDFSEDTYRTLTAVDCCLMVIDAAKGVEDRTRKLMEVTRLRDTPILTFMNKLDRDIRDPMELLDEVENELKIGCAPITWPIGCGKLFKGVYHLYKDETYLYQTGKGHTIQEVRIVKGLNNPDLDAAVGEDLAQQLRDELELVQGASNEFDEELFLAGEITPVFFGTALGNFGVDHMLDGLVAWAPAPMPRQTDTRTVEASEEKFTGFVFKIQANMDPKHRDRVAFMRVVSGKYEKGMKLRQVRTGKDVVISDALTFMAGDRSHVEEAYPGDILGLHNHGTIQIGDTFTQGEMMKFTGIPNFAPELFRRIRLKDPLKQKQLLKGLVQLSEEGAVQVFRPISNNDLIVGAVGVLQFDVVVARLKSEYNVEAIYESVNVATARWVESADAKKFEEFKRKNETQLALDGGDNLTYIAPTMVNLNLTQERYPDVQFRKTREH", "text": "FUNCTION: Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. FUNCTION: Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily."}
{"protein": "MKTFSDRWRQLDWDDIRLRINGKTAADVERALNASQLTRDDMMALLSPAASGYLEQLAQRAQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNRIKRKTLDEADIARESAAIREMGFEHLLLVTGEHQAKVGMDYFRRHLPALREQFSSLQMEVQPLAETEYAELKQLGLDGVMVYQETYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDNWRVDSYMVAEHLLWLQQHYWQSRYSVSFPRLRPCTGGIEPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDRVIPLAINNVSAFSKTQPGGYADNHPELEQFSPHDDRRPEAVAAALTAQGLQPVWKDWDSYLGRASQRL", "text": "FUNCTION: Catalyzes the radical-mediated cleavage of tyrosine to 2- iminoacetate and 4-cresol. SIMILARITY: Belongs to the radical SAM superfamily. ThiH family."}
{"protein": "MDDYEKSKVLTKRYKKLKKLLKMVYGYDNFRPRQYEIINKVINGEDVCAILMTSAGKSLCFQIPALYLDKPAIIISPLISLMEDQRLILEKLGISSCCYNSNVENKAQMRKDIMQFKYKFIYVSPESVVHLKDLIVKLEDFQGISLIAIDEAHCISAYGFDFRTAYREITFFKEILPNVPILALTATATNIVAKDICKVLQLKTNEPIKASFDRPNLYLEVRTKSKNPANDIVPIINKYPNQSVIIYCLTKKETQKIADILTVHKVVCGIYHAGLSNEHKTKTHTNFINNKIKIVVATIAFGMGINKPDVRVVIHYGAPKNIEGYYQEIGRAGRDGEKSYCYAFYNFQDFMIQRRFISQNNNPNYQKTQLALLEQMKKYVTLRTCRRKILLEYFDEETKEKCDFCDNCCGVHKNIVNENVTSKQNVQSEAKLIIELIESIPNRNFGVNMYINILRGSKNKAISPAIRKNKYYGLGSKHSSEWWKEVFDNLIKQGFLQSVSLKTGKFPIQVVKVTNKGVTWVSMADLGSLLDNIDNSVKLDPVEMVASV", "text": "SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily."}
{"protein": "MGVELRSYVYLDNLQRQHASYIGTVATGFLTLPGDASVWIEISPGIEINRMMDIALKAAVVRPGVQFIERLYGLMEVHASNQGEVREAGRAVLSALGLTERDRLKPKIVSSQIIRNIDAHQAQLINRQRRGQMLLAGETLYVLEVQPAAYAALAANEAEKAALINILQVSAIGSFGRLFLGGEERDIIAGSRAAVAALENLSGREHPGDRSRE", "text": "FUNCTION: Probably part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. It is thought that this protein controls transport of RuBisCO reactants in and out of the carboxysome; residual densities in the 4 X-ray structures suggest that differing compounds bind in interior pockets, depending on the open or closed state of the pore. SUBCELLULAR LOCATION: Carboxysome Note=This cyanobacterium makes beta-type carboxysomes. SIMILARITY: Belongs to the EutL/PduB family."}
{"protein": "MSLLRNRLQDLPALCLCVLVLACIGACQSEAYEGTPSPPPKLKMSHWSLVTGRMKELLEPVLKRTRDRWQWFWSPSTFRGFMQTYYDDHLRDLGPRTKAWLLKSKESLLNKTHSLCPRIVCGDKDQG", "text": "FUNCTION: May participate in lipoprotein metabolism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C4 family."}
{"protein": "MRGAVHIFIMLLLATASDCAVITGACERDIQCGAGTCCAISLWLRGLRLCTPLGREGEECHPGSHKIPFLRKRQHHTCPCSPSLLCSRFPDGRYRCFRDLKNANF", "text": "FUNCTION: Potently contracts gastrointestinal (GI) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells. Induces proliferation and differentiation, but not migration, of enteric neural crest cells. Directly influences neuroblastoma progression by promoting the proliferation and migration of neuroblastoma cells. Positively regulates PTGS2 expression and prostaglandin synthesis. May play a role in placentation. May play a role in normal and pathological testis angiogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AVIT (prokineticin) family."}
{"protein": "MASLKKSLFLVLFLGFVSVSICEEEKRQEDEDEHEEEGENQEEGSEEKRGLFSVLGSVAKHVVPRVVPVIAEHLG", "text": "FUNCTION: Cationic amphipathic alpha-helical antimicrobial peptide with weak or no activity against both Gram-positive and Gram-negative bacteria (PubMed:12709067). Is weakly active against E.coli (MIC=25 uM), E.cloacae (MIC=50 uM), K.pneumoniae (MIC=25 uM), and S.haemolyticus (MIC=50 uM) (PubMed:12709067). Has no activity against S.typhimurium, S.enteritidis, B.megaterium, and S.aureus (MIC>100 uM) (PubMed:12709067). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily."}
{"protein": "MARLNSKAVAAAVVLAAVVLMMAGREASAALSCGQVDSKLAPCVAYVTGRASSISKECCSGVQGLNGLARSSPDRKIACRCLKSLATSIKSINMGKVSGVPGKCGVSVPFPISMSTNCNNVN", "text": "FUNCTION: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). SIMILARITY: Belongs to the plant LTP family."}
{"protein": "MSGELKRGLEGVLVAESKLSFIDGDAGQLVYCGYDIEDLARDASYEEVLYLLWHGALPTGEELDAFSDELAAHRDLDDGVLDVARELAEQDESPMAALRTLVSAMSAYDESADFEDVTDREVNLEKAKRITAKMPSVLAAYARFRRGDDYVEPDESLNHAANFLYMLNGEEPNEVLAETFDMALVLHADHGLNASTFSAMVTSSTLSDLYSAVTSAIGTLSGSLHGGANANVMRMLKDVDDSDMDPTEWVKDALDRGERVAGFGHRVYNVKDPRAKILGAKSEALGEAAGDMKWYEMSVAIEEYIGEEKGLAPNVDFYSASTYYQMGIPIDLYTPIFAVSRAGGWIAHVLEQYEDNRLIRPRARYTGEKDLDFTPVDER", "text": "FUNCTION: Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. SIMILARITY: Belongs to the citrate synthase family."}
{"protein": "MTAIFLMSVLFGLACGQAMSFCIPTEYMMHVERKECAYCLTINTTICAGYCMTRDFNGKLFLPKFALSQDVCTYRDFMYKTVEIPGCPHHVTPYFSYPVAVSCKCGKCDTDYSDCIQEAVKMNYCTKPQKPHVVGLSI", "text": "FUNCTION: Indispensable for the control of thyroid structure and metabolism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
{"protein": "MNSNISAQNDSALNSTIQNGTKINQFIQPPWQIALWSVAYSIIVIVSLVGNIIVMWIIIAHKRMRTVTNYFLVNLAFAEASMSAFNTVINFTYAIHNHWYYGLIYCKFHNFFPISAVFTSIYSMTAIALDRYMAIIHPLKPRLSATATKIVICVIWSFSFCMAFPLGYYADVYPMEGGDICYLNWPDSEENRKYEQVYQVLVFCLIYILPLLVIGCAYTFIGMTLWASEIPGDSSDRYHEQVVAKRKVVKMMIVVVCTFAICWLPFHIFFLLQTLHEMTQKFYQQFYLAIMWLAMSSTMYNPIIYCCLNDRFRIGFKHVFRWCPFIRAGEYEGLELKSTRYLQTQSSMYKISRIETTVSSVLNTNDEEAEENGKSSKRLSLDLTSNGSSRSVCKTMSDSSSFYSNNLA", "text": "FUNCTION: This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKNGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN", "text": "FUNCTION: Probably involved in acid resistance. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family."}
{"protein": "MKKLVATAPRVAALVEYEDRAILANEVKIRVRFGAPKHGTEVVDFRAASPFIDEDFNGEWQMFTPRPADAPRGIEFGKFQLGNMVVGDIIECGSDVTDYAVGDSVCGYGPLSETVIINAVNNYKLRKMPQGSSWKNAVCYNPAQFAMSGVRDANVRVGDFVVVVGLGAIGQIAIQLAKRAGASVVIGVDPIAHRCDIARRHGADFCLNPIGTDVGKEIKTLTGKQGADVIIETSGYADALQSALRGLAYGGTISYVAFAKPFAEGFNLGREAHFNNAKIVFSRACSEPNPDYPRWSRKRIEETCWELLMNGYLNCEDLIDPVVTFANSPESYMQYVDQHPEQSIKMGVTF", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-gulosides leading to 3-dehydro-D-gulosides. Probably functions in a metabolic pathway that transforms D-gulosides to D- glucosides. Is also able to catalyze the reverse reactions, i.e. the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D- gulosides leading to D-gulosides. In vitro, can oxidize D-gulose and methyl beta-D-guloside, and reduce methyl alpha-3-dehydro-D-guloside and methyl beta-3-dehydro-D-guloside. However, the actual specific physiological substrates for this metabolic pathway are unknown. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MESMLNKLKSTVTKVTADVTSAVMGNPVTREFDVGRHIASGGNGLAWKIFNGTKKSTKQEVAVFVFDKKLIDKYQKFEKDQIIDSLKRGVQQLTRLRHPRLLTVQHPLEESRDCLAFCTEPVFASLANVLGNWENLPSSISPDIKDYKLYDVETKYGLLQVSEGLSFLHSSVKMVHGNVTPENVILNKSGAWKIMGFDFCVSSSNPSEQEPKFPCKEWDPNLPSLCLPNPEYLAPEYILSVSCETASDMYSLGAVMYAVFNQGRPIFEVNKQDIYKSFSRQLDQLSRLGSSSLTSIPEEVREHVKLLLNVTPTVRPDADQMTKIPFFDDVGAVTLQYFDTLFQRDNLQKSQFFKGLPKVLPKLPKRVIVQRILPCLTSEFVNPDMVPFVLPNVLLIAEECTKEEYIKLILPELGPVFKQQEPIQILLIFLQKMDLLLTKTPPDEIKNSVLPMVYRALEAPSIQIQELCLNIIPTFANLIDYPSMKNALIPRIKNACLQTSSLAVRVNSLVCLGKILEYLDKWFVLDDILPFLQQIPSKEPAVLMGILGIYKCTFTHKKLGITKEQLAGKVLPHLIPLSIENNLNLNQFSSFIAVIKEMLSRLESEHRTKLEQLHVMQEQQRSLDIGNQMSTSEETKVAHSGSQQIDKVFNNIGADLLSGSESENREDGMQGKQKRGSLTLEEKQKLAKEQEQAQKLKSQQPLKPQVHTPIAPIKQTKDLTDTLMENMSSLTSLSVSTPKISASSTFTPVPSTGLGMMFSTPIDNTKRNLTNGLNANMGFQTSGFSMPVNPNQNFFSGTGTAGVTTMSLGAPPTMSNFSPLTIPPASVKQPQQRPTDMSALNNLFGPQKPKVSMNQLSQQKPNQWLNQFAPPQGSPVMGSAAMGTQGNVMGQAAFGMQGNPFFNPQNFAQPPPTTMTSSSSASNDLKDLFG", "text": "FUNCTION: Component of the AP2-containing clathrin coat that may regulate clathrin-dependent trafficking at plasma membrane, TGN and endosomal system. A possible serine/threonine-protein kinase toward the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L-lysine has not been confirmed (By similarity). By regulating the expression of excitatory receptors at synapses, plays an essential role in neuronal function and signaling and in brain development (PubMed:26203146). SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle Golgi apparatus, trans-Golgi network membrane Endosome membrane Note=Colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes. SIMILARITY: Belongs to the protein kinase superfamily."}
{"protein": "MAALLLLNRVSRSTSSISLHRVAGTLGFNSFNAQIHGDRISGTLFRVRSLATLAEGASHFNEMVSVNQRKYYLLGGKGGVGKTSCAASLAVKFASHGHPTIVVSTDPAHSLSDSFSQDLSGGVLKPVQGVDSPLLALEITPEIMKDEIKRQTGDKSVKNMMDSMGLGMFAGELGDLNLEDMLNAASPGIDEIAAISKVLQFMEAPEYSRFTRIVFDTAPTGHTLRLLSLPDFYDSSISKITKLKKKITAAASAFKLVFGKKEIQQKELPNELDQLKERMEKVRNVFRDVDTTEFVIVTIPTVMAINESSRLHASLRKENVPVHRLIVNQLLPQSESDCKFCSIRRKEQTRVLGLIQNDTELSGLKLIQSPLLDAEIRGVPALKFMGDLIWK", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the arsA ATPase family."}
{"protein": "MTTKNMNTPPGSTQENEIDLLRLVGELWDHRKFIISVTALFTLIAVAYSLLSTPIYQADTLVQVEQKQGNAILSGLSDMIPNSSPESAPEIQLLQSRMILGKTIAELNLRDIVEQKYFPIVGRGWARLTKEKPGELAISWMHIPQLNGQDQQLTLTVGENGHYTLEGEGFTVNGMVGQRLEKDGVALTIADIKAKPGTQFVLSQRTELEAINALQGTFTVSERSKESGMLELTMTGDDPQLITRILNSIANNYLQQNIARQAAQDSQSLEFLQRQLPEVRSELDQAEEKLNVYRQQRDSVDLNLEAKAVLEQIVNVDNQLNELTFREAEISQLYKKDHPTYRALLEKRQTLEQERKRLNKRVSAMPSTQQEVLRLSRDVEAGRAVYLQLLNRQQELSISKSSAIGNVRIIDPAVTQPQPVKPKKALNVVLGFILGLFISVGAVLARAMLRRGVEAPEQLEEHGISVYATIPMSEWLDKRTRLRKKNLFSNQQRHRTKNIPFLAVDNPADSAVEAVRALRTSLHFAMMETENNILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLFTVSNEHGLSEYLAGKDELNKVIQHFGKGGFDVITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQAGVNIKGAILNGVIKRASTAYSYGYNYYGYSYSEKE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the etk/wzc family."}
{"protein": "MSFRKVNIIILVLAVALFLLVLHHNFLSLSSLLRNEVTDSGIVGPQPIDFVPNALRHAVDGRQEEIPVVIAASEDRLGGAIAAINSIQHNTRSNVIFYIVTLNNTADHLRSWLNSDSLKSIRYKIVNFDPKLLEGKVKEDPDQGESMKPLTFARFYLPILVPSAKKAIYMDDDVIVQGDILALYNTALKPGHAAAFSEDCDSASTKVVIRGAGNQYNYIGYLDYKKERIRKLSMKASTCSFNPGVFVANLTEWKRQNITNQLEKWMKLNVEEGLYSRTLAGSITTPPLLIVFYQQHSTIDPMWNVRHLGSSAGKRYSPQFVKAAKLLHWNGHLKPWGRTASYTDVWEKWYIPDPTGKFNLIRRYTEISNIK", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 8 family."}
{"protein": "MLDSVASKPELAELLTLTKTEQILRLAQINVELEQLSAQERVKWALENLEGEFAVSSSFGIQAAVMLHLVTQQKPDIPIILTDTGYLFAETYQFIDQLKAQLNLNLKVYRAKESANWQEARYGKLWEQGIEGIEKYNKINKVEPMRRALREQNVGTWFSGLRREQSQSRAGLPILSIQNGVFKFLPVIDWTNKDVHYYLEEHGLSYHPLWEQGYLSVGDTHTSRKWEPGMSEEETRFFGLKRECGLHEDDGSEQDGSGI", "text": "FUNCTION: Catalyzes the formation of sulfite from phosphoadenosine 5'- phosphosulfate (PAPS) using thioredoxin as an electron donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily."}
{"protein": "MSLSVSFIFLLVASIGAVVADSENVLVLTESNFEETINGNEFVLVKFYAPWCVHCKSLAPKYDEAADLLKEEGSDIKLAKVDATENQALASKFEVRGYPTILYFKSGKPTKYTGGRATAQIVDWVKKKSGPTVTTVESVEQLEELKGKTRVVVLGYFKDAKSDAATIYNEVADSVDDAFFAVAGSAEVAAAASLNEDGVALIRTDGDDSETSTIAEAEITNTIALKQWLHAYKLSAVTEFTHESAQEIVGGDLKKFHFLIIRKSDSSFDETIAKFTEVAKKFRAKIVFVLLDVDVEENARILEFLGVDAKNTPANRIVSLADQVEKFKPQEGEDFEAFTNSYLEGKSAQDLKAQDLPEDWNALPVKVLVASNFNEIALDETKTVFVKFYAPWCGHCKQLVPVWDELAEKYESNPNVVIAKLDATLNELADVKVNSFPTLKLWPAGSSTPVDYDGDRNLEKFEEFVNKYAGSASESETASQDHEEL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the protein disulfide isomerase family."}
{"protein": "MGSRPRSPSAFPAPWWGQQPGGPGPAKRLRLEEPAGPEPRVAPSLEDPAGTPAVGALTSIVVLAAGCALRVPLDDVDLVLELPPTSILRVSLDGHTLILIPEVLLSSVDERSGAQDDSSAGLEVDVFLGALREDVVVEQEVFCASVPEIAAQEEAYEEDADPEFPELQMDSAAGSAAGLYSSARSMFSPYREGPIPEPCALAPNPSSEGHSPGPFFDPEFRLLEPVPSSPLQPLPPSPRVGSPGPHAHPPLPKRPPCKARRRLFQE", "text": "SIMILARITY: Belongs to the PRR23 family."}
{"protein": "MKNLLEQIQSRLDELNKAERKVAEVILQNPQQATRFSIAALAQAAAVSEPTVNRFCRSFGMSGYPELKIQLAQSLASGAAFVTQAVAEDDGPEAYTRKIFSNTIASLDSAHKLLDPRVIDRAVDLLIQARQIHFFGLGASASVALDAQHKFFRFNLAVSAQADVLMQRMIASVAHTGDLFVVISYTGRTRELVEVAHLARENGASVLGLTAAGSPLARASTLCLDIPLPEDTDIYMPMTSRIVQLTVLDVLATGVTLRRGVDFQPHLRRIKESLVPTRYPLDEDN", "text": "FUNCTION: Involved in regulation of glucose metabolism. Transcriptional repressor of the gap-1 gene and of the edd-glk-gltR-2 and zwf-pgl-eda operons. Acts by binding directly to an inverted pseudopalindromic sequence in the promoter region."}
{"protein": "MRLCICFVLLAVIVCASADNPFTRGGRFVLDAAGGAWDMLRAYRDMREANHIGADKYFHARGNYDAARRGPGGAWAARVISDARENWQGGVSGRGAEDTRADQEANAWGRNGGDPNRYRPPGLPSKY", "text": "FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL complex. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SAA family."}
{"protein": "MLTEQQRRELDWEKTDGLMPAIVQHAVSGEVLTLGYMNPQALDKTIESGHVTFFSRTKQRLWTKGETSGHVLNVVSIAPDCDNDTLLVLANPVGPTCHKGTSSCFGDASHQWLFLYQLEQLLAERKTADPASSYTAKLYASGTKRIAQKVGEEGVETALAATVNDRFELTNEASDLMYHLLVLLQDQDLNLTTVIDDLRKRHQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family."}
{"protein": "MPLRLLLLLLWLWGLQWAETDSEGQTTTGELYQRWEHYGQECQKMLETTEPPSGLACNGSFDMYACWNYTAANTTARVSCPWYLPWFRQVSAGFVFRQCGSDGQWGSWRDHTQCENPEKNGAFQDQTLILERLQIMYTVGYSLSLTTLLLALLILSLFRRLHCTRNYIHMNLFTSFMLRAAAILTRDQLLPPLGPYTGDQAPTPWNQALAACRTAQIMTQYCVGANYTWLLVEGVYLHHLLVIVGRSEKGHFRCYLLLGWGAPALFVIPWVIVRYLRENTQCWERNEVKAIWWIIRTPILITILINFLIFIRILGILVSKLRTRQMRCPDYRLRLARSTLTLVPLLGVHEVVFAPVTEEQVEGSLRFAKLAFEIFLSSFQGFLVSVLYCFINKEVQSEIRQGWRHRRLRLSLQEQRPRPHQELAPRAVPLSSACREAAVGNALPSGMLHVPGDEVLESYC", "text": "FUNCTION: This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family."}
{"protein": "MNPAHLLVLPAVCVSFLGASIIPPQSLNLIQFKDMIRCTIPCERTWGEYADYGCYCGKGGSGRPVDALDRCCYVHDNCYGEAQKRNCNPYMKSYSFKCAKRTLFCYDAPGSCARFVCDCDRTAALCFGDSEYIGRHKNIDTKRHCQ", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
{"protein": "MVVLGQKFPEVEVQTTHGRMRLPDHYRGKWFVLFSHPADFTPVCTTEFVEFARNYDKFKAMNTELIGLSIDQVFSHIKWIEWIKEKFNVEIPFPVIADDQGELARMLGMISPYKGTNTVRAVFIVDPEGYIRAMLYYPQETGRNIPEILRLVEALQTADKYGVATPANWHVDRYEFKPSSIVGNDVIIPPASSLEEKKDREERAKKGEIECFDWWFCHKKLE", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily."}
{"protein": "MATMEELKLQIETLQSELCKLKATSAGGAREKIEKMSSEVVDSNPYSRLMALQRMGIVSEYERIRQKSVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAAKTLNFINPDVKILTNNYNITTVESFDKFLNAIKTGGIEEGTPVDLVLSCVDNFEARMAINTACNELSLNWFESGVSENAVSGHIQFIRPGDTACFACAPPLVVAENIDEKTLKREGVCAASLPTTMGIVAGMLVQNTLKYLLNFGTVSDYLGYNALIDFFPKMSLKPNPTCDDRFCIDRQKDYAARPKEERVEEVPEEETPLHEENLYGIELVAEDDTQGSQPSTGTTHSISTGLKLAYEPPASTKHSETTSTTAVSDDVSLDELMAQMKSM", "text": "FUNCTION: E1-like enzyme which activates UFM1. SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5 subfamily."}
{"protein": "MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISKSLKESEALPEKEGEELGEGERPEEDAAALELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPAERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGQVEVLKATEMVEVGADDDEGGAERGEAGDLRRGSSPDVHALLEITEESDAVLVDKSDSD", "text": "FUNCTION: Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity). SUBCELLULAR LOCATION: Membrane, caveola Cell membrane Microsome Endoplasmic reticulum Cytoplasm, cytosol Mitochondrion Nucleus Note=Translocates to the cytoplasm from the caveolae upon insulin stimulation (PubMed:17026959). Colocalizes with CAV1 in lipid rafts in adipocytes. Localizes in the caveolae in a caveolin-dependent manner (By similarity). SIMILARITY: Belongs to the CAVIN family."}
{"protein": "MSKQDDMRAYLPPFLTSLKEMAELLKAEAPEFDKQNDSIFDLTDQLFVPTATWGLSRWEKILNVPRESGDTDEIRRLRLISKMSNIPPITYRAIEQAVNRFLKNPSAQVRLLPGEYRFNVDINVDDLQHMNELIEAIENMKPAHLAYTLRGGLNETLRIKDTVILNHRRYRTASELKVGYSVTLNNNEVVLT", "text": "SIMILARITY: To B.subtilis YqcA."}
{"protein": "MLRRKPSNASDKEPTQKKKLSLQRSSSFKDFAKSKPSSPVVSEKEFNLDDNIPEDDSGVLTPEDSGKSGKKLGKKWRAVISRTMNRKMGKMMVKALSEEMGDTLEEGSASPTSPDCSLDSPGPEKMALAFTEQEEREPPSLSRQTSTGSELCSPGPGSGSFLEESPAPQYTGPFCGRARVHTDFTPSPYDHDSLKLQKGDVIQIVEKPPVGTWLGLLNGKLGSFKFIYVDVLPEEAVGPVRPSRRQSKGKRPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKELRETHLNELNIMDPQHRAKLLTAAELLLDYDTGSEEAEEGAESSQEPVAHTVSEPKVDIPRDSGCFEGSESGRDEAELAGTEEQLQGLSLSGAP", "text": "FUNCTION: May function as a signaling adapter protein in lymphocytes."}
{"protein": "MTFKRFSPLSSTSRYARLLAVASGLVAAAALATPSAVAAPEAESKATVSQLADASSAILAADVAGTAWYTEASTGKIVLTADSTVSKAELAKVSNALAGSKAKLTVKRAEGKFTPLIAGGEAITTGGSRCSLGFNVSVNGVAHALTAGHCTNISASWSIGTRTGTSFPNNDYGIIRHSNPAAADGRVYLYNGSYQDITTAGNAFVGQAVQRSGSTTGLRSGSVTGLNATVNYGSSGIVYGMIQTNVCAEPGDSGGSLFAGSTALGLTSGGSGNCRTGGTTFYQPVTEALSAYGATVL", "text": "FUNCTION: Has a primary specificity for large aliphatic or aromatic amino acids. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MSGTTHHHATFPAVEAAAFTRRHLDDLAAGLLGTVRVPGFFGRPALDTMLTSLHRVPVVSFDLDRMHHPMARFGTALNDYRTPELALDADRYWHDADTARRQWAGIGMTPDPLELALDALGRAWGVRPAPATIGGRPAFVGMLREVNDGTFIHYDDINREYRGGLFDQKIVAQLAFNAWLAAPREGGTTTVWRHRWEPADENRRHGYGFQPTAVADDPYVTVAPAAGDALLFNANNYHVVHPGAPGQRRIALACFLGVTAGGELVVWS", "text": "FUNCTION: Involved in the biosynthesis of terminal alkyne-containing amino acids such as L-beta-ethynylserine, that are produced as antibiotics by S.cattleya. Catalyzes the hydroxylation of the dipeptide L-gamma-glutamyl-L-propargylglycine, leading to L-gamma-glutamyl-L- beta-ethynylserine. Cannot use L-propargylglycine as substrate."}
{"protein": "MRLTVWTYEGPPQVGAMRVATAMRGVHYVVHAPQGDSYADLLFTMIERRPGRPAVSYTSFQARDLGTDTAALFKTAAADAVARFQPEALLVGSSCTGELIQDDPGGLAKALGLSIPVIPLELPSYQRKENWGAAETFYRLVRTMAGPAAPAPGTPRAPRPAGQRPRCNLLGPTALGFRHRDDVQAVVALLGRMGVDVAVVAPLGASPADLARLGEADFNVVLYPEIADTAVRWLERAFGQPSVRTVPIGVGATRAFIAEVAAVAGVDPAPALAEESLRLPWWSRSVDSTYLTGKRVFIFGDATHAVAAARVATEEFGFEVVGLGTYAREYARELRACAGALGLEALITDDYLDVEAAIADAHPDLVLGTQMERHIAKRLGVPCAVISAPVHVQDFPARTAPQMGFDGANVLFDTWVHPLMMGLEEHLLMMFRDDFEFHGDAAPSHLSAHRPTGEAVGDAVGEPPAAPRDQAAPAATLDGSAAQSDPARTTPPGAPSWEDSAEKELRKVPFFVRGKARRNTERFAAERGLASISVETLYDAKAHFGR", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex. SIMILARITY: Belongs to the ChlB/BchB/BchZ family."}
{"protein": "MALKSKPGIMNITPGSKISVIRSKRVIQANTISSCDIIISDGKISSVLAWGKHVTSGAKLLDVGDLVVMAGIIDPHVHVNEPGRTDWEGYRTATLAAAAGGITAIVDMPLNSLPPTTSVTNFHTKLQAAKRQCYVDVAFWGGVIPDNQVELIPMLQAGVAGFKCFLINSGVPEFPHVSVTDLHTAMSELQGTNSVLLFHAELEIAKPAPEIGDSTLYQTFLDSRPDDMEIAAVQLVADLCQQYKVRCHIVHLSSAQSLTIIRKAKEAGAPLTVETTHHYLSLSSEHIPPGATYFKCCPPVRGHRNKEALWNALLQGHIDMVVSDHSPCTPDLKLLKEGDYMKAWGGISSLQFGLPLFWTSARTRGFSLTDVSQLLSSNTAKLCGLGIVKEPLKWVMMLIWSSGILTKSFRCKKMIFITRISSPHIWDSFFKEKSWLLLFEGLLFISKGSMLPNQLENLFLYTLWSLVKPVHPVHPIIRKNLPHI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family."}
{"protein": "MTAAHKLTYGQRAARFTNPAAKALLETMERKKSNLSVSVDVVKSADLLAIVDTVGPYICLIKTHVDVVEDFDSSLVTKLQALAEKHDFLIFEDRKFADIGNTVALQYSSGVHKIASWSHITNAHPVPGPSIISGLASVGQPLGRGLLLLAEMSTKGSLATGAYTEAAVQMARENRGFVIGFIAQRRMDGIGAPPGVNVEDEDFLVLTPGVGLDVKGDGMGQQYRTPKQVVQEDGCDVIIVGRGIYGKDPSKVEEIRRQAERYQAAGWAAYIERVNALV", "text": "SIMILARITY: Belongs to the OMP decarboxylase family."}
{"protein": "MNYEVVIPAAGQGKRMNAGKNKLFIEAKGIPVIIHTLKVFENHDACKRIILVINEQEFGEFNTLLKTYHFKTPIEMVPGGRERQQSVFAGIKAAGKEETVLVHDGARPFIKREYIEQLVEKAKETGAAIVAVPVKDTIKRVQDGEIAGTIERSSLWAAQTPQAFRLSILMNAHLEAEAKGFLGTDDASLVEEAGGTVAIIQGDYQNIKLTTPDDLLVAEAILEAEKRNEHV", "text": "FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily."}
{"protein": "MNISRMEQRVLHVLAQGGYIRHQREDGHICEIECFTREGYLLSDCTMAVFQQLRRKRLIESRMGSPYRISFKGRENVRAQLNNR", "text": "SIMILARITY: Belongs to the UPF0386 family."}
{"protein": "TEGPYFYVPMVNTTGIVRSPYEYPQYYLVNPAAFAILGAYMFFLIIVGFPVNFMTLYVTLEHKKLRTPLNYILLNLAVADLFMVIGGFTTTMYTSMHGYFVLGRLGCNLEGFFATLGGMISLWSLAVLAIERWVVVCKPISNFRFGENHAIMGVSLTWGMALACTVPPLVGWSRYIPEGMQCSCGIDYYTRAEGFNNETFVLYMFCCHFTVPLTIIFFCYGRLLCAVKEAAAAQQESETTQRAEREVTRMVVIMVIGFLVCWLPYASVAWFVFTHQGSEFGPLFMTIPAFFAKSSAIYNPMIYICMNKQFRHCMITTLFCGKNPFEGEEEGASSTKTEASSASSVSPA", "text": "FUNCTION: Photoreceptor required for image-forming vision at low light intensity. While most salt water fish species use retinal as chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of retinal and 3-dehydroretinal (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cell projection, cilium, photoreceptor outer segment Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "AEPLASQLKEPIAGGGWWAA", "text": "FUNCTION: Inhibits trypsin and chymotrypsin."}
{"protein": "MKLQLHLALSLLAAIVAANPIRLDQRQITGNELRDGSCHDVTFIFARGSTELGYLGSTVGPATCNVLKLRKPGQVACQGVAPAYIADLASNFLPQGTNQIAINEAKSLFELAASKCPNTKIVAGGYSQGAAVMHAAISTLSSTVQDQIKGVVLFGDTRNKQDGGRIPNFPTDKTKIICAFGDLVCEGTLVITAAHLSYIDDVPDAADFLVGKL", "text": "FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (By similarity). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (Probable). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family."}
{"protein": "MKNYKAYLIDLDGTMYKGNEEIDGAAQFISYLNNQNIPHLYVTNNSTKEPEEVASKLNTMGIVAQADEVVTSALATAEFIAEESPGATVYMLGGSGLSNALTAQGLVLKDDEFVDYVVVGLDEQVTYEKLSTATLGVRNGAKFISTNQDVSIPKERGFLPGNGAITSVVSVSTGVQPVFIGKPEPIIMNKALEILDLDRSDVAMVGDLYDTDIMSGINVDIDTIHVQTGVTTKEEIEKKSVPPTYTFKDLNEVIKELEK", "text": "FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family."}
{"protein": "MIYAGILAGGIGSRMGNVPLPKQFLDLDGKPILVHTVEKFLLTSEFDKIFIATPQKWISHTKDTLRKHHITDDRIEVVQGGSDRNETIMNIISAAEKENGISDDDVIITHDAVRPFLTRRIIKENIESVLKYGAVDTVITATDTIITSADGDSIQSIPVRSEMYQGQTPQSFNVNLLRNSYNDLSDEDKQIMTDACKILVVAGKQVKLVMGELYNIKITTPYDLKVANSIIKGGMLSD", "text": "FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to D- ribitol 5-phosphate. SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI subfamily."}
{"protein": "MKYRDLRDFLALLEQRGELKRISLPIDPYLEMTEIADRTLRAGGPALLFENPKGYTMPVLCNLFGTPERVALGMGQESVNALRDVGKLLAFLKEPEPPKGFRDLLDKAPQFRQVLHMPTKRLNSAPCQEQIWQGEDVDLGRIPIMHCWPGDAAPLITWGLTVTRGPHKERQNLGIYRQQVLGKNKVIMRWLSHRGGALDFQEWTQQNPGQRFPVAVALGADPATILAAVTPVPDTLSEYAFAGLLRGSKTKVVKCASCDLDVPASAEIVLEGYLETGETATEGPYGDHTGYYNETDSFPVFTITHITQRRDALYHSTYTGRPPDEPAVMGEALNEVFVPILQKQFPEIVDFYLPPEGCSYRLAVVTIKKQYAGHAKRVMMGVWSFLRQFMYTKFVIVCDDDINARNWKDVIWAMTTRMDPARDTVLMENTPIDYLDFASPVSGLGSKMGMDATNKWPGETQREWGTPIEMDRTVRARVDAIWDQLAILNNGHES", "text": "FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the UbiD family."}
{"protein": "MADLPASLLILNGKSADNEQLREAIMLLRDEGIKIHVRVTWEKGDAARFVDEARQLGVATVIAGGGDGTINEVATALIQCEGNVIPALGILPLGTANDFATSVGIPVALDKALKLAIAGNAIEIDIAQVNKETCFINMATGGFGTRITTETPEKLKAALGGVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLKPDEENPNIIDGASAWFDIQAPHDITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR", "text": "FUNCTION: Probably phosphorylates lipids; the in vivo substrate is unknown. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS lipid kinase subfamily."}
{"protein": "MYFHSTAIILFLNKIDLFEIKITHTNITVAFPDYEGPRERDCALEYIRVQFISLNNNKNRKIYQHVTSATDTARIQVVIDMLFDIIISASLKMVGV", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (By similarity). Plays role in innate immunity and maintaining survival in response to metabolites of E.coli (PubMed:21108728). This might be by regulating the expression and signaling of genes such as lys-8, ins- 7 and daf-28 (PubMed:21108728). Has a role in lifespan to promote longevity (PubMed:17187771, PubMed:21108728). SIMILARITY: Belongs to the G-alpha family."}
{"protein": "ARDAYIAKPHNCVYECYNPKGSYCNDLCTENGAESGYCQILGKYGNACWCIQLPDNVPIRIPGKCH", "text": "FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active on both mammals and insects, since it inhibits inactivation of rNav1.4/SCN4A, hNav1.5/SCN5A, mNav1.6/SCN8A and insect BgNav1 and DmNav1 channels (PubMed:23637230). In vivo, it shows paralytic activity in mice (PubMed:4091860). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MSSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSASYKATIGADFLTREVLVDDRQVTMQLWDTAGQERFQSLGVAFYRGADCCVLVFDVNNSKSFDALDSWRDEFLIQASPRDPDNFPFVVLGNKIDVEESKRVISTKRAMTFCQSKGGIPYFETSAKEAINVEQAFEVIARNALAQEESEEFSGDFQDPINIHIDNDRDGCAC", "text": "FUNCTION: Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). Required for fungal morphogenesis, vacuole fusion, autophagy, stress resistance and pathogenicity (PubMed:25991510). SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MPLRGLAKAKNFTLGPTAPMKTFTENVHSQNNEINNLKKIDKTHNLTNNSQNEKLYKYESQIKSSFDRIVPTLKEIARIQHHEDFINTAQSISKQNLGINLPTHILDKSWVKPLDMRALYAWCAFKQHEKLSDNFFENDPLEGSFGSPNANNFETALLDCGIHLLDITPCSDGRLAHSVAYVMRIPFSAVRRRSHAGALFDIENTVNRWVKTEHKRYRENNPNEAHEDTRYLKIVTYHFSSVDPLHQGCAAHGSDDKLAAKEGSEKLLAFKEAVENSFCCGASVDLMLIGLDTDTDSLKIHLSSSDGKIDLENTISSLDIYNSTINFSKDEAEKEICQIISGNSNKVQLKGLDKFVYKLIVNNISQIDYVKKFHKGSYEDIGHAERFIGVGIGFKEVHLRNLTYFAHLDTVEEGAPDLDVGVKIFTGLNVSQDLPIPIVIRFDYSGKVPGAKERAAKDCYRVNNAISIRYKSLVDKGLLHTCLTIRDRDNIHSAQIIGMSLDQKTKEAH", "text": "FUNCTION: Reversible hydration of carbon dioxide (PubMed:14729686). Essential for photosynthetic carbon dioxide fixation, supplies CO(2) to RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) in the carboxysome (Probable). There are estimated to be 29 CsoSCA oligomers per carboxysome (PubMed:22155772). SUBCELLULAR LOCATION: Carboxysome Note=While the protein is very difficult to identify due to its low abundance, the enzyme activity fractionates with the carboxysome. This cyanobacterium makes alpha-type carboxysomes. SIMILARITY: Belongs to the beta-class carbonic anhydrase family. CsoSCA subfamily."}
{"protein": "MLRIDNLDKRYKTGDLALKGVSLHIGAGDIVGLIGPSGAGKSTLIRCVNRLVPPTGGSIRLGDTELTRLGGADLRRARRRIGMIFQEFALIERLTVMENVLSGRLGYVGFWASWFRRFPQADVQRAFALLARVGLSDQVDKRADALSGGQRQRVGIARALAQDPELLLIDEPTASLDPKTSRQVMRLITELCAERRLAAIVNIHDVALAQMFLPRIVGLRAGEVVYDGPASGLTPDVLTSIYGEEDWSKTSDDVEIVDAAPRAADLSAPLKLDPALARL", "text": "FUNCTION: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Phosphonates importer (TC 3.A.1.9.1) family."}
{"protein": "MLPSLQSLTKKVLAGQCVPTNQHYLLKCYDLWWHDGPITFDHNLKLIKSAGIKEGLDLNTALVKAVRENNYNLIKLFAEWGANINYGLVSVNTEHTWDLCRELGAKETLNEEEILQIFIDLKFHKTSSNIILCHEVFSNNPILQKVNNIKMRIEIFWELRELIEKTDLLNNEFSLSTLLLKYWYAIAIRYNLKEAIQYFYQKYTHLNTWRLTCALCFNNVFDLHEAYEKDKIHMDIEEMMRIACIKDHNLSTMYYCYVLGGNINQAMLTSIQYYNIENMFFCMDLGADAFEEGTIALGEGYKLIKNILSLKIYSPATTPLPKSTDPEIIDHALKNYVSKNMMIFLTYDLR", "text": "FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. SIMILARITY: Belongs to the asfivirus MGF 360 family."}
{"protein": "MWSLRGLRLAAGHCFRLCERNVSSPLRLTRNTDLKRINGFCTKPQESPKAPTQSYRHRVPLHKPTDFEKKILLWSGRFKKEEEIPETISFEMLDAAKNKIRVKVSYLMIALTVAGCVYMVIEGKKAAKRHESLTSLNLERKARLREEAAMKAKAD", "text": "FUNCTION: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues. May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition. May be involved in hypoxia- induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0389 family."}
{"protein": "MVDESTRKTLSSIPLLQTKAGPRDKELWVQRLKEEYQALIKYVQNNKSSDSDWFRLESNKEGTKWFGKCWYVHNLLKYEFDVEFDIPVTYPATAPEIALPELDGKTAKMYRGGKICLTDHFKPLWSRNVPKFGIAHAMALGLAPWLAVEIPDLIEKGVVAYKEKGETSS", "text": "FUNCTION: E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UFC1 subfamily."}
{"protein": "MAMKKLLWVVLSLSLVLGVANSFDFHEKDLESEESLWDLYERWRSHHTVSRSLGEKHKRFNVFKANVMHVHNTNKMDKPYKLKLNKFADMTNHEFRSTYAGSKVNHHKMFRGSQHGSGTFMYEKVGSVPASVDWRKKGAVTDVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDKEENQGCNGGLMESAFEFIKQKGGITTESNYPYTAQEGTCDESKVNDLAVSIDGHENVPVNDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGDCNTDLNHGVAIVGYGTTVDGTNYWIVRNSWGPEWGEQGYIRMQRNISKKEGLCGIAMMASYPIKNSSDNPTGSLSSPKDEL", "text": "FUNCTION: Thought to be involved in the hydrolysis of stored seed proteins. In vitro, catalyzes the hydrolysis of proteins, such as azocasein. Shows a preferential cleavage for Asn-|-Xaa in small molecule substrates such as Boc-Asn-|-OPHNO(2). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Vacuole, aleurone grain. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MPKTKHWHYSIPPEELDDERTAKAFIRELRISPKHAREICRAIRGMPLDRAKEFLRRVIRKEEAVPFRKHKKKVPHRRQIRPGWDAGRFPEKAAREILRVLEHAEANAEYKGLDTDRLYIKHIAAHKGRVIRGWIPRAFGRATPFNTPTTHIEVILEER", "text": "FUNCTION: The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. FUNCTION: This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL22 family."}
{"protein": "MRPTLLWSLLLLLGVFAAAAAAPPDPLSQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYQVQFKYTDSKWFTADIMSIGVNCTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPENIEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQVILISVGTFSLLSVLAGACFFLVLKYRGLIKYWFHTPPSIPLQIEEYLKDPTQPILEALDKDSSPKDDVWDSVSIISFPEKEQEDVLQTL", "text": "FUNCTION: Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG) (PubMed:8124716, PubMed:7673114, PubMed:7615558). Ligand binding stimulates activation of the JAK/STAT signaling pathway (PubMed:8124716, PubMed:7673114, PubMed:15356148). Required for signal transduction in contrast to other receptor subunit responsible for ligand binding (PubMed:7673114). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cytoplasmic vesicle membrane; Single-pass type I membrane protein Golgi apparatus membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Cytoplasm Note=Has low cell surface expression and high cytoplasmic expression in T cells. The bias towards cytoplasmic expression may be due to ligand-independent receptor internalization and recycling. SIMILARITY: Belongs to the type II cytokine receptor family."}
{"protein": "MKIKVASAVLAVSILFSGWLYWGSDLKVEQVLTSNEWQSTMVTVITDNLPDDTVGPLRRVNVESNVKYLPNGDYIRVANIKLFAQGSTAESTINISEKGRWEVSDNYLLVSPSEFKDISSSQSKDFSEAQLRLITQIFKLDAEQSRRIDVVNEKTLLLTSLNHGSTVLFRN", "text": "FUNCTION: Interacts with ToxR and stimulates its activity. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein; Periplasmic side."}
{"protein": "MHVKKYLLKGLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIICEGPKKKAMWFVLTLLFTSLVCWQWGLFIKTYLNWEVSVSLSIGFKTMDFPAVTICNASPFQYSKVQHLLKDLDELMEAVLGRILGPELSQVNDTRALNLSIWHHTPLVFINEQNPHHPVVLDLFEDNFNGSASNSPAPGRPCSAHRCKVAMRLCSHNGTTCTFRNFSSATQAVTEWYTLQATNIFAQVPNQELVAMGYPAERLILACLFGAEPCNYRNFTPIFHPDYGNCYIFNWGMTEKALPSANPGTEFGLKLILDMGQEDYVPFLTSTAGARLMLHEQRSYPFIKEEGIYAMAGMETSIGVLVDKLQRKGEPYSQCTKNGSDVPIQNLYSNYNTTYSIQACIRSCFQEHMIRECGCGHYLYPLPHKRKYCNNQEFPDWAHCYSALRISLAQRETCIYACKESCNDTQYKMTISMAVWPSEASEDWIFHVLSQERDQSSNITLSRKGIVKLNIYFQEFNYRTIEESAANNIVWLLSNLGGQFGFWMGGSVLCLIEFGEIIIDFVWITIIKLVALAKSVRQKRAQARYEGPPPTVAELVEAHTNFGFQPDLATPGPDVEAYPHEQNPPIPGTPPPNYDSLRLQPLDVIESDSEGDAI", "text": "FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane Note=Apical membrane of epithelial cells. SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1B subfamily."}
{"protein": "MSHSRFKSAKSAMRKLKTEQRKFGDRVSQHTSPRVNRWFKWMAPGLFVKRWMVISAVGLTLMFLGLAIWVKLTPIFRITEFVSDTLGFLTNLLPNYVSGPLILALGLFFVFWGQSRTVGSISEVLQPDNDQELVDVLLAHRRLNKGAKIVVVGGGTGLSTLLRGLKHYSANITAIVTVADDGGSSGRLRREMGMLPPGDIRNCIGALADEEKLLTELFQYRFKAGDGLSGHSFGNLFLTAMAEITGDLEMAAIACSKVLAVRGKVLPATLDDVKLWAEMEDGRYVEGESNIPEAQGRIRRIGCLPESPKALPAVLKAIKAADYIIIGPGSLYTSILPNLLIPEIQTAIAKAKVPRIYICNVMTQPGETDNYTVSDHLTAIDQVSSARLYDAVLVQRNPPSAPVLKKYAAENSHPVYLDRQAVIEKGCRIVLANVMQEDEKSHQVRHDPQRLARVLMRWYGGQ", "text": "FUNCTION: Required for morphogenesis under gluconeogenic growth conditions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gluconeogenesis factor family."}
{"protein": "MTEMDFDLEQIQKYELPDFETALLFSIVAKKNFLVLFDAEQRKLNDEISNEELIQKSVGDVMQKRTDFKINFKYQCINHVTDEMISEIQKCELDDYKNLETMEHVDEKGDRSANIAGVDQNVTIEFYLVEDIDRQSLADYYQLGRLMREGYIFNVQHNGIANNKKYWKLFIGTVAWKRDEYIIPDDILQLGAADKKYSHKHGQSFKLKSFSTGFEDWIRHKFWLVTTLAMPNIKPTIEVQAADDTASFSSVVITKDEAKEEEAITGSSDGAEKIISGDYKNYDNIHIQASLRRYILDIMVHIRTHRLTFNARGGGIHKNCYSNMITLSKIICIKDHKSFVVPQHVRLAAMWFLPLQLSVIDDSLKDNSILYGSKPELVRELMKRVVYVRNKQIIDMDNPLFMEALIVKSALKKIVPPV", "text": "FUNCTION: May be involved in telomere capping. SIMILARITY: Belongs to the MTC2 family."}
{"protein": "MAQWEMLQNLDSPFQDQLHQLYSHSLLPVDIRQYLAVWIEDQNWQEAALGSDDSKATMLFFHFLDQLNYECGRCSQDPESLLLQHNLRKFCRDIQPFSQDPTQLAEMIFNLLLEEKRILIQAQRAQLEQGEPVLETPVESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFCFRYKIQAKGKTPSLDPHQTKEQKILQETLNELDKRRKEVLDASKALLGRLTTLIELLLPKLEEWKAQQQKACIRAPIDHGLEQLETWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDPLTKGVDLRNAQVTELLQRLLHRAFVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQGFRKFNILTSNQKTLTPEKGQSQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWFNLLSPNLQNQQFFSNPPKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLPFWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTMSGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDELQQPLELKPEPELESLELELGLVPEPELSLDLEPLLKAGLDLGPELESVLESTLEPVIEPTLCMVSQTVPEPDQGPVSQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEIMPNGDPLLAGQNTVDEVYVSRPSHFYTDGPLMPSDF", "text": "FUNCTION: Signal transducer and activator of transcription that mediates signaling by type I interferons (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state (PubMed:9020188, PubMed:23391734). In addition, has also a negative feedback regulatory role in the type I interferon signaling by recruiting USP18 to the type I IFN receptor subunit IFNAR2 thereby mitigating the response to type I IFNs (PubMed:28165510). Acts as a regulator of mitochondrial fission by modulating the phosphorylation of DNM1L at 'Ser-616' and 'Ser-637' which activate and inactivate the GTPase activity of DNM1L respectively (PubMed:26122121, PubMed:23391734, PubMed:9020188). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocated into the nucleus upon activation by IFN-alpha/beta. SIMILARITY: Belongs to the transcription factor STAT family."}
{"protein": "RDCGKMCEEETWKG", "text": "FUNCTION: Probable toxin. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MGQQLSWEEAEAAGEMDVAELQEWYKKFVVECPSGTLFMHEFKRFFKVTGNEEASQYVESMFRAFDKNGDNTIDFLEYVAALNLVLRGSLEHKLKWTFKIYDKDRNGCIDRLELLDIVEAIYKLKKACRAELDLEHQGQLLTPEEVVDRIFLLVDENGDGQLSLTEFIEGARRDKWVMKMLQMDINPGCWITQQRRRSAMF", "text": "FUNCTION: Stimulates two retinal guanylyl cyclase (GCs) GUCY2E and GUCY2F when free calcium ions concentration is low, and inhibits GUCY2E and GUCY2F when free calcium ions concentration is elevated (By similarity). This Ca(2+)-sensitive regulation of GCs is a key event in recovery of the dark state of rod photoreceptors following light exposure (By similarity). May be involved in cone photoreceptor response and recovery of response in bright light (PubMed:25673692). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Note=Subcellular location is not affected by light or dark conditions."}
{"protein": "MATAMTVSSKLRGLLMQQLRGTSQLYFNISLRSLSSSAQEASKRAPEEVSDHNYESIQVTSAQKHVLHVQLNRPEKRNAMNRAFWRELVECFQKISKDSDCRAVVVSGAGKMFTSGIDLMDMASELMQPSGDDAARIAWYLRDLISKYQKTFTVIEKCPKPVIAAIHGGCIGGGVDLVSACDIRYCTQDAFFQIKEVDMGLAADVGTLQRLPKVIGNQSLVNELTFSARKMMADEALDSGLVSRVFQDKDAMLNAAFALAADISSKSPVAVQGSKINLIYSRDHSVDESLDYMATWNMSMLQTQDIIKSVQAAMEKRDTKSITFSKL", "text": "FUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4- trans-dienoyl-CoA. SUBCELLULAR LOCATION: Mitochondrion Peroxisome. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MTGADDPARPAVGPQSFRDAMAQLASPVTVVTVLDAAGRRHGFTAGSVVSVSLDPPLVMVGIALTSSCHTAMAAAAEFCVSILGEDQRAVAKRCATHGADRFAGGEFAAWDGTGVPYLPDAKVVLRCRTTDVVRAGDHDLVLGTPVEIRTGDPAKPPLLWYRRDFHTPTPTTPALA", "text": "FUNCTION: Provides the reduced form of flavin mononucleotide for the PIIA synthase reaction."}
{"protein": "MAKPDNRNDNVEKLQEMVQDTIENLEEAHETLQNNSLSRDQRQAIMEKNKRREESIRSFRNEIKDEYQDLH", "text": "SIMILARITY: Belongs to the Tlp family."}
{"protein": "MLTLGGERTSGESVRKQNVLAACSFANFVKTSLGPVGLDKMLVDDVGDVTITNDGATILKLLDVEHPAAKILVQLAQLQDEEVGDGTTSVVILAAALLKNADELISRFVHPTTVINGYRLACREACKYIQEHMAYDVNKLGKAGLINVARTAMSSKLINLDADMFSQMAVDALMAVEVSGGPKGPVYPIKAVNILKAHGRSMSESMLIDGYALNCTAASQQMPRIIKKAKIAFLDFSLQKVKMKLGVQVVVKDPAQLEAIRQREADITKERIQKILNAGANVILTTGGIDDLCMKYFVEVNAMAVRRCKKVDLKNMAKATGGQLIVSLADMEGDEVFDPTKLGNAEEVSQERICDDELIILRGPKVHPSASIILRGANDFYVDEMERSLHDALLVVKRVLESKRIVPGAGACETAVSIYLENYALTLSSREQLAIAEFARAMLSIPKQLAVNAGVDSTELVARLRSCHNSSQSKPDQAHNKWWGLDLNNQYVADCKEIGVFEPLVSKIKSLKFATEAAITILRIDDLIKLKEEKQPDHDGDECGY", "text": "FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
{"protein": "MDIRPNHTIYINNMNDKIKKEELKRSLYALFSQFGHVVDIVALKTMKMRGQAFVIFKELGSSTNALRQLQGFPFYGKPMRIQYAKTDSDIISKMRGTFADKEKKKEKKKAKTMEQAAAAANKKPGQGTPNAANTQGTAAPNPQVPDYPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENDGQAGAARDALQGFKITPSHAMKITYAKK", "text": "FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RRM U1 A/B'' family."}
{"protein": "MTRGNQRELARQKNMKKQSDSVKGKRRDDGLSAAARKQRDSEIMQQKQKKANEKKEEPK", "text": "FUNCTION: Positive regulator of amyloid protein aggregation and proteotoxicity (By similarity). Induces conformational changes in amyloid proteins, such as HTT, driving them into compact formations preceding the formation of aggregates (By similarity). FUNCTION: Positive regulator of amyloid protein aggregation and proteotoxicity (PubMed:20723760). Induces conformational changes in amyloid proteins, such as HTT, driving them into compact formations preceding the formation of aggregates (PubMed:20723760). SIMILARITY: Belongs to the SERF family."}
{"protein": "MTTRILTGITPTGTPHLGNYAGAIRPAILASRRSDVDSFYFLADYHALIKCDDPARIQRSRLEIAATWLAGGLDVERATFYRQSDIPEIPELTWLLTCVSAKGLLNRAHAYKAAVDRNVEAGEDPDAGVTMGLYSYPVLMAADILMFNAHKIPVGRDQVQHVEMARDIGQRFNHLFGNGREFFVLPEAVIEENVATLPGLDGRKMSKSYDNTIPLFSPSRQLKDAIARIVTDSRAPGEPKDPDSSHLFLLYSAFASAEQVAAFRQELLEGLAWGEAKQRLFQLLDNELGEARERYQALIAKPDDIEDILLAGAAKARRIATPFIAELREAVGLRSLREPLKSAESGKKKAAKAARLVSFRDDDGSFRFRLLDAAGEQLLLSRAFADGKAAGAVSKRLLAGETADLRAEGNAFGLWLDGEAVAQSPAFADAAARDAAIERTREALAPQE", "text": "FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MDFHSCLYDIAERLGNEELAALKFLCLDHIPQKKQESINDVLVLFQRLQEEGMLEEDNLSFLKELLFHISRRDLLSRVLKSSPEEMVRELQVLGKAQVSAYRVMLFKLSEDMDKEDLKSFKFLLITEIPKCKLQDNSSLLDIFVEMEKRTILAENNLVTLKSICFRVNRSLLGRIDDYERSSTERRMSTEGGEELPVSVLDEVTIKMQDMWDSPGEQESESLNSDNVYQMKSKPRGYCLIFNNNNFSKAREDIPKLSNMRDRKGTNYDEEALSKTFKELHFEIVSFSDCTASQIHEVLVSYQSKDHKGKDCFICCILSHGDKGIVYGTDGKEASIYELTSYFTGSKCPSLAGKPKIFFIQACQGNNFQKAVPVPDETGLEQEHVLEEDSSSYKNYIPDEADFLLGMATVKNCVSYRDPTRGTWYIQSLCQSLRERCPRGEDILSILTGVNYDVSNKDNPRNMGKQMPQPIFTLRKKLFFPPN", "text": "FUNCTION: Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (By similarity). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death (PubMed:10197541). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (By similarity). Binding to the adapter molecule FADD recruits it to either receptor TNFRSF6/FAS mediated or TNFRSF1A (PubMed:10197541). The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (By similarity). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (By similarity). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (By similarity). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-325', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (By similarity). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-D (GSDMD): GSDMD cleavage promoting release of the N-terminal moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis (By similarity). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (By similarity). Cleaves PARP1 and PARP2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase C14A family."}
{"protein": "MSRYLGPRVRVIRRLGALPALTNKSPKKRTIAPGEHAHKTRKLSEFAVQLQEKQKLQYYYGITNSQLARYFRQARRSKSSTGLALLTMLETRLDHLVYRAGFAPTLPAARQLVNHGHVKVNGKKVTIASWACEVNHVIEVKSSSPPKPPEYLPPYLQLSNGTLTVTQPVQKEWLAFVVNELLVVEYYTRVGA", "text": "FUNCTION: With S5 and S12 plays an important role in translational accuracy. FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
{"protein": "MKINSNTIIIGKKVILVPYKKKHVEKYWKWMQSEEIREQTASEELTIEEEFENQESWFKDDHKITFIILDKDLLLENEKDSNGYSNENDIKSMIGDVNIFFNQYEDEGTAELEVMIAEPTSRRKGLAREAISIIMGYGIEHLSTITKKYIVKIGESNQPSIQMFKSMNFKQIGSVNVFKEILLEFENGENNINLLNLKNNDNYKSLIFKNWE", "text": "SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily."}
{"protein": "MERRMKAGYLDQQVPYTFSSKSPGNGSLREALIGPLGKLMDPGSLPPLDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENLAFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDPPRQIAIKSPAPGALGQSPLQPFPRAEQRNFLRSSGTSQPHPGHGYLGEHSSVFQQPLDICHSFTSQGGGREPLPAPYQHQLSEPCPPYPQQSFKQEYHDPLYEQAGQPAVDQGGVNGHRYPGAGVVIKQEQTDFAYDSDVTGCASMYLHTEGFSGPSPGDGAMGYGYEKPLRPFPDDVCVVPEKFEGDIKQEGVGAFREGPPYQRRGALQLWQFLVALLDDPTNAHFIAWTGRGMEFKLIEPEEVARLWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCEPEALFSLAFPDNQRPALKAEFDRPVSEEDTVPLSHLDESPAYLPELAGPAQPFGPKGGYSY", "text": "FUNCTION: Transcriptional activator (PubMed:19307308, PubMed:31552090). May play a role in keratinocyte differentiation (PubMed:31552090). FUNCTION: (Microbial infection) Binds to the enhancer of the adenovirus E1A gene and acts as a transcriptional activator; the core-binding sequence is 5'-[AC]GGA[AT]GT-3'. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family."}
{"protein": "MRVSGQSIIAISLFTLSLYIHRVQARPFVLVLSNEDLNGGFNDNGAYESSDFDEFGESEPKSEEELDPGSWRRIFETNESTVHASASPQYYSGLHKILSAASEGNTTLMEEAVSEIDSSASSGDPHAQSVMGFVYGIGMMRETSRSKSILHHHFAAAGGNMQSKMALAFRYLRQNMYDKAVELYAELAETAVNSFLISKDSPMAEPVRIHIGTEENKDALRKSRGEEDEDFQILEYQAEKGNSVAMHKIGLFYYFGLRGLRRDHAKALYWFSKAEFNGLGYLYVKGYGVDKRNYTKAREYFEMAANNEDPSGHYNLGVLYLKGTGVKKDVRHATKYFFVAANAGQPKAFYQLAKMFHTGVGLTKNLEMATTFYKLVAERGPWSSLSRWALEAYLKGDVGKAFILYSRMSELGYEVAQSNAAWIVDKYGERSMCMGVYGFCTDKERHDRAHSLWWRASEQGNEHAALLIGDAYYYGRGTERDFVRAAEAYMYAKSQSNAQAMFNLGYMHEHGEGLPFDLHLAKRYYDQALQSDTAAKLPVTLALASVWVRRNYADTALVQVLNSLPEVHQKVVEWVENGMLEEVVLDPVGANVAQPLAAPVAFPQ", "text": "FUNCTION: May be involved in the endoplasmic reticulum (ER) quality control system called ER-associated degradation (ERAD). SIMILARITY: Belongs to the sel-1 family."}
{"protein": "MKKRASVDSKESEDPPQEDYSLDPLDVDANSKTPPAKPHTFSVSKSRNRLFGKSDLEESSPIDCSFREGEAASCPTITVSSVVTSPRPADGPTSTRQLTQDSIPTSAEKPLKLYDRRSIFDAVAQNNCQDLDSLLPFLQKSKKRLTDTEFKDPETGKTCLLKAMLNLHNGQNDTISLLLDIARQTNSLKEFVNASYTDSYYRGQTALHIAIERRNMVLVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILILGAKLYPTLKLEELTNKKGFTPLALAASSGKIGVLAYILQREIPEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFIYCLYMIIFTMAAYYRPVDGLPPYKMKNTVGDYFRVTGEILSVIGGFHFFFRGIQYFLQRRPSVKTLFVDSYSEILFFVQSLFLLASVVLYFSHRKEYVACMVFSLALGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNESLSAEPHRWRGPGCRSAKNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHSAQPEEVHLKHFSGSLKPEDAEVFKDSAVPGEK", "text": "FUNCTION: Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli (PubMed:12243775). Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis (By similarity). SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein Cell projection, dendritic spine membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV1 sub-subfamily."}
{"protein": "MAGRLRGPAVPGGGESSDSDEDGWDIGYTERPDKLKDSLLSEEKDEVLKRALTTGDGSLLEELLNSGMQVDSSFRFGWTPLMYAASIANVDLVRILLDRGANASFSKDQHTVLMAACSARVPEERILKTAELLLSRNASPNATCRKRMSPLMYAAREGHSQLVALLVGHGAEINAQDDNGYTALAWAARHGHKTTVLKLLELGADKTLQTQDGKTPAEIAKRNKHPELFSMLSLTLNPLHGKFQNITKEENICKFLITDSEKSRDHGFSSYSAFGDLEIFLHGLQLEHLTELLKERDITLRQLLTLRKDDFTKIGITNVRDQKKIMDAVEELQVEEIKFEELPEVMKLEFSGDEFLNFLLKLSKQCGHLTTAVQDIISQFPVHSHKIVLEWGSPECFTSVCEDLVHNAQNLGEEVGKLKHLIQKLHNDQKNDSCRIPPMENVSTGKKRLWKRAAVTVCGFGLLFIVCKLTFLRK", "text": "FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with pi-bodies suggests a participation in the primary piRNAs metabolic process. Required prior to the pachytene stage to facilitate the production of multiple types of piRNAs, including those associated with repeats involved in the regulation of retrotransposons. May act by mediating protein-protein interactions during germ cell maturation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to pi-bodies, a subset of the nuage which contains primary piRNAs (By similarity)."}
{"protein": "MVNFVSAGLFRCLPVSCPEDLLVEELVDGLLSLEEELKDKEEEEAVLDGLLSLEEESRGRLRRGPPGEKAPPRGETHRDRQRRAEEKRKRKKEREKEEEKQTAEYLKRKEEEKARRRRRAEKKAADVARRKQEEQERRERKWRQGAEKAKQHSARKEKMQELGIDGYTRQLEGEVESLEAERRKLLQEKEDLMGEVNYWQGRLEAMWLQ", "text": "FUNCTION: Contributes to the regulation of viral RNA transcription by interacting with host proteins involved in transcriptional activation such as ATF4, or CREB1, and by inhibiting their activity. Additionally, HBZ suppresses host NF-kappa-B-driven transcription mediated by host RELA as well as transcription of some classical NF-kappa-B target genes, including IL8, IL2RA, IRF4, VCAM1, and VEGFA. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the HTLV-1 HBZ protein family."}
{"protein": "MVICLLLCTPTDIFVVASPEVNETQEYVPVNVYHDTDVTRKKIVTAQFECYQKIMKDNDHNKIGPVCNRTWDGWLCWDDTEAGFTSEQYCPDYFQDFDPSELVTKICSDNGHWFLHPESNRTWTNYTRCNEHTNEGRMTAMNLFYLALIGHGLSLTSLLISLGIFFYFKSLSCQRITLHKNLFFSFVLNSVITIIWLTAVANNQELVQRNPTSCKVSQFIHLYLFGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYLLGWGFPLIPASIHAIARSYYYNDNCWISSNTSLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESSLYMKAVRATLILVPLLGIQYVLLPYKPEGRVSSEIYDYIMHILMHYQGLLVATIFCFFNGEVQGVLRRHWNQYRIQFGSTFAHSDAMRSASYTASSITEVQGCYSIDSHTEHLNGKGAPLDIETSILKSENPFT", "text": "FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) (By similarity). Receptor specificity may be modulated by accessory proteins. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family."}
{"protein": "MPRSWTDIVAEKRAIRDEKLTKCYGENVPSDPRIIAAKDIQALTKLLEARNVTAEAVVLAHIAKAKEAHQRTNCLTEICFDEALEHARELDAFQQEHGRLKGPLHGVPVSLKDQFNLKGLDSTLGYVGRAFHPAASDCVLVKVLKQLGAVILAKTNLPQCILWGETDNPLWGLTTHPMNPEYTPGGSSGGEGTLLALNGSMLGWGTDIGGSIRVPSHMNGLWGFKPSSGRFSYEAVAVSQDGQQQIPSVVGPMARTLSTITLASKAMIEAECWRLDPQLPPMPWRKDVFQEYLQKPLVIGIMVDDGTVKVHPPIERVFKEFCKKLEAAGHELVPWDTSLNADCIKIMDEHYIADGGEDIRRDMAAGGEPYMPHVQNLVDRGSAISVYEYWQLNKRKKATQAAYNTMWNATKSSSGKPVDVLLVPTMPHTAIPHRTLRYPGYTKLFNMLDYSALSFPAGTALKALDSVCTGEYEPRNAADAWNWSLYDIEKMDGYSVGLQIVGRRMEEEKVLGAAHQVQQLL", "text": "FUNCTION: Amidase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2- AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N- malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N- malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable). SIMILARITY: Belongs to the amidase family."}
{"protein": "MSNAEASRVYEIIVESVVNEVREDFENAGIDEQTLQDLKNIWQKKLTETKVTTFSWDNQFNEGNINGVQNDLNFNLATPGVNSSEFNIKEENTGNEGLILPNINSNNNIPHSGETNINTNTVEATNNSGATLNTNTSGNTNADVTSQPKIEVKPEIELTINNANITTVENIDDESEKKDDEEKEEDVEKTRKEKEQIEQVKLQAKKEKRSALLDTDEVGSELDDSDDDYLISEGEEDGPDENLMLCLYDKVTRTKARWKCSLKDGVVTINRNDYTFQKAQVEAEWV", "text": "FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and implicated in the regulation of basal transcription. Interacts with TBP (the TATA-binding protein). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Imported to nucleus via interaction with KAP122. SIMILARITY: Belongs to the TFIIA subunit 1 family."}
{"protein": "MGCAASKLDNEDAVRRCKDRRRLMKEAVYARHHLAAAHADYCRSLRITGSALSSFASGEPLSVSDQTPAVFLHTPPPPLSEQSPAKFVPPRFSPSPAPSSVYPPSTSPSVASSKQPSVMSTSSNRRRKQQPKPRLPHILSESSPSSSPRSERSNFMPNLYPSAYQNSTYSATPSHASSVWNWENFYPPSPPDSEFFNRKAQEKKHNSDNRFNDEDTETVRSEYDFFDTRKQKQKQFESMRNQVEEETETEREEVQCSEWEDHDHYSTTSSSDAAEEEEEDDDRESISEVGTRSEFGSTVRSNSMRRHHQQPSPMPQVYGGAEQSKYDKADDATISSGSYRGGGDIADMKMVVRHRDLKEIIDAIKENFDKAAASGEQVSQMLELGRAELDRSFSQLKKTVIHSSSLLSNLSSTWTSKPPLAVKYRIDTTALDQPNSSKSLCSTLDRLLAWEKKLYEEIKAREGFKIEHEKKLSQLQSQEYKGEDEAKLDKTKASITRLQSLIIVTSQAVTTTSTAIIRLRDTDLVPQLVELCHGFMYMWKSMHQYHETQNSIVEQVRGLINRSGKGESTSELHRQATRDLESAVSSWHSSFSSLIKFQRDFIHSVHAWFKLTLLPVCQEDAANHHKEPLDAYAFCDEWKLALDRIPDTVASEAIKSFINVVHVISAKQADEHKIKKRTESASKELEKKASSVRNLERKYYQSYSMVGVGLPESGPDNQHMLDARDPLSDKKSELAVCQRRVEEEMVKYSKAIEVTRAMTLNNLQTGLPGVFQSLTSFSALFMESLQTVCTRSYSIK", "text": "FUNCTION: Required for nitrate signaling. Regulates expression of the nitrate-responsive genes NIA1, NIR1, NRT2.1 and NPF6.3/NRT1.1. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MASVSPLAKYKLVFLGDQSVGKTSIITRFMYDKFDTTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAVIVYDVANRQSFLNTSKWIEDVRTERGSDVIIVLVGNKTDLVDKRQVSIEEGDNKARDYGVIFIETSAKAGFNIKPLFRKIAAALPGMETLSSTKQEDMVDVNLKTSSNSAQGEQQRGGCAC", "text": "FUNCTION: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid- anchor. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MIETSQTIPELVSWAKDREFSLNLPTERLVFLLAIAIYNNERLDGEMLEADLVDIFRHTMNAFEQSTDAIATRANNAINELVNNVVNRFSSEFTEGLAIYRLTPLGVGVSDYYIRQREFSALRLSVQLSIVADEIQRASDSAEEGVENNESEHFWRRNVFAPLKYSVAEIFDSIDLSQRIMDENQQSIKDEIAELLTKDWQAAISSCERLLDETSGNLRELQDTLNAAGDKLQAQLLRIQDCVIGRDDLYFIDQLITDLQSKLDRIISWGQQAIDLWIGYDRHVHKFIRTAIDMDKNRVFSQRLRNSIHHYFDHPWFLWTAQAERLVDLRDEEMVLREDDALGELPEELQYESLSDLHDQIVEHMQGLLIAYRENNRPIDLSLVLKEQLENYPLSRHFDVARIIVDQAVRLGMANDDLSGIYPDWQAINKRGAEVQAHVIDKY", "text": "FUNCTION: Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Not required for mini-F plasmid partitioning. Probably acts via its interaction with MukB and MukE. Overexpression results in anucleate cells. It has a calcium binding activity. SUBCELLULAR LOCATION: Cytoplasm, nucleoid Note=Restricted to the nucleoid region. SIMILARITY: Belongs to the MukF family."}
{"protein": "MAEDNLTLDEFGGAMLASEAPIELSDKTAADLAPVFDVPVNISAVLGRANMSVAQLLQLGQGSILELDRKVGEAIDIYVNNRLVARGEVVVVDERLGVTMTEIIKDGDQG", "text": "FUNCTION: FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Bacterial flagellum basal body. SIMILARITY: Belongs to the FliN/MopA/SpaO family."}
{"protein": "MSPPLYSVLLEDENSVFLLDLDLSSPMGFHAYPHLPILDSSIANWSLPFSISDETFRESKKLKRTMIPISSADFSISSSSSLSVSVNSIPRLNFRDHIRTYKRYLAAEELPEDTNSSESVVGAEEDGCADGMRLVQLLIACAEAVACRDKAHASMLLSELKSNALVFGSSFQRVASCFVQGLAERLTLIQPIGSGAGVSQSMMNIMDAASEEMEEAYRLVYETCPHIQFGHFVANSTILEAFEGESFVHVVDLGMSLGLPHGHQWRGLIHSLANRASGHGRVRRLRITAIGLCIARLQAIGDELSDYANNLGINLEFSVVQKNLENLQPEDIKVNDDEALVVNSILQLHCVVKESRGALNSVLQMIHGLSPKVLVMVEQDSSHNGPFFLGRFMESLHYYSAIFDSLDAMLPKYDTKRAKMEQFYFAEEIKNIVSCEGPLRMERHERVDQWRRRMSRAGFQAAPIKMVAQAKQWLLKNKICDGYTVVEEKGCLVLGWKSKPIVAASCWKC", "text": "FUNCTION: Transcription factor acting as a regulator of arbuscular mycorrhiza (AM)-related genes (e.g. PT4, STR and RAM2) (PubMed:25560877). Required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis) (PubMed:25560877). Also involved in restricting mycorrhizal colonization of the root meristem (PubMed:25560877). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family."}
{"protein": "MEAAVAAAAAAAGAVTTAVAPPPGAAVSNGVATAPPPFLMKTYEMVDDPATDAVVSWGPGNNSFVVWNTPEFARDLLPKYFKHSNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGQKHLLKTINRRKPTHGNNQVQQPQLPAAPVPACVEVGKFGMEEEIEMLKRDKNVLMQELVRLRQQQQTTDHQLQTLGKRLQGMEQRQQQMMSFLAKAMHSPGFLAQFVQQNENSRRRIVASNKKRRLPKQDGSLDSESASLDGQIVKYQPMINEAAKAMLRKILKLDSSHRFESMGNSDNFLLENYMPNGQGLDSSSSTRNSGVTLAEVPANSGLPYVATSSGLSAICSTSTPQIQCPVVLDNGIPKEVPNMSAVPSVPKAVAPGPTDINILEFPDLQDIVAEENVDIPGGGFEMPGPEGVFSLPEEGDDSVPIETDEILYNDDTQKLPAIIDSFWEQFLVASPLSVDNDEVDSGVLDQKETQQGNGWTKAENMANLTEQMGLLSSHHTG", "text": "FUNCTION: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HSF family. Class A subfamily."}
{"protein": "MLKKLLSCCITSALCFHSSLAFSQPNEIADSAELQQAPDTLPATLMLAPDDIAIADRYIVVFQQPQMMASSSPEFEQFTQQSVDRMSGLYSIQVESVFDHSISGFVANLSPEQLKDLRSDPRVDYIEQDRILSLDPIVSADANQTNAIWGLDRIDQRNLPLDNNYSANFDGTGVTAYVIDTGVNNAHVEFGGRSVSGYDFVDNDADASDCNGHGTHVAGTIGGSLYGVAKNVNLVGVRVLSCSGSGSTSGVIAGVDWVAANASGPSVANMSLGGGQSVALDSAVQSAVQSGVSFMLAAGNSNADACNYSPARVATGVTVGSTTSTDARSSFSNWGSCVDVFAPGSQIKSAWYDGGYKTISGTSMATPHVAGVAALYLQENSSVSPSQVEALIVSRASTGKVTDTRGSVNKLLYSLTDADCGQDCGGPDPTPDPEGKLTSGVPVSGLSGSSGQVAYYYVDVEAGQRLTVQMYGGSGDADLYLRFGAKPTLNAWDCRPFKYGNNETCTVSATQSGRYHVMIQGYSNYSGVSIQANY", "text": "SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MTVTRVVDTSCRLGEGPVWHPDEKRLYWVDIESGRLHRYDPETGAHDCPVETSVIAGVTIQRDGSLLAFMDRGRVGRVVDGDRRESARIVDSPTRFNDVIADPAGRVFCGTMPSDTAGGRLFRLDTDGTVTTVETGVGIPNGMGFTRDRERFYFTETEARTVYRYAYDEETGAVSARERFVESPETPGLPDGMTVDSAGHIWSARWEGGCVVEYDADGTELGRFDVPTEKVTSVAFGGPDLDSLYVTTAGGDGDGSAGEGDESTGDAAGALFRLDVAATGRPEFRSDVRLG", "text": "FUNCTION: Pentonolactonase involved in D-arabinose and D-xylose catabolism. Catalyzes the hydrolysis of both L-arabino-gamma-lactone and D-xylono-gamma-lactone to the corresponding acids. Can also hydrolyze D-galactono-gamma-lactone and D-glucono-delta-lactone. SIMILARITY: Belongs to the SMP-30/CGR1 family."}
{"protein": "MEVKDIVFMNKGDGENSYVKSAGLTLKVIAKTQPMVQKAVQSLFKGTHSAPLQVVNVADLGCALGPQPLESMSIVIESIVEKCGELGCEMPEIQFHLNDLAGNDFNTLFKGLSVVQEKYKNVSWFAMGAPGSFHGRLFPRNSMHLVHSCYSVHWLSKAPKITSEEGLPLNKGKIYMSKTSPPAVKEAYLSQFEEDFSSVLRFRSPELAPDGRMVLILNGRQSADPTEKDICYLRDLLAEALSYLVSEGLIDEEKLGSFNVPYYNPSQEEVERVIDKEGSFTTEFSDTVVLEIGGKNAWSDPGLRIKGYRCFSEPVLSHQFGEEVMDKLFDKAEEILAEDYKQGKEATKNISIVVVLKKKTNQTWT", "text": "FUNCTION: Involved in the biosynthesis of theobromine. SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family."}
{"protein": "MTSLDDSVLTKKNIALLDNATNYIRPAIDYFHFKFNYDSLDVSTTWRLLLKMRKHKLLRLPSCSSENEFDYSIYMARLYHCIWRRWSIKHFNLDEYKIDPLSINWNKEIDVTVLYGPDLVGIHEREQPTPTDFPMGNIKEQGKQLLDVRKEGSASSLLKKGSVFYSKGKWLSQRSISFDDTVRRRDIDKRGRFRESCVLINDVEQFQNYSIVWDESRHRYRRQALPDTYDYEHLYPNGDETPRNTPHDNIIIHQNLHSITEGSYIYIK", "text": "SIMILARITY: To yeast YKR075c."}
{"protein": "MKAVVQRVTRASVTVGGEQISAIGRGICVLLGISMEDSQKELEHMVRKILNLRVFEDESGKHWSKSVMDKEYEVLCVSQFTLQCVLKGNKPDFHLAMPTEQAESFYNSFLEQLRKSYRPELIRDGKFGAYMQVHIQNDGPVTIELESPAPGAASSDPKQLSKLEKQQQRKEKTRAKGPSESSKERNAPRKEDRSASSGAEGDVSSEREP", "text": "FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. FUNCTION: ATPase involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Associated with chromatin at some replication origins containing functional DNA-unwinding elements (By similarity). SIMILARITY: Belongs to the DTD family."}
{"protein": "MEGLSSKAQTMGREDDNRSSKMKVFHSELVYGDNHNISIKKADLTGQHKMMLLLSSALRIGSVHMDVSRILVKWCPYITPNMNTTIGITIKNNHHDDMSNINDMSTYISVKGKMSEALQITWHPASTLVYKKGMSCIFPWVVDVDTGSTEQESGSPALGEIKIWCYFKMQYHKPSTRHIARAEIAPSIEWGNTNFPYYVPFAMIRRARGIRPLDVFSTNQYSMFLEDVIKHVGTDSIKESDIVPIMSTMSQEDMMMINEKNKTCLLKRGGSYCSCKDVIENVVKEINMNRDRKYDNHGLLLSGYIAGSTSGRFQTVPMLSDISY", "text": "FUNCTION: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma."}
{"protein": "MKNNQFAIVPTDSETAIAELTKIHFITPDMDALTTVPAVYQALLAKSLPEVHTASGLTHKFNNIMATSQHTLSEWLADATIVNNQVFYNVGLQLLGFLPGQDFELADPLLAMRDIHLPMVGDSAFDREALYYAWYLLLNTRGNNGQTLIESLTTRGYFVPFYQLPNDQKPLFFNGKAQAVFDTNALIRDVVYVEAPLDTDHDGQRDLLKVEILRPAETETGLKVPVLYTASPYNQGINDQAGDAQMHNVDVPLTAKEPDENTYADVEFQPTTAQLPAARTATTTTDTAEETFSREKSYTLNDYFLARGFAVVYAAGIGSIDSDGLAPTGDVDETTSTVAIIEWLTGKRQAFTNRDGNIAIKAWWCNGAVAMTGRSYLGTLATAAATTGVAGLKTIISEAAISSWYDYYRDNGLVVAPDTFQGEDTDVLAAEVFSRSLKAGDAHQIQPAFDQKLAELTADQDRASGNYNRFWDERNYLKNVDKIKADIIMVHGLNDWNVKPRNVANLWDKLQAVPVTKKLILHQGQHIYINNLQSLDFTDMMNLWLSHKLYGLDNHAETLLPNVLVQDNTQAQTWHGYDNWWQDTTDALDFKVQYKELVPADHTVDQRAAHFTDKLPDKLFDHYKHHLDSWQRDLLQEDKLNPLYDHRLLFKSWQAPEDQLLVGIPHVAGSVAVNKNFGMLSFMLIDFGAARRLTVSPQILAAKALDLGYHWREDDLKDFKLAGETPFKMITKGHLNLQNRHHPWHAEAIQPNVFYDFSVDLQPLFHHLLKGHQLGLVIYATDMKMTIRGNQDLQYSLNLNDIRLHVPMKKITD", "text": "FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S15 family."}
{"protein": "MSTFLQDNGDLSAVLVKFAPFAVAVIAILAAWKFTGSSKPRKVLNPSEFQNFVLKEKTDISHNVAIYRFALPRPTDILGLPIGQHISLAATIEGQPKEVVRSYTPISSDNEAGYFDLLVKAYPQGNISKYLTTLKIGDTLKVRGPKGAMVYTPNMCRHIGMIAGGTGITPMLQIIKAIIRNRPRNGGNDTTKIDLIFANVNEEDILLRDELEKLAKEDDGFRIFYVLNNPPPGWNGGFGFVTAEMIKEHLPAPAKDVKILLCGPPPMVSAMKKATESLGYTKARPVSKLEDQVFCF", "text": "FUNCTION: NADH-dependent reductase for dph3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L- methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. By reducing dph3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2- thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
{"protein": "MCDSDIKVKQLEKRASGQAFELILSPPSMDAAPDLSITSPKKKECSLEEIQKKLEAAEERRKLHEAEILKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTTKMETIKENREAQIAAKLERLREKDKKVEEIRKGKECKEPSEK", "text": "FUNCTION: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. It prevents assembly and promotes disassembly of microtubules (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the stathmin family."}
{"protein": "MSHLALKDLFSGFFVIDDEEEVEVPDKQQQVNEAPAKEQSQQTTKQNAIKSVPQKSASRYTTTSEERNNRMSNYSKNNSRNVVTMNNATPNNASQESSKMCLFEPRVFSDTQDIADELKNRRATLVNLQRIDKVSAKRIIDFLSGTVYAIGGDIQRVGTDIFLCTPDNVEVAGSITDHIENMEHSFD", "text": "FUNCTION: Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to the division site, in a FtsZ-dependent manner. SIMILARITY: Belongs to the SepF family."}
{"protein": "MCALVPPLYPNFGWPCGDHSFYETDDVSNTFLDFPLPDLTVTHENVSSENNRTLLDNPVVMKKLNHNASERERRKKINTMFSSLRSCLPPTNQTKKLSVSATVSQALKYIPELQEQVKKLMKKKEELSFQISGQRDLVYTDQNSKSEEGVTSYASTVSSTRLSETEVMVQISSLQTEKCSFGNVLSGVEEDGLVLVGASSSRSHGERLFYSMHLQIKNGQVNSEELGDRLLYLYEKCGHSFT", "text": "FUNCTION: Plays a role in metal homeostasis. Confers tolerance to high zinc (Zn) and nickel (Ni). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLNERIQPGMIFLLTVSLCHFMEYRAVQAGNCWLQQSKNGRCQVLYRTELSKEECCKTGRLGTSWTEEDVPNSTLFKWMIFHGGAPHCIPCKETCENVDCGPGKKCKMNKKNKPRCVCAPDCSNITWKGSVCGIDGKTYKDECALLKAKCKGVPELDVQYQGKCKKTCRDVLCPGSSSCVVDQTNNAYCVTCNRICPEPTSPDQYLCGNDGITYGSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCSAGKKCLWDSRVGRGRCALCDDLCGESKSDDTVCASDNTTYPSECAMKQAACSTGILLEVKHSGSCNSIVEDTEEEEEEEEPDYSFVISSW", "text": "FUNCTION: Binds directly to activin and functions as an activin antagonist which plays a role in neural induction. The short isoform is a more potent inhibitor of activin than the long isoform. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MAKASEHFFYVLKCSDNSYYGGYTTDVIRREAEHNAGIRCKYTKTRRPVKVIHFEKFETRSEATKAEAAFKKLSRKNKDAYLIQREESE", "text": "SIMILARITY: Belongs to the UPF0213 family."}
{"protein": "MWRLKVADGGNDPYIYSMNNFIGRQIWEFDPNAGTPEERAEIERLRHHFTKNRHKGFPSADLLWRVQLLREKNFKQSIPAVKVGDGEEISYEMALDAMRRGAHFLAAIQASDGHWPSETSGPLFYVCPLLICMYIMGFMDKVFSPEHKKEMMRYIYNHQNEDGGWGLHVGGHSNMFCTTFNYISLRLLGEEPDVEAVCKARNWIHDHDGVTSILSWGKTWLSILNVFDWSASNPMPPEYWMLPTWVPIHPSNMMCYTRITYMPMSYLYGKRFQAPLTPLVLQLRDELHTQPYDQINWRKVRHMCATEDLYFPHPFVQDLLWDTLYLLSEPLMTRWPFNKLIRQKALNETMRHIHYEDENSRYITIGCVEKPLCMLACWVEDPNSEYVKKHLARIPDYLWMAEDGMKMQSFGSQSWDAALAMQALLSCNITREIGSVLNSGHDFIKNSQVRNNPPGDYKSMFRYMSKGSWTFSDCDHGWQVSDCTAENLKCCLLLSLLPPDIVGEKMEPERFYDAVNVILNMQSKNGGLPAWEPASSYYWMEWLNPVEFLEDLIIEHQHVECTSSALQAILLFRKQYPGHRRKEINNFINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENCEAVRKGANFLRKIQNPEGGFGESYLSCPYKRYIPLDGKRSNLVQTAWGMMGLICAGQADVDPTPIHRAAKLLINSQTEDGDFPQEEITGEFFKNCTLHFAAFREVFPVMALGEYCNKVPLPSKKK", "text": "FUNCTION: Oxidosqualene cyclase involved in the biosynthesis of bryonolic acid. Converts oxidosqualene to isomultiflorenol. SIMILARITY: Belongs to the terpene cyclase/mutase family."}
{"protein": "MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTMGHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQPKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARSYCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRLPIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD", "text": "FUNCTION: Has a threefold preference for the hydrolysis of ATP over ADP. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GDA1/CD39 NTPase family."}
{"protein": "MGKFFTPYALIIFVFLIQACSSPSKTIFEGVRMTIPYRVVLGETLSFSQKKQAQKEIDQIFDHIDQIFNNWNPFSEISRINRSETLEPISLSPELFSFLCEIDRFHTFSDGRFDPTLGALKNLWLLHLKSQTLPPQELLHSYKQNTGWHLLSLDKTNHTLKKLSPSVQLDLCGAVKGFAVDLLGIFCSQFCQNYYVEWGGEIKTSGKHPSGRSWAIASSATPEILHLNNSSIATSGNQYQRWYVNKKIYTHILDPLTGIPLEESSYPILAVSVIDENCAFADAMATALTTFTSKQEALDWAKKKHLCVYITDKNAS", "text": "FUNCTION: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein such as NqrB and NqrC, two subunits of the NQR complex. SUBCELLULAR LOCATION: Cell inner membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the ApbE family."}
{"protein": "MQRLCVYVLIFALALAAFSEASWKPRSQQPDAPLGTGANRDLELPWLEQQGPASHHRRQLGPQGPPHLVADPSKKQGPWLEEEEEAYGWMDFGRRSAEDEN", "text": "FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family."}
{"protein": "MAKNPPENCEGCHILNAEALKSKKIRKSLKICGLVFGILALTLIVLFWGSKHFWPEVSKKTYGMEHTFYSNGEKKKISMEIDPITRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAEKPIENRDFLKNSKILEICDNVTMYWINPTLIAVSELQDFEEDGEDLHFPTSEKKGIDQNEQWVVPQVKVEKTRRTRQASEEDLPVNDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV", "text": "FUNCTION: May be an angiogenesis inhibitor. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein Nucleus envelope. SIMILARITY: Belongs to the chondromodulin-1 family."}
{"protein": "MNCVCRLVLVVLSLWPDRVVAPGPPAGSPRVSSDPRADLDSAVLLTRSLLADTRQLAAQMRDKFPADGDHSLDSLPTLAMSAGTLGSLQLPGVLTRLRVDLMSYLRHVQWLRRAGGPSLKTLEPELGALQARLERLLRRLQLLMSRLALPQAAPDQPVIPLGPPASAWGSIRAAHAILGGLHLTLDWAVRGLLLLKTRL", "text": "FUNCTION: Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production (PubMed:8913282). Also promotes the proliferation of hepatocytes in response to liver damage (PubMed:22253262). Binding to its receptor formed by IL6ST and either IL11RA1 or IL11RA2 activates a signaling cascade that promotes cell proliferation, also in the context of various cancers (PubMed:10026196, PubMed:23948300). Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3 (PubMed:23948300, PubMed:22253262). The interaction with the membrane- bound IL11RA and IL6ST stimulates 'classic signaling', whereas the binding of IL11 and soluble IL11RA to IL6ST stimulates 'trans- signaling' (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily."}
{"protein": "MPCPTGVTRCSAGVSSLARCLHTCPVLEGVTKANLSKLRKKTGFTFVNCRKALEKFENDLEQAEKWLKEQAQKEGWAKATKLQDRQTAQGLVGVAQEGTMATMVEVNCETDFVARNPKFRQLVTQVAMATLGDVKAHPQWTLGWLKALHTGEELKQLQIGDTTLGDLTALTIGTLGENIQIRRAMYYSVPPIPTKHVGVYVHAPVAGTTGGQSGSCALGKYGALVAFRRKNTEFQNFNAAELGRRLGQHVVGMSPLTVGEMPEVREEEGEKKDGDKQDEEERSTDSDEDETQMLRQTFLLDPTMTVGEMTRQQGIELLDFVRFECGEVEES", "text": "FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the EF-Ts family."}
{"protein": "MRMCTPIRGLLMALAVMFGTAMAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHEVYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLGKNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIRKSPDSPDGEDDRVYFFFTEVSVEYEFVFRVLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSHGKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQDFEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQTESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNLARVFWKFQNGVLKAESPKYGLMGRKNLLIFNLSEGDSGVYQCLSEERVKNKTVFQVVAKHVLEVKVVPKPVVAPTLSVVQTEGSRIATKVLVASTQGSSPPTPAVQATSSGAITLPPKPAPTGTSCEPKIVINTVPQLHSEKTMYLKSSDNRLLMSLFLFFFVLFLCLFFYNCYKGYLPRQCLKFRSALLIGKKKPKSDFCDREQSLKETLVEPGSFSQQNGEHPKPALDTGYETEQDTITSKVPTDREDSQRIDDLSARDKPFDVKCELKFADSDADGD", "text": "FUNCTION: Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling (PubMed:20877282). Regulates GABAergic synapse development (By similarity). Promotes the development of inhibitory synapses in a PLXNB1-dependent manner (By similarity). Modulates the complexity and arborization of developing neurites in hippocampal neurons by activating PLXNB1 and interaction with PLXNB1 mediates activation of RHOA (PubMed:19788569). Promotes the migration of cerebellar granule cells (PubMed:16055703). Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro) (PubMed:8876214). Induces endothelial cell migration through the activation of PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway (PubMed:16055703). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the semaphorin family."}
{"protein": "MEESAGTPFHDPKYFVSPFILNTDEGRYLVLKAIKLCNVRTIDCMKQETSCVLKVDKPQSPCPISSSDSAPKCYMQQTSPQQQRQAPQLRFINTGALSNLFANTTDKAARVINQ", "text": "FUNCTION: Plays an essential role in virion assembly and morphogenesis. Also plays a role in the inhibition of host immune response by dysregulating mTOR. Sequesters host RICTOR and RPTOR, thereby disrupting mTORC1 and mTORC2 crosstalk. In turn, blocks the host antiviral response in part through mTOR-dependent degradation of cGAS, the primary poxvirus sensor. SUBCELLULAR LOCATION: Virion Note=Major component of the virion comprising about 10% of the virion mass. SIMILARITY: Belongs to the orthopoxvirus OPG062 family."}
{"protein": "MSVPTLPTGPTVDLAQAAERLIKGRRAVRAFRPDEVPEETMRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAMLFAPNNTEARIAGDMGIYAQTLMLAMTAHGIASCPQALLSFYADTVRAELGVENRKLLMGISFGYADDTAAVNGVRIPRAGLSETTRFSR", "text": "FUNCTION: Confers resistance to antitubercular drugs benzothiazinone (BTZ) and dinitrobenzamide (DNB). Inactivates BTZ and DNB by reducing an essential nitro group of these compounds to amino group or to hydroxyl amine, respectively, using NADH or NADPH as source of reducing equivalents; two electrons are transferred (PubMed:22069462, PubMed:20624223). Able to reduce the nitro group of bicyclic nitroimidazole PA-824, but not of quinone menadione, nitrofurazone, methyl-4-nitrobenzoate, 4-nitrobenzene methyl sulfonate or 4- nitroacetophenone (PubMed:20624223). SIMILARITY: Belongs to the nitroreductase family."}
{"protein": "MAAKTSNLVALLLSLFLLLLSISSQVGLGEAKRNLRNNLRLDCVSHPSPPPPHRSMAPPIFVPPSTSHKGQGP", "text": "FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (PubMed:33514716, PubMed:34535661, PubMed:31001913). Inhibits root growth and regulates root meristems (PubMed:34535661, PubMed:31001913). Prevents general growth and development (PubMed:31001913). Exhibits antibacterial effects against Pseudomonas syringae pv. tomato DC3000, Ralstonia solanacearum, Bacillus subtilis and Agrobacterium tumefaciens, thus being an antimicrobial peptide (AMP) (PubMed:31001913). SUBCELLULAR LOCATION: Cell membrane Secreted, extracellular space, apoplast Note=The precursor of SCOOP14, PROSCOOP14, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP14 in the apoplasm. SIMILARITY: Belongs to the serine rich endogenous peptide (SCOOP) phytocytokine family."}
{"protein": "MNIEKAKRLAKEKLPEKRYNHSLRVAETAIKLAEIYDGDTSKVELAGVLHDFCKYDDLGKMYQIVRQYELGNDLLSYGSEILHGPVCAAIMEHEYGINDEEVLMAIKYHTTGRQQMTKTEKLIFIADYIEPGRTIPGVDDIRDMAYNQGSLDKTIYEISKRTVLFLIQKDITVYNKTIDCLNYYNYSDERIKDD", "text": "FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ADP (PubMed:32152217). Can also hydrolyze Ap3A, Ap5A, Ap4G, Ap4U and Gp4G, always releasing ADP or GDP as one of the products, but it exhibits a marked preference for Ap4A, which is mainly exerted at the substrate affinity level (PubMed:32152217). SIMILARITY: Belongs to the Ap4A hydrolase YqeK family."}
{"protein": "MYQHIVVLTGAGISAESGLRTFRDQDGLWEEHHIEDVATPEGYAKDAELVERFYNSRWEQLHCGTVMPNAAHLALAKLEAEFSGQLLVVTQNIDDLHERAGSRRLLHMHGELSKGRCPRSRQTFLLREPFGVNNGCTCCIPAQRLRPHVVWFGEMPLGMDRIHDALDNCDLFIAIGTSGTVYPAAGFVDTANHHGAQTVEVNLQSPDRHSQFQYHLTGRAGELVPKLVDTILAGRVIGSDLAE", "text": "FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sirtuin family. Class III subfamily."}
{"protein": "MSDGGAPTVEFLRHGGRIAMAHRGFTSFRLPMNSMGAFQEAAKLGFRYIETDVRATRDGVAVILHDRRLAPGVGLSGAVDRLDWRDVRKAQLGAGQSIPTLEDLLTALPDMRVNIDIKAASAIEPTVNVIERCNAHNRVLIGSFSERRRRRALRLLTKRVASSAGTGALLAWLTARPLGSRAYAWRMMRDIDCVQLPSRLGGVPVITPARVRGFHAAGRQVHAWTVDEPDVMHTLLDMDVDGIITDRADLLRDVLIARGEWDGA", "text": "FUNCTION: Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
{"protein": "MGQFTVVSLGLLAVFLSLSGAKGDNCPANWISRNGVCNKLFPDRKTWLEAEMYCRALKPGCHLASLHRDSDSTVLAWYISDHFKGAGHVWIGLRDTNRKRTWKWSDRTSTNYFSWNQGEPNNVQDNENCVHLWAPSGYLKWNDEPCASLHPFICQYKL", "text": "FUNCTION: Mannose-binding lectin which recognizes specific carbohydrate structures and agglutinates a variety of animal cells by binding to cell-surface glycoproteins and glycolipids. May be a calcium-dependent lectin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the true venom lectin family."}
{"protein": "MQIITTALVCLLLAGMWPEDVDSKSMQVPFSRCCFSFAEQEIPLRAILCYRNTSSICSNEGLIFKLKRGKEACALDTVGWVQRHRKMLRHCPSKRK", "text": "FUNCTION: Cytokine that is chemotactic for monocytes but not for neutrophils. Binds to CCR8. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MNGIQVDINRLKKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL", "text": "FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity. FUNCTION: This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MRIHSPYPASWALAQRIGYLYSEGEIIYLADTPFERLLDIQRQVGQCQTMTSLSQADFEARLEAVFHQNTGESQQIAQDIDQSVDLLSLSEEMPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARLDIAEKRIPQDGRISLRIGRRNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGIILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFTPVSPQQAQMFKYHQLAVTTIGTPVGCPHCHQSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQHKALIKNGLQKVISGDTSWDEVMRVASATLESEA", "text": "FUNCTION: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in the cytoplasm. SUBCELLULAR LOCATION: Cell inner membrane Note=Membrane association is not an intrinsic property but requires the GspL gene product. SIMILARITY: Belongs to the GSP E family."}
{"protein": "MATSAAAVQDEPATRFAKDQLKAIIERIERLEEEKKTISDDIRDVYAEAKGNGYDVKALRTIVRMRKQDANERAEQETILETYMQALGML", "text": "SIMILARITY: Belongs to the UPF0335 family."}
{"protein": "MDSVDRLKTYLATYDNLDSALQDANESEERREDKYLQDLFIEDQGDKPTPSYYQEEESSDSDTDYNAEHLTMLSPDERIDKWEEDLPELEKIDDDIPVTFSDWTQPVMKENGGEKSLSLFPPVGLTKIQTEQWKKTIEAVCESSKYWNLSECQILNLEDSLTLKGRLMTPDCSSSVKSQNSVRRSEPLYSSHSPGPPLKVSESINLWDLKSTEVQLISKRAGVKDMTVKLTDFFGSEEEYYSVCPEGAPDLMGAIIMGLKYKKLFNQARMKYRL", "text": "FUNCTION: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N(0). Plays a role in virion assembly (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the vesiculovirus protein P family."}
{"protein": "MRSPGAQDNVSVSQGMRAMFYMMEPSETAFQTVEEVPDYVKKATPFFIFLILLELVISWILKGKPSGRLDDALTSISAGVVSRLPSLFFRSLEVTSYIYIWENYRLLELPWDSTWTWYFTFLGVDFGYYWFHRMAHEINIFWAAHQAHHSSEDYNLSTALRQSVLQQYSSWVFYCPLALFIPPSVFAVHIQFNLLYQFWIHTEIIRTLGPLEVILNTPSHHRVHHGRNRYCIDKNYAGTLIIWDRIFGTFEAENEQVIYGLTHPIGTFEPFNVQFHHLLYIWTTFWTTPGFCHKFSVLFKGPGWGPGKPRLGLSEEIPEVTGQEVPFSSSASQLLKIYTVLQFAVMLAFYEETFANTAVLSQVTLLLRIFFFILTLTSIGFLLDQRSKAATMETFRCLLFLTLHRFGHLKPLIPSLSFAFEIFFSVCIAFWGVRSITQLTSGSWKKP", "text": "FUNCTION: Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family. TMEM195 subfamily."}
{"protein": "MTQEVPRRLEPSPFEWKGDAGPSVKTLRPHAIPSVAIDLASVTKSYGDKPVVDGLSFTVAAGECFGLLGPNGAGKSTITRMILGMTTPATGVITVLGVPVPSRARLARMGIGVVPQFDNLDSEFTVRENLLVFGRYFRMSTREIEAVIPSLLEFARLENKVDARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHIMEEAERLCDRLCVLEAGRKIAEGRPHVLIDEKIGCQVIEIYGGNPHELSALVSPHARHVEVSGETVFCYALDPEQVRVQLDGCAGVRFLQRPPNLEDVFLRLTGRELKD", "text": "FUNCTION: Part of the ABC transporter complex NodIJ involved in the export of the nodulation factors (Nod factors), the bacterial signal molecules that induce symbiosis and subsequent nodulation induction. Nod factors are LCO (lipo-chitin oligosaccharide), a modified beta-1,4- linked N-acetylglucosamine oligosaccharide. This subunit is responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Lipooligosaccharide exporter (TC 3.A.1.102) family."}
{"protein": "MSAPAQPPTEGAEGAAPGGGPPGPPPNMTSNRRLQQTQAQVEEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFESSAAKLKRKYWWKNCKMMIMLGAICAIIVVVIVIYFFA", "text": "FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein Synapse, synaptosome. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle membrane; Single-pass type IV membrane protein Synapse, synaptosome. SIMILARITY: Belongs to the synaptobrevin family."}
{"protein": "MMRYEDVSQLSLMNLTYEEQRLENIRKNEDLLRSLGLGAPSEATTLATPSNLKTAGNQRRYNDTLVGKSNTGRNRSDSPRKRPTKDREDLNLVPQSAIKRRQSVRLGGKEKPNYTREQVTFNSDRDTPNTPSRQIKSTHSHPGSEEEDIRQVKTRTLGVRVHNPKTFGHIPGIGVGKWWATRMEASADAVHAPTVAGISGNAHEGAWSVALSGGYPDDIDLGYAFTYTGCGGRDLKGTKQNPKNLRTAPQTSHQSFDNPLNAALKRSAETRNPVRVIRGFKLQSKYAPPTGYRYDGLYIVEKAWMAKGLTNGLMVCRYAFKRMDDQGPLPQKDLDHDDDNKA", "text": "FUNCTION: Involved in the maintenance of DNA methylation (PubMed:31955845). Binds hemimethylated DNA (PubMed:31955845). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSHPQSHRYFSVNAPAGGERHLALDEKGVLCLTVVDPATRKLLIPLSCVYPTQAQQRTTIPSLCQLFLNGRCRQGTQCHQVHAALDVVAALRSQVDYLPICCALHGDRDYVNALDNRSWMSRVVVHVPDATYGGGYIPLARFSYTTPISRILREVNARLESGVSVAAVDGGGHPKRMVLNACDFKICGLHTLDRCRYAEECIFLHICKEIVVDVNNGSGDYSLTSQARDGGEPGPRGAKKGSVFVSVSRQQRVRGRPLSYPTVEYQTPFPLRSYEGSMSYNAVSDINSDCSWVSGRYPTGAYMESRMDAAPLPSLAPRFVQGHPGVPRCYSSTTTSTTTTAAAREDAAMYGAGGCWDRWSSPESGCAPCAFVGSCSDCHYADNNNYSGCNGYAYGSRNGYGSDGPNCYFCPGDECSSTHLCPNGTSSSVPQPVESVSSASVSARAWQHNPYGVTPTGGISD", "text": "FUNCTION: RNA-binding protein involved in regulation of mRNA stability (PubMed:31743541). Promotes mRNA stabilization by recruiting MKT1 and PBP1 (By similarity). Stabilizes transcripts encoding mitochondrial proteins (PubMed:31743541)."}
{"protein": "MSAKKPVVLLILDGYGYSERTKYNAVYAAQTPVYDNLWKTCPNTLIDTSGMAVGLPAGQMGNSEVGHTTIGAGRVVYQSFTRINKSISDGDFFTNPEYVKAIDSAIANDRAVHILGLLSEGGVHSHQDHLYAMINMAVERGAKQVYLHAFLDGRDTPPRSAEASLQKAQDVFAKLGTGRVASIVGRYFALDRDNRWDRVKTAYDVMVTGEAEFDALTAVDGLKAAYERGENDEFVKATVICGEDEEVATINDGDSVIFMNFRPDRAREITRALIDENFTGFDRGETHPAIAHFVQTTEYASDIKAPIAFPPEDLSNSFGEYIAGLGKTQLRIAETEKYAHVTFFFNGGNEVVYPGEDRILVPSPKVATYDLQPEMSAPEVTDKLVEAIESGKYDAIICNYANCDMVGHSGLFDAAVKAVEAVDVALGRVLAAVKKVDGEALITADHGNVEEMFDEETGQPHTQHSTLPVPFIFVSSRKGKLASGGSLADVAPTILALMDLPQPKEMTGRNLITLEG", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family."}
{"protein": "MHKIFSKNNLIFFVFVAFIFVVIVLQFFVSSENATKVNLSQTFEPISWLHLLGTDDYGRDLFTRIIIGARSTLFVTVLTLIAIVVIGVTLGLFAGYKKGWIERLVLRFIDVGLSIPEFIIMIALASFFQPSLWNLVISITVIKWMNYTRLTRSIVNSEMNKPYIKMAQLFHVPTRTILIRHLTPKIIPAIIVLMVVDFGKIILYISSLSFIGLGAQPPTPEWGAMLQQGRDFISSHPIMLIAPASVIAITILIFNLTGDALRDRLLKQRGEYDESH", "text": "FUNCTION: Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily."}
{"protein": "MLQRAASNAYSWWWASHIRTKQSKWLEQNLQDIEEKVQYVLKLLQEDGDSFAKRAEMYYKKRPELISFVEESYRAYRALAERYDHISTELQNANTTIASVFPDQVPNFAMDDDIDMSKFAKRSNISGANVPNVPKLPVKDLKSAVRVATKKLQPRKSMKYTGGSTNVVVKSSGLSKPEAMGEIDKLQKEILALQTEKEFVKSSYEIGLSKYWEFEKGIKEKQERICGLQDEFGESVAIEDEEARRLMTETAIKSCQEKLVELQEKQEKSYEEAREEHVKIKESKEKLRSMASQFLGDESVFAKDDGDEVRRTAELDHEIKEMSRKKKELESVKEKIREHFESGANSSLNGTDMAEKVDELVNKVISLESAVSSQTALIQRLRNETNGLQTQISTLETDKALLADDKSDLRNKLKEMEEKLKALQDLDRNVLDKSSNLQTHFDDACHNLDNLSGGNLHEVKPESESDNLAISIEPQKDLEGEKRTLDISEEIKEHQKETGEEKKEAPVKSVKFEQTRNATIAEDSTIPSTNPDTVLESTEKVDSDLEKQDASDKTDSVLDNVLENQAASDQTDSVLDSVLEKQGESDKIDSVPSNVSEKESDISFNGEQQEDQKEKEGEPDWKEMFMKGMENREKHLLTEYTTILRNFKDMKKTLDETKTKMKTENATKDDEIKLLREKMSLLQKGLGDSNDLMENQLSNDDYSIGFMAAENQNMSLVEEQFRLNIDELLEENLDFWLRFSTAFGQIQSYDTSIEDLQAEISKLEQRRKQDGSSTAKYALRSDVRPLYVHLREINTDLGLWLEKGAALKEELKSRFESLCNIQDEITKALKSSAEDDDFRFTSYQAAKFQGEVLNMKQENNKVADELQAGLDHITTLQLEVDKTLGKLIDEFALSGSKNKSDLDLQHSDSRSRVPLRSFIFGSKQKRAKPSIFSCMHPSLYRKMKTST", "text": "FUNCTION: Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex. SIMILARITY: Belongs to the NET family."}
{"protein": "MSAKKASQPMLNTTGSLQEGEMGKMFHGKCLRIVSPESPAKLYCCYGVIMVLSVAVVALSVALSVKMTPQISTINTYAACPRNWIGVGNKCFYFSEYASNWTFSQTFCKAQEAELARFDTEEELNFLSRYKGSFDYWIGLHRESSEHPWKWTDNTQYNYSLSIRGVERYAYLNDIGISSARVYADKRWSCSKLNSYSLQCKTPFSPM", "text": "FUNCTION: Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
{"protein": "MDFTIFPPEFNSLNIQGSARPFLVAANAWKNLSNELSYAASRFESEINGLITSWRGPSSTIMAAAVAPFRAWIVTTASLAELVADHISVVAGAYEAAHAAHVPLPVIETNRLTRLALATTNIFGIHTPAIFALDALYAQYWSQDGEAMNLYATMAAAAARLTPFSPPAPIANPGALARLYELIGSVSETVGSFAAPATKNLPSKLWTLLTKGTYPLTAARISSIPVEYVLAFVEGSNMGQMMGNLAMRSLTPTLKGPLELLPNAVRPAVSATLGNADTIGGLSVPPSWVADKSITPLAKAVPTSAPGGPSGTSWAQLGLASLAGGAVGAVAARTRSGVILRSPAAG", "text": "FUNCTION: During M.tuberculosis and HIV-1 co-infection, can stimulate transcription from the long terminal repeat (LTR) of HIV-1 in monocyte/macrophage cells. Interaction with human TLR2 activates the NF-kappa-B transcription factor, which binds to the promoter region of the HIV-1 and induces HIV-1 gene expression. FUNCTION: Induces pro-inflammatory responses (PubMed:22427668, PubMed:27481848). Induces host TLR1/2 heterodimerization, which causes an increased recruitment of IRAK1, MYD88, and protein kinase C epsilon (PRKCE) to the downstream TLR-signaling complex that translocates PRKCE into the nucleus in an IRAK1-dependent manner. PRKCE-mediated phosphorylation allowed the nuclear IRAK3 to be exported to the cytoplasm, leading to increased activation of ERK1/2, stabilization of MAPK phosphatase 1 (MKP1), and induction of TNF-alpha with concomitant down-regulation of MAP kinase p38 (PubMed:27481848). FUNCTION: Induces pro-inflammatory responses. SUBCELLULAR LOCATION: Secreted, cell wall Cell surface Note=Not secreted but surface exposed. Mainly localized in the cell wall fraction regardless of PE11 co- expression. SUBCELLULAR LOCATION: Secreted, cell wall Cell surface. SIMILARITY: Belongs to the mycobacterial PPE family."}
{"protein": "MTLDNLKHSAILSTLFKMADDNDLLGASEFIKDRLYFATLRSKPKSTANTHYFSTDEEFVYENFYADFGPLNLAMLYRYCCKLNKKLKSFTLTRKRIVHYTSFDQRKRANAAVLIGAYAVIYLKKTPEEAYRALISGSNASYLPFRDASFGNCTYNLTVLDCLQGIRKALQHGFLNFETFDVNEYEHYERVENGDLNWITPGKLLAFSGPHPKSKVENGYPLHAPEAYFPYFRKHNVTTIVRLNKKIYDAKRFTDAGFDHYDLFFVDGSTPSDIITRRFLHICESTSGAVAVHCKAGLGRTGTLIGCYLMKHYRFTSAEAIAWIRICRPGSIIGPQQHYLEEKQASLWAHGDSLRSKQRQYQDRSVPQLISSMDNLSISTSIFKSHSLDRMEENDYAENDLGMTQGDKLRALKGRRQPRSATTGAIRVEDVKVHTRSPSQPLSRMKPPASSQGSISPLKSSKVPASSSSSSSSSSVSASAKRIGRSSSSSTNLKSTRLASSLGNLYEPNTESISSGKPPSPSSFTPHPVRTTYNYHYEVNNNNNQYSTTSSPSKSLGYNLNHSGPSGASANARLSAGEQGHQRNPPAGLSGLSTRHLSRSIPSLQSEYVQY", "text": "FUNCTION: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, spindle Cell projection, kinocilium Note=Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the mitotic spindle pole and at the central spindle (By similarity). Present along both the transient kinocilia of developing cochlear hair cells and the persistent kinocilia of vestibular hair cells (By similarity). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class CDC14 subfamily."}
{"protein": "MRVISRARSACTWTSCTSLSPCSTSCPPSPAAPTLLRRRSLPQQRRRPSSSPNRRVRGVTTSPCPTRSLVYKRRVGAPQRLCAETVATMQAQEANALLLSRMEALEWFKKFTVWLRVYAIFIFQLAFSFGLGSVFWLGFPQNRNFCVENYSFFLTVLVPIVCMFITYTLGNEHPSNATVLFIYLLANSLTAAIFQMCSESRVLVGSYVMTLALFISFTGLAFLGGRDRRRWKCISCVYVVMLLSFLTLALLSDADWLQKIVVTLCAFSISFFLGILAYDSLMVIFFCPPNQCIRHAVCLYLDSMAIFLTLLLMLSGPRWISLSDGAPLDNGTLTAASTTGKS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytomegalovirus US12 family."}
{"protein": "MTKSDLLFDKFNDKHGKFLVFFGTFVDTPKLGELRIREKTSVGVLNGIIRFVNRNSLDPVKDCLDHDSSLSPEDVTVVDIIGKDKTRNNSFYFPGFVDTHNHVSQYPNVGVFGNSTLLDWLEKYTFPIEAALANENIAREVYNKVISKTLSHGTTTVAYYNTIDLKSTKLLAQLSSLLGQRVLVGKVCMDTNGPEYYIEDTKTSFESTVKVVKYIRETICDPLVNPIVTPRFAPSCSRELMQQLSKLVKDENIHVQTHLSENKEEIQWVQDLFPECESYTDVYDKYGLLTEKTVLAHCIHLTDAEARVIKQRRCGISHCPISNSSLTSGECRVRWLLDQGIKVGLGTDVSAGHSCSILTTGRQAFAVSRHLAMRETDHAKLSVSECLFLATMGGAQVLRMDETLGTFDVGKQFDAQMIDTNAPGSNVDMFHWQLKEKDQMQEQEQEQGQDPYKNPPLLTNEDIIAKWFFNGDDRNTTKVWVAGQQVYQI", "text": "FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family."}
{"protein": "MSVCQTNPLNTLVSKSGYRFGQPNQHQQSIAQQQSRPRNNALDHQFSQFTGASGPSFAHPQHQQLPMAAVVANATTAASTTSNTATASDHHVWIDQFANMQVHDKTEFPTDYKQMYSQYEARGASYSMGAPVMVSHSQMFPRHQQSLMVNQLESQAYASSSAKLDEQFAELERQVQDDEKEQQQDKDDDFHLKETSPLDEDQRQLKEAAQSIYTTLSDKSSTTSSKFSNSKFLGLMRNISDGVITLKKNPDEDKYTELYSPSTGETFGEEYFPVQDSVLGDPLDSIGDLSNMSSSEAAAKVYHNSV", "text": "FUNCTION: Mediates peroxisomal import of proteins containing a C- terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7 (By similarity). Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal (By similarity). PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX21 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome Note=Cycles between the cytosol and the peroxisome. SIMILARITY: Belongs to the peroxin-21 family."}
{"protein": "MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAASEEQARRLCDDYDAAAHEFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVARPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEEVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDQRGASGEELGDLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEEENEGFHTIPACWWWGTVSMTTVGYGDVVPETVGGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRSSGQREFEDLLSSVDGVSDVSLETSRDTSQEGRSTDLETQAPREPAKSHSY", "text": "FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:9305895). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). SIMILARITY: Belongs to the potassium channel family. S (TC 1.A.1.2) subfamily. Kv9.1/KCNS1 sub-subfamily."}
{"protein": "MGDGGAERDRGPKRREEPGGRSGRHGEHRGAEDLRADTGSASPREIAGTSASSPAGSRESGGDSDGQQALGETDHCRRILVRDAKGTIREIVLPKGLDLDRPKRTRTSFTAEQLYRLEMEFQRCQYVVGRERTELARQLNLSETQVKVWFQNRRTKQKKDQSRDLEKRASSSASEAFATSNVLRLLEQGRLLSVPRAPSLLALTPGLPGLPASHRGTSLVDPRNSSPRLNPMPSASASSPLPPPLPAICFSSAPLLDLPAGYKLGSSAFEPYSRLEQQKVGSPGQSDKKADI", "text": "FUNCTION: Transcription factor that may function in dorsoventral specification of the forebrain. Regulates the expression of Wnt signaling antagonists including the expression of a truncated TCF7L2 isoform that cannot bind CTNNB1 and acts therefore as a potent dominant-negative Wnt antagonist. Plays a crucial role in eye development and, in particular, in the specification of the ventral optic vesicle. May be a regulator of axial polarization in the retina. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EMX homeobox family."}
{"protein": "MSLTMKNVEGFVIFLVIFTSTAAVPQLQKALDGREYLIETELKYNWHQAWHECARHDQQLVTIESADKNNAIIDLVKRVVGKSHNLWLGGNDEYSSSRDYGRPFFWSPTGQAFSFAYWSENNPDNYKHQEHCVHIWDTKPLYQWNDNDCNVKMGYICEPNHFRETYDQALKQKCEAIKITNSKISTEFDQLHAKQSLEFDSITQNVAKVNEDWKIEIQKLQNATQIAIQQIMENHEKKIRDLSDNLLKQLQDSNEQLKQSTDHMNASFGEKLKGQQAENNEIC", "text": "FUNCTION: Role in the defense system of the organism against microorganisms. This lectin binds galactose."}
{"protein": "MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVTPLPAILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTVLTF", "text": "FUNCTION: Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism. In vitro can also catalyzes the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal. Catalyzes in the oxidative direction with higher efficiency. Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MNNNQCMRKKLDELRNIARSYNISITGKKKQQLCDEIIDYQKNNPPRRSPSPRRSPSPRRISPECEQWLANKGINPRTGKAIKIGGPTYKKLEMECKEASPKIPSPVRQPSPVHSPVRSPVRQPSPVRFVEKTKGALNKMKKDQLIDFAQSLGLNPGKLLKPALVDLIFVNQKPPRRSPSPRRSPSPRRSPSPRRSPSPRPVFVEKTKGALNKMKKDQLIDLAQSLGLNPGKLLKPALVDLIFVNQKPVEPIRASSSSRSSRSTRRSSSTKPSRRSSSRSRRSSSRSRRSSSRSRRSSSRSRRSSRRSTSRSRSLSKRSIRNISTVGDLEDLVASNLPIAIPESLSRSLSPSRTDFHEAEIELGSDFDLNNLPENRIAELKQLNVLAKQNGFRMINVPLDGNCMFSVIGRAFNTSSSVIRQHTVDYLRRCKGSFDHIPANIDDPTINWNDYIDRLEEDACWGDNTALFAASLALNFQAHILQVAGGDEGSWIRFGVNETNMGRIVNMGYLDNFHYIALEPFSGRLDILSIPSTHSKCPPPEISNRRDEEIRRDEEVEDEVIGERIVREAEVIERELRQEEELTSIVSTKRSLRPSIPPKISTEHRRTPKLRPSVPRPSSIRQSQPNVAALARLETLTKIKDIIDALQRPLENKLSTLTNTEKAIMQCIGVA", "text": "FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation."}
{"protein": "MLDKLKESLRNSPVIKKGEYDYFVNPVTDGIPLTEPELLEEIADEIVRRFNPDPASVDKIVCIEAMGIHHATVLSLKTRIPFVVVRKRRYGLPGEVAVHQMTGYSEGELYINGVDGDDRVMVIDDVVSTGGTLLAVLEALREMEVEVVDVVTVIDKGEGSRVVKERTGFTVRSLVKADVVDGRVTVEDIPDGG", "text": "FUNCTION: Catalyzes a salvage reaction resulting in the formation of IMP that is energically less costly than de novo synthesis. Prefers hypoxanthine, has 66% activity with guanine while activity with adenine, xanthine, uracil, orotate, or cytosine is negligible. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. Archaeal HPRT subfamily."}
{"protein": "MAAEWASRFWLWAALLIPVAAVYEDQVGKFDWRQQYVGKLKFASLEFSPGSKKLVVATEKNVIAALNSRTGEILWRHVDKGTAEGAVDAMLLHGQDVITVSNGGRIMRSWETNIGGLNWEITLDTGSFQALGLVGLQESVRYIAVLKKTTLALHHLSSGHLKWVEHLPESDSIHYQMVYSYGSGVVWALGVVPFSHVNIVKFNVEDGEIVQQVRVSTPWLQHLSGACGVVDEAVLVCPDPSSRSLQTLALETEWELRQIPLQSLDLEFGSGFQPRVLPTQPNPVDASRAQFFLHLSPSHYALLQYHYGILSLLKNFPQTALVSFATTGEKTVAAVMACRNEVQKTSNSEDGSMGSFSEKSSSKDSLACFNQTYTINLYLVETGRRLLDTTTTFSLEQSGTRPERLYIQVFLKKDDSVGYRALVQTEDHLLLFLQQLAGKVVLWSREESLAEVVCLEMVDLPLTGAQAELEGEFGKKAAIQDGLLGMFLKRLSSQLILLQAWTSHLWKMFYDARKPRSQIKNEINIDTLARDEFNLQKMMVMVTASGKLFGIESSSGTILWKQYLPSVKPDSSFKLMVQRTTAHFPHPPQCTLLVKDKESGMSSLYVFNPIFGKWSQVAPPVLKRPILQSLLLPVMDQDYAKVLLLIDDEYKVTAFPATRNVLRQLHELAPSIFFYLVDAEQGRLCGYRLRKDLTTELSWELTIPPEVRRIVKVKGKRSSEHVHSQGRVMGDRSVLYKSLNPNLLAVVTESTDAHHERTFIGIFLIDGVTGRIIHSSAQKKAKGPVHIVHSENWVVYQYWNTKARRNEFTVLELYEGTEQYNATAFSSLDRPQLPQVLQQSYIFPSSISAMEATITERGITSRHLLIGLPSGAILSLPKALLDPRRPEIPTEQSREENLIPYSPDVQIHAERFINYNQTVSRMRGIYTAPSGLESTCLVVAYGLDIYQTRVYPSKQFDVLKDDYDYVLISSVLFGLVFATMITKRLAQVKLLNRAWR", "text": "FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N- exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMC1 family."}
{"protein": "MSDILNVSQQREAITKAAAYISAILEPHFKNTTNFEPPRTLIICGSGLGGISTKLSRDNPPPVTVPYQDIPGFKKSTVPGHSGTLMFGSMNGSPVVLMNGRLHGYEGNTLFETTFPIRVLNHMGHVRNLIVTNAAGGINAKYQACDLMCIYDHLNIPGLAGQHPLRGPNLDEDGPRFLALSDAYDLELRKLLFKKWKELKIQRPLHEGTYTFVSGPTFETRAESKMIRMLGGDAVGMSTVPEVIVARHCGWRVLALSLITNTCVVDSPASALDESPVPLEKGKATHAEVLENGKIASNDVQNLIAAVMGEL", "text": "FUNCTION: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine (By similarity). SIMILARITY: Belongs to the PNP/MTAP phosphorylase family."}
{"protein": "MKAQKFSKASLLDDEDDYSTQLDRILARRKKSQKEDSGDLDTISFGSLSKAQARLQTEERESKKKVKKVKKPKVLKKQEEDFQPPSDISDDGEFFEEPSQDHQSRTSDRHSKEEPRSKSKHAPSESSAKKRVSKVREIPGLLNGSGSSSLYQDVRFDTAFGKADLQKARENYKFLDEYREKEITELNKILQDDMTEQLLSEREINTIKYKIQSLKSRVDTLKNRDLENEIVRDYKRNHKNFFLKNSDKRKLVQKAKFDSMKPSQREKVIERKRKRQLGREFKQLEFNQK", "text": "FUNCTION: Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRP36 family."}
{"protein": "MALRSISFNQDYTCLAAGFDAAYKVYNCDPFGECFQKADDGGANLVEMLFSTSLIAVVGIGDKPANTMRKLKIINTKRKAVICELTFPTAILYVKMNRKRLVVVLVDQIFVYDVSCMKLLHSIEASAGLDDRIICDLCADDESVLVFQQSGSSDELAANAGTVVVFDALQIQPINVIECHRSPLQRIAVSKDGRLLATASVKGTIVRVFRVADGRKVHEFRRGSYTAQISCLSFNVDATVLCCSSNTGTVHFFRLDDVDRRRSTGSIDANIDGSETLPRESSITEEESSEINRLINSQLGGHNGFAKKKSAESLKNFIWSKSKTYLPSQINSILEPKRDYAFIKLTTEVESVVGLVDNNCYVATRAGDFFVYSVQPGQCVLLKHYKIE", "text": "FUNCTION: Involved in peroxisome sequestration to the vacuole during macropexophagy. Also required for microautophagy. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Note=Vacuolar and other perivacuolar punctate structures. SIMILARITY: Belongs to the WD repeat PROPPIN family."}
{"protein": "MASASATATLLKPNLPPHKPTIIASSVSPPLPPPRRNHLLRRDFLSLAATSTLLTQSIQFLAPAPVSAAEDEEYIKDTSAVISKVRSTLSMQKTDPNVADAVAELREASNSWVAKYRKEKALLGKASFRDIYSALNAVSGHYVSFGPTAPIPAKRKARILEEMETAEKALTRGR", "text": "FUNCTION: Probably involved in repair of photodamaged photosystem II (PSII). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Associated with PSII on the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the Psb27 family."}
{"protein": "MMACRDPKPGAKRLVRAQTLQKQRRAPVGPRAPPPDEEDPRLKCKNCGAFGHMARSTRCPMKCWKAALVPPTLGKKEGKENLKPWKPQVEANPGPLNKDKGEKEERPRQQDPQRKALLHIFSGKPPEKPLPNRKGSTESSVYLRVASGPMPVHTTSKRPRVDPVLADRSATEMSDRGSALASLSPLRKASLSSSSSLGPKERQTGAAADIPQPAVRHQGPEPLLVVKPTHSSPEGGCREVPQAASKTHGLLQAISPQAQDKRPAVTSQPCPPAATHSLGLGSNLSFGPGAKRPAQAPIQACLNFPKKPRLGPFQIPESAIQGGELGAPEYLQPPPATTELGPSTSPQMGRRTPAQVSSVDRQPPHSRPCLPTAQACTMSHHPATSHDGAQPLRVLFRRLENGRWSSSLLAAPSFHSPEKPGAFLAQSPHVSEKSEVPRVRVPPNVLYEDLQVSSSSEDSDSDLE", "text": "SIMILARITY: Belongs to the FAM90 family."}
{"protein": "MTHLVLLLCCCVGSVCAFFSDLVKFENVTAHAGARVNLTCSVPSNESVSRIELGRGYTPGDGQLPLAVATSNNGTHITNGGYNYSLTLEWVNDSNTSVSLIIPNVTLAHAGYYTCNVTLRNCSVASGVHCNYSAGEEDDQYHANRTLTQRMHLTVIPATTIAPTTLVSHTTSTSHRPHRRPVSKRPTHKPVTLGPFPIDPWRPKTTWVHWALLLITCAVVAPVLLIIIISCLGWLAGWGRRRKGWIPL", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Epstein-Barr virus BILF2 protein family."}
{"protein": "MFSTSRIISRINYNFLRKSHYSTKTVAEQAKGRFTPLIQKLSAVQQPIMYWANVSKELVQQVYHSQKIAPPSNTHSPFLFWKSQSSEAWGRNFFIAVEIVGIFCAGQMVGRRKITPYH", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane. SIMILARITY: Belongs to the ATPase g subunit family."}
{"protein": "MQLLCVFCLVLLWEVGAASLSEVKLHLDIEGHASHYTIPWTELMAKVPGLSPEALWREANVTEDLASMLNRYKLIYKTSGTLGIALAEPVDIPAVSEGSMQVDASKVHPGVISGLNSPACMLSAPLEKQLFYYIGTMLPNTRPHSYVFYQLRCHLSYVALSINGDKFQYTGAMTSKFLMGTYKRVTEKGDEHVLSLIFGKTKDLPDLRGPFSYPSLTSAQSGDYSLVIVTTFVHYANFHNYFVPNLKDMFSRAVTMTAASYARYVLQKLVLLEMKGGCREPELDTETLTTMFEVSVAFFKVGHAVGETGNGCVDLRWLAKSFFELTVLKDIIGICYGATVKGMQSYGLERLAAVLMATVKMEELGHLTTEKQEYALRLATVGYPKAGVYSGLIGGATSVLLSAYNRHPLFQPLHTVMRETLFIGSHVVLRELRLNVTTQGPNLALYQLLSTALCSALEIGEVLRGLALGTESGLFSPCYLSLRFDLTRDKLLSMAPQEAMLDQAAVSNAVDGFLGRLSLEREDRDAWHLPAYKCVDRLDKVLMIIPLINVTFIISSDREVRGSALYEASTTYLSSSLFLSPVIMNKCSQGAVAGEPRQIPKIQNFTRTQKSCIFCGFALLSYDEKEGLETTTYITSQEVQNSILSSNYFDFDNLHVHYLLLTTNGTVMEIAGLYEERAHVVLAIILYFIAFALGIFLVHKIVMFFL", "text": "FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis. The heterodimer gH/gL targets also host EPHA2 to promote viral entry. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). SIMILARITY: Belongs to the herpesviridae glycoprotein H family."}
{"protein": "MSSSAASPLFAPGEDCGPAWRAAPAAYDTSDTHLQILGKPVMERWETPYMHSLAAAAASRGGRVLEVGFGMAIAASRVQQAPIKEHWIIECNDGVFQRLQNWALKQPHKVVPLKGLWEEEAPTLPDGHFDGILYDTYPLSEETWHTHQFNFIKTHAFRLLKPGGILTYCNLTSWGELMKSKYTDITAMFEETQVPALLEAGFQRENICTEVMALVPPADCRYYAFPQMITPLVTKH", "text": "FUNCTION: Converts guanidinoacetate to creatine, using S- adenosylmethionine as the methyl donor. Important in nervous system development. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family."}
{"protein": "MSFNVNWNSLETESLSSWTKELLTDALNSGKRPNILASGIQIKDLNFGKVGPSFEILEIGELDKDRFRGIFKINYEGDFHLTLHTKVQANPLKIYSSNSLDREVNQFDEMNNFVTPDFLLCNDPFALPLDLKLSDIKISGIGIIVFSQTKGLTLVFRNDPLDSIKVSSTFDTVQVLANFLQSQIEDQIGDLFRETLPTLIHELSLKYTSLNESNFSDLQSKLKSKMNNLDTEDLEKISINDVNSEFNYSSTNLRKNMNLFNSRETLNLSIPKLKNIVQRSHLEKFNKHLPNLVSTLNLNLNLPDVNVNNNIAPSQNNNCIPIDLLINNNNNLENILTEISSIQTSSYYNKLNSNNNGSKPNRRVIKLGGKKSKKASSANPLDQTPEYSEVSTLIDDSMEHSTIEHSTFESPVSLEHANLIDLKQPKPMRCTRDISIDTSKPILSHSHFHANGNSNTNSPHHPNSSLLRGVGLGNNYFNFTSNQQISTSHIENDEDRLMNKKSNNYIDIKSINNKSVDSKNIDQWKKLDFDKASLRQNCSSPQHNVFEVPPPPPYQY", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria- endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MDM34 family."}
{"protein": "MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNELSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSAGATVGIMIGVLVGVALI", "text": "FUNCTION: (Microbial infection) Receptor for E.coli Dr adhesins. Binding of E.coli Dr adhesins leads to dissociation of the homodimer. FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression (PubMed:2803308, PubMed:10910050, PubMed:10864933). Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:2803308). Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells (PubMed:10910050). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Apical cell membrane Cell surface Note=Localized to the apical glycocalyx surface. SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family."}
{"protein": "MNSSPPPANSANGDTTNNGENGQDLNLNFLDKIRLSAKRDAKEDEGEELPTELNTINSAGGFLVVSPDKLSVKYTNTNLHGHDVGVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKFTKDDAVGGGINYASQEFFFTKNGTIVGKIPKDIRGHLFPTVAVHSQNEEVLVNFGKKKFAFDIKGYEASERNKQQLAIEKISIPPNIGYGLVKTYLLHYGYEETLDAFNLATKNTVPPIHIDQENAIDEDDSSYALKQRKNLRQLVRNGEIDTALAELQKLYPQIVQDDKSVVCFLLHCQKFIELVRVGKLEEGVNYGRLELAKFVGLTGFQDIVEDCFALLAYEKPEESSVWYFLEDSQRELVADAVNAAILSTNPNKKDVQRSCHLQSHLEKLLRQLTVCCLERRSLNGDQGETFRLRHVLNNNR", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, perinuclear region Note=Associates predominantly in the form of large cytoplasmic complexes. SIMILARITY: Belongs to the RANBP9/10 family."}
{"protein": "MENKWFLLMVRDDFKGGKITLEKALKLLEKLDIQCNTIHVKYIFKDNDRLKQGRITIEEFRTIYRIITYREEIIEIFNTYSENRKILLEKNLVEFLMREQYTLDFNKSIASEIIQKYEPIEEVKQAHQMSFEGFRRYMDSSECLLFDNKCDHVYQDMTHPLTDYFISSSHNTYLISDQLWGPSDLWGYISALVKGCRCLEIDCWDGSQNEPVVYHGYTFTSKLLFKTVIQAINKYAFLASEYPVVLSLENHCSPSQQEVMADSLLATFGDALLSYTLDNFSDRLPSPEALKFKILVRNKKIGTLHETLERKGSDMHGKVEEFEEEEEIEQEEDGSGAKEPEPVGDFQDDLAKEEQLKRVVGIPLFRKKKIKISMALSDLVIYTKVEKFKSFHHSHLYQQFNESNSIGESQARKLTKLAAREFILHTRRFITRVYPKALRADSSNFNPQEFWNVGCQMVALNFQTPGVPMDLQNGKFLDNGCSGYVLKPRFLRDKKTKFNPHKVQIDSNPLTLTIRLISGIQLPPSYQNKADTLVIVEIFGVPNDQMKQQSRVIKKNAFNPRWNETFTFVIQVPELALIRFVAENQGLIAGNEFLGQYTLPVLCMNRGYRRVPLFSKMGESLEPASLFIYVWYIR", "text": "FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. SUBCELLULAR LOCATION: Nucleus Cytoplasm, perinuclear region Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity)."}
{"protein": "MPDSVEDTSTISLRICLEGHANALALNKDNNQIALAGRSLLKVYSINSNGFTESCNMRGKNQNLSYSANDVAWSTLDSNLLATAATNGVVSVWDLSKFGRQKQLLVYNEHERTAHTVTFHSSEPNILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKFSPHTQNIFSAVSENGTVQLWDMRKWDKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMDGRPGLEHTIHTIAVVGRVKWRPERTYHIASCALVVDYSVHVWDIRRPYIPFASFNEHTNVTTGIAWQGSDSHCLLSISKDSTIYKHAFKDATRPALKANAQGASLGRFGDISFANKIKEYEPKTSGASNTKSSSFIRRKTNVAGSIQFHLDHSKMYKFMVNDTFSGYPLSESVSRPTQEHESFIGCARELVISGKKLSELCEHNAEVSKKYGKHNATTLWNFIKLFYGSNHFEPPFEHRSSFSNQKNPMNSRRATQVASDWPQQRTELGQDLNGNTPETAHEIDVANVDDDTLGSSGVEHPPTSSVILSETQIISEITFDNFELLRNGFIYVGPTECPKALAFPALHHDVQAARPQLDLKASDHEKSPPPHVPTVLKVSHVPPIPMWEPHKFVSDALMLMNDVGDVQTALTVLIALGEARKLLPIDDALVEHWFYTYVDQLHRYELWNEACEVINRSWLRSVQQLNQHSTAMHTNCGECGRPMGGKVGWYCDKCKSMQSAKCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCPKCGHLCAYS", "text": "FUNCTION: An essential component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:27166823, PubMed:23723238). The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation (PubMed:27166823, PubMed:23723238). GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation and growth under nutrient replete conditions and during female oocyte development (PubMed:27166823, PubMed:23723238). This GATOR2 component is required for activating TORC1 and promoting cell growth in both germline and somatic cells (PubMed:27166823, PubMed:23723238). In addition to its role in regulation of the TORC1 complex, functions independently of TORC1 to promote the acidification of lysosomes and facilitates autophagic flux (PubMed:27166823). SUBCELLULAR LOCATION: Lysosome Cytoplasmic vesicle, autophagosome Note=Localizes to lysosomes and autolysosomes under fed and starved conditions (PubMed:27166823). In female egg chambers, localizes primarily to autophagosomes and autolysosomes during amino-acid starvation (PubMed:27166823). SIMILARITY: Belongs to the WD repeat WDR24 family."}
{"protein": "MIILWLILALSALLYWLHRANKDYHILSFFTKRIRLKDGTPVEIIAPIAKGKTIFGNTLDLYGRDHAGVFNYSRERAKEMGTSYIEYVFGKAIYNIIDADSAENVLNHPNLITKGLVYNFLHPFLRTGLLTSTGKKWHARRKMLTPTFHFNILNQFQEIFKTESQKFLLQFEGQDEVTITLHDVIPRFTLNSICETAMGVKLDEMAEKGDRYRENFSQIEECFIRRLSNPLLWGDKLFEMFAAKDFASALDVVHRFSSEIIAKRRDLLKDELDKSSSTADDDGFVSKKRFAMLDTLIYAEKDGLIDHIGICEEVDTLMFEGYDTTSIGLIFGLMNMSLNPDKQELCYQEIQEHIDDDLSNLDVGQLNKLKYLEYFMKETTRLFPSVPIMGREAVQETELANGLILPKGAQITIHVFDIHRNAKYWDSPEEFRPERFLPENVQDRHTYAYVPFSAGQRNCIGKKYAMQEMKTLMVVLLKQFKVLKAIDPQKIVFHTGITLRTQDKIRVKLVRRT", "text": "FUNCTION: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MGQRPQLRLVKALLLLGLNPVSTSLQDQQCESLSLASNVSGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHIAVIINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLISAFILRNATWFVVQLTVSPEVHQSNVAWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFVCIGWGVPFPIIVAWAIGKLYYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWRRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV", "text": "FUNCTION: G-protein coupled receptor for CRH (corticotropin-releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endosome Note=Agonist-binding promotes endocytosis. SIMILARITY: Belongs to the G-protein coupled receptor 2 family."}
{"protein": "MSEKVDVGESVKGDASENAVKEVAERPIVMIDNYDSFTWNVVQYLSNLEKRYPIMVFRNDEITVDELEKLNPLKLVLSPGPGHPARDGGICNEAISRFAGKIPILGVCMGLQCIFETMGGKVDSAGEIIHGKVSKINHDGLGFYQGIPQNISVTRYHSLAGKISSLPDCLDVTSWTENGVIMGARHKKYAIEGVQYHPESILSEYGKEYIQNFLNLTAGTWEENGIVMPTKNNAFNAAMRENSNSVSSTKIRKQESILEKIHAQRLIDIAESKRKPGLSVGDLQTYLNLNIAPPCINFYERLKQSKPALMAEVKRASPSKGDIKLDANAAIQALTYAQVGASVISVLTEPKWFKGSLNDLFVARKAVEHVANRPAILRKDFIIDPYQIMEARLNGADSVLLIVAMLSREQLESLYKFSKSLGMEPLVEVNCAEEMKTAIELGAKVIGVNNRNLHSFEVDLSTTSKLAEMVPDDVILAALSGISSPADVAHYSSQGVSAVLVGESLMRASDPAAFARELLNLSSSEISNGKKTSTPLVKVCGTRSLLAAKTIVESGGDLIGLIFVEKSKRKVDLSVAKEISHFVHTTNRKHISPKKAVTGQSWFDHQYENLASSPHPLLVGVFQNQPLEYIRSIIAEVNLDIVQLHGQEPFEWIHMLDRPVIKVFPLNSSEISRPNYHIVPLIDAYVGGESGGLGKKVDWEAASFIPVSYVLAGGLTPKNVQDAISVSRPAVVDVSSGVETDGKQDLEKIKAFINAVKEL", "text": "FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities."}
{"protein": "MKVTLFVTCLVDMFETNVGKATVEVLERLGCEIEFPEAQVCCGQPAYNSGHVESAKEAMKHMIETFEDAEYIVTPSGSCATMFHEYPHVFKDDPKWAARAQKVADKTYELTQFIVDVLKVTDVGASLKGTATMHKSCHMTRMLGVKEAPGILLSNVKGLTVKELPNVQNCCGFGGTFSVKMTPISEQMVDEKVDSVMETGADYLIGADCGCLLNIGGRIERLGKKVRVMHIAEVLNSRS", "text": "FUNCTION: Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. SIMILARITY: Belongs to the LutA/YkgE family."}
{"protein": "MQVQCQQSPVLAGSATLVALGALALYVAKPSGYGKHTESLKPAATRLPARAAWFLQELPSFAVPAGILARQPLSLFGPPGTVLLGLFCLHYFHRTFVYSLLNRGRPYPAILILRGTAFCTGNGVLQGYYLIYCAEYPDGWYTDIRFSLGVFLFILGMGINIHSDYILRQLRKPGEISYRIPQGGLFTYVSGANFLGEIIEWIGYALATWSLPALAFAFFSLCFLGLRAFHHHRFYLKMFEDYPKSRKALIPFIF", "text": "FUNCTION: Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5- alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology. SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the steroid 5-alpha reductase family."}
{"protein": "MDFEDDYTHSACRNTYQGFNGMDRDYGPGSYGGMDRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGGGSRFGPYESYDSRSSLGGRDLYRSGYGFNEPEQSRFGGSYGGRFESSYRNSLDSFGGRNQGGSSWEAPYSRSKLRPGFMEDRGRENYSSYSSFSSPHMKPAPVGSRGRGTPAYPESTFGSRNYDAFGGPSTGRGRGRGHMGDFGSIHRPGIVVDYQNKSTNVTVAAARGIKRKMMQPFNKPSGTFIKKPKLAKPMEKISLSKSPTKTDPKNEEEEKRRIEARREKQRRRREKNSEKYGDGYRMAFTCSFCKFRTFEEKDIELHLESSSHQETLDHIQKQTKFDKVVMEFLHECMVNKFKKTSIRKQQTNNQTEVVKIIEKDVMEGVTVDDHMMKVETVHCSACSVYIPALHSSVQQHLKSPDHIKGKQAYKEQIKRESVLTATSILNNPIVKARYERFVKGENPFEIQDHSQDQQIEGDEEDEEKIDEPIEEEEDEDEEEEAEEVGEVEEVEEVEEVREGGIEGEGNIQGVGEGGEVGVVGEVEGVGEVEEVEELEEETAKEEPADFPVEQPEEN", "text": "FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro. SUBCELLULAR LOCATION: Nucleus matrix. SIMILARITY: Belongs to the AKAP95 family."}
{"protein": "MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVTPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNRFLRLRPGTHKEDILPALKRVQAGHLINAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCGVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSLHPEFISMFGPRGAEQLGIYRHHHNHRHDLQGRIVLRRGNDRS", "text": "FUNCTION: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. FUNCTION: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family."}
{"protein": "MDLQLTTNSTDSGDRGGSSNESLQRQPPSQYSPAEVAGLAAVVSFLIVFTIVGNVLVVIAVLTSRALKAPQNLFQVSLASADILVATLVMPFSLANELMNYWYFGKVWCVIYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPRRIKGIIVTVWLISAVISFPPLISLYRDPEDDLYPQCELNDETWYILSSCIGSFFAPCIIMVLVYVRIYRVAKLRTRTLSEKRTVPEGSSQTENGLSRPPVGAGPSTAAAAAASLRLQAGENGHYHLHHHHHHLHHHHHHHHHQLRKSAELEDIELEESSTSENRRRRRSREEAAARKGSRGFSFSFSSTKGGQSAGAGSRLSRASNRSLEFFSTHRRRKRSSLCRRKVTQAREKRFTFVLAVVMGVFVVCWFPFFFTYSLYGICREACQVPETLFKFFFWIGYCNSSLNPVIYTIFNQDFRRSFKHILFKKKKKTSLQ", "text": "FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2C sub-subfamily."}
{"protein": "MSLELHFAVSQFLYKKAELCDNYDWDAYIDLYDEDSEYHIPQWIDDHNYVQDPNQGLSYIYYEDRSGLEDRVFRIRTGKAASATPLPRTQHNIHNVQVKTLEDGLIEAKVSWRTLYNRQGLEGCFYGRATYVLRPTEDSFRIRRQHSVLLNDKIDSVLDFYHV", "text": "FUNCTION: Component of anthranilate dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into anthranilate to form catechol. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family."}
{"protein": "MAAARNLRTALIFGGFISMVGAAFYPIYFRPLLRLEEYQKEQAVNRAGIVQEDVQPPGLKVWSDPFGRK", "text": "FUNCTION: [Phoenixin-14]: Peptide involved in a broad spectrum of regulatory functions (PubMed:27440717, PubMed:28844870, PubMed:29364701, PubMed:28965207, PubMed:30609107). Is a ligand for GPR173 (PubMed:27440717). As part of the reproductive cycle, it regulates gonadotropin-releasing hormone (GnRH) signaling in the hypothalamus and pituitary gland which augments the release of luteinizing hormone (PubMed:22963497, PubMed:27440717). More specifically, it regulates the expression of transcription factors CEBPB and POU2F1/OCT1 through the cAMP-PKA signaling pathway, which subsequently regulate the expression of GNRHR and KISS1 (By similarity). Plays a protective role in memory retention through activation of GNRHR (By similarity). Regulates the secretion of AVP by hypothalamic neurons (PubMed:29364701). Plays a role in the transduction of the itch sensation (By similarity). Induces anxiolytic effects, reducing behavior associated with anxiety (By similarity). Regulates food intake as well as satiation and satiety by increasing NUCB2 expression in neurons (PubMed:28844870, PubMed:30930149). In the ovary, it regulates follicular growth by stimulating granulosa cell proliferation by increasing the expression of GPR173, CREB1, CYP19A1, KITLG, FSHR, and LHCGR (By similarity). It also increases the production of estradiol (E2) (By similarity). In the heart, it regulates contractility and relaxation by activating the AKT1-NOS3 and MAPK1-MAPK3 signaling pathways (PubMed:28965207). It also plays a cardioprotective role during ischemia, where it activates the SAFE and RISK pathways (PubMed:28965207). Stimulates the proliferation and differentiation of preadipocytes (PubMed:30251651). In pancreatic islet cells, it induces proliferation of islet cells as well as the production of INS1 and INS2 through activation of the MAPK1-MAPK3 signaling pathways (PubMed:31422055). FUNCTION: [Phoenixin-20]: Peptide involved in a broad spectrum of regulatory functions (PubMed:27440717, PubMed:28844870, PubMed:29364701, PubMed:28965207, PubMed:30609107). Is a ligand for GPR173 (PubMed:27440717). As part of the reproductive cycle, it regulates gonadotropin-releasing hormone (GnRH) signaling in the hypothalamus and pituitary gland which augments the release of luteinizing hormone (PubMed:22963497, PubMed:27440717). More specifically, it regulates the expression of transcription factors CEBPB and POU2F1/OCT1 through the cAMP-PKA signaling pathway, which subsequently regulate the expression of GNRHR and KISS1 (By similarity). Plays a protective role in memory retention through activation of GNRHR (By similarity). Regulates the secretion of AVP by hypothalamic neurons (PubMed:29364701). Plays a role in the transduction of the itch sensation (By similarity). Induces anxiolytic effects, reducing behavior associated with anxiety (By similarity). Regulates food intake as well as satiation and satiety by increasing NUCB2 expression in neurons (PubMed:28844870, PubMed:30930149). In the ovary, it regulates follicular growth by stimulating granulosa cell proliferation by increasing the expression of GPR173, CREB1, CYP19A1, KITLG, FSHR, and LHCGR (By similarity). It also increases the production of estradiol (E2) (By similarity). In the heart, it regulates contractility and relaxation by activating the AKT1-NOS3 and MAPK1-MAPK3 signaling pathways (PubMed:28965207). It also plays a cardioprotective role during ischemia, where it activates the SAFE and RISK pathways (PubMed:28965207). Stimulates the proliferation and differentiation of preadipocytes (PubMed:30251651). In pancreatic islet cells, it induces proliferation of islet cells as well as the production of INS1 and INS2 through activation of the MAPK1-MAPK3 signaling pathways (PubMed:31422055). FUNCTION: [Small integral membrane protein 20]: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly (By similarity). Promotes the progression of complex assembly after the association of Mt-Co1/Cox11 with Cox4I1 and Cox6c (By similarity). Chaperone-like assembly factor required to stabilize newly synthesized Mt-Co1/Cox1 and to prevent its premature turnover (By similarity). SUBCELLULAR LOCATION: [Phoenixin-14]: Secreted. SUBCELLULAR LOCATION: [Phoenixin-20]: Secreted. SUBCELLULAR LOCATION: [Small integral membrane protein 20]: Mitochondrion inner membrane; Single- pass membrane protein."}
{"protein": "MNAPPAFESFLLFEGEKITINKDTKVPNACLFTMNKEDHTLGNIIKSQLLKDPQVLFAGYKVPHPLEHKIIIRVQTTPDYSPQEAFTNAITDLISELSLLEERFRTCLLPLRLLP", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family."}
{"protein": "MRCSLLTPTSYRFHYPNPFRSLESIPPLSNSRYRIESGSPSSFKFSAPSLQRHSSVSVKAFDDDTFDFYTGDIFAATYAISSSEGEESDGDYALNVVTETTAQKLGKFPRGRKKHRIRYGINLGLLAFLSLLLLLMDSFAWKIVRLPLPPYFLSMPFFTSAILVTLAGYIFVPLLDRLRVHEPIRTLGPVPHNRRPTIPTMGGLFFVPIGVVVAIALNKVSSIEVLGAAAATVAFAAIGLIDDSLSLYSENNNGLSAKIQLLLEAAVGTCFAFWLETASLSSPYGMKMLVPLPSPLGLVFLGKLYLLLTSFYFVSMGNLVKATDGLDGLAGGIAALCFVAMAIAVLPICSDLSVFGASMAGACFGFLLHNRYRASVSMGDTGSLALGGALAAMAACSGMFFPLFISSGVAVLEASSVIIQVVYYSTTKRLKGKGRRIFKTIPFHHHLRLNGLKEPMIVTMAYVISSLLSLSAAYIGLISA", "text": "FUNCTION: May be involved in glycosylation events. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily."}
{"protein": "MARLLLFPSQACVDPGRHLLLHPPVSRPRAVRSGPPPAAPRRTGVVSLPGRCPPPLCWNHHPFLPCRSSKRGWVVFASENVQEISSHLPRKDERRSGNLLLRFSALPYCTMAWLSTAQLAQSSVGEKLNMVYEVGELFELGIQLSYLLILIGLLGAGTFFVIRQVLVRRELDLSAKELQEQVRSGDASATEYFELGAVMLRRKFYPAAIKYLQQAIDKWDRDEQDLAQVYNALGVSYKRENKLDKAIQQFQKAVELQPGYVTAWNNLGDAYEQQKDLKSALKAFEEVLLFDPNNKVARPRVDDLRPRVSMYKGVPVKSEKR", "text": "FUNCTION: Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI). Functions as PSI biogenesis factor. Cooperates with PSA3 to promote the stable assembly of PSI in the thylakoid membrane. May target primarily the PsaC subunit. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein Note=Copurifies with PSI."}
{"protein": "MQIIEITEPEQADFKQERQIAVGIDFGTTNSLIAIATNRKVKVIKSRDDKELIPTTIDFTNENFIIGNNKGLRSIKRLFGKTLKEILNTPALFSLIKDYLEANSSELKLNFANKQLRISEIAAEVFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGDDIDVVITQYLCNKFDLPNSVDTLQLAKKAKETLTYKDSFNNDNISINKQTLEQLILPLVERTINIAKECLEQAGNPKIDGIILVGGATRTPLIKTELSKAFKVQHISKRFRQDEFKGEPAGRIKIREHRQVLQNSLVSNFMEYAVDILSDIDPDKAVVWGAALQAENLTAPHTNSLLIDVVPLSLGVELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAVDCRSLARFELKGLPPMKAGNIRAEVTFAIDADGILSVSAYEKISNTSHTIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAIIEAEALIFSIERAIAELTALLSESEISIINSLLDNIKEAAHARDRILINNSIKEFKSKIKKSMNTKLNIIINDLLKGKNINQTK", "text": "FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (By similarity). SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MGEPSKEEYKIQCFDAETQQLLKTALKDPGAVDLEKVANVIVDHSLQDSVFSKEAGRMCYAIIQAESKQAGQSVFRRGLLNRLQQEYQTREQLRARSLQGWVCYVTFICNIFDYLRVNNMPMMALVNPVYDCLFRLAQPDSLSKEEEVDCLVLQLHRVGEQLEKMNGQRMDELFVLIRDGFLLPAGLSSLAQLLLLEIIEFRAAGWKTTPAAHKYYYSEVSD", "text": "FUNCTION: Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the MIF4GD family."}
{"protein": "MAIRSSGRKLSFEILSQNSSFENDDTSIRRSSSDPITGNVASESPRDYGKRKRSKKKKKKVNQVETILENGDSHSTIITGSSGDFGETTTMFENRLNYYGGGGSGSSGGGCVVTLLDGQTVHHNGFNFGELRQRNVNGSVDGSNDERWSDTLSSDKKLYMEETSVELSPSENPPFQEVQHQFPRSEINGNVVRRLDTEASLDWKQLVADDPDFLSAETRSPMKYFMEEIYGGISLRSTTTPGNDIERERIYDTIFRLPWRCEVLIDTGFFVCVNSFLSLLTVMPIRVLLIFMDAFKNRQFRRPSASELSDLACFLVLATGTILLGRTDISLIYHMIRGQSTIKLYVVYNILEIFDRLCQSFCGDVFGALFSSAKGLSISPPEKLRFSTWRFVSDLALTMAASILHSFILLAQAITLSTCIVAHNNALLALLVSNNFAEIKSSVFKRFSKDNIHGLVYADSIERFHISAFLVSVLAQNILESEGAWFGNFIYNATTVFFCEMMIDIIKHSFLAKFNDIKPIAYSEFLQALCEQTLNIRPEDRKTNLTFVPLAPACVVIRVLTPVYAAHLPYSPLPWRMLWMVILFVITYIMLTSLKVLIGMGLRKHATWYINRCRRRNSSHLHND", "text": "FUNCTION: Probable component of the calreticulin 3 (CRT3) complex, acting probably as a co-chaperone involved in protein retention in the endoplasmic reticulum lumen. Required for micropylar pollen tube guidance. Plays an essential role in cell plate orientation or positioning in early embryo patterning. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Endoplasmic reticulum lumen Note=Exclusive ER lumen localization and no membrane localization in PubMed:21954464. SIMILARITY: Belongs to the TAPT1 family."}
{"protein": "MKVLLHLPALLASLTLLQTAASASDDPTAETDIIHDTVEEVKVWVNKAFLDSRDRLKMAMTTKIHSTRHLSDYLKHAKGRTRTAIRSGQVWEESLKKLSQFLTNVTGQGLDLTLLSWEAGCDPPAPTMTCNISSPYRTITGYCNNRKNPALGSANRALARWLPAEYEDGLSLPYGWTPGKMRNGFPLPQPREVSNQIAAYLNEEDVLDQKRSMLFMQWGQIVDHDMDFAPETEMGSDTYTKAQCDEHCIQGDNCFPIMFPPGDPKLKTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASLVYSPEPSLANRLRNLSSPLGLMAVNEEVSDNGRPFPPFVKMKPSPCEVINATAGVPCFLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKWIPPYQGYNESVDPRISNVFTFALRFGHLEIPSTVYRLDENYQPWGSESELPLHTVFFNTWRLVKDGGIDPLVRGLLAKNAKLMHQNKMMTGELRNKLFQPNHTIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAKKLMDLYGTPSNIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRESLQKMSFSRLVCDNTGIDKVPLNPFQANAYPHGFVDCSSIDKLDLSPWASVKE", "text": "FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism (By similarity). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (PubMed:34127712). SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Expressed in the cytoplasm in intestinal epithelial cells. SIMILARITY: Belongs to the peroxidase family."}
{"protein": "MNFFLYFRTIFLIQLYFFNYSTFGCSASSTSVQSDTTNQVSVSCPKYTTIYTSGTSPDTKTIYPESTSTKSITTSTQSHSSPVIVVSTVGTVTETTISGSTEYTTTIPAEGITSGTVEIVEPTAGTVTETITSGTLPFTTTLAQASGTVSGTVEIVSPKNNPTTVYSGTVATTETFSSSTVVVIPTAICDGVRGLEYAVYDYTISSSMNEFCYPKNGQTDVFAFNEPAYFGSSDLDQSSPLFTGVFSSTDDIPEWASSWYLPPYPPQASDMASTYCACKVIVYQFFLRIPETDTYTLVVNNVDDVFFGWFGDKAISGWSNNNFDAYSYWHESPNMGLGTVGMGNFTVGNYPEGYFLPVRFVVANGAYIGGFDFYFTSDSTGPLATTSYSYTKTCTQQFLPFGQGNGGVNGPTEKLS", "text": "FUNCTION: May be involved in agglutination during conjugation or other aspects of colony formation (By similarity). Induces flocculation when overexpressed (PubMed:23236291). FUNCTION: May be involved in agglutination during conjugation or other aspects of colony formation. SUBCELLULAR LOCATION: Cell surface. SIMILARITY: Belongs to the mam3/map4 family."}
{"protein": "MAQSLALSLLILVLAFGIPRTQGSDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWVQQLMQHLDKTPSPQKPAQGCRKDRGASKTGKKGKGSKGCKRTERSQTPKGP", "text": "FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "NTEAFFGQGTRLTVV", "text": "FUNCTION: J region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). SUBCELLULAR LOCATION: Cell membrane."}
{"protein": "MEPPMDPSGGEQEPGAVRLLDLPWEDVLLPHVLSRVPLRQLLWLQRVSRAFRALVQLHLARLRRFDAAQVGPQIPRAALAWLLRDAEGLQELALAPCHEWLSDEDLVPVLARNPQLRSVALAGCGQLSRRALGALAEGCPRLQRLSLAHCDWVDGLALRGLADRCPALEELDLTACRQLKDEAIVYLAQRRGAGLRNLSLAVNANVGDTAVQELARNCPELQHLDLTGCLRVGSDGIRTLAEYCPALRSLRVRHCHHVAEPSLSRLRKRGVDIDVEPPLHQALVLLQDMVGFAPFVNLQV", "text": "FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation and bone mass maintenance. Also mediates ubiquitination of SMURF2 and WWP2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBXL15 family."}
{"protein": "MGREFLGLFEEWADSYDQSVEGYDEEYREVFANYEDILNTVASKAGSVVLEFGVGTGNLTKKLLEQGKTVYGIEPSEPMRKKAREKLGDKVLIVDGDFLQFPLPPKPIDTIVSTYAFHHLTDEEKGEAIAKYSQLLKKGDKIVFADTAFRDRQAFQRAIEEARERGFHHLADDLGREYYTTLDVLTKLFKENGFTVTFTQKNAFVWVMEAVKQ", "text": "FUNCTION: Could be a S-adenosyl-L-methionine-dependent methyltransferase. SIMILARITY: Belongs to the methyltransferase superfamily. YrrT family."}
{"protein": "MNALAATSRNFKQAAKLLGLDSKLEKSLLIPFREIKVECTIPKDDGTLASYVGFRVQHDNARGPMKGGIRYHHEVDPDEVNALAQLMTWKTAVANIPYGGAKGGIGCSPGDLSISELERLTRVFTQKIHDLIGIHTDVPAPDMGTNSQTMAWILDEYSKFHGYSPAVVTGKPVDLGGSLGRDAATGRGVLFATEALLAEHGKGIAGQRFVIQGFGNVGSWAAQLISEAGGKVIAISDVTGAVKNVDGLDIAQLVKHSAENKGIKGFKGGDAIAPDSLLTEECDVLIPAALGGVINKDNANDIKAKYIIEAANHPTDPEADEILSKKGVLILPDILANSGGVTVSYFEWVQNIQGFMWDEEKVNAELRTYITRAFGNVKQMCRSHSCDLRMGAFTLGVNRVARATVLRGWEA", "text": "SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
{"protein": "MKTLVLVAVLGVASLYLLSSASEVQQLSPAEEEFRAFVSTFGGLFETEERGVDSEDCRAMFGGCGEDNDCCLHLGCKTTKLPPFANPYCAWDGTTGRK", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 27 (ICK-3) subfamily."}
{"protein": "MNAELIVQLGSLALITVAGPAIIVLLFLKQGNL", "text": "FUNCTION: A core subunit of photosystem II (PSII). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Ycf12 family."}
{"protein": "MALFRMLFLCAVLVLLTSKEGMSYEEPENDEGVACTGQYAESFCLNGGTCRYIQSIGEYYCICNGDYTGHRCEKKQV", "text": "FUNCTION: Has both toxic and EGF activity. Its EGF activity consists of rounding cells (morphological change) and inducing tyrosine phosphorylation of the EGFR in A431 cells, but with a lower potency that human EGF. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the EGF domain peptide family."}
{"protein": "MATTPINGHATKSPSLDAAEARRLKHNHADVVIIGAGVLGCALAVALGRQGRSVILLEASLKEPDRIVGELLQPGGVQALEKLGLRDCLEGIDSIPVKGYYVSYFNDPVPIPYPKPTPASPPPEGRCFHHGRFVMKLREAAMACPNVSVVETKATDLVTCSHTQQVLGVECTSKDNVRACYFGHLTVVADGYASKFRKQHHPHTPKVSSRFWGLELIDTKLPMPYYGHVLLSDNAPILLYQIGTHETRILVDIPENLPSASVKNGGVKSHMRNVVLPSLPESVQPAFIAALEQGQLRSMPNSFLPAATNTTPGLVILGDALNMRHPLTGGGMTVAFNDVVTLRNLLSPEKVPNLGDTKRVMKQLSTFHWERKKAASVINILAQALYSLFAADNQYLRALQRGCFRYFQLGLVDGPAGLLGGLIQKPSVLFVHFFSVALLSLWVLLREYPPYLFPVALFKCIMTFWTACVVIFPYMLIEAFC", "text": "FUNCTION: Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16110826) (Probable). Erg1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)- sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4- methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)- tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Microsome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the squalene monooxygenase family."}
{"protein": "MSRSPDAKEDPVECPLCMEPLEIDDINFFPCTCGYQICRFCWHRIRTDENGLCPACRKPYPEDPAVYKPLSQEELQRIKNEKKQKQNERKQKISENRKHLASVRVVQKNLVFVVGLSQRLADPEVLKRPEYFGKFGKIHKVVINNSTSYAGSQGPSASAYVTYIRSEDALRAIQCVNNVVVDGRTLKASLGTTKYCSYFLKNMQCPKPDCMYLHELGDEAASFTKEEMQAGKHQEYEQKLLQELYKLNPNFLQLSTGSVDKNKNKVTPLQRYDTPIDKPSDSLSIGNGDNSQQISNSDTPSPPPGLSKSNPVIPISSSNHSARSPFEGAVTESQSLFSDNFRHPNPIPSGLPPFPSSPQTSSDWPTAPEPQSLFTSETIPVSSSTDWQAAFGFGSSKQPEDDLGFDPFDVTRKALADLIEKELSVQDQPSLSPTSLQNSSSHTTTAKGPGSGFLHPAAATNANSLNSTFSVLPQRFPQFQQHRAVYNSFSFPGQAARYPWMAFPRNSIMHLNHTANPTSNSNFLDLNLPPQHNTGLGGIPVAGEEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA", "text": "FUNCTION: Has E3 ubiquitin ligase activity, promoting ubiquitination and degradation of target proteins (PubMed:11823428, PubMed:22159038, PubMed:26575292). Involved in activation of the JAK/STAT pathway (PubMed:11823428, PubMed:22159038). Catalyzes ubiquitination of methylated RBM15 (PubMed:26575292). Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA (PubMed:29861391). As part of the PINK1-regulated signaling, upon mitochondria damage, ubiquitinates ABCE1 and thereby recruits autophagy receptors to the mitochondrial outer membrane to initiate mitophagy (PubMed:29861391). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MEFESVFKMHYPYLAAVIYDDSSTLKDFHPSLTDDFSCVHNVHHKPSMPHTYEIPSKETIRGITPSPCTEAFEACFHGTSNDHVFFGMAYTTPPTIEPNVSHVSHDNTMWENDQNQGFIFGTESTLNQAMADSNQFNMPKPLLSANEDTIMNRRQNNQVMIKTEQIKKKNKRFQMRRICKPTKKASIIKGQWTPEEDKLLVQLVDLHGTKKWSQIAKMLQGRVGKQCRERWHNHLRPDIKKDGWTEEEDIILIKAHKEIGNRWAEIARKLPGRTENTIKNHWNATKRRQHSRRTKGKDEISLSLGSNTLQNYIRSVTYNDDPFMTANANANIGPRNMRGKGKNVMVAVSEYDEGECKYIVDGVNNLGLEDGRIKMPSLAAMSASGSASTSGSASGSGSGVTMEIDEPMTDSWMVMHGCDEVMMNEIALLEMIAHGRL", "text": "FUNCTION: Transcription activator that recognizes the motif 5'-TAACGG- 3' in the promoter of endosperm-induced genes (PubMed:27681170, PubMed:25194028, PubMed:19066902). Promotes vegetative-to-embryonic transition and the formation of somatic embryos from root explants in a WUS-independent manner but via the expression of embryonic genes (e.g. LEC1, LEC2, FUS3 and WUS) (PubMed:18695688). May play an important role during embryogenesis and seed maturation (PubMed:19066902, PubMed:25194028). Together with MYB115, activates the transcription of S-ACP-DES2/AAD2 and S-ACP-DES3/AAD3 thus promoting the biosynthesis of omega-7 monounsaturated fatty acid in seed endosperm (PubMed:27681170). Regulates negatively maturation genes in the endosperm (PubMed:25194028). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAPMSLLQQLEAIESTLLEKEADRNSRQKRCLGENVPCGDFPCCGKLACEKTFGYGWWYKSPFCVKPSKG", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 03 (ICK-30- 40) subfamily."}
{"protein": "LALLFLVLSAGSGFTQGVRNHVTCRINRGFCVPIRCPGRTRQIGTCFGPRIKCCRSW", "text": "FUNCTION: Has bactericidal activity. Active against E.coli ML35 and S.aureus 502A. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MMSIPMELMSIRNPNSTLLYRAHSRPPVKLCAPPRSLLPSRRHFSAPRAVVSYPGIRFGFTSPEVLLNRSVVAFAASHEDSGESGVEVGKEKSDIDVEDDTSKEAWKQTLESFKEQVSKMQSVSSEAYSVNSQKAMTVLKETSEQLRIQAEKAKEELGTKAKVVSEEGREYILKAAEESPSDVKEIVEAFASTEDLKNVSRANDFHVGIPYGLLLLVGGFINFMVSGSIPAIRFGVILGGALFALSLASLKSHRKGESSTKFLKGQMAIVAIIFLRELRLLLSQKSTFLGFFTTLTSGGVLGFYLYKMVVKREKGPTLEDGGEDESSDGFVRSEG", "text": "FUNCTION: May be involved in free fatty acids export from the plastids. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM14 family."}
{"protein": "MFPARWHNYLQCGQVIKDSNLICFKTPLRPELFAYVTSEEDVWTAEQIVKQNPSIGAIIDLTNTSKYYDGVHFLRAGLLYKKIQVPGQTLPPESIVQEFIDTVKEFTEKCPGMLVGVHCTHGINRTGYMVCRYLMHTLGIAPQEAIDRFEKARGHKIERQNYVQDLLI", "text": "FUNCTION: Plays a role in the regulation and processing of late viral mRNAs by displaying RNA 5'-triphosphatase and diphosphatase activities. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class CDC14 subfamily."}
{"protein": "MRVVILGSGVIGVTSAWYLAQAGHQVTVVDRQEGPGLETSAANAGQISPGYAAPWAAPGIPLKALKWLFQRHAPLAMSLDGSLFQLRWLWQMLRNCDSTHYAQNKARMVRLAEYSRDCLAQLRRTTTIDYEGRQLGTLQLFRTPQQYENAARDIAVLREAGVPYRLLPTAQLSTVEPALAVAGVRLSGGLHLPHDETGDCQLFTRHLAQQAAQSGVHFIFSTQVLRLLRSGARIQGVQCGHDTLVADAYVVALGAYSTGLLQDIVAIPVYPLKGYSLTLPIDDPDAAPRSTVLDESYKVAITRFDRRIRVGGMAEVVGFDMSLPLARRRTLERVVRDLYPRGGLLPQASFWSGLRPATPDGTPLVGATPLENLYLNTGHGTLGWTMACGSGQLLADIISGVTPTIRVDDLSVSRYTA", "text": "FUNCTION: Oxidative deamination of D-amino acids. SIMILARITY: Belongs to the DadA oxidoreductase family."}
{"protein": "MSSSRNTHWCHRCQRAVRLHGQEPVCFYCGGGFVEELDMAQASPFDMFRSHRGVVERDQTFDLMDAFSVFMRNRLAERSHDREIRGRTISSGPENFPGLAPLLIFGGQVPYRLTGDNAVEALFNGGSPGIGITRGNTGDYFFGPGLEELFEQLSAGTTRRGPPPAPRSAIDALPTIKIAQRHLRSSDSNCPVCKDEFELGSEAKQMPCNHIYHSDCIVPWLVQHNSCPVCRQELPSASGPSSSQNRTTPTRNYRSSSSSSSSNSRENGNERRNPFSSFWPFRSSGSSSSSTQNRGGTRNSDTSDENHNYHQQQHQQSYMGYSGWPFDY", "text": "FUNCTION: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro."}
{"protein": "MASLPAPPTPLGSCPRGRGGGRVVARPRRAGLACAARSCYRFRTDDDGVVDVAVSGEDGDGGGGGYAVSVEVPGTRGREGGLVLRASGSGEGVPLAPAAGGASLAAELSFDPTRAPFYLSFLLTDASGAEIRTHRKTSFRVPVGVGPGSPAPLGMSISGDGAVNFAVYSKNANAVSLYLYAAAVGGGGGDEPALEIDLDPYIHRTGNVWHVSLASVDGYVSYAFCCGGIRRPLLDPYAKVIGDFVSSNSVYDEGVTAPSMRCFASLAIAPSYNWGRDRHPRLPLEKLVVYRANVALFTKDRSSGLPDDAAGTFTGLSAKVEHFRSLGVNAILLEPVFPFHQVKGPYFPYHFFSPMNLYSSKGLSVSAIKSMKDMVRVMHRNGIEVLLEVVFTHTAEGESECQTISMRGIDNSSYYIANGIAGCKASILNCNHPVTQKLILDSLRHWVLDFHVDGFCFINAPFLVRGPGGEYLSRPPLLEAITFDPVLSMTKIIADPWSPLDISNVQFPFPHWKRWAEVNTRFSIDVRKFLKREALISDLATRLCGSGDLFSTRGPAFSFNHVSRNSGLSLVDLVSFSNDDLLSESSWNCGEEGPSENSAVLQTRLRQIRNFLFILFVSLGVPVLNMGDECGHSAAGSVSYKDRGPLNWRGMKTTFVKEVTGFISFLTALRSRRGDIFQRREFLKLENIHWYGSDLCEPGWDDPTSNFLCMHINAEVDEMAADSVRGDLYICFNANEESVSAALPALAEGSVWLRLVDTSLAFPGFFATESNPKVQQVPGLSSYHVEAHTCVLFESKSALA", "text": "FUNCTION: Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch (PubMed:16953433, PubMed:21436381). Works together with ISA1 as heterooligomer. The heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1 homooligomer for various branched polyglucans in vitro, but no marked differences exist in chain preferences for debranching of amylopectin and phytoglycogen between these forms (PubMed:16953433, PubMed:21436381). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
{"protein": "MSFSEFYQRSINEPEQFWAEQARRIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPLPPGCIQTIWGDDGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLDQIRQAMEE", "text": "FUNCTION: Catalyzes the synthesis of propionyl-CoA from propionate and CoA. Also converts acetate to acetyl-CoA but with a lower specific activity (By similarity). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MTTSLLLHPRWPESLMYVYEDSAAESGIGGGGGGGGGGTGGAGGGCSGASPGKAPSMDGLGSSCPASHCRDLLPHPVLGRPPAPLGAPQGAVYTDIPAPEAARQCAPPPAPPTSSSATLGYGYPFGGSYYGCRLSHNVNLQQKPCAYHPGDKYPEPSGALPGDDLSSRAKEFAFYPSFASSYQAMPGYLDVSVVPGISGHPEPRHDALIPVEGYQHWALSNGWDSQVYCSKEQSQSAHLWKSPFPDVVPLQPEVSSYRRGRKKRVPYTKVQLKELEKEYAASKFITKEKRRRISATTNLSERQVTIWFQNRRVKEKKVVSKSKAPHLHST", "text": "FUNCTION: Transcription factor which plays a role in hair follicle differentiation. Regulates FOXQ1 expression and that of other hair- specific genes (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Abd-B homeobox family."}
{"protein": "MSRFLNVLRSWLVMVSIIAMGNTLQSFRDHTFLYEKLYTGKPNLVNGLQARTFGIWTLLSSVIRCLCAIDIHNKTLYHITLWTFLLALGHFLSELFVYGTAAPTIGVLAPLMVASFSILGMLVGLRYLEVEPVSRQKKRN", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERG28 family."}
{"protein": "MRWRDRIAVLCFPPGLMLTVAALILFFIHMGVFASDVHNFCVIHNYDHMSFRYTVVLIFSQVISIGWAAMGSLYAEMTGDKFLRCFALTILILNGAMFFNRLCLEFLAINYREERH", "text": "FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane; Multi-pass membrane protein."}
{"protein": "MKLKDFAFYAPCVWGTTYFVTTQFLPADKPLLAALIRALPAGIILILGKNLPPVGWLWRLFVLGALNIGVFFVMLFFAAYRLPGGVVALVGSLQPLIVILLSFLLLTQPVLKKQMVAAVAGGIGIVLLISLPKAPLNPAGLVASALATMSMASGLVLTKKWGRPAGMTMLTFTGWQLFCGGLVILPVQMLTEPLPDLVTLTNLAGYLYLAIPGSLLAYFMWFSGLEANSPVIMSLLGFLSPLVALLLGFLFLQQGLSGAQLVGVVFIFSALIIVQDISLFSRRKKVKPLEQSDCVIK", "text": "FUNCTION: Involved in pectinase, cellulase, and blue pigment regulation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EamA transporter family."}
{"protein": "MFQVAGLIVFCGLLAQTTALLEALPLGKALPLALDQSPTDLVGSLTSTLSNGLLSEGVLGILGNLPLLDILKAGGNTPSGLLGGLLGKLSSTIPLLNDIVDLQITDPQLLELGLVQSPDGHRLYVTIPLSLVLNVKTSVVGSLLKLAVKLNITVELLAVKDEQGKSHLVLGDCTHSPGSLKISLLDGLGPLVPQDLLDSITGVLDNVLPGLVQGEVCPLVNEVLSHLDVTLVHSIVDALIQGQEFVIKV", "text": "FUNCTION: Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus. Plays a role in the airway inflammatory response after exposure to irritants. May attract macrophages and neutrophils. SUBCELLULAR LOCATION: Secreted Note=Apical side of airway epithelial cells. Detected in airway surface liquid, nasal mucus and sputum (By similarity). SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. Plunc family."}
{"protein": "MKKIAFDSEKYLNLQRDHILERINQFEGKLYMEFGGKMLEDFHAARVLPGYEPDNKIRLLKELKDQVEIVIAINANNIEHSKARGDLGISYDQEVLRLIDTFNELDIYVGSVVITQYSGQPAADLFRSQLEKNGIASYIHYPIKGYPTDMDHIISPEGMGKNDYIKTSRNLVVVTAPGPGSGKLATCLSNMYHDQINGIKSGYAKFETFPVWNLPLHHPVNLAYEAATADLDDVNMIDPFHLQTYGKTTVNYNRDIEIFPVLKRMLERILGKSPYASPTDMGVNMVGFAIVDNDAAIEASQQEIIRRYYQTILDFKAERVSESAVKKIELLMNDLGITPLDRKVTVVARDKAESTGEPALALELPNGEIVTGKTSELFGPTAAVLINAIKKLAHIAKETKLIEPEYVKPIQGLKINHLGSRNPRLHSNEILMALAITAMENQDAANAMQQLGNLKGSEAHSTVTLTDEDKNVLRKLGIHVTMDPVYQYDRLYRK", "text": "SIMILARITY: Belongs to the UPF0371 family."}
{"protein": "MAACGAEERQRTGRLSALSVYRRAAGPGRLERRRRGTPLPAGGKRTKARLRRGAAGGGGPERAAPPQGAAVSDRVERAGSSEAKQGDLKTNPSGPPAKAPAGNLETKSPGGPLTTSVGPRAKAPAGSPEAKPPGDPATSPGGGGVPGLLRRLGRLEDSRRRAAELFRWLVAPAAPEEFARQHWERAPLLVQRGDPGYYAGLFSTADFDAILRSGDVHFGTHLDVTSYAEGVRETHNPVGRALPAVVWDFYQNGCSLRLLSPQAFSTTVWHFLSILQEHFGSMAGANTYLTPPGTQGFAPHYDDIEAFVLQLEGKKHWRVYGPRTSSEALPQFSSANLTQAELGEPLLEVVLEAGDLLYFPRGFIHQADCLPDAHSLHITVSSYQRNSWGDFLEKLLPAALQMALEEDLEYRQGLPMDCLGYMGVANSDAVDARRTAFVEKVQHLIKKLVDYAPIDAAMDQRAKSFLHDCLPPVLTQSEKQLSVYGFPARWQDGGPRNVDIQITKDTEVRLLHHGVVRLCNEEAGVMLYYTTENSRVYHKEEPKYLEIDPEYTDSIEFLLSSYPNHVSVDTLPCDALEDKISLATLLFEKGILTTKKPLVQV", "text": "FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes demethylation of non-histone proteins (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Note=Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli. SIMILARITY: Belongs to the ROX family. NO66 subfamily."}
{"protein": "MLSPRRFILVVTILGLLGHNLTHVLNSPHRILLDTDVDTDDFIALLYLLKLNKTEFDLVGITLSANSWTNAGHGVNHIYDILYMMGRDDITVGVGGEGGILEDGTILPDVGDYLPIIEQGMTTAGGCRYRQSIPKGRIQKIDSNYGFRKHFLPQGNRRYTPLEQPTAQKVIVDKVSEGPISIFVIGSHTNLALFMMSNPHLKHNIQHIYVMGGSVRCQNPNGFCGNLFTDYTSNPYAEFNIFTDPFAAYQVFRLLWFL", "text": "FUNCTION: May be involved in the degradation of extracellular nucleosides. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast Note=Present in the apoplastic fluid. SIMILARITY: Belongs to the IUNH family."}
{"protein": "MIRGLFVGRFQPVHKGHIKALEFVFSQVDEVIIGIGSAQASHTLKNPFTTGERMEMLIRALEEAGFDKRYYLIPLPDINFNAIWVPYVESMVPRFHVVFTGNSLVAQLFKERGYKVVVQPMFKKDILSATEIRRRMIAGEPWEDLVPKSVVEYIKEIKGVERLRNLATNLESSEKELQAPIRVPEY", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family."}
{"protein": "MSAVVVDAVEHLVRGIVDNPDDVRVDLITSRRGRTVEVHVHPDDLGKVIGRGGRTATALRTLVAGIGGRGIRVDVVDTDQ", "text": "FUNCTION: A probable RNA-binding protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KhpA RNA-binding protein family."}
{"protein": "MKVLGLIVEYNPFHNGHLYHLEESKKISGADFVVCVMSGNFIQRGEPAIVNKWARTKMALSAGADLVIELPLSCAMASAEYFASGAVRILNDIGIVDYICFGSEHGDVKTLDYIAQILVEEPESYKSFLKEELDNGLSYPAARESALKKYTAHSINIPQIISSSNNILGIEYLKALRRIKSSIIPLTIKRINNDYNTENITGSISSASSIRKYISTSNSTSFDDVLAMTMPKTSVDILFEEFSAGRGPVFKEDFYPVVTSLIRKMTPEQIRNFAYVSEGLENRIKSAADTAGTYEELVESICTRRYTKTRVQRILMGILMGVTSKDLDMLSRFDSPQYARILGFNSKGKQLLSQIKKKSSIPLVLKLSDFIKSCDPVLKRKLELEILATDLYVMCYKNPAFRKAGQEFTQNIIIM", "text": "FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac- AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TmcAL family."}
{"protein": "MNWELCDDYPSKAPPETCNKVDGARRCRTSCNNEGYGGANCNLKGKVKVCECTILRVCLPHHKRPPHVPKPPK", "text": "SIMILARITY: Belongs to the DEFL family."}
{"protein": "MPKHEFSVDMTCEGCAEAVSRVLNKLGGVEFNIDLPNKKVCIDSEHSSDTLLATLNKTGKAVSYLGPK", "text": "FUNCTION: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense (By similarity). SIMILARITY: Belongs to the ATX1 family."}
{"protein": "MAVSAVPHPSKQAQASEEGINQEKCINEEYKIWKKNSPFLYDLIITRALEWPCMSLQWYPEQQIFAEHGYTEQKMFLGVRADVGKYLLAVASIQLPYLNQTVPPTTMEGASAGDESSLRVNISNLYSHPESVCSAKLMPQDDSCVATVGNYHNDVLVFDKESFESYSSASESPLKPKYRLTKHTQPCTSVCWNFLSKGTLVSGSQDATLSCWDLNAYNESDSASVLKVHISSHEKQVSDVRFHYKHQDLLASVSYDQYLHVHDIRRPDASTKPARSVHAHSGPIHSVAFNPHNDFILATCSTDKTIALWDLRNLNQRLHTLEGHEDIVTKISFSPHEEPILASTSADRRTLVWDLSRIGEDQPAEEAQDGPPELLFMHGGHTSCTIDMDWCPNYNWTMATAAEDNILQIWTPSRSIWGNEQLEEDATAYLS", "text": "FUNCTION: Has a role in chromatin assembly and chromosome segregation. Involved in the deacetylation of histones. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat HIR1 family."}
{"protein": "MPKSWPIVISSHSFCFLPNSEQERKMKDLNFHAATLSEEESLRELKAFDETKAGVKGIVDTGITKIPRIFIDQPKNLDRISVCRGKSDIKIPVINLNGLSSNSEIRREIVEKIGEASEKYGFFQIVNHGIPQDVMDKMVDGVRKFHEQDDQIKRQYYSRDRFNKNFLYSSNYVLIPGIACNWRDTMECIMNSNQPDPQEFPDVCRDILMKYSNYVRNLGLILFELLSEALGLKPNHLEEMDCAEGLILLGHYYPACPQPELTFGTSKHSDSGFLTILMQDQIGGLQILLENQWIDVPFIPGALVINIADLLQLITNDKFKSVEHRVLANKVGPRISVAVAFGIKTQTQEGVSPRLYGPIKELISEENPPIYKEVTVKDFITIRFAKRFDDSSSLSPFRLNN", "text": "FUNCTION: Catalyzes the C4-hydroxylation of desacetoxyvindoline. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MRDRTHELRQGDNISDDEDEVRVALVVHSGAARLSSPDDEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSVNTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQVTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARKKKVMIAICVSVTVLILAVIIGITITVG", "text": "FUNCTION: Plasma membrane t-SNARE that mediates docking of transport vesicles (By similarity). Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane (By similarity). In neurons, recruited at neurite tips to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) which promotes neurite tip surface expression of the dopamine transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (PubMed:32963038). Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein Cell projection, neuron projection Note=Localizes to neurite tips in neuronal cells. SIMILARITY: Belongs to the syntaxin family."}
{"protein": "MAKIGLFFGSDTGTTRKIAKQIKDMFDDEVMAKPLNVNRADVADFMAYDFLILGTPTLGDGQLPGLSANAASESWEEFLPRIADQDFSGKTIALFGLGDQVTYPLEFVNALFFLHEFFSDRGAKLVGRWPAKGYGFEDSLAVVEGEFLGLALDQDNQAALTPERLKGWLSLIAADFGLVLPA", "text": "FUNCTION: Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase. SIMILARITY: Belongs to the flavodoxin family."}
{"protein": "MFASRAIRMMSMRPMARTMATKAAAPVKVPVQLFGLDGTYATALYTAAAKESDLSKTEGSLAKLRDVFAQQPEVAQIVSNPTLSHEDKQTVVNVLSQAVGGDKTLTNFLTVISDNNRLALIPGIIEKFETLVNASKGLVEATVTSASELDKKTVNRIQAAIAGSSFVGEGELKLNLKVNPDILGGLIVEVAERTVDVSVASKIARLNHVLSEPI", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27373333). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (PubMed:27373333). Part of the complex F(0) domain and the peripheral stalk, which acts as a stator to hold the catalytic alpha/ATP1(3)beta/ATP2(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (PubMed:27373333). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix. SIMILARITY: Belongs to the ATPase delta chain family."}
{"protein": "MRLCLFLCLVLLGPRMATLRRSQKKKIQEVPPAVTTAPPGSRDFVFDLYRALAAAAPAQNIFFSPLSITVSLAMLSLGAQSNTKAQILEGLGIGPGEGSEEELHSASQRLLRELQQPQDSLQLSLGNALFTKPRLPIQEAFLGAMRTLYLADTFPTNFEDPEGAKKKINDYVAKQTKGKIVDLIKSLDGTQVMVMVNYIFFKAKWETSFNLKSTHEQDFYVTPETVVRVPMMKQQDQFYYLLDRNLSCKVVGVPYQGNATAFFILPREGEMEQVENGLKEKTLKKWLRMPMKRRLELYLPKFSIEGSYQLEEVLPKLGIRDIFTSDADLTGISNHSSIRVSEMVHKAVVEVDESGTQAAAATGMVITFKSARLGSQRIVFNRPFLVLIVKNSKHILFLGKVTRP", "text": "FUNCTION: Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and pro-inflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue- and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C- catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary- type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space Note=Localized on the plasma membrane overlying the acrosomal head of spermatozoa of ependymal spermatozoa and ejaculated sperm. Localized at the equatorial segment of acrosome-reacted spermatozoa. Localized in alpha granules in resting platelets and on the external plasma membrane and within the surface-connected cannalicular system in activated platelets (By similarity). SIMILARITY: Belongs to the serpin family."}
{"protein": "MNNPAMTIKGEQAKKQLIAAALAQFGEYGMNATTREIAAQAGQNIAAITYYFGSKEDLYLACAQWIADFIGEQFRPHAEEAERLFAQPQPDRAAIRELILRACRNMIKLLTQDDTVNLSKFISREQLSPTAAYHLVHEQVISPLHSHLTRLIAAWTGCDANDTRMILHTHALIGEILAFRLGKETILLRTGWTAFDEEKTELINQTVTCHIDLILQGLSQRSL", "text": "FUNCTION: Regulates transcription of the cecR-ybhGFSR operon and the rhlE gene, which altogether are involved in the control of sensitivity to cefoperazone and chloramphenicol. Represses the cecR-ybhGFSR operon and activates the rhlE operon. Acts by binding to a palindromic sequence within the intergenic spacer located between these two divergently transcribed operons. FUNCTION: Regulates transcription of the cecR-ybhGFSR operon and the rhlE gene, which altogether are involved in the control of sensitivity to cefoperazone and chloramphenicol. Represses the cecR-ybhGFSR operon and activates the rhlE operon. Acts by binding to a palindromic sequence within the intergenic spacer located between these two divergently transcribed operons. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSTTLGQESKTDWASLDSDEEVQRISDKVNQLNTSENKNEDQKATNLSDRLGPKITENVDAKSEQDKATNTIAEDANTKQSENDESNLIPNKNEVRVKLADLQADPNSPLFSVKSFEELELKPELLKGIYSMKFQKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFALTMLSRVDASVPKPQAICLAPSRELARQIMDVVTEMGKYTEVKTAFGIKDSVPKGAKIDAQIVIGTPGTVMDLMKRRQLDARDIKVFVLDEADNMLDQQGLGDQSMRIKHLLPRNTQIVLFSATFSERVEKYAERFAPNANEIRLKTEELSVEGIKQLYMDCQSEEHKYNVLVELYGLLTIGQSIIFCKKKDTAEEIARRMTADGHTVACLTGNLEGAQRDAIMDSFRVGTSKVLVTTNVIARGIDVSQVNLVVNYDMPLDQAGRPDPQTYLHRIGRTGRFGRVGVSINFVHDKKSWEEMNAIQEYFQRPITRVPTDDYEELEKVVKNALKM", "text": "FUNCTION: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Note=Nuclear pore complex cytoplasmic fibrils. SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily."}
{"protein": "MDLLGLKELDNNKLVSKAKENGVEFSDLFLLSSGYLRDRENASASVSSKNERMVLNEERQNCWTKRNDPKGLTYYQLLKPSEVEILSRPETRRKRMACQVFFLNYYISTIEYHKLRKERLEEFTACTSSLKQSKQKRLWKEHCGRERAFLRKKRTKIQCSHFDLLVKLGQGGYGSVWLAKKRNTHELLAMKMMKKSTLQQLNEVKHILNERDILTNTNSEWLVKLYYAFQDKEKVYLAMEYVPGGDFRTFLTTKGLLHENQTRFYLAEMVAAISAVHKLGYMHRDLKPENFLIDQKGHIKLSDFGLSTAIVTSNQVNRLQHALVSAVNPQRPYLTQKQRRNIYKALLEKNENKVNSVVGSPEYMAPEVVYGKKYDRTVDYWSLGCICYECLVGYPPFSGSTLQETWTNLYYWREMLQRPSKNENGIYDKKARSVSDEAWSFITKCLTEPTSRFQSTIEIQKHPFFKRLHWNGLRKRAVPPFVPRLENQLDTSYFDDFNDEQVLDAYKDVYEKQRKAEQKAKSNGVMNGNQRQFLGFTFKYRPNARKPLVGRHREKRQLRKEKPEKKNNSTKQKDLITVSHNKGTTAIEDLDEDKRSKTKGHKTKSSRVHRLLERKGKDLYEFLL", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MVEKEEAVISEEEAAQYDRQIRLWGLEAQKRLRTSRVLLVGMRGLGAEVAKNLILAGVKALTLLDHEQVSSEDSRAQFLIPSGSLGQNRAEASLNRARNLNPMVSVEADTENINQKSDDFFTQFDVVCLTSCPSDLLVRVNHICHKHNIKFFTGDVYGYHGSMFADLGEHEFVEEKAKVTKAKPLVEDGPEAKKAKIDPTETILVKKKVQFCPLKDALEIDWRSEKAKSALKKTPTDYFLLQVLMKFRTDKGRDPQPSSYQEDSELLLQICSDVLDSLGVSPDLLPKDFASYCFSEMAPVCAVVGGVLGQEIVKALSLRDAPHNNFFFFDGKTSNGIVDCLGSK", "text": "FUNCTION: The heterodimer acts as an E1 ligase for sumo1, sumo2, and sumo3. It mediates ATP-dependent activation of sumo proteins followed by formation of a thioester bond between a sumo protein and a conserved active site cysteine residue on uba2/sae2 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ubiquitin-activating E1 family."}
{"protein": "MKKRLTITLSESVLENLEKMAREMGLSKSAMISVALENYKKGQEK", "text": "FUNCTION: Regulates the plasmid copy number. Binds to the RepAB promoter thus controlling the synthesis of the plasmid replication initiator protein RepB. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family."}
{"protein": "MIDFWLAAGLLLLIALSFLLIPVLRGRRAQREEDRTALNVALYQERVAELQVQQDEGVLNAAQLDTGRAEAARELLADTEGVEKPRESRLGKPLPFLAAFLVPVLGVVLYLHYGASDKVELTREFSQPPVSMADMTQRLERAAAAQPDSAEGLYFLGRAYMAQDRSADAAKVFERTVALAGRQPELLGQWAQAQYFADNKQWSPKVQALTDEALKLDPKEVTSLGLLGIAAFEGQRYQEAIDYWNRLLAQLPPQDNSRVALQGGIDRAAEKLKESGGTVAHKTVMTVRVDLSAEAKAKTLPSDSVVHLRPRRLRPTGTVGGQARYRR", "text": "FUNCTION: Required for the biogenesis of c-type cytochromes. Possible subunit of a heme lyase (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein; Periplasmic side. SIMILARITY: Belongs to the CycH family."}
{"protein": "MGMAMRCVLVLFSVSPVLLLFNFEMLEVALHLASREKELDTAAVTPSASLSFLSRFRIMLGMNHHRSRGRRHKRYSEAPAPAPAPVPAHQARSEAPAPLVHVPRKGMPSTHRSHIAPARSPVHKVKDGGHTKIPRSAIVALGVVGLCLVVLGVVIAAFSVRRSRKFKKVCTKAFKPFRHGSRDQRSPAATRKVSSHPSPDPLTLSSIVQYQQNLPNLKQSSESKSLSIQSTIPMGTELIVSDHAVINNSQSDEVESFHSIPCSDLSAGSITELPQQICDRRAIMNRSEYFLQTHDSPSDSSYQSLSPDCTSRLSPKDQTFTASSHLSLRSKTCPEKSDGENAEINCHDGLEITCISGSMEHQEAPIEERARINFRNPPSQHIFPPSYRTDTSQSKINIAFTMTNSKVESSSKESSRIETSSSMGIPKPAPPPPPQKNPPPNLKGQCYGQPPPPPPLPLQIQVGKDGSPLPRLKPLHWDKVRAAPNRSMVWNDIRSSSFEFEFDEQMIKSLFAYNLQGSMKDEEAMNKTASTTKHVIEHHRLQNTTILLKTLNANTSQVCNSVIQGNGLSVQQLEALVKMKPTKEEEEKLLNYDGDINMLDPAENFVKVLLTIPMAFPRMEVMLYKENFDDEVAHIKMSFAMIEGACTELKSSKLFLRLLEAVLKTGNRMNVGTLRGGASAFKLDALLKLADIRGTDGKTTLLHFVVKEMARSKGLKALEKLNETPSSCHDTPTEREEYSSMGTEFVSELSNELGNVKKVASIDLDTLRNSISNLSCGLAQLRNLVEKDLASDDKNNNFLQCMKSFLNHAENTMQGLKADEAQVLLNVRELTEYYHGEVSKDESNLLQIFIIVKDFLGLLDKVCREMRGTKHNQTLNLVLPLK", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the formin-like family. Class-I subfamily."}
{"protein": "MPKLGMQSIRRRQLIDATLEAINEVGMHDATIAQIARRAGVSTGIISHYFRDKNGLLEATMRDITSQLRDAVLNRLHALPQGSAEQRLQAIVGGNFDETQVSSAAMKAWLAFWASSMHQPMLYRLQQVSSRRLLSNLVSEFRRELPRQQAQEAGYGLAALIDGLWLRAALSGKPLDKPLAHSLTRHFITQHLPTD", "text": "FUNCTION: Repressor involved in the biosynthesis of the osmoprotectant glycine betaine. It represses transcription of the choline transporter BetT and the genes of BetAB involved in the synthesis of glycine betaine (By similarity)."}
{"protein": "MLKFLLKFRKRRRPVVVPRFVRFIVYVVLFTVAVQRVKQERDAHLRRYEERLRKNRARRRQSFP", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HHV-5 US34A protein family."}
{"protein": "MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV", "text": "FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,- dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and eating behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MPFGNTHNKWKLNYSAAEEFPDLSKHNNHMAKALTLDIYKKLRDKETPSGFTLDDVIQTGVDNPGHPFIMTVGCVAGDEECYEVFKDLFDPVIEDRHGGYKPTDKHKTDLNQDNLKGGDDLDPNYVLSSRVRTGRSIKGIALPPHCSRGERRLVEKLCIEGLATLTGEFQGKYYPLSTMSDAEQQQLIDDHFLFDKPISPLLLASGMARDWPDGRGIWHNNDKSFLVWVNEEDHLRVISMQKGGNMKEVFRRFCVGLKKIEEIFVKAGRGFMWNEHLGYVLTCPSNLGTGLRGGVHVKIPHLCKHEKFSEVLKRTRLQKRGTGGVDTEAVGSIYDISNADRLGFSEVEQVQMVVDGVKLMVEMEKRLENGKSIDDLIPAQK", "text": "FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP:guanido phosphotransferase family."}
{"protein": "MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMEESNPPTGASGRAGAGASGRAGAGASGRAGAGAGAVASAGSGDGAVASAGNGANPGADAKRSTSTPATTTTTTTTNDAEASTSTSSENPNHNNAKTNPKGKEVQEPNKANTETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLNNSSNIASINKFVVLISATLVLSFAIFI", "text": "FUNCTION: May play a role in the merozoite attachment to the erythrocyte. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Note=During host erythrocyte invasion by merozoites, carried into invaded erythrocytes where it is rapidly degraded."}
{"protein": "MPSRGCSCWLLSLALLCSLAAAKEQYHEFVIRETTVKRLCKSHNIMTVNGQFPGPTLEINEGDSLIINLINRGRYNMTLHWHGVRQMRTGWSDGPEYVTQCPVRPGQSYRYRFTVAAQEGTLWWHAHSSWLRATVYGALLIRPRDGTSYPFDVQPTRELAPILLGEWWDMNPVDVVRAATRTGAAPNISDALTVNAQPGDLYSCSSHDTAVFPVTSGETNLLRFINAALNTELFVSLAGHNMTVVAADASYTKPYTTSLLLLAPGQTTDVLVTFDQPPGRYYLAARAYASAQGVPFDNTTTTAIFDYGAANNASSAAIAMPTLPAYNDTTAATAFTTNLRGLRKAELPSRVDESLFFTVGVGLFNCTNATAQQCGGPNGTRFAASINNVSFVLPSSTSILQAHHHGAPGGVFTADFPANPPVQFDYTAQNVSRALWQPVAGTKVYKLKYGSAVQVVLQGTNIFAGENHPIHLHGYDFYILAEGLGNFDAGADTGKFNVEDPPMRNTVGVPVNGWAVIRFVADNPGVWLMHCHLDVHITWGLAMAFLVDDGVGELQSLEAPPPDLPLC", "text": "FUNCTION: Lignin degradation and detoxification of lignin-derived products. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MELDEVIITRAIFDEYSKTFLDYTEVDVALIGGGPANLVAARYLAEAGAKVAIYEQKLSLGGGMWAGGMMFPRIVVQEEACRILDDFGIRYKEYQPGYYVANSVESVGKLISGATSAGAEVFNLVSFEDVMIRENDRVTGIVVNWGPVTVQRLHVDPLMIRTKLVIDGTGHEAVVCNTILRKIPNAKIGNLGKLGEKPMWSEVGEQLVVDATKEIYPGLIVAGMAANAATCSPRMGPVFGGMLLSGEKAAKLALEKLKEL", "text": "FUNCTION: Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. SIMILARITY: Belongs to the THI4 family."}
{"protein": "MTFLQVTIKMVAREASGHSYLVACWQPILILMLGTVLSGSATGCPSRCECSAQERSVVCHRRKLITLPEGIPIDTRLLDLSKNRLKAINPEEFLNYPQLEDLQLNENIISVIEPGAFSNLLGLRTLGLRNNNLKLIQLGVFTGLSNLTRLDISENKIVILLDYMFQELYNLKELEVGDNDLVFISHRAFHGLSSLEQLTMERCNLTSVPTEAFSHLHNLLTLKLRHLNVNVIRDFSFRRLYRLKILEIANWPLLESLTAKSLHGLNITTLSITNCNLTAVPYVAIQHLVYLRFFNLSFNPIEVVEGNKMHNLLRLQAFHLVGGRLVSIEPYSFKGLNYLRVLNVSSNSLSTLEESAFHSVGNLETLALHDNPLACDCRLLWVFRRRWRLNFNRQQPSCETPEFLQGKEFKDFPDVLPPNYFTCQKSKIRDHKAIHRFVDEGTTVQFPCQADGDPTPMIMWQSPKKQFITTKSIGRLSVSLDGTLEVRYAQIQDNGTYTCFAVNAGGNDTRLAHLHVHSYSPNWPHQPNKTFAFILNQPSDNSANGTGAMDPFPFDMKTLIIATTMGFISFLGVVLFCLVLLFLWSRGKGNAKPNIEIEYVPRKVDGENSPNEGSHKISMKMI", "text": "FUNCTION: May play a role in regulating axonal regeneration and plasticity in the adult central nervous system. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MTILAWCIAWVLDFIIGDPQHWPHPVRWIGRLITFVQRIVRRYCPGDKALRIGGGVMWVVVVGVTWGVAWGVLALAQRIHPWFGWSVEVWMIFTTLAGRSLARAAQEVERPLRENDLAESRIKLSWIVGRDTSQLQPAQIYRAVVETVAENTVDGIIAPLFFLFLGGAPLAMAYKAVNTLDSMVGYKHEKYRAIGMVSARMDDVANYLPARLSWLLLGIAAGLCRLSGWRALRIGWRDRYNHSSPNCAWSEACVAGALGIQLGGPNNYFGERVDKPWIGDAQRGISVDDISRTIRLMWVASTLALALFIAARCGLSGVA", "text": "FUNCTION: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. However, the true cosubstrate could be (R)-1-amino-2-propanol O-2-phosphate, leading to cobinamide phosphate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CobD/CbiB family."}
{"protein": "MDPNCSCATRDSCACASSCKCKECKCTSCKKSCCSCCPAGCTKCAQGCICKGALDKCSCCA", "text": "FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family."}
{"protein": "MSDKFQDRTMAFAGICQAAYLVQKVARDGSCDEAALRESLSSILVTNPSQPLEVFNNTHLAIRDGYRALVEQLGADGSQKNAELTRYVVSLIALERKLAKRKDILNMLGERISQIGRQQQHFDLLDEQILANMASIYSDLISPIGPRIQVAGTPLFLQQPLVQHKVRALLLAGIRACVLWRQLGGSRTQIIFARKKMVELAKRY", "text": "SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the HflD family."}
{"protein": "MELKILEKSDDEMKMEIAGESHTLLNMLKIILLEDERVHTASYDMKHVTISEPVLFIKTENADPIDVVKAAVAKLITECEEFVTVFNKAVE", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family."}
{"protein": "MVLTIRAILWVTLITIISLEFIIGILGNVFIALVNIIDWVKRGKISAVDKTYMALAISRTAFLLSLITGFLVSLLDPALLGMRTMVRLLTISWMVTNHFSVWFATCLSIFYFLKIANFSNSIFLVLKWEAKKVVSVTLVVSVIILIMNIIVINKFTDRLQVNTLQNCSTSNTLKDYGLFLFISTGFTLTPFAVSLTMFLLLIFSLWRHLKNMCHSATGSRDVSTVAHIKGLQTVVTFLLLYTAFVMSLLSESLNINIQHTNLLSHFLRSIGVAFPTGHSCVLILGNSKLRQASLSVILWLRYKYKHIENWGP", "text": "FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor T2R family."}
{"protein": "MAALMRVKDSSRCLLLLAAVLMVESSQLGSSRAKLNSIKSSLGGETPAQSANRSAGMNQGLAFGGSKKGKSLGQAYPCSSDKECEVGRYCHSPHQGSSACMLCRRKKKRCHRDGMCCPGTRCNNGICIPVTESILTPHIPALDGTRHRDRNHGHYSNHDLGWQNLGRPHSKMPHIKGHEGDPCLRSSDCIDGFCCARHFWTKICKPVLHQGEVCTKQRKKGSHGLEIFQRCDCAKGLSCKVWKDATYSSKARLHVCQKI", "text": "FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the dickkopf family."}
{"protein": "MDSQKKLTFPLAVGLFIFMLCIIISCLFLLHVEPHIPLFLSVVMLSAAALWFGFPWKSIEKGIVDGIKNGVQPIIVLALIGILIGAWMYSGAIPTMTVYALSFIEPSHLLLTALFSCMIISTLVGSSLTTVSTIGVALIGVASAAGVPLEWTAGAVICGACFGDKMSPMSDTTNFAAGIGEIPIFEHIRHMMGTTIPALLITVVLFYFLGSSVSADAASTDNIQQVITGIKDAANVTPWALLSPLLVVLLAMKRVSVIPVLTAGIISSGILTAIFVPYSSLQAFMTALQNGTTFETDNEAAAKIINRGGLQSMMGSVSLIMIAFALGGLMEKIGLISALLEGVMKGIRSKGRLVAATVCSSIGVNLATGEQYLSILIPGQSFKSLYDKRNIQRKFLTRSLEDGGTLINPLIPWGVSGAFMASALGVPVIDYIPFTFFLYISPMISILIGFVKK", "text": "FUNCTION: Is a secondary, electrogenic Na(+)/H(+) antiporter that catalyzes Na(+) uptake and proton efflux. Makes modest contributions to pH homeostasis in the alkaline range of pH but is not contributor to Na(+) resistance. Appears to have a repressive effect on growth and on alkaline phosphatases production in the presence of sodium, by affecting the transcription of the phoP/phoR two-component regulatory system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter family."}
{"protein": "MSVFDLPRLHFAGTATTRLPTGPRNGLVDLSTHSVVMDGERFPASRPAAEYHAYLDRVGGKGTAFAGNGYFAIDAGITAVERAAGEVDTGDLLVGRAVDVWGHYNEYLATTFNRARIFDVDPSSSWTSTVMIGQFGFGRLGRSHDVGYVFTGGVHGMQPPRWHEDGRVLHQFTVPAGEDMTWFGSAADSPAAARLRELVESGEADGLVVQLALSDAGPAPMPHAQQWRLRGTIAPWHAGEPRTCPAGRLLTPHNLTADLRGDHVSLNLISFRPPTGISGLELRTADTDRFIARVPADDPHGVVTVPAAEGGDEALCVVGTTAAGERIVVSREREVTVHVDDASVFLEHPRGPGDSDQDAEIAVRTYVRGEPAAATIHIGQYFNPRAFPLDEHATAASATPEDLDVVALCVDGTRWSRHCVISTDENGDGRFLLRGARPGATRLLLSAEGATPFDGLTAAAAYDNDDSLGLWSGLASVAVRVLPDHWWMDDIPRDKVTFDLLYREVFAFYELLYSFMGEEVFSLADRFRVETHPRLIWQMCDPRNRAKTYYMPPTRDLTGPQARLLLAYLRAQNSDVVVPVIEPSHTRSGTPISTRTDLVRALRHGVAIELAVMLQYLYAAFSIPTHGAGQELVSRGDWTPEQLRLMCGDGGETTDGGVRGSLLGVAREEMIHFLVVNNVLMAVGEPFHVPDLDFGTINDTLMVPLDFSLEALGLGSVQRFIQIEQPEGLTGAVRLGDLPVPVREAEDFHYASLSELYGDIREGLQRVPGLFLVERGRGGGEHHLFLRESVNAVHPDYQLEVDDLSSALFAIDFVTEQGEGHVLTDEDTGEESHYDTFVRVADLLMKERLTAADTRRAQWSPAYPVARNPTVHGGGQSKELVTSPVARELMVLFNKSYFMMLQLMVQHFGGSPDASLRRSKLMNAAIDVMTGVMRPLAELLVTVPSGRHGRTAGPSFELDEKPAFIPRADVARRAISLRFRHLAESARTCALVPDKVVRNLDFLADQFATEGPR", "text": "FUNCTION: Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the hydrogen peroxide-dependent dimerization of two L-tryptophan-derived molecules (imine form of indole 3-pyruvate (IPA)), to form dichlorochromopyrrolic acid (CPA), the precursor for the six-ring bisindolopyrrolocarbazole scaffold of the rebeccamycin. The hydrogen peroxide is provided together with iminoindolpropanoate by RebO. Due to the instability of indole 3- pyruvate (IPA), which is hydrolyzed in solution and exits in equilibrium with the predominant ketone form of IPA, the concerted functioning of the RebO/RebD system appears to prevent the buildup of significant amounts of IPA and its imine in solution, effectively shepherding the imine further down the biosynthetic chain. SIMILARITY: Belongs to the RebD family."}
{"protein": "MTQGPGGRAAPEPEAPTTFCALLPRMPQWKFAAPGSFLGRGPAAARVAGAAEAQPEPGVPALAAVLGACEPRCAAPCPLPALGRCRGSGSRGARGTPDVADEWVRKGGFIHKPAHGWLHPDARVLGPGVSYIVRYMGCIEVLRSMRSLDFNTRTQVTREAINRLHEAVPGVRGSWKKKAPNKALASILGKSNLRFAGMSISVNISVDGLNLSVPATRQIIANHHMQSISFASGGDTDMTDYVAYVAKDPINQRACHILECCEGLAQSVISTVGQAFELRFKQYLHSPPKAVVPPERLTGLEESAWGDGEVTADHDYYNSIPGKEPPLGGLVDSRLAVTQPCALTTLGGLGQGLSPAWRDVRGLPWDMGPSGAVPPGDGYVQADARGPHDYEEHLYVNTQGLDALELEDTSETPLQPEDSPKKDLFDMRPFEDALKLHECSVAAGITAASLPLEDQWPSPPTRRAPIAPTEEQLRQEPWYHGRMSRRAAEKLLRADGDFLVRDSITNPGQYVLTGMHAGQPKHLLLVDPEGVVRTKDVLFESISHLIDYHLKNGLPIVAAESELHLRGVVSREP", "text": "FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons (By similarity)."}
{"protein": "MGSASSKTRKDKAKSSTIAACPTDTAAAKACPTRLDDGLAQVAMFAGLRQVTMGVLRIDYDYQTNLGDILDPRSFDFRLVSATVEGLTFKRAQEGEPLPCYVMSNLDGAVKKLIDAGADFIVGDCGFLVYWQVYVRDFAQQYAGGRACPVMLSSLVLSLPLLATIPVGGKIGILTASKGSLMKMQKKLASVIELQKEEARTRAVPAAVQPSGIEINFSDPRFKVVGLDTVNSFKTALADDSGVDDRRSIAIEIAKYCKQVACEDPAICAWLIECTEAGGFSWAIKLGTGLPVWDPVTIGRFLSLGFTSSLPSVALTLGETGQVALDPNETDVSKGRPTKAEHRFGPEFEEMLQ", "text": "FUNCTION: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle. FUNCTION: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle. SIMILARITY: Belongs to the aspartate/glutamate racemases family. ALMA1 subfamily."}
{"protein": "MADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQKEGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENINNDEDPEGSVDPEGQGS", "text": "FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
{"protein": "MNAQLTMEAIGELHGVSHEPVPAPADLLGGSPHARSSVAHRGSHLPPAHPRSMGMASLLDGGSGGGDYHHHHRAPEHSLAGPLHPTMTMACETPPGMSMPTTYTTLTPLQPLPPISTVSDKFPHHHHHHHHHHHPHHHQRLAGNVSGSFTLMRDERGLASMNNLYTPYHKDVAGMGQSLSPLSSSGLGSIHNSQQGLPHYAHPGAAMPTDKMLTPNGFEAHHPAMLGRHGEQHLTPTSAGMVPINGLPPHHPHAHLNAQGHGQLLGTAREPNPSVTGAQVSNGSNSGQMEEINTKEVAQRITTELKRYSIPQAIFAQRVLCRSQGTLSDLLRNPKPWSKLKSGRETFRRMWKWLQEPEFQRMSALRLAACKRKEQEHGKDRGNTPKKPRLVFTDVQRRTLHAIFKENKRPSKELQITISQQLGLELSTVSNFFMNARRRSLDKWQDEGSSNSGNSSSSSSTCTKA", "text": "FUNCTION: Transcriptional activator. Binds the consensus sequence 5'- DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR. Important for liver genes transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CUT homeobox family."}
{"protein": "MPCHNQQLNNNSESPEHAAKHVRFAQSSAAAAETCQNDAEQPEYQTTSEIHQQIGPQLKLLPLNDQIRELQTIIRDKTTSRGDFVFCADRLIRLVVEEGLNQLPYSECTVTTPTGHKYEGVKFEKGNCGVSIMRSGEAMEQGLRDCCRSIRIGKILIQSDEETQKAKVYYAKFPPDISRRKVLLMYPILSTGNTVIEAVRVLTEHGLQAKHIILLSLFSTPHGARSIVQEFPDITILTTEVHAVAPTHFGQRYFGTD", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the UPRTase family."}
{"protein": "MSSCVVTTSCFYTISDSSIRLKSPKLLNLSNQQRRRSLRSRGGLKVEAYYGLKTPPYPLDALEPYMSRRTLEVHWGKHHRGYVDNLNKQLGKDDRLYGYTMEELIKATYNNGNPLPEFNNAAQVYNHDFFWESMQPGGGDTPQKGVLEQIDKDFGSFTNFREKFTNAALTQFGSGWVWLVLKREERRLEVVKTSNAINPLVWDDIPIICVDVWEHSYYLDYKNDRAKYINTFLNHLVSWNAAMSRMARAEAFVNLGEPNIPIA", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Plays important role in chloroplast development, particularly in the maintenance of thylakoids membranes. Seems to act as a heterodimer with FSD2. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MAIPETQKGVIFYEHGGELQYKDIPVPKPKPNELLINVKYSGVCHTDLHAWQGDWPLDTKLPLVGGHEGAGIVVAMGENVTGWEIGDYAGIKWLNGSCMSCEECELSNEPNCPKADLSGYTHDGSFQQYATADAVQAARIPKNVDLAEVAPILCAGVTVYKALKSAHIKAGDWVAISGACGGLGSLAIQYAKAMGYRVLGIDAGDEKAKLFKELGGEYFIDFTKTKDMVAEVIEATNGVAHAVINVSVSEAAISTSVLYTRSNGTVVLVGLPRDAQCKSDVFNQVVKSISIVGSYVGNRADTREALDFFSRGLVKAPIKILGLSELASVYDKMVKGQIVGRIVVDTSK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MSFTSLPLTEINHKLPARNIIESQWITLQLTLFAQEQQAKRVSHAIVSSAYRKAEKIIRDAYRYQREQKVEQQQELACLRKNTLEKMEVEWLEQHVKHLQDDENQFRSLVDHAAHHIKNSIEQVLLAWFDQQSVDSVMCHRLARQATAMAEEGALYLRIHPEKEALMRETFGKRFTLIIEPGFSPDQAELSSTRYAVEFSLSRHFNALLKWLRNGEDKRGSDEY", "text": "FUNCTION: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:24722491). Acts as a regulator of the SsaN/SctN2 ATPase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Detected in both the soluble and membrane fractions. SIMILARITY: Belongs to the SctL stator family."}
{"protein": "MQNNNRQELQTLRDLIRYAVSRLNAARVALGHGSDNAWDEAVYLVLHGLHLPPDTLDPFLDARVLPSERSRVLDLIDRRVTERLPAAYLTGEAWLRGHRFHVDRRVIVPRSPIAELLDEGLAPWVRDPLQVERALDMCTGSGCLAILAALAFPVAQVDAVDVSSDALEVAARNVAEYGLQDRLTLRQGNLFEALPAAAYDVIVCNPPYVNQASMGALPQEYRHEPALALAGGADGMDLVRRILAAAPGYLSADGVLVLEIGHERDHFEAAFPDLQPVWLDTAESSDQILLLTREQLNT", "text": "FUNCTION: Methylates large ribosomal subunit protein uL3 on a specific glutamine residue. SIMILARITY: Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily."}
{"protein": "MADKEAAFDDAVEERVINEEHKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQKEGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGSVDPEGQGS", "text": "FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere Note=Localizes to chromatin as part of the PRC2 complex. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
{"protein": "MVGHAATDVPPTMAVKIFSAGVAACVADIITFPLDTAKVRLQIQGECLTSSAFRYKGVLGTIITLAKTEGPVKLYSGLPAGLQRQISFASLRIGLYDTVQEFFTTGKEASLGSKISAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGPKPRYTGTYNAYRIIATTEGLTGLWKGTTPNLTRNVIINCTELVTYDLMKEALVKNKLLADDVPCHFVSAVVAGFCTTVLSSPVDVVKTRFVNSSPGQYTSVPNCAMMMLTREGPSAFFKGFVPSFLRLGSWNIIMFVCFEQLKRELMKSRQAMDCAT", "text": "FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance (By similarity). Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane (PubMed:26038550). However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MESMFEDDISILTQEALGPSEVWLDGPGDPSLGGDMCSASHFALITAYGDIKERLGGLERENATLRRRLKVYEIKYPLITDFGEEHGFPLYELKDGSLLEVEKVSLQQRLNQFQHELQKSKEQEEQLGEMIQAYEKLCVEKSDLETELGEMRALVETHLRQICGLEKQLQQQQGLRDAAFSSLSPPAVPASACPDLDLHYLALRGGPALGHAGWPGPTSVSVSELERRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAQDLASNQSECDMAWVKRVGDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQARNAGQRHSPLSQRHSPAPACPSPSPPARPPPCAPCQSPAAQRRSPVPPCPSPQQRRSPASPSCPSPVPQRRSPVPPSCQSPSPQRRSPVPPSCPAPQPRPPPPPGERTLAERVYAKPPSHHAKAGFQGRRSYSELAEGAAYAGASPAWLQAEAATLPKPRAYGGELYGRPLSPRRAFEGIRLRFEKQPSEEEEWAMPASPPSPEAGTIRCASFCAGFPIPESPAATAYAHAEHAQSWPSINLLMETVGSDIRSCPLCQLGFPVGYPDDALIKHIDSHLENSKI", "text": "FUNCTION: Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Essential for the efficient induction of IRF-dependent transcription following infection with Sendai virus."}
{"protein": "MKFNVANPTTGCQKKLEIDDDQKLRAFYDKRISQEVSGDALGEEFKGYVFKIKGGCDKQGFPMKQGVLTPGRVRLLLHRGTPCFRGHGRRTGERRRKSVRGCIVSPDLSVLNLVIVKKGENDLPGLTDTEKPRMRGPKRASKIRKLFNLKKEDDVRTYVNTYRRKFTNKKGKEVSKAPKIQRLVTPLTLQRKRARIADKKKKIAKANSDAADYQKLLASRLKEQRDRRSESLAKKRSRLSSAAAKPSVTA", "text": "FUNCTION: Component of the 40S small ribosomal subunit (By similarity). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family."}
{"protein": "MSRNLDSPVQTQMAVAVFKTPLTGASKMEGKQHHKHQHLQRQSSGRRVFVQTETGCVLGMELDRSDNVHTVKRRLQIALNFPTEESSLTYGDMVLTNDLSAVRNDSPLLLKRNFMHRSSSTPCLSPTGRDLQQKDRSGPIEILGHSDCFSIVKHMVKDIVKAMKMGVEPLPVHSGLGGAYYFRNKRGESVAIVKPTDEEPFAPNNPKGFVGKALGQPGLKSSVRVGETGFREVAAYLLDYGRFANVPPTALVKITHSVFNVNDGVKGNKPREKKLVSKIASFQKFVAHDFDASDHGTSSFPVTSVHRIGILDIRIFNTDRHGGNLLVKKLDGVGMFGQVELIPIDHGLCLPETLEDPYFEWIHWPQASLPFSDEEVDYIQSLDPVKDCDMLRRELPMIREACLRVLVLCTIFLKEASAYGLCLAEIGEMMTREFRPGEEEPSELEVVCIEAKRSVTERDVFSPRSDVVGEAEFQFDLDCDDLESVYSSKIQLTDDYFTKNPFSNGRSSLGKLEESIKEEEEDEEEEEDKTENTVPMIIMKDSFFSSAAFHDKAPSLSKLSTSMKNTHLSDTTRKNPKPLTRGKSENTSSGHKSANEQLPVSASFVKVADMKEDEWVLFLERFQELLGPAFAKRKTATLSKRQRLGTSCQF", "text": "FUNCTION: The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5- bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3) (By similarity). Undergoes autophosphorylation and phosphorylates serine/threonine residues of protein substrates (PubMed:17880284). SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K subfamily."}
{"protein": "AKAGVNKPELLP", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid."}
{"protein": "MDFPSIKIKDFEGPFDLLLHLIKKNQMDIYNVEISKITNQYLKYIDEMKFMDLEITSEFIVVAATLIEIKSKHLLPKIKKDEEEDEEDQEKNLIEKLILYKKIKKAAEFFKDRYVNSGELYTKKPEIIEEINLTNNNEDIFKNLTLLELYNMYNNLLEIYNNKQNKANVIQKRIYVDKYKIEDKLKYLLGLIENNEVSKFSEIIDKCECKLECIVSFLALLEMVKLKKVRVYQSDSFDNILIERRQDDREE", "text": "FUNCTION: Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with two foci at the outer edges of the nucleoid region in young cells, and at four foci within both cell halves in older cells. SIMILARITY: Belongs to the ScpA family."}
{"protein": "MNVDFIAGINNLGEKIYTCEPFKTSFQNPFIVALIITAVVLVVFFAICNPPVDKKRKTKTAIYVYICIVALLFLHYYVLNHQLNDIYNKSNMDVIVSSIHDKYKGGDEIIPPISPPSVSNELEEDQPKKIAAGSKPADSKPADSKPASSADSKPLVPLQEVIMPSQYNN", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein Virion. SIMILARITY: Belongs to the asfivirus B169L family."}
{"protein": "MSHVVRPILIILASVAIYTKYYLSFQNGFIDLLSTMGSQGSLAGLQDGLRSHYTGLDPLDKFLKACNVFFWPIFHGTSPALSLYAIAFAGSMIPMWLILLMHTCVKSSIVEIVMINALTGLLVQGIGPGVMMCVLLAMRSTSMEEFAVTSIPAVSILGPNDLPLSLVVCYILPLALSSLPAPASISVPSKQLFIASWQGWPLYIALAVGIAHSLRYGYRRSRPQQLFRHAYAFALACSIISHVGLLLISFLSIYPKSPFLSLHSADLHPQSLLVPRLPWQEVKITSLESGVLRFLHWDYSISSTGALLWCYDVYWEDRMRGKGWIAFFSLSSQLATMSLAFGPCSVALALYWTALSKNLMKNEHVRKR", "text": "FUNCTION: Part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ (PubMed:26213965). Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase PC-15 which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase penD (Probable). A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase PC-16 and the P.simplicissimum ptmI-ortholog not yet identified in P.crustosum, leads to the production of the prenylated form of penijanthine (Probable). The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase PC-22 (Probable). A series of oxidation steps involving 4 cytochrome P450 monooxygenases (PC-21, PC-05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14) are required for the transformation of PC-M4 to penitrems A and E. Synthesis of these final products is proposed to proceed via penitrems D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC- 14, PC-23) (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family."}
{"protein": "MKRTYQPSRVKRNRKFGFRARMKTKGGRLILSRRRAKGRMKLTVSDEKKKY", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
{"protein": "ACCSTSFCGFPICSSVGTCGSSCGQPTCSQTSCCQPTSIQTSCCQPISIQTSCCQPTCLQTSGCETGCGIGGSIGYDQVGSSGAVSSRTRWCRPDCRVEGTSLPPCCVVSCTSPSCCQLYYAQASCCRPSYCGQSCCRPACCCQPTCIEPVCEPTC", "text": "FUNCTION: The keratin products of mammalian epidermal derivatives such as wool and hair consist of microfibrils embedded in a rigid matrix of other proteins. The matrix proteins include the high-sulfur and high- tyrosine keratins, having molecular weights of 6-20 kDa, whereas the microfibrils contain the larger, low-sulfur keratins (40-56 kDa)."}
{"protein": "MQTLNRRNFPGRQHPDRVIQFGEGNFLRAFVDWQLDLLNEHTDLDAGIVIVRPIDSDFPPALDTQDGLYTTIIRGLNEQGEAVREPRLIRSVNREINVYRQFDEYLALAHDPNIRFVFSNTTEAGISYHADDRLSDAPPVSFPAKLTRLLYERFCHFDGAADKGWVLLPCELIDYNGVALKELVLRYAAQWELTSTFTAWLNDHNTFCSTLVDRIVTGYPRAEVEALQQEMGYQDTFWDTAEHFYLFVIQGPLWLAEELRLNKLDLNVRIVDDIKPYKERKVAILNGAHTALVPVAFLAGLDTVGESMNDALIGKFVEKTIAEEIVPVLDLPHDELTSFAQAVLSRFRNPFIQHQLLSISLNGMTKFRTRILPQLLTYRERHGELPARLTFALAALIAFYRGERSGEGDALQAYPLQDDAHWLERYSTLWAGVKENTVSLAELVNVVLRDADHWEQDLTQVPGLAAQVTEQLQTIVERGMRAAVEGYC", "text": "SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB subfamily."}
{"protein": "MFRGATLVNLDSKGRLSVPTRYRDQLIENASGQMVCTIDINHPCLLLYTLPEWEIIEQKLSRLSSMNPQERRVQRLLLGHASECQMDNSGRLLIAPVLRQHAGLTKEVMLVGQFNKFELWDETTWYQQVKEDIDAEQSDSGVLSDRLQDLSL", "text": "FUNCTION: Negatively regulates its own expression and that of the subsequent genes in the proximal part of the division and cell wall (dcw) gene cluster. Acts by binding directly to DNA. May also regulate the expression of genes outside the dcw cluster. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the MraZ family."}
{"protein": "MEEEVPGFYGESGKSVQATLSSLKMLDVGKWPIFSLCSEEELQLIRQACVFGSAGNEVLYTTVNDEIFVLGTNCSGCLGVGDIQSTIEPRRLDSLTGKKIASLSYGSGPHIVLATTDGEVFTWGHNAYSQLGNGTTNHGLVPCHISTNLSNKQVIEVACGSYHSLVLTSDGEVFAWGYNNSGQVGSGSTANQPIPRRVTGCLQNKVVMNIACGQMCSMAVVDTGEVYVWGYNGNGQLGLGSSGNQPTPCRVAALQGIRVQRVACGYAHTLVLTDEGQIYAWGANSYGQLGTGNKSNQSYPTPVVVEKDRIIEIAACHSAHTSAAKTQGGHVYMWGQCRGQSVILPHHTHFCCTDDVFACFATPAVTWRLLSVEPDDHLTVAESLKREFDNPDTADLKFLVDGKYIYAHKVLLKIRCEHFRSSLEDSEDDIVEMSEFSYPVFRAFLEYLYTDNISLSPEEAVGLLDLATFYSETRLKKLCQQTIKQGICEENAIALLSAAVKYDAQDLEEFCFRFCINHLTVVTQTSGFAEMDHDLLKNFISKASRVGAFKN", "text": "SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome Note=Mainly found in the acrosomal cap region."}
{"protein": "MERRTLLVVLLVCSCVVAAAAEASPSRWPSPGRPRPFPGRPNPIFRPRPCICVRQPCPCDTYGGNRW", "text": "FUNCTION: Antimicrobial peptide that has a large activity spectrum with activity against Gram-positive, Gram-negative bacteria, as well as against fungi. Shows activity at micromolar concentrations. Displays minimal inhibitory concentration (MIC) values lower than minimal bactericidal concentrations (MBC). May have a dual mode of action depending on the peptide concentrations. At MIC concentrations, the peptide penetrates into the cytoplasm of target cells (tested on the Gram-negative E.Coli). The two inner membrane proteins YgdD and SbmA may be required for this uptake. At concentrations higher than MIC, arasin may act by disrupting membranes. Does not show hemolytic activity."}
{"protein": "MQSQIVCHGCRNILLYPRGAPSVCCAVCHAVSSTAPSPGMDIAHLICGGCRTLLMYTRNATSVRCSCCDTVNLVRPVSSIAHLNCGQCQTVLMYPYGAPSVKCAICNFITNTGMNTMRHLPPNGTSYTAPSTSAPTTQSQNVTVVVENPMTVDAKGKLVSNVVVGVTTGGKK", "text": "FUNCTION: Putative zinc finger that may be involved in programmed cell death and defense response. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPGNNHNDRPVALIMSRLSRDPRDCIHHTVDTRGMTPGKIIHQVIPPHPTQMRHTNRPSPPVILNLQILSEGGHVCARDVDTADPVPRAGPERTIQWGTDRDATEELASPAPEEIYEDNDSW", "text": "FUNCTION: Plays an essential role for the viral pathogenicity. SIMILARITY: Belongs to the novirhabdovirus NV protein family."}
{"protein": "MLTVLVDYDSGNLHSAEKAFQRMATETGAGQVLVSDRPEDVARADRIVLPGDGAFPACRRALGSYGGLSEAIEEAVTRRARPFLGICIGMQMMATRGLEHEETPGFGWIAGEVVRIAPSDPHLKVPHMGWNDLTVDHPHPVLTGIETGDHAYFVHSYHFQVAHDAERLAHADYGADITAIVGRDTMVGTQFHPEKSQKTGLRLIANFLTWKP", "text": "FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MARCRHHSGYVADDEASHSMCSARVQLPKKPLVPEMGPASKLGHVPHPPSTCGSSALQNQRRNKRHPQPFSHFLDFLTESHVLDSLETVVEKATERMAAMKTEAGVPLVEVQDPVEVPSGGRRAHARPSLSTVHRHRVRPTLCTGHPNNYPSSSSSMSDSHSSLMAGWLGSHSRDSDLGAQGLGSLPPVKDRLLLEKNLKRLLQLERKGKGLSQSCSKRDSLLWDLLGSQTSFQWTQEQPLSWFSELLGSSSGVPEASEPRPGEQEPICKREFNKEIKSLLSQLESLDLPGYCPLREPHRTLNFLADHRLFPALQSVVNQAVDKLRGARCRDGRPLFPTSLEPPSELQVQRNLPPLGSEPAKPTNSGQPHPTVSSPKTPQRKHKDRGGSPSMSSAQVATRFKLKVTPMEKPDIPSPSLHSREKEPDSDPKLQNPPVSLSSRQRAQPWRGLHLTLPAPGIVVEVACGQGHLRVVTPPLACPYPHSSCYLLPELSPVTSSSPSSLCPEVTSSKVGPDMSLQEKGSLTHHS", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome."}
{"protein": "MNPTRYARICEMLARRQPDLTVCMEQVHKPHNVSAIIRTADAVGVHEVHAVWPGSRMRTMASAAAGSNSWVQVKTHRTIGDAVAHLKGQGMQILATHLSDNAVDFREIDYTRPTCILMGQEKTGITQEALALADQDIIIPMIGMVQSLNVSVASALILYEAQRQRQNAGMYLRENSMLPEAEQQRLLFEGGYPVLAKVAKRKGLPYPHVNQQGEIEADADWWATMQAAG", "text": "FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type II methylase, which methylates only a subset of tRNA species. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family."}
{"protein": "MNFKYSILFICFVKVLDNCYAADDLTTLRNGTLDRGITPDCTFNEKDIELHVYSRDKRNGIILKKEILKNYDLFQKSQISHQIAILIHGFLSTGNNENFDAMAKALIEIDNFLVISVDWKKGACNAFASTNDVLGYSQAVGNTRHVGKYVADFTKLLVEQYKVPMSNIRLIGHSLGAHTSGFAGKEVQRLKLGKYKEIIGLDPAGPSFLTNKCPNRLCETDAEYVQAIHTSAILGVYYNVGSVDFYVNYGKSQPGCSEPSCSHTKAVKYLTECIKRECCLIGTPWKSYFSTPKPISQCKRDTCVCVGLNAQSYPAKGSFYVPVDKDAPYCHNEGIKL", "text": "FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (By similarity). May act as an allergen and induce hemolytic activity (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MRLPGIPDEEFIRVEKIPMTKEEIRVLALSKARLFDGAKFIDIGSGTGSVTVEAGLVVGEKGKVWAIEKDKDAVELTKKNVEKFKLNNVVIIEGEAPEALDHVDSEVDAIFIGGTERLEEILLSSDKKLKNGGRIVIDAILLETVNKALSTLNQMGYKTDVIEVIIAKGMKTSKGYAMISRNPIFIVYGEKP", "text": "FUNCTION: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7. SIMILARITY: Belongs to the methyltransferase superfamily. Archaeal-type CbiT family."}
{"protein": "MQRPAIIAERAPNLDPAVLAAMQSQPSGVTASDDWTAAMDRIMALTARSPDAFRQQPQANRFSAILEAVVPSRTNPTHEKVLTIVNALLDSKAIRKDEAGLIYNALLERVARYNSTNVQANLDRMGTDVKEALAQRERFHRDGNLGSLVALNAFLSTQPANVPRGQEDYTNFISALRLMVTEVPQSEVYQSGPDYFFQTSRQGLQTVNLTQAFKNLQGLWGVRAPVGDRSTLSSLLTPNSRLLLLLIAPFTNTNSLSRDSYLGHLVTLYREAIGQAQVDEQTYQEITSVSRALGQEDTGSLEATLNFLLTNRRQQVPPQYTLNAEEERILRYVQQSVSLYLMREGATPSAALDMTARNMEPSFYASNRAFINRLMDYLHRAAAMNGEYFTNAILNPHWLPPPGFYTGEFDLPEGNDGFLWDDVTDSLFSPAVIGHHGKKEAGDEGPLLDSRASSPFPSLTSLPASVNSGRTTRPRLTGESEYLNDPILFPVRDKNFPNNGIESLVDKMSRWKTYAQERREWEERQPRPVRPPRQRWQRRKKGAHAGDEGSDDSADDSSVLDLGGSGNPFAHLRPQGCIGSLY", "text": "FUNCTION: Structural component of the virion that acts as a cement protein on the capsid exterior which mediates the interactions between the hexons, including the peripentonal hexons, and reaches all the way to the penton vertices. Two hexon linking proteins IIIa, one from each facet, stabilize the unique edge interface between a pair of facets. As the virus enters the host cell, hexon linking proteins IIIa are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in the serotype specificity of the packaging of viral DNA via its interaction with packaging protein 3. SUBCELLULAR LOCATION: Virion Host nucleus Note=Surrounds the border of each facet on the capsid exterior. Present in around 60 copies per virion. SIMILARITY: Belongs to the adenoviridae hexon-linking protein IIIa family."}
{"protein": "MSQHETPLYTGLKKHASRQPVQFHIPGHKKGAGMDPEFRQFIGENALSIDLINIEPLDDLHAPKGIIKQAQDLAAEAFGADHTFFSVQGTSGAIMTMVMAVCGPGDKIIIPRNVHKSIMTAIVFSGAVPIFIHPEIDNELGISHGITLESAKRALTEHPDAKGLLVINPTYFGVAADLKSIVELAHSFDVPVLVDEAHGVHIHFHDELPLSAMQAGADIAATSVHKLGGSLTQSSILNMREGLVSKDRVQSILSMLTTTSTSYLLLASLDVARKRLATEGRQLAEETLKLANQTRDRLNQIEGIYCVGSEILGSKAAYSYDPTKLIISVKSLGLTGHDVEKWLRESFNIEVELSDLYNILCIFTPGDSQNDADRLVEALTEIAQQMSEQDVTHQQTEVLLPEIPLLAMTPRDAFYANTEVIPLKEASGRIIAEFVMVYPPGIPIFIPGEIITEENISYIFKNLDAGLPVQGPEDSTLHMIRVIKEQKAIQ", "text": "FUNCTION: Catalyzes the formation of agmatine from arginine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family."}
{"protein": "MDRGSLLPFQLWCPRPFSKYSQNQPRPPSTALKPPVCPDTSSGTEPDHRPAHLESTPPAVAAEAPTSQPAPLLSTAASGDEGRVLLDTWYVIKPGNTKEKVAFFVAHQCGGSSRASSMKVKGHWGSDSSKAKRRRRCLEPTKAPPDQGGREGTPATEVTPTSSGDDVDLVSVAEMVALVEQRAALALQSYPRPSTPAPVVFVSADQGGPAKGLGSERRSGGGDCSRVAEAVAHFEAQRDSPPTKGLRKEERPGPGPGEVRIAFRISNVREPHSPDGNLPNGGGGRPGCAYPGSPGPGTRAKDKITCDLYQLISPSRDALPSNVEFLLARADEASEGETPAPTRPEDTPPAPPPPPARDCGASGFHVDVVVTGVVDACIFFGKDGTKNVKEETVCLTVSPEEPPPPGQLFFLQSRGPEGPPEPPPADIPSTVPGPDDSEGTTDTSLCRLYRHVSHDFLEIRFKIQRLLEPRQYMLLLPEHVLVKIFSFLPTRALAALKCTCHHFKGIIEAFGVRATDSRWSRDPLYRDDPCKQCRKRYEKGDVSLCRWHPKPYHHDLPYGRSYWMCCRRADRETPGCRLGLHDNNWVLPCNGVGGGRAGREEGR", "text": "FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex."}
{"protein": "MKWLVILGLVALSECLVIIPLTKVKSIRENLREKDLLLNFLKEHPYNMIQKFGLKGSLCSPKISCLRLWNYLDMVYVGNITIGTPPQLFSVIFDTASSDLWVPSNQCHSRACVTHRSFNPTLSSTFQSSNRTVKLAPHSGLVSGLLGYDTVQIGRFKSENQAFGLSQSEPVKELENAFFDGVLGLGYPSLAIQGTTPVFDNLRKQGQIPEPVFALYLSTNTKKGSVLMIGGVDNNFFTGNLKWVPLSARNYWQITLDRITWRGVVVGCTRGCQAILDSGSAFLLGPSRQISSIQKIIQARFIENEYQVRCCARTTLADFIFTINNVQYPVPARAYIRKGSTPRRCYSNFSGGTESLGKEETWILGEVFLRLYFTVFDRGQNRIGLRIAV", "text": "FUNCTION: Appears to be proteolytically inactive. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MNSPISLDMGAITYNMDDLYKELAIYSNSTEIPLQDSIFCSTEEGPLLTSFKTIFMPVAYSLIFLLGMMGNILVLVILERHRHTRSSTETFLFHLAVADLLLVFILPFAVAEGSVGWVLGTFLCKTVIALHKINFYCSSLLLACIAVDRYLAIVHAVHAYRRRRLLSIHITCSTIWLAGFLFALPELLFAKVVQPHNNESLPQCIFSQENEAETRAWFASRFLYHTGGFLLPMLVMAWCYVGVVHRLLQAQRRPQRQKAVRVAILVTSIFLLCWSPYHIVIFLDTLERLKAVNSSCELSGYLSVAITLCEFLGLAHCCLNPMLYTFAGVKFRSDLSRLLTKLGCAGPASLCQLFPGWRKSSLSESENATSLTTF", "text": "FUNCTION: Cytokine receptor that binds to B-lymphocyte chemoattractant (BLC). Involved in B-cell migration into B-cell follicles of spleen and Peyer patches but not into those of mesenteric or peripheral lymph nodes (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSPSLNEPERLNRQAQGLACNECRARKLRCDRVRPTCGTCESLGVTCTPNSVRQPRGPRKGYLKTLQSRISALERQWNGQQKAAGGSPGESPPCSEGGQTLRAVSESTSDGVHDEDHANGARPPSSQSSIEQPILQPTVSLDGISALHGFAPVNSPFAFALPGTDPSKTVDLFSHMECFPSMPTKLDPRAYVPQQLTPNSTMSNGQFDLPTDLSVTSEFQLPELMKADLSHLYFDRVHPFAPILNKRRYFARAARPVSEQGAMTCLQHAMWTLAAWLGSQFKHIQKDLYIYTRGLLEKWELNMHPGNPPIELAQARLFLAIYEIMQVNYERGWLSAGRCFRLIQLMKLHEIDVPDGISESGISFGEIEERRRTFWMAYSLDRFINLINKMPLTLNEQVIFTRLPAPEGAFQRERPVQTQFLSEFMAGDDDLQIVSPFSACIVVMTISGRCLSHQQQCMVERAYGGMPQDFITRHQWLEGILMSKGKAIVDCISNDLDDELTDPMLLFTNMAAHATTLLLGMTMQTGLCNYESLISGFEERATEAAQKILHLCQRLNECGYFKVHPFTPIPLVFCAEWAQGRKNQNPAFEPLHNSMLCSLRDLSVVNMLAETCLARLNDSNPQMETDMSKSQS", "text": "FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSVENVERLSPEQADAFFGQSSVDLISRALGGQVLGCSDDFFASCENLINPADPIRKAGVFVETGAWYDGWETRRHNTAPCDWVIVKLGPSSGRVTGCEIDTTFFNGNHAPEVSVEAAFLPEGNPDAKTNWTPILPKLPCGPTQRHIYRFKEIPQQNFTHVRLCMYPDGGIARFRLYGNVVPVFPADLDARLDLAHMYLGGLVVQCSDQHFGKKDNLLLPGRGVNMGDGWETARSREKGHVDWVIVKLGARGYIDDALIDTNHFKGNYPKEVILEAIDSPDHIPGPDAQWVTILPARKLGPHMEHVFTNLQNNSTPMTHVRMIIIPDGGVKRLRIYGRRAAN", "text": "FUNCTION: Utilization of purines as secondary nitrogen sources, when primary sources are limiting. SIMILARITY: Belongs to the allantoicase family."}
{"protein": "MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSVKTSVPSSKSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGSFPSQVTATSGNGDFGDWSAFNQAPSGPVASSGEFFGSASQPAVELVSGSQSALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQNTDMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNVMTQSFGAVNLSSPSNMLPVRPQTNALIGGPMPMSMPNVMTGTMGMAPLGNTPMMNQSMMGMNMNIGMSAAGMGLTGTMGMGMPNIAMTSGTVQPKQDAFANFANFSK", "text": "FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Membrane; Peripheral membrane protein. Cytoplasmic vesicle, clathrin- coated vesicle. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network. SIMILARITY: Belongs to the epsin family."}
{"protein": "MSQVEFEMACASLKQLKGPLSDQEKLLVYSFYKQATQGDCNIPVPPATDVKAKAKWEAWMVNKGMSKMDAMRIYIAKVEELKKNETC", "text": "FUNCTION: May be involved in the energy metabolism of the mature sperm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ACBP family."}
{"protein": "MKVQITNSRTEEILKVQANNENDEVSKATPGEVEESLRLIGDLKFFLATAPVNWQENQIIRRYYLNSGQGFVSCVFWNNLYYITGTDIVKCCLYRMQKFGREVVQKKKFEEGIFSDLRNLKCGIDATLEQPKSEFLSFLFRNMCLKTQKKQKVFFWFSVAHDKLFADALERDLKRESLNQPSTTKPVNEPALSFSYDSSSDKPLYDQLLQHLDSRRPSSTTKSDNSPPKLESENFKDNELVTVTNQPLLGVGLMDDDAPESPSQINDFIPQKLIIEPNTLELNGLTEETPHDLPKNTAKGRDEEDFPLDYFPVSVEYPTEENAFDPFPPQAFTPAAPSMPISYDNVNERDSMPVNSLLNRYPYQLSVAPTFPVPPSSSRQHFMTNRDFYSSNNNKEKLVSPSDPTSYMKYDEPVMDFDESRPNENCTNAKSHNSGQQTKQHQLYSNNFQQSYPNGMVPGYYPKMPYNPMGGDPLLDQAFYGADDFFFPPEGCDNNMLYPQTATSWNVLPPQAMQPAPTYVGRPYTPNYRSTPGSAMFPYMQSSNSMQWNTAVSPYSSRAPSTTAKNYPPSTFYSQNINQYPRRRTVGMKSSQGNVPTGNKQSVGKSAKISKPLHIKTSAYQKQYKINLETKARPSAGDEDSAHPDKNKEISMPTPDSNTLVVQSEEGGAHSLEVDTNRRSDKNLPDAT", "text": "FUNCTION: Binds to the DNA sequence mediating pheromone induction (called the pheromone response element = PRE) which is found in the upstream control region of several a-, alpha- and haploid-specific genes. Involved in mating of haploids and in pseudohyphae formation in diploids. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the STE12 transcription factor family."}
{"protein": "MDAEAARSYSLEQVQALYSFPFQQMMAEVPNMAVTTGQQVPAVAPNMATVTEQQVPEDAPVQEPAPEAPKRRKRKPRAAEPQEPVEPKKPATSKKSGKSTKSKEKQEKITDAFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIERNADVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENPCNGEPCGIASNGLTAHSAEPRGEAAPSDVPNGQWMAQSFAEQIPSFNNCGTREQEEESHA", "text": "FUNCTION: DNA glycosylase that plays a key role in active DNA demethylation: specifically recognizes and binds 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites and mediates their excision through base-excision repair (BER) to install an unmethylated cytosine (PubMed:21817016). Cannot remove 5- hydroxymethylcytosine (5hmC). According to an alternative model, involved in DNA demethylation by mediating DNA glycolase activity toward 5-hydroxymethyluracil (5hmU) produced by deamination of 5hmC (PubMed:21722948). Also involved in DNA repair by acting as a thymine- DNA glycosylase that mediates correction of G/T mispairs to G/C pairs: in the DNA of higher eukaryotes, hydrolytic deamination of 5- methylcytosine to thymine leads to the formation of G/T mismatches. Its role in the repair of canonical base damage is however minor compared to its role in DNA demethylation. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family."}
{"protein": "MTDYAISKKSKRSLWIPILVFITLAACASAGYSYWHSHQVAADDKAQQRVVPSPVFYALDTFTVNLGDADRVLYIGITLRLKDEATRSRLSEYLPEVRSRLLLLFSRQDAAVLATEEGKKNLIAEIKTTLSTPLVAGQPKQDVTDVLYTAFILR", "text": "FUNCTION: Controls the rotational direction of flagella during chemotaxis. FUNCTION: Controls the rotational direction of flagella during chemotaxis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FliL family."}
{"protein": "MSYRKTVVSARRDQKKGRVGGLTEEQKQEIREAFDLFDTDGSGTIDAKELKVAMRALGFEPKKEEIKKMIADIDKAGSGTIDFEEFLQMMTSKMGERDSREEIIKAFKLFDDDNTGFITLKNLKRVAKELGENLTDEELQEMTDEADRNGDGQIDEDEFYRIMKKTSLF", "text": "FUNCTION: This calcium-binding protein is found in the basal body complexes (the functional homolog of the centrosome in animal cell). In mitotic cells it is specifically associated with the poles of the mitotic spindles at the sites of the duplicated basal body complexes (By similarity). SIMILARITY: Belongs to the centrin family."}
{"protein": "GKCGDINAPCKAECDCCGYTTCDCYWGN", "text": "FUNCTION: Insecticidal neurotoxin that reversibly inhibits the N- methyl-D-aspartate (NMDA)-subtype of ionotropic glutamate receptor (GRIN) and inhibits inactivation of insect sodium channels (Nav). In vivo, is highly toxic to insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 05 subfamily."}
{"protein": "MGRKTLCESETVCRDVTINGSAGCLQNVGPPPTNLFQPPRRPGLGTLGKPIRLLANHFQVQIPKIDVYHYDVDIKPEKRPRRVNREVVDTMVRHFKMPIFGDNQPGYDGKRNMYTAHPLPIGRDRVDLEVTLPGEGKDQTFKVTIQWVSVVSLQLLLEALSGHLSEVPDDSVQALDVITRHLPSMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWNMMLNIDVSATAFYRAQPVIEFMCEVLDVQNINEQTKPLTDSQRVKFTKEIRGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLQLENGQAMECTVAQYFKQKYSLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLVKSNSMVGGPDPYLKEFGIVVHNEMTELTGRVLPAPMLQYGGRNKTVATPNQGVWDMRGKQFYAGIEIKVWAVACFAPQKQCREDLLKSFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFKHLKLTYVGLQLIVVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNVVKTSPQTLSNLCLKINAKLGGINNVLVPHQRPSVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDGHPSRYCATVRVQTSRQETTQELLYSQEVIQDLCNMVRELLIQFYKSTRFKPTRIIYYRGGVSEGQMKQVAWPELMAIRKACISLEEDYRPGITYIVVQKRHHTRLFCSDKTERVGKSGNVPAGTTVDSTITHPSEFDFYLCSHAGIQGTSRPSHYQVLWDDNCFTADELQLLTYQLCHTYVRCTRSVSIPAPAYYARLVAFRARYHLVDKDHDSAEGSHVSGQSNGRDPQALAKAVQIHHDTQHSMYFA", "text": "FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the argonaute family. Ago subfamily."}
{"protein": "MSSGYSSAPSVSHTSSDTDLNRIDSYDDGAEETTDEQRMCGLSELVTSCLTSSRLKAIDEEDEEENCNDIEIVGLSKTTTKVKRSKKVLSCPIVSSSTKKENGNAAPFLKSSQFTDVPPTIRFYTKGTKVTKPARKIQARLTWCHNSLLPIVMRQTLAASHFTVVDESLFYVGYWGRHLKSAQYRALQPHQKVNHFPGAFHIGRKDRLWMHIRKQQERFEGEFDIMPFTYILPTDRQELLKYLETDASRHVIVKPPASARGTGISVTRKPKDFPTTATLVAQHYIERPLTINRAKFDLRLYAYVPTFEPLRVYIYDQGLVRFASVPYSHSVSTISNKYMHLTNYSINKLAEADGVANKPVPKWTLHHLWEHFDEMGVDREKIQREIEEVIIKAFISTEKPIREHMSRFLEQEFICYELFGIDIILDEDYKPWLLEVNISPSLHSGTPLDVSVKAPLAKDVLNLAGVYVPPSFDKLSDADYSTRPRNGRKNREQLIKEASWVAAYKDQLGVIDNRIFKRLTPEDTRALVEFEDELERIGDFKLVFPTAHTSHYQKYFAETIYMNILLQQWQIAQEDDRSIGINRLEQLCRQKHMQSDQETSF", "text": "FUNCTION: Monoglutamylase which modifies tubulin, adding a single glutamate on the gamma-carboxyl group of specific glutamate residues of target proteins (PubMed:32747782). Involved in the side-chain initiation step of the polyglutamylation reaction but not in the elongation step. Preferentially modifies beta-tail tubulin over the alpha-tubulin (PubMed:32747782). Involved in side-chain glutamylation of tubulin in sensory cilia (PubMed:20519502, PubMed:27635036, PubMed:29849065). Together with ttll-5 and ttll-11, required for male mating (PubMed:27635036). SIMILARITY: Belongs to the tubulin--tyrosine ligase family."}
{"protein": "MFSNIDHKAVAALLHGQGCANILKTVLDNCKVSSVSTEPLINTILDSFSLALSSVNSPNRQPHHESSSRDMAGLVPQRSSKKKICGVKGLEIYRDDSPNPRLDDGFTWRKYGQKTIKTSLYQRCYYRCAYAKDQNCYATKRVQMIQDSPPVYRTTYLGQHTCKAFGVHDNTYGSEMINFDQVVSESVMRQLATIGEQAVLMEDEANHIMNQEYDINDYLVDDEVFWGNEFPLFSSEDLMLF", "text": "FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis- acting element (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group III family."}
{"protein": "MNETMKAEIESQDDELFDLTPSYLKKEIMVLACGNILFADDGFSVHVIEKLNKILTDKEKQKIALVDAGAGAPQQVLTLIDENSKTKKIIVVDVIDWGIKPGEIKIIEKDELPNPKYHRLDSHDWPLAPLLREVAEKYNIEVKVVGCQAKYISEPDVYIGLSEEVEKAVDKAVEIILRELRGD", "text": "SIMILARITY: Belongs to the peptidase A31 family."}
{"protein": "MVNNRVTESTTTAVSSNGGPPKACAGCGGKIADRFLLYSMERYWHTRCLKCSCCQAQLGEIGTSCYTKSGMILCRNDYIRLFGSSGACSACGQSIPASEMVMRAQGSVYHLKCFTCATCRNRLVPGDRFHYVNGAIFCEHDRPTGLLSGHLNPLQSNPPMLPDQKVC", "text": "FUNCTION: Acts as a positive cofactor of GATA transcription factors to establish the identity of the ventral mesoderm during gastrulation. Down-regulation in the dorsal mesoderm is necessary for the proper formation of this territory since, when present, lmo4 may bind ldb1 and restrict the availability of this cofactor for Spemman organizer transcription factors. At neurula stages, suppresses primary neuron differentiation and modulates gene expression at the Isthmic Organizer of the midbrain-hindbrain boundary (By similarity)."}
{"protein": "MIMASSAAASISMITLRNLSRNHQSHQSTFLGFSRSFHNQRISSNSPGLSTRARSTTSSTGGFFRTICSSSSNDYSRPTKIQELNVYEFNEGDRNSPAVLKLGKKPDQLCLGDLVPFTNKLYTGDLTKRIGITAGLCVLIQHVPEKKGDRFEASYSFYFGDYGHISVQGPYLTYEDTFLAITGGSGVFEGAYGQVKLRQLVYPTKLFYTFYLKGVAADLPVELTGKHVEPSKEVKPAAEAQATQPGATIANFTN", "text": "FUNCTION: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the allene oxide cyclase family."}
{"protein": "MAQEITHPTIVDGWFREISDTMWPGQAMTLKVEKVLHHEKSKYQDVLIFKSTTYGNVLVLDNVIQATERDEFAYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHDSVEEAWLCDIDEAVIRLSKEYLPEMAASYSHPKVKTHIGDGFQFLRDYQNTFDVIITDSSDPEGPAETLFQKEYFQLLNSALTEKGVITTQAESMWIHLPIIKDLKKACSEVFPVAEYSFVTIPTYPTGTIGFMVCSKDKTCNVKKPLREISDEKEAELYRYYNKKIHEASFVLPTWAAKELN", "text": "SIMILARITY: Belongs to the spermidine/spermine synthase family."}
{"protein": "MTNNKVALVTGGAQGIGFKIAERLVEDGFKVAVVDFNEEGAKAAALKLSSDGTKAIAIKADVSNRDDVFNAVRQTAAQFGDFHVMVNNAGLGPTTPIDTITEEQFKTVYGVNVAGVLWGIQAAHEQFKKFNHGGKIINATSQAGVEGNPGLSLYCSTKFAVRGLTQVAAQDLASEGITVNAFAPGIVQTPMMESIAVATAEEAGKPEAWGWEQFTSQIALGRVSQPEDVSNVVSFLAGKDSDYITGQTIIVDGGMRFR", "text": "FUNCTION: Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MFAQQPRSAPAPFYEKVKQAISEKIHSGVWRPHDRIPSEAELVAQFGFSRMTINRALRELTDEGLLVRLQGVGTFVAEPKGQSALFEVRSIAAEIVARHHQHRCEVLLLEETRADHIQATALSVPEGTRIFHSLMVHYENEVPVQIEDRCVNAAVVPDYLHQDYTATTPHDYLSLIAPLTEGEHIVEAVQATAEECALLHIHAHDPCLLIRRRTWSTTHIVSHARLLFPGSRYRLQGRFGS", "text": "FUNCTION: Repressor which binds to the hutP region in the histidine utilization (hut) operon. It blocks the expression of all the hut genes in the absence of inducer."}
{"protein": "MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPIPTQKDEPIIRIQP", "text": "FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:25217505, PubMed:24985707). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed:25217505, PubMed:24985707). Also active toward p-coumaroyl-CoA and sinapoyl-CoA (PubMed:25217505, PubMed:24985707). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:24985707). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily."}
{"protein": "MAKKKPVEKNGLVYKEFQKQVSNLKKAGLIPKTLDVRKVKPTKHYKGLVSKYKDVATGGAKLAAIPNPAVIETLEARGESIIKKGGKAYLKARQQINQRGQIVNPFTVRVTKRGEVVRRYRKTTPEGKPVYITQRELPIKFENMEQWLTELKAAGFQLQPGEQIYFTFNGNYSRRTYTSFDEAFNKFMTYDIIIDAVAGKLKVEDEADLVKSVGFQRISGPEAKAYNRNRIVLPEMQFSQAAKKKYKRRQKRGYGSKGV", "text": "FUNCTION: Acts as a primer for viral genomic replication. DNA terminal protein is covalently linked to the 5'-ends of both strands of the genome through a phosphodiester bond between the beta-hydroxyl group of a tyrosine residue and the 5'-phosphate of the terminal deoxyadenylate. This protein is essential for DNA replication and is involved in the priming of DNA elongation (By similarity). SUBCELLULAR LOCATION: Virion. Host nucleus. SIMILARITY: Belongs to the tectivirus DNA terminal protein family."}
{"protein": "MIPIKFKGRTISRGCAEGEVLISRDPISFLGSVDPRTGIVVEEKHSLAGKSIKGKVLVFPHGKGSTVGSYVMYQLKKNEAAPAAIINLETEPIVAVGAIISEIPLVDMLEKDPYEFLKDGDTVLVNGSEGYIELLKQGEGQAKK", "text": "SIMILARITY: Belongs to the UPF0107 family."}
{"protein": "METNCPNILYLSGITIEECLQSKKTSTDALNTNGDEAEVEKKLPSVFTSVSKWVTYSSFKCWTCHLYFKTVPKFVPTYMRENERGEIEMGVLGNFCSFSCAASYIDLHYTEPKRWEARELLNMLYRFFTSQWISYIRPALSYTMRKEYGGKLSEEAFISELHTLEESISSKDIFI", "text": "SIMILARITY: Belongs to the asfivirus B175L family."}
{"protein": "MNIRQSGKYYEYKTLEILEKNGFKALRIPVSGTGKQALPDLIATKNNTIYPIEVKSTSKDVVTVRNFQIEKLFKFCEIFNFCECHPLVTVYYKKYKIVIVYELSQDVRTKEKIKFKYGINS", "text": "FUNCTION: A structure-specific endonuclease that binds and cleaves the four-way Holliday junctions in DNA created during repair and rearrangement by the ubiquitous process of homologous recombination. Introduces paired nicks in opposing strands; on immobile junction cleaves 2 bases 3' of the junction point, on mobile strands the cleavage site varies. Cleaves Y and loop-out structures with much lower efficiency. Binds 4-way junction DNA but not sequence-identical linear dsDNA. SIMILARITY: Belongs to the Holliday junction resolvase Hjc family. Hje subfamily."}
{"protein": "MVQQRGARAKRDGGPPPPGPGPAAEGAREPGWCKTPSGHIKRPMNAFMVWSQHERRKIMDQWPDMHNAEISKRLGRRWQLLQDSEKIPFVREAERLRLKHMADYPDYKYRPRKKSKGAPAKARPRPPGGGGGGSRLKPGPQLPGRGGRRASGGPLGGGAAAPEDDDEDEEEELLEVRLLETPGRELWRMVPAGRAARGPAERAQGPSGEGAAASAASPTLSEDEEPEEEEEEAATAEEGEEETVVSGEEPLGFLSRMPPGPAGLDCSALDRDPDLLPPSGTSHFEFPDYCTPEVTEMIAGDWRSSSIADLVFTY", "text": "FUNCTION: Transcription factor that binds to DNA at the consensus sequence 5'-ACCAAAG-3' (PubMed:18505825, PubMed:18403418, PubMed:30190287). Acts as a transcriptional activator (PubMed:18505825, PubMed:18403418, PubMed:30190287). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (PubMed:18505825, PubMed:18403418). Involved in the differentiation of naive CD4-positive T-cells into peripherally induced regulatory T (pT reg) cells under inflammatory conditions (PubMed:30190287). Binds to the promoter region of the FOXP3 gene and promotes its transcription, and might thereby contribute to pT reg cell differentiation in the spleen and lymph nodes during inflammation (PubMed:30190287). Plays a redundant role with SOX4 and SOX11 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (PubMed:20596238). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKKIMLVFITLILISLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEINYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNSVDNPIE", "text": "FUNCTION: A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Acts as major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. Can be reversibly inactivated by oxidation. SUBCELLULAR LOCATION: Secreted Host membrane; Multi-pass membrane protein Host cell membrane; Multi-pass membrane protein Note=Secreted as soluble protein that then inserts into the host membrane and forms pores formed by transmembrane beta-strands. SIMILARITY: Belongs to the cholesterol-dependent cytolysin family."}
{"protein": "MKKLLPILIGLSLSGFSSLSQAENLMQVYQQARLSNPELRKSAADRDAAFEKINEARSPLLPQLGLGADYTYSNGYRDANGINSNATSASLQLTQSIFDMSKWRALTLQEKAAGIQDVTYQTDQQTLILNTATAYFNVLNAIDVLSYTQAQKEAIYRQLDQTTQRFNVGLVAITDVQNARAQYDTVLANEVTARNNLDNAVEQLRQITGNYYPELAALNVENFKTDKPQPVNALLKEAEKRNLSLLQARLSQDLAREQIRQAQDGHLPTLDLTASTGISDTSYSGSKTRGAAGTQYDDSNMGQNKVGLSFSLPIYQGGMVNSQVKQAQYNFVGASEQLESAHRSVVQTVRSSFNNINASISSINAYKQAVVSAQSSLDAMEAGYSVGTRTIVDVLDATTTLYNAKQELANARYNYLINQLNIKSALGTLNEQDLLALNNALSKPVSTNPENVAPQTPEQNAIADGYAPDSPAPVVQQTSARTTTSNGHNPFRN", "text": "FUNCTION: Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family."}
{"protein": "MDHAEENEILAATQRYYVERPIFSHPVLQERLHTKDKVPDSIADKLKQAFTCTPKKIRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPIFGLYSSFYPVIMYCFLGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLKESYNVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGLCNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYKVLGKLPETDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSNALKRKTGVNPAVIMGARRKAMRKYAKEVGNANMANATVVKADAEVDGEDATKPEEEDGEVKYPPIVIKSTFPEEMQRFMPPGDNVHTVILDFTQVNFIDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTRNRFFENPALWELLFHSIHDAVLGSQLREALAEQEASAPPSQEDLEPNATPATPEA", "text": "FUNCTION: Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Lateral wall of outer hair cells. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family."}
{"protein": "MAETYDFLFKFLVIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNVGGKTVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNSLAAWLTDARTLASPNIVVILCGNKKDLDPEREVTFLEASRFAQENELMFLETSALTGENVEEAFLKCARTILNKIDSGELDPERMGSGIQYGDISLRQLRQPRSAQAVAPQPCGC", "text": "FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (PubMed:14697203). Protein transport (By similarity). Probably involved in vesicular traffic (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (PubMed:14697203). FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (By similarity). Protein transport. Probably involved in vesicular traffic (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADITAIKRLSDMGFKVTVTGGLVLEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG", "text": "FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization. SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily."}
{"protein": "MDRRIFGLETEFGVTCAFEGQRKLSPDEVARYLFRKVVSWGRSSNVFLKNGARLYLDVGSHPEYATPECDDVRQLVVHDRAGERTLEGLLTDAERRLEEEGIAGEVFLFKNNTDSAGNSYGCHENYLVSRHGEFGKLSDVLIPFLVSRQLIVGAGKVVQTPRGAVYSLSQRADHIWEGVSSATTRSRPIINTRDEPHADAERYRRLHVIVGDSNMSETTTMLKLGATDLVLRMVEEGVVLREMTMENPIRAIREISHDMTGRKPVRLANGREASALEIQEEYLEKAKEFVESRGLQTPTIKRVLDLWERALRAVATQDFSLVDREVDWVIKKKLLDRYMAKHDLPLTSPRIARLDLAYHDIHRKRGLHYMLAERGMAERVCSDIEVFEALSVPPQTTRAKLRGDFVRAAQEKRRDFTVDWVHLKLNDQAQRTVLCKDPFKAVDDRVERLIDSM", "text": "FUNCTION: Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine. SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup- conjugating enzyme subfamily."}
{"protein": "MLTLDTLNTMLAVSEEGMVEEMILALLASPQLVIFFEKFPRLKNAVTADLPRWREALRSRLKDARVPPELTEEVMCYQQSQLLSTPQFIVQLPQILALLHRLHSPYTAQAKQLTESNSTFTPALHTLFLQRWRLSLVVQATTLNQQLLEEEREQLLSDVQERMTLSGQLEPTLAENDNAAGRLWDMSAGQLKRGDYQLIVKYGEFLAAQPELMQLAEQLGRSREAKSVPKKDAPMETFRTLVREPATVPEQVDGIQQGDDILRLLPPELATLGITELEYEFYRRLVEKQLLTYRLHGEAWREKVTERPVVHQDVDEQPRGPFIVCVDTSGSMGGFNEQCAKAFCLALMRVALADNRRCFIMLFSTDVVRYELSGPEGIEQAIRFLSQRFRGGTDIASCFRAIIERMQGREWFDADAVVISDFIAQRLPDDVVSKVGELQRLHQHRFHAVAMSAHGKPGIMRIFDHIWRFDTGMRSRLLRRWRR", "text": "SIMILARITY: Belongs to the ViaA family."}
{"protein": "METPPIVIDNGSYEIKFGPSTNKKPFRALNALAKDKFGTSYLSNHIKNIKDISSITFRRPHELGQLTLWELESCIWDYCLFNPSEFDGFDLKEGKGHHLVASESCMTLPELSKHADQVIFEEYEFDSLFKSPVAVFVPFTKSYKGEMRTISGKDEDIDIVRGNSDSTNSTSSESKNAQDSGSDYHDFQLVIDSGFNCTWIIPVLKGIPYYKAVKKLDIGGRFLTGLLKETLSFRHYNMMDETILVNNIKEQCLFVSPVSYFDSFKTKDKHALEYVLPDFQTSFLGYVRNPRKENVPLPEDAQIITLTDELFTIPETFFHPEISQITKPGIVEAILESLSMLPEIVRPLMVGNIVCTGGNFNLPNFAQRLAAELQRQLPTDWTCHVSVPEGDCALFGWEVMSQFAKTDSYRKARVTREEYYEHGPDWCTKHRFGYQNWI", "text": "FUNCTION: Component of the SWR1 complex which mediates the ATP- dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the actin family. ARP6 subfamily."}
{"protein": "MEKAENEKKPSAVSDVGAWAMNVTSSVGIIMANKQLMSSSGFGFSFATTLTGFHFALTALVGMVSNATGLSASKHVPLWELLWFSLVANISIAAMNFSLMLNSVGFYQISKLSMIPVVCVMEWVLHSKHYSREVKASVMVVVVGVGICTVTDVKVNAKGFICACTAVFSTSLQQISIGSLQKKYSIGSFELLSKTAPIQAISLLIFGPFVDYFLSGRFISTYKMTYSAMLCILLSCALAVFCNISQYLCIGRFSATSFQVLGHMKTVCVLTLGWLIFDSEMTFKNIAGMVLAVVGMVIYSWAVELEKQRKSKVIPHGKHSMTEDEIKLLKEGIEHMDLKDMELGNNKA", "text": "FUNCTION: Nucleotide-sugar transporter that transports UDP-rhamnose or UDP-galactose and UMP in a strict counter-exchange mode. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9) subfamily."}
{"protein": "MPSSKRTAAIIVAAGRGLRAGAGGPKQYRTIGGRTVISRAMEAFCQHPDVFAVQPVLNPDDLSMFNQAAAQFRYRPPANGGATRQASVRAGLEALAADAPDIVLIHDAARPFVTPALITRAIDAADKAGAAVPAIAVTDTIKQVDESGAVNATPDRAKLRIAQTPQAFHFDMILDAHRRAAREGRDDFTDDAALAEWVGLTVATFEGDAANMKLTTPEDFVREEARLAAALGDIRTGTGYDVHAFGEGDHLMLCGVKVPHNCGFLAHSDGDVGLHALVDAILGALADGDIGSHFPPSDPQWKGAASDKFLKYAVDRVTARGGRVANLEVTMICQQPKIGPLRDQMRARIADITGVAISRIAVKATTSERLGFTGREEGIAATASATIRLPWNDKGRDT", "text": "FUNCTION: Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF). SIMILARITY: In the C-terminal section; belongs to the IspF family. SIMILARITY: In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily."}
{"protein": "MKPHLKQWRQRMLFGIFAWGLLFLLIFIYFTDSNPAEPVPSSLSFLETRRLLPVQGKQRAIMGAAHEPSPPGGLDARQALPRAHPAGSFHAGPGDLQKWAQSQDGFEHKEFFSSQVGRKSQSAFYPEDDDYFFAAGQPGWHSHTQGTLGFPSPGEPGPREGAFPAAQVQRRRVKKRHRRQRRSHVLEEGDDGDRLYSSMSRAFLYRLWKGNVSSKMLNPRLQKAMKDYLTANKHGVRFRGKREAGLSRAQLLCQLRSRARVRTLDGTEAPFSALGWRRLVPAVPLSQLHPRGLRSCAVVMSAGAILNSSLGEEIDSHDAVLRFNSAPTRGYEKDVGNKTTIRIINSQILTNPSHHFIDSSLYKDVILVAWDPAPYSANLNLWYKKPDYNLFTPYIQHRQRNPNQPFYILHPKFIWQLWDIIQENTKEKIQPNPPSSGFIGILIMMSMCREVHVYEYIPSVRQTELCHYHELYYDAACTLGAYHPLLYEKLLVQRLNMGTQGDLHRKGKVVLPGFQAVHCPAPSPVIPHS", "text": "FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6- sialyltransferase activity toward oligosaccharides that have the Gal- beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
{"protein": "MAHSVKIYDTCIGCTQCVRACPTDVLEMVPWNGCRAKQIASAPRTEDCVGCKRCESACPTDYLSVRVYLRQETTRSMGLAY", "text": "FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side."}
{"protein": "MPEQGIEAQLRLQRGAFRLDAHLQLPANGISVLLGRSGSGKTTLLRAIAGLERAEGFLQVGGQLWQDATCFRPPHQRSLGYVRQASELLPHLDVRANLEFGYRRIPRARRRLGLDEVIALFGLEDLLDQRAEWLPNGPRQRVAIACALLTSPDLLLLDAPLICLDRHSRAQILPALEQLRGQLRIPLLYVTHSQDEVTRLADHLILLDKGKTFASGPPGRLLSDPRLPLNHPDEAAVVLIGQVEHHDPHYRLSTVRVPGGTLSVSLSRLPPGAETRVRIFARDVSLSLDPPHNSSILNILRVRIADLFHEQDSARVMVRLDLDSACILARITRLSADRLGLAPGLQVYAQIKSVALME", "text": "FUNCTION: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Molybdate importer (TC 3.A.1.8) family."}
{"protein": "MAETWVSEIMTQALGCLQAFSSEFALEWESSDMKAAIFKLLLGWIVLSLTAILLAWKSYGPTVNSIYYRQGMGGQNGGTPEYPARFPVWESSSTESLKRHQE", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TCTA family."}
{"protein": "MLAQSCCLRLLILLLLFTTIGSVPKKSLKYFTNRKLRERRIKLFGTKKTEIQSLLISTWNYTDANLQAWSVLQQGPRRTRQAVIQGCMACQNQRCGRLLTGRSSPDTEGALTLEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEYLTDARTRNVLKKWRSNGCQPNFWRDVHPSPAENCGPYSPLPEHMHQHPMHQEYAIIQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRHLPAFLAVEAMRAGKEPDKAAELVVQRLLRHNTEFNGAVVVVNRRGIYAAACAGLDEFHFVVSGGKEYLSMARVERVKCLERENEVIDGGPKGLFPTIPEKHKVP", "text": "SIMILARITY: Belongs to the Ntn-hydrolase family."}
{"protein": "MDVLFEDNAPLSPTTSSLMPSNGDPRLYGNDLNAGDANTSDAFNWTVDAENRTNLSCEGCLSPPCFSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDPGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDIIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKKDAKSTDNDYSMVALGKQHSEDAPTDNINTVNEKVSCV", "text": "FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5- dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, dendrite Cell projection, axon Cytoplasmic vesicle Membrane, caveola Presynapse. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRWLWPLAVSLAVILAVGLSRVSGGAPLHLGRHRAETQEQQSRSKRGTEDEEAKGVQQYVPEEWAEYPRPIHPAGLQPTKPLVATSPNPGKDGGTPDSGQELRGNLTGAPGQRLQIQNPLYPVTESSYSAYAIMLLALVVFAVGIVGNLSVMCIVWHSYYLKSAWNSILASLALWDFLVLFFCLPIVIFNEITKQRLLGDVSCRAVPFMEVSSLGVTTFSLCALGIDRFHVATSTLPKVRPIERCQSILAKLAVIWVGSMTLAVPELLLWQLAQEPAPTMGTLDSCIMKPSASLPESLYSLVMTYQNARMWWYFGCYFCLPILFTVTCQLVTWRVRGPPGRKSECRASKHEQCESQLNSTVVGLTVVYAFCTLPENVCNIVVAYLSTELTRQTLDLLGLINQFSTFFKGAITPVLLLCICRPLGQAFLDCCCCCCCEECGGASEASAANGSDNKLKTEVSSSIYFHKPRESPPLLPLGTPC", "text": "FUNCTION: G-protein coupled receptor (PubMed:27072655). Has been shown to bind the neuroprotective and glioprotective factor prosaposin (PSAP), leading to endocytosis followed by an ERK phosphorylation cascade (PubMed:23690594). However, other studies have shown that prosaposin does not increase activity (PubMed:27072655, PubMed:28688853). It has been suggested that GPR37L1 is a constitutively active receptor which signals through the guanine nucleotide-binding protein G(s) subunit alpha (PubMed:27072655). Participates in the regulation of postnatal cerebellar development by modulating the Shh pathway (By similarity). Regulates baseline blood pressure in females and protects against cardiovascular stress in males (By similarity). Mediates inhibition of astrocyte glutamate transporters and reduction in neuronal N-methyl-D-aspartate receptor activity (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, cilium membrane; Multi-pass membrane protein Note=Associates with the basal membrane of Bergmann glia cell primary cilia. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MIFGGAFDPLHQAHIYIAKRAVQAIKAQKLYFVPTAKAFFKSPIKASNQARLAMLRVALKALPQMAVSNFDIKAQNGFSFNTVQHFKQRFPNAELYFLIGSDKLSELAKWHNIEQLQKLCRFVCYERFGYPIDEQLVQQFNVRLLGKCPLDLASSEMFGSHKFRQIPAKVLHYIHQHNIYLKTILQTLLDEPRMQHCLRVGQLAKTLAVANKLDGKTAYTAGAYHDLAKQLPQAQLEKLAKVAGVNDYPSWKVLHSYAGAYILKHWYGLNNSAVFSAIWNHTVPPQKMSQLDMIIYLADKLEPMRVHEEWAKGIDITALVKLAKKDLKLAYQITLKYVRSLQKN", "text": "FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ADP. FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). SIMILARITY: In the N-terminal section; belongs to the NadD family. SIMILARITY: In the C-terminal section; belongs to the Ap4A hydrolase YqeK family."}
{"protein": "ALAGDHFFRF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
{"protein": "IRCTGSKECYSPCYKATGCPNAKC", "text": "FUNCTION: Blocks voltage-gated potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 06 subfamily."}
{"protein": "MKHLAAYLLLTLGGKATPSAADVKAVLESVGIEADSDRLDKLISELEGKDVNELIAEGSSKLASVPSGGAGGAAAAGGAAAAGGAAEAAPEEAKEEEKEESDDDMGFGLFD", "text": "FUNCTION: Plays an important role in the elongation step of protein synthesis. SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family."}
{"protein": "MVANKERAIKRKASEGGAKPEPITSKQEPLDESNDEDNSNESDYESDKENLLGSIENEGEDSSDSDGEYATDDDEDDVLSFESLNSDGEEEDEEEDAGTTLEEVEREAEEDDDEEDGEDDEEADSADDVNSDSSPEEDEGDLEDSSDEELEEEEEEEEAKENGKEKPAKAKAERKQREEQFESDDEPLPDDLKLGRIEDVLGTGEKKTRGLGVFPPVPKRKGKAAQDEYAAGDTSDEEDIRNTVGNIPMHWYDEYKHVGYDWDAKKIIKAKKGDAIDDFLQRMEDPNFWRTVTDPQTGQKVVLSDEDIGLIKRIMSGRNPDAEYDDYEPFIEWFTSEVEKMPIRNIPESKRSFLPSKAEKHKIGRYVHALKMGWMKTMAEKRRLEAIRRQPKFYMLWTTDHGKEEMRRIHDHVAAPKRMLPGHAESYNPPPEYLFDEKELEEWNKLANQPWKRKRAYVPQKYNSLREVPGYTRYVKERFLRCLDLYLAPRMRRSRVAVGAEYLIPKLPSPRDLQPFPTLQNLIYTGHTSLIRCISVEPKGEYIVTGSDDMTVKIWEISTARCIRTIPTGDIVRSVAWCPNSKISLVAAASGKRVLLINPKVGDYMLVKKTDDLLTEAPRSDTVDSERIRSAVQWGEVTEEEKKLGVRIVITHFREVRQVTWHGRGDYFATVMPDGAYRSVMIHQLSKRRSQVPFSKSKGLIQCVLFHPIKPCLFVATQRHIRVYDLVKQLMMKKLYPGCKWISSMAIHPKGDNLLIGTYEKRLMWFDLDLSTKPYQQLRIHNAAIRSVAFHPRYPLFASAGDDRSVIVSHGMVYNDLLQNPLIVPLRRLKNHAVVNDFSVFDVVFHPTQPWVFSSGADNTVRLYT", "text": "FUNCTION: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family."}
{"protein": "MECYRCGVSGCHLKITCSAEETFCYKWLNKISNERWLGCAKTCTEIDTWNVYNKCCTTNLCNT", "text": "FUNCTION: This toxin is described as enhancing presynaptic acetylcholine release, but neither experimental results, nor references to other sources are available. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Orphan group XIX sub-subfamily."}
{"protein": "MVPKLFTSQICLLLLLGLLAVEGSLHVKPPQFTWAQWFETQHINMTSQQCTNAMRVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII", "text": "FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities. SUBCELLULAR LOCATION: Lysosome Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule. SIMILARITY: Belongs to the pancreatic ribonuclease family."}
{"protein": "MITLIIFSFLSFLLGIILSFTAYKFRSQEDPIVAIVNELLPQSQCAQCGYSGCYPYAKAIVENSEKINKCIPGGTDLISAISSVLSIEVPEKNLIITHKKQKNNTVLINESNCVGCSKCASFCPVDAIVGAPNFIHTVLQEFCTGCNICLLHCPTNCIEIKKETYEE", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily."}
{"protein": "MSKTKIYINGKLIGTCENPEEFVEEMRKKRRSGEVSPEMNITHYPENHEIYIFTDPGRARRPLIIVEDGEPLLTEEHLEKLETGEMSWDDLIAAGIIEYLDAEEEENAYIAMSPDEINDEHTHLEIDPSTMLGICAGIIPFANHNSSPRNTMEAGMTKQALGLYASNYDLRTDTRAHLLHHPQVPIVKTRIIDVTGYDERPSGQNFVVAVMSYEGYNMEDALILNKASLERGLARSSFFRSYEAAERRYPGGQEDRFEIPEKGVRGYRSESDYRHLDEDGIINPEAEVSSGDVLIGKTSPPRFLEEIDEFGTVAERRRETSVTVRHGEKGIVDAVLLTETVEGSRLAKIRVREQRQPELGDKFASRHGQKGVVGLIVSQEDMPFTEDGIVPDLIVNPHAIPSRMSVGQVLEMLAGKAACMEGRRVDGTPFTGEDEDDIKEALRANGFETAGVESLYNGITGERIEAEIFIGVAYYQKLHHMTTDKVYARSRGPVQVLTRQPTEGRAREGGLRFGEMERDCLIAHGAALALKERLLDESDKYEALVCADCGMIAVYDKIRDKKYCPICEDSESFPVEVSYAFKLLLDELKSLCIFPKLILEDKA", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this organism) is implicated in DNA promoter recognition and in nucleotide binding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA polymerase beta chain family."}
{"protein": "MMLRLLSSLLLVAVASGYGPPSSHSSSRVVHGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISRDLTYQVVLGEYNLAVKEGPEQVIPINSEELFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNKTPCYITGWGRLYTNGPLPDKLQQARLPVVDYKHCSRWNWWGSTVKKTMVCAGGYIRSGCNGDSGGPLNCPTEDGGWQVHGVTSFVSAFGCNFIWKPTVFTRVSAFIDWIEETIASH", "text": "FUNCTION: Efficient protease with alanine specificity but only little elastolytic activity. SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily."}
{"protein": "MNYFDNKIDQFATYLQKRNNLDHIQFLQVRLGMQVLAKNIGKLIVMYTIAYILNIFLFTLITNLTFYLIRRHAHGAHAPSSFWCYVESIILFILLPLVIVNFHINFLIMIILTVISLGVISVYAPAATKKKPIPVRLIKRKKYYAIIVSLTLFIITLIIKEPFAQFIQLGIIIEAITLLPIFFIKEDLK", "text": "FUNCTION: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP. FUNCTION: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AgrB family. SIMILARITY: Belongs to the AgrB family."}
{"protein": "MTLPASLKGFETLDIFNISSVRNICELNKHAEHVSIKNLPLIDISVGNDDVWFHLEDGTIVNGKSYKSICEKTLGFLGFIGIILLDSEDTLEEIRLSKTQCKRRIIYLILKEDTEFLLCGIVYALENLPIKGQTLLKLRDIIKKISVTLPVSKLLACTCQKLISILRYIFYDDKQQDVLDKVPPIIQLYYESKTANIHMLNLFFKSHDNDDTCTLSLNTRRLQDDSKYLIDFLKSAICDAFSKEYKMTEIEKTSLH", "text": "FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm. SUBCELLULAR LOCATION: Virion Virion tegument Host cytoplasm Host Golgi apparatus. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 1 family."}
{"protein": "MPVEYYLWLAAILFGIGLLGVLTKRNALILMMSVELMLNAANLTFLAFARRSGDLAGHAIAFFVIAVAAAEAAVGLAVVIAIYRSRGAINVDEVRVLSE", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
{"protein": "MRALIIGVGQCGTKIADLFALVDFDTIALNTSRGDLEYLKHIPHDRRILIGESITGGKGVNANPLLGREAMKRDLPLVMRKIGSIVGYEDVDIFFLTFGFGGGTGAGGTPVLAEALKEEYPDSLVVAIGALPLKEEGIRPTINAAITIDKLSKVADSIIAIDNNKLKESGDDISSAYEKINYTIVERIASLLALVDVPGEQTLDASDLKFVLKAFGSFATVGYAKADASKVKNLSRLIIKSFESEGLYLDANIESALYGLVAIHGPPEVLKASDIFEALDYLTSKIRGKQIFRGFYPDPRERDVEVVTLLSGIYESKSIENIVRTAKEYARSFMQAKSEAETKKKELLTGLPDFDDVYPSLEATGSDDPEGFAEYREVSR", "text": "FUNCTION: Involved in cell shape control. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CetZ family."}
{"protein": "MKLSLSKVTSGARLGVISNFGRNGDKTLEVPGCLLYTKTASPPHLTHDTLQTIEGVPAVTHITLSTLAEHQEVLEEYKEGIGKFAGLPDAVFYCSTHDPVSPCPTGYNTNKAVSLWGSGGRIEMTTQKFISAQRVLRPDWFQCLSDGEVTPGGNSRKRIKKSVDRSLVFLDECLQLLSEHEELKPCVLIGAVEGGDLLDERLRSARETAKRPVGGFLLDGFHGISAGNEAKLSLVSAVTAELPEDKPRFIHGVGRPDEVLEFIQRGVDLFDSCFPYQVTERGCALIFTHCHRPDPETAVLEKSEMSDTERNGDVGAEIEEPDADQAEMTPFEICLKEKRFREDFGPLLEGCTCYCCRNHSRAYVHHLLMAKELLAGILLMIHNFQHYFSFFSSIRAALRDGEIKALAELIRKQNS", "text": "FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Note=May associate with the mitochondrion outer membrane. SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily."}
{"protein": "MANNIIPNVSSGDLVGSTPTFPPNAVVRGDFLYLRDVDGNQIPGRTVSDGDEITVLFISNEKNIVLVQYPTSSGYRQGYVTNATSIIKYKDDYSWVNGSTPEPVYDFDKTTQIGTLDPRERAVVLYKVDGMTYVAYDTGKGKLTKSGLVHYEGSGSSTGGGSFNGVAPGEVVPGGFTYENNAEVVGDELYLRDANGNLIPGRSVSVGDKITVLDVGYTKQLALVQYPAGDVVRQGYVTNATNLIRYFNQYSWHNGSTSEEVLDENGGHLGSLNPYEAATLLYEKNGMKHVVYDTNKGPNTKSGYVKYEGAAATRVDIPYPSITNAQKIVYGISGRGRELAAYKVGNGSNSLVFVCAIHGWEDNWAADGIELTRIGNGLIEHFQNAGTNNWSLYIIPVANPDGLSEGFTNNGPGRCTIVGAVDCNRDFPLGFSPGGVPRYHSGSEPLSVSESKSLHDFIQGVKNRTSGEMCVIDLHGWEGAAIGNPEIGEYFRNQFGFGQRSGYGDNRGFMIGWAKSIGAKAALIELPGSTKSHSDVVNGRYLQKIINAVTNLIGGSGGSSSGGSSFSDVSYEATGEVINVQSFLNVREGAGLYTNSIGQLRQGNKVNIVAKNGDWYKIKYGSEYGYVNSGYIIILKNNTSVKLEDWQEDCIKFGWGPITKEKYLEYMDSTRLYKSIENDISQAIKNKSLINVINPLNFSVSEMIACTQIVFNNETTSFFRDEWYSKSNPNFIVKYKKLSNGQIIVLDRINIKKPEKLKTKIPKAAKGAFKDTIKFEFFKGIDGWFTAISGAISIGSDLSVFQSNGELKSNEDIAKALAAAVIVNGVETMFCAFLGGFIAQCIAPEFPIVAAVAGAIVSAIAAFAIGYFVDNHEKEKYLMNSFKGLIDYLF", "text": "FUNCTION: May function as an ionophore."}
{"protein": "MDNALLSLTHEQQQAAVEQIQELMAQGVSSGEAIQIIANRLREAHQNNTSENNS", "text": "SIMILARITY: Belongs to the UPF0181 family."}
{"protein": "MNHLQQRQLFLENLLVGVNSTFHQMQKHSVNTCCQSLQKILDHLILLQTIHSPAFRLDRMQLRQMQTLACLWIHQHNHGHQAMLGAIKWISPLIKELV", "text": "SUBCELLULAR LOCATION: Host cytoplasm Host mitochondrion Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus A NSP6 family."}
{"protein": "MNLSSASSTEEKAVTTVLWGCELSQERRTWTFRPQLEGKQSCRLLLHTICLGEKAKEEMHRVEILPPANQEDKKMQPVTIASLQASVLPMVSMVGVQLSPPVTFQLRAGSGPVFLSGQERYEASDLTWEEEEEEEGEEEEEEEEDDEDEDADISLEEQSPVKQVKRLVPQKQASVAKKKKLEKEEEEIRASVRDKSPVKKAKATARAKKPGFKK", "text": "FUNCTION: Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. SUBCELLULAR LOCATION: Nucleus Note=Found in the oocyte nucleus before nuclear membrane breakdown, after which it is redistributed to the cytoplasm. SIMILARITY: Belongs to the nucleoplasmin family."}
{"protein": "MTRNERIFHAVLFELMALAIIVPAAALITGKGSSDLALVGIGLSLYTVVWNYIYNLYFDKWFGSNRADRSLAMRLGHTVGFEGGLIFISIPVIAWFLEITFLRALMLEAGFLVFFLFYATGFNWLYDKVQPFGKMRKLLV", "text": "FUNCTION: Mediates the efflux of short-chain diamines when energized by an electrochemical gradient (By similarity). Confers resistance to chlorhexidine, benzalkonium, proflavine and acriflavine. Mediates efflux of both proflavine and acriflavine via an energy-dependent mechanism (PubMed:25670776). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the proteobacterial antimicrobial compound efflux (PACE) (TC 2.A.117) family."}
{"protein": "MSSISDTQVYIALVVALIPGLLAWRLATELYK", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaM family."}
{"protein": "MSFLWAKEFCVLKYPYKLFITHKFSYLLRFETVTLNNIRSPQFYAKLTFSHHQPTVSGTMSTELKFISKYLQISIPETKEGPVSSLFKAVSEQKPELLGNTDFEKAQILEWTTKAFSPIETQSIVEQLDEFLKSSTFIAQDSGISVADLAVYARIHSYICGLSAKEGYKLNNVCRWFDFIQHQESVMEAANSMSMKLANIDLNAPKIQRPSVIKKDKKEKKEGKPSQEASVKSVEKAPKGLEGAKKEKQNKKEKKDKKDKKDKKEKAPKEPPKAATPVPSMIDFRIGFIEKAVKHPNADSLYVSTIHCGDAEGPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVFCASSPDKSVVEFVLPPENAEIGDRLTFEGFDTEEPEAQLNPKRKIWEAIQPGFTSGEDLICGYKDESGLHRLFVKGKKDLGFCKAQTVVNGTLS", "text": "FUNCTION: Binds to tRNA and functions as a cofactor for the methionyl- tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C- terminal part (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the tRNA-aminoacylation cofactor ARC1 family."}
{"protein": "GLWNKIKEAASKAAGKAALGFVNEMV", "text": "FUNCTION: Possesses a potent antimicrobial activity against Gram- positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MELQVVGANALTVSETTFGREFNEALIHQVVVAYAAGARQGTRAQKTRAEVSGSGKKPWRQKGTGRARAGDIKSPIWRSGGTTFAAKPQDHSQKVNKKMYRGAIKSILSELVRQDRLVVVEKFELDAPKTKVLVQKLKDLAVEDALIITASLDENLFLAARNLYKVDVRDVQGIDPVSLIAFDKVIVTVDAVKQIEEILA", "text": "FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. FUNCTION: Forms part of the polypeptide exit tunnel. FUNCTION: Forms part of the polypeptide exit tunnel. FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). FUNCTION: This protein when expressed in E.coli represses both transcription and translation of the endogenous S10 operon. As the H.influenzae S10 leader can be regulated in vitro by the E.coli L4 protein this strongly suggests the endogenous protein controls its own S10 operon in a similar fashion. FUNCTION: Protein L4 is a both a transcriptional repressor and a translational repressor protein. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader. L4 controls the translation of the S10 operon by binding to its mRNA (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uL4 family. SIMILARITY: Belongs to the universal ribosomal protein uL4 family."}
{"protein": "MNLHGVSGHHEPNSEPPIPTGSSSPKLKISPKLNRWSRGRALRSGVKLDRPIPRSDNSPRRQVTEAQPTDEADKKTTAIDVEVTAGKSIYLVSDGTGWTAEHSVNAALGQFEDFSLNRGSSVNTHLFSWVEDEERLIEIIKQAAKEGAMCFYTLANPSMAKSAKQACDQLGVLSVDILGPIIEGIASHLGVSPSGLTRGAPGRVKTLNDAYFKRIEAIEFTIKQDDGTLPENLSKADIVLVGVSRTGKTPLSTYIAQKGYKVANVPFVMGVEPPRTLFQVEPRKVFGLKIQLVVLQAIRRTRVKTLGVDTEAENNYSGIDLVRKELDFASRIYERNPGWAVIDVTNKAIEETAAVILRLYHDGRDTSTTVPRISKRY", "text": "FUNCTION: Bifunctional serine/threonine kinase and phosphorylase involved in the dark/light-mediated regulation of PPDK by catalyzing its phosphorylation/dephosphorylation. Has a much lower phosphotransferase activity than PDRP1 (PubMed:21883547). Can use ADP as a high specificity substrate and GDP as a lower affinity substrate, but has no activity with UDP (PubMed:21414960). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PDRP subfamily."}
{"protein": "MSSNPENSGVNANNNTGTGNADAITGAQQNMVLQPRQLQEMAAKFRTLLTEARNVGETTPRGKELMFQAAKIKQVYDALTLNRRRQQAAQAYNNTSNSNSSNPASIPTENVPNSSQQQQQQQQQTRNNSNKFSNMIKQVLTPEENQEYEKLWQNFQVRHTSIKEKETYLKQNIDRLEQEINKQTDEGPKQQLQEKKIELLNDWKVLKIEYTKLFNNYQNSKKTFYVECARHNPALHKFLQESTQQQRVQQQRVQQQQQQQQQQQQQQQQQQQQQQQRQGQNQRKISSSNSTEIPSVTGPDALKSQQQQQNTITATNNPRGNVNTSQTEQSKAKVTNVNATASMLNNISSSKSAIFKQTEPAIPISENISTKTPAPVAYRSNRPTITGGSAMNASALNTPATTKLPPYEMDTQRVMSKRKLRELVKTVGIDEGDGETVIDGDVEELLLDLADDFVTNVTAFSCRLAKHRKSDNLEARDIQLHLERNWNIRIPGYSADEIRSTRKWNPSQNYNQKLQSITSDKVAAAKNNGNNVASLNTKK", "text": "FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II- dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF12 family."}
{"protein": "MWPNGSSLGPCFRPTNITLEERRLIASPWFAASFCVVGLASNLLALSVLAGARQGGSHTRSSFLTFLCGLVLTDFLGLLVTGAIVVSQHAALFEWHAVDPGCRLCRFMGVVMIFFGLSPLLLGATMASERFLGITRPFSRPVVTSQRRAWATVGLVWAAALALGLLPLLGLGRYTVQYPGSWCFLTLGAESGDVAFGLLFSMLGGLSVGLSFLLNTVSVATLCHVYHGQEAAQQRPRDSEVEMMAQLLGIMLVASVCWLPLLVFIAQTVLRNPPAMSPSGQLSRATEQELLIYLRVATWNQILDPWVYILFRRAVLRRLQPRLSTRPRSLSLQPQLTQRSGLQ", "text": "FUNCTION: Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G- protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C and adenylyl cyclase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MERHEQILKEIAFLELRLQSLKLELEFVRSSGSEQKGKIEPFRPNSECSATPMQTAIGKESSNPLMAISLPKAEKKHSKASEVPSPHKTVKEFSEIPKDFLRPNQGIQIPKKNEDHSSSSSKEEKGIQNPKKDFYVVYNGPYAGIYDHWGTAKKATNKIPGVSYKKFKDMLSARTSADIYTNAQFGEKLKYIPGATTSPKSFAEALTTRPSNMKSLGKPKFIKIEEDDDVGFNPEFDLKSFLYIYKYGRNLEEEHFLTDRAFTIDKKEISYLNFVNNSDPEGILESFKAGLVRFIYPSTNLQELRLLPKVLKSSVQRFRKKCIKDSEKEIFLKIKSTIPCWEDYYNGLDDSVSYRPNYLVQIGISKGVNYQPSQKMEAVVLKEQWQGIAEEKAIEFFQAIEDILSNEKIFIIYCDDRILIYSSSPKERTKEDLMAILNFQSEVSSCKLLGFHSDKICSYLNKKASVGKPYSCPQKGKAVITSGPSFSVEDTLSDTE", "text": "FUNCTION: Enhances the translation of downstream ORFs on polycistronic mRNAs derived from carnation etched ring virus. SUBCELLULAR LOCATION: Host cytoplasm. Note=Found in cytoplasmic occlusion bodies. SIMILARITY: Belongs to the caulimoviridae viroplasmin family."}
{"protein": "MKTYAIIEAGGEQLQVEPGRFYNIRHLSLRGVNFWGQNTKLLLYRVLMIRHQSATVLGNPWVQNATVKGRILDARRDDKLVIYKMRAKKKTRRKRGHRQGLTRFVVDAICLNGKVLLD", "text": "FUNCTION: This protein binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family."}
{"protein": "MSKVFKKTSSNGKLSIYLGKRDFVDHVDTVEPIDGVVLVDPEYLKCRKLFVMLTCAFRYGRDDLEVIGLTFRKDLYVQTLQVVPAESSSPQGPLTVLQERLLHKLGDNAYPFTLQMVTNLPCSVTLQPGPEDAGKPCGIDFEVKSFCAENPEETVSKRDYVRLVVRKVQFAPPEAGPGPSAQTIRRFLLSAQPLQLQAWMDREVHYHGEPISVNVSINNCTNKVIKKIKISVDQITDVVLYSLDKYTKTVFIQEFTETVAANSSFSQSFAVTPILAASCQKRGLALDGKLKHEDTNLASSTIIRPGMDKELLGILVSYKVRVNLMVSCGGILGDLTASDVGVELPLVLIHPKPSHEAASSEDIVIEEFTRKGEEESQKAVEAEGDEGS", "text": "FUNCTION: May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins. SUBCELLULAR LOCATION: Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment. SIMILARITY: Belongs to the arrestin family."}
{"protein": "MKKKTYQFEKFLKNTFDQFSIKQNEVLVEDDLNDIIMNVCGKALVLMINEKREMNLLMGNTPEERYQYFENEYSSTGKAFEEIKDKFPVIYIDLKNSINSYLKLVSQIMKDFKKDYSLLVERKIIEEHSTISTMKIKGDLHNGKAVIEITTNKSKLIYKPKSLSNDVFFNNFLKYMDSFFIKEGKSTKYKENFYLVNTLDMKTYGWVEYVDKKPINSFEEARNYYRKIGVLLSVAYTLNLTDLHFENVISQGENPCIIDLETMFNMPMFVKDYKNESRNIINGKIMDSVVSTGMLPVLGIDSLFGGDPSGILGGTFSKEERVIINPFRDDIKFQKIVVRSVFKDHIPFFNNNNEKRYCKPKDYVNDIIKGFEKTYKIIVKNKEKILGFLKKESSSVTCRILFRNTMEYSVLLNAAKSPVYSNKREEIFEKLSTFNRGLGNDIIKSEISQINTLSIPYFNCQVDSNLIKNMDGETIFEHTLTPFKCFLSKYRRLCVDDMEQQVKLIRFSIQSQEQLFKDGEQFSLYKKQKGSQEDLLIAINELSSILENNAYIGTSDDTINWMSLGIADNDQILFESLENDIYKGISGIGLALLEYYEFYPNINTKKILKLIYKNISKDFINTNNEPQNYGFYVGLIGEYSFLRKYEKVFHKTSSCNILKNILKDFTPEKCQTILPSDDVIAGEAGIIIYISNLNNYLEYRDEIDILLKSLSNKIKLKESIASYAHGNSGIATAFVHGYKVTKNEKYLKIFHELWNLENSSKLRRGWTDSRKVDSSYSSQWCHGASGQAIARMEWITVNKTARFLSNSELIKVKKELGELIDILKKEGMYTDNFCLCHGILGNLLILNTYQENFDNKNINLKNEILNNYYSVCNYGLNKGWICGLGTEFYSYGLMTGISGILYGLIRQVKQKNNFGVLMPYVD", "text": "FUNCTION: Could be implicated in the processing or the export process of the lantibiotic lacticin 481/lactococcin DR."}
{"protein": "FNMESDSFEDLWKGEDFSNYSYSSDLPPSLPDVAPCRPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRYLVKFICLSIWGLSLLLALPVLLFRRTVYSSNVSPACYEDMGNNTANWRMLLRILPQSFGFIVPLLIMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYSLVLLADTLMRTQVIQETCERRNHIDRALDATEILGILHSCLNPLIYAFIGQKFRHGLLKILAIHGLISKDSLPKDSRPSFVGSSSGHT", "text": "FUNCTION: Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MPKYYCEYCDIYLTHSSPVGRRQHIQGRKHISAKIEYFQNLLREEGITPQNFLGFLGNRAFNNMLGNPMMNNMMPGNFPMHMKHGGMKHHSHYSRHSHRHHMSHGRYNRERHGHHSYSSKYHSHPMHMNSNSIGNPSGFSNGKYSGSFFSSPNAMHGNGKMFNNTIRDLVSNVNIDSDPVKDSQNGERVGDNAIDKVSSGMHDQGDRGDLGDHADHADHAGPVSATDGTANGNDQVSVDA", "text": "FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family."}
{"protein": "MKGVDDAFLGVGDKPGLDIWCIMGSNLIAIEKSLHGKFYTGNTYIILSTVELKSGVRQHNVHYWVGEEAKEEDCLTASDKAIELDVALGSNTVQYRETQGEESDKFLSYFKPCIIPIQGSLSSHMRIYGDKSKDTTMFRCEGEHVARVTEVPFSRSSLDHKAVFVVDTESKIFLFSGCNSSMQTRAKALDVVKHLKENRHCGRCEIATIEDGKLVGDSDAGDFWNLFGGYAPIPRDVQDTVMTELMTTSSKKLFWINKRNLVPVETNLLEREMLNSDRNYILDCGTEVFLWMGMTTLVSERRTSVTALEDYVRCEGRQSNARSVILTEGHETVEFKMHFQHWPKNAVPKLYEAGREKVAAIFKHQGYDVTEIPEDKPRHFISCNGSLKVWLVDNGSVTLLCTEEQEQLYNGDCYIIRYSYIEDGKDYHLFFAWSGLNSINEDRVAAASLMSGMIDSVKGHAVVAQVFEGREPEMFFLVFKSLIIFKGGRSMAYKNFVSQRSDANGWYQKNGVALFRVQGLKHDCIRAIQVDLAASSLNSSHCYILQAGGSFFTWLGSLSSPSDHNLLDRMMDKLCPLKQSLLVREGSEPDRFWEALGGRSEYLREKQVKDWPADPHLYTCHFEQGLFKAKEVFSFSQDDLVTEEILILDCVEELHIWVGHQSGVLSKEQALDIGKMFLQAGIHQDGRRPIDTTMYIVTEGDEPRFFTSFFNWDYSKQTMLGNSFERKLAILKGISQKLETPERSLRKSSSSSLPRRSPGTSSSEPTTPEQRAAARTFASASTGKLLRERSPAALSPSLSTPSPSPRSRSSASSSPASWNSTPSTVARRLFPPSLHASAEAVATGTPRRR", "text": "FUNCTION: Ca(2+)-independent actin-binding protein. Binds actin microfilaments (MFs). Involved in actin filament bundling, severing and capping. Caps the barbed end of actin filaments and protects them from disassembly. Promotes VLN3-mediated MF severing. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the villin/gelsolin family."}
{"protein": "MQQEKELVKQKAKELLLDLLSIYTPSKNETNATKFFEKISNEFNLKLEILPDSNSFILGEGEILLASHVDTVPGYIEPKIENEVIYGRGAVDAKGPLISMIIAAWLLNEKGIKVMVSGLADEESTSIGAKELTLKNFNFKHIIVGEPSNGTDIVVEYRGSIQLDIMCKSTPEHSSSAKSNLIVDISKKIIEVYKQPENYDKPSIVPTIIRAGESYNVTPAKLYLHFDVRYAINNKRDDLINEIKDKFQECGLKIVDETPPVKVSINNPVVKSLTRALLKQNIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLEHTNQEKITLDEIYIGVKTYMLAIEELWQKS", "text": "FUNCTION: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine and the release of L-ornithine from [LysW]-L-ornithine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20A family. LysK subfamily."}
{"protein": "MLSTKRLRVLELYSGIGGMHYALNLANIPADIVCAIDINPQANEIYNLNHGKLAKHMDISTLTAKDFDAFDCKLWTMSPSCQPFTRIGNRKDILDPRSQAFLNILNVLPHVNNLPEYILIENVQGFEESKAAEECRKVLRNCGYNLIEGILSPNQFNIPNSRSRWYGLARLNFKGEWSIDDVFQFSEVAQKEGEVKRIRDYLEIERDWSSYMVLESVLNKWGHQFDIVKPDSSSCCCFTRGYTHLVQGAGSILQMSDHENTHEQFERNRMALQLRYFTAREVARLMGFPESLEWSKSNVTEKCMYRLLGNSINVKVVSYLISLLLEPLNF", "text": "FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). Can also methylate cytosine 38 in tRNA(Glu), albeit to a lower level, but not tRNA(Lys). Pmt1-dependent tRNA methylation is induced by nitrogen limitation and depends on the nutrient-sensing protein kinase sck2. Does not have DNA-methylation activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
{"protein": "MRRIFLFDENSLNSSSTIDTSSASTIDTSFASQCTNFSSGQASGTQDTHAGIFEDCPGLNPNDERVVELQCEIREKCEALTQDPEMGLILGEALHAESDNVPFLQSIADDLTQNGVSGEAFQEALNIVGQAAASPLDQFEIVPLIPMHIGNFYFSFTNSSLFMLLTLSFFLLLIHFVTKKGGGNLVPNAWQSLVELLYDFVLNLVKEQIGGLSGNVKQMFFPCILVTFLFLLFCNLQGMIPYSFTVTSHFLITLALSFSIFIGITIVGFQRHGLHFFSFLLPAGVPLPLAPFLVLLELISYCFRALSLGIRLFANMMAGHSLVKILSGFAWTMLCMNDIFYFIGALGPLFIVLALTGLELGVAILQAYVFTILICIYLNDAINLH", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family."}
{"protein": "HQQFHCAAAEGQAKKSFSCKYCEKVYVSLGALKMHIRTHTLPCKCHLCGKAFSRPWLLQGHIRTHTGEKPFSCQHCNRAFA", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family."}
{"protein": "MLRFVSSQTCRYSSRGLLKTSLLKNASTVKIVGRGLATTGTDNFLSTSNATYIDEMYQAWQKDPSSVHVSWDAYFKNMSNPKIPATKAFQAPPSISNFPQGTEAAPLGTAMTGSVDENVSIHLKVQLLCRAYQVRGHLKAHIDPLGISFGSNKNNPVPPELTLDYYGFSKHDLDKEINLGPGILPRFARDGKSKMSLKEIVDHLEKLYCSSYGVQYTHIPSKQKCDWLRERIEIPEPYQYTVDQKRQILDRLTWATSFESFLSTKFPNDKRFGLEGLESVVPGIKTLVDRSVELGVEDIVLGMAHRGRLNVLSNVVRKPNESIFSEFKGSSARDDIEGSGDVKYHLGMNYQRPTTSGKYVNLSLVANPSHLESQDPVVLGRTRALLHAKNDLKEKTKALGVLLHGDAAFAGQGVVYETMGFLTLPEYSTGGTIHVITNNQIGFTTDPRFARSTPYPSDLAKAIDAPIFHVNANDVEAVTFIFNLAAEWRHKFHTDAIIDVVGWRKHGHNETDQPSFTQPLMYKKIAKQKSVIDVYTEKLISEGTFSKKDIDEHKKWVWNLFEDAFEKAKDYVPSQREWLTAAWEGFKSPKELATEILPHEPTNVPESTLKELGKVLSSWPEGFEVHKNLKRILKNRGKSIETGEGIDWATGEALAFGTLVLDGQNVRVSGEDVERGTFSQRHAVLHDQQSEAIYTPLSTLNNEKADFTIANSSLSEYGVMGFEYGYSLTSPDYLVMWEAQFGDFANTAQVIIDQFIAGGEQKWKQRSGLVLSLPHGYDGQGPEHSSGRLERFLQLANEDPRYFPSEEKLQRQHQDCNFQVVYPTTPANLFHILRRQQHRQFRKPLALFFSKQLLRHPLARSSLSEFTEGGFQWIIEDIEHGKSIGTKEETKRLVLLSGQVYTALHKRRESLGDKTTAFLKIEQLHPFPFAQLRDSLNSYPNLEEIVWCQEEPLNMGSWAYTEPRLHTTLKETDKYKDFKVRYCGRNPSGAVAAGSKSLHLAEEDAFLKDVFQQS", "text": "FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family."}
{"protein": "MEAEDEYSAGCSFSLMCQEDSTDLDDDGGGGGCFAGDGRADLLLVYNAAAAADDEDEEEVEEYMDHLVSKESSFCSSSSSTSSSSCCFSDAGGESAAAAAPMDWFALARRATVKWILETRGCFGFCHRTAYLAIAYFDRFCLRRCIDRSVMPWAARLLAVACVSLAAKMEEYRAPALSEFRAGVGDDGYEFSCVCIRRMELLVLSTLDWRMAAVTPFDYLPCLSSRLRRHVGGGGGAGASAALIFSAAEAASVLDHRPSTVAAAAVLAATHGALTREALESKMSGLSPSFLLDKEDVFACYSAMLSQPTSPASKSTTTTTGKRSSSSSCSESTDAASSYDATAASFPAAASCGSKRMRLELPGGILR", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily."}
{"protein": "MADLSFSDGDPTVRTLLRRVLETADSRTPMRRRSTRINAQRRRSQTPYSNRQGSQTKTSARKQSHGARSVGRSTRVQGRGRLEEQTPRTLLRNILLTAPESSTVMPDPVVKPAQVPEVARSSRRESSRGSLELHLPELEPPSTLAPGLTAPGKRKQKLRLSVFQQEVDQGLPLSQEPRRSRSADVSSLASSFNLTFVLPGQPETVERPGLARRRPIRQLVNAGALLQDLEDNSLASALPGDSHRTPVAALPMDVGLEDTQPFSQSLAAFSLSGKHSLPSPSRPGVEDVERVMGPPSSGTRLQSRMSRSGPAASPSPFLEPQPPPAEPREAVGSNEAAEPKDQEGSSGYEETSARPASGELSSSTHDSLPAEQPPPSPGVAVLSSEPLESVTAKCPSRTQTAGPRRRQDPHKAGLSPYVKFFSFCTKMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRRQGLVTDQVSQHVLVERYLPLEYRQQLIPCAFSGNSVFPAQ", "text": "FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3- containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Chromosome, centromere, kinetochore Note=Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore, and may connect it to the outer kinetochore via its N-terminus. SIMILARITY: Belongs to the CENP-T/CNN1 family."}
{"protein": "HAAFTVAHEIGHLLGLSHDDSKFCEENFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQIPGPEELPGQTYDASQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPKNNGRYCTGK", "text": "FUNCTION: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that shows proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration. Participates in the development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
{"protein": "MQWTKPAFTDLRIGFEVTMYFEAR", "text": "FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. PQQ is probably formed by cross-linking a specific glutamate to a specific tyrosine residue and excising these residues from the peptide (By similarity). FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. PQQ is probably formed by cross-linking a specific glutamate to a specific tyrosine residue and excising these residues from the peptide. SIMILARITY: Belongs to the PqqA family. SIMILARITY: Belongs to the PqqA family."}
{"protein": "MCKGLAALPHSCLERAKEIKIKLGILLQKPDSVGDLVIPYNEKPEKPAKTQKTSLDEALQWRDSLDKLLQNNYGLASFKSFLKSEFSEENLEFWIACEDYKKIKSPAKMAEKAKQIYEEFIQTEAPKEVNIDHFTKDITMKNLVEPSLSSFDMAQKRIHALMEKDSLPRFVRSEFYQELIK", "text": "FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm Membrane. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm."}
{"protein": "MPAARTGTLAAVALILLCGAAVLGRPAPDDLCFADVRRTGMAPSRPLGPVLNLAASDLTSRVSVRAVDASRGCALALLDMAETVVPGGPRAADVVDVGWAYQDGDCMVPLAYRQYFNCTGGALPGQNVCAGLSETRIRGGFGTSDYALYGTSLVLRPGLYDRGTYIYFLGYGPDDIYVGSVTLMVGADIHKYPCGLDRGLGVALHHKSGPARPLTEDDATGDWACGCFPAVVEVDVVWGNVSAAELGLADPIDYADEGGEVEVLEDEAGSASGNLPQDDPDPDLADCRTVGLFSESDMFRTARGPESLLIGAVAKDVLTVPLNLPPGRSYEALRNASLECNSRPRETGDAAVVVMSLQEPARLERRPDARATDPEFGLFGLPDDPAVRRGILIGLAIALLVLLFSLVIVLVCACRLARAAKAARRARAATFAKSNPAYEPMLRV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the herpesviridae glycoprotein G family."}
{"protein": "MILIPRMLLVLFLLLPILSSAKAQVNPAICRYPLGMSGGQIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVEPDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGYIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPNAISFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSEALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSDSSMFNNNRSSSPSEQGSNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPVQPSGPEGVPHYAEADIVNLQGVTGGNTYSVPAVTMDLLSGKDVAVEEFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQGDE", "text": "FUNCTION: Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416). It functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up- regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily."}
{"protein": "QICTNCCAGRKGCSYFSEDGTFICKGESNPENPKACPRNCDGRIAYGICPLS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I20 (potato type II proteinase inhibitor) family."}
{"protein": "MEKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIQIFKDIPTLEDLAETLKKEKLKAKGLAPSRKRKKEVDAASPAPSTSSTVKTEGAEATPGAQKRKKTTKEKSGPKGSKVSKEQTQPPCPAGAGMSTAMGRSPSPKTSSSAPPNTSSTENPKTVAKCQATPRRSVLQKGPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQKFEVPNKIINRAKETLKIDILHKQASGNIVYGVFTLHKKTVNQKTTIYKIQDDRGKMDVVGTGQCHNIPCEEGDKLQLYCFRLRKKNQMSTLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQSQLPNPSEAGTTFPESHLWTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEESHFPGPFMTSIGPAESYPHTPQMPPSTPSSSFLTTKSEDTISKMNDFMRMQILKEESHFPRPFMTSIGPAESYPHTPQMPPSTPSSSFLTTWKPKLQTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATEKEVFRVKVFNIDLKEKFTPKKIIAISNYVCRNGFLEVYPFTLVADVNADPKMEIPKGLIRSANITPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFF", "text": "FUNCTION: Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the HIN-200 family."}
{"protein": "MKAEFKRKGGGKVKLVVGMTGATGAIFGVRLLQWLKAAGVETHLVVSPWANVTIKHETGYTLQEVEQLATYTYSHKDQAAAISSGSFDTDGMIVAPCSMKSLASIRTGMADNLLTRAADVMLKERKKLVLLTRETPLNQIHLENMLALTKMGTIILPPMPAFYNRPRSLEEMVDHIVFRTLDQFGIRLPEAKRWNGIEKQKGGA", "text": "FUNCTION: Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions (PubMed:18388975). Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase (By similarity). SIMILARITY: Belongs to the UbiX/PAD1 family. YclB subfamily."}
{"protein": "MKMKVLEVVGLAISIWLMLTPPASSNIVFDVENATPETYSNFLTSLREAVKDKKLTCHGMIMATTLTEQPKYVLVDLKFGSGTFTLAIRRGNLYLEGYSDIYNGKCRYRIFKDSESDAQETVCPGDKSKPGTQNNIPYEKSYKGMESKGGARTKLGLGKITLKSRMGKIYGKDATDQKQYQKNEAEFLLIAVQMVTEASRFKYIENKVKAKFDDANGYQPDPKAISLEKNWDSVSKVIAKVGTSGDSTVTLPGDLKDENNKPWTTATMNDLKNDIMALLTHVTCKVKSSMFPEIMSYYYRTSISNLGEFE", "text": "FUNCTION: Possesses antiviral potency. Inhibits viral infection of plants (tobacco mosaic virus) (PubMed:10403789). Inhibits protein synthesis in both prokaryotes and eukaryotes (PubMed:8034016, PubMed:10403789). SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
{"protein": "MGKAALQDPHGGIWYFAYGSNLRLSVLENRGIKALDIKAVIVPSHYLTFDIFGIPYAEPSFASVAPFAREKKTTLRLGDSPASRDVPPVQGLAYLLNPRDYRQLVISEGGGVAYDEVEVHASILDKDGKPDPGATLIARTLQAKYPWRPNGAPSARYLGLISTGCKQNEPLTAYSDYIDSLPAYEPPTSLHAKVGGLLFLMFWRPPLRLLIRLIRVNTDQDGHCPQWLGWIILTLYGLMWSYHDNIHSKIWGRGDGRKLHFEETPAKEVPVRH", "text": "FUNCTION: Gamma-glutamyl cyclotransferase-like protein; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L- tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L- serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT- mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MFPSPALTPTPFSVKDILNLEQQQRSLASGDLSARLEATLAPASCMLAAFKPEAYSGPEAAASGLAELRAEMGPAPSPPKCSPAFPAAPTFYPGAYGDPDPAKDPRADKKELCALQKAVELDKAETDGAERPRARRRRKPRVLFSQAQVYELERRFKQQRYLSAPERDQLASVLKLTSTQVKIWFQNRRYKCKRQRQDQTLELLGPPPPPARRIAVPVLVRDGKPCLGDPAAYAPAYGVGLNAYGYNAYPYPSYGGAACSPGYSCAAYPAAPPAAQPPAASANSNFVNFGVGDLNTVQSPGMPQGNSGVSTLHGIRAW", "text": "FUNCTION: Transcription factor required for the development of the heart and the spleen (PubMed:9584153, PubMed:19483677, PubMed:22560297). During heart development, acts as a transcriptional activator of NPPA/ANF in cooperation with GATA4 (PubMed:9584153). May cooperate with TBX2 to negatively modulate expression of NPPA/ANF in the atrioventricular canal (PubMed:12023302). Binds to the core DNA motif of NPPA promoter (PubMed:19483677). Together with PBX1, required for spleen development through a mechanism that involves CDKN2B repression (PubMed:22560297). Positively regulates transcription of genes such as COL3A1 and MMP2, resulting in increased pulmonary endothelial fibrosis in response to hypoxia (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NK-2 homeobox family."}
{"protein": "MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE", "text": "FUNCTION: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. FUNCTION: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at mid-cell. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at mid-cell. SIMILARITY: Belongs to the ZapA family. Type 1 subfamily. SIMILARITY: Belongs to the ZapA family. Type 1 subfamily."}
{"protein": "MVKLRLKRYGRKKRPFYRVIAIDSRCRRDGKALKELGFYDPIAGKTQLDVPNIIFYLKAGAQTSETVGNLLQKAKVFNQLSLLN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MNLYLLLGALAIFSLVYDKKENSIFLYLLILFLVFIIVSPAIISKNTESTVEDIPSHKAKSVRKKLEIEQALDAILNKNTSSID", "text": "FUNCTION: Plays an essential role in budded virion (BV) and occluded derived virion (ODV) development. Participates in intranuclear microvesicle formation, ODV envelopment, and subsequent embedding of virions into occlusion bodies. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus."}
{"protein": "MSTQVLIVGGGIGGLTLAAMCRRIGVSCRVLERSAALEPVGAGISLAPNALRALDQIGLYDYVRQEGQPVRKIRVYRNQTQWSEIDFQWLERTFGYPVYSIERHGFHRRLYDAAGGSETVNLGAEVAKVIPPQEEAEGVSVVLKDGRRYTGNVLVGADGVRSVVRRALMATINSPPGQSGAVGEDEDAADVIQFTGRVHLSGYTHPLDHLGPADEGIAYWMLYDRSILTTWPCRDHRQWFVGAVPSKLKDPNRSVWKHADHNTINQVYGSEYHPFAPDFHFRDVVKHAERVVASDVFHQTTFPPMAAGRIAMLGDASHAMTSFFGQGACQAIEDATELASALGMIDVRPTDAETILQGYRHSRERRGRDLVVFSDRFALLHTGRLLGSWGPFVRQMVYTWMPLWGWKWALQWLYGHQPTLVEQRNEAAKKTA", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds (PubMed:24106156). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP (PubMed:24106156). The enoyl reducrase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine (PubMed:24106156, PubMed:26414728). Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J (PubMed:26414728). The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation (PubMed:26414728). The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro- gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H (PubMed:26414728). Pyranonigrin H is substrate of pynH for dehydration- mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G (PubMed:26414728). The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E (PubMed:26414728). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
{"protein": "MAMKLYGDEMSACVARVLLCLHEKNTEFELVPVNLFACHHKLPSFLSMNPFGKVPALQDDDLTLFESRAITAYIAEKHRDKGTDLTRHEDPKEAAIVKLWSEVEAHHFNPAISAVIHQLIVVPLQGESPNAAIVEENLENLGKILDVYEERLGKTKYLAGDTYTLADLHHVPYTYYFMKTIHAGLINDRPNVKAWWEDLCSRPAFLKVSPGLTVAPTTN", "text": "FUNCTION: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Phi family."}
{"protein": "MKLMIFTGLVLFAIVRLIEAQAENEKPCLPEYKVCTHAPGNCCSDLVCDCYGRYKSGAQIGRNCFCLQKGVIYKREN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 08 (U8-Lctx) subfamily."}
{"protein": "MAVARARVLGVQWLQRASRNVMPLGARTASHMTKDMFPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPKLPDRSQHERDPWYSWDQPGLRLNWGEPMHWHLDMYNRNRVDTSPTPISWHVMCMQLFGFLAFMIFMCWVGDVYPVYQPVGPKQYPYNNLYLERGGDPSKEPERVVHYEI", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFB8 subunit family."}
{"protein": "MLQTFPRVAKCVRAYSSKPTLGPKFQSLDEIKEYIFKDTISANEFLTQSERAKDRELPVPPRETVLKLLKLSGLPTKGADIERIQRNLSEQISFINILHDTDLDDSLNVKYARLLPRENATLSYGDLIVRANSGKNSELAEISGSWDSTSRASMRKDGYFIVREEFLDNRD", "text": "FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for proper protein synthesis within the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the GatF family."}
{"protein": "MHVPIRLLEWFKVEQTLVIQKKKRFGFSQGIGITLLIAIVAKYLAELPFLNIMGQLVIAILIGMVWRAAIGVPHDAIAGTNFASKKLLRFGIILLGMRLNLVDIAKAGPKVLVIAAVVITFTIFVVYGLTKVFKVEKKLGILTACGTAICGAAAVVAIAPQVKAKDDETAVGAAIIAILGTIFTLIYTLLYPVLGLSPYGYGVFSGATLHEIAHVIAAAAPGGSAAVDIAVIVKLTRVAMLVPVAILIGLWFGKSEGSKEKRSWRDLPIPWFIFGFLAMSAVHSLGIIPEVVAGYIVVIAYMLIAMAMAGLGLNVEFKTFRKLGSKAFVAGLIGSVCLSVLGYVLVYALGFM", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0324 family."}
{"protein": "MDESLAELGEHILGTLEESVLGFHVAFGELNVLAQAQSIARVLKFLRDDPACRFGTLLDITAVDYPQRPERFDVVYHLLSMHQNQRIRVTVRTNEETAVPSVVAVYPSANWYERETFDMYGVLFSDHPDLRRILTDYGFNGYPLRKDFPLTGYVEVRYDDDEKRVVYEPVKLVQEFRNFDFMSPWEGAEYLLPGDEKAEH", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 30 kDa subunit family."}
{"protein": "MAAAPSHPAGLPGSPGPGSPPPPGGLDLQSPPPLLPQIPAPGSGVSFHIQIGLTREFVLLPAASELAHVKQLACSIVDQKFPECGFYGLYDKILLFKHDPTSANLLQLVRSAADIQEGDLVEVVLSASATFEDFQIRPHALTVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNCSGARKRRLSSTSLASGHSVRLGSSESLPCTAEELSRSTTDLLPRRPPSSSSSSSSSSFYTGRPIELDKMLMSKVKVPHTFLIHSYTRPTVCQACKKLLKGLFRQGLQCKDCKFNCHKRCATRVPNDCLGEALINGDVPMEEAADYSEADKSSISDELEDSGVIPGSHSESALHASEEEEGEGHKAQSSLGYIPLMRVVQSVRHTTRKSSTTLREGWVVHYSNKDTLRKRHYWRLDCKCITLFQNNTTNRYYKEIPLSEILAVEPAQNFSLVPPGTNPHCFEIITANVTYFVGETPGGAPGGPSGQGTEAVRGWETAIRQALMPVILQDAPSAPGHTPHRQASLSISVSNSQIQENVDIATVYQIFPDEVLGSGQFGVVYGGKHRKTGRDVAVKVIDKLRFPTKQESQLRNEVAILQSLRHPGIVNLECMFETPEKVFVVMEKLHGDMLEMILSSEKGRLPERLTKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLLNQGYNRSLDMWSVGVIMYVSLSGTFPFNEDEDINDQIQNAAFMYPASPWSHISSGAIDLINNLLQVKMRKRYSVDKSLSHPWLQEYQTWLDLRELEGKMGERYITHESDDARWDQFVAERHGTPAEGDLGGACLPQDHEMQGLAERISIL", "text": "FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:17226786, PubMed:20819079). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (PubMed:17226786). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-718 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (By similarity). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (By similarity). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (PubMed:20819079). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (By similarity). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (By similarity). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (By similarity). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (By similarity). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (By similarity). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Golgi apparatus, trans-Golgi network Note=Translocation to the cell membrane is required for kinase activation. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuclear accumulation is regulated by blocking nuclear export of active PRKD2 rather than by increasing import. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily."}
{"protein": "MAASSEEETDRRPIRRVRSKSDTPYLAEVRISLNLETAEEVERLAAMRSDSLVPGTHTPPIRRRSKFATLGRLFKPWKWRKKKSEKFKQTSAALERKISMRQSREELIKRGVLKEMYDKDGDLHNEEGLMENGQAVSSGSSSLPIITELELTSMAGDTCAYEVLPTSELMDGTVSEDLSSEPGSLSQDPSYKPAMLLPPKKTVGFPVDQEDTPVKQITLLKQPPALPPKPISRIANHIADSGAPVKLPCMPGKMSPPLPPKKVMICMPLGGTDFPYGPYSNQKSSQHHHTVLPSQLAAHQLQYGSQHFSTGSSSISIHPSIPPGCRVIEELNKTLAMTMQRLESSGLHGGESITKSGLSGYCDMRQVPTVVIECEDDKENVPHETSYDDSSCLYSRDEEEDDDDDDDDEDDDSSLYTNSLALKVLRKDSLAIKLSNRPSKRELEEKNILPMQTDEERLESRQQIGTKLTRRLSQRPTAEELEQRNILKPRNEQEEQEEKREIKRRLTRKLSQRPTVEELREKKILISFSDYVELADAQDYDRRADKPWTRLTAADKAAIRKELNEFKSTEMEVHELSRHLTRFHRP", "text": "FUNCTION: Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. SUBCELLULAR LOCATION: Cytoplasm Synapse Nucleus Note=Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import (By similarity). SIMILARITY: Belongs to the phosphatase and actin regulator family."}
{"protein": "MTTLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAIEAGTSSDALTTAVAGLGYEATLADAPPTDNRAGLLDKMRGWIGAADKPSGNERPLQVVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRVAHIAHLRRESPFDGGMPPTSPTILRERLLAQQQARVEELRHAKYEGILDGNSAITVLHGEARFKDDQSLIVSLNEGGERVVMFDRCLVATGASPAVPPIPGLKESPYWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHMDGEFVLTTTHGELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFSKDVKQLSCCAG", "text": "FUNCTION: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MGLLSKKASCNTHGQDSSYFWGWEEYEKNPYDEIKNPDGIIQMGLAENQLSFDLIESWLAKNPDAANFQREGQSIFRELALFQDYHGLPSFKNAMADFMSENRGNRVSFNPNKLVLTAGATPANETLMFCLADPGDAFLLPTPYYPGFDRDLKWRTGAEIVPIQCKSANGFRITKVALEEAYEQAQKLNLKVKGVLITNPSNPLGTTTTRTELNHLLDFISRKKIHLISDEIYSGTVFTNPGFISVMEVLKDRKLENTDVFDRVHIVYSLSKDLGLPGFRVGVIYSNDDFVVSAATKMSSFGLISSQTQYLLSALLSDKTFTKNYLEENQIRLKNRHKKLVSGLEAAGIECLKSNAGLFCWVDMRHLLKSNTFEAEIELWKKIVYEVKLNISPGSSCHCNEPGWFRVCFANLSEETLKVALDRLKRFVDGPSPTRRSQSEHQRLKNLRKMKVSNWVFRLSFHDREPEER", "text": "FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MELVMKDAQSLTVSETTFGRDFNEALVHQVVVAYAAGARQGTRAQKTRAEVTGSGKKPWRQKGTGRARSGSIKSPIWRSGGITFAAKPQDHSQKVNKKMYRGALKSILSELVRQDRLIIVEKFAVEAPKTKLLVQKLKDMALEDVMIVTHEVDENLFLAARNLYKVDVRDVTAIDPVSLIAFGKVVMTAEAVKQVEEMLA", "text": "FUNCTION: Forms part of the polypeptide exit tunnel. FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). FUNCTION: This protein when expressed in E.coli represses both transcription and translation of the endogenous S10 operon. As the M.morganii S10 leader can be regulated in vitro by the E.coli L4 protein this strongly suggests the endogenous protein controls its own S10 operon in a similar fashion. FUNCTION: Protein L4 is a both a transcriptional repressor and a translational repressor protein. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader. L4 controls the translation of the S10 operon by binding to its mRNA (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uL4 family."}
{"protein": "MSYYDIDAILTDAEPLKAGTKVNLPLWLAEMLAIANTGDVEGKSFVSFDLPPAMGNDVVQALKADPRAVPLRDHSAHFYGLAIHMMELSEEQELAAALRKTFITRASEVALHAQGPEQDATGRWISIDLIHIDLTRARRLGQLGSRPSNRGLGSASPIPEHCAPHMTKNDELRPLQPADTEVGELLLSLHIELSHPTPTMFSRSDPT", "text": "FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GINS3/PSF3 family."}
{"protein": "MTENTKTHVILLSCGSFNPITKGHIHMFEKAREYLHKTGRFIVIGGIVSPVHDSYGKPGLVPSRHRLTMCQLAVQSSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSTTPVIGQPQNETSAIYQNTVNKSVAIKFWGKMSESLGKICCVRPHMDRFTFVDENANLGTAMRYEEIELRILLLCGSDLLESFCIPGLWNESDMEVIVGDFGIVVVPRDGADTERIMNHSSVLRKHKDNIIVVKDEIDHPMSIVSSTKSRLALQHGDGHVVDYLSQPVIDYILQSQLYINASG", "text": "FUNCTION: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor. Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons. Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16. SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor Cytoplasmic vesicle membrane; Lipid-anchor Cytoplasm Cell projection, axon Note=Delivered to axons with Golgi- derived cytoplasmic vesicles. SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family."}
{"protein": "MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGNDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQSGTAVSLEEKPLQPKSNYAVTGLYFYDNSVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEEIAYRKGFIDAEQIKNLAKPLSKNAYGQYLLNMIKGY", "text": "FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase family."}
{"protein": "MGLPRRAGDAAELRKSLKPLLEKRRRARINQSLSQLKGLILPLLGRENSNCSKLEKADVLEMTVRFLQELPASSWPTAAPLPCDSYREGYSACVARLARVLPACRVLEPAVSARLLEHLWRRAASATLDGGRAGDSSGPSAPAPAPASAPEPASAPVPSPPSPPCGPGLWRPW", "text": "FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MILLLLALISATTAFQGDVVNLTLNEQATVTLDECMYFLDTLQNSSTLPPGEYGIKITHSCLGNEQIEIRTNTTTDVITIKVEKDPNPEESLVEAENEVLSLRKEVQRLEGEVSYYKKLFEVLNKINVDLYDKLQNLATENDELKRELELYKSKAGNYSQLIDELRLELSKMNETVRQLQATNEDLQANLTKIDAELSRASANLELFQTLFFVTLSFLVGSAFALMRR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: To A.fulgidus AF_1225."}
{"protein": "MEISWGRALWRNFLGQSPDWYKLALLIFLIINPLIFLVNPFIAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVMIGMTSPSHVRAEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKALLSLSFCLAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRGEDNDILDDSHIDQHFKVILEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWSFGDFFLRMSPITVPVLVCGLLTCLLVERMGWFGYGEKLPEKVRQVLQQYDDQSRLQRTRQDKVRLIVQALIGIWLVIALALHLAEVGLIGLSVIIMATSLTGVTDEHAIGKAFTESLPFTALLTVFFSIVAVIIDQSLFSPIIHFVLQASEHAQLTLFYLFNGLLSSISDNVFVGTIYINEAKAAMENGTISLNQFELLAAAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTIVLTCVGLLCVEFTLAPMTEWMTQQGWLATLS", "text": "FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter family."}
{"protein": "MRTLISHRQCVTSPFLISAASPPFPGRCFKLSSFTPPRHRRFSSLSIRNISHESADQTSSSRPRTLYPGGYKRPELAVPGLLLRLDADEVMSGNREETLDLVDRALAKSVQIVVIDGGATAGKLYEAACLLKSLVKGRAYLLIAERVDIASAVGASGVALSDEGLPAIVARNTLMGSNPDSVLLPLVARIVKDVDSALIASSSEGADFLILGSGEEDTQVADSLLKSVKIPIYVTCRGNEEAKEELQLLKSGVSGFVISLKDLRSSRDVALRQSLDGAYVVNNHETQNMNELPEKKNSAGFIKLEDKQKLIVEMEKSVLRETIEIIHKAAPLMEEVSLLIDAVSRIDEPFLMVIVGEFNSGKSTVINALLGKRYLKEGVVPTTNEITFLCYSDLESEEQQRCQTHPDGQYVCYLPAPILKDINIVDTPGTNVILQRQQRLTEEFVPRADLLVFVLSADRPLTESEVAFLRYTQQWKKKFVFILNKSDIYRDARELEEAISFVKENTRKLLNTENVILYPVSARSALEAKLSTASLVGRDDLEIADPGSNWRVQSFNELEKFLYSFLDSSTATGMERIRLKLETPMAIAERLLSSVEALVRQDCLAAREDLASADKIISRTKEYALKMEYESISWRRQALSLIDNARLQVVDLIGTTLRLSSLDLAISYVFKGEKSASVAATSKVQGEILAPALTNAKELLGKYAEWLQSNTAREGSLSLKSFENKWPTYVNSKTQLGIDTYDLLQKTDKVSLKTIQNLSAGTTSKRLEQDIREVFFVTVGGLGAAGLSASLLTSVLPTTLEDLLALGLCSAGGYVAIANFPYRRQAIIGKVNKVADALAQQLEDAMQKDLSDATSNLVNFVNIVAKPYREEAQLRLDRLLGIQKELSDIRSKLQLLQVDIDNLHVSRDEMRL", "text": "FUNCTION: Probable membrane-remodeling GTPase that plays a unique role in the in the determination of thylakoid and chloroplast morphology and regulates organization of the thylakoid network. Not involved in the determination of mitochondrial morphology or ultrastructure. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein Note=Localizes in a punctate pattern in chloroplasts. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily."}
{"protein": "MSSPMPQSSLNNSQVANMIDESNETPSTTPPMISNTNTPVPEIEMEEPNAPQDNTVAPNSIDGEKVQEENEDDDEQEEEEEEEEEEEESLSLPLSKIKKIFKMDPDYLAASQSAVYATGLATELFIQYFTEQSLVLAKMDKRKKLQYKDFSNAVASQDSLNFLSDTVPKTQPIGELINSKKVNVNSHDNNEIREIDNTEIDEIEVDEPVNATRKVKPLAKGQQTLNFSATNTATESINPMPIKKSVISDIVTTDNETEVTSKEATEEVEDQDVIMIN", "text": "FUNCTION: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTENHTPSTTQPTLPAPVAEAAPIQANPAPSASVTATAAAATAAVNNAPSMNGAGEQLPCQWVGCTEKSPTAESLYEHVCERHVGRKSTNNLNLTCQWGTCNTTTVKRDHITSHIRVHVPLKPHKCDFCGKAFKRPQDLKKHVKTHADDSEIRSPEPGMKHPDMMFPQNPRGSPAATHYFESPINGINGQYSHAPPPQYYQPHPPPQAPNPHSYGNLYYALSQGQEGGHPYDRKRGYDALNEFFGDLKRRQFDPNSYAAVGQRLLGLQALQLPFLSGPAPEYQQMPAPVAVGGGGGGYGGGAPQPPGYHLPPMSNVRTKNDLINIDQFLEQMQNTIYESDENVAAAGVAQPGAHYVHGGMNHRTTHSPPTHSRQATLLQLPSAPMAAATAHSPSVGTPALTPPSSAQSYTSNRSPISLHSSRVSPPHEEAAPGMYPRLPAAICADSMTAGYPTASGAAPPSTLSGAYDHDDRRRYTGGTLQRARPAERAATEDRMDISQDSKHDGERTPKAMHISASLIDPALSGTSSDPEQESAKRTAATATEVAERDVNVAWVEKVRLLENLRRLVSGLLEAGSLTPEYGVQTSSASPTPGLDAMEGVETASVRAASEQAREEPKSESEGVFYPTLRGVDEDEDGDSKMPE", "text": "FUNCTION: Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including PACC itself) and represses transcription of acid- expressed genes. Specifically recognizes and binds the consensus sequence 5'-GCCARG-3'. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pacC/RIM101 family."}
{"protein": "MLTRRMQCLRGAGVFRTVAALPLLAQRPNFYRPLTCSALRRNNDHSYRHESRKDKEMQDLKESRKMREQEALDDAAFRNTFEFAVEKTRDSDGKSPEPEVEIDVDREAQTPWDPVGSQSRHETRQEHRERFDDIKKTLPSSVHESQPQMYKWFGEKMDQIQAGALTAGQTLNEVTGYKAIEKLKLSIEKLEDEVLEARAEVREAKRMYSDAISERSNSQREVNELLQRKHNWTPADLERFTELYRNDHANEHSVNDAKKRLGECEHHVEDLTLQLSKQILTRYHEEQIWSDKIRRASTWGTWILMGFNVVLFIVVQLGLEPWKRRRLVGSFEDKVKESLQEWEARNEARRLEEATMAATATQAITELQRRIESPHVSKADVVEAEAEINSIKTNLATWFKEREEEEKEEIAKEAHELAVIAEDPDMTDVHHKPHPPQPVDTERVVRPHLVENFEHHVADPVHHPTLPITSTPVLEEDAPPPRIHPLVQMSPDSPDDGTKTFTATRDGYDVHPLVVRPTTPPHFMLQVWGAAKLSVESATNKTVAVVRSTFQTAEQRPFESTIVASLGGLCGGLVTFLYLR", "text": "FUNCTION: Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SHE9 family."}
{"protein": "MTSAQNESQALGDLAARQLANATKTVPQLSTITPRWLLHLLNWVPVEAGIYRVNRVVNPEQVAIKAEAGAGSEEPLPQTYVDYETSPREYTLRSISTLVDIHTRVSDLYSSPHDQIAQQLRLTIETIKERQELELINSPEYGLLAQATPEQTIQTLAGAPTPDDLDALITKVWKTPSFFLTHPLGIAAFGREATYRGVPPPVVSLFGAQFITWRGIPLIPSDKVPVEDGKTKFILVRTGEERQGVVGLFQPGLVGEQAPGLSVRFTGINQSAIATYLVTLYTSLAVLTDDALAVLDDVAVDQFHEYK", "text": "FUNCTION: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers, probably involved in sulfur metabolism (By similarity). Probably encapsulates cysteine desulfurase (Probable). SUBCELLULAR LOCATION: Encapsulin nanocompartment Cell membrane. SIMILARITY: Belongs to the encapsulin family. Family 2A subfamily."}
{"protein": "MAGFPGKEAGPPGGWRKCQEDESPENERHENFYAEIDDFAPSVLTPTGSDSGAGEEDDDGLYQVPTHWPPLMAPTGLSGERVPCRTQAAVTSNTGNSPGSRHTSCPFTLPRGAQPPAPAHQKPTAPTPKPRSRECGPSKTPDPFSWFRKTSCTEGGADSTSRSFMYQKGFEEGLAGLGLDDKSDCESEDESNFRRPSSHSALKQKNGGKGKPSGLFEHLAAHGREFSKLSKHAAQLKRLSGSVMNVLNLDDAQDTRQAKAQRKESTRVPIVIHLTNHVPVIKPACSLFLEGAPGVGKTTMLNHLKAVFGDLTIVVPEPMRYWTHVYENAIKAMHKNVTRARHGREDTSAEVLACQMKFTTPFRVLASRKRSLLVTESGARSVAPLDCWILHDRHLLSASVVFPLMLLRSQLLSYSDFIQVLATFTADPGDTIVWMKLNVEENMRRLKKRGRKHESGLDAGYLKSVNDAYHAVYCAWLLTQYFAPEDIVKVCAGLTTITTVCHQSHTPIIRSGVAEKLYKNSIYSVLKEVIQPYRADAVLLEVCLAFTRTLAYLQFVLVDLSEFQDDLPGCWTEIYMQALKNPAIRSQFFDWAGLSKVISDFERGNRD", "text": "FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors. SUBCELLULAR LOCATION: Virion tegument. Host nucleus Note=Localizes to the centrosome and more precisely to the periphery of the centriole, tightly encircling the tubulin-rich centrioles. SIMILARITY: Belongs to the herpesviridae thymidine kinase family."}
{"protein": "MMMDILMYLFETYIHSDSELQVDQDELEDELLRAGFHQDDIYKALHWLEDLAALQDTENQAAITMCSNTSMRIYTSREISRINMECRGFLLFLEQINVLTTEIREMVIDRVMGLETSEFELDDLKWIILMVLFNVPGNESAYTQMEELLYTKEQGILH", "text": "SIMILARITY: Belongs to the Smg family."}
{"protein": "MSEAEASVVATAAPAATVPATAAGVVAVVVPVPAGEPQKAGGGAGGGGGAASGPAAGTPLHAPGPRTPGNQATAASGTPAPPARSQADKPVLAIQVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKRNNPRKFLRSVGDGETVEFDVVEGEKGARAANVTGPGGVPVKGSRYAPNRRRFRRFIPRPRPAAPPPMVAEAPSGGTEPGSEGERAEDSGQRPRRRRPPPFFYRRRFVRGPRPPNQQQPIEGSDGVEPKETAPLEGDQQQGDERVPPPRFRPRYRRPFRPRPPQQPTTEGGDGETKPSQGPTDGSRPEPQRPRNRPYFQRRRQQPPGPRQPIAAETSAPINSGDPPTTILE", "text": "FUNCTION: Major constituent of messenger ribonucleoprotein particles (mRNPs) (PubMed:10076007, PubMed:12297523, PubMed:12648488). Involved in the regulation of the stability and/or translation of germ cell mRNAs (PubMed:15031116). Binds to Y-box consensus promoter element (PubMed:10076007, PubMed:12297523, PubMed:12648488). Binds to full- length mRNA with high affinity in a sequence-independent manner (PubMed:10076007, PubMed:12297523, PubMed:12648488). Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity (PubMed:10076007, PubMed:12297523, PubMed:12648488). Its binding with maternal mRNAs is necessary for its cytoplasmic retention (PubMed:10076007, PubMed:12297523, PubMed:12648488). May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (PubMed:15665108). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "LKCKNKLVPFLSKTCPEGKNLCYKMTLKKVTPKIKRG", "text": "FUNCTION: Hemextin AB complex: specifically inhibits the activation of FX (F10) by the TF-FVIIa complex (extrinsic tenase complex (ETC)) (IC(50)= 100 nM, Ki=25 nM) by non-competitively inhibiting the enzymatic activity of FVIIa. FUNCTION: Hemextin A (monomer): exhibits mild anticoagulant activity. It specifically inhibits the activation of FX (F10) by the TF-FVIIa complex (extrinsic tenase complex (ETC)) by non-competitively inhibiting the enzymatic activity of FVIIa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IB cytotoxin sub-subfamily."}
{"protein": "MPCSTEAMEKAGHGHASTPRKRSLSNSSFRLRSESLNTLRLRRIFDLFDKNSDGIITVDELSRALNLLGLETDLSELESTVKSFTREGNIGLQFEDFISLHQSLNDSYFAYGGEDEDDNEEDMRKSILSQEEADSFGGFKVFDEDGDGYISARELQMVLGKLGFSEGSEIDRVEKMIVSVDSNRDGRVDFFEFKDMMRSVLVRSS", "text": "FUNCTION: Could be involved in calcium metabolism in pollen. Binds 3 calcium ions."}
{"protein": "MLSSIKCVLVGDSAVGKTSLLVRFTSETFPEAYKPTVYENTGVDVFMDGIQISLGLWDTAGNDAFRSIRPLSYQQADVVLMCYSVANHNSFLNLKNKWISEIRSNLPCTPVLVVATQTDQREVGPHRASCINAIEGKRLAQDVRAKGYLECSALSNRGVQQVFECAVRTAVNQARRRNRRKLFSINECKIF", "text": "FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. Inhibits the activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38 by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively regulates leukotriene production in neutrophils (By similarity). Negative regulator of hematopoietic progenitor cell proliferation, survival and migration. Critical regulator of thymocyte development and T-cell antigen receptor (TCR) signaling by mediating recruitment and activation of ZAP70 (PubMed:17028588). Required for phosphorylation of CD3Z, membrane translocation of ZAP70 and subsequent activation of the ZAP70-mediated pathways. Essential for efficient beta-selection and positive selection by promoting the ZAP70-dependent phosphorylation of the LAT signalosome during pre-TCR and TCR signaling. Crucial for thymocyte maturation during DN3 to DN4 transition and during positive selection. Plays critical roles in mast cell function by facilitating phosphorylation of SYK in Fc epsilon RI-mediated signal transduction. Essential for the phosphorylation of LAT, LCP2, PLCG1 and PLCG2 and for Ca(2+) mobilization in mast cells. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor; Cytoplasmic side Note=Colocalizes together with ZAP70 in the immunological synapse. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MGFNNLVSLAALIEKVFPIRYTPAGIPVLDIILKHESWQEENGQQCLVQLEIPARILGRQAEEWQYRQGVYVHVEGFLAQKSRRSLMPMLRIQNIQEYKG", "text": "FUNCTION: Stimulates the DNA unwinding activity of PriA helicase, which does not seem to require single-stranded DNA-binding by PriB. Activates DNA-dependent ATP hydrolysis catalyzed by PriA. SIMILARITY: Belongs to the PriB family."}
{"protein": "MQSTSKYNCDSDYIAGRNYNTKRTNGREELSTGLTNEETGVVNISDENNIFFKKNIDYVKGSRIGKYKLIKTLGKGSCAKVVQAEDCETGEYVAIKIIERTPKQLSDIRIYREALICSLFNHPHIIKLLDFFHTTEYFFLIFEYVDGQQLYDIILNKGYLDEDEARKYFRQIISAVDYSHRNSVVHRDLKIENILIDRNDNIKLIDFGLSNFYDADDLLGTFCGSLYFAAPELLLGTRYTGPEIDVWSLGVILYVMLVGKVPFDDENIHALQNKIKSCKFKFEKTISPEAQDLITNMILSSDARINLENVKKSKWTNLGYKNLTNNFMTLRKPIIEINKNILRALQAAMFFQFTDMERVLMQYLQICKGDKHSLEQTYWCKKPVVILYYLTMEKFNELNYKSIPIDIDTGMNTKSLIDITIEKQPIIIYNFVRFTNAKKNNNPYNLFFSRSVFEPEMEFLNMTKDVSLDSCNISEDENKKHNFPKIKQSIIKGLFKGIKIKNGDKDYVKNAIIKILLDLDITYEANEKSYFCSYSHSGVECHFKIDLYFNILLLEHYVVLNCLNRKKDNFKLVTELIKEKLEEIGDTSNYPENAI", "text": "FUNCTION: Serine/threonine protein kinase involved in regulation of exocytosis. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily."}
{"protein": "MTGREGGKKKPLKQPKKDGKEMDEEDMAFKQKQKEQQKAMEAAKQKAAKGGPLVTGGIKKSGKK", "text": "SIMILARITY: Belongs to the TMA7 family."}
{"protein": "MMRARVPLLLLGILFLASLSASFATSLREEEESQDNPFYFNSDNSWNTLFKNQYGHIRVLQRFDQQSKRLQNLEDYRLVEFRSKPETLLLPQQADAELLLVVRSGSAILVLVKPDDRREYFFLTSDNPIFSDHQKIPAGTIFYLVNPDPKEDLRIIQLAMPVNNPQIHEFFLSSTEAQQSYLQEFSKHILEASFNSKFEEINRVLFEEEGQQEGVIVNIDSEQIKELSKHAKSSSRKSLSKQDNTIGNEFGNLTERTDNSLNVLISSIEMEEGALFVPHYYSKAIVILVVNEGEAHVELVGPKGNKETLEYESYRAELSKDDVFVIPAAYPVAIKATSNVNFTGFGINANNNNRNLLAGKTDNVISSIGRALDGKDVLGLTFSGSGDEVMKLINKQSGSYFVDAHHHQQEQQKGRKGAFVY", "text": "FUNCTION: Major seed storage protein. SUBCELLULAR LOCATION: Vacuole, aleurone grain. Vacuole. Note=Cotyledonary membrane-bound vacuolar protein bodies. SIMILARITY: Belongs to the 7S seed storage protein family."}
{"protein": "MSGQSLTDRITAAQHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDFTKVKRGADGVMRTMNTEKLLKTVPIIQNQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLKVAEQVGIDRGDIPDLSQAPSSLLDALEQHLASLEGKKIKDSTAASRATTLSNAVSSLASTGLSLTKVDEREKQAALEEEQARLKALKEQRLKELAKKPHTSLTTAASPVSTSAGGIMTAPAIDIFSTPSSSNSTSKLPNDLLDLQQPTFHPSVHAMSAAPQVASTWGDAVDDAIPSLNPFLTKSSGDVHLPISSDVSTFTTRTPTHEMFVGFSPSPVTQPHPSAGLNVDFESVFGNKSTNVAVDSGGGLLKPTVASQNQSLPVAKLPPNKLVSDDLDSSLANLVGNLGIGNGTTKNDVSCSQPGEKKLTGGSNWQPKVAPTTAWSAATMAPPVMAYPATTPTGMIGYGIPPQMGSVPVMTQPTLIYSQPVMRPPNPFGPVPGAQIQFM", "text": "FUNCTION: Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly. Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature. In addition to binding to clathrin, mediates the endocytosis of small R- SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8. In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors. Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF). SUBCELLULAR LOCATION: Cell membrane Membrane, clathrin-coated pit Golgi apparatus Cytoplasmic vesicle, clathrin-coated vesicle Nucleus Note=Colocalized with clathrin in the Golgi area. Interaction with PIMREG may target PICALM to the nucleus in some cells. SIMILARITY: Belongs to the PICALM/SNAP91 family."}
{"protein": "MANSFPLRVLPTIDPSAGHTFITPSKRIHESEDVSEFLISKAYVDIMTFLLQLNRAMIPVKLADGTVQSWPINTDAVEFSAPVRQLQQLLTKLEELLAEAPPDTGPRRFGNISFRRWYELVESRASELLGECLPSELLQAKSSDPNSVTAEAELKAYFLGSWGSPQRLDYGTGHELSFLAFLAGIWKLNGFPKTTPGVEERAIVLGVIQPYLELVRTIIKRYTLEPAGSHGVWGLDDHSFIPYILGSAQLAPAISETDPTPEEGSLPGAPSPNGVTKAHIVERERLTNMYFSAIGFIYDVKKGPFWEHSPMLYDISGIQAGWGKINKGMIKMYNAEVLSKFPVVQHFPFGSLFSWDRDPNAVPPPTSAHMSTTQSQSRGPAVPSAGQTPPSGTRAPWATATQAAPPAGAGTAAPWAAKRDGCTPGKPPTSLPDTSRLPPGPMAPTRAPWAASSTGQAPGGDPTHVPTKAPWAK", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A- phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PTPA-type PPIase family."}
{"protein": "MLAVQNMKFGIFLLWWGWVLAAESTAHWPGREVHEPSRKGSRPQRQRRGAHDDAHKQGSPILRRSSDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSSNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKERKLREKISCTCGLPQPRGVMLDSSYSDGEVNDLGGYMPENGEKPDRMMVQLTLASERGSPQRKGQRGSYVSMRINTHAIDKYSRIIFPAAYILFNLIYWSIFS", "text": "FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission (By similarity). SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi- pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRR1 sub- subfamily."}
{"protein": "MLLILLSVALLALSSAQSLNEDVSQEESPSVISGKPEGRRPQGGNQPQRTPPPPGKPEGRPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGQPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPHPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGSPSQGGNKPQGPPPHPGKPQGPPPQEGNKPQRPPPPGRPQGPPPPGGNPQQPLPPPAGKPQGPPPPPQGGRPHRPPQGQPPQ", "text": "FUNCTION: Acts as a receptor for the Gram-negative bacterium F.nucleatum. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MIKHIEAFLASKTISENTLKSYRYDLNQFLMLIDHKLSDEKLVLYQKSLNHLSASAKKRKFSTVNQFLHYLYKVNVTDRFFELSGKVSLPSTKVPFTYQLDDKRFYQKTQHPSGQLIALLILELGLLPSELSKLRLSEIDLDFQLIRVDNGSTVKVLSFSQAILKHLSEMEVGSTYLFENKGKPYSRQWFFNQLNAFLLEIGYDQLSAQSLREQFIIREKEKGTSLMELTQKLGLKSPITLEKYYRL", "text": "FUNCTION: Putative tyrosine recombinase. Not involved in the cutting and rejoining of the recombining DNA molecules on dif(SL) site. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerD-like subfamily."}
{"protein": "MKRRPRKWKKKGRMRWKWIKKRIRRLKRQRKKERGLI", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL41 family."}
{"protein": "MNRNGVITCALGGLLLSQAATHQAMAADLSVQVNQFFQQQYPDKESQVKVVIKTPQNQWPQCDMPEITLPANARPWGNISLSVRCDGVRRFIQTQVQVSGHYAVAARQLAAGEKMTLQDIKMKQGRLDTLPPGALLEPNFAQGAVSLRQINAGQPLTRNMLRRLWIIKAGQDVQVLALGEGFNVNSNGKAMNNAAIQDNVRVRMASGQIVSGTVADDGTVHILL", "text": "FUNCTION: Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the FlgA family."}
{"protein": "MFSGAGRPSKEQIKQYDNLAVGEMKKGASVAAVLLLTPFVISFFQKMRA", "text": "FUNCTION: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Note=Outer membrane- anchored. SIMILARITY: Belongs to the Tom5 family."}
{"protein": "MRGGEELDGFEGEASSTSMISGASSPYQPTTEPVSQRRGLAGLRCDPDYLRGALGRLKVAQVILALIAFICIETIMECSPCEGLYFFEFVSCSAFVVTGVLLILFSLNLHMRIPQINWNLTDLVNTGLSTFFFFIASIVLAALNHKTGAEIAAVIFGFLATAAYAVSTFLAMQKWRVSVRQQSTNDYIRARTESRDVDSRPEIQRLDT", "text": "FUNCTION: Acts as a backup for CMTM6 to regulate plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. May protect PD- L1/CD274 from being polyubiquitinated and targeted for degradation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chemokine-like factor family."}
{"protein": "MERPAAGEIDANKCDHLSRGEEGTGDLETSPVGSLADLPFAAVDIQDDCGLPDVPQGNVPQGNPKRSKENRGDRNDHVKKRKKAKKDYQPNYFLSIPITNKKITAGIKVLQNSILRQDNRLTKAMVGDGSFHITLLVMQLLNEDEVNIGTDALLELKPFVEEILEGKHLTLPFHGIGTFQGQVGFVKLADGDHVSALLEIAETAKRTFQEKGILAGESRTFKPHLTFMKLSKAPMLWKKGVRKIEPGLYEQFIDHRFGEEILYQIDLCSMLKKKQSNGYYHCESSIVIGEKDRKEPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSVKAEEGDRNGDGSDNNRK", "text": "FUNCTION: Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). Isoform Delta may be involved in shuttling aquaporin-2 (AQP2) to the plasma membrane. SUBCELLULAR LOCATION: [Isoform Gamma]: Nucleus Cytoplasm. SUBCELLULAR LOCATION: [Isoform Delta]: Nucleus Cell membrane Note=Cotranslocates with AQP2 to the plasma membrane in response to arginine-vasopressin (AVP) stimulation in inner medullary collecting duct (IMCD) cells."}
{"protein": "MRRGFGPLSLAFFLFLLALLTLPGDGNQGSVAGSCSCDRTISSGTQIPQGTLDHIRKYLKAFHRCPFFIRFQLQSKSVCGGSQDQWVRELVDCFERKECGTGHGKSFHHQKHLPQASTQTPEAAEGTPSDTSTPAHSQSTQHSTLPSGALSLNKEHTQPWEMTTLPSGYGLEARPEAEANEKQQDDRQQEAPGAGASTPAWVPVLSLLAIVFFLTAAMAYVLCNRRATQQNSAGLQLWYTPVEPRP", "text": "FUNCTION: Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo. Also acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
{"protein": "MAEVSGAALSQAGWYLSDEGVEACTSSPGKGSINDIILIALNTDLRTIGKKFLPSDINGGKVEKLEGPCVLQIQKVRNVAAPKDNEESQAAPRMLRVQMTDGHTSCTAVEFSYISKISLNTPPGTKVKLSGTVDIKNGFLLLSDSNTTVLGGEVEHLIDKWALQRSLLKHNRSNIGAEGGPPPFLPFGQKCASNVQVDSRELDRRKTLQVSLPAKPANDNDEFEKQRTAAIAEVAKSKETKTFGGGGGGARSNLNIGAAGHRNREVLQKEKASKSESKNEGVYRELVDEKALKHITEMGFSKEASRQALMDNANNLEAALNVLLNSSKQKPAVGPPARGRGKGRGRGRSEDEEDLGTARPSAPSTLFDFLESKMGTLNVEEPKSQPQHLHQGQHRGWNAEQNGMKDGTQSRHLPRNDTRQPRNERPPRFQKDTPTSKSTVENSVLSRNRGSERPSSSSGSDVWAEERIKCDRPYSRYDRTKDASHPLGLQHNDGAFKKRENSMQNRPGRGPLYAEAKENPLPPEFVDYNNQRRGRRENQTGHPDHCYERKPRTMNSEAVSGLKIEKHFSVNTDYPRPVQSNSLGVPNGETAPPLKGRRVGPIKSAGPVTAVPYDDKIFYNSGPKRRSGPIKPEKVIESSIPVEYAKVWKPGDECFALYWEDNKFYRAEVEALHSSGMTAVVKFTDYGNYEEVLLSNIKPVQTEAWEEEGTYDHTIEFRRGGDGQPRRSTRPTQQFYQPPRARN", "text": "FUNCTION: Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. Plays a role in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, acts as an antiviral factor that participates in the assembly of stress granules together with G3BP1. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. Associated with actively translating polyribosomes. Component of stress granules."}
{"protein": "MESVDTELTSFNNMVAKSSYPVRILHHNNGISEDEEGGSGVEPYVGLEFDTAEEAREFYNAYAARTGFKVRTGQLYRSRTDGTVSSRRFVCSKEGFQLNSRTGCTAFIRVQRRDTGKWVLDQIQKEHNHELGGEGSVEETTPRPSRAPAPTKLGVTVNPHRPKMKVVDESDRETRSCPGGFKRFKGGGGEGEVSDDHHQTQQAKAVTGTEPYAGLEFGSANEACQFYQAYAEVVGFRVRIGQLFRSKVDGSITSRRFVCSREGFQHPSRMGCGAYMRIKRQDSGGWIVDRLNKDHNHDLEPGKKNDAGMKKIPDDGTGGLDSVDLIELNDFGNNHIKKTRENRIGKEWYPLLLDYFQSRQTEDMGFFYAVELDVNNGSCMSIFWADSRARFACSQFGDSVVFDTSYRKGSYSVPFATIIGFNHHRQPVLLGCAMVADESKEAFLWLFQTWLRAMSGRRPRSIVADQDLPIQQALVQVFPGAHHRYSAWQIREKERENLIPFPSEFKYEYEKCIYQTQTIVEFDSVWSALINKYGLRDDVWLREIYEQRENWVPAYLRASFFAGIPINGTIEPFFGASLDALTPLREFISRYEQALEQRREEERKEDFNSYNLQPFLQTKEPVEEQCRRLYTLTVFRIFQNELVQSYNYLCLKTYEEGAISRFLVRKCGNESEKHAVTFSASNLNSSCSCQMFEHEGLLCRHILKVFNLLDIRELPSRYILHRWTKNAEFGFVRDMESGVSAQDLKALMVWSLREAASKYIEFGTSSLEKYKLAYEIMREGGKKLCWQR", "text": "FUNCTION: Putative transcription activator involved in regulating light control of development. SUBCELLULAR LOCATION: Nucleus Note=The nuclear localization is independent of the light treatment. SIMILARITY: Belongs to the FHY3/FAR1 family."}
{"protein": "MAEQLTDQALVERVQQGDKKAFNLLVSRYQNKVAGLLTRYVSRNDIPDVVQESFIKAYRSIESFRGESAFYTWLYRIAVNTAKNYLTAQGRRPPNEDILAEDAENYDVGTHLRDVDTPENEMLSSELERIVFDTIHNLPEDLKTAITLRELEGLSYEDIAEIMDCPVGTVRSRIFRAREMIENKIQPLM", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Associates with the inner membrane via RseA. SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily."}
{"protein": "MVSSSPVSPSKETDRKSGEKWTAEDPSRPAKWWYSTFHTVTAMIGAGVLSLPYAMAYLGWGPGTFVLAMTWGLTLNTMWQMVQLHECVPGTRFDRYIDLGRYAFGPKLGPWIVLPQQLIVQVGCNIVYMVTGGKCLKQFVEITCSTCTPVRQSYWILGFGGVHFILSQLPNFNSVAGVSLAAAVMSLCYSTIAWGGSIAHGRVPDVSYDYKATNPGDFTFRVFNALGQISFAFAGHAVALEIQATMPSTPERPSKVPMWQGVIGAYVVNAVCYFPVALICYWAFGQDVDDNVLMNLQRPAWLIAAANLMVVVHVIGSYQVFAMPVFDLLERMMVNKFGFKHGVVLRFFTRTIYVAFTLFIGVSFPFFGDLLGFFGGFGFAPTSFFLPSIMWLIIKKPRRFSVTWFVNWISIIVGVFIMLASTIGGLRNIIADSSTYSFYA", "text": "FUNCTION: Amino acid transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family. Amino acid/auxin permease (AAAP) (TC 2.A.18.2) subfamily."}
{"protein": "MDLLATTSAVAVSSYALLSTIYKSAQALYAQPTNPSSLQNDLEQAGVVLPSVDVIVPCFNEDPNTLSECLASIASQDYAGKLRVIVVDDGSANRDLLGPVHKIYASDPRFRIILMAKNVGKRKAQIAAIRSSSGDLVLNVDSDTILAVDVVTKLVSKMQDPDVGAAMGQLVASNRNETWLTK", "text": "FUNCTION: Involved in the synthesis of Nod factor, a sulfated N-acyl- beta-1,4-tetrasaccharide of N-acetylglucosamine which initiates a series of events in the host plant species leading eventually to nodulation. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the NodC/HAS family."}
{"protein": "MSDIALTVSMLSLVAVLGLWIGNWRIYGVGLGIGGVLFGGIIVGHFAQRYQLDLNSDMLHFIQEFGLILFVYSIGIQVGPGFFSSLRVSGLRLNAFAVLMVLISGLITAAIHKLFAVPLPIILGIFSGAVTNTPALGAGQQILTDLGSNPSQIDLMGMGYAMAYPFGICGILLVIWLIRLLFRINIDAEARDFDSRNGHSHELLQTMNIMVRNPNLSGLSIQEVPILNSDTIVCSRLKRGDFLMVPLPTTQIESGDLLHLVGQKQELENARLVIGEQVDTSLSTRGTELQVSRVVVTNERVLGKKIRDLNLKQRYDVVISRLNRAGVELVAGNNATLQFGDILNLVGRPQAIDAVAAIVGNAQQKLQQVQMLPVFIGIGLGVLLGSVPLFIPGFPAALKLGLAGGPLVVALILGRIGSIGKLYWFMPPSANLALRELGIVLFLAVVGLKSGGNFIDTLLNGEGVTWIGYGILITAIPLLTAALLARLMIKMNYLTLCGMLAGAMTDPPALAFANGLHATSGAAALSYATVYPLAMFLRIMSPQLLALLFWSV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family. YidE subfamily."}
{"protein": "MCSVARHMESIMLFTLLGLCVGLAAGTEAAVVKDFDVNKFLGFWYEIALASKMGAYGLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTRISGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHILKHDLTCVNALQSGQI", "text": "FUNCTION: Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 13-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation. SUBCELLULAR LOCATION: Secreted Note=Synthesized by the mid and distal caput of the epididymis and secreted into the epididymal lumen. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MPKSVMIVEDNELNMKLFRDLIEASGYETIRTRNGLEALDLAREHRPDLILMDIQLPEVSGLEVTKWLKDDDELRHIPVIAVTAFAMKGDEERIRQGGCEAYISKPISVPRFIETIKSYLGDA", "text": "FUNCTION: Essential protein that is involved in the control of cell division, probably through the regulation of ctrA. Its phosphorylation status is regulated by PdhS (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Localized at one pole of the cell. Colocalizes with PdhS (By similarity)."}
{"protein": "MPINQKIPTWFAVPAVFAVLSVISYQTLIVPENLEGAKNVLTMAKTIPIPVAGPESIEFDPKGEGPYAAVVDGRILKWRGDDLGWVDFAYTSPHRGNCSKTEVVPTCGRPLGLTFEKKTGDLYICDGYLGLMKVGPEGGLAELIVDEAEGRKVMFANQGDIDEEEDVFYFNDSSDKYHFRDVFFVAVSGERSGRVIRYDKKTKEAKVIMDNLVCNNGLALNKDRSFLITCESGTSLVHRYWIKGPKAGTRDIFAKVPGYPDNIRLTSTGDFWIGLHCKKNLIGRLIVKYKWLGKLVEKTMKLEYVIAFINGFKPHGVAVKISGETGEVLELLEDKEGKTMKYVSEAYERDDGKLWFGSVYWPAVWVLDRK", "text": "SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the strictosidine synthase family."}
{"protein": "MSKIYVLDTNVLLQDPNAIFSFEENEVVIPAVVLEEVDSKKRYMDEVGRNARHVSKLIDALRQKGRLHEHVPLDTGGTLRIELNHRSFHQLQEIFIEKTNDNRILAVAKNLSLEEETKENGRPVILVSKDVLVRVKADAIGLLAEDFLNDRVVDNDEMYSGYKDLYISQQLFSSFYGKNQISVNDVKQHAFYPNQFALMKDELGGSSSAVGIADKTGTVLKRLVFDDEHIWGIRPKNVQQTMALELLLREDIPLVTLIGKAGTGKTLLALAAGLLQTEDLGIYKKLVVARPIVPVGKDIGYLPGEKEEKLKPWMQPIFDNLEFLFNAKKPGELDAILAGIGSIQVEALTYIRGRSIPDQFIIIDEAQNLTRHEVKTLLTRVGEGSKIVLMGDPEQIDHPYLDSLNNGLAYVVERFKGQPISGSVKLLKGERSGLAQLAADLL", "text": "SIMILARITY: In the C-terminal section; belongs to the PhoH family."}
{"protein": "MITAADFYHVMTAMVPLYVAMILAYGSVKWWRIFTPDQCSGINRFVALFAVPLLSFHFISTNNPYTMNLRFIAADTLQKLMVLAMLTAWSHLSRRGSLEWTITLFSLSTLPNTLVMGIPLLKGMYGEFSGSLMVQIVVLQCIIWYTLMLFMFEYRGARMLITEQFPDTAANIASIVVDPDVVSLDGRRDAIETETEVKEDGRIHVTVRRSNASRSDIYSRRSMGFSSTTPRPSNLTNAEIYSLQSSRNPTPRGSSFNHTDFYSMVGRSSNFGAADAFGVRTGATPRPSNYEDDASKPKYPLPASNAAPMAGHYPAPNPAVSSAPKGAKKAATNGQAKGEDLHMFVWSSSASPVSDVFGGGAPDYNDAAAVKSPRKMDGAKDREDYVERDDFSFGNRGVMDRDAEAGDEKAAAAAGADPSKAMAAPTAMPPTSVMTRLILIMVWRKLIRNPNTYSSLIGLIWSLVCFRWNFEMPAIVLKSISILSDAGLGMAMFSLGLFMALQPHIIACGNKVATYAMAVRFLAGPAVMAAASFAVGLRGTLLHVAIVQAALPQGIVPFVFAKEYSVHPSILSTAVIFGMLIALPITLVYYILLGL", "text": "FUNCTION: Acts as a component of the auxin efflux carrier. Seems to be involved in the polar auxin transport which may promote adventitious root emergence and control tillering. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family."}
{"protein": "MGNSVMEKIKGGLVVSCQALEDEPLHSAFIMSKMALAAVQGGAVGIRANTAKDIRAIQSEIDVPIIGIYKKDYDDSDVFITPTLKEVREICETGVEIVAMDATTRKRPHNEDLKDILSAIRKEFPNTLFMADTASIEDVYYADSLGFDLIGTTLYGYTEETANKNISDDDFSHLKEVLKSTKRPVIAEGKIDSPSKARQVLTLGCYAVVVGGAVTRPQEITTRFTNEIQKIQEERGK", "text": "FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N- acetylglucosamine-6-phosphate (GlcNAc-6-P). SIMILARITY: Belongs to the NanE family."}
{"protein": "MGRYTLALLPLIVFGGIAHGAKMLYDQDFHGKNIAEIPSALSHQGADAEPAAARRATLPALTDAAIKGKLTLVNVFASWCLPCRDEHPVLKELAKDGRLNIVAINYKDQSDNALRFLGELGNPYQAIGIDPNGKAAIDWGVYGIPESYLVGADGTILYKRVGPSTNISLKEGLVPAMEKALGKPVS", "text": "FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Also acts as a disulfide oxidoreductase in cytochromes c biogenesis. The cysteines of apocytochromes c must be in the reduced state for covalent linkage between the two moieties to occur (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily."}
{"protein": "MHRENYFSKIAFCLLGVLFLSCITSVQTVSGDAASHEERMNNYRKRVGRLFMEQKAAQPDAVKLPSGLVFQRIARGSGKRAPAIDDKCEVHYTGRLRDGTVFDSSRERGKPTTFRPNEVIKGWTEALQLMREGDRWRLFIPYDLAYGVTGGGGMIPPYSPLEFDVELISIKDGGKGRTAEEVDEILRKAEEDREDM", "text": "FUNCTION: Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the FKBP-type PPIase family."}
{"protein": "MSFFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPGL", "text": "FUNCTION: Catalyzes the NADH-dependent reduction of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5- methyltetrahydrofolate. FUNCTION: Catalyzes the NADH-dependent reduction of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate (PubMed:9922232). Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate. Can also use NADPH as the reductant, but much less effectively than NADH (PubMed:9922232). SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family."}
{"protein": "MQPQELKTIMGSGLLSFPLTDFDSEGHFNARGYAERLEWLAPYGASALFAAGGTGEFFSLTADEYPAIIETAVQTCRGKVPIIAGAGGPTRFAIQCAQAAEKAGAHGILLLPHYLTEAGQEGLAAHVEAVCKSVKFGVIVYNRGQSRFTPETLARLAERNANLVGFKDGVGDIELMNSIYMKMGDRFAYLGGLPTAEVYAAAYKALGTPVYSSAVFNFIPKTAMDFYHAVANDDQATQHRLLRSFFMPYLALRNRMPGYAVSIVKAGAKIVGHDAGPVRAPLTDLKADEMAALKALIDQLGPQ", "text": "SIMILARITY: Belongs to the DapA family."}
{"protein": "MLHTLHRSPWLTDFAALLRLLSEGDELLLLQDGVTAAVDGNRYLESLRNAPIKVYALNEDLIARGLTGQISNDIILIDYTDFVRLTVKHPSQMVW", "text": "FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrH/TusB family."}
{"protein": "MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDPSINCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRVHLLYK", "text": "FUNCTION: Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites. FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:9872316, PubMed:9872744, PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10906333, PubMed:10773016, PubMed:10075644, PubMed:9872744, PubMed:24305054). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine- tuning of inhibitory synaptic transmission (PubMed:9844003). Pre- synaptic GABA receptor inhibits neurotransmitter release by down- regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:9844003, PubMed:9872316, PubMed:10075644, PubMed:9872744, PubMed:22660477). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). Activated by (-)-baclofen, cgp27492 and blocked by phaclofen (PubMed:9844003, PubMed:9872316, PubMed:24305054). SUBCELLULAR LOCATION: [Isoform 1E]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane; Multi-pass membrane protein Cell projection, dendrite Note=Colocalizes with ATF4 in hippocampal neuron dendritic membranes (By similarity). Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane (PubMed:15617512). SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily."}
{"protein": "MRTVRTLLIDNYDSFTYNLFQMLAEVNGAAPLVVRNDDTRTWQALAPGDFDNVVVSPGPGHPATDTDLGLSRRVITEWDLPLLGVCLGHQALCLLAGAAVVHAPEPFHGRTSDIRHDGQGLFANIPSPLTVVRYHSLTVRQLPADLRATAHTADGQLMAVAHRHLPRFGVQFHPESISSEHGHRMLANFRDLSLRAAGHRPPHTERIPAPAPAPAPAPAPAPPASAPVGEYRLHVREVACVPDADAAFTALFADAPARFWLDSSRVEPGLARFTFLGAPAGPLGEQITYDVADRAVRVKDGSGGETRRPGTLFDHLEHELAARALPATGLPFEFNLGYVGYLGYETKADSGGEDAHRGELPDGAFMFADRMLALDHEQGRAWLLALSSTRRPATAPAAERWLTDAARTLATTAPRPPFTLLPDDQLPALDVHYRHSLPRYRELVEECRRLITDGETYEVCLTNMLRVPGRIDPLTAYRALRTVSPAPYAAYLQFPGATVLSSSPERFLRIGADGWAESKPIKGTRPRGAGPAQDAAVKASLAAAEKDRSENLMIVDLVRNDLGQVCDIGSVHVPGLFEVETYATVHQLVSTVRGRLAADVSRPRAVRAAFPGGSMTGAPKVRTMQFIDRLEKGPRGVYSGALGYFALSGAADLSIVIRTIVATEEAATIGVGGAVVALSDPDDEVREMLLKAQTTLAALRQAHAGATASDRELLAGSLR", "text": "FUNCTION: Involved in pristinamycin I biosynthesis (PubMed:9044253). Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine (By similarity). SIMILARITY: In the C-terminal section; belongs to the anthranilate synthase component I family."}
{"protein": "MSYFTIQNEDLPQGFTFRPHDKIYDSLWEMMDDGYFPSTIPLKTTINGVDMPSVGWLEVDEGLYDILIDGLDVLRPTDEEMIVSATGWPLEKNRALILNFFRNLRMDIIGTYTLQRSFITIMSIVLFGDQNPRLRRKKRSRVSLGKMLFDLALRMRSKIRRMKLTEVQVTGQNLVKDLCLLHILDLQKRLVTRGTIAEKRFFTAIEQAPCNYEPKRYGMKKKHMNFMFESDRKNLTVHPTLVNLEEHWITFESARERLLDTTFTKDWPVVGSL", "text": "FUNCTION: Acts as a weak IFN antagonist. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the phlebovirus NS-S protein family."}
{"protein": "MEAVYLVVNGLGLVLDVLTLVLDLNFLLVSSLLASLAWLLAFVYNLPHTVLTSLLHLGRGVLLSLLALIEAVVRFTCGGLQALCTLLYSCCSGLESLKLLGHLASHGALRSREILHRGVLNVVSSGHALLRQACDICAIAMSLVAYVINSLVNICLIGTQNLFSLVLALWDAVTGPLWRMTDVVAAFLAHISSSAVAMAILLWTPCQLALELLASAARLLASFVLVNLTGLVLLACVLAVTVTVLHPDFTLRLATQALSQLHARPSYHRLREDVMRLSRLALGSEAWRRVWSRSLQLASWPNRGGAPGAPQGDPMRVFSVRTRRQDTLPEAGRRSEAEEEEARTIRVTPVRGRERLNEEEPPGGQDPWKLLKEQEERKKCVICQDQSKTVLLLPCRHLCLCQACTEILMRHPVYHRNCPLCRRGILQTLNVYL", "text": "FUNCTION: E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud (PubMed:27368102). Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the ubiquitin conjugating enzyme UBE2J1 (PubMed:27368102, PubMed:33472082). Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING (PubMed:25254379, PubMed:32614325). Also required to limit type I interferon response by promoting autophagic degradation of IRF3 (PubMed:25254379). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
{"protein": "MSVKIENIQCELLSKNWFKLHKYTFDLKTDEGTSVQQIREVYDRGNGATILLYNRQQGTVVLIEQFRMPTYVNGNASGMLLEACAGLLDNDSPEACIRREAMEETGYQVDKVQKLFEAYMSPGGVTELVYFFAAEYHPDQKITDEVGVEDEVIEVVELPFHDALAMVADGRIKDGKTIMLLQYAQIHFFPSSLTPQRC", "text": "FUNCTION: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP- mannose as its preferred substrate, yielding GMP and mannose-1- phosphate. SIMILARITY: Belongs to the Nudix hydrolase family. NudK subfamily."}
{"protein": "MSAANPETPNSTISREASTQSSSAAASQGWVLPEGKIVPNTVFVGGIDARMDETEIGSCFGRYGSVKEVKIITNRTGVSKGYGFVSFVNDVDVQKIVGSQIHFHGKKLKLGPAIRKQKLCARHVQPRPLVVNPPPPPQFQNVWRNPNTETYLQPQITPNPVTQHVQSAANPETPNSTISREASTQSSSAAASQGWVLPEGKIVPNTVFVGGIDARMDETEIGSCFGRYGSVKEVKIITNRTGVSKGYGFVSFVNDVDVQKIVGSQIHFHGKKLKLGPAIRKQKLCARHVQPRPLVVNPPPPPQFQNVWRNPNTETYLQPQITPNPVTQHVQAYSAYPHSPGQVITGCQLLVYNYQEYPTYPDSAFQVTTGYQLPVYNYQPFPAYPRSPFQVTAGYQLPVYNYQAFPAYPNSPFQVATGYQFPVYNYQPFPAYPSSPFQVTAGYQLPVYNYQAFPAYPNSPFQVATGYQFPVYNYQAFPAYPNSPVQVTTGYQLPVYNYQAFPAYPSSPFQVTTGYQLPVYNYQAFPAYPNSAVQVTTGYQFHVYNYQMPPQCPVGEQRRNLWTEAYKWWYLVCLIQRRD", "text": "FUNCTION: RNA-binding protein that plays an essential role in spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. Nuclear at some stages of spermatozoide development. Localizes both to the nuclei and cytoplasm of spermatozoide differentiation. Nuclear in fetal gonocytes and in spermatogonial nuclei. It then relocates to the cytoplasm during male meiosis. SIMILARITY: Belongs to the RRM DAZ family."}
{"protein": "MAHFPDTSGMTGVLRPLRIEGDILDLEVEGEIPAQLDGTFHRVHPDAQFPPRFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAYRNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEGYTNFDGKLKNQTFSAHAKIDPVTGNFCNFGYAATGLLTTDCSYFEIDPAGNLLFETEFQVPYYCMMHDYGLTEHYAIFHIVPCSPNWDRLKAGLPHFGFDTTLPVWLGVVPRGPGVTNKDVRWFKAPKTIFASHVMNAFEEGSKIHFDTPQAENNAFPFFPDIHGAPFDPVAARPYLHRWTVDLGSNSEDFAEVRQLTSWIDEFPRVDARYVGQPYRHGWGLVMDPEMEMEFARGRASGFKMNRIGHWDHATGKEDSWWCGPQSIIQEPCFVPRMADSAEGDGYIIALVDNLITNYSDLVVLDALNLKDGPIGRAKLPIRLRSGLHGNWADASKLPIAA", "text": "FUNCTION: Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene). SIMILARITY: Belongs to the carotenoid oxygenase family."}
{"protein": "MASPSKGNDLFSPDEEGPAVVAGPGPGPGGAEGAAEERRVKVSSLPFSVEALMSDKKPPKEASPLPAESASAGATLRPLLLSGHGAREAHSPGPLVKPFETASVKSENSEDGAAWMQEPGRYSPPPRHMSPTTCTLRKHKTNRKPRTPFTTSQLLALERKFRQKQYLSIAERAEFSSSLNLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPSSFSLPFPISSPLQAASIYGASYPFHRPVLPIPPVGLYATPVGYGMYHLS", "text": "FUNCTION: Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antagonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter (By similarity). FUNCTION: Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antagonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Msh homeobox family."}
{"protein": "MAAQQRDCGGAAQLAGPAAEADPLGRFTCPVCLEVYEKPVQVPCGHVFCSACLQECLKPKKPVCGVCRSALAPGVRAVELERQIESTETSCHGCRKNFFLSKIRSHVATCSKYQNYIMEGVKATIKDASLQPRNVPNRYTFPCPYCPEKNFDQEGLVEHCKLFHSTDTKSVVCPICASMPWGDPNYRSANFREHIQRRHRFSYDTFVDYDVDEEDMMNQVLQRSIIDQ", "text": "FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination of various substrates (PubMed:23645206, PubMed:25165885). In turn, participates in the regulation of many biological processes including cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive immunity (PubMed:25165885, PubMed:28708287). Acts as negative regulator of NF-kappa-B-dependent transcription by promoting the ubiquitination and stabilization of the NF-kappa-B inhibitor TNFAIP3 (PubMed:25165885). May promote the ubiquitination of TRAF6 as well (PubMed:28708287). Acts also as a negative regulator of T-cell activation (PubMed:25165885). Inhibits cellular dsRNA responses and interferon production by targeting MAVS component for proteasomal degradation (PubMed:25165885). Ubiquitinates the CDK inhibitor CDKN1A leading to its degradationand probably also CDKN1B and CDKN1C (PubMed:23645206). This activity stimulates cell cycle G1-to-S phase transition and suppresses cellular senescence. May play a role in spermatogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MEVTDVRLRRVNTEGRMRAIASITLDGEFVVHDIRVIDGNNGLFVAMPSKRTPDGEFRDIAHPINSNHRGKIQDAVLAEYHRLGEVEVEFEEAGAS", "text": "FUNCTION: Essential for sporulation. Interferes with or is a negative regulator of the pathway leading to asymmetric septation. SIMILARITY: Belongs to the SpoVG family."}
{"protein": "MAQIDIRQVRKSYGKTPTLHGVDLSFDSGEFVVILGPSGCGKSTLLRMIAGLEEITSGEIAIGGRVVNTLEPRERGCAMVFQNYALYPHMSVAANIGYALKVAGVPKAERQRRIEETAKIVGLSDYLERKPAALSGGQRQRVAMARAIIREPAVFLFDEPLSNLDAKLRVSMRAEIRKLHQRLSATSIFVTHDQVEAMTLADRLVVMNKGNVEQVGHPLDIYHRPASTFVASFIGSPAMNLFTTKVEVETPAVILSGTPVKLFPETALELRGRNVTVGIRPEQCVVSMDGPGVPAIVDFVEELGSGRIVHADIAGETFSAAIGEDLLVKPGQRIHLDLPTAHLHFFDPATGKRIETEGTAETARSKNETLLAV", "text": "FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn- glycerol-3-phosphate (G3P) import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. sn-glycerol-3- phosphate importer (TC 3.A.1.1.3) family."}
{"protein": "MVKAYLKFVQDKVFGLISTSNSILDGSGKLAITGCGERISIWDLRKQVLNQSLYEEDIKAEVTNVCLSKDGALLASGYSDGSIRIWSMSDYQLQAVFNGHRGSVTTMTFNRLGNILVSGSKDTEVIVWDIITESGLFRLRGHRDQITSVKLLERSNHLITSSKDGFIKIWDTETQHCIQTIVGHRNPIWGIDVNPDETRLCSCTSDNQIRFWRIPSNERQREDGSGIEPKFIVNTPINSAVIIPDEINEDGSKKENSNNSNNNDIDDLEIISEEEFAKYYGSITVKAESVSGVRFDPTNKILAVQSTGKFVDLFKITHYDTMKLEEISIVEEMRHRQTIKTSSKVRFFSFGNDIKHWNKFVITLAGNSLEAYEIKEKEQGGGAFEVSSTLDQAGHRSDIRSLSLSSNDQMLVSTSSESVKVWNMKSLSCIRSIACDYGLCTVFAPGNLHVIVGTKTGTIEVFELASAARVASIKAHEGSVWSLVLTPDLRGVTSGGADKLVKFWDFELIASQENSKHKVLNLSLTKTLKVESDVLALKYSADNKFLAVSLLDNTVKIFYTDTVKFHLSLYGHKLPVMCLDISDDSTLIITGSADKNIKIWGLDYGDCHKSFFAHDDSIMQVSFIPSTHHFISASKDKRIKYWDADKFEHIQTIEAHHGEVWSLAMGSVGDFFISGSHDRSIRIFNQTETPIFVESDRQREMEQTWEATLEDDTRMRTKEMLEENAAAGKQTLETIMAGEDILDAIELCVQEKFKIDEYEKLLKTTKNQDEIPLYQPNIIMLGLSPSEYLWNRINRIRPSDLEEALRVLPFSVMRTLFEYFNLWVDQSGKSVEFIFKCSFFLIQTHQNQLSVSTEFIPILQHLNTSIKNRLQKERFTLGFNRSALSFVKREIEINQQYKFFDSDLYLNKNNKNNKDKDSNNNKKDNKKDNKKDNEKSLKRNRK", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the WD repeat WDR3/UTP12 family."}
{"protein": "MVRGIRGAITVEEDTPEAIHQATRELLLKMLEANGIQSYEELAAVIFTVTEDLTSAFPAEAARQIGMHRVPLLSAREVPVPGSLPRVIRVLALWNTDTPQDRVRHVYLREAVRLRPDLESAQ", "text": "FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MLESTALFSATTIHLDRLMCAFNCMTPFGQRDDVLITIDRDGLTFIRQNNHAAEIQLFLAKELFQYYSIREGFEGEIQLCMKLNHLLDTVSVANRDKDDVVECTLSYDGEGTPFMLILEDSMITEQVEYATYLVGEMDRTGLELDRARLEFECILKGDVLYSALRDLREIGCKECYLYIVTSSRARPMFALVSRGQLGLSKIILPSERSVLEKLEVYENDSTTLIHDAPVIGLFDFAALDKLRPSTKIASKVLIRKDVHGLLAVNILSDTNAILVPEKRELIRASRSVSAEYPTVVIEVFLLEKASVGDIDVRDVHQLMLTSPAHRRSGFADSGSRIVSVTPTATSAAHTGAGSLLGLAPPSAFPAEETQDPDESYHPAPSNTDIPLFL", "text": "FUNCTION: Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the rad1 family."}
{"protein": "MPSEPSAPLPQPLPPDGGWGWVVVCASFISIGFSYAFPKAVTVFFKDIQEIFNTTSSQIAWISSIMLAVMYAGGPISSVLVNNYGSRPVVIVGGLLCCIGMILASYSNSVIELYLTVGFIGGLGLAFNLQPALTIIGKYFYRRRPLANGCAMAGSPVFLSTLAPFNQYLFNNYGWKGSFLILGGIFLHSCVAGCLMRPVGPSPNTKKSKSKVGSRHDSTLKKASKVSTAQKVNRFLDFSLFMHRGFLIYLSGNVILFLGIFAPIIFLAQYAKHIGVDDYNSAFLLSVMAFIDMFARPSVGLIANTSLIRPRIQYLFSSAIIFTGICHLLCPLATTYSALVVYVVFFGLGFGSISSLLFECLMDIVGATRFSSAVGLTTIVECCPVLFGPPLAGKLLDITGEYKYLYIASGTVVLVSGTYLLIGNAINYRLLDKERKREKAKKKKSASHASREMEALNRSKQDEVTVKASNAHNPPSDRDKESNI", "text": "FUNCTION: Proton-coupled monocarboxylate symporter (PubMed:21792931). Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm Basolateral cell membrane; Multi-pass membrane protein Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (PubMed:21792931). SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
{"protein": "MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL", "text": "SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family."}
{"protein": "MYPTDPRQLNTERQIYLDKQFFVDVFSIPACVRNTNGDLSATNEKFSKEFIGSLDIKEWFYSLPVQVATSFLREELDAMSLPSSMNKIQSVAIGDKLWLVQFIPLIYGEVVNVLWLFFCKNSNVIVDYCRGLRTNITNDRMLEFKNKSTEIQWKVFILYSFGFCHESIASLLSITNGSSRNAISEVYKFFGIHSKHDLLMIFHTSRMHSLFFDELFFILKCAE", "text": "FUNCTION: This protein is essential for positively regulating the expression of transfer genes that are involved in the conjugal transfer of DNA between bacterial cells. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MATAIRLLGRRVSSWRLRPSPSPLAVPRRAHSILPVDDDINGLNEEQKQLRHTISKFLQENLAPKAQEIDQTNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCVNQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMKLKAEKKGDHYVLNGNKFWITNGPDADILVVYAKTDLTAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANVLSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMASRQYVYNVAKACDEGHIIPKDCAGVILYAAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFR", "text": "FUNCTION: Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl- CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MAFLKKSLFLVLFLGLVSLSICDEEKRENEDEENQEDDEQSEMRRGLRSKIKEAAKTAGKMALGFVNDMAGEQ", "text": "FUNCTION: Antibacterial peptide with activity against Gram-positive and Gram-negative bacteria (By similarity). May also be active against fungi (Probable). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MKIRASVRKICTKCQLIRRKGRIRVICSNPRHKQRQR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
{"protein": "MPMISVLGKMFLWQREGPGGRWTCQTSRRVSSDPAWAVEWIELPRGLSLSSLGSARTLRGWSRSSRPSSVDSQDLPEVNVGDTVAMLPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPSDSPAALESAFSSYSDLSEGEQEARFAAGVAEQFAIAEAKLRAWSSVDGEDSTDDSYDEDFAGGMDTDMAGQLPLGPHLQDLFTGHRFSRPVRQGSVEPESDCSQTVSPDTLCSSLCSLEDGLLGSPARLASQLLGDELLLAKLPPSRESAFRSLGPLEAQDSLYNSPLTESCLSPAEEEPAPCKDCQPLCPPLTGSWERQRQASDLASSGVVSLDEDEAEPEEQ", "text": "SIMILARITY: Belongs to the FAM131 family."}
{"protein": "MVFLLCFFLVADVSYGINGDCELPKVVGPCRARFPRYYYNSSSKRCEKFIYGGCGGNANNFHTLEECEKVCGVRSRDSPKEN", "text": "FUNCTION: Serine protease inhibitor that inhibits both tissue and plasma kallikreins. Has hemolytic activity. Inhibits voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily."}
{"protein": "MEFVQYACNGAVAEIILNRPDAHHALNEQMLSELKEAVEMAAASEALIVLLRGSGKGFSAGGDIRMMTSEHDPDQFKRLMDTIEAVTLNLYQMKKVTIAAIHGAAAGLGLSLALCADIVLAEKNAVLAMNFIGIGLVPDGGGHYLLKKRIGEAKAKKLIWSGKKLSASEAADMGLLDGTFAGDPAEGARPIIETLLASPLLAMIETKGIFQSLQIEELKKVLSLERSAQERMRRTKDHQEGIRAFLEKREPKFQA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "AVKTITLNLVSPSANRYATFLTEIRDNVRXRSLDYSHSGIDVIGAPSSRDSXLNINFQSP", "text": "FUNCTION: Single-chain ribosome-inactivating protein. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
{"protein": "MDTWTLLLVLHTSLLLPWAEGATPTLRFVAVGDWGGVPNAPFHTAREMANAKQIGKVVQMLGAHFILSLGDNFYFSGVQSVSDKRFQETFEDVFSDRSLQNVPWYVLAGNHDHIGNVSAQIAYSKVSKRWNFPSPFYRLRFRIPRTNVSVAIYMLDTVTLCGNSNDFLSQQPERPRNLELARTQLAWLKRHLADAKEDYVLVAGHYPVWSIAEHGPTHCLVKKLQPLLVKYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNFMDPSTQHQRSVPNGYLRFHYGAENSLGGFAYLEITPKEMTVTYMEASGKSLFKTRLPKRAKA", "text": "SUBCELLULAR LOCATION: Lysosome."}
{"protein": "MLPLLRCVPRVLGSAVPSLRAAAPASPFRQLLTPGPRLCARPFGLLSVRAGSERRPGLLRPRGPCACGCGCGLLHTEGDKAFVDFLNDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLMRKVAGEKITVTFNINNSIPPTFDGEEEPTQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSSGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYISFLEDLKSFVKSQ", "text": "FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA- binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense. FUNCTION: (Microbial infection) During bacterial infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B (InlB). SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Cell membrane; Peripheral membrane protein; Extracellular side Secreted Cytoplasm Nucleus, nucleolus Note=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes. SIMILARITY: Belongs to the MAM33 family."}
{"protein": "METYTGIPEELKFAVLERIQPTEPEREKLFAIQEELASQVKIAAEKLGIPGVLVKMVGSAARGTWLSGTHDIDVFISFPEETSRKDLETLGMAIAREVARYAEHAEDRHAEHPYLNITYKGFDVDLVPCFRVASASQIKSAVDRTPFHNDFVKPRIKGHEDEVLLLKQFMRGGGVYGSELKTQGFSGYLTELLVIRYGSFKNTIYAACSWKPGEKIDIMQHGEIEHEEPLVVIDPTDPRRNVAAALSLDKFCTFIDHCREFLKNPELSFFFPAPILPLEDSEILEKLESRKSTQLAVVFKTPDVVEDVLFPQLYKMEQAVAALLKEYDFTVIKTGVWSGNTETAVMMELISGTLPNVKKHIGPPVWVKVHAEKFKEKYQAADGVFGGYIENGKYIFEILRKYPTARGLLEDRLMSCSLGKQVHQSVNEGFEIIENAGICRLKEYDFRIYLRKWI", "text": "FUNCTION: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily."}
{"protein": "MPSLLISVLFLHIAIYIINTIGASTIDSLLWLIYTKLPTSASCMAREQHQMKLEVVQLKREMNATSSQDEFAKWAKLRRRHDKALEEYEVKNKQFSRFKSLFDVAVKALRWAGTSGLILLLQFWFSKTPIFTLPPSWIPWQVEWVLSFPRAPMGTVSIQVWGGACAVMVALVGEAIGATVRYLYGSKDSMEAIKVGAGAVEKEKKRQ", "text": "FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WRB/GET1 family."}
{"protein": "MAAAAELSLLEKSLGLSKGNKYSAQGERQIPVLQTNNGPSLTGLTTIAAHLVKQANKEYLLGSTAEEKAIVQQWLEYRVTQVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADILLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH", "text": "FUNCTION: Positive modulator of ATM response to DNA damage. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytosol Nucleus Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage."}
{"protein": "MRKLWGLYLGLLDNHPLVTKSLSTGFLMGTGDILAQRLEHKFKDEKSQFKLDYKRVATMSTVGIFYSGPMLHYWYRSLDIMVKGEGRSVIIKKMLIDQLLFAPVAIGGFMTVTNFINNKGELKNLENFTKELFYAVKINWLIWPAAQIINFSLVPPNLRVLYSSIISIFWGMFLSHISFDKDHHIRNQNKEIN", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family."}
{"protein": "MRNHVLAASISMLSLLAIMGDTDSKTDSSFLMDSQRCMRHHYVDSISHPLYKCSSKMVLLARCEGHCSQASRSEPLVSFSTVLKQPFRSSCHCCRPQTSKLKALRLRCSGGMRLTATYRYILSCHCEECSS", "text": "FUNCTION: Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt- dependent activation of FZD4, suggesting the existence of a Wnt- independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTPIVTVLICLRLSLGPRTHVQAGTLPKPTLWAEPGSVITQGSPVTLWCQGILETQEYRLYREKKTAPWITRIPQEIVKKGQFPIPSITWEHTGRYRCFYGSHTAGWSEPSDPLELVVTGAYIKPTLSALPSPVVTSGGNVTLHCVSQVAFGSFILCKEGEDEHPQCLNSQPRTHGWSRAIFSVGPVSPSRRWSYRCYAYDSNSPHVWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPGESLTLQCVSDVSYDRFVLYKEGERDFLQLPGPQPQAGLSQANFTLGPVSRSYGGQYRCSGAYNLSSEWSAPSDPLDILIAGQFRGRPFISVHPGPTVASGENVTLLCQSWGPFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSAHSGTYRCYGSLSSNPYLLSHPSDSLELMVSGAAETLSPPQNKSDSKAGAANTLSPSQNKTASHPQDYTVENLIRMGIAGLVLVVLGILLFEAQHSQRSL", "text": "FUNCTION: May act as receptor for class I MHC antigens. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTTEHSKVSLGLDEDVSKRIEPSVSLWQFYLSKMISMDIEQVVTLSLAFLLAVKYIFFEQAETESTLSLKNPITSPVATPKKAPDNCCRREPVLSRRNEKLSSVEEEPGVNQDRKVEVIKPLVAETESTSRATFVLGASGGCSPVALGTQEPEIELPSEPRPNEECLQILESAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSTKLPEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDGKEYQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETPEGFAVIKDAFDSTSRFARLQKLHVTMAGRNLYIRFQSKTGDAMGMNMISKGTEKALVKLQEFFPEMQILAVSGNYCTDKKPAAVNWIEGRGKTVVCEAVIPARVVREVLKTTTEAMIDVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVRSHMVHNRSKINLQDLQGTCTKKAA", "text": "FUNCTION: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HMG-CoA reductase family."}
{"protein": "MTKSTYVELGEEKTSNQKGNMKRGVSILDFILRLIAIVATLASAIAMGTTDESLPFFTQFVRFRANYDDLPTLRFFVVASAIVSGYLILSLPLSILHIIRSSAGMTRVIFIILDTVMLGLLTAGSSAAASIVYLAHKGNRKANWFAFCQQYNSFCERISGSLIGSFIAIPLFIMLILLSALVLSRR", "text": "FUNCTION: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal apoplasm and the extraorganismal apoplasm and prevents lateral diffusion (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Very restricted localization following a belt shape within the plasma membrane which coincides with the position of the Casparian strip membrane domain in the root endodermis. SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP) family."}
{"protein": "MPLAKDPLHPSPEEEKRKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH", "text": "FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Required for proper rRNA processing and maturation of 18S rRNAs. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family."}
{"protein": "MEAGRTAVLRVKRKLGTEPAEALVLACKRLRSSAVELETPKTSPEGLERAAENNVFQLVATVRSQEEPVQPLLRAALRPSQGSQQRIRHHLRASAREIRQEGRYRVVFSRRSSGIPSDSLESEDASGTAKAADDANFQLLDLVHEEDAEVAAAAISCKKSDPDVILCNCVELIREGLNVSQCGPSSGHQKEQKDDFVYDIYCLERATPGWIENILSVQPYSHEWELVNDDQQPEDIYDDEDDENSENNWRNEYPEEENSDEDEDSRGSDNYSSSEERDNSRQPMWSKYPLDVQKEFDYDSPHDLDSD", "text": "FUNCTION: Directs RNA polymerase II nuclear import. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the IWR1/SLC7A6OS family."}
{"protein": "MNFTRIDLNTWNRREHFALYRQQIKCGFSLTTKLDITALRTALAETGYKFYPLMIYLISRAVNQFPEFRMALKDNELIYWDQSDPVFTVFHKETETFSALSCRYFPDLSEFMAGYNAVTAEYQHDTRLFPQGNLPENHLNISSLPWVSFDGFNLNITGNDDYFAPVFTMAKFQQEGDRVLLPVSVQVHHAVCDGFHAARFINTLQLMCDNILK", "text": "FUNCTION: This enzyme is an effector of chloramphenicol resistance in bacteria. SIMILARITY: Belongs to the chloramphenicol acetyltransferase family."}
{"protein": "ATDLQAGYVADSNFTEAWKKVVPNVDPPKTPSAFMXP", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase delta chain family."}
{"protein": "MRRQRRSITDIICENCKYLPTKRSRNKRKPIPKESDVKTFNYTAHLWDIRWLRHRARNTR", "text": "SIMILARITY: Belongs to the ninE family."}
{"protein": "MSLLLLTDVDLLINLILLFQKKLSLKEAIVFSLAVFGIVEAYYYWKNRSSESE", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein."}
{"protein": "MHLPQMGYDRAITVFSPDGRLFQVEYAREAVKRGATAIGIKCKEGVILIADKRVGSKLLEADTIEKIYKIDEHICAATSGLVADARVLIDRARIEAQINRLTYDEPITVKELAKKICDFKQQYTQYGGVRPFGVSLLIAGVDEVPKLYETDPSGALLEYKATAIGMGRNAVTEFFEKEYRDDLSFDDAMVLGLVAMGLSIESELVPENIEVGYVKVDDRTFKEVSPEELKPYVERANERIRELLKK", "text": "FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1A family."}
{"protein": "MDRYAAAGDEAADRARQQERHYQLLSALQSLVKELPSSFQQRLSYTTLSDLALALLDGTVFEIVQGLLEIQHLTEKSLYNQRLRLQNEHRVLRQTLRQKHLEAQQSCRPHNLPVLQAAQQRELEAMEHRIREEQQAMDRKIVLELDRKVADQQSTLEKAGVAGFYVTTNPQELTLQMNLLELIRKLQQRSCQVGKAAL", "text": "FUNCTION: May have a role in early embryogenesis. SIMILARITY: Belongs to the gonadal family."}
{"protein": "MDIVPISPYERMRPLRESKELRIKSFDDHRWPHKNNPVMTKNMIENYFYYIGINDKIQCVHCGGVISGFLEEDTHRISYEHRRHFPKCPVGKYRHPGYHLDAERLKSFKNWRYENIVRKMDLVAAGLFYTGIEDRCACHQCGNELYEWEAGDNPKEEHKRLFPDCKLSSY", "text": "FUNCTION: May act as an apoptosis inhibitor."}
{"protein": "MSDNEDNFDGDDFDDVEEDEGLDDLENAEEEGQVNVEILPSGERPQANQKRITTPYMTKYERARVLGTRALQIAMCAPVMVELEGETDPLLIAMKELKARKIPIIIRRYLPDGSYEDWGVDELIITD", "text": "FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family."}
{"protein": "MASSLNEDPEGSRITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEATDIKITVYTL", "text": "FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose (PubMed:23481255, PubMed:23474714, PubMed:21849506). Specifically acts as a glutamate mono-ADP- ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to glutamate residues on proteins (PubMed:23481255, PubMed:23474714). Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG to become a substrate for OARD1 (PubMed:23481255). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21849506). Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O- butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively (PubMed:21849506). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus Chromosome Note=Localizes both in the nucleoplasm and in the nucleolus (PubMed:29712969). Relocalizes to the nucleoplasm in response to DNA damage (PubMed:29712969). Recruited to DNA lesion regions following DNA damage (PubMed:23481255)."}
{"protein": "MEARSKLLDGTTASRRWTRKLVLLLPPLLLFLLRTESLQGLESDERFRTRENECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:11229364). Regulates the activation of NF- kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum Note=Not secreted. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily."}
{"protein": "MKILFVLISILYAVYRFSSEEDVDSAYLANELEPVEDINSEQYAALEPKEEQERSCAGMGQDCKDDCDCCLNIATCNCWFGRYFCSCTFGDYQTCLRKKGKCKRNRPQSCPRSNLNRKKG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 05 (agouti) family."}
{"protein": "MLPYTLIQEADDRLRKRVRRTELIHSHHFSEKLGIPIYFKCENLQRTGAFKIRGALNFMTSQPREALAKGVITASAGNHAQGVAFSADLLGVPSTVFMPESTPPQKVFATRDYGAEVVLTGRNFDEAYAAAVQAQEERGALFVHPFDDPLVMAGQGTIGLEVLQELPDVANILVPIGGGGLIAGIATAIRETHPHVRIIGVETAAAPSAHYSLQKGKIVQVPVTVTLADGIAVKKPGVNTFPIIRDLVDEVVLVEEEEIALAIVALLERTKLLVEGAGAVPLAALLNRRVTDLSGKTVCVLSGGNIDVKTISVVVERGLVAAGRYLKLKVELDDLPGALARLATEIAEAKANISIITHDRRSKSLPIGKTEVLIELETRGFEHIQEVISHLQGVGYLVDVLK", "text": "FUNCTION: Catalyzes the conversion of threonine to 2-oxobutanoate and ammonia. Functions in the threonine-dependent pathway of isoleucine biosynthesis, which is the minor pathway for isoleucine biosynthesis in G.sulfurreducens. Also displays serine ammonia-lyase activity, yielding pyruvate from L-serine. SIMILARITY: Belongs to the serine/threonine dehydratase family."}
{"protein": "MAQRAFPNPYADYNKSLAENYFDSTGRLTPEFSHRLTNKIRELLQQMERGLKSADPQDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKHSLNCLSRRSITFLCGDAGPLAVAAVLYHKMNSGKQAEDCITRLIHLNKIDPHVPNEMLYGRIGYIFALLFVNKNFGEEKIPQSHIQQICETILTSGEKLSRKRNFTTKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLHVSQGKLHSLVKPSVDFVCQLKFPSGNYPSCLDDTRDLLVHWCHGAPGVIYMLIQAYKVFKEEHYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDAKYLYRACKFAEWCLDYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKAKFPAFEL", "text": "FUNCTION: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4- dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the LanC-like protein family."}
{"protein": "MNKSRQKELTRWLKQQSVISQRWLNISRLLGFVSGILIIAQAWFMARILQHMIMENIPREALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYLGELDFGHYDTGVTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGAADSLKTFMETPLAHPQRGEAELASTDPVTIEAEELFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLADWDVIWVMQDGRIIEQGRYAELSVAGGPFATLLAHRQEEI", "text": "FUNCTION: Conversely, a more recent study suggests an alternative function of CydDC: authors suggest that CydDC does not mediate the export of L-cysteine but rather reduces cytoplasmic L-cystine to L- cysteine (PubMed:32900959). The principle function of CydDC would be to maintain the reduced state of cytoplasmic L-cysteine, thereby providing an important connection between sulfur metabolism, oxidative stress and resistance to antibiotics (PubMed:32900959). FUNCTION: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm (PubMed:12393891, PubMed:16040611). Export of these thiol- containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes and formation of correct disulfide bonds in periplasmic and secreted proteins (Probable). CydD contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation (PubMed:24958725). Required for the assembly of functional cytochrome bd-type quinol oxidases and periplasmic c-type cytochromes (PubMed:7934832, PubMed:8181727, PubMed:15470119). Overexpression of CydDC under anaerobic conditions also results in the formation of a heme biosynthesis-derived pigment, P-574 (PubMed:12375104). CydDC binds heme b, but heme is probably not transported by the complex and instead has a role in regulating ATPase activity (PubMed:24958725). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Cysteine exporter (TC 3.A.1.129.1) family."}
{"protein": "MGSLAAEKTVTGWAARDASGHLTPYNYTLRKTGPEDVVVKVLYCGICHTDIHQAKNHLGASKYPMVPGHEVVGEVVEVGPEVTKYSAGDVVGVGVIVGCCRECHPCKANVEQYCNKRIWSYNDVYTDGRPTQGGFASAMVVDQKFVVKIPAGLAPEQAAPLLCAGLTVYSPLKHFGLMSPGLRGGVLGLGGVGHMGVKVAKSMGHHVTVISSSARKRGEAMDDLGADAYLVSSDAAAMAAAGDSLDYIIDTVPVHHPLEPYLALLKLDGKLILMGVINQPLSFISPMVMLGRKAITGSFIGSMAETEEVLNFCVDKGLTSQIEVVKMDYVNQALERLERNDVRYRFVVDVAGSNIDDADAPPA", "text": "FUNCTION: Involved in lignin biosynthesis (PubMed:16443696, PubMed:21912859). Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde and sinapaldehyde to their respective alcohols (PubMed:16443696). Plays the major role in monolignol biosynthesis. Functions cooperatively with COMT in the culm internodes for the biosynthesis of monolignols, the lignin precursors. May be involved in lignin biosynthesis in leaves and roots (PubMed:21912859). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MCGIFGYCNYLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAIDGDEADSTFIYKQIGKVSALKEEITKQNPNRDVTFVSHCGIAHTRWATHGRPEQVNCHPQRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYNTNLQNGHDLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEKKLKVDFVDVEFPEENAGQPEIPLKSNNKSFGLGPKKAREFEAGSQNANLLPIAANEFNLRHSQSRAFLSEDGSPTPVEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDGELHIHRSRREVGASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRIDYENNKVILGGLKAWLPVVRRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDRVSKIDRRIEIIQGLKLIPGQIKQVLKLEPRIKKLCATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSIEQVTARKGHPIIICNENDEVWAQKSKSIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVTVE", "text": "FUNCTION: Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins)."}
{"protein": "MRTPMLLALLALATLCLAGRADAKPGDAESGKGAAFVSKQEGSEVVKRLRRYLDHWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV", "text": "FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family."}
{"protein": "MSVSALRLIRVRRLSTSGPAVKRALPWRDIRRIAKVTGAIVFGGCVFITYEVVTLNQALTIDTSAILQEKQKSYIYPTHSTNREQESLASGLTIKTRRELHKAARKFLEITSRVLHHPLDEHLSHLDADPHECALWVLLKRSRSADRAVRHLAVQELAHNHHWRDYQYQTAAQVVDQRTAVALARIPNVDLRFFLPPPPLPHTEDDISIEDGLRQLLASLPQSDVDQCVQYFTSLALRESSQSLASQRGGLWCFGGNGLPYAQSLTSTPSEKVETFCLQALVQHSKVRSHCEHIVANGGLQLLQRVYQLRRDSPKIQRNIVRIIGNLALNENLHTTIVQSGWMSVLAEMIQSPHIMQASHAARALANLDRDAVRQKYQDGVYILHPQCRTNQPIKADVLFVHGLLGAAFKTWRQKDCDVTDDEKLEGVREDYTECWPKSWLAADCPNLRILSVEYDTHLSDWNSKCPVENQRKSLAFRSQELLRKLKDAGVGERPVIWVAHSMGGLLVKKMLLDAAKDPDLSSLIKNTKGILFYSVPHHGTFMAEYSVSVRYLLFPSIEVKELCRDSPALRDLNENFLNIAKDREFKVLSFAETVPTYIGPMLKILVVPAHSADLGIGDLIQVDVDHLNICKPEKKDTFLYKRTLQFIQDALGGRRIK", "text": "FUNCTION: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation-acylation reaction to produce phosphatidylglycerol-36:1. May be involved in bis(monoacylglycerol)phosphate biosynthetic pathway (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Endoplasmic reticulum Mitochondrion Note=Localizes at the endoplasmic reticulum and at the endoplasmic reticulum-mitochondria interface. SIMILARITY: Belongs to the SERAC1 family."}
{"protein": "MADTRELPVFAYIDDIKQLQELRQYLNKHESVKLDPTGPAETAKNLVEICSTLHVLPLWSQDVDLVLNSISSLIVVVPGEKCEPVVDAFIKNVSPKFYKGIGWGSHAGIAVRVLSNLYKGYSNFHTVQEKIFMALVDMCAEARLIGELECNLETLHDRFNTWQTPVEGQREILRAVHRALLVDQRADQAAKVMTALLGTYTEKDAATARDDAMECVRTAVVDPKSFSFDHLERLSAVKALKSSDPLMFTALELFISGTLKDYQQFVAKNPKFVTDYLKVDEVILLKKIRLLTLMSLAEEKNEIKLDELAKQLDIHADETLEEFVIDAIQVNAISGKINEMANTLIVSSYQHRRFGSDQWVLLEKRLKVLIANLKQTHNNVHEVNQRIEAL", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-1 targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit M family."}
{"protein": "MPVNCSSCEERRAVLRRPKTGHSLCKDCFFHAFEEEIHHTIVSAKLFNPGEKVGIGASGGKDSTVLAHVLKVLNERYAYGLDLILVSVDEGISGYRDDSLETVKRNQQQYELPLKIVSYQELYGWTMDQIVKQVGLKNNCTFCGVFRRQALDRGAMMLGVNKICTGHNADDIAETVLMNFLRGDIARLRRCTSITTGSEGAIPRCKPLKYAYEKEIVLYAYFKKLDYFSTECIYSPNAYRGHARAFLKDLEAIRPSSIMDIIHSGENLSVKEDVRMPVQGTCTRCGYISSQSLCKACVLLEGLNRGLPKLGIGKHHKLHHKLLSQEPLSEQEERKLKAVDF", "text": "FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily."}
{"protein": "MLRVLPRALRLPCSWRFSGARDCASHATTRTPEIQVQALTGPNQGITEILMNRPNARNALGNVFVSELLEALAQLREDQQVRVLLFRSAVKGVFCAGADLKEREQMSDVEVGTFVQRLRGLMSEIAAFPVPTIAAMDGFALGGGLELALACDLRIAASSAVMGLIETTRGLLPGAGGTQRLPRCLGVALAKELIFTGRRLNGAQARELGLVNHAVAQNEEGNAAYHRALALAQEILPQAPIAVRLGKVAIDRGMEVDIASGMAIEQMCYAQNIPTQDRLEGMAAFREKRAPKFVGK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MRPLCMTYWWLGLLATVGAATGPEADVEGTEDGSQREYIYLNRYKRAGESPDKCTYTFIVPQQRVTGAICVNSKEPEVHLENRVHKQELELLNNELLKQKRQIETLQQLVEVDGGIVSEVKLLRKESRNMNSRVTQLYMQLLHEIIRKRDNALELSQLENRILNQTADMLQLASKYKDLEHKFQHLAMLAHNQSEVIAQLEEHCQRVPAARPMPQPPPAAPPRVYQPPTYNRIINQISTNEIQSDQNLKVLPPSLPTMPALTSLPSSTDKPSGPWRDCLQALEDGHSTSSIYLVKPENTNRLMQVWCDQRHDPGGWTVIQRRLDGSVNFFRNWETYKQGFGNIDGEYWLGLENIYWLTNQGNYKLLVTMEDWSGRKVFAEYASFRLEPESEYYKLRLGRYHGNAGDSFTWHNGKQFTTLDRDHDVYTGNCAHYQKGGWWYNACAHSNLNGVWYRGGHYRSRYQDGVYWAEFRGGSYSLKKVVMMIRPNPNTFH", "text": "FUNCTION: Induces sprouting in endothelial cells through an autocrine and paracrine action. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MQVIVALAALGSLAAPALGFSIPRGVPVSQSMIDVKLSSTGNSMVKATITNNGNRALNLLKFHTIMDSNPTRKVSIESEDGKEIQFTGMMPTYKEKDLKPSYFIFLPPKGTVEHSFDIARTHDLSRGGKFTLKAEGMVPIAEENGTEITGAAKYHSNELHMTIDGEKAASVENAFGIVKRGPLTRINKRTSIDMQSCGNNQELQALTAALKASAQLSSMSAQAVSQNQDKYMEYFKDPQYMQTVQSRFQAVAQESSSTTGGGTTYHCSDTMGGCEEGVLAYTLPSQNEVFNCPIYYSDLPPLSNECHAQDQATTTLHELTHNPAVQEPFCEDNGYGYERATALSAEKAVQNADSYALFANGKLNLITLMLIDPD", "text": "FUNCTION: Probable secreted metalloprotease that shows high activities on basic nuclear substrates such as histone and protamine (By similarity). May be involved in virulence. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M35 family."}
{"protein": "MSLLPPEQRQLLHRCILNYIRSQVPGDGAEGETGGQTEERHVMNSLAKWLRVDPDGLDGEKAADGSLLPRKWSSIVRLQRRIIELEKEIQELTDENENLRENGPSSPANGALKSWLPRERPSFSISAGASVTSVKLHPELPLVFIATDAGKLQCYDLMNYTMPVASVQAHMRGITAIDAYVGEDSQCLVATASKDLHCKVFRFVDSELQLIRTLSGHEHIVSHIKIWNNSTNTLVASCSRDLTCKVWDIANGWCLKSFQPHTEWVRCLDVMGDFVVTGSNDCTVRLSHWPTGRSLSFGTGHEFPVEKIRIIPLQPPESAEHSHRFNTHDEDYLPLGFSHVISTSRDGTLRIWQVPLPRFVAHRAPQPNPARPYFNLVATLKGHSSWVRDVRVRGKHAFSCSDDRSIKVWDLSTCEVVRSINNLHSGFINCIDIDCGGLNRQLLVSGGADGKLVILMK", "text": "FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein- mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules and the mitotic spindle poles. SIMILARITY: Belongs to the WD repeat LIS1/nudF family."}
{"protein": "MDEADFSEHTTYKQEDLPYDGDLSQIKIGNDYSFTSKKDGLEVLNQIIFIADDPQEKAMHSETCGNTAVTIPLGKITENAANKKDEKEKQCTAALHIPANEGDASKSSISDILLHHLSKEPFLRGQGIDCETLPEISNADSFEEEAIIKSIISCYNKNSWPKEQTPELTDQLNPKRDGENSNKPGSATTTEENTSDLEGPVAAGDSSHQENVNVLTKTKGPGDKQKSYQGQSPQKQQTEKANSGNTFKYGQGQVHYQLPDFSKIAPKVKIPKNKIINKPLAIAKQASFSSKSRDKPTLVQDSLETTPESNCVEKQHQEQKGKITEPSQQIQMEPIVHIHQELLTGIESEASLSKLSPTSQKGTSSSSSYIFQKISQGKQMCQKLKEQTDQLKTKVQEFSKRIKQDSPYHLQDKKLVLEKLQGHLELLEQNFLATKDKHLTLQQQVHKHESTIVGDFDPERKVEGEIFKLEMLLEDVKEKMDESKYTSAPSLPVSSPVTLDDLASTFSSLSNEIPKEHPGHPSGPRGSGGSEVTGTPQGGPQEAPNEELCELAPQTYLNGHYGDAAAQNKPDQVAMRLSSNSGEDPNGTPRRQDCAEMTAPSPSCAFCRRLLEWKQNVEKKGHGRINCGRFSIVLHEKAPHSDSTPNSDTGHSFCSDSGTEMQSNKCQDCGTKIPTSRRACRKEPTKEFHYRYNTPGQNYSNHSKRGAFVQPHSLDESKNSSPSFLKPKRICSQRVNSKSFKGEHEPTPGKKKLQAFMTYSSDPATPSPHFYSCRISGSKSLCDFDSTEEIKSEILNSALDHALRTATILKETTDQMIKTIAEDLAKAQRWRNRLKY", "text": "SIMILARITY: Belongs to the AKNA family."}
{"protein": "MSKRNPKILKIFLYMLLLNSLFLIIYFVFHSSSFSPEQSQPPHIYHVSVNNQSAIQKPWPILPSYLPWTPPQRNLPTGSCEGYFGNGFTKRVDFLKPRIGGGGEGSWFRCFYSETLQSSICEGRNLRMVPDRIVMSRGGEKLEEVMGRKEEEELPAFRQGAFEVAEEVSSRLGFKRHRRFGGGEGGSAVSRRLVNDEMLNEYMQEGGIDRHTMRDLVASIRAVDTNDFVCEEWVEEPTLLVTRFEYANLFHTVTDWYSAYVSSRVTGLPNRPHVVFVDGHCTTQLEETWTALFSGIRYAKNFTKPVCFRHAILSPLGYETALFKGLSGEIDCKGDSAHNLWQNPDDKRTARISEFGEMIRAAFGLPVNRHRSLEKPLSSSSSSASVYNVLFVRREDYLAHPRHGGKVQSRLINEEEVFDSLHHWVATGSTGLTKCGINLVNGLLAHMSMKDQVRAIQDASVIIGAHGAGLTHIVSATPNTTIFEIISVEFQRPHFELIAKWKGLEYHAMHLANSRAEPTAVIEKLTEIMKSLGC", "text": "FUNCTION: Glycosyltransferase involved in the xylosylation of N-glycans (PubMed:10781814, PubMed:12943552, PubMed:15013764, PubMed:15686448). Possesses beta-1,2-xylosyltransferase activity, transferring xylose from UDP-xylose to the core beta-linked mannose of N-glycans (PubMed:10781814, PubMed:12943552, PubMed:15013764, PubMed:15686448). Involved in the biosynthesis of glycoprotein bound N-glycans (PubMed:15686448, PubMed:22024534). Does not require metal ions for its activity (PubMed:15686448). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Note=Localizes in medial cisternae of Golgi apparatus."}
{"protein": "MATAASTSAAAVAAASRLLVRRAPPRLLRRLPRAALAASRPSPPSSSSYGAAAVALGRQPLGHRARMGHTAAAAAAAGPALGLTKPNAVEPPQVSFAAKDVEFSEWKGDILAIAVTENDLVKGSDSKFENAVLKKLDGQLGGLLSEASAEEDFTGKAGQSVVLRLPGQGFKRVGLIGLGQNAPSTTTACKGIGESVASVAKSAQASSAAIVFASVGGIQEDFKLTAAAAIASGTVLGLHEDSRYKSESKKVHLKQVDLIGFGSGPEVDQKLKYANDLSSGVIFGKELVNSPANVLTPAVLAEEASNIASTYSDVFTATILDVEKCKELKMGSYLGVAAASANPPHFIHLCYKPPGGNAKRKLAIVGKGLTFDSGGYNIKTGPGCSIELMKFDMGGSAAVFGAAKALGQIKPPGVEVHFIVAACENMISGTGMRPGDIVTASNGKTIEVNNTDAEGRLTLADALVYACNQGVDKIIDLATLTGACVVALGPSIAGIFTPSDELAKEVAAASEISGEKFWRMPLEESYWESMKSGVADMVNTGGRQGGSITAALFLKQFVDEKVQWMHIDMAGPVWNDKKRAATGFGVSTLVEWVLKNSS", "text": "FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the peptidase M17 family."}
{"protein": "MMAAGAALALALWLLMPPVGVGGAGPPPIQDGEFTFLLPAGRKQCFYQSAPANASLETEYQVIGGAGLDVDFTLESPQGVLLVSESRKADGVHTVEPTEAGDYKLCFDNSFSTISEKLVFFELIFDSLQDDEEVEGWAEAVEPEEMLDVKMEDIKESIETMRTRLERSIQMLTLLRAFEARDRNLQEGNLERVNFWSAVNVAVLLLVAVLQVCTLKRFFQDKRPVPT", "text": "FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side. Plays a positive role in IL-33-mediated IL-8 and IL-6 production by interacting with interleukin-33 receptor IL1RL1. Plays also a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMP24/GP25L family."}
{"protein": "MEISDILFDDLVVGEINDDFICVICSHLQVDIYQCVEGHFACKNCFLKMIELKKQCMTCRCEIKSIESLSKNRYLEKEVRKLNIYCPNSFSDLKNSIKDENACKDIITIEGLETHLKNCKFTLKECPNNKNCNDDNKNKECLKIRQGEFDHHLKECPNSLIKCEHCSIEITRSKQTDHIENHCLKVLKQCEFCFKLIERGEFNNHQDTICLSKLIKCPFNEGGCVDLVKRSDIKEHLSVLAGEHLLYSITMINSLSLKLEKSNSELQESISYSRLLKKDFKELKKSKSYSGRWVIEKWSEKLKQYGKGQSIQFQKFNTSTSPSSAFSYFTLRLFPNGQYNGETISIHLVKLFRNKSRISFSFEIENHINPSSNEEIDSRFLFGNLNDYYSTIFYKEYNKENGFISEDDTLVIHFNVEILKYYDDTFITK", "text": "FUNCTION: Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TNF receptor-associated factor family."}
{"protein": "MATMAATKVPEVRDVTRIERIGAHSHIRGLGLDDALEPRQVSQGMVGQLASRRAAGVILEMIKEGKIAGRAVLIAGQPGTGKTAIAMGMAQALGSDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEVQIDRPATGTGAKVGKLTLKTTEMETIYDLGTKMIESLTKEKVQAGDVITIDKATGKITKLGRAFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIECFSFLNRALESDMAPVLIMATNRGITRIRGTNYQSPHGIPIDLLDRLLIISTSPYNEKETKQILKIRCEEEDVDMSEDAYTVLTRIGLETSLRYSMQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFMFNEMKTDTMDTS", "text": "FUNCTION: Has single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). Proposed core component of the chromatin remodeling INO80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP- dependent nucleosome sliding (By similarity). Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes (By similarity). SUBCELLULAR LOCATION: Nucleus Dynein axonemal particle. SIMILARITY: Belongs to the RuvB family."}
{"protein": "MQIQCFESITQKYPQFPTALLANEEPIQNGEPFILYGTKLDITKLEKFQQKCGQNFQIFDVWMVAKNIIVLLKGQWFSDFIKFTHDVEVDIAKLDFSPKLSQAGLLVMDMDSTAIQIECIDEIAKLAGVGELVSAITESAMRGELDFEQSLRCRVGTLKGAPESILQQVRENLPLMSGLVETIQTLQKYGWKTAIASGGFTYFADYLKALLQLDFAASNQFDIEDGKLTGLVKGDVVDAQYKAKTLQHLLEEYGIDSRHSIAIGDGANDLAMMNVAGLGVAFHAKPKVQPQAQIVVNFADLTALLCLLSANDRI", "text": "FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P-Ser). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family."}
{"protein": "MVAEVQKQAPPFKKTAVVDGIFEEISLEKYKGKYVVLAFVPLAFSFVCPTEIVAFSDAAKKFEDQGAQVLFASTDSEYSLLAWTNLPRKDGGLGPVKVPLLADKNHSLSRDYGVLIEKEGIALRGLFIIDPKGIIRHITINDLSVGRNVNEALRLVEGFQWTDKNGTVLPCNWTPGAATIKPDVKDSKEYFKNANN", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:10681558, PubMed:11741925, PubMed:15210711). Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily."}
{"protein": "MLNKSFAMYVYVQQFHRDMPPTPVFVYGQSLQTATFPGPTIVARYNVPLYVTWENHLPDAHILPWDPTVPTAIPKNGGVPTVVHLHGAAQAPDSDGHAFAWFTRDFAENGSTWTQKTYTYPNVQPAAGNIWYHDHALGLTRASLLAGLLAAYIVEWPELEMPFNLPSGEFDLHLVIADRKFNVDGTIFMDTVGAVPSVHPQWQPEYFGEVITVNGKAWPFQAVQRRRYRLRILNASNARYLNIRFSNGLPFTVIASDATYLSRPVTVSNLLLSPAEIFDVIVDFSLVVNPNATDIELLNSAPYPFPTGTPANATLDGKVMAFNVSAKWQVGDDMPMQEPENSTVVPEIGVPFAKVTALPPTMKTRYIVLYENMTSNDPNTAKTMNLYINGLRLEDPPTETPISGTTELWHVINLTPDNHPLHLHLAEFQAVQMLQLVDPDTFKSCMLKHNDTFACNLDQHAVGALQPVPEEEKTWKNVVKIPPAYVTSVVVAFRLVHNNMPYPFDATAAPGYVYHCHILDHEDNAMIRPLTLLP", "text": "FUNCTION: Multicopper oxidase that may play a role in the maintenance of inorganic phosphate homeostasis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MAQINENYLKLPGSYLFSEIARRVNEFKVQNPDADIIRLGIGDVTRPLAPVVVEAMKQAVEEMGRAETFRGYGPEQGYDFLIEKIIANDYAPRGVQLGMDEVFVSDGAKSDTANFQEIFGVDNIMAVTDPVYPVYVDSNVMAGRTGNYDIEKGQYGRIIYLPCTEEGDMKPELPTAPVDMIYLCFPNNPTGMTLTKEELKVWVDYARENKAIILFDSAYEAFIREEGVPRSIYEVEGAREVAVEFRSFSKTAGFTGTRCAYTVVPKDIMIYDSTGEGHSLNKLWLRRQTTKFNGVSYPVQAGAAAVYTEEGKKQIQATIDYYMENARIIREGLQEAGFKVFGGVNAPYIWMKTPGTMGSWEFFDKLMTEAHVVGTPGAGFGANGEGFFRLTAFGTRENTEKAIERIKARMK", "text": "FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL- diaminopimelate. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily."}
{"protein": "MEVTGLSAPTVNVFISSSLNSFRSQKRYSRSLTVAEFKCKLQLVVGSPASCMELELYGPDDKFCCKLDQDDALLGSYPVDDGCRIHVIDHSGARLGEYEDISKVEKYEISQEAYEQRQDSIRSFLKRNKLGRFNEEERAQQEAENSQRLIEEEAQASTIPVGSRCEVRTPGQPPRRGTVMYVGLTDFKPGYWIGIRYDEPLGKNDGSVNGKRYFECQAKYGAFVKPSVVTVGDFPEEDYGLDEM", "text": "FUNCTION: Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer. Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Note=Colocalizes with microtubules. In differentiated neurons, located in the cytoplasm. In differentiating neurons, accumulates at the growth cone. SIMILARITY: Belongs to the TBCB family."}
{"protein": "MSEIKDVIVQGLWKNNSALVQLLGLCPLLAVTSTATNALGLGLATTLVLTLTNLTISTLRHWTPAEIRIPIYVMIIASVVSAVQMLINAYAFGLYQSLGIFIPLIVTNCIVVGRAEAFAAKKGPALSALDGFSIGMGATCAMFVLGSLREIIGNGTLFDGADALLGSWAKVLRLEIFHTDSPFLLAMLPPSAFIGLGLMLAGKYLIDERMKKRRAEAAAERALPNGETGNV", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrDE/RnfAE family."}
{"protein": "MLSRLSERCTIATGLEQVLRHYVWSAAWLRDAEPAAAASENIDLSGLMERAGRAAYDVFANLYTSQKHWLILVGSGNNGGDGYVIARHAREAGKIVTVLRMPHSKPLPTEAASAQHAWKAVGGTESTMSPGAPLQLPADVDLIVDGLLGTGICGPPREQYADVIRHINGLPVPRVAIDIPSGLNAETGEAAGACVKADHTATFICLKPGLLTGQAKDYVGQLHYRSLGLEDWMTAPERMRVALCRRVALDDVYEYFGIRRSALAHKGSCGKAILVGGDHGFGGAALMSAEACVTVGAGLTRVLTRPEYAAPLLTRCPEAMVTAVETDTGEQLKQQMLEAFEWASTLAVGPGLGTGAYGQAALTAALRHAELHQDKTLVLDADALNLLAGCLHGREGGAAAGARKHLPVLPNSIITPHPGEAARLLDCRVADVEKDRLAAARRLAAILGGTCLLKGPGTIVHCHSSAKTAIVDAGNAGMASGGMGDVLTGLLAGLAAQRMHDTFDTTCAGALVHGVAADMVAAEDGRGTRGIRATELIHRVPLIVNASGPSPASRQRPSGQ", "text": "FUNCTION: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity). SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD family. SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP family."}
{"protein": "MSCCGGNCGCGSGCQCGSGCGGCKMYPEMAEEVTTTQTVIMGVAPSKGHAEGLEAGAAAGAGAENGCKCGDNCTCNPCNCGK", "text": "FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals. SIMILARITY: Belongs to the metallothionein superfamily. Type 15 family."}
{"protein": "SKCFSPGTFCGIKPGLCCSVRCFSLFCISFE", "text": "FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. Potent paralytic toxin in vertebrate and invertebrate systems. Its binding appears to be voltage-dependent. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
{"protein": "MIKLDMTILDSLKENKALRKLLFSGHFGLEKENIRVTSDGKLALTPHPAIFGPKEDNPYIKTDFSESQIEMITPVTDSIDDVYNWLENLHNIVSLRSKNELLWPSSNPPILPAEKDIPIAEYKTPDSPDRKYREHLAQGYGKKIQLLSGIHYNFSFPEALIDGLYDEISLPNESKRDFKNRLYLKVAKYFMKNRWLLIYLTGASPVYLADFTKTKQEEKLRDGSSALHDGISLRNSNAGYKNKESLYVDYNSFDAYISSISNYIEAGKIESMREFYNPIRLKNAHTDQTVESLAKHGVEYLEIRSIDLNPLEPNGISKEALHFIHLFLIKGLLSEDRELCENNQQLADENENNIALNGLSKPAIKNCDNEEMALADAGLLELDKMNDFIQSLRPEDTYFQAIIEKQKERLLHPEKTIAAQVKEQSATAGFIEFHLNQAKTYMEETEALAYKLIGAEDMELSTQIIWKDAIARGIKVDVLDRAENFLRFQKGDHVEYVKQASKTSKDNYVSVLMMENKVVTKLVLAENNIRVPFGDSFSDQALALEAFSLFKDKQIVVKPKSTNYGWGISIFKNKFTTEDYQEALNIAFSYDSSVIIEEFIPGDEFRFLVINDKVEAVLKRVPANVTGDGIHTVRELVEEKNMDPLRGTDHLKPLEKIRTGPEETLMLSMQKLSWDSIPKANETIYLRENSNVSTGGDSIDYTAEMDDYFKEIAIRATQVLDAKICGVDIIVPRETIDRDKHAIIELNFNPAMHMHCFPYQGEQKKIGDKILDFLFE", "text": "FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine. SIMILARITY: In the N-terminal section; belongs to the glutamate-- cysteine ligase type 1 family. Type 2 subfamily."}
{"protein": "MKIIVPATSANLGAGFDSIGIAVNLYLTVEVLGESRDWKIDHDLGENIPTDERNLLLTTLSAVLEDKNVALSAKFHLKMTSEVPLARGLGSSSSVIIAGIELANQLAKLNLTSDEKLKLACEIEGHPDNVAPALLGNLVIASTVAGKTSHIVADFPSCALLAFVPDYELKTVESRKVLPNELTYKEAVAASSIANVLTASLLTNNLEVAGQMMEADRFHESYRASLIPELQLLREIGHEFGAYGTYLSGAGPTVMLLVPDDKLTLLTEKIMEKNLTGHLYPLKIDNKGLQVEESVF", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase subfamily. SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase subfamily."}
{"protein": "MASKYERILSDCRSKNVLWEDPDFPAVQSSVFYYQTPPFTFQWKRIMDLADSGSGAVAANSSAAPVFLNESAEFDVVPGKMGDRWLVSCLGLLSSLRNLFYRVVPADQTLASAHGVFRFRLWWCGEWVEVLVDDRLPTINGRLAFMQPQASNCFWAALLEKAIAKLHGSYEALKYGTRSDGLTDLLGGVVRQMPILSDNIRPQTLKELLTTTCIVTCLADKSATVAKKNLAERMPNGILVNVNYRLSSLDKVKTLMGDSVQLVCLKDTFSSKPFGEKTHFLGDWSPMSKTWERVSQVERARLIRQLGPGEFWLSFCDFVEIFSTMEVVYLDTETSNDEEMLKSRPLHWKMKMHQGQWKRGVTAGGCRNHESFHINPQLLISVQDEQDLVIALNQHTAVEPKVIGFTMYTWDGEYMLSECLQKDFFKNHVSYLNSDYGNTRHVSYHTHLEAGHYVLIPTTYEPAEEAHFTVRILGTGSFRLSCLETQTMILLDPFPALKSTDAERCGGPKVKSVCQYEPVYMQLADENKTINCFELHELLEACLPNDYIKGCANIDICRQVIALQDRSGSGRITFQQFKTFMVNLKSWQGVFKMYTKEKAGILRAERLRDALCDIGFQLSTDIMNCLIQRYIRKDGTLRLSDFVSAVIHLTTAFNQFHLKNYGQVNVIEVHLHDWIKSILSC", "text": "FUNCTION: Not known; does not seem to have protease activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C2 family."}
{"protein": "MATPLSQVRQNYHQDCEAAVNRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDRDDWENGLTAMECALHLEKNVNQSLLELHKLATEKNDPHLCDFIETHYLDEQVKAIKELGDHVTNLRKMGAPKYGMAEYLFDKHTLGHSDES", "text": "FUNCTION: Inhibits translation of various mRNA species in vitro. Associates with a 35S prosome-like particle that contains non- translated mRNAs in a complex with proteins. May be involved in pre- translational regulation of some mRNA. FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferritin family."}
{"protein": "MSEVLFPAVRRRVVRPLARLFPSLRMSHARVLERTDHMTTTLEHPPVQHAQADIASGVLDIETGGKGRLRGRNLQPEPADPALSPALIRRHGLRRGDLVEGVCGDRRTLTDVVRVNGRTPDRRSRPHFADLTPLHPHERLRLEHPAAGLAGRVVDLLAPVGKGQRGLIVAPPKTGKTVLLQQFAAAVAGNHPEARLMVVLLDERPEEVTDMRRSVRGEVYSSTFDRSARQHIALAELVIERAKRLVEAGEDVVILLDSLTRLCRAHNNAASSGGRTLSGGVDAGALLGPKRFFGAARKAEEGGSLTILATALVETGSRADDFYFEELKSTGNMELRLSREPASRRVFPAVEPVGSGTRREELLLSGAETTALRGLRRALVARDGQSGLETLLERLRRTPDNATFLRQVQPTLPAG", "text": "FUNCTION: Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template. SIMILARITY: Belongs to the Rho family."}
{"protein": "MRLLPRLLLLLLLVFPATVLFRGGPRGSLAVAQDLTEDEETVEDSIIEDEDDEAEVEEDEPTDLVEDKEEEDVSGEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVIVGLHQLLESRKRKRPVQKVEMGTSSQNDVDMSWIPQETLNQIMQSRRDKASPRRLPRKRAQKRSVGSDE", "text": "FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the TRAP-alpha family."}
{"protein": "MLAIATLHVALQVFGAFSLSHAAAVTLEHRSAGNSNIAAIPAKWDVYGYLFNVTVGSPPQNITMLSDMTWMAPFVRSGRCLSQFNPELCVAQGQSFFNEHDSTTFGNTTFAQATWPVTAFAPNFTVDYGRDKFCIGNICNKDILMQVSDFPYPGSVVPVIPFGGIFGLAPTPKTITETSEPVNFQAWKNGNMGPLVGWHTCEVLKSAASCQGGDAQLVFGGTDTTMYSAKKIQSYEIQNPEWLSDAFYPSTPPRSNYWTVVDEGSEGLGAPLSLNGYKYLVRHIKSAKLASKAIVQNIQQQGSSGYNTANQDWYTVSCDGLDEFPNLVYQLDGRKKYTISPGDYVTKLTDMPGSVCYLNVNVWKYGRTENGDARVVLLGKAFLKRKYLVLNFEERSFGLAPLLTG", "text": "FUNCTION: Secreted aspartic protease; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (PubMed:23932525). The other FUS cluster members are not essential for fusarin C biosynthesis (PubMed:23932525). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MGYQLFEFENLEDCHKALIERFKEFFNAALKKHHQVSVAFSGGRSPISLLQKLSVLDLKWHECLISLVDERIIEASHEDSNAKLLHDYLLQNNALKASFTPLLPEKISGDTNELLDFANQHFKQPHLAILGMGTDGHTASLFPETSAFLNEEKENIVLTKPTNAPYERLSMSINALENCEKLFLSISGVEKRGVLEKALKENAPYSLPIARILHSKKVTTEVFYAKN", "text": "FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily."}
{"protein": "MSITTMKGVTSESPAEALSRFQTTGLTLNNPKDLYWMTEFLKEEFYDKGNYYYPIKTVCDGELIETELFCPFEPKLSPHYIQLYNSRDERSNLYAVPPKKTDMKKYNRINCEKMGSLMAPNSNYDDTEMVSLFYSMMYYLNDQTAHLKLPEEDIQPELVDELNDHVLQYLSVFLSIFKPREPQDLERIWNFLDFYQPYFKKVDGKIILHEKYQGRTPPQIGLIKKITGYVLERFAPKKNITQVIYEVIRYIKGIKQEIKIRGDKSFTLSLKEYDEFRDQVTSSPMAHSITDLTYDDFSYKAYMNPLFIKLEDLTSEIITYFNDVCTCDRERLDDDPFNSVFILRDLHSLNYVKSCDLVVKHAHDKLSKFLEIKQTLLKESTNENEKKAIAQMIKTREDSLIGYTIHEICCVTNGYARDHKPLMKDYLEKNIFKKLKATN", "text": "FUNCTION: Magnesium-dependent glutamate N-prenyltransferase: part of the gene cluster that mediates the biosynthesis of kainic acid (KA) and derivatives, natural products with neurochemical activity acting as ionotropic glutamate receptor (iGluR) agonists, thus being neurotoxins (PubMed:30995339). Catalyzes the conversion of L-glutamic acid (L-Glu) to prekainic acid in the presence of dimethylallyl diphosphate (DMAPP) (PubMed:30995339, PubMed:32457155). Can also use geranyl diphosphate (GPP) as substrate, thus leading to the formation of N-geranyl-L- glutamic acid (L-NGG) (PubMed:32457155, PubMed:30995339). SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MPRAPKRQRCMPEEDLQSQSETQGLEGAQAPLAVEEDASSSTSTSSSFPSSFPSSSSSSSSSCYPLIPSTPEEVSADDETPNPPQSAQIACSSPSVVASLPLDQSDEGSSSQKEESPSTLQVLPDSESLPRSEIDEKVTDLVQFLLFKYQMKEPITKAEILESVIRNYEDHFPLLFSEASECMLLVFGIDVKEVDPTGHSFVLVTSLGLTYDGMLSDVQSMPKTGILILILSIVFIEGYCTPEEVIWEALNMMGLYDGMEHLIYGEPRKLLTQDWVQENYLEYRQVPGSDPARYEFLWGPRAHAEIRKMSLLKFLAKVNGSDPRSFPLWYEEALKDEEERAQDRIATTDDTTAMASASSSATGSFSYPE", "text": "FUNCTION: Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNLSFCVQALLLLWLSLTAVCGVPLMLPPDGKGLEEGNMRYLVKPRTSRTGPGAWQGGRRKFRRQRPRLSHKGPMPF", "text": "FUNCTION: Endogenous ligand for the apelin receptor (APLNR) (PubMed:11336787, PubMed:11359874, PubMed:26611206). Drives internalization of the apelin receptor (PubMed:11359874). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (PubMed:11336787). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates (By similarity). Plays a role in early coronary blood vessels formation (By similarity). Mediates myocardial contractility in an ERK1/2-dependent manner (PubMed:26611206). May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior (PubMed:10617103, PubMed:11359874). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Note=Abundantly secreted in the colostrum (By similarity). Lower level in milk (PubMed:10525157). Decreases rapidly within several days after parturition in milk, but is still detectable even in commercial milk (By similarity). SIMILARITY: Belongs to the apelin family."}
{"protein": "MEHFDVAIIGLGPAGSALARKLAGKMQVIALDKKHQCGTEGFSKPCGGLLAPDAQRSFIRDGLTLPVDVIANPQIFSVKTVDVAASLTRNYQRSYININRHAFDLWMKSLIPTSVEVYHDSLCRKIWREDDKWHVIFRADGWEQHITARYLVGADGANSMVRRHLYPDHQIRKYVAIQQWFAEKHPVPFYSCIFDNAITDCYSWSISKDGYFIFGGAYPMKDGQTRFTTLKEKMSAFQFQFGKAVKSEKCTVLFPSRWQDFVCGKDNAFLIGEAAGFISASSLEGISYALDSADILRSVLLKQPEKLNTAYWRATRKLRLKLFGKIVKSRCLTAPALRKWIMRSGMAHIPQLKD", "text": "SIMILARITY: Belongs to the CbrA family."}
{"protein": "MKKIVSLVCVLVMLVSILGSFSVVAASPVKGFQVSGTKLLDASGNELVMRGMRDISAIDLVKEIKIGWNLGNTLDAPTETAWGNPRTTKAMIEKVREMGFNAVRVPVTWDTHIGPAPDYKIDEAWLNRVEEVVNYVLDCGMYAIINVHHDNTWIIPTYANEQRSKEKLVKVWEQIATRFKDYDDHLLFETMNEPREVGSPMEWMGGTYENRDVINRFNLAVVNTIRASGGNNDKRFILVPTNAATGLDVALNDLVIPNNDSRVIVSIHAYSPYFFAMDVNGTSYWGSDYDKASLTSELDAIYNRFVKNGRAVIIGEFGTIDKNNLSSRVAHAEHYAREAVSRGIAVFWWDNGYYNPGDAETYALLNRKTLSWYYPEIVQALMRGAGVEPLVSPTPTPTLMPTPSPTVTANILYGDVNGDGKINSTDCTMLKRYILRGIEEFPSPSGIIAADVNADLKINSTDLVLMKKYLLRSIDKFPAEDSQTPDEDNPGILYNGRFDFSDPNGPKCAWSGSNVELNFYGTEASVTIKSGGENWFQAIVDGNPLPPFSVNATTSTVKLVSGLAEGAHHLVLWKRTEASLGEVQFLGFDFGSGKLLAAPKPLERKIEFIGDSITCAYGNEGTSKEQSFTPKNENSYMSYAAITARNLNASANMIAWSGIGLTMNYGGAPGPLIMDRYPYTLPYSGVRWDFSKYVPQVVVINLGTNDFSTSFADKTKFVTAYKNLISEVRRNYPDAHIFCCVGPMLWGTGLDLCRSYVTEVVNDCNRSGDLKVYFVEFPQQDGSTGYGEDWHPSIATHQLMAERLTAEIKNKLGW", "text": "FUNCTION: Multifunctional enzyme involved in the degradation of plant cell wall polysaccharides. Displays endoglucanase activity against carboxymethyl cellulose (CMC) and barley beta-glucan (PubMed:3066698, PubMed:1991028). Also catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc) (PubMed:19338387). SUBCELLULAR LOCATION: Secreted. SIMILARITY: In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family. SIMILARITY: In the C-terminal section; belongs to the carbohydrate esterase 2 (CE2) family."}
{"protein": "MADKLFSIRNYFFLGSYQSCIGEALKFSSKNEEEKQEKDVYLYRSYIAQGQAFIPLKEIPAATKSADLAAVRRYAEFRNNPAAKKKILAEVQEEVASRNIKSEIAAVLAATILNEADLSQDAFRAVSRFEGLEARASKVFILIKMNKRKLAIGEVKKMNQIDEDATLSQLANALVTSFGASGKVKDALYIYSEMSDKYGRTTDLEMHQAVVSILTQDYAAAEELLESALERDNKDADVLINSIVSAQLNEKDDDVVERFISQLKHEHPNHPWVIDFNEKEAEFDRVASDSRA", "text": "FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. SIMILARITY: Belongs to the COPE family."}
{"protein": "MSYVIDRRLNGKNKSTVNRQRFLRRYREHIKKAVEEAVSRRSIMDMEHGEQISIPGRDIDEPVLHHGRGGKQTIVHPGNKEFTAGEHIPRPQGGGGGGGRGKAGNSGEGMDEFVFQITQEEFLEFMFEDLELPNLVKRHLTGADTFKTVRAGIANEGNPSRINIVRTLRSAHARRIALTGSSRALLREAQKELDRLRVEEPDNFTDIQEVEQEIERLKARINRLPFLDTFDLKYNLLVKQPNPSSKAVMFCLMDVSGSMTQATKDIAKRFFILLYLFLKRNYERIEVVFIRHHTSAREVDEEEFFYSRETGGTIVSSALKLMQEIMAERYPASDWNIYAAQASDGDNWNDDSPICRDILSKQIMPHVQYYTYVEITPREHQALWYEYERIGDAFPDTFAQQQLVSAGDIYPVFRELFQRRLAT", "text": "SIMILARITY: Belongs to the UPF0229 family."}
{"protein": "MRVAGAAKLVVAVAVFLLTFYVISQVFEIKMDASLGNLFARSALDTAARSTKPPRYKCGISKACPEKHFAFKMASGAANVVGPKICLEDNVLMSGVKNNVGRGINVALANGKTGEVLDTKYFDMWGGDVAPFIEFLKAIQDGTIVLMGTYDDGATKLNDEARRLIADLGSTSITNLGFRDNWVFCGGKGIKTKSPFEQHIKNNKDTNKYEGWPEVVEMEGCIPQKQD", "text": "FUNCTION: May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition. SUBCELLULAR LOCATION: Secreted Cytoplasmic vesicle Note=Cytoplasmic in some cancer cells. SIMILARITY: Belongs to the FAM3 family."}
{"protein": "MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGPGDSPTFPRFRAIQLEPAEPGQAWGRQSPRRLEDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSLEPEEPKRPVPAERGSSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGPGRERGESPTTPPTPTPAPCPTEPPPSPLICFSLKTPDSPPTPAPLLLDLGIPVGQRSAKSPRREEEPRGGTVSPPPGTSRSAPGTPGTPRSPPLGLISRPRPSPLRSRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFQGGPQDCRAQTKDMGAQAPWVPEAGP", "text": "FUNCTION: Activates the JUN N-terminal pathway. Required for serum- stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen- stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Location is cell cycle dependent. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily."}
{"protein": "MALDLLVVSAGSLALKVLRVTPLITTTILLVNRLAQYFALSTFLPPHTSPKKIDHVGAAFQHWLQTVVPRVWTGVISIVLFTRVALILNLFVRPDDLAGSNARFLYGVGLFLSFAHLSVAPKMLKFEKRMMSPETVPHVAMELLAGWMKVNNIRFWIVDVPFWVVGVWATLEGLKA", "text": "FUNCTION: Part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety (PubMed:28365998). The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP-bound dec-4-enoate (PubMed:28365998). The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec- 4-enoyl-ACP thioester, which may be prone to spontaneous hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased electrophilicity of the carbonyl (PubMed:28365998). 2-hydroxydec-4-enoic acid can then be further oxidized by poxM to yield the alpha-ketoacid 2-oxodec-4- enoicacid, which is reductively aminated by the aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid (PubMed:28365998). The Hybrid PKS-NRPS synthetase poxE then performs condensation between the octaketide product of its PKS modules and the amino group of (S,E)-2- aminodec-4-enoic acid which is activated and incorporated by the adenylation domain (PubMed:28365998). The resulting aminoacyl product can be cyclized by the Diels-Alderase PoxQ and reductively released by the reductive (R) domain of poxE to yield an aldehyde intermediate (PubMed:28365998) (Probable). The released aldehyde is then substrate for a Knoevenagel condensation by the hydrolyase poxO followed by an oxidation at the 5-position of the pyrrolidone ring (PubMed:28365998). The presence of the olefin from the amino acid building block allows for migration of the substituted allyl group to occur (PubMed:28365998). This allylic transposition reaction takes place in a conjugate addition, semipinacol-like fashion to yield a succinimide intermediate (PubMed:28365998). Iterative two-electron oxidations of the C7 methyl of the succinimide intermediate to the carboxylic acid can be catalyzed by one of two remaining cytochrome P450 monooxygenasess poxC or poxD to yield oxaleimide A (PubMed:28365998). Subsequent oxidation yields the maleimide scaffold oxaleimide I (PubMed:28365998). Both oxaleimide A and oxaleimide I can undergo oxidative modifications in the decalin ring to yield the series of products oxaleimides B to H (PubMed:28365998). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MPGATSHVPLLSVVIPTYNRAALLDRTLGTLARQTTALEDFEVVVSDDGSTDTTRDVVRSYEDRLRIKYVFQEDLGYRVASARNGGARLASAPLLAFLDTGVLAGPQYVQSVLAAHAGPAPAKVVLGCCYGYDPRNPHPELHSLVEEFPPEEAVRRVGDAPWFQDMRLPEFTAVDFDLSRMHMPWLWFWTLNVSLPAADFWRVGGFDEDFTGWGGEDIELGYRLHAHGIPMTVSRESWGIEAPHERTHEANVSSLMLNCDRFVRKHPSLLPELFWAVTNRGIFGSVETERLRFEEWASQARGQQVLDEIAIGLDTLPPSQHTQRVAVFGSGTEGLPITPRQNVELFLCDYDEGVLARQESRDDAAVSTWHLSGLRTPWPDQHFDLVIITSRMDGPRQAWGEAFTKEAHRIASSVVEPSLRGD", "text": "FUNCTION: Involved in the biosynthesis of the antifungal agent validamycin A (PubMed:16632251). Catalyzes the final attachment of glucose from UDP-alpha-D-glucose to validoxylamine A to yield validamycin A (PubMed:16632251, PubMed:18563934). UDP-glucose is the most efficient glycosyl donor, whereas GDP-glucose and ADP-glucose are much less efficient (PubMed:16632251). ValG also utilizes UDP-galactose as substrate to produce the new validamycin analog, 4''-epi-validamycin A (PubMed:18563934). SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MAANPSGQGFQNKNRVAILAELQEKRKLLMQNQSSTNHPGASIALARSPLNKDFRDHAEQQHIAAQQKAALQHAHAHSSGYFITQDSAFGNLILPVLPRLEAE", "text": "FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Localizes to nuclear foci following DNA damage. SIMILARITY: Belongs to the SOSS-C family."}
{"protein": "MSRNLIVGLDVGTSKICTVVAEVNLNDQLEIVGIGTSISRGVRKGVLINIEAALDSISNSIEAAELISGCDITSLSVSMSGSSVEGTNSRGVVAINSKTREINEEDVERVIEAAKAIVIPMDREILHVIPQEFIVDGIPHIKNPIDMMGIRLEGEVHIITGSSSSSQNLVRCVNRAGFAVDEVVLGSLASSYATLSKEEREMGVLFIDMGKGTTDIILYIDGSPYYTGVIPIGVNRVTLDIAQVWKVPEDVAENIKITAGIAHPSILESQMETVIIPNLGTRPPQEKSRKELSVIINSRLREIFEMMKAEILKRGLYNKINGGIVLTGGGALFPGISNLIEEVFNYPARIGLPMSINGIGEEHIDPKFSSALGLVLYKHEQQKFNKLKKVSSKVKRKNKISSKLKGWFLKEWF", "text": "FUNCTION: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to the membrane through a conserved C-terminal amphipathic helix. SIMILARITY: Belongs to the FtsA/MreB family."}
{"protein": "MIKALIFDFDGLILDTETHEYEVLQEIFEEHGSVLPLSVWGKVIGTAAGFRPFEYLEEQIGKKLNHEELTQLRRERFAKRMESEKARPGVEAYLNAAKDLGLKIGLASSSDYKWVSGHLKQIGLFDDFEVIQTADDVEEVKPNPELYLLAAKNLGVSPAECLAFEDSVNGSIAAKRAGMKCVIVPNKVTGTLMFEDYDHRLESMAEMELALLLDHLNSQN", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family."}
{"protein": "MLQTSNYSLVLSLQFLLLSYDLFVNSFSELLRMAPVIQLVLFIIQDIAILFNIIIIFLMFFNTFVFQAGLVNLLFHKFKGTIILTAVYFALSISLHVWVMNLRWKNSNCFVWTDGLQTLFVFQRLAAVLYCYFYKRTAVRLGDPRFYQDSLWLRMEFMQVRR", "text": "FUNCTION: Required for ciliogenesis. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Cell projection, cilium Note=Localizes to vesicles en route to the base of cilium. SIMILARITY: Belongs to the TMEM138 family."}
{"protein": "MSDTTEVPRQSSENDQDNNLERTNSLKSPDVTNNIPSLFKLAAEWQINNPQETFQNHILENDVLKKINEITHLIRESYKDLSSQDGMMSKQQQEKMDWDLFCTVPVNIIEQYTKDMDEIYEKMERLAKQQRLWCESAFQIDVERCGDSILNAETWMKKKERHLEYKNIEMERSANEIKETIQRLTDDR", "text": "FUNCTION: Probable transcriptional activator involved in meiotic prophase and synaptonemal complex (SC) assembly."}
{"protein": "MDDDGGGSPGHYGGGGIHLVCEYCGHGSEYAEDDADDGFFTCRQCSAIHTSTQNTATNPFDFPMTPAHLSAHRRPTQPTPTPKPFPAPRGAATGAAAPDFDDLGEPSEPRDFATGANAWGNPEDVAARVRWRYVRGLQVILQRQLEALVERHRVGSLAASLAGTIWLRWVAASKVFDEMWVHKMLAIAASVEEGHSASKDKQSELEGDAQKSQSSYEFLFLRSLRMMLPVYSTLAVCFLACHVARETILPTDICRWAMEGKLPYVAAFTQVDKLLGSSLNDCPLSSRQLFRPTRVIGAWQLEAAAGSIAQKIGLLLPSVNFYLIAQRFLKELSLPIEKILPHACRIYEWAMPAELWLSSNPGRVPSRVCVMAILIVALRVLYGINGQGIWESIAQTENAVGSDPEASAPHSIEPDSNNSEEFDARELLCTLAASYDKINVGHDYSKEVHSYLKYCKDVVFTGMTFSLEEEHLIDIFWDMYKGKEVMLLDENAKLCQEKLRTTNGVNKRCRDGRFADTKCCSTPLGNCALQSIKSKMEENGFCYVSPRKRLVSDGYLLYTRRESSGSLIYVAHADYYILLRPFAKLAEVDVRVLHSSVLKLERRLGWIEERVGRSLNTLQNLHDEASDDERPVSD", "text": "FUNCTION: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRN7/TAF1B family."}
{"protein": "MRALIIVDVQNDFCEGGSLAVTGGAALARAISDYLAEAADYHHVVATKDFHIDPGDHFSGTPDYSSSWPPHCVSGTPGADFHPSLDTSAIEAVFYKGAYTGAYSGFEGVDENGTPLLNWLRQRGVDEVDVVGIATDHCVRQTAEDAVRNGLATRVLVDLTAGVSADTTVAALEEMRTASVELVCSS", "text": "FUNCTION: Is involved in the activation of the first-line antituberculous drug pyrazinamide (PZA) by converting it into the active form, pyrazinoic acid. FUNCTION: Catalyzes the deamidation of nicotinamide (NAM) into nicotinate (PubMed:18201201). Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide (By similarity). SIMILARITY: Belongs to the isochorismatase family."}
{"protein": "MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGDKGKQGGPTYYIATNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPVLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKRKEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQSFTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP", "text": "FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the actin family."}
{"protein": "MPLNGDLDRQIEQLMECKPLGEADVKILCDQAKAILVEEYNVQPVKCPVTVCGDIHGQFYDLIELFRIGGNAPDTNYLFMGDYVDRGYYSVETVSLLVALKVRYRDRLTILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALIESQVFCLHGGLSPSLDTLDNIRSLDRIQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDIATQFNHNNGLSLISRAHQLVMEGYNWCQEKNVVTVFSAPNYCYRCGNMAAILEIGEKMEQNFLQFDPAPRQVEPDTTRKTPDYFL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily."}
{"protein": "MAQQRALPQSKETLLQSYNKRLKDDIKSIMDNFTEIIKTAKIEDETQVSRATQGEQDNYEMHVRAANIVRAGESLMKLVSDLKQFLILNDFPSVNEAIDQRNQQLRALQEECDRKLITLRDEVSIDLYELEEEYYSSSSSLCEANDLPLCEAYWRLDLDTDSADGLSAPLLASPETGAGPLQSAAPVHSHGGGPGPTEHT", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 22 family."}
{"protein": "MAQGEVLEFEEIVRTRQDALLRTPPGLVPDPVDAQDLLQTALARTYGRWEGIADKRLADAYLRRVMINTRTEWWRARKLEEVPTEQLPDARVEDSTEQHADRALLMDAMKVLAPKQRSVVVLRHWEQMSTEETAAALGMSAGTVKSTLHRALARLREELETRDLDARALEREERERCAAA", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is required for the synthesis of the antibiotic actinomycin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily."}
{"protein": "MALAGKQYEGSLNNSRPNLWPSSIPGGKNEIITSLVTALDSMCTALSKLNTEVACIALHEESAFVVGTEKGRCFLNSRKELQADFQRFCIGAHKKDQENEVKRRNRDGIQNIQHVPLGPTSDIYLLRKMVEEIFEVLYSEALGKSNIVPVPYVKVMKEPGSVVVLGLPDGISFRKPAEYDLKSLMLILKHSHNIRFKLRIPTEESIREPKSCSELNSPPTSATKVIPETSQCHRLPIQEHPSSASNFPYSVSQPNQISLEPKQEVHSNMLGTNAVNQMLVQRPSAENNHDLSDCCGQQSPVAGSSLRQNVLASKHLLFSIVHDKTDKWDSFLRETEDINILRECVQILFNSRYAGALGLDHMVPVPYRKIACHPEAVEINGFPDKIPFKRPCTYGVPKLKRILEERHNIHFTIKSMFDQRIFDGTTFTKETTKSDSSSLGEEACSENQKAAALDMLGFPTGSRSEKSSISDECEPGTSSETTGVKLIKLEAEDPDIMQIAVPGTSSETSGVKIIKLESEDPDLIQITVPGTSNETSGVKPKLESEDPDLIQIAVPDRLAECVKNHLAPEDPSYVLDTGKVCDDRPCGVLRNENKHLDGIGDIIRQLRKHVENLFNRKYAKAIGASGPVKVPYAKFLMYPEDLFVLGLPEGVAFRRPNCFGITKLRRILEYSDGIQFVVKRPELISEGLEDCVVGSPGTLGFNDKSNEVILDETNTRPSFQESFDARLSRIDIANTLREQVQVLFNKKYGEALGIKYPVQVPYKRIKNNPGSVIIEGLPPGIPFRKPCTFGSQNLERILAVADKIRFTVTRPFQGLIPRPDDEDANRLGEKVILREQVKELFNEKYGKALGLDQPALIPYKLIRDNPDAVEVRGMPNDIPFRNPNSYDLHRLENILKAQDQIQMVVIKQLEPFPEICSEPPKIKNGNTGPKRKRKRVSEGNSISSASSNCSSSSSSSSNMDPISSAHHVSLVQWPMYMLDYGGLNMQLPGPINY", "text": "FUNCTION: Transcription factor that activates a subset of organizer- specific genes. Binds to the distal element (DE) of the gsc promoter to regulate its expression. In the presence of pou5f1.1/oct-25, forms a repression complex on the promoter of the gsc and mix2 genes to inhibit their transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFII-I family."}
{"protein": "MELLLFVMSLILLTFSKAIPLFNHNSFYFEKLDDCIAAVINCTKSEVPLLLEPIYQPPAYNEDVMSILLQPPTKKKPFSRIMVTDEFLSDFLLLQDNPEQLRTLFALIRDPESRDNWLNFFNGFQTCSPSVGITTCIRDNCRKYSPEKITYVNNFFVDNIAGLEFNISENTDSFYSNIGFLLYLENPAKGVTKIIRFPFNSLTLFDTILNCLKYFHLKTGVELDLLKHMETYNSKLPFRSSRPTILIRNT", "text": "FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH. SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein; Extracellular side Host cell membrane; Peripheral membrane protein; Extracellular side Host Golgi apparatus, host trans- Golgi network Note=gL associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the host trans- Golgi where secondary envelopment occurs. Found in Golgi-like bodies of fibroblasts. In T-lymphocytes, found in the endoplasmic reticulum. SIMILARITY: Belongs to the herpesviridae glycoprotein L family."}
{"protein": "MDPRLREEVVRLIIALTSDNGASLSKGLESRVSALEKTSQIHSDTILRITQGLDDANKRIIALEQSRDDLVASVSDAQLAISRLESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTELSTLTLRVTSIQADFESRISTLERTAVTSAGAPLSIRNNRMTMGLNDGLTLSGNNLAIRLPGNTGLNIQNGGLQFRFNTDQFQIVNNNLTLKTTVFDSINSRIGATEQSYVASAVTPLRLNSSTKVLDMLIDSSTLEINSSGQLTVRSTSPNLRYPIADVSGGIGMSPNYRFRQSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHICLPAFDGFSIADGGDLSLNFVTGLLPPLLTGDTEPAFHNDVVTYGAQTVAIGLSSGGAPQYMSKNLWVEQWQDGVLRLRVEGGGSITHSNSKWPAMTVSYPRSFT", "text": "FUNCTION: Fiber-like molecule that attaches the virion to the host cell membrane by binding to the primary receptor F11R/JAM-A and to sialic acid containing proteins (coreceptor). The interaction of sigma-1 with F11R is required for NF-kB activation and apoptosis. Binding to both sialic acid and F11R is required to induce maximal levels of apoptosis. SUBCELLULAR LOCATION: Virion. Note=Found in the outer capsid (36 copies). SIMILARITY: Belongs to the orthoreovirus sigma-1 protein family."}
{"protein": "MPRVEVGLVIHSRMHARAPVDVWRSVRSLPDFWRLLQVRVASQFGDGLFQAGLAGALLFNPDRAADPMAIAGAFAVLFLPYSLLGPFAGALMDRWDRRWVLVGANTGRLALIAGVGTILAVGAGDVPLLVGALVANGLARFVASGLSAALPHVVPREQVVTMNSVAIASGAVSAFLGANFMLLPRWLLGSGDEGASAIVFLVAIPVSIALLWSLRFGPRVLGPDDTERAIHGSAVYAVVTGWLHGARTVVQLPTVAAGLSGLAAHRMVVGINSLLILLLVRHVTARAVGGLGTALLFFAATGLGAFLANVLTPTAIRRWGRYATANGALAAAATIQVAAAGLLVPVMVVCGFLLGVAGQVVKLCADSAMQMDVDDALRGHVFAVQDALFWVSYILSITVAAALIPEHGHAPVFVLFGSAIYLAGLVVHTIVGRRGQPVIGR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. SIMILARITY: Belongs to the major facilitator superfamily. Drug:H(+) antiporter-3 (DHA3) (TC 2.A.1.21) family."}
{"protein": "MKEVRVVICGDQGVGKSSLISALIQEDNVTSIPKVFPIISIPSNPDSNDDVSLVLVDTQSDSNEREYLAAEIKKANVICLVYSDNYSYERVSIFWLPYFRSLGVNVPIVLCENKSEDLDNYQGLHTIEHEMIPLINEFKEIEACILCSALEKINVNELFYMCRACVIYPITPLWDAKERTMRKATIHALSRIFFLIDKNNDDLLSVDELNSLSEKCFSKNLSIEDASEILSKVKEICPEGVYEGQLTLPGFLAYNRVQVENGKQESTWGILRAFHYTDSLSLDDSYLSPKFEVAPGQIVELSPKGYRFLVDLFYQFDRDNDGALNNEELSALFRHTPGLPEIWVSSQFPNSTVLNEHGYVTYNGWLAQWSMITLFDYKTTLAYLAYLGFDTDGRGHNTDALKVMRKRVSQNRKVSKYDRNVFLCFVVGSKSCGKTALLSSFINNNTNRLTPNTVVNSVEFQSTQRYLVLSEIGETDLDILAEPKSLEACDILCLLYDSSNPNSFSFIANLLNLYPDLQKIPCVFAATKADLDRQQQRYPVQPDEFTKQLGLPSPTHISTAAIWNTSKEFFIQLAESAQYPASSIIRIPEEDSNKTNYQLVAALTAFGALLLSVGGSLTWKIIKHQYYSKK", "text": "FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the mitochondrial Rho GTPase family."}
{"protein": "MPAKKKTTRRNTKKELQKKAATRKMIAFFVGLLLILFALARLGIVGILLYNIVRLFIGSLAIILLLLVAAIMILSVFRKQFLKENKRIIPAIILTFIGLMFVFQIRLHQGLNETFHLIWSDLTAGRVIHFVGSGLIGAIITEPAKALFSVIGVYIIAAVLWLVAIYLMIPGLFPKMREDLHQRLAKWKEKRAEKVEAKKAVKALKKLEEEKEIPEPQTILPEAENSLFTSAPVEIPINIPEAPFEENENPVLEENPVDDEPVNFMNTNNYNGNYKLPTIDLLAEVPVKNQSGERENVRKNIGILEETFKSFGIGANVESAVVGPSITKYEIKLATGTKVSRVVNLSDDLALALAAKDIRIEAPIPGKSLVGVEIPNAEVAMVGFREMWEAGKTNPSKLLEIPLGKSLDGGIRTFDLTRMPHLLVAGSTGSGKSVAVNGIITSILMKALPSQVKFLMVDPKMVELSVYNDIPHLLIPVVTNPRKASRALQKVVDQMEERYELFSRYGVRNIAGYNEKVQRYNAESDEKMLELPLIVVIVDELADLMMVASKEVEDAIIRLGQKARAAGIHMILATQRPSVDVISGLIKANVPSRIAFAVSSGTDSRTILDTNGAEKLLGRGDMLFKPIDENHPVRLQGAFLSDDDVEAVVTFIKDQSEAQYDESFDPGEVDENQVGTGASNTGSGDPLFEEARNMVIIAQKASTAQLQRALKVGFNRASDLMNELEAQGIVGPAKGTTPRKVLVSPDGEFIGGVEE", "text": "FUNCTION: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the difSL recombination site, which is located within the replication terminus region (By similarity). Required for activation of the XerS recombinase, allowing activation of chromosome unlinking by recombination. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Located at the septum. SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family."}
{"protein": "GSAPPGDPVEGKHLFHTICILCHTDIKGRNKVGPSLYGVVGRHSGIEPGYNYSEANIKSGIVWTPDVLFKYIEHPQKIVPGTKMGYPGQPDPQKRADIIAYLETLK", "text": "SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MAFQFSNNPESNETTNNPAPHVLGLPRPPSVGGISSRVTDMSEDGDQSQTNTMSSHVPHRHSVSRRGPPPARSSIASTSQITNRPGSSASRLSRTHIPSLAASGFFRPMSSQRLQAHRGRPATNHTVSTEDWGDQMNQNRRSLISNSTFPNSLSAADQEVPPSRGTEFTDPIIPDRIHSNASPTANTTTVRSESANLIRDRERPPHLNLKVDYKGTNENETPERSPLSFLSLQNRNAPADNRDSRAHARLSSADSSPQSIEKKPELAKSRNKGRNYEYFVGNTIFLGGGRFQNSRDKPVNIATGLLVLVPTGLFFGFSGPWLWHNISPAIPVLFAYVFYLCFSSFIHASVVDPGVIPRNLHQMPPVDPSQDPLAIGPPTNDWVMVKLATSDVAAMDVPVKYCKTCSIWRPPRCYHCRVCDNCIETLDHHCVWLNNCVGRRNYRYFFAFVSTSTLLALFLLGASLAHILVYRSREGISFSDAIDKWRVPFAMVIYGALAAPYPASLWAYHLFLVGRGETTREYLNSHKFAKADRHRPFTQGNVIRNWIAVFGRPRPPTYMQFKEYYQEGDQRLSTVKRRFLPRNTEPQNDIEMQHVPPPNSA", "text": "FUNCTION: Palmitoyltransferase specific for Ras proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily."}
{"protein": "MKEIIAIIRPNKINRTKEVLDALGFSSMTANAVFGRGRQKAIVGEVTFAIQNKDLREEEGSMRYIPKRMISLVVPDEDASLVVESIMKVNKTGQIGDGKIFVCPIEDAVRVRTKESGEDAIL", "text": "FUNCTION: Could be involved in the regulation of nitrogen fixation. SIMILARITY: Belongs to the P(II) protein family."}
{"protein": "MSDICDANKLKHRFRGYFPVVIDVETAGFNSQTDALLEIAVTLLKMDDEGMLGIDKTLHFHIEPFEGANLEPAALAFNGIDPNNPLRGAVSEKEAFLDIFKAVKKAQKAADCHRCIIVAHNAAFDHGFVSKAIERCDLKRSPFHPFATFDTATLAGLAIGHTVLAKACMMAGIPFDNKEAHSALYDTERTAELFCYIVNRWKQLGGWPLLAAAGAQDAESDTEE", "text": "FUNCTION: Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis. SIMILARITY: Belongs to the RNase T family."}
{"protein": "MPDRTPDEVLRQTLAILAPGTDLRDGLERILRGRTGALIVLGFDRVVDSLSTGGFALDVEFSATRLRELAKMDGAIVLDRDVSRIVRAAVQLVPDSSIETSESGTRHRTAERVAKQTGFPVISVSQSMRIVAVYTGNRRYVLEGSDAILGRANQALQTLERYRARLDEVTGTLSALEIEDLVTVRDVCSVVQRIEMVSRIADEISGYVVELGVDGRLLSLQLDELVGGVGPDRELVVRDYLEASRYEGPLEAVLESLAGLHQSDLVDLSQVARVLGFSVGGDSLDSAVSPKGFRLLNRVPRLPGAIVERLVDQFGDLQKLLAASIDDLMTVDGVGEQRARAVREGLSRLAESSILERYV", "text": "FUNCTION: Participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions. FUNCTION: Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. SIMILARITY: Belongs to the DisA family."}
{"protein": "MKMFKSLRLLPHIVSPFQKCYSTDLISLVGVPRVKITKGQNRYLLVNIHTHGFTKYGRVIVRGADVDNHLAVFDSILEELEPEGICAKILGGGRILNEAENKKIKIYGTSRTFGGADHTRTRNILQAWTTYKDFKITVKQ", "text": "FUNCTION: JanA and janB regulate somatic sex differentiation. SIMILARITY: Belongs to the janus family."}
{"protein": "MASHEEILADKAIFAYLHRMIGDEGIELIRRFPTDKEYSDEELAEVTKINLNSVRNTLYTLYEHRLAKYRRIKNNETGWLTYLWELELDNMYDSVSKDLEIILEKLRKRYKYESENAFYNCPNCGNTITFSDAMDSQFVCQECENKMVHFDNDLLVNALQKRIARIEENLGHV", "text": "FUNCTION: Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation complexes. Seems to translocate with the RNA polymerase following initiation and acts by binding to the non template strand of the transcription bubble in elongation complexes. SIMILARITY: Belongs to the TFE family."}
{"protein": "MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDSRLKLLEIKPETSHLPGKTELITETEFITKMSVDLRRFLSCKLYTSEVDLPLKKDGFTSESTTLEALLRGEGIEKKMDTKEEDPIQEIQRVLENDENADEVNEEEDLEEDIPKRKNRPRGRPKTPTWKKIFQKNARGSGGGRRRNDAASQDDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAREQETRSSPVHRNENHKPQKGPDGVIIPNNYCDFCLGGSNMNKKSGRPEELVSCSDCGRSGHPTCLQFTTNMTEAVKTYQWQCIECKSCSLCGTSENDDQLLFCDDCDRGYHMYCLNPPVFEPPEGSWSCHLCRELLRERASAFGFQA", "text": "FUNCTION: Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4. In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex) and plays a role in neural development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the requiem/DPF family."}
{"protein": "MTEITDRYFDDLIARLTGLRGRLAEPMAKAAELITAAALADNRVYVFGTGHSHMMAEELHYRAGGLAITVPILCGAIMLQDGAAASSHFERIKGAVLPILERYGIREGDVLIVVSNSGVNAAPIEAARYAREKGAAVIAVTSVTYSNAIAKGRTQLLSLADVVLDNDAPAGDAVLEMEGSSLKVGPVSTALGVTILNAIFADVAAKLVGKGDAPIYLSANMPGSGEVNRELVARYRDRNPHL", "text": "SIMILARITY: Belongs to the UPF0309 family."}
{"protein": "MKLIILDRDGVVNQDSDAFVKSPDEWIALPGSLQAIARLTQADWTVVLATNQSGLARGLFDTATLNAIHDKMHRALAQMGGVVDAIFMCPHGPDDGCACRKPLPGMYRDIARRYDVDLAGVPAVGDSLRDLQAAAQAGCAPWLVQTGNGRKTLAQGGLPEGTRVCEDLAAVAEQLLQEA", "text": "FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GmhB family."}
{"protein": "MKTRIFIGSSSEGIDVAKRIKTFFAPEYDCFLWTDDIFRNNESFLETLVKSASLFDFGFMVFSADDKTTIRDQHFESPRDNVLFEYGLFLGRVGLDRAFVIAETDAKIPTDMLGITQTRYETIVNSKGIKVATDSLESSLQKLKKQIDENVQLGHLGLLPSTVIAISYFEGFVKLAAEWLVENTPELMINNHKFNKASLKIVMPESLDTDIKRSAMMYYKRHGLEEARIDTKHRNYPIHFASKTEDGILEVYDMPTILTGIDKAIDMYFRVGHIGKTNEQKLAEDHEMNNFKRVLQLLINEDAFCRECVEIIEPQP", "text": "FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system (PubMed:32839535). FUNCTION: The effector protein for this CBASS system. Binds c-di-GMP (synthesized by the cognate CdnE encoded upstream in the same operon) but not c-di-AMP, 2'-3'-cGAMP, 3'-3'-cGAMP or cUMP-AMP (tested without the N-terminal TIR domain) (PubMed:32877915). Upon activation by c-di- GMP forms filaments which hydrolyze NAD(+); filament formation is required for enzyme activation (By similarity). SIMILARITY: In the C-terminal section; belongs to the bacterial STING family."}
{"protein": "MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC", "text": "FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis. FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. SUBCELLULAR LOCATION: Host cell membrane; Lipid-anchor; Cytoplasmic side Virion Secreted Host Golgi apparatus membrane Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. SIMILARITY: Belongs to the lentivirus primate group Nef protein family."}
{"protein": "MASAPVLQPSPKRTVASHVPFADLCSTLERIQTCKSRPEKTKYFKDFLDSWRKFHSALHQKEKDVTDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPKDGKDAVKLLNYRTPTGSRGDAGDFAMIAYFVLKPRSPKRGRLTVEQVNELLDAIANNNAAKNKGLVKKSLLQLITQSTALEQKWLIRMIIKDLKLGVSQQTIFSIFHPDAAELHNVTTDLEKVCRQLHDPSVSLSDVSIMLFSAFKPMLAAIADVQQIEKQMNNQVFYIETKLDGERMQMHKDGDVYKYFSRNGFDYTQQFGASPVDGSLTPFIHNVFKSDIQNCILDGEMMAYNPETQTFMQKGNKFDIKRMVEDSDLQTCFCVFDVLMINDQKLAHESLSKRYKILSNVFTPLTGRIHVVHKKSARTRKEVIDALNEAIDNREEGIMVKDPMSTYKPDKRGEGWLKIKPEYVNGLMDELDLLIVGGYWGKGSRGGMMSHFLCAVAETPAPNEKPTVFHSICRVGSGYTMKELYDLGLKLAKHWKPYNRKDPPCNILCGTEKPEMYIEPCNSVIVQIKAAEIVNSDMYKTDCTLRFPRIEKIREDKEWYECMTLDMLEHLRSRAEGKLASKHLYIDEYDEPQEKKRRTVPKVKKVIGIAEQFKAPDLSNVNKVSSMFEDVEFCVMTGMGRYSKSELESRIAECGGSVVQNPGPDTYCVIVGAENVRVKNIIASNKYDVVKAEWLLQCFQSKMLVPWQPAFMIHMSPETREHFAREYDCYGDSYTADTDVAQLKEVFSRVKDNKKMPLDLIAELEERYSWNSCKLCIFRGNTIYVDYYAIINKPSTKIHGTRLSIRALELRFYGAKVVPLLEEGVSHVVIGEDHSRVKEMKALRRMFGKKFKIVSELWVTESVKEGVPKNETQFLI", "text": "FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination. Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed. Joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. LIG4 is mechanistically flexible: it can ligate nicks as well as compatible DNA overhangs alone, while in the presence of XRCC4, it can ligate ends with 2-nucleotides (nt) microhomology and 1-nt gaps. Forms a subcomplex with XRCC4; the LIG4-XRCC4 subcomplex is responsible for the NHEJ ligation step and XRCC4 enhances the joining activity of LIG4. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
{"protein": "MTDTSFKYFMLKKLAWYWSFVELIKGFVITLKYMFKPKVTLRYPMEKGPLSPRFRGEHALRRYPNGEERCIACKLCEVICPAQAIVIEAEEREDGSRRTTRYDIDMIKCIYCGLCQEACPVDAIVEGPNFEFATETREELMYNKEKLLRNGEVWEDAIALRLKKNRPYY", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family."}
{"protein": "MTLLYQMVHFALFASVAGECVTTLFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSSEDPTKWYTCILKDSVTETLPMVNMTGAISGYSSKQCLHHISACSKDMYVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATRHFPSIKDRNTCLLKNTQTGTPTSITKLHEVVSGFSLKSCGLSNLACIRDIFPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFLSEEWPTASERNLCLLKTSSSGLPSARFRKNRAFSGFSLQHCQHSVPVFCHSSFYRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYSPSQESCNGGKGKCYLKLSANGSPTKILHGTGSISGYTLRLCKMDNVCTTKIKTRIVGGTQSVHGEWPWQITLHVTSPTQRHLCGGAIIGNQWILTAAHCFNEVKSPNVLRVYSGILNQSEIKEDTSFFGVQEIIIHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGYRKLRDKIQNTLQKAKVPLMTNEECQAGYREHRITSKMVCAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWILEKTQGP", "text": "FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein subfamily."}
{"protein": "MLDATLKSQLKTYLERVTQPIEIVASLDDGAKSRELHDLLVEIASLSNLITFSADGTDARRPSFSLNRPGADISLRFAGIPMGHEFTSLVLALLQVGGHPSKASAEVIEQIQALEGEFNFETYFSLSCQNCPDVVQALNLMAVLNPNVRHVAIDGALFQDEVESRKIMAVPSIYLNGEVFGQGRMGLEEILGKIDTNAGARQAEKINAKEAFDVLVVGGGPAGAAAAIYAARKGIRTGVAAERFGGQVLDTLAIENFISVQETEGPKLATALEEHVKQYDVDIMNLQRGEALIPAAEGGLHEVRLAGGASLKAKTVILATGARWREMNVPGEQEYRGRGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVAQVTLIEFDSQLRADAVLQRKLRSLPNVNVITSALTTEVLGNGEKVTGLRYKDRSTDEQHEVALEGIFVQIGLLPNTDWLKGTVELSPRGEIIVDAKGQTSIPGVFAAGDVTTVPYKQIVIAVGEGAKASLAAFDHLIRTSAPA", "text": "FUNCTION: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein (By similarity). FUNCTION: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "KERAMHVGRKKGQIVDTVVQEQRPSVLLELGAYCGYSAVRMARLLLPSARLLTIELNPDNAAIAQQVVDFAGLQDRVTVVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGCGRFECTHFSSYLEYSQMVDGLEKAVYKGPGSPAQP", "text": "FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Single-pass type II membrane protein; Extracellular side. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family."}
{"protein": "MPYFTIDTNKPQDSISSAFLKKAPNVVPKALGKPESYVSIHVNGGQPMVFGGSEDPCPVCVLKSIGCVGPKVNNSHAEKLYKLLADELKIPKNRCYIESVDIEASSMAFNGSTFG", "text": "FUNCTION: Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MIF family."}
{"protein": "MEVSSEQQLFFMREAVALGERGRIFAPPNPWVGCVIVKNGCIIGRGWHKGIGSPHAEVCAFQDQTSSLVGADVYVTLEPCCHFGRTPPCVDLLIKSKVSSVYIALLDPDPRVCKRGVARLKEAGISVYVGIGHEEAKASLQPYLHQRETGLPWVVMKTAASLDGQTSDRRGISQWISGEQARLDVGRLRAESQAVIVGSRTVCLDNPRLSARMPSGDLYERQPLRVVVDSRGSVPLDARVWNPDSGNVLLATTEQCSKEHIQKLEDRGVEVWKSSPQQVDLKRLLQYLAEKGCLQVLVEGGARLHSAFWREHLVNAGVIYWGPKFLGDQGSPMLRDLQLCLDNAEHVKITKTFLVGDSVKTCFECVGREDG", "text": "FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate. SIMILARITY: In the C-terminal section; belongs to the HTP reductase family. SIMILARITY: In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MEWGSESAAVRRHRVGVERREGAAAAPPPEREARAQEPLVDGCSGGGRTRKRSPGGSGGASRGAGTGLSEVRAALGLALYLIALRTLVQLSLQQLVLRGAAGHRGEFDALQARDYLEHITSIGPRTTGSPENEILTVHYLLEQIKLIEVQSNSLHKISVDVQRPTGSFSIDFLGGFTSYYDNITNVVVKLEPRDGAQHAVLANCHFDSVANSPGASDDAVSCSVMLEVLRVLSTSSEALHHAVIFLFNGAEENVLQASHGFITQHPWASLIRAFINLEAAGVGGKELVFQTGPENPWLVQAYVSAAKHPFASVVAQEVFQSGIIPSDTDFRIYRDFGNIPGIDLAFIENGYIYHTKYDTADRILTDSIQRAGDNILAVLKHLATSDMLAAASKYRHGNMVFFDVLGLFVIAYPSRIGSIINYMVVMGVVLYLGKKFLQPKHKTGNYKKDFLCGLGITLISWFTSLVTVLIIAVFISLIGQSLSWYNHFYVSVCLYGTATVAKIILIHTLAKRFYYMNASAQYLGEVFFDISLFVHCCFLVTLTYQGLCSAFISAVWVAFPLLTKLCVHKDFKQHGAQGKFIAFYLLGMFIPYLYALYLIWAVFEMFTPILGRSGSEIPPDVVLASILAGCTMILSSYFINFIYLAKSTKKTMLTLTLVCAITFLLVCSGTFFPYSSNPANPKPKRVFLQHMTRTFHDLEGNAVKRDSGIWINGFDYTGISHITPHIPEINDSIRAHCEENAPLCGFPWYLPVHFLIRKNWYLPAPEVSPRNPPHFRLISKEQTPWDSIKLTFEATGPSHMSFYVRAHKGSTLSQWSLGNGTPVTSKGGDYFVFYSHGLQASAWQFWIEVQVSEEHPEGMVTVAIAAHYLSGEDKRSPQLDALKEKFPDWTFPSAWVCTYDLFVF", "text": "FUNCTION: Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M28 family."}
{"protein": "MNQTLETGTTTVGITLKDAVIMATERRVTMENFIMHKNGKKLFQIDTYTGMTIAGLVGDAQVLVRYMKAELELYRLQRRVNMPIEAVATLLSNMLNQVKYMPYMVQLLVGGIDTAPHVFSIDAAGGSVEDIYASTGSGSPFVYGVLESQYSEKMTVDEGVDLVIRAISAAKQRDSASGGMIDVAVITRKDGYVQLPTDQIESRIRKLGLIL", "text": "FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin- like activities. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MKKTIGLILILASFGSHARTEIATKNFPVSTTISKSFFAPEPRIQPSFGENVGKEGALLFSVNLTVPENVSQVTVYPVYDEDYGLGRLVNTADASQSIIYQIVDEKGKKMLKDHGAEVTPNQQITFKALNYTSGEKKISPGIYNDQVMVGYYVN", "text": "FUNCTION: Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. SUBCELLULAR LOCATION: Fimbrium."}
{"protein": "MPRKKPFSVKQKKKQLQDKRERKRGLQDGLRSSSNSRSGSRERREEQTDTSDGESVTHHIRRLNQQPSQGLGPRGYDPNRYRLHFERDSREEVERRKRAAREQVLQPVSAEVLELDIREVYQPGSVLDFPRRPPWSYEMSKEQLMSQEERSFQEYLGKIHGAYTSEKLSYFEHNLETWRQLWRVLEMSDIVLLITDIRHPVVNFPPALYEYVTGELGLALVLVLNKVDLAPPALVVAWKHYFHQCYPQLHIVLFTSFPRDTRTPQEPGGVLKKNRRRGKGWTRALGPEQLLRACEAITVGKVDLSSWREKIARDVAGASWGNVSGEEEEEEDGPAVLVEQLTDSAMEPTGPSRERYKDGVVTIGCIGFPNVGKSSLINGLVGRKVVSVSRTPGHTRYFQTYFLTPSVKLCDCPGLIFPSLLPRQLQVLAGIYPIAQIQEPYTSVGYLASRIPVQALLHLRHPEAEDPSAEHPWCAWDICEAWAEKRGYKTAKAARNDVYRAANSLLRLAVDGRLSLCFYPPGYSEQRGTWESHPETAELVLSQGRVGPAGDEEEEEEEELSSSCEEEGEEDRDADEEGEGDEDTPTSDPGSCLTARNPYALLGEDEC", "text": "FUNCTION: Possible regulatory or functional link with the histocompatibility cluster. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family."}
{"protein": "METKDIEILIQKFALQNAYKHGSVPQAGAVTGKLLGTHPELRPHAKELMPIVQKVLADIGQMSQDEIKAKLSEIAPELIEELSVKKEVRRGLPPLDTSMLKPGQKVTLRIAPNPNGPPSLGNARGIIVNHEYARMYDGVFIMRFDDTDPSIKKPMIEAYTWYVEHAKWLGCPPDKVVAASDRLPLYYEQAEKLIDLGKAYVCTCDNEVFHDLKEAGKPCPHRETPPAENMEKWKKMLAGGYGGKEAVLRIKTDIAHKDPAMRDWVAFRIVTEPHPKTGTKYMVWPMLDFESAMEDHFLGVTHIIRGKDLMKTADKQKYIYRYLGWEYPHVSHWGRVRLLGFGKFSTSVMKKGIEAGEYRGWDDPQLPTVVALKRRGIEPEAIRNVMINMGVTETDIEFSMDTLYAENRKIVDPKANRYFFVPDPVVLKVNGAPFTTAKAPLHPQDHKRGFREMCVAENPEILIPKSDADNARPGDILRLKDLYNVRITGSDPLTGDYIGNDLSVLKQGAKIVQWVTREGGVPTRVIGPDGEFHGIAECDIRNELNNVVQFERFAFVRIDTINGVVLAYYTHP", "text": "FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily."}
{"protein": "MAGGTIWKGYIHFADTDVAVKLHAAVKAERIQFHLLHKRDHVKLHQQMICAYEKIPVPTEAQTKGFEVEEGKYIIVDPDELEQTAPESSRMIEVHEFVKTGQIDPIFLDRVYYLEPDLHSEGYSELVGALQEMGAEGICTWTMRNRSYLGALQASGKILRLNTLRYADEVISVKSLELQESPVSEKELKIGSDLINQLTTPFQPQKFENEHEKKLQKLIEKKARGEKIALLRPRLLKPTASDKLLQALEESLKKVA", "text": "FUNCTION: With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. SIMILARITY: Belongs to the prokaryotic Ku family."}
{"protein": "APSLRLRF", "text": "FUNCTION: Neuropeptide. May be involved in the regulation of adult diapause. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
{"protein": "MVEVPSFRSNEHFPQLCDKVTVKWDKKRGRFVEAIEDIPIGTVVCVETGITVNVDPQNCYRCLKITENASFAYCKNCEEFYEPDEIACGEFDELGIFKLAAHLVFSYPFADIASLVQSSDPEPPSCAPKALSTQDIEAIFQLTPFPEIGEAFKAPAIQNAIKRIVESLETDENWGRLDQISRTMTFTKALRIMAERSAKNAHTIYSIEQIESQEDNLPMATGLFPISSIFNHSCTPNISGFFVRNTFIFVSQGVRAREELLDSYGVTYHQHTFEQRTNFLASVSGFICHCESCFKMKSLKVLEKPKKYPETIATNASCFTDITSYTENIPRGSKELENLIIAFARRPDSETYTELIFQFWKKFVENAKFRGITYDPYLVRPYVEMTILAWNKEVGCENEEKMSLLIVTHRLLRNCYVDLHPLSELVVKLVNVVANQNADEINRTLEKLKLRARMLWKYSEQSEDL", "text": "SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
{"protein": "MAAQVTESDQIKQFKEFLGTYNKLTENCFMDCVKDFTTREVKPEETTCSESCLQKYLKMTQRISMRFQEYHIQQNERWPQKPDY", "text": "FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the small Tim family."}
{"protein": "MVQKQQASAGPGTEPKKRRRVGFSPADTGVEANECIKIYLVSSKEEVDSSDISSVKPVDLNDFFDGDGKIYGYQGLKINVWINSISLHSYADITYQSTINGDKGITDLKSALQNIFAETIVDTKDEFLQTFSTQRDFIRNMVSNGEVMHAGATDGSSKNAEVVPSDPQVIRMEIGSPNAGLLYSRLVPLVLLFVDGSNPIDVTDPDWHLYLLIQKKEEKEDPLYRIVGFTAIYKFYRYPDRLRMRLSQILVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVEEPSEKFQHIRTCIDINRLRSFDPIKPDIDSAVQTLTKGKLSKKAQIPRFTPPLNAIEKVRESLKINKKQFLKCWEILIYLALDPIDKYMEDYTSVITNHVRTDILGKDIETPKKQVVDVPSSFEPEASFVVFKSVNGEEANTNVQVDENKPDQEQQLKQLVEERIREIKLVAEKVSKSGQTLKV", "text": "FUNCTION: Acetylates soluble but not nucleosomal H4 (By similarity). Acetylates 'Lys-12' of histone H4. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the HAT1 family."}
{"protein": "MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDIAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEGKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPQLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLMAIHQEKCRQEGTFKRLALPA", "text": "FUNCTION: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. SIMILARITY: Belongs to the NMT1/THI5 family."}
{"protein": "MNRNRKGHDLENIEHRFTDEDLAGLKEQKLFNGKWIILEKKEKRGAAYCYLVCDKPCKKFGILYLEIGEDNVTTIANQVDFYHQQSSLGYSHRFSALIDAGIINNHVFFMVVRIRAGPTLHDLLKCLSSDKMSVTTASFLAVDMISAIEILSASGWVLRNFDSKQWMLDIKTRQFYLADATDITVSSDKRHRAIDEIHLRTAESIDLHWKTGDLIYAPRSFVDRDQSHRMTELDMMEMMLYVLYDWTHGKLPWKSSKSRERIMEMKELFIENLQKEPEETNKVEQQIDVDVWFDIALRNFAKHLKVAKEEQEKLEKLPVRGGAWCPKGPRAGAQISTVNYRGIIDDFYKIVCSGRPAWALHWRDVMLDWDRKLENTPETSKMFEAYEKHQRSLEISEEWERLQATREHYTVMKNHTETEMAKNQAAIVEYLMPEEEAKEEPIDKKKDPEEEAAAAVVGKKRRGRKPKKKDDPKMELKDEVKDLKDFVVEESTSASSSAPKKRPCCSSGSPLKSSGGRRRGCEIRRK", "text": "FUNCTION: Nuclear factor required for the production of piwi- interacting RNA (piRNA) precursors (PubMed:24696457). Specifically required for piRNAs produced from loci associated with the Ruby motif (PubMed:24696457). Promotes binding of the transcription factor snpc-4 at piRNA genomic clusters (PubMed:25373775). Required for normal fertility (PubMed:24696457). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Concentrated in nuclear foci of pachytene germ cells (PubMed:25373775, PubMed:24696457). Colocalizes with snpc-4 in nuclear foci in a mutually dependent fashion (PubMed:25373775)."}
{"protein": "MKVASIFLLTALVLMSLSGNSGANILGREAKCTNEVNGCPRIYNPVCGTDGVTYSNECLLCMENKERQTPVLIQKSGPC", "text": "FUNCTION: In the male reproductive tract, binds to sperm heads where it modulates sperm capacitance by inhibiting calcium uptake and nitrogen oxide (NO) production. FUNCTION: Serine protease inhibitor which exhibits anti-trypsin activity. In the pancreas, protects against trypsin-catalyzed premature activation of zymogens. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKKTTLKFAALTLLGLSNLALADAASELQMRLAKVDVLSAEFVQTVTSGSGKNVQQGSGKLQIKRPNLFRMETKTPQETQIISDGKTLWFYDPFVQQVTAQWVKNAVNNTPFVLLTSNDKSHWHQYTVTQQSDTFVLKPTLSTSNIKQFDIRVDANGILRNFSTTEKDGQTNLYVLRNITNQTLSDSLFQFKPEKGVEVDDQRKK", "text": "FUNCTION: Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane) (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the LolA family."}
{"protein": "MENRWQVMIVWQVDRMRIRAWKSLVKHHMYISGKARGWFYRHHYESPHPRISSEVHIPLGDAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLYYFDCFSESAIRKAILGYRVSPRCEYQAGHNKVGSLQYLALTALITPKKTKPPLPSVKKLTEDRWNKPQKTKGHRGSRTMNGH", "text": "FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells. SUBCELLULAR LOCATION: Host cytoplasm Host cell membrane; Peripheral membrane protein; Cytoplasmic side Virion Note=In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor. Incorporated in virions at a ratio of approximately 7 to 20 molecules per virion. SIMILARITY: Belongs to the primate lentivirus group Vif protein family."}
{"protein": "MKRELEGSYESERKRGVAQVKAEYVVGAASNVRVDEEEAGSERFVQGEFGGKKNKKKRGQNKNRDNRQQKETHALCPKYVLADVTNQVDLCTFGDNCRFVHDIPTYLEHKRPEITDSVFKTCPVFETLGYCPMGFKCRFLSSHMDKETHKLLGEYPSDLASASHEINHITQDQKYDLIKKRFPFSKSELVLEILDSFQEENREMHREAEKVKEDQQDNEDEQKEKAPQVVQRELEAQKRRQRQKDLYLQYKDTRFFAQEKKPLDLRHKKIVSPLTTVGNLPYRRLMRTLGADVTYSEMALAVPLVQGTNSEWALPKAHESEYPGFGVQVACSKGWQASKAAEALATYIPNGISEINLNSGCPIDLLYRQGSGSALLDNPARMIRCLNAMNYVSGDIPITVKIRTGTKEGHPIADTLVRRLVFETDVAAITLHGRSRQQRYTKVADWDYVSQVAKALRQAEADFMESPQGKESHHDEKTRHTQFVGNGDIFNYTDWYQHLEDPEVDSCMVARGALIKPWIFEEINAQQHLDKTSSERLEILKTYSKFAMDHWGTDEYGIALGRRFFCEFMSFFHRYIPVGILERVPVQLNERPPLWKGRDDMETLLGSSDVKDWIKLSEMFFGPTEDSFVFTPKHKSSSYK", "text": "FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the Dus family. Dus3 subfamily."}
{"protein": "MAEQQKIKKSPHVLLIPFPLQGHINPFIQFGKRLISKGVKTTLVTTIHTLNSTLNHSNTTTTSIEIQAISDGCDEGGFMSAGESYLETFKQVGSKSLADLIKKLQSEGTTIDAIIYDSMTEWVLDVAIEFGIDGGSFFTQACVVNSLYYHVHKGLISLPLGETVSVPGFPVLQRWETPLILQNHEQIQSPWSQMLFGQFANIDQARWVFTNSFYKLEEEVIEWTRKIWNLKVIGPTLPSMYLDKRLDDDKDNGFNLYKANHHECMNWLDDKPKESVVYVAFGSLVKHGPEQVEEITRALIDSDVNFLWVIKHKEEGKLPENLSEVIKTGKGLIVAWCKQLDVLAHESVGCFVTHCGFNSTLEAISLGVPVVAMPQFSDQTTNAKLLDEILGVGVRVKADENGIVRRGNLASCIKMIMEEERGVIIRKNAVKWKDLAKVAVHEGGSSDNDIVEFVSELIKA", "text": "FUNCTION: Involved in the biosynthesis of steviol glycosides in leaves (PubMed:15610349). Converts steviol to the mono-glycoside steviolmonoside (PubMed:15610349). Converts the mono-glycoside steviolmonoside to the bi-glycoside rubusoside (PubMed:15610349). Converts the bi-glycoside steviolbioside to the tri-glycoside stevioside (PubMed:15610349). Converts the tri-glycoside rebaudioside B to the tetra-glycoside rebaudioside A (PubMed:15610349). SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MYHGMNPSNGDGFLEQQQQQQPQSPQRLLAVILWFQLALCFGPAQLTGGFDDLQACADPGIPENGFRTPSGGVFFEGSVARFHCQDGFKLKGATKRLCLKHFNGTLGWIPSDSSICVQEDCRIPQIEDAEIHNKTYRHGEKLIITCHEGFKIRYPDLHNMVSLCRDDGTWNNLPICQGCLRPLASSNGYVNISEFQTSFPVGTVIYYRCFPGFKLDGSAYLECLHNLIWSSSPPRCLALEVCPLPPMVSHGDFVCHPRPCERYNHGTVVEFYCDPGYSLTSDYKYITCQYGEWFPSYQVYCIKSEQTWPSTHETLLTTWKIVAFTATSVLLVLLLVILARMFQTKFKAHFPPRGPPRSSSSDPDFVVVDGVPVMLPSYDEAVSGGLSALGPGYMASVGQGCPLPVDDQSPPAYPGSGDTDTGPGESETCDSVSGSPELLQSLYSPPRCQESTHPASDNPDTIASTAEEVASTSPGVDIADEIPLMEEDP", "text": "FUNCTION: Acts as complement inhibitor by disrupting the formation of the classical C3 convertase. Isoform 3 inhibits the classical complement pathway, while membrane-bound isoform 1 inhibits deposition of C3b via both the classical and alternative complement pathways. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MEKLLALIVVLVILLSLALFYLCNILWLRAVKIRKKLRRQGIRGPKPTFLYGNTKEIKRIRQELKLSQKQGTNNFISTLFPHFLLWRETYGPVFLYSTGAMEILQVSHPDMVKDIGRWTPSELGKPNYLKKSRKALFGGGLFTENGDEWAYQRKIIAPEFFMDKIKGMIQLIEDATVPVLEAWEDMIDDEGGCREIVVDDYLRNLSADVIARACFGSSFTKGEEIFCKLRQLQKAIARQDSFVGLSALWKYLPTKSSQEIQMLDEQVRLLILDVAKEQHHYQDSHNSLVNAIIDGAQDGRSAAEAEDFIVGNCKTIYFGGHESTAVTAIWCLMLLATHPEWQERARAEAMEVCRGRSTLDVDALRRLKIVTMVIQETLRLYPPASVMMREALTDVKLGSIEVPRGTIVQVPRLMLHLDKEAWGADADEFRPDRFANGVAAACRAAHMYVPFGHGPRTCIGQNLAMAELKVVLARLLTKFAFSPSPRYRHSPAFRLTIEPGFGLPLMVTKLP", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MLPYKTLLLALGFFFTVQCHFFASASSFDIADNNQNGVRLLRSPEKTDEERGAVDALKSELSFMKLNWAARSKITPKEKLVAKQAKEMSNTKEKLSKIEAKLQAKAVKAEQKVKDQAIKAEQNLKAKNEKAAQQLKALQQNELEKLAKQAAKDDKMYNRWLMAEMTPDDVYKKFKFKELAKKGIYPTTSVNYKHYKNYRTIYYARYPKLLEKLDA", "text": "FUNCTION: Effector that might be involved in host plant infection. SUBCELLULAR LOCATION: Secreted Host cell membrane. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MTTFNAKPDFSLFLQALSWEIDDQAGIEVRNDLLREVGRGMAGRLQPPLCNTIHQLQIELNALLGMINWGYVKLELLAEEQAMRIVHEDLPQVGSAGEPSGTWLAPVLEGLYGRWITSQPGAFGDYVVTRDVDAEDLNSVPTQTIILYMRTRSNSN", "text": "FUNCTION: May have a major role in the perfection of crystallization, involved either in the pore structure itself or in the organization of the pores within the linear array of terminal synthesizing complexes (TCs)."}
{"protein": "MKNILIFPFLSISTGHHHVADALQAELESQGLAAEKIDIFSHSYRRLEKLSSVAYLKWIQYFPKTYSGIYRLLACGEFQHDKRYFMYEWLFTQQMRHILQEKQPDIAFCTHALPSYLLNRLKPEYPNLTVVNVYTDFFVNQLWGRKNIDYHFVPSTEVKKQLISEGIDQNNIYLTGIPVHQNFEMESADTLQHHPPYTIIITGGSMGVGGILKWVQELSPGGKILYKILCGRNEKLYSYVKSLHHPLIEAIPYLHSKAEMNRLYEQATGIMTKPGGVTISECLQKRLPVFIYHALPGQEEMNLNLLHERKLVTDMRNWDMQKAEEYIAAFFQSNEQMKEYKKHVNGYLGEMSDRKIKDVLKRIIWKQKNTLLK", "text": "SIMILARITY: Belongs to the glycosyltransferase 28 family."}
{"protein": "MYHSAKRRSSSRLMMFIIALIIFIFGLGLNLSVGASDISIIDSLKYLFVWDGSKEQLIISTLRLPRTLIGVFVGASLAVAGALMQAMTRNPLASPQIFGVNAGASLFVVASLVILPASPYSSVIFAFAGAAAGGAIVYMIASSGGMTPVKLALSGMAVHLFLSSMTQAIIILNESGEDVLYWMTGAIDGSNWQDVITIAPFSVIGIGLALVFSGSVSVLGLGDETAKGLGQNMNGIRILISLIILILSGASVAVAGPIGFVGLLVPHIVRKLIGEHYQYVLPFSALFGAILLVYADVLARWIAFPYESPVGIVTAIIGTPFFLYLARKGRNLK", "text": "FUNCTION: Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Involved in the translocation of the substrate across the membrane (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily."}
{"protein": "MTTGDCCHLPGSLCDCTDSATFLKSLEESDLGRPQYVTQVTAKDGQLLSTVIKALGTQSDGPICRICHEGGNGERLLSPCDCTGTLGTVHKTCLEKWLSSSNTSYCELCHTEFAVERRPRPVTEWLKDPGPRHEKRTLFCDMVCFLFITPLAAISGWLCLRGAQDHLQFNSRLEAVGLIALTIALFTIYVLWTLVSFRYHCQLYSEWRRTNQKVLLLIPDSKTATTIHHSFLSSKLLKFASDETTV", "text": "FUNCTION: E3 ubiquitin-protein ligase which may be involved in endosomal trafficking. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein."}
{"protein": "MSVVVGGVEYSLNNWARYEIKRRAAELESVNYYPHCEYIMPEDIVVSILGSKPNCPFLEALKRFHDFLKKRRIIFKGEYLVIPWMGAQDVADMIHHVENRINLDHLEDLAHMLKLITYHKSFDTCINQAFEHLYAFKFPDANIETHELKHIRQLEKKMYGYILRLEKLQTVLTFYIEFLLKQV", "text": "SIMILARITY: Belongs to the asfivirus S183L family."}
{"protein": "MGKLQDGIAIKRINDAITTFKNYKLGELEQGGSMAINTLSNVRAHVGLAWPAILRNCLIHTSSHLGFMKFMIDIATTWKVGAFTLLGSVGDEDPFTDVDLIYTKTCLHLGLKDNDFLQFPEEFAYEANSFLEAQSMNARVDMLTGVHNIEDKYVFRIESISKFLKAYYTASEDVAYLTGFIKPDGSKESILSAELLKAQVTSEVLRVRNLITTKIQQYINLYEDSQLPHFRRAALSYTQDWDVDGGVPAALPQPDTTDDESPVTKPGASAPTVSKGADQPEDEEIIHKKVDASKDAPPKAVSSGNVSARGIPAFLEDDMSEMDAPDGFHDYLTREHENNFDLAQLGLAPSV", "text": "FUNCTION: Minor outer capsid protein. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Found in the peripheral regions of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the phytoreovirus minor outer capsid protein P9 family."}
{"protein": "MADAKAQKRQKFDNVFPKLREELLAYLNQEGMPQDAVSWFQRNLDYNVPGGKLNRGISVVDSVEILKGRKLNDDEYFKAALLGWCVEFLQAFFLVSDDMMDQSVTRRGQPCWFRVEGINLIAINDSFMLEGAIYYLLKKHFRSEPYYVHLLELFHDTTFQTEIGQLIDLITAPEDHVDLSKFSLAKHQKIVIYKTAYYSFYLPVALAMYTCGVPHAPANDPYALAQSILIPLGEYFQVQDDFLDFAAPPEVLGKVGTDIVDNKCSWCVNAALARASPAQRRVLDDNYGLKDKEAEARVKALYEELGIRDEFAAYEERAYARIVGLIETIPAEGADVGAGDVRLKREVFKAFLDKIYKRQK", "text": "FUNCTION: Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). The second module involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins (By similarity). This module also plays a key role in the biosynthesis of triterpenes such as ganoderic acids (GA), a group of highly oxygenated lanostane-type triterpenoids which are well recognized as a main group of unique bioactive compounds in the medicinal mushroom Ganoderma lucidum (PubMed:22203490, PubMed:31253150). Activity by the mevalonate kinase first converts mevalonate into 5-phosphomevalonate (By similarity). 5-phosphomevalonate is then further converted to 5- diphosphomevalonate by the phosphomevalonate kinase (By similarity). The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate (PubMed:22203490). The isopentenyl-diphosphate delta- isomerase then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity). Finally the farnesyl diphosphate synthase FPS catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:18540102, PubMed:31253150). SIMILARITY: Belongs to the FPP/GGPP synthase family."}
{"protein": "MNTPMFTRTSSLERTLETNKVLKNTYFLLSMTLVTSAIAAMATMAIGISPIVALVMQLAAIGILFFVMPKAINSSSGLVWTFVFTGLMGGALGPMLNFYAAMPNGPIVIAQALGLTGMVFLGLSAYTITSKKDFSFMRNFLFAGLIIVIVAALINIFVGSTVAHLAISSVSALVFSGFILFDTSRIVRGEETNYISATISMYLNILNLFTSLLSILGIMNNND", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family."}
{"protein": "MSQLGSAVPSSNLPEGLPVSSLALLILVLIPCVLLLLLLNCLFVGYKLFRMTRRKRDRYGSEMSLMHSSYSTRQRITRFSDEPPVAPNRKTNYVSVSEPMLAPPITSSLTSSAERRATGQRAMFLRPDGATYAGSESLRVPHWRTSAPVLVQSSDSDMERVNTVPPNSPVLRVTPNGFSVPMTSLRRSSTMELESTSLDKIHVECESASIIPQENSCYVVSSSSSARGSGLDSDFGASAGVSLRILSMDSDGFPGSAWASALEWDYYDPSYVTQNHVPKHRPQAPPITTKQYWV", "text": "FUNCTION: Key maternal determinant of the dorsal organizer and body axis formation in vertebrates that acts by promoting stabilization of beta-catenin (ctnnb1) (PubMed:30467143). Localizes on the plasma membrane of the future dorsal blastomeres in early blastulas and binds to and promotes the tankyrase-mediated degradation of axin (axin1 and axin2) (PubMed:30467143). Axin degradation results in stabilization and nuclear translocation of beta-catenin (ctnnb1) for activating organizer-specific target gene expression (PubMed:30467143). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Enriched on the plasma membrane of blastomeres only in a small region in which the dorsal organizer will form. SIMILARITY: Belongs to the huluwa family."}
{"protein": "MVLSDLDIKEPDSPESGLNGSDDMVREHETESKGNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLEKEGEWKGKVSFLDREIEISDASQVEKEISEAQIAIAGEGMGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPHDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQDVDPQGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQHRLSLDKALQRERIFFEDHTHFRDLLEEGRATIPCLAERLTNELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFSLIEKIDTFNKEIISTIEGEEHVGQYDSRLFTKVRAEFCKWSAVVEKNFEKGHEAIRKEIKQFENRYRGRELPGFVNYKTFEIIIKKQVIVLEEPAVDMLHTVTDIIRNTFTEVSGKHFSEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKKKKSNHYYQSEDSEPSTAEIFQHLMAYHQEVSTRISSHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLERLSRARQRLAKFPG", "text": "FUNCTION: Interferon-induced dynamin-like GTPase with antiviral activity. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, perinuclear region Note=Binds preferentially to negatively charged phospholipids. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG", "text": "FUNCTION: Plays a role in the mitochondrial apoptotic process (PubMed:10772918, PubMed:16113678, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816, PubMed:11060313, PubMed:16199525). Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM) (PubMed:21458670). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis (PubMed:11060313, PubMed:16199525, PubMed:10772918, PubMed:16113678, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). Promotes activation of CASP3, and thereby apoptosis (PubMed:11060313, PubMed:16199525, PubMed:10772918, PubMed:16113678, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform Delta]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform Alpha]: Mitochondrion outer membrane; Single-pass membrane protein Cytoplasm Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane. Upon Sendai virus infection, recruited to the mitochondrion through interaction with IRF3 (PubMed:25609812). SIMILARITY: Belongs to the Bcl-2 family."}
{"protein": "MTVVSGASKASGADLLDYDVVVARFDPVFGLEVHVELSTVTKMFCGCATTFGAEPNTQVCPVCLGLPGSLPVLNRAAVQSAIRIGLALNCEIVPWCRFARKNYFYPDVPKNYQISQYDEPIAINGYLEVPLEDDTTWRVEIERAHMEEDTGKLTHLGSETGRIYGATTSLIDYNRAGVPLIEIVTKPIEGAGVRAPQIARAYVKALQDLLRTLDVSDVRMDQGSMRCDANVSLKPIGTVEFGTRSEIKNVNSLKSVEMAVRYEMQRQGAILVSGGRIAQETRHFHEDGYTSPGRAKETAQDYRYFPDPDLEPVAPSRELVEQLRQTIPELPWLSRKRIQQEWGISDEVMRDLVNAGAVELVAATVKNGASSEQARAWWGNFLVQKANEANITLDELAITPAQVAVVVALVDEGKLSIRLARQVVEGVLAGEGEPEQVMVDRDLALVRDDSVMQAAVDEALAADPDVAEKIRGGKVAAAGAIVGAVMKTTRGQADAARVRELVLAICGQG", "text": "FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity). FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln). SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily. SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily."}
{"protein": "MPPTQAESVIKNIIREIGQECAAHGEIVPETLVAFMVKAVVLDPSNGFNTDRTLTKSDVQKLVKLCVNRLLDSKNPSLDTIKMQVYFDMNYTSREEFLEEHHQVIESRLSSVSREITDSRACVREELESLYRKIVSYVLLRSGLGSPTDIKIVREATAALQSVFPQTELGTFLTLSKKDKERQLKELTMIVTGIRLFNRDCGKGGEGIDDLPAILQEAIPATTQHVDSQLEVVQEQAYRYTAILEKVAKNPLMSQELQPYMLREALYNVRQCEIFLQVILSDIITCAQEVEMMIKQLEAQLEQLKLTVKSKTAVPTSQVFPIFIALSNLWTSFQDETVLISILSNLTTHLEPFLGAHDLFFPEKVMQVLLDGVTVKTDVCRIKEHIEDKVNVADFKKLEWLFPETTANFDKLLIQYRGFCAYTFATTDGLLLPGNPSIGILKYKDKYYTFNTRDAAYSFAENPENYIDIIREKAKRNAELIQLLELHQQFESLIQYSQMKEVDKRYIKPITKCETGTQTDTHLLPPTIVRSYEWNEWELRRKAIKLANLRRKVTHSVQTDHSHMRRENCSQVYPSKDVGTQSMREGSSRVPRPQIYIAGLRGGQTKTTYGVKVNLTRAVDET", "text": "FUNCTION: Essential for sperm motility and is involved in the regulation of the beating frequency of motile cilia on the epithelial cells of the respiratory tract (By similarity). Required for the establishment of radial spokes in sperm flagella (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body. SIMILARITY: Belongs to the CFAP206 family."}
{"protein": "MSGRMKEVVSWSPEEVTNWLMENAVPEYCEPLKSFTGQDLINLTEEDFKKTPLSRVSSDSGQQLLHMIETLKMAHHIEAHKNGHVNGHIHVSVNNTAHENGFSSKTKLNGVPNGYKKEMIKIPMPEPERLQYPMEWGKTFLAFIYALFCFIFTTVTISVVHERVPPKEVQPPLPDAFFDRFDRVQWAFSICEINGMILVGLWLVQWLLLKYKSIISRRFFCIVCTLYLYRCITMYVTTLPVPGMHFKCSPKLFGDWESHLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVILTLTYLFIKEYSPRRLWWYHWLCWTLSMVGMFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQVLKEASQTNLLARVWWYKPFQYFEKNVQGIVPRSYHWPFPWPVLHRGRQVKYSRLVNDT", "text": "FUNCTION: Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Golgi apparatus SMS1 directly and specifically recognizes the choline head group on the substrate, requiring two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Major form in macrophages. Required for cell growth in certain cell types. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the sphingomyelin synthase family."}
{"protein": "MHTVLYSNMKNMFQLLSFLCVSLLVAGDVHHHAACSTVCSLKGILDSVSDLTDLAKERLATLQNPICSKDKAFYMETYTNVTQNKAEKNGLPINCATVYQQGNRTSGIYMIWPLFLNHPISVFCDMETAGGGWTVIQRRGDFGQPIQNFYQTWESYKNGFGNLTKEFWLGNDIIFVLTNQDSVVLRVDLEDFEGGRRYAEAVEFLVRSEIELYKMSFKTYKGDAGDSLSQHNNMPFTTKDRDNDKWEKNCAEAYKGGWWYNACHHSNLNGMYLRGPHEESAVGVNWYQWRGHNYSLKVSEMKIRPIIFVPGEGLPK", "text": "FUNCTION: Lectin involved in innate immunity. Agglutinates all types of human erythrocytes, Gram-positive and Gram-negative bacteria. Has a stronger agglutinating activity towards Gram-negative bacteria than towards Gram-positive bacteria. Specifically recognizes acetyl group- containing substances on agglutinated cells. The hemagglutinating activity was inhibited by EDTA, acetyl group-containing mono- and disaccharides, N-acetyl derivatives of amino acids, other acetyl group- containing substances, propionamide and benzamide. Enhances the antimicrobial activity of big defensin against Gram-positive bacteria but not against Gram-negative bacteria. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MDQKQIEEIVRSVMASMGQAAPAPSEAKCATTTCTTPVTSESCALDLGSAEAKAWIGVENPHRADVLTELRRSTVARVCTGRAGPRPRTQALLRFLADHSRSKDTVLKEVPEEWVKAQGLLEVRSEISDKNLYLTRPDMGRRLCAEAVEALKAQCVANPDVQVVISDGLSTDAITVNYEEILPPLMAGLKQAGLKVGTPFFVRYGRVKIEDQIGEILGAKVVILLVGERPGLGQSESLSCYAVYSPRIATTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR", "text": "FUNCTION: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12. SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the EutC family."}
{"protein": "MFIKKIKAKANNNEINVIIEIPMNSGPIKYEFDKESGALFVDRFMQTTMSYPCNYGFIPDTLSNDGDPVDVLVVAHHPVVPGSVIKCRAIGVLMMEDESGLDEKIIAVPTSKLDITFDHIKELDDLCEMLKKRIVHFFEHYKDLEKGKWVKVTGWGDKVKAETLIKEGIDRN", "text": "FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase family."}
{"protein": "MRDPVSSQYSSFLFWRMPIPELDLSELEGLGLSDTPTYESKDSSSVGKMNGQASGTEQKNPEGDPLLEYSTFNFWRAPIASIHSVDLDLL", "text": "FUNCTION: Cofactor for the transcription factor TCF7. Involved in regulation of lymphoid development by driving multipotent hematopoietic progenitor cells towards a T-cell fate. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Continuous nuclear export is followed by degradation. SIMILARITY: Belongs to the MLLT11 family."}
{"protein": "MVPRVWSLMRFLIKGSVAGGAIYLVYDQDPLGPSDKSQAALQKAEEVVPPAVYQFSQYVCEQTGLKIPQLPAPPKFNFHIRDYWNSGVIKVMSALSVAPSKAREYSKEGWEYLKERTK", "text": "FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Constituent of mature MICOS complex, it is required for the formation of cristae junction (CJ) and maintenance of cristae morphology. Required for the incorporation of MICOS10/MIC10 into the MICOS complex. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein Note=Enriched at crista junctions. SIMILARITY: Belongs to the MICOS complex subunit Mic13 family."}
{"protein": "WCSTCLDLECGASRECYDPCFKAFGRAHGKCMNNKCRCYT", "text": "FUNCTION: Inhibits high conductance calcium-activated potassium channels (KCNMA) (By similarity). Inhibits Shaker B potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 12 subfamily."}
{"protein": "MAQVVMSALPAEDEESSESRMVVTFLMSALESMCKELAKSKAEVACIAVYETDVFVVGTERGRAFVNTRKDFQKDFVKYCVEEEEKAAEMHKMKSTTQANRMSVDAVEIETLRKTVEDYFCFCYGKALGKSTVVPVPYEKMLRDQSAVVVQGLPEGVAFKHPEHYDLATLKWILENKAGISFIIKRPFLEPKKHLGGRVLAAEAERSMLSPSGSCGPIKVKTEPTEDSGISLEMAAVTVKEESEDPDYYQYNIQGPSETDGVDEKLPLSKALQGSHHSSEGNEGTEVEVPAEDSTQHVPSETSEDPEVEVTIEDDDYSPPTKRLKSTEPPPPPPVPEPANAGKRKVREFNFEKWNARITDLRKQVEELFERKYAQAIKAKGPVTIPYPLFQSHVEDLYVEGLPEGIPFRRPSTYGIPRLERILLAKERIRFVIKKHELLNSTREDLQLDKPASGVKEEWYARITKLRKMVDQLFCKKFAEALGSTEAKAVPYQKFEAHPNDLYVEGLPENIPFRSPSWYGIPRLEKIIQVGNRIKFVIKRPELLTHSTTEVTQPRTNTPVKEDWNVRITKLRKQVEEIFNLKFAQALGLTEAVKVPYPVFESNPEFLYVEGLPEGIPFRSPTWFGIPRLERIVRGSNKIKFVVKKPELVVSYLPPGMASKINTKALQSPKRPRSPGSNSKVPEIEVTVEGPNNSSPQTSAVRTPTQTNGSNVPFKPRGREFSFEAWNAKITDLKQKVENLFNEKCGEALGLKQAVKVPFALFESFPEDFYVEGLPEGVPFRRPSTFGIPRLEKILRNKAKIKFIIKKPEMFETAIKESTSSKSPPRKINSSPNVNTTASGVEDLNIIQVTIPDDDNERLSKVEKARQLREQVNDLFSRKFGEAIGMGFPVKVPYRKITINPGCVVVDGMPPGVSFKAPSYLEISSMRRILDSAEFIKFTVIRPFPGLVINNQLVDQNESEGPVIQESAEASQLEVPVTEEIKETDGSSQIKQEPDPTW", "text": "FUNCTION: Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box (By similarity). Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Colocalizes with BTK in the cytoplasm. SIMILARITY: Belongs to the TFII-I family."}
{"protein": "MADGWDAEKIFNTTVFGFTYDDLILMPGHIDFGVNDVDLSTRITRNLHVRTPIVSSPMDTVTEHRMAIGCALMGGMGVIHNNMETARQVAEVQKVKRYENGFILDPFVLRPSDSVADVYRIKEKYGYSSVPITDTGMLGGKLLGIVTSRDIDFLTDVHTPLSEVMTSDLVVGHEPVQLAEANELLRESKKGKLPIVNDNFELVALISRNDLKKNREFPLASKDSNKQLLVGAAVSTKPHDIERAKALQEAGADVLVVDSSQGDSIYQVDLVKRLKAAFPELQIIGGNVVTARQAKSLIDAGVDGLRIGMGSGSICTTQVVCAVGRAQATAVYHVCKYAREHGDVPCIADGGIQNSGHVMKALALGANAVMMGSMLAGTEEAPGEYYFHNGVRVKTYRGMGSLDAMRAGTRRTASPPARGLRSPEASPSTAASSGGASRASALSEASPSAKSEASRTSTSTGSAARYFAENQTIRVAQGVSGCVVDKGTVMQLIPYVIQGVKHGMQDIGARTLRDLHAQLVGGELRFDVRSGAAQREGDVHDLHSFERKLYA", "text": "FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IMPDH/GMPR family."}
{"protein": "MAEAAALVWIRGPGFGCKAVRCASGRCTVRDFIHRHCQDQNVPVENFFVKCNGALINTSDTVQHGAVYSLEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQKRLERLQRKLVEPKHCFTSPDYQQQCHEMAERLEDSVLKGMQAASSKMVSAEISENRKRQWPTKSQTDRGASAGKRRCFWLGMEGLETAEGSNSESSDDDSEEAPSTSGMGFHAPKIGSNGVEMAAKFPSGSQRARVVNTDHGSPEQLQIPVTDSGRHILEDSCAELGESKEHMESRMVTETEETQEKKAESKEPIEEEPTGAGLNKDKETEERTDGERVAEVAPEERENVAVAKLQESQPGNAVIDKETIDLLAFTSVAELELLGLEKLKCELMALGLKCGGTLQERAARLFSVRGLAKEQIDPALFAKPLKGKKK", "text": "FUNCTION: Inhibits translesion DNA synthesis by preventing monoubiquitination of PCNA, this is necessary to counteract damage due to ultraviolet light-induced replication stress (PubMed:27906959). SDE2 is cleaved following PCNA binding, and its complete degradation is necessary to allow S-phase progression following DNA damage (PubMed:27906959). FUNCTION: Plays a role in ribosome biogenesis by enabling SNORD3- and SNORD118-dependent cleavage of the 47S rRNA precursor (PubMed:34365507). Binds ncRNA (non-coding RNA) including the snoRNAs SNORD3 and SNORD118 (PubMed:34365507). FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of relatively short introns featuring weak 3'-splice sites (ss) and high GC content (PubMed:34365507). May recruit CACTIN to the spliceosome (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the SDE2 family."}
{"protein": "MFALSKVLRRSQSLRLGACNAVYSKLDIPLGERNIAIESNALIHDKHEALPRFYELSWSSSTGRRSLSSDAGAKTTGDDDDLEDKNVDLATPDETSSDSEDGEEFSGDEGDIEGAELELHVPESKRPSEMFKAIVSVSGLSVGSALDKWVEQGKDTNRKEFESAMLQLRKRRMFGRALQMTEWLDENKQFEMEERDYACRLDLISKVRGWYKGEAYIKTIPESFRGELVYRTLLANHVATSNVRTAEAVFNKMKDLGFPLSTFTCNQMLILYKRVDKKKIADVLLLLEKENLKPNLNTYKILIDTKGSSNDITGMEQIVETMKSEGVELDLRARALIARHYASAGLKEKAEKVLKEMEGESLEENRHMCKDLLSVYGYLQREDEVRRVWKICEENPRYNEVLAAILAFGKIDKVKDAEAVFEKVLKMSHRVSSNVYSVLLRVYVDHKMVSEGKDLVKQMSDSGCNIGALTWDAVIKLYVEAGEVEKAESSLSKAIQSKQIKPLMSSFMYLMHEYVRRGDVHNTEKIFQRMKQAGYQSRFWAYQTLIQAYVNAKAPAYGMKERMKADNIFPNKRLAAQLAKADPFKKTPLSDLLD", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PPR family. P subfamily."}
{"protein": "MRKGYMTVRSNKCIADHIYQMVLEGEIAEVCGAPGQFLHIKVSDSLTPLLRRPISIADINKAARQVTIIFRKDGEGTRLLSLKQEGDQLDVLGPLGNGFPAESLEQGKTALLVGGGIGVPPLYELSKQLTNRGVHAIHVLGFASAKDVFYEQEFSRFGRVYVATADGTRGSKGFVTDVIENEGLQFDCIMACGPTPMLKALKQRYPDKEVYLSMEERMGCGIGACFACVCHTEESETSYVKVCLDGPVFKAQEVLL", "text": "FUNCTION: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+). SIMILARITY: Belongs to the PyrK family."}
{"protein": "MTRYCRGLSQRQAFLLLTVLALLFILLFVVKDPRAKDSRCQFIWKNDASAQENQQKAEPQVPIMTLSPRVHNKETTSVSSKDLKKQEREAVQGEQAEGKEKRKLETIRPAPENPQSKAEPAAKTPVSEHLDKLPRAPGALSTRKTPMATGAVPAKKKVVQATKSPASSPHPTTRRRQRLKASEFKSEPRWDFEEEYSLDMSSLQTNCSASVKIKASKSPWLQNIFLPNITLFLDSGRFTQSEWNRLEHFAPPFGFMELNQSLVQKVVTRFPPVRQQQLLLASLPTGYSKCITCAVVGNGGILNDSRVGREIDSHDYVFRLSGAVIKGYEQDVGTRTSFYGFTAFSLTQSILILGRRGFQHVPLGKDVRYLHFLEGTRDYEWLEAMFLNQTLAKTHLSWFRHRPQEAFRNALDLDRYLLLHPDFLRYMKNRFLRSKTLDTAHWRIYRPTTGALLLLTALHLCDKVSAYGFITEGHQRFSDHYYDTSWKRLIFYINHDFRLERMVWKRLHDEGIIWLYQRPQSDKAKN", "text": "FUNCTION: Protein sialyltransferase specifically expressed in goblet cells that plays a key role in intestinal host-commensal homeostasis (PubMed:35303419). Conjugates sialic acid with an alpha-2-6 linkage to N-acetylgalactosamine (GalNAc) glycan chains linked to serine or threonine in glycoproteins (PubMed:10788794). Catalyzes the formation of the sialyl-Tn (S-Tn) antigen, an antigen found in intestinal goblet cells (PubMed:35303419). Protein sialylation in globlet cells is essential for mucus integrity and is required to protect the intestinal mucus against excessive bacterial proteolytic degradation (PubMed:35303419). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
{"protein": "MRRIDPSKLELEERLVTVNRVAKVVKGGRRFRFAALVVVGDKNGHVGFGTGKAQEVPEAIRKAVEDAKKNLIEVPMVGTTIPHEIIGRFGAGNILLKPASEGTGVIAGGPVRAVLELAGVADILSKSLGSNTPINMIRATLQGLSELKRAEDVAKLRGKSVEELLG", "text": "FUNCTION: With S4 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
{"protein": "MPKNLRFSVFLLFLLCINSVFGEFGPEDAQYNETEARMLLSLSAAAYSLDVTPCIGRTFSPAENQTLLSTFSVRCDFVGNPCAGYIVVSDVLQQITVVFRGTKTSSQLLLEGWTTLKPSSDFYGMGLVNTYFRSGHEKTWQYVQDALSISQYRNYDVYVTGHSLGGALAGLCAPRIVHDGLRQSQKIKVVTFGEPRVGNIEFSRAYDQLVPYSFRVVHSGDVVPHLPGCVKDLSYTPPAGSDGSMPCDPVSTNGGYHHAIEIWYPGNMTQGDPFMVCTGLPRDEDFGCSDSLKVNLGDTNQGVWDHRNYFGVEVPDFGKGGCDPSMTFKGPPTKTGVLSLVGSVFGRKRRSIR", "text": "FUNCTION: Probable lipase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MGCDGGTIPKRHELVKGPKKVEKVDKDAELVAQWNYCTLSQEILRRPIVACELGRLYNKDAVIEFLLDKSSEKALGKAASHIKSIKNVTELRLSDNPAWEGDKGSTKGDKHDDLQRARFICPVVGLEMNGRHRFCYLRCCGCVFSERALKEIKAEVCHTCGAAFQEDDVIVLNGTKEDVAMLQTRMEERRLRAKLGKKTKKPKAAESVSKSDISEEAPGPSKMKAGKPEETSLDSREKKTSSAPRSAAAHGSSSGKAGKPVCGAPKRSIADSGESEAYKSLFTTHSSAKRSKEESAHWVTHTSYCF", "text": "FUNCTION: Replication termination factor which is a component of the elongating replisome. Required for ATR pathway signaling upon DNA damage and has a positive activity during DNA replication. Might function to facilitate fork pausing at replication fork barriers like the rDNA. May be globally required to stimulate ATR signaling after the fork stalls or encounters a lesion. Interacts with nascent DNA. SUBCELLULAR LOCATION: Chromosome Note=Localizes at the replication fork. SIMILARITY: Belongs to the rtf2 family."}
{"protein": "MLFMVKFRWETEFKETDIGKIPKDWDVKKIKDIGEVAGGSTPSTKIKEYWGGDIPWITPKDLANYEYIYISRGERNITEKAVKECSLRIFPKGTILLTSRAPIGYVAIAKNPLTTNQGFRNIIPKDGVVSEYLYYLFKTKTMSEYLKDISGGSTFPELKGSTLKEVEIPYPSPEEQQKIATVLSYFDDLIENKKKQNEILEKIALELFKNWFIDFEPFKNEEFVYNDELDKEIPKGWEVKRLGDILKVESGSNAPQREIYFENAKIPFVRVKHLVKGVCIESSDFINELALKDYKMKLYNEKSIIFQKSGESLKEARVNIVPFKFTAVNHLAVIDSSMLNEKHYFIYCLLRFLLKEIVYSVKGTTLPYLKISDIENKYIIIPPQPILQKFHSLVQPLFEKIINNQKQIMVLKKIRDALLPKLVFGELRVEEL", "text": "FUNCTION: The specificity (S) subunit of a type I restriction enzyme; this subunit dictates DNA sequence specificity. The M and S subunits together form a methyltransferase (MTase) that methylates A-3 on the top and A-2 on the bottom strand of the sequence 5'-CCAN(5)GTR-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. After locating a non- methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage. SIMILARITY: Belongs to the type-I restriction system S methylase family."}
{"protein": "MEEFAEGNDDEQMIFSDIEDLTAHGIGMTDIIKLKQAGVCTVQGVHMSTKRFLLKIKGFSEAKVDKLKEAASKMCPANFSTAMEISQNRKKVWSISTGSEALNGILGGGIQSMSITEVFGEFRCGKTQMSHTLCVTAQLPRDMGGAEGKVAFIDTEGTFRPDRIKAIAERFGVDADQAMENIIVSRAYNSEQQMEYITKLGTIFAEDGQYRLLIVDSIMALFRVDYSGRGELSERQQKLNIMLARLNHISEEFNVAVFVTNQVQADPGAAMMFASNDRKPVGGHVMAHASATRLLLRKGRGEERVAKLNDSPDMPEAECSYVITPGGIADVS", "text": "FUNCTION: Required for meiotic recombination and cell cycle progression. Binds to single and double-stranded DNA, in the presence of magnesium, and exhibits DNA-dependent ATPase activity. Promotes DNA strand annealing and strand exchange via DNA recombinase activity and forms helical and stacked ring nucleoprotein filaments. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RecA family. DMC1 subfamily."}
{"protein": "MDAVELARRLQEEATCSICLDYFTDPVMTACGHNFCRECIQMSWEKGKGKKGKKKQKGSFPCPECREMSPQRNLRPNRLLTKVAEMARQHPGLHKRDLCQIHQEPLKLFCQDDQTPICVVCREAQEHRMHRVLPLDEAAREYKLRLEEDIKYLREEMMKTETLQAKEEQTLTEWQERVKERRERILEEFQKVVLFLVEEERRLLQILKKEEDDTLGKLQDSKASLDHQSRSLDLILLQLEEQTQQEPLQMLQDVKDTLTRKESLSMQYPEVVLPVAIKTVCRVPGQIEVLKSFQEDVVPDPSTAYPYLLLYESRQRRYLSPPPEGSAPYSKDRFLAYPCAVGQKSFSSGRHYWEVGMNLTGDALWALGVCRDNVSRKDRVLKSPENGFWVVQLSKGKKHLPLLPNSIPVTLTEPPSHMGIFLDFQAGEVSFYSVNDGSHLHSFSQVAFPGPLLPFFCLGSPKSGQMVISTVTMWVKG", "text": "FUNCTION: E3 ubiquitin ligase that plays important roles in the regulation of neuronal apoptosis, selective autophagy or cell proliferation. Stimulates the degradation of kinetochore ZW10 interacting protein ZWINT in a proteasome-dependent manner, leading to negative regulation of cell proliferation. Inhibits autophagic degradation of diverse known targets while contributing to autophagy of midbodies. Autophagy-inhibitory activity involves MCL1, which TRIM17 assembles into complexes with the key autophagy regulator BECN1 (By similarity). Controls neuronal apoptosis by mediating ubiquitination and degradation of MCL1 to initiate neuronal death. In addition, regulates NFAT transcription factors NFATC3 and NFATC4 activities by preventing their nuclear localization, thus inhibiting their transcriptional activities. Decreases TRIM41-mediated degradation of ZSCAN2 thereby stimulating alpha-synuclein/SNCA transcription in neuronal cells (By similarity). Prevents the E3 ubiquitin-ligase activity of TRIM28 and its interaction with anti-apoptotic BCL2A1, blocking TRIM28 from ubiquitinating BCL2A1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Lysosome. SIMILARITY: Belongs to the TRIM/RBCC family."}
{"protein": "MEGGRAPACTTQVSFVCQRCSQPLKLDTSFKILDRLTIQELTAPPLTAAPARPGDAQEESALSEEAFTEGRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNITENECQNYKRCLEILEKMNEDDKEKLQTELKELALEEEQLIQELEDVEKNRKIVAEDFERVRAEAERLEQEEAQYQKEYCEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK", "text": "FUNCTION: Plays a central role in autophagy (By similarity). Acts as core subunit of different PI3K complex forms that mediate formation of phosphatidylinositol 3-phosphate and are believed to play a role in multiple membrane trafficking pathways such as initiation of autophagosomes, maturation of autophagosomes and endocytosis (By similarity). Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Endoplasmic reticulum membrane; Peripheral membrane protein Mitochondrion membrane; Peripheral membrane protein Cytoplasmic vesicle, autophagosome. SIMILARITY: Belongs to the beclin family."}
{"protein": "MTRPKAYFDISIGGTPKGRIVFELYKDVVPKTAENFLKLCEGKSGMAKSKPDVPLSYKGSIFHRVIKDFMIQFGDFTNFDGTGGESIYGEKFEDENFEIKHDKPFLLSMANAGPNTNGSQAFITCVPTPHLDGKHVVFGEVIEGKRLVRLIEKQQTEDGTDKPMHDVKVEGCGLLPDDYEVPADAEQTPTDEFGDNYEESLKDDAKVDLKKVETVIKAIETVKDIGTKQFKEQNYEVALAKYKKCDKFLKEYFPDDLNEEDMKKINDFKVTVPLNIAIAALKSKDYRSVMVACSEVLYAEAADAKAKAKALYRRGLAYYHVNDTDMALADLEMATTFQPNDAAIAKAINDTIKKRKQETEKQKKSLSKMFG", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D subfamily."}
{"protein": "MPEQDKDPRVQENPDDQRTVPEVTGDARSAFWPLRDNGGPSPFVPRPGPLQTDLHAQSSEIRYNHTSQTSWTSSSTKRNAISSSYSSTGGLPGLKQRRGPASSRCQLTLSYSKTVSEDRPQAVSSGHTRCEKGADTAPGQTIAPTGGSPRSQDSRPRRRKIPLLPRRRGEPLMLPPPLELGYRVTAEDLHLEKETAFQRINSALHVEDKAIPDCRPSRPSHTLSSLATGASGGPPVSKAPTMDAQQDRPKSQDSLGLLAPLASAAEVPSTAPVSGKKHRPPGPLFSSSDPLPATSYHSRDTAQVTSLIPATFTAASRDAGMRRTRSAPAAATAAPPPSTLNNTSGSLLNAVDGGPSHFLASATAAARAQRSEVRYNQRSQTSRTRSCLKRNASSSSSSHSSTEGLQELKRRRGPASSHCQLAHSSSNTVSEDGPQAVSSGHRCENKAGTAPGQTLAPRGGSPRSQASRPHINSALYVEDKAISDCRPSRPSHTLSSLATGASGGPPVSKAPTMDAQQDRPKSQDCLGLVAPLASAAEVPSTAPVSGKKHRPPGPLFSSSDPLPATSSHSRDSAQVTSLIPATFTAASRDAGMRRTRPGTSAPAAAAAALPPSTLNPTSGSLLNAVDGGPSHFLASATAAARAQRSEVRYNQRSQTSRTRSCLKRNASSSSHSSTEGLQELKRRRGPASSHCQLAHSSSNTVSEDGPQAVSSGHRCENKAGTAPGQTLAPRGGYPRSQASRPRINSALHVEDKAISDCRPSRPSHTLSSLATGASGGPPVSKAPTMDAQQDRPKSQDCLGLLAPLASAAEVSSTAPVSGKKHRPPGPLFSSSDPLPATSSHSGDSAQDTSLIPAPFTPASRDAGIRRMFRVRNCLRGLGLFLLVFSFFFLLTWASFSF", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the POM121 family."}
{"protein": "MVNLGSIWQNLLASQAPLQSMTGNATTMAGLATYSLPQLPYAYNALEPYISAQIMELHHSKHHQTYVTNLNNALKVHVAAIASSDIPAQIAQQPAIKFNGGGHINHSLFWKNLAPAETPETNYSKAAPSLAAEIEKTWGSFDEFKKAFSAALLGIQGSGWGWLVKESTAEKGRLRIITTKDQDPVVGGEVPVFGVDMWEHAYYLQYLNGKAAYVENIWKVINWKTAEERFQGSREDAFADLKALL", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MSSGLRAADFPRWKRHIAEELRRRDRLQRQAFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPSGLHVVSVDKGSRAVLWAQP", "text": "FUNCTION: Plays an essential role in both canonical and non-canonical autophagy: interacts with ATG12-ATG5 to mediate the lipidation to ATG8 family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP) (PubMed:12665549, PubMed:18849966, PubMed:19898471, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:33586810). Acts as a molecular hub, coordinating autophagy pathways via distinct domains that support either canonical or non-canonical signaling (PubMed:33586810). During canonical autophagy, interacts with ATG12- ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to ATG8 proteins, to produce a membrane-bound activated form of ATG8 (By similarity). Thereby, controls the elongation of the nascent autophagosomal membrane (By similarity). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, probably by catalyzing conjugation of phosphatidylserine (PS) to ATG8 (By similarity). Non- canonical autophagy plays a key role in epithelial cells to limit lethal infection by influenza A (IAV) virus (PubMed:33586810). Regulates mitochondrial antiviral signaling (MAVS)-dependent type I interferon (IFN-I) production (By similarity). Negatively regulates NOD1- and NOD2-driven inflammatory cytokine response (PubMed:24238340). Instead, promotes an autophagy-dependent antibacterial pathway together with NOD1 or NOD2 (PubMed:19898471, PubMed:19966812, PubMed:24238340). Plays a role in regulating morphology and function of Paneth cell (By similarity). SUBCELLULAR LOCATION: Cytoplasm Preautophagosomal structure membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Lysosome membrane; Peripheral membrane protein Note=Recruited to omegasomes membranes by WIPI2 (PubMed:24954904). Omegasomes are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localized to preautophagosomal structure (PAS) where it is involved in the membrane targeting of ATG5 (PubMed:24954904). Localizes also to discrete punctae along the ciliary axoneme (PubMed:24954904). Upon activation of non-canonical autophagy, recruited to single- membrane endolysosomal compartments (By similarity). SIMILARITY: Belongs to the WD repeat ATG16 family."}
{"protein": "MQKLFIVLLLFCILRLDAEVDGRRATFCKQPGCQEACKKENKNGRCVDKFDNNFSYNICRCY", "text": "FUNCTION: May block potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 23 subfamily."}
{"protein": "MINLFLLKYKTAFSTFLKPFAYLSLILSVCFYSIQAQAFPVFAQQAYENPREATGRIVCANCHLAQKPVEIEVPQAVLPDTVFEAVVEVPYDLSLQQVTGNGTKGPLNVGAVVILPEGFTLAPKDRISSELKEKTKGLIITPYNEANPNILVVGPVPGKDHQKLVFPVLSPNPAENKNVHFIKYPVYVGANRGRGQVNPTGEKSNNTVYTSPIDGQIVKLEKSDNVTSFSIKSKTGDIITVKVPFGPDILVKEGQTLVADQQLTNDPNVGGFGQVETEIVLQSPARVKGLIAFFFTVILAQILLVLKKKQFEKVQLAEMNF", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome f family."}
{"protein": "MEGSAKASVASDPESPPGGNEPAAASGQRLPENTPPCQQVDQPKMQKEFGEDLVEQNSSYVQDSPSKKRKLDVEIILEEKHSEDDGGSAKRSKLERGDVSEDEPSLGRLNQTKRKLQPQDDEVPQKLQKLEEGHSSAVAAHYNELQEVGLAKRSQSRIFYLRNFNNWIKSILIGEILEKVRQRKTRDITVLDLGCGKGGDLLKWRKGRISRLVCADIADISMKQCQQRYEDMRCRRDNEHIFSAEFITADCSKELLVEKFRDPEMYFDVCSCQFACHYSFESQVQADTMLRNACGRLNPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGNYPLFGCKYDFNLEGVVDVPEFLVYFPLLTEMAKKYNMKLIYKKTFLEFYEEKIKNNENKMLLKRMQALEQYPAHENSKLASEKVGDYTHAAEYLKKSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ", "text": "FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'- terminal GpppC. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family."}
{"protein": "MLEQQRNPADALTVSVLNSQSQVTNKPLRDSVKQALRNYLSQLDGQDVNELYELVLAEVEHPMLDMVMQYTRGNQTRAATMLGINRGTLRKKLKKYGMG", "text": "FUNCTION: Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters. SIMILARITY: Belongs to the transcriptional regulatory Fis family."}
{"protein": "MAFIAALGLLMAGICPAVLCDGTLGRDTLSHEDHGKGRQLHSLTLASSNTDFALSLYKKLALRNPDKNVVFSPLSISAALTILSLGAKDSTMEEILEGLKFNLTEITEEEIHQGFGHLLQRLSQPEDQVEINTGSALFIDKEQPILSEFQEKTRALYQAEAFIADFKQPNEAKKLINDYVSNQTQGKIAELFSDLEERTSMVLVNYLLFKGKWKVPFNPNDTFESEFYLDEKRSVKVPMMKIKEVTTPYVRDEELSCSVLELKYTGNASALFILPDQGKMQQVESSLQPETLKKWKDSLIPRIINDLRMPKFSISTDYSLKEVLPELGIKKVFSQQADLSRITGTKDLYVSQVVHKAVLDVDETGTEATAATGVATVIRRQPRTLNFNRPFMVVITDMDSQSILFVAKITNPK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
{"protein": "MMKREVINKTRGTSLGAVRFARTFMSRFRGLMLRRDVETGLVLEIPVGRGRYGSGIHMFFMLVPLDVLFVDGDMRVVDSVTLRPWQIYNPRKPARYVIELREGKIRDSGTRVGDTIEFRDLQS", "text": "SIMILARITY: Belongs to the UPF0127 family."}
{"protein": "MRVTNRSLKGREGEIAVTAETLDDLWHLKYIIEKGDLVFSVTKRKADSASDKIRPEKVEKVKVRLGIRVDDLEFHKFANRLRLHGMIERGMDVGSYHTLNIEIGTNLSVIKEHWKNDQLQRIKDAEEASKRPKVVMVAIEEGDADIGFVHHYGIEIYSHIRQSSGKRETGLRNEFFREVVEQLRHAVPEEASIVIAGPGFTKEDFIKYFQETEPAMASKALIEDTSMIGMSGFQEVLRRGAVDRIMQESRIARESALMEDLIREISMDGKAAYGLGDVKNALNFGAVETLLVADETLREGREKGEDIDKLLREVEQAQGKVVVFSTAFEPGEKLHKLGGIAALLRFKVRG", "text": "FUNCTION: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota subfamily."}
{"protein": "MGRLISVRFSLLVVFLSLSGIGAGLCCPLGWSSFDQHCYKVFEPVKNWTEAEEICMQQHKGSRLASIHGSEEEAFVSKLASKALKFTSMWIGLNNPWKDCKWEWSDNARFDYKAWKRRPYCTVMVVKPDRIFWFTRGCEKSVSFVCKFLTDPAV", "text": "FUNCTION: EMS16 is a potent and selective inhibitor of alpha-2/beta-1 (ITGA2/ITGB1) integrin and acts as a potent antagonist of platelet aggregation and cell migration. Binds specifically to the I domain of the alpha-2 subunit, in a metal ion-independent fashion. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
{"protein": "MTQFITHKWLAALGLASSIAAFPALAAKDVVVAVGSNFTTLDPYDANDTLSQAVAKSFYQGLFGLDKDMKVKNVLAEGYTVSDDGLTYTITLRQGVKFQDGADFNAAAVKANLDRASNPDNHLKRYNLYKNIAKTEVVDPATVKITLKQPFSAFINILAHPATAMISPQALEKYGKDIGFHPVGTGPYQLETWNQTDFVKVKKFAGYWQQGLPKLDSITWRPVTDNNTRAAMLQTGEAQFAFPIPYEQAALLAKNKNLELVASPSIMQRYISMNVTQKPFDNPKVREALNYAINRQALVKVAFAGYATPATGVVPPSIAYAQSYQPWPYDPAKARELLKEAGYPDGFSTTLWSSHNHSTAQKVLQFTQQQLAQIGVKARITAMDAGQRAAEVEGKGQKESGVRMFYTGWSASTGEADWALSPLFASQNWPPTQFNTAFYSNKQVDSDLAAALKTNDPQEKTRLYKEAQDIIWKESPWIPLVVEKLVSAHSKNLTGFWIMPDTGFSFDDADLK", "text": "FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Binds glutathione. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
{"protein": "MQRFAAKRSVQNISVSLWRRCISSTSQAATASVKDSDEFQARLPPFAYTPPPYTGPSADVILSKRKEFLSPSMFCLYRKPLNIVDGKMQYLFDESGRRYLDAFAGIAVVNCGHCHPDVVEPVINQIKRLQHPTVLYLNHAIADFSEALASKLPGDLKVVFFTNSGTEANELALMMAKLYTGCQDIVAVRNGYHGNAAATMGATGQSMWKFNVVQNSVHHALNPDPYRGVFGSDGEKYAKDLQDLIQYGTTGHIAGFICEAIQGVGGIVELAPGYLSAAYDTVKKAGGLFIADEVQSGFARTGNFWGFEAHNVVPDIVTMAKGIGNGFPLGAVVTTPEIAGVLTRRSYFNTFGGNSVSTTAGLAVLNVIEKEKLQENAAMVGSYLKEKLTQLKEKHEIIGDVRGRGLMLGVELVSDRKLKTPATAETLHIMDQMKELGVLIGKGGYFGNVFRITPPLCFTKDDADFLVEAMDYSMSKM", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MYLPQEIIRRKRDNKVLTTEEINFFIQGVAKNTVSEGQIAAFAMAVYFNEMTMPERIALTCAMRDSGMVIDWSHMNFDGPIVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLESIAGYNIMPNNDLFGKVTKEAGVAIIGQTGDLAPADKRVYATRDVTATVDNISLITASILSKKLAAGLDSLVMDVKVGSGAFMPTYEASEELAKSIVAVANGAGTKTTALLTDMNQVLASTAGNALEVREAIRFLTGEYRNPRLYEVAMALCAEMLVIANLAKDEQEACIKLQAVLDNGKAAECFGKMVFGLGGPNDIIENYDNHLETAQIIKPVFADKSGFVNTMDTRDLGMAVVGMGGGRRVASDTIDYAVGLSDMIRLGQTVDSNQPLAMIHARNEDQWQQAADAVKAAIVISEEQPEATPEVYRKVRSQDV", "text": "FUNCTION: The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family."}
{"protein": "SLGSPAVAEPAVIAE", "text": "FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA (By similarity). SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon wounding. SIMILARITY: Belongs to the PDGF/VEGF growth factor family."}
{"protein": "MHFLQNAVVAATMGAALAAAAPLEKRSCTFTSASAAKSGKSSCSTITLDNIAVPAGETLDLTGLKKGTTVIFEGETTFGYKEWKGPLISMSGTDITVKQASGAKINCDGARWWDGKGSNGGKTKPKFFQAHKLDQSSITGLKVYNTPVQGFSILADHLTITDVTIDNSAGTSKGHNTDAFDIGQSTYITIDGATVYNQDDCLAINSGEHITFTNGYCDGGHGLSIGSIGGRSDNTVNDVTISNSKVLNSQNGVRIKTIYGKTGTVENVKFEDITLSDISKYGIVVEQDYENGSPTGTPTNGVKVEDITFKKVTGSVKSSGTDIYILCGSGSCSNWTWSGVDVTGGKKSSKCKNVPSGASCSD", "text": "FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall. FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall (By similarity). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
{"protein": "MDVKWEGFSGVEMEEVKRNVFLTTLEQLKGWARSSSLWPLTFGLACCAIEMMAVGGAHYDLDRFGSFFRASPRQADVMIVSGTVTKKMAPLLRRLYDQMPEPKWVIAMGSCATAGGPYVKSYSVVKGVDQIVPVDVYIPGCPPNPAALIYGIHKLKEKIRLEAKTGKKVL", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MAKRALGIGKQNKTAKKQKKSDSPTPEPTPASQIQVEIEEGVDPDDELVQLRGLWKTYFNSDRDDELVLNGIVHECDRLLREKENTEQAKDKEKPHTELSDEFHAIYALALSELTIFRAGDESMDEKDCRKAVAQFFDAALERCDIGLSQFPDSGLLKLTHAKIVLQRIPLQYISKLTSESKNAKKLKLHEQLEQAKRDLVLDFKYRDLVFDVLQLLDDLLDICENWGQGADDDEEPLGSDTEEQVRDLELPAEHPLSQIRAETPENFSFLREKLKELLATLPKPDTKDVDSKDVELYRSVARKLGQLHLRAAEPASQAFLLLTYESTGEKEMHGFSAPQAQAEALSLVRAAVKYLEEAREDDEPQTWVDIAEALTSLGNLYDAESKEQEECYKKAEDILKKANKATHGKYQDVLDNLLEAKD", "text": "FUNCTION: Required for correct translation termination and probably involved in regulation of hypoxic gene expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETT1 family."}
{"protein": "MRRLPTREVVDMKMVVAVIRPEKLECVKKALEERGFVGMTVTEVKGRGEQKGIRLQFRGREVEVDLLQKTKVEVVVSDDAVDEVVEAIVSSARTGKFGDGRIFVIPVEKSVKIRTGDEEV", "text": "FUNCTION: Involved in the regulation of nitrogen metabolism (By similarity). Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell (By similarity). Regulates the activity of the ammonia channel Amt3 via direct interaction (Probable). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the P(II) protein family."}
{"protein": "MRIVLDAERCVGAGQCEATAPELFTQGDDGLGLVRDRPVTPELLGPAREAVDRCPVRAIRIESSVRTGWARGAG", "text": "FUNCTION: Specific electron transport protein capable of effectively supporting cytochrome P450 MycCI activity in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic."}
{"protein": "MSRDPILSLPWPDARPLPDTFFDRDALLVARELLGKVIRHRQGNLWLAARIIETEAYYLEEKGSHASLGYTEKRKALFLDGGHIYMYYARGGDSLNFSAGGPGNAVLIKSGHPWLDRISDHTALERMQSLNPDSQGRPREIGRLCAGQTLLCKAMGLKVPEWDAQRFDPQRLFVDDVGERPSQVIQAARLGIPKGRDEHLPYRFVDAAFAAFCTRNPLRRGQVAGRDYHLLGHQDPHLQ", "text": "SIMILARITY: Belongs to the DNA glycosylase MPG family."}
{"protein": "MSTPDNRSVNFFSLFRRGQHYAKTWPMEKRLAPVFVENRVIRMTRYAIRFMPPVAVFTLCWQIALGGQLGPAVATALFALSLPMQGLWWLGKRSLTPLPPSILNWFYEVRGKLQEAGQALAPVEGKPDYQALADTLKRAFKQLDKTFLDDL", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0208 family."}
{"protein": "MSTKSMIRDVELAEEVLSKKAGGPQGSRSCWCLSLFSFLLVAGATTLFCLLHFGVIGPQREEQSPAGPSFNRPLVQTLRSSSQASSNKPVAHVVANISAPGQLRWGDSYANALKANGVELKDNQLVVPTDGLYLIYSQVLFRGHGCPSTPLFLTHTISRIAVSYQTKVNILSAIKSPCHRETPEGAEAKPWYEPIYQGGVFQLEKGDRLSAEINQPEYLDYAESGQVYFGIIAL", "text": "FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity). FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. SUBCELLULAR LOCATION: [C-domain 2]: Secreted. SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted. SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane; Single-pass type II membrane protein. SUBCELLULAR LOCATION: [C-domain 1]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the tumor necrosis factor family."}
{"protein": "MTQRAQDALLSFSQRYVDAWQQQHQSLPRNEELVDIVSPCVEEKSGDAVLWKHYPREQFADFTNVETGIELTLHEDVKTFYGAQFSADMNATFDGNELTLLQIWSDDDFECLQENILGHLVTQRRLKLKPTVFIAATDAELDVISICNLTGNVILERLGTKNRDVLAETLAEFLEKLQPAV", "text": "FUNCTION: Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Loosely associated with the cytoplasmic side of the inner membrane, probably via SecY. SIMILARITY: Belongs to the Syd family."}
{"protein": "MRLLYGIRAHHDKIWSVSSHQKLPLLATGSSDKTSAIFRLSETEKFPRVTTLDDTHTRSIRSVMFKPPIDDTVVDENELLDPPTLAMGSFDAKLSVWQAELPQDNDEDMDQEPREIWKQERKVVERAAQWELMAVIEGHEHEVKAVAWNCHGSLVASCSRDKTIWIWETDPDTLEEFECISVLTEHQQDVKHVIWHPTQNLLASSSYDDTICIYRQEYDDDDWGCAAVLNGHQGTVWCSAFEHPKSPSASETTVRLVSASDDLTVRIWSTSKEGSETNHDALPSSIKSSNEMQWDQECILPSAHTYPVYSVVWSSVSGRIASAGADGKIAVYKQTDGVWEIEGVTSAAHGVHEINTLAWSKLDDNREVLVSGGDDGYVNVWE", "text": "FUNCTION: Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Preferentially localized to the nucleus. SIMILARITY: Belongs to the WD repeat CIA1 family."}
{"protein": "MSDILNNLIHLLKLEKIDDLIFRGESQDLGFRQVFGGQVVAQALSAAMQVAPEDRILHSCHAYFLAPGDSQYPIIYDVETLREGRNFSALCVKAIQHKNTICHVTASFQVPEKGFEHQNTMPNVGAPEDFTDENVMLQKVAQTLPEPLNEKFAAERPFEVRTKYLNNPFNGTKLPAEQYSWFKTNGETPLDIKIQQCLLAYFSDFHCILTALHPHEKGFLQKGMKVATIDHSIWFHRPFDLNHWHLHAIESNNAFGGRGLAQGQIFSQDGQLIATTQQEGLIRFSE", "text": "FUNCTION: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA. SIMILARITY: Belongs to the C/M/P thioester hydrolase family."}
{"protein": "MSVEASRTCFLIDSLLNKKPKEELETEEEDEEEDEEEELSSSEVTSENDMETESASSSASSVGQPKPDFSAFHKIFSNLDFAKLAAVKRNGHHQPMLFRPECFFPLELSKHLHLVQQTFQMNVLQNLGHTLPLPFVPMLKNVAPAQKRLNNKRASYVDHSQKGNLKKYRCDVCDKTFSRSNTLITHKRIHTGEKPFKCEHCGRAFRQPGNLTRHRLTHTTVKPYVCGLCDKAFNRASNLHTHMRTHTNV", "text": "FUNCTION: Required in the M3 pharyngeal motor neuron to guide the growth cone of the sister M2 motor neuron during axon development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "DEPDGVPTRQKQ", "text": "FUNCTION: Does not function as a hemocyanin. SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily."}
{"protein": "MVITLLNLNKKHYLLILFFILLNGCSIDKNIILNKKQKQHKIFNLPITHTSKETHNFNYQDNKQSNNNYLEPLFEDYKPRNVGDILTIILQENTSASNSVSNNSIHNGNSNFDIDIGNARAFDDPNGILNKIELNSSIKNNFLGKGSSSANNTFVGLITVIVDRILPNGNLEVSGSKNITINDGIEKICFYGIVNPHTISKNNSVLSTKVANTNITYISSGPINIGSKINWLQRLFVSLFTLSK", "text": "FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family."}
{"protein": "MLVLLAATFFIYISRLTSTDALQLIQRGLRGKSETFDANATIVPEISESKRVIFGPKPTDLQHEEALVASYADPFKAALSIFKLLGANKFHQMTSSKTQLRYAFVKLRRWSQRPIAEPKRSWWQWRSKTGNKSRDDLAQKRGFRSWWSGRHKAKNAKRVA", "text": "FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus Host cytoplasm Note=Localizes to speckle-like structures within the nucleus. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MRTLWIMAVLLLGVEGSLIQFETLIMKVAKKSGMFSYSAYGCYCGWGGQGQPQDATDRCCFVHDCCYGKVTGCDPKMDIYTYSEENGDIVCGGDDPCRKAVCECDKAAAICFRDNKDTYDWKKYWRFPTKNCQESVPC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that shows a moderate inhibition of ADP-induced human platelet aggregation when tested on platelet rich plasma. Exhibits high hydrolytic activities and prefers the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
{"protein": "MSLPTTSSPLTNDQEFAKPVRNGKIFENPKSFTNWGGRPGLTNIFKLVLRETSHENLPSDKKVLDSTLPVHNITADDFHSESGLFATWLGHATVLVDLEGVKFVTDPVWADRASFTSFAGPKRYRPPPMKLEDLPDLDFAVVSHDHYDHLDADAVKRITNLNPQIKWFVPLGLKKWMKNQGIGADGSNTVTELNWGESSEFVKNGKTITIWCLPAQHSGQRGLSDHNHRLWSGWAVIGENRRFYFPGDTGFCDVEFKKIGEKLGPFDLAAIPIGAYEPRWFMKSHHINPDEAVEVHKLVRARNSIGIHWGTYPMGTTEYYLEPRDKLKELMDAREDLKDTSFVTVDMGEIWEASDR", "text": "FUNCTION: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (PubMed:25423491). NAEs are bioactive lipids that are involved in diverse physiological processes such as growth and lifespan (PubMed:21562563, PubMed:25423491). SIMILARITY: Belongs to the NAPE-PLD family."}
{"protein": "MYSTKCTNFFLEIIFYVIFCTLFLLVLEKMSKLLSWIVIVCLFVFAISSKCSAQNYGINVPITGSMDVVLANSTQDQIGLTSTLCIYYPKAADTEIADPEWKATVTQLLLTKGWPTTSVYLNEYQDLVTFSNDPKLYCDYNIVLAHYTNDVALDISELAEFLLYEWLCNPMDVTLYYYQQTSEPNKWIAMGTNCTIKVCPLNTQTLGIGCQTTNTDTFEILTMSEKLAIIDVVDGVNHKVDYTVATCKINNCIRLNPRENVAIIQVGGPEVLDISENPMVIPKVSRMTRMNWKKWWQVFYTIVDYINTIITTMSKRSRSLDVSSYYYRV", "text": "FUNCTION: Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum lumen Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. SIMILARITY: Belongs to the rotavirus VP7 family."}
{"protein": "MSWTTPKRAFIGAATAEGGTKLNAFDNALLKLGIGNVNLVKLSSVIPAHIEWMEKVHDVPIGMLLPTVYAHIESDEPGMTISAALGVGISKNNEGGLIYEYSGYCTKEEAEEMVRKMVEEGFRQRGWELGEFKVASAEITVKDKPAAAIAVVVMFPY", "text": "SIMILARITY: Belongs to the PdaD family."}
{"protein": "MRSFIKSHRKSNSLESDSDIDFKQLKRKNASTSQLSPPRYNTDYYDPVTSSPKTPTHSHTTSDSLPQKHSPGFESLHRLFNNKLFKKASNSSLNSYLANTDSQSRRSSKDQDPLAPSFHVLKTSSNPASQDSELPVIKGVITHTWGNHSKHNDPHVIVLNDPKTSFETLRSSDLEPPPRLTSKTTRSSVSSERSWSTRDHSMSPPLTSINQDIDIPEDMATRSKNTLINKKKMENRQARIHSNDDLIAMRKNSSDTLPQTAEFFASDKLPGDSTPILEIPESPPPVITLEKYNSSLSDAKELSRSKNVRSNRTSVVSMTQSEESRWSNHLMVNSNHNQNKLRDSDDSDYSNAIDEEDDDDADDDDEASQFSFEYSNLSGRTPSVKYYSKPEPKQMVYIDDLYDDEDFDEDMNYYDENEVSEFLQEEMASNKNNINTDTSVLKDLSSPSINDHSNEKPIYKPTIQMRVNKPKVHRYNDLFALSDEDDPSFNDDDEFDEDEEEGGDDNDEEDEIDEEYDQKVSDECGQSIELQSDDIHSDYGVEYYNDFGGDLNLQNDVQKHHINKEQQYISDEEFDDAITDFNMAKHIIEEEVVLDKAEALRYQKDAEPVQSKTSEDVVNYVDEDSNLRINEKLEKGDVTYQKPTLLTEVKNKQFQKKPVASFADIFNLESDSEEDINNEDGLTGLSDVGLDEDDAVSSPILQSPFESQSLAEGLVSPVICTPGKPNIINKQIIPTIKCEPSSPQEKTIENNKSHTASNFKEYGLNHPLPPPARSQALKFHDLNSELDSELPALMSNLYFIDETEEDAYNELNDVTRDEDEYLDEINTVPEDFNFSDTENDNNAAKRMLRRSNKGSFRSTYSFTDKPQGVTTESSPIKNKLEVNNKTVTFFSSPGWSKSPGSEIGMQRSKSPVKPSSGYRPFGQGSKQFPITPSHEPNYSIEEDRIASTDEILESRTPPTTYMAPSPAFIPNYSLSPIQEASSSVTNSPKR", "text": "FUNCTION: Involved in maintenance of polarized growth and daughter- cell-specific transcription. SUBCELLULAR LOCATION: Cytoplasm Bud Bud neck Bud tip. SIMILARITY: Belongs to the ZRG8 family."}
{"protein": "MFRSNARALNRALERLKNVQTKVNEALKRSGIQEKSLERKLRIWLRKVEENVPLGELILEKRSSCAIWLSDKDVEILEKVKRLEEQGQDLIKKISVNKSSREIVERVLGPSFHPQKTALEMLDKLKDCLKKKNVQKIGVWGMGGVGKTTLVRTLNNDLLKYAATQQFALVIWVTVSKDFDLKRVQMDIAKRLGKRFTREQMNQLGLTICERLIDLKNFLLILDDVWHPIDLDQLGIPLALERSKDSKVVLTSRRLEVCQQMMTNENIKVACLQEKEAWELFCHNVGEVANSDNVKPIAKDVSHECCGLPLAIITIGRTLRGKPQVEVWKHTLNLLKRSAPSIDTEEKIFGTLKLSYDFLQDNMKSCFLFCALFPEDYSIKVSELIMYWVAEGLLDGQHHYEDMMNEGVTLVERLKDSCLLEDGDSCDTVKMHDVVRDFAIWFMSSQGEGFHSLVMAGRGLIEFPQDKFVSSVQRVSLMANKLERLPNNVIEGVETLVLLLQGNSHVKEVPNGFLQAFPNLRILDLSGVRIRTLPDSFSNLHSLRSLVLRNCKKLRNLPSLESLVKLQFLDLHESAIRELPRGLEALSSLRYICVSNTYQLQSIPAGTILQLSSLEVLDMAGSAYSWGIKGEEREGQATLDEVTCLPHLQFLAIKLLDVLSFSYEFDSLTKRLTKFQFLFSPIRSVSPPGTGEGCLAISDVNVSNASIGWLLQHVTSLDLNYCEGLNGMFENLVTKSKSSFVAMKALSIHYFPSLSLASGCESQLDLFPNLEELSLDNVNLESIGELNGFLGMRLQKLKLLQVSGCRQLKRLFSDQILAGTLPNLQEIKVVSCLRLEELFNFSSVPVDFCAESLLPKLTVIKLKYLPQLRSLCNDRVVLESLEHLEVESCESLKNLPFVPGNTGMINEQMAWEYMSRTLG", "text": "FUNCTION: Probable disease resistance protein. SIMILARITY: Belongs to the disease resistance NB-LRR family."}
{"protein": "MSKFVITCIAHGENLPKETIDQIAKEITESSAKDVSINGTKKLSARATDIFIEVAGSIVQKDLKNKLTNVIDSHNDVDVIVSVDNEYRQAKKLFVFDMDSTLIYQEVIELIAAYAGVEEQVHEITERAMNNELDFKESLRERVKLLQGLQVDTLYDEIKQKLEVTKGVPELCKFLHKKNCKLAVLSGGFIQFAGFIKDQLGLDFCKANLLEVDTDGKLTGKTLGPIVDGQCKSETLLQLCNDYNVPVEASCMVGDGGNDLPAMATAGFGIAWNAKPKVQKAAPCKLNTKSMTDILYILGYTDDEIYNRQ", "text": "SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family."}
{"protein": "MNWLPEAEAEEHLKGILSGDFFDGLTNHLDCPLEDIDSTNGEGDWVARFQDLEPPPLDMFPALPSDLTSCPKGAARVRIPNNMIPALKQSCSSEALSGINSTPHQSSAPPDIKVSYLFQSLTPVSVLENSYGSLSTQNSGSQRLAFPVKGMRSKRRRPTTVRLSYLFPFEPRKSTPGESVTEGYYSSEQHAKKKRKIHLITHTESSTLESSKSDGIVRICTHCETITTPQWRQGPSGPKTLCNACGVRFKSGRLVPEYRPASSPTFIPSVHSNSHRKIIEMRKKDDEFDTSMIRSDIQKVKQGRKKMV", "text": "FUNCTION: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the type IV zinc-finger family. Class A subfamily."}
{"protein": "MAALLLLFLFLFASSALSQDSLIGVNIGTEVTNMPSPTQVVALLKSQNINRVRLYDADRSMLLAFAHTGVQVIISVPNDQLLGISQSNATAANWVTRNVAAYYPATNITTIAVGSEVLTSLTNAASVLVSALKYIQAALVTANLDRQIKVSTPHSSTIILDSFPPSQAFFNKTWDPVIVPLLKFLQSTGSPLLLNVYPYFDYVQSNGVIPLDYALFQPLQANKEAVDANTLLHYTNVFDAIVDAAYFAMSYLNFTNIPIVVTESGWPSKGGPSEHDATVENANTYNSNLIQHVINKTGTPKHPGTAVTTYIYELYNEDTRPGPVSEKNWGLFYTNGTPVYTLRLAGAGAILANDTTNQTFCIAKEKVDRKMLQAALDWACGPGKVDCSALMQGESCYEPDDVVAHSTYAFNAYYQKMGKASGSCDFKGVATVTTTDPSRGTCVFPGSAKSNQTLGNNTSALAPSANSTTSGCIPKYYHHPHASFGDLTLLSLLLIIALVFL", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
{"protein": "MNLHLVDSDGHLEAEKKLTEYLTSIVAPSVSPSRGSATADGDYGNGALEAVGLNYHVVGVFGGQSSGKSTLLNHLFGTHFQMLDETVRRGQTTKGAFMALANTALAGLEASDVAVVAPRLAPSAADRSSRLNHAVAAAVTNNTTGGAPPTGSPLLVLDFEGTDGLERGEDQCFERQLSLFGLSIVDTLIINMWAVDVGRFNAANLSLLRTIFEVNLQLFSHSNYEAEEKPTLLVVLRDFTEDDPLPSLTTVRKSFDTIWESITRPAQFEDTSIDALFHLKYYVMPHYRLQKEEFMASVETLRRWFGDSRCSDYLFSYHSMFRGVPLDGLPAYLTNCWAAIRTSKDLDIPTQREMLAQHRCKEAKEQELMTYRDFARGYEDRLLRGEMLLRLSEVLDEEMETRLTAFYRQTKLYSSAVVGQYANELETELVDATMQVLNRLSKAIATEVLSNVESRVLNSVEESLRQLLKSAQTLPFSAGEDSSTTEPAEAHDADEDAARLLGAQRMDSAACQRLVRGFWRTLSIQVKEVVAEVAAMPPRAHLYGRYAVLIVQDPTTRLNVLNIVTDAFFQKVKSRLVSMANSACDTMHSGFERSLTYNSDGTVRFFATTRGLQKAVPAAVQAGLVVLGSLFYFRLKLVSAAVSDDDDLDTGATAALPQSRSARRVRHNRCHIVFDDNDAEAAFYLSYSTLDTAPKYPCDVPVPTLDCDREEVGVAADCVLLSQQATVRAYELYKQKCDFTTQLQLRAAEAGNQRLPAWVIPALFILGWNELLYVLTSPALLVLVVVICAVFFRQFFVSQWHAFEETGPASVVIPVRTVVHALSALVRSLLGDGQGSCPERAARNGSDVVASGEREMAHVKVTSTHADPAPSNTTVPTAQATMRHRTTHKLD", "text": "FUNCTION: Probable GTP-binding protein that may be involved in cell development. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily."}
{"protein": "MYQTTTLKDKIKLFIIILLPILITQVSINLMSFFDTMMSGQFSARDLAGVAIGSSLWVPILTGINGIVLSITPIIAHLIGAKNKKDIPQVIQQGIYLSFVLSIIIIVIGGIALDPILQAMSLEKEVQRIAKYYLITLGTGIVPLFLFHTIRSFMDGLGQTRSSMIIILISLPINAVLNYILIFGKFGIPAFGGIGAGIATSLTYWIISGISIFMIHRVYPFHSYKVFQKILPPTLSYWADQLKIGLPIGLAIFFETSIFSAVTLLMSEYNTNTIAAHQAAMNFASLLYMLPLSVGMALTIAVGFEVGAKRLHDAKRYTYLGIMGGLFIAIFAGIILYTFDDVVARLYNSNPEVIELTKQFIIFAIFYQLADAIGAPIQGALRGYKDVNMTLVIALISYWIIGLPTGYLLANYTALEPFGYWVGIIVGLSTGAIALLARLLFIQKKSV", "text": "FUNCTION: Multidrug efflux pump. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MQPPWGLALPLLLPWVTGGVGTSPWDYGLSALAHQPGVCQYGTKMACCYGWKRNNKGVCEAMCEPRCKFGECVGPNKCRCFPGYTGKTCTQDVNECGVKPRPCQHRCVNTHGSYKCFCLSGHMLLPDATCSNSRTCARLNCQYGCEDTEEGPRCVCPSSGLRLGPNGRVCLDIDECASSKAVCPSNRRCVNTFGSYYCKCHIGFELKYIGRRYDCVDINECALNTHPCSPHANCLNTRGSFKCKCKQGYRGNGLQCSVIPEHSVKEILTAPGTIKDRIKKLLAHKRTMKKKVKLKMVTPRPASTRVPKVNLPYSSEEGVSRGRNYDGEQKKKEEGKRERLEEEKGEKTLRNEVEQERTLRGDVFSPKVNEAEDLDLVYVQRKELNSKLKHKDLNISVDCSFDLGVCDWKQDREDDFDWHPADRDNDVGYYMAVPALAGHKKNIGRLKLLLPNLTPQSNFCLLFDYRLAGDKVGKLRVFVKNSNNALAWEETKNEDGRWRTGKIQLYQGIDTTKSVIFEAERGKGKTGEIAVDGVLLVSGLCPDDFLSVEG", "text": "FUNCTION: May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. SIMILARITY: Belongs to the nephronectin family."}
{"protein": "MAAVTAALVKELRERTGLGMMECKKALVEAEGDIERAIDDLRKSGQAKAAKKAGRTAAEGAIAVAVSGDGKTAIMVEINSETDFVARDDNFLGFANKVAEAALAAAKTEAADIAGVELADGSTVEQAREALIQKIGENIQVRRAAILSAESALGAYVHGGKIGVLVALKGGDEALGRDVAMHVAAVAPQVVNPSEVPESDLEREKEIIRAQPDMAGKPAEIVEKMLGGRIQKFLKEISLVEQPFVKD", "text": "FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EF-Ts family."}
{"protein": "MLRHRNCLCEKTFKLVRLTSSRQRVLSFGFLTISPSNSLMEPKKSFNFLVFVVALSYIFSLYQVLALTPEGIILYALLFLLNFVFAFVVNDTAIAIKYLFVLMAMRAINLIYSLPLDEDAIRMFAGYRLLHGVNPYLPMPTVFNHYDVPIGLRTLTEYGGFVERLIYPGLSVFAGVAEYALGYVIFNVVIYVTFILISYVFLRNKSTEALIFAVLWLLFGGVNLATLLLTVGILLRKYNGFFVGLAISYNQLYTLIAPFLVIYYLAEGKKEVLRQVAYALFGFLITNVPFMVWDFKLWFSAMLYSVSQPIVPIGFSISRETYMGFFPIPFKVYEYLFITMYIASIVIYAIMFKIVAKWAYVFPAISMIAYPRTLLGYITSWLPPAFFFFFTRTEGNVKVAKLKPLGTAVLIAIMIMPIFVPALTSTDVNTPFTFKVTKVYVGTYGNVYKMSINATVYSPTVKNITFVVIPDFYPFYNTYLWWSTVNVTVGQNYFNITPLAPSQEIGFNNATYTVVGVYGPYYYFVTLVLVSNGTMFSNFTYTPKE", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein."}
{"protein": "MAGVITASEPSWIAPFSGLSPRQFGKLVTVLRREGADAVRKGRPWSLPLEDRALLVAAYWRTNLTMRQLAPLFGVSKSAADRIIDHLGPMLALQPRKRFAKDTVLIVDGTLVPTRDHTIAERSKNYRYSTNHQVVIDADTRLVVVVGRPLAGNRNDCKAWEESGAKAAVGKTLTIADGGYPGTGLVIPHRRERGQAGLPDWKEEHNKSHKQVRARVEHVFARMKTWKILRDCRLKGDGVHHAMLGIARMHNLALTG", "text": "FUNCTION: Involved in the transposition of the insertion sequence IS112 which inactivates the SalI restriction-modification system. SIMILARITY: Belongs to the transposase 11 family."}
{"protein": "MEERQITIVDEKGNEHLCEIIFTFDADKFGKKSYVIFSPIGEVDEDGDPIYDAMAYEQNEEEGGVLLPIESEEEWEMVQETFNTIADEQEAE", "text": "SIMILARITY: Belongs to the UPF0473 family."}
{"protein": "GWKDWLKKGKEWLKAKGPGIVKAALQAATQ", "text": "FUNCTION: Shows a broad spectrum of activity against both Gram-positive and Gram-negative bacteria. Has also antimicrobial activity against S.cerevisiae. Has insecticidal and non-hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ponericin-G family."}
{"protein": "MVLKVYVSGMSGNKEVKKRQQRVLMILDSKNIKYDTVDITEPGKESEKELMQNKSTSNGGTVSDPEPRHPLPPQLFNDDEYCGDYDAFDMANEIDTLEVFLKLAPADTTAVSTAQIELKQENGDAKKEEAETEAEDKKTEAGDGDVDVKEEAAEKAEV", "text": "SIMILARITY: Belongs to the SH3BGR family."}
{"protein": "MAAKIIDGKTIAQQVRSEVAQKVQARIAAGLRAPGLAVVLVGSNPASQIYVASKRKACEEVGFVSRSYDLPETTSEAELLELIDTLNADNTIDGILVQLPLPAGIDNVKVLERIHPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTFGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGDWIKEGAIVIDVGINRLENGKVVGDVVFEDAAKRASYITPVPGGVGPMTVATLIENTLQACVEYHDPQDE", "text": "FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP. FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family."}
{"protein": "MEDFVRQCFNPMIVELAEKTMKEYGENPKIETNKFAAICTHMEVCFMYSDFHFINERGESIIVEPGDSNALLKHRFEIIEGRDRNMAWTVVNSICNTTGVGKPRFLPDLYDYKEDRFIEIGVTRREIHIYYLEKANKIKSEETHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRRLADQSLPPNFSSLDNFRAYVDGFEPNGYIEGKLSQMSREVNARIEPFLKTTPRPLRLPCGPPCFQRSKFLLMDALKLNIEDPSHEGEGIPLYDAVRCMKTFFGWKEPTIVKPHEKGINSNYLLAWKQVLAEIQDIEDEKKIPRIKNMKKTSPLKWALGENMAPEKVDFDDCKDVSDLKQYDSDEPEFRSLASWIQNEFNKACELTDSSWLELDEIGEDVAPIEHIASMRRNYFTAEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCILEIGDMVLRTAIGQVARPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEEGSIGKVCRTLLAKSVFNCLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFDLGGLYESIEECLINDPWVLLNASWFNSFLTHALR", "text": "FUNCTION: Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus Note=PB1 and PA are transported in the host nucleus as a complex. SIMILARITY: Belongs to the influenza viruses PA family."}
{"protein": "MAEVRARVDFKVGAKSNIDAEILSFRGLKTDKEHVAVIFKQADQTQDTPLVRMHSECLTGDVFHSSRCDCGEQLEETIQRMGESGGVILYLRQEGRGIGLYNKIDAYRLQSQGMNTYEANNHLGFDDDLRDFTEAAQMLEALGIKKIRLVTNNPKKIRELAEYGIEIVEVVNTSAHIKDGNENYLRAKVSHGKHNLKV", "text": "FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. SIMILARITY: Belongs to the GTP cyclohydrolase II family."}
{"protein": "MVSSTWGYDPRAGAGDLVITTTAAGAVTIAVLLFQTVCGDCGPPPDIPNARPILGRHSKFAEQSKVAYSCNNGFKQVPDKSNIVVCLENGQWSSHETFCEKSCDTPERLSFASLKKEYFNMNFFPVGTIVEYECRPGFRKQPSLSGKSTCLEDLVWSPVAQFCKKKSCPNPKDLDNGHINIPTGILFGSEINFSCNPGYRLVGITSILCTIIGNTVDWDDEFPVCTEIFCPDPPKINNGIMRGESDSYKYSQVVIYSCDKGFILFGNSTIYCTVSKSDVGQWSSPPPQCIEESKVPIKKPVVNVPSTGIPSTPQKPTTESVPNPGDQPTPQKPSTVKVPATQHEPDTTTRTSTDKGESNSGGDRYIYGFVAVIAMIDSLIIVKTLWTILSPNRRSDFQGKERKDVSK", "text": "FUNCTION: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the receptors of complement activation (RCA) family."}
{"protein": "MGGLEFCDQTSWYQIFIAFSLTYTPIAIYSLKVFRGTLAGIVNIFIFINCCVSFVYLMYHHSVTNTIALSLGAVIALVWGIYTLVKIVDWLVIRCRLCFLGRSYILAPPSHVDTSDGRQSLTTSLTTAFVVRKPGSTLVNGQLVPDFQRLVLGGKKAVSKGAVNLLKYVSK", "text": "SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein."}
{"protein": "MNKIWKLKNVKVGVAPILWTNDDMPELGGDISFDRAISEMAQAGYQGTEIGNKFPKDAKILLRELKKYNLEIASAWFSGYIISDFEKNFQDFQKHCLFLKALGAKVVVFSEQTYSIQGQNKPLFKDKPYFTNQEFENLAQGLNKFGKWSKQHGIELVYHHHMGTGIQSLKETEKILELTDPEFVSLIFDTGHFAHAGEDIVFCLKRLISRIRHIHLKDIRKEKINELKAKNLSFLEGVKQGIFTVPGDGDIQNYPLFFELLAKNNYQGWLIVEAEQDPRKANPLEYAKKAMDYLRSLISW", "text": "FUNCTION: Catalyzes the dehydration of inosose (2-keto-myo-inositol, 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol). SIMILARITY: Belongs to the IolE/MocC family."}
{"protein": "MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSEEDKKGFTKLVYQNIFTAMQSMIRAMETLKILYKYEQNKANAVLIREVDVEKVMTFEQPYVSAIKTLWNDPGIQECYDRRREYQLSDSAKYYLSDVDRIATPGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Cytoplasm. SIMILARITY: Belongs to the G-alpha family. G(q) subfamily."}
{"protein": "MEGERMNAFPSTMMDEELNLWDFLERAAALFGRKEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALREQYKNYYGGA", "text": "FUNCTION: Catalyzes the esterification of a number of long chain fatty acids with CoA, resulting in the formation of long-chain fatty acyl- CoA. Myristate (C14) is the most efficiently processed fatty acid, followed by palmitate (C16). Also catalyzes the esterification of stearate (C18) and laurate (C12), but at lower efficiency. Does not catalyze the esterification of the unsaturated fatty acids mysteroleic and palmitoleic acids in vitro. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MSTKAWNASRLSGPDPSTPWSLKKPLQHGSRPPKGKRLTVCPPTRPKQTIRISASHASQQLDQAKAACLAVTIRDLEEATAVMRSWEHSLVTPQCIAPRYSIIMFMITAVKRLRESKMLTLSWFNQALMMVSKSGEEMRNLRTAMWILANLIPREVLPLTGDLLPSLQQQEPPMLKQ", "text": "SIMILARITY: Belongs to the morbillivirus protein C family."}
{"protein": "APKNIVLFGATGMTGQVTLGQALE", "text": "FUNCTION: Broad specificity oxidoreductase that catalyzes the NADPH- dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MTLQEQIMKALHVQPVIDLKAEIRKRVDFLKDYVKKTGAKGFVLGISGGQDSTLAGRLAQLAVEEIRNEGGNATFIAVRLPYKVQKDEDDAQLALQFIQADQSVAFDIASTVDAFSNQYENLLDESLTDFNKGNVKARIRMVTQYAIGGQKGLLVIGTDHAAEAVTGFFTKFGDGGADLLPLTGLTKRQGRALLQELGADERLYLKMPTADLLDEKPGQADETELGITYDQLDDYLEGKTVPADVAEKIEKRYTVSEHKRQVPASMFDDWWK", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. SIMILARITY: Belongs to the NAD synthetase family."}
{"protein": "MFSKMFNYFASSSKTHLDNTQESAINCGQHSAEAASYAVKTLPQILLGLITFKEISGSVMTGYAFGFALPEFAKVIVKSLASTIFFHPTASMVGTVAVTVAANSENVVECIKNTAHALYDAGSTVYEGTLCAVNGAAAAATFVYDNVCSTDVQLSGNAIEAVL", "text": "SIMILARITY: Belongs to the UPF0416 family."}
{"protein": "MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINSVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKVITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPTKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKTQPPPSQPLPQSQPKQPQAPPTSQQPPSAPAQALPTQAQATPQHQQQLFLKQQQQQQTAPPAQQPAGTFYQQPQQQAQAPQFQAVHPAAQQPVIAQFPVVSQGSSQQQLIQNFYQQQQQQQQLATALHQQQLLTQQAALQQKTTAAAAPQPQAQPAAAASPAPAQEPAQIQAPVRQQPKVQTTPPPTIQGQKLGSLTPPSSPKAQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRASQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKYPEKLGGSAESLIPGFQPTQGDAFAASSFSAGTAEKRKGGQTMDSSLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLIDCSLLSNPTTDLLEEFAPIAISAPAHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL", "text": "FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Membrane, clathrin-coated pit Presynapse Note=Active when found in clathrin- coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MAANKNKNQSSLVLHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDKIPLLVVGNKSDLEDRRQVPMDEARGKAEEWGVQYVETSAKTRANVDKVFFDLMREVRTKKMSENKDKNGKKSGKSKKGFKQRCCLL", "text": "FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis. In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission (By similarity). Regulates the actin cytoskeleton to play a role in gastrulation or neurulation. During the cleavage stages, the GTP-bound form induces a cortical reaction that affects the localization of pigment granules. Activated by the FGF pathway via ras and ral-GDS, but independently of raf. Directs ralbp1 to the plasma membrane (By similarity). Involved in ligand-dependent receptor mediated endocytosis of the EGF and insulin receptors (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Midbody Note=During late cytokinesis, enriched at the midbody. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
{"protein": "GPLAVAINAAYMQTYIGGVSCPYICSRRLNHGVLLVGYGSAGYAPIRLKEKPYWVIKNSWGENWGENGYYKICRGRNICGVDSMVSTVAAVHTTSQ", "text": "SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MAASFSGPSMIMEEEGRFEAEVAEVQAWWNSERFKLTRRPYTARDVVALRGNLKQSYASNELAKKLWRTLKTHQANGTASRTFGALDPVQVTMMAKHLDSIYVSGWQCSSTHTTTNEPGPDLADYPYDTVPNKVEHLFFAQQYHDRKQREARMSMSREERARTPYVDYLKPIIADGDTGFGGTTATVKLCKLFVERGAAGVHIEDQSSVTKKCGHMAGKVLVAISEHINRLVAARLQFDVMGVETLLVARTDAEAANLIQSNVDTRDHQFILGVTNPNLRGKSLATLLATGMANGKTGAELQATEDNWLAMAQLKTFPECVMDAIKNMNAGEDEKRRRMNEWMNHTSYDKCLSYEQGREIADRMGLKNLFWDWDLPRTREGFYRFKGSVMAAVVRGRAFAPHADIIWMETAKPDFAECTAFAEGVKSMHPEIMLAYNLSPSFNWDASGMTDEQMRDFIPRIARLGFCWQFITLGGFHADALVIDTFAKDYARRGMLAYVERIQREERKNGVDTLAHQKWSGANYYDRYLKTVQGGISSTAAMGKGVTEEQFKETWTRPGAMEMGSAGSEVVAKARM", "text": "FUNCTION: Involved in storage lipid mobilization during the growth of higher plant seedling. SUBCELLULAR LOCATION: Glyoxysome. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family."}
{"protein": "MPNPAETTTQVRLDKWLWAARFYKTRSLARDQIEGGKVHYNGQRSKPGKAVEAGALIRVWQGQDEREVRVLQVSEQRKSAPLAQLLYEETEASLKKRAENSEARRFNSQFAPSPERRPDKQERRQLIKVKQY", "text": "FUNCTION: May play an important role in binding of nucleic acid. More specific for RNA (By similarity). SIMILARITY: Belongs to the HSP15 family."}
{"protein": "MSNRGRQPSGPPPSRKRETKWSGKPKRYANFGAQSFDTVITGHLTQEQLDAYQRYFRIEEISNFLSVAKQQHKSIVDVLPSAKVDETDHYKRDPSPPPKYDKNGNRTNTRERRVTEALEKERHELVELAASSIKNYMIPSNYRRPSRTVERLYVPVKDYPDINFVGFLIGPRGNTLKKLQEDSGARLQIRGKGSVKEGKSSDGFGSSQTGTDIQDDLHVLITADSPLKISKAVKLVNEIIDKLIFSPQGMNFMKRDQLKELAVLNGTLRETKPFDPEAHEKKQQQQMDITKIVCKICGNIGHIARDCKQNNGKRPLDDNAENEPTTINKKARTDVPPPPPPPPPPAPPSSSTEISKQVPPPPPPPPPPAPSAAASGFATTENYKQGLVPPPPPPPPPPPPPVRSALVNFENNSKVLLTKEKEESGSSELKNTGESSSSSSGVPPSPPPPSSNVPR", "text": "FUNCTION: Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BBP/SF1 family."}
{"protein": "MGNKNIKPSKENRLSILSKDKMDSFKRGSWATSSFREKSRATIQRFSSLRREHIKVDHPDKFLELKRGIYKIIQKSSSIDVDKRTKLMSNIKTMMINPFMIEGLMTSLENLDPDNKMSYSSVMILGEFDIINISDNEAAFEFINSLLKSLLLLNTRQLKLLEYSISNDLLYAHINALEYIIKNTFNVPERQLILRGQYLTPIFSDLLKYAGLTIKSNILMWNKQFIKPVSDLYTSMRLLHCVTESYKVIGMG", "text": "SIMILARITY: Belongs to the orthopoxvirus A47 protein family."}
{"protein": "MNQMNQTIIDAFHFRHATKEFDPTKKISDEDFNTILETGRLSPSSLGLEPWHFVVVQNKELREKLKAYSWGAQKQLDTASHFVLIFARKNVTAHTDYVQHLLRGVKKYEESTIPAFENKFDDFQESFHIADNERTLYDWASKQTYIALANMMTSAALLGIDSCPIEGFDLDKVTEILSDEGVLDTEQFGISVMVGFGYRAQEPKHGKVRQNEDDIISWIE", "text": "SIMILARITY: Belongs to the nitroreductase family."}
{"protein": "MLHQGIILREGHVTRTIYNLIKDKRYEDVIECITSFGEAANTRAGLSTLGHCYYHAQKYEEAATCYEQLCQLAPKEAKYRFYYAQSLYQAGIFADALRVLKQMGDQEDELREQCLQLQSAILYSSEDFAGAQSLLNQRAGGTADTLNDEGCLLFQADQHEAAVQRFQAALQVGGFNPLVAYNVALAHFQKKQRAQALDYTSEIVERGMRNHPELGIGAQMDIPDGGARSVGNPITMAISGITQALNLKAAIEFQDGNEEAARDALLDLPPRAESELDPVTLHNMALTDVEGPVAGLRKLAFLLELGAPSCPKETFANILLICCKNELYETAADILAEHTDLTYKYLSQYLYELLDSLITAQTSAELAEKKLGTLASSLAGKLRSLAAKVQEVRATNEQQALRDALKDYEQALELYLPVVMARAWISWRDDDFVGAEREFHASAEFCSENSIWRLNAGHVLFMQGDKYNEAAAFYEPIVRQHSDDIMSVSAAVLANLCVSYIMTFQNEEAEELMRKVEKAEEMKGNLGKQYHHLCIVNLVVGTLYCAKSNYEFGLSRIAHALESGSGNRLYADTWLHVKHCILGLLTGMAKQNIILPYATVQEVLNFLRFCESYGLFTPANIFSATEQVPEEPLTIGLEARKLRLLLIKLSEYDNF", "text": "FUNCTION: Required for polyglutamylation of axonemal tubulin in sensory cilia. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip. SUBCELLULAR LOCATION: Cell projection, cilium. SIMILARITY: Belongs to the TTC30/dfy-1/fleer family."}
{"protein": "MNWLNSEAFVLFDQHIIWSDMVGNILGLITLALGFRRSLWTWPVQFLSGLVLFGAFYGHLTGSAGKQAVVMAVALYGWYQWNRGTDKAADGKVSVRFATWAERGAMIAAAAVGTVAVALLFKAYPSLSWDPWPDAYIFVGTIVAMYAQARGMVEFWFAWLLVDLVGVPLNFANGYAFSGFVYVIYGALVLWGMRDWWLRSRRDSRPVLEGAPA", "text": "FUNCTION: Transports riboflavin and roseoflavin (PubMed:17541777, PubMed:22136195, PubMed:28406895). Can also transport FMN and FAD (PubMed:28406895). May confer roseoflavin resistance to S.davawensis, which naturally produces this antibiotic during stationary growth phase (PubMed:22136195). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake permease (TC 4.B.1) family."}
{"protein": "MSIQQIIEQKIQKEFQPHFLAIENESHLHHSNRGSESHFKCVIVSADFKNIRKVQRHQRIYQLLNEELNHSIHALALHLFTPEEWKAQNETVPHSTKCAGIGR", "text": "FUNCTION: Transcriptional regulator that plays an important role in general stress response. SIMILARITY: Belongs to the BolA/IbaG family."}
{"protein": "MAESILKSAKINRNVGQVLKSYLRVLKLSKKPSREEFLMISKVAGAGILVIGFVGFLIYVLLTEVPKWV", "text": "FUNCTION: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma family."}
{"protein": "MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWEQSLLEKFSTELNQQLNDLEACVIQEVGVEETPLMNVDSILAVKKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSKIFQERLRRKE", "text": "FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha/beta interferon family."}
{"protein": "MRDEVFKRPIKKQFEFDESVVSVFDDMVSRSVPYYCDVQALISLILSKNLSPNAKVFDLGCSTATTLLEIFKLRSDLSLNGVDSSEAMIKTARNRSLAYLANLNLYVSDILDFDFSGSDAVILNYTLQFIRPIKREEFIKKIYSNLKSGGIFIFSEKLVYEDKKLTLDMIEIYENYKHSQGYSKFEIAQKRQALENILIPYSENENKELCLNAGFKSVETIFKWANFATFIAFK", "text": "FUNCTION: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family."}
{"protein": "MKTLLLTLVVMTIVCLDLGYTLTCYMNPSGTMVCKEHETMCYRLIVWTFQYHVLYLKGCSSSCPGGNNCACCSTDLCNN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily."}
{"protein": "MKITTKVLIIGSGPAGLSAAIYTARAALKPILINGMQPGGQLTITTDVENYPGFAETVQGPWLMEQMYMQAKNVGTEIVSDYVEKVDLSKRPFKVFTGAGNEYDAESIIICTGAEAKWLGIASEQKFRGFGVSACATCDGFFFKNQEIVVVGGGNSAVEEALYLTNHANKVTIVHRRDSFRAEKILQDRLFKNSKISVIWDHVVDEIVGSNKPKSVTGVKIQNVHTKEISLLNCSGVFIAIGHAPNTGLFTGQIVMDDDNYIITKSGTTRTSVEGVFAAGDVQDKIYRQAVTAAGTGCMAALEAEKFLNK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MPSTDLLKLKDFEPYLEILEAYSTKAKNYVNGYCTKYEPWQLIAGSVLCTLLVVWVYELIFQPESLWSRFKNKLFRLIRKMPFIGRKIQQQLTKAKKDLVKNMPFLKLDKDYVKTLPAQGLSTAEVLERLKEYSSMDVFWQEGKASGAVYSGEPKLTELLVQAYGEFTWSNPLHPDIFPGLRKLEAEIVRMTCSLFNGGPDSCGCVTSGGTESILMACKAYRDLALEKGIKTPEIVAPESAHAAFDKAAHYFGMKIVRVAQKKNMEVDVRAMKRAISRNTAMLVCSAPQFPHGVIDPIPEVAKLAVKYKIPFHVDACLGGFLIVFMEKAGYPLEKPFDFRVKGVTSISADTHKYGYAPKGSSVVMYSNEKYRKYQFFVDADWQGGIYASPSIAGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIFILGDPQLSVIALGSNDFDIYRLSNMMSAKGWNFNYLQFPRSIHFCITLVHTRKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQATIDRKMVAEISSVFLDSLYSTDPVTQGNQMNGSPKPR", "text": "FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis (By similarity). Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP (By similarity). Seems to play a role in establishing neuronal contact sites and axonal maintenance (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine- 1-phosphate lyase subfamily."}
{"protein": "LKNIMPELEVRSRRIGGQKYQIPSEVRPERKQSLGLRWLVQFAQKRNEKTMQQKLAKEIIDAASGNGLAVKKREEIHRMAEANKSFAHYRW", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MTKHSGIDPLTQISPNQHVLIRLPSDNLKIVELKANAIVSLGKFGAFRVNEIIGYRFGTTFDIVYDGVEEEFVKGTQTMIGKISVLENRLKASSPALENSSENNRGLINLGSVVQEMSMAEIEAMKREAASGDAIISKMIESHKSFHQKTVHSQEKYLKRKKQKFAKFFTVEYLDSSGLLHYLIEKGDVLRVMDISQESLGMALNLANINSNGQYLCIDETGGLIVYAMLERMFAGDSNSKANGKIVVVHENEHPNLDLLKFSSYSDNFIQRHVKTISVLDFFEPAKEADIKSLFKPLSAEEINDLKSNKKSAYFRRLKWYHNQLSNIEVAASSFDGLLVASTLYLPTLIPRLGEKIHGSRPIVCYSQYKEPLLELSHSLYENLNYLAPSLLETRCRPYQTVRGKLHPLMTMKGGGGYLMWCHRVLPAAEPKLHQETLEKSEIKNSDEEGDEDAHKLDQEKQVIKRRKPNEDNEKL", "text": "FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)- methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TRM6/GCD10 family."}
{"protein": "MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQNLLVEERLAGATLLIFANKQDLPGALSSNAIREALELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFMAD", "text": "FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase- activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle. SUBCELLULAR LOCATION: Nucleus Mitochondrion intermembrane space Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm. Mitochondrion. Note=The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
{"protein": "MDNEKGTSSSDLTTRQRKPLGWKAMPYIIGNETLERLATFGLMANFMVYMVREYHMDQVQAVTLINTWSALTNFAPIIGAFISDSYTGKFNTIVFGSIAELLGMLVLTFTSLVPNLRPPPCTADQITGQCIPYSYSQLYVLLSGLFLLSVGTGGIRSCSVPFSLDQFDDSTEEGREGSRSFFSWYYTTHTIVQLVSMTLVLYVQNNISWGIGFAIPTVLNFFALLLLFVGTRYYVFVKPEGSVFSGVFKVLVAAYKKRKARFTSGIDYHQPLLETDLQSNKLVLTDQFRFLNKAVIVMNNDEAGNEEWRTCTVRQIEDIKSIISIIPIFASSIIGFLAMNQQQTFTVSQALKMDLQFPGTSYLIPPASITVISLLNIGIWLPFYETVLVRHIENITKQNGGISLLQKVGIGNIFSISTMLISGIVERKRRDLSLNGVKMSVFWLTPQQVLMGFYQVFTIVGLTEFFNKQVPINMRSIGNSLLYLGLSLASYLSSAMVSIVHSVTARGGQSWLTDDIDKSKLDCFYYFIAALSTLNFIFFFWCARRYRYRNYSNEQ", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
{"protein": "MGVPSPVRRVCVTVGALVALACMVLAGCTVSPPPAPQSTDTPRSTPPPPRRPTQIIMGIDWIGPGFNPHLLSDLSPVNAAISALVLPSAFRPIPDPNTPTGSRWEMDPTLLVSADVTNNHPFTVTYKIRPEAQWTDNAPIAADDFWYLWQQMVTQPGVVDPAGYHLITSVQSLEGGKQAVVTFAQPYPAWRELFTDILPAHIVKDIPGGFASGLARALPVTGGQFRVENIDPQRDEILIARNDRYWGPPSKPGIILFRRAGAPAALADSVRNGDTQVAQVHGGSAAFAQLSAIPDVRTARIVTPRVMQFTLRANVPKLADTQVRKAILGLLDVDLLAAVGAGTDNTVTLDQAQIRSPSDPGYVPTAPPAMSSAAALGLLEASGFQVDTNTSVSPAPSVPDSTTTSVSTGPPEVIRGRISKDGEQLTLVIGVAANDPTSVAVANTAADQLRDVGIAATVLALDPVTLYHDALNDNRVDAIVGWRQAGGNLATLLASRYGCPALQATTVPAANAPTTAPSAPIGPTPSAAPDTATPPPTAPRRPSDPGALVKAPSNLTGICDRSIQSNIDAALNGTKNINDVITAVEPRLWNMSTVLPILQDTTIVAAGPSVQNVSLSGAVPVGIVGDAGQWVKTGQ", "text": "FUNCTION: May directly or indirectly regulate the accessibility of the key branch point intermediate, monoacyl phosphatidylinositol tetramannoside (AcPIM4), to the elongating alpha-1,6 mannosyltransferases which could regulate the lipoarabinomannans (LAMs) biosynthesis. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
{"protein": "KKIDTRTGKTMEKTEKKIELSLKNMKTAT", "text": "FUNCTION: Has antibacterial activity against strains of L.monocytogenes, L.lactis, B.subtilis, S.typhi, S.aureus, C.perfringens, E.aerogenes and M.luteus but not against E.coli, S.sonnei, S.pneumoniae, S.faecalis, P.aeruginosa, K.pneumoniae or P.vulgaris. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTSDLDTRLDLLRNITSKVGAFALARFGNLSHIVIETKGEADYVSAADRDAESLARRLIHAQFPADAIVGEEQLGDAEVDHWLIDPIDGTANFLSGIPLWAVSIAFVRNKEPVLGAVALPALDTLLWASVDGPLHGTGSVSPLVGAQPIAFGIGRNRTWPLAHRLEVEAAFEARGYHIVCLGSCAAALAMVAAGRLAGYVEHGTHLWDCAAGHVLCRAAGAPSSILFEADGKVAIIAAPQHLRVTAKADARSLSEKHIFDPGSDRISHRMESSAD", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
{"protein": "MLPLPLIANGKGFIRALENDGALAVYAPLEGGYEGRYQRRLRANGYASISLSARGLGDVEAYLMQVHGVRPAHLGKKNIAQEGAVGPIYFAQPIAGYQLENLPAQSKGLVLWILEGYILSQTEIQDLISLTKRVPKLKVVLEMGGDRVFRWQPLLDCLQAA", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I NdhN subunit family."}
{"protein": "MAPSGSGGVRRRCRRVLYWIPVVFISLLLGWSYYAYAIQLCIVSMENIGEQVVCLMAYHLLFAMFVWSYWKTIFTLPMNPSKEFHLSYAEKELLEREPRGEAHQEVLRRAAKDLPIYTRTMSGAIRYCDRCQLIKPDRCHHCSVCDKCILKMDHHCPWVNNCVGFSNYKFFLLFLAYSLLYCLFIAATDLQYFIRFWTNGLPDTQAKFHIMFLFFAAAMFSVSLSSLFGYHCWLVSKNKSTLEAFRNPVFRHGTDKNGFSLGFSKNMRQVFGDEKKYWLLPVFSSQGDGCSFPTCLVNQDPEQPSTPAGLNSTVKNPENHQFPAKPLRESQSHLLKDSQTWTESSANPGKGKAGMSNPALTMENET", "text": "FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes (PubMed:15603741). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). In the nervous system, plays a role in long term synaptic potentiation by palmitoylating AKAP5 through which it regulates protein trafficking from the dendritic recycling endosomes to the plasma membrane and controls both structural and functional plasticity at excitatory synapses (PubMed:25589740). In dendrites, mediates the palmitoylation of DLG4 when synaptic activity decreases and induces synaptic clustering of DLG4 and associated AMPA-type glutamate receptors (PubMed:15603741). Also mediates the de novo and turnover palmitoylation of RGS7BP, a shuttle for Gi/o-specific GTPase- activating proteins/GAPs, promoting its localization to the plasma membrane in response to the activation of G protein-coupled receptors. Through the localization of these GTPase-activating proteins/GAPs, it also probably plays a role in G protein-coupled receptors signaling in neurons (PubMed:21343290). Also probably plays a role in cell adhesion by palmitoylating CD9 and CD151 to regulate their expression and function. Palmitoylates the endoplasmic reticulum protein CKAP4 and regulates its localization to the plasma membrane. Could also palmitoylate LCK and regulate its localization to the plasma membrane (By similarity). SUBCELLULAR LOCATION: Postsynaptic density Postsynaptic recycling endosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Note=Translocates to postsynaptic density when synaptic activity decreases. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MNYLIMFSLALLLVIGVESGRDGYIVDSKNCVYHCYPPCDGLCKKNGAKSGSCGFLVPSGLACWCNDLPENVPIKDPSDDCHKR", "text": "FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin seems to specifically act on Nav1.6/SCN8A sodium channel (PubMed:31668811). In vitro, it inhibits the proliferation of the prostate cancer cell line DU145 (IC(50)=15 uM). It shows low effect on the adhesion of DU145 cells to fibronectin (at 15 uM) and is inactive on DU145 cells migration (PubMed:31668811). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MERAAPSRRVPLPLLLLGGLALLAAGVDADVLLEACCADGHRMATHQKDCSLPYATESKECRMVQEQCCHSQLEELHCATGISLANEQDRCATPHGDNASLEATFVKRCCHCCLLGRAAQAQGQSCEYSLMVGYQCGQVFQACCVKSQETGDLDVGGLQETDKIIEVEEEQEDPYLNDRCRGGGPCKQQCRDTGDEVVCSCFVGYQLLSDGVSCEDVNECITGSHSCRLGESCINTVGSFRCQRDSSCGTGYELTEDNSCKDIDECESGIHNCLPDFICQNTLGSFRCRPKLQCKSGFIQDALGNCIDINECLSISAPCPIGHTCINTEGSYTCQKNVPNCGRGYHLNEEGTRCVDVDECAPPAEPCGKGHRCVNSPGSFRCECKTGYYFDGISRMCVDVNECQRYPGRLCGHKCENTLGSYLCSCSVGFRLSVDGRSCEDINECSSSPCSQECANVYGSYQCYCRRGYQLSDVDGVTCEDIDECALPTGGHICSYRCINIPGSFQCSCPSSGYRLAPNGRNCQDIDECVTGIHNCSINETCFNIQGGFRCLAFECPENYRRSAATLQQEKTDTVRCIKSCRPNDVTCVFDPVHTISHTVISLPTFREFTRPEEIIFLRAITPPHPASQANIIFDITEGNLRDSFDIIKRYMDGMTVGVVRQVRPIVGPFHAVLKLEMNYVVGGVVSHRNVVNVHIFVSEYWF", "text": "FUNCTION: Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the fibulin family."}
{"protein": "WKPFKKIEKAVRRVRDGVAKAGPAVAVVGQAT", "text": "FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Has also activity against fungi. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cecropin family."}
{"protein": "MFNFNDKIVFDDKKYDVLTVGEMLVDMISTDYGDDFECDTYKKYFGGSPANIAINSKMLGINSIIVSSVGNDGLGKFLLKKLQEHHIEIKYVRQVDYSTSMVLVTKSKSSPTPIFYRDADYHIEYSDELKYLIENTKIVHFSSWPISRNPSRSTVEILIDECKKYDVLVCYDPNYHSMIWERGHDGREYIKSLIAKVDIIKPSEDDAERIFGKDTPENQLKKFLDLGAKLVILTLGKDGAIVSNGEETIRFNTLADEVVDTTGAGDAFWSGFYSGLIKGYTLKKSLELGFAVSAYKLRYVGAIVDLPDIDTIKSMYDLKKLR", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-fructose 6- phosphate to fructose 1,6-bisphosphate. Together with the adjacently encoded sucrose 6'-phosphate phosphorylase, may be involved in a new pathway for the degradation of sucrose. Cannot phosphorylate D- fructose. SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
{"protein": "INWKKIASIGKEVLKAL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MCD family. Mastoparan subfamily."}
{"protein": "MERRNPSERGVPAGFSGHASVESGCETQESPATVVFRPPGDNTDGGAAAAAGGSQAAAAGAEPMEPESRPGPSGMNVVQVAELYPELRRILTITEDGQGLKGVKRERGACEATEEARNLAFSLMTRHRPECITFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNSRVRHNVASDCGCFMLVKSVAVIKHNMVCGNCEDRASQMLTCSDGNCHLLKTIHVASHSRKAWPVFEHNILTRCSLHLGNRRGVFLPYQCNLSHTKILLEPESMSKVNLNGVFDMTMKIWKVLRYDETRTRCRPCECGGKHIRNQPVMLDVTEELRPDHLVLACTRAEFGSSDEDTD", "text": "FUNCTION: Plays a major role to prevent cellular inhibition of viral genome replication. Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in cooperation with viral E4orf6. This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM. Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest. E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain. E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function. SUBCELLULAR LOCATION: Host nucleus Host cytoplasm Note=Colocalizes with host TP53 to host PML nuclear bodies. PML localization of E1B-55K is necessary for E1B- 55K-dependent SUMOylation of TP53. SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family."}
{"protein": "MRLSYLSLALAIIFVLTIMHASNVEAKASADPEPDAVGSINVKNLMDMIREQITSRLKK", "text": "FUNCTION: May have antimicrobial properties, like most ant linear peptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily."}
{"protein": "MPKGKNLHVKIGDNVKIISGFDKNKTGEVTKIYRNTGKILVKGINFKFKHIKPNTESDVGEIKQFEAPIHHSNVKLI", "text": "FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
{"protein": "MESGNIVNAQPELSGIIDGSKSYMYEQLWKLCAGPLCDIPKLGEKIYYFPQGNIELVEASTREELNELKPICDLPSKLQCRVIAIQLKVENNSDETYAEITLMPDTTQVVIPTQNENQFRPLVNSFTKVLTASDTSGGFFVPKKHAIECLPPLDMSQPLPTQELLATDLHGNQWRFNHNYRGTPQRHLLTTGWNAFTTSKKLVAGDVIVFVRGETGELRVGIRRAGHQQGNIPSSIISIESMRHGVIASAKHAFDNQCMFIVVYKPRSSQFIVSYDKFLDAVNNKFNVGSRFTMRFEGDDFSERRYFGTIIGVSDFSPHWKCSEWRNLEVQWDEFASFSRPNKVSPWEIEHLMPALNVPRPSLLKNKRLREVNEIGSSSSHLLPPILTQGQEIGQLSVASPMNISLTYRDTTEDVMNPSRLLMSYPVQPMPKLNYNNQMVTQIEENITTKTGTNFRLFGVSLVTPSVIKDPIEEIGSEISKLTEGKKFGQSQTLRSPTEIQSKQFSSTRTCTKVQMQGVTIERAVDLSVLNGYDQLILELEELFDLKGQLQTRNQWEIAFTDSDDDKMLVGDDPWPEFCNMVKKILIFKRGGQKLEVQ", "text": "FUNCTION: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARF family."}
{"protein": "MHRAPSPTAEQPPGGGDSARRTLQPRLKPSARAMALPRTLGELQLYRVLQRANLLSYYETFIQQGGDDVQQLCEAGEEEFLEIMALVGMATKPLHVRRLQKALREWATNPGLFSQPVPAVPVSSIPLFKISETAGTRKGSMSNGHGSPGEKAGSARSFSPKSPLELGEKLSPLPGGPGAGDPRIWPGRSTPESDVGAGGEEEAGSPPFSPPAGGGVPEGTGAGGLAAGGTGGGPDRLEPEMVRMVVESVERIFRSFPRGDAGEVTSLLKLNKKLARSVGHIFEMDDNDSQKEEEIRKYSIIYGRFDSKRREGKQLSLHELTINEAAAQFCMRDNTLLLRRVELFSLSRQVARESTYLSSLKGSRLHPEELGGPPLKKLKQEVGEQSHPEIQQPPPGPESYVPPYRPSLEEDSASLSGESLDGHLQAVGSCPRLTPPPADLPLALPAHGLWSRHILQQTLMDEGLRLARLVSHDRVGRLSPCVPAKPPLAEFEEGLLDRCPAPGPHPALVEGRRSSVKVEAEASRQ", "text": "FUNCTION: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Isoform 2 is not localized to the nucleus. SIMILARITY: Belongs to the NAB family."}
{"protein": "MSHELLRQPKWRVIDQSHFGPLFDAKQSFAIDDALCTAVGAGQSDAVVRTWVHENTVVLGAADTKLPYIDEAISFLRQEGYRVVVRNSGGLAVVLDSGVLNISLIFPETKNTIAIEQGYEAMYALMAAMLASYGARVEAGEIVGSYCPGSYDLSIGGKKFAGISQRRVRGGVAVQIYLCVNGSGAARAELIRRFYELGRQGEKTKFAYPDVVPTVMASLSELLGCELSIDELLVALWRTLQSFGGELYSSALENGEWNWYEQYWARIVERNETALKGELLAGE", "text": "FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes. SIMILARITY: Belongs to the octanoyltransferase LipL family."}
{"protein": "MHPDLSPHLHTEECNVLINLLKECHKNHNILKFFGHCNDLDREMRKCLKNEYSERRTRSREHGAAMRRRLSDPPEEAGR", "text": "FUNCTION: May be involved in cytochrome c oxidase biogenesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the CMC family."}
{"protein": "MSSRVLTPDVVGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVDLDDQLYQEPQAAPVAVPMGKFAMYPDWQPDADFIRLAALWGVALREPVTTEELASFIAYWQAEGKVFHHVQWQQKLARSLQIGRASNGGLPKRDVNTVSEPDSQIPPGFRG", "text": "FUNCTION: This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N' (By similarity). FUNCTION: This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'. SIMILARITY: Belongs to the DnaT family. SIMILARITY: Belongs to the DnaT family."}
{"protein": "MSVCLAITKGIAVSSIGLYSGLLASASLITSTTPLEVLTGSLTPTLTTLKNAATALGAFASTFFCVSFFGAPPSLRHPYLLYGMLVAPLSSFVLGCASNYQSRKYSKVSKESSLFPEDSKLAASELSDSIIDLGEDNHASENTPRDGKPAATTVSKPAEALHTGPPIHTKNLIAATAIAIVGFVQAVIGVYGEGQFI", "text": "FUNCTION: Involved in the selective degradation of mitochondria via autophagy during starvation and at post-log phase. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATG33 family."}
{"protein": "MGNWVVNEGISIFVILVWLGMNVFLFVWYYRVYDIPDKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRIRRQLDRNLTFHKMVAWMIALHTAIHTIAHLFNVEWCVNARVNNSDPYSIALSDIGDKPNETYLNFVRQRIKNPEGGLYVAVTRLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAQRIVRGQTAESLLKHQPRNCYQNISQWGKIENCPIPEFSGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPVVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFKACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNKAPNLRLKKIYFYWLCRDTHAFEWFADLLQLLETQMQEKNNTDFLSYNICLTGWDESQASHFAMHHDEEKDVITGLKQKTLYGRPNWDNEFKTIGSQHPNTRIGVFLCGPEALADTLNKQCISNSDSGPRGVHFIFNKENF", "text": "FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=As unassembled monomer may localize to the endoplasmic reticulum."}
{"protein": "MTHEEHHEAKTLGIGKAIAVLTSGGDAQGMNATVRAVVRVGIFTGLRVFFVHEGYQGLVDGGEHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLNDLQKDGKITAEERTKSSYLNIVFLVGSIDNDFCGTDMTIGTDSALHRIVEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNTAVRLPLMECVQVTKDVTKAMDEKRFDEAIKLRGRSFMNNWEVYKLLAHVRPPVSKGGLHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKNLEQISANITKYNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSIGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQVNVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGNPTPFDRNFATKMGAKATNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHISRKRSGEAAV", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily."}
{"protein": "MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSQEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTAHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREACGSSSYVASIVDGGESRSEKGDSSRY", "text": "FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKAGMFYCASQASTATANGERTVTARAIDRHNPIIKDGRRSFTAPCSSGDDYVAPYRQLSKITRVPSSSGDGKSVQVDKGRRSNSGSLMKLISYDVSLARKSFGCVVATPKTPPGSTRYLLGSDPVSLAGSTGQDTVATEESEASAPKRGSSGPVEEKKKSSGSGSDQVVVLRVSLHCHCRGCQGKVKKHLSKMQGVTSFNIDFASKKVTVTGDITPLEVLGCLSKVKNAQFWTPPPPSIPRANPET", "text": "FUNCTION: Heavy metal-associated protein involved in salt tolerance. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAQYALEAGVSWLATSVSVVASGTWQFAKWTHKYVMQQAEELEADEPEESYFQQMVDKEKEFHNYVRQQIICMWLFMLLYLFAYWLISRLKRKTEREALYAGEEDYFVYRVSVWISSTATATSIGSLTLLPFSVIGVELLQLYDGNYYLQWLSYSLIGALWNYVFVLSNVSLFVLLPFSYFFIESQGFSTSKIGNDMTQRIYEAMAISFLFAFVLLCLAEVVLTILDYPVSFLSITSVNLPLIYSCVSFIGAVLLLISTPYGFAKMFSLARDFLVTEETADIEEENSEQSEDVTEPKNSSSDETIHQVDRSDTPHLEDVVNDITENVDADGEFRKDSDSGIESGSTEEMRLNTDDEEMGINDSDDKSAFGDDGDLGNSTPTKNKKKRRKHDYAATTPIVRKWDKDVPKKPKNPNFDYRNLKEYVKEARRQRSSLSESDDYWFGSPPRSSFSANYYSSRFSRWKHNSETGLNPSSSLLVDPFASGDFHEASSSEASSTPLSPARRTKSEEAIWKPVLHTVKSSKLYKRAIEKQGRLVKLFMSLRFPVAAAALLVLTTCSLIMVATNTLKLLFGYRSLPVYAQYIEVHTRHSFGLFGACIETLLIIYVMITSFVGLYSLPVLRSLRPVRKDTPMPTIIINSSIVLVVASALPVAVNTVGMTTFDLLGSHSSLQWLGSFRVVVAYNTLFVVLSVAFLFNQLTASMRRQIWKWICQLRCGIRRESDADETIEILRGDKKSN", "text": "SIMILARITY: Belongs to the LIMR family."}
{"protein": "MDAENGEGQVQVHLKTKQEHYAVPDVPYAIDGTMTTVELNTFLNALLRNKSGDESAIDFDFLVFDEYLRGRLCDHLKEKAISFEDAIEIEYVERFPAPQPQDCLLHDDWVSAVKVSGKWILTGCYDNTLNIWTHKGKHILTIPGHTAPIKAVDWISLDNDIGRFVSSSQDQTVMLWQWNVDSNAVECVSICKGHERGVDSISVSPDATRFATGSWDTMLKVWSAAEDDAGGDAASSKRPKENGVRTPIMTLQGHRESISAVQWIDTSTLLTTSWDHTMKIWDLSLEGIKTEISTNKSIFDASYSNLNRLIVTASADKNLRLYDPRTNQGSIVRNTYLGHNAWVQTVMWSTTEEFLFVSGAYDNQNKLWDCRSPKAPLYDLLGHGEKVLDIDWSNPKYICSGGADNTVRVFKSRKAGVETMDDK", "text": "FUNCTION: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family."}
{"protein": "MAASSLEQKLSRLEAKLKQENREARRRIDLNLDISPQRPRPTLQLPLANDGGSRSPSSESSPQHPTPPARPRHMLGLPSTLFTPRSMESIEIDQKLQEIMKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTESPRTSGVLSQPHLPFFR", "text": "FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by pro-inflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (PubMed:28111074). SUBCELLULAR LOCATION: Nucleus. Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily."}
{"protein": "MSFVCGISGELTEDPVVSQVSGHIFDRRLIVKFIAENGTDPISHGELSEDQLVSLKSGGTGSAPRNVSGTSIPSLLKMLQDEWDTVMLNSFSLRQQLQIARQELSHSLYQHDAACRVISRLSKELTAAREALSTLKPHTSAKVDDDVSIDESEDQQGLSEAILAKLEEKSKSLTAERKQRGKNLPEGLAKTEELAELKQTASHTGIHSTGTPGITALDIKGNLSLTGGIDKTVVLYDYEKEQVMQTFKGHNKKINAVVLHPDNITAISASADSHIRVWSATDSSSKAIIDVHQAPVTDISLNASGDYILSASDDSYWAFSDIRSGKSLCKVSVEPGSQIAVHSIEFHPDGLIFGTGAADAVVKIWDLKNQTVAAAFPGHTAAVRSIAFSENGYYLATGSEDGEVKLWDLRKLKNLKTFANEEKQPINSLSFDMTGTFLGIGGQKVQVLHVKSWSEVVSLSDHSGPVTGVRFGENARSLVTCSLDKSLRVFSF", "text": "FUNCTION: Probable ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Core component of the NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity (By similarity). Together with emb-4, necessary for interaction of rnp-4, a probable exon junction complex component, with mRNAs and spliceosomal snRNAs. Plays a role in nuclear retention of unspliced mRNAs. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat PRP19 family."}
{"protein": "MATPHINAQMGDFADVVLMPGDPLRAKYIAENFLDNAVQVCDVRNMFGYTGTYKGRKISVMGHGMGIPSCSIYVTELIKDYGVKKIIRVGSCGAVNEGIKVRDVVIGMGACTDSKVNRIRFKDHDFAAIADYKMVKAAEEAAKARGIDVKVGNLFSAELFYTPDPSMFDVMDKYGIVGVEMEAAGIYGVAAEYGAKALAICTVSDHIKTGEQTTSEERQNTFNEMIEIALDSVLIGDQAGY", "text": "FUNCTION: Catalyzes the reversible phosphorolytic breakdown of the N- glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1- phosphate. SIMILARITY: Belongs to the PNP/UDP phosphorylase family."}
{"protein": "MAVSADYQVKFPESGDLYSILAAEGIEFLLSHSGEVPLEYIHGKTICLFFSAIWCRPCKDFTPELIKLYENLQNRGEELEIIFVSFDHDMTSFYEHFWCMPWLAVPFNLSLLNKLRDKYGISRIPSLVPLYSDEISVAEDVIGLIEDYGSEAFPFTKKRKEELKAIDDSKRLGGQLEKLLTHESRNYVVARNGSKVLVSKLVGKTIGLYFGAHWCPPFRSFTSQLVDVYNELATTDKGSFEVILISTDRDSREFNINMTNMPWLAIPYEDRTRQDLCRIFNVKLIPALVIIGPEEKTVTTNAREMVSLYGSRSFPFTESRIVELKACLKKEGDSLPRKVKDNKHEHELKLDMAKAYVCDFCKKQGRFWAFSCNACDYDLHPTCVEEEEALLV", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions. SIMILARITY: Belongs to the nucleoredoxin family."}
{"protein": "MNVLITGGAGFLGLQLARLLLQRGTLNLDGQPVAIKRLTLLDVVAPQGLDDARVRVVTGDLSDPAVLRQAIDTDTGAVFHLAAVVSGQAEADFDLGMRVNLDASRALLETCRELGHQPRVLFTSSVAVYGGQLPPVVQDDTALNPQSSYGVQKAIGELLLSDYSRRGFVDGRVLRLPTISVRPGKPNAAASSFASGIIREPLSGVAANCPVAPETPLWLLSPRAAVAALVNGIELAGERLGNRRVVNLPGLSVTAAGMIEALRRVAGNAVADRVTWEREARVENIVGTWPAAWNAERALALGFQSDASFDEVIRAYMEDAGLAK", "text": "FUNCTION: Catalyzes oxidation of D-erythronate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+). SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MTLRSCETFLRRSLRFSTALNLTAFPEHEQLYLRVSSGCSVFRPQTVRKCLFHWTPACTVSQGVFLDRLQKGAAVTDESLCNQPVSVSPDRAQQFSLLMKDPDQPENAKSLKVAIVGSPNAGKSTLTNQLLGRKLFAVSSKVHTTRSRAVGVLTENDTQIVLLDTPGLTTQIKAKRHQLENSLLVDPFKSLKEADLVVVLVDVSDKWTRSKLSYEVLKCLALNPDVPAVLVLNKVDLLKNKALLLDITAQLTEGMVNGKKIRIHGASKPVRKAAAGANSRLKEKKAAGSLEDEADHEDKLKALKSHGGWPHFKDVFMLSSIDHEDVETLKRYLFVAAKPCQWQYHSEVLTDQSPEDVCFNTIREKLLQNLPKEVPYTMTQEIEVWKESEDGVLDISIKLYVQKETHMKMVIGPGGQLITRINQEAGNDLMKIFLCNVRLKISVKLRK", "text": "FUNCTION: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small subunit assembly (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix Mitochondrion inner membrane; Peripheral membrane protein Note=Localizes on the matrix side on the mitochondrial inner membrane. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family."}
{"protein": "MIPPTSAQVTAEQNVLQTFFSHLGNFSYDKAKDHVEKEKEGNKSAGASWSLMLAALAHLAAAQKAYHSMSFLGQKQGGQLFFSRKDSIRTNYTSLYNELKKVVTTGRNAVGGTAPHLEELLSHLSEQLCYFVQAHMEIADFYEKMYTLSSQKFINAEELVKILEAILKKYSSRFHHPTLSPLESGFQLEVDVLAHLLKAQFLIYEWKFLPALVNLHNAHTKLQTWGQIFEKQKETKKHLFGGQSQKVAQPPHLFLWLMKFKNLLLAKFSFYFHEALSRQTSEMKTLTAKTNPDYFGKISSFIRKYDAVNVSLIYDTRGSENFQGHGYHHPDSYREAPKGMDQYPAVVSLPNDRPIMHWPNVIMIMTDKSADLNTLEKVVHFYDDKVQSTYFLTRPEPNFTIVVIFESKKSERDSHFTSFLNELSQSLKGSRAFASLKPGSKV", "text": "FUNCTION: As part of the KICSTOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. SUBCELLULAR LOCATION: Lysosome membrane. SIMILARITY: Belongs to the KICS2 family."}
{"protein": "MMVHCAGCERPILDRFLLNVLDRAWHIKCVQCCECKTNLSEKCFSREGKLYCKNDFFRRFGTKCAGCAQGISPSDLVRKARSKVFHLNCFTCMVCNKQLSTGEELYVIDENKFVCKDDYLSSSSLKEGSLNSVSSCTDRSLSPDLQDPLQDDPKETDNSTSSDKETANNENEEQNSGTKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLGGRLDESEMLGSTPYTYYGDYQSDYYAPGGNYDFFAHGPPSQAQSPADSSFLAASGPGSTPLGALEPPLAGPHGADNPRFTDMISHPDTPSPEPGLPGALHPMPGEVFSGGPSPPFPMSGTSGYSGPLSHPNPELNEAAVW", "text": "FUNCTION: Plays an essential role in the regulation of neuronal differentiation and migration during development of the central nervous system. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MASTSCFLHHHALTAAARSSSSPRQAALPKSPQLLVCRAQKQQPAQEEEGGVVSRRLALTVLIGAAALGSKVSPADAAYGEAANVFGKPKSNTDYLPYSGDGFKLSIPSKWNPSKEREFPGQVLRYEDNFDSNSNLSVIINPTDKKSIKDFGSPEEFLSKVDYLLGKQAYFGKTASEGGFDPDAVATANILEATASNVNGKDYYFVSVLTRTADGDEGGKHQLITATVNDGKLYICKAQAGDKRWFKGARKFVEGAASSFSVA", "text": "FUNCTION: May be involved in the regulation of photosystem II. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane. Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the psbP family."}
{"protein": "MSRELHDVDLAEVKPLVEKGESITGLLQEFDVQEQDIETLHGSLHVTLCGTPKGNRPVILTYHDIGMNHKTCYNPLFNSEDMQEITQHFAVCHVDAPGQQDGAPSFPVGYMYPSMDQLAEMLPGVLHQFGLKSVIGMGTGAGAYILTRFALNNPEMVEGLVLMNVNPCAEGWMDWAASKISGWTQALPDMVVSHLFGKEEIHNNVEVVHTYRQHILNDMNPSNLHLFISAYNSRRDLEIERPMPGTHTVTLQCPALLVVGDNSPAVDAVVECNSKLDPTKTTLLKMADCGGLPQISQPAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLEGTRSRSHTSEGPRSRSHTSEGSRSRSHTSEDARLNITPNSGATGNNAGPKSMEVSC", "text": "FUNCTION: Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy (By similarity). Has a role in cell trafficking notably of the Schwann cell and is necessary for the maintenance and development of the peripheral nerve myelin sheath. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cell membrane Note=Mainly cytoplasmic but differentially localized to other regions. Associates with the plasma membrane in intestinal epithelia and lactating mammary gland. Translocated to the nucleus in a p53/TP53-dependent manner. In prostate epithelium and placental chorion, located in both the cytoplasm and in the nucleus. No nuclear localization in colon epithelium cells. In intestinal mucosa, prostate and renal cortex, located predominantly adjacent to adherens junctions. Cytoplasmic with granular staining in proximal tubular cells of the kidney and salivary gland ducts. Recruits to the membrane of recycling/sorting and late endosomes via binding to phosphatidylinositol 4-phosphate. Associates with microtubules. Colocalizes with TUBG1 in the centrosome. Cytoplasmic location increased with hypoxia. Phosphorylated form found associated with centromeres during S-phase of mitosis and with the plasma membrane (By similarity). SIMILARITY: Belongs to the NDRG family."}
{"protein": "MAQHHLWILLLCLQTWPEAAGKDSEIFTVNGILGESVTFPVNIQEPRQVKIIAWTSKTSVAYVTPGDSETAPVVTVTHRNYYERIHALGPNYNLVISDLRMEDAGDYKADINTQADPYTTTKRYNLQIYRRLGKPKITQSLMASVNSTCNVTLTCSVEKEEKNVTYNWSPLGEEGNVLQIFQTPEDQELTYTCTAQNPVSNNSDSISARQLCADIAMGFRTHHTGLLSVLAMFFLLVLILSSVFLFRLFKRRQGRIFPEGSCLNTFTKNPYAASKKTIYTYIMASRNTQPAESRIYDEILQSKVLPSKEEPVNTVYSEVQFADKMGKASTQDSKPPGTSSYEIVI", "text": "FUNCTION: Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (By similarity). Increases proliferative responses of activated T-cells and SH2D1A/SAP does not seem be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A-dependent pathway. May serve as a marker for hematopoietic progenitor cells (PubMed:11564780, PubMed:12115647, PubMed:12928397, PubMed:12962726, PubMed:16037392) Required for a prolonged T-cell:B-cell contact, optimal T follicular helper function, and germinal center formation. In germinal centers involved in maintaining B-cell tolerance and in preventing autoimmunity (By similarity). In mast cells negatively regulates high affinity immunoglobulin epsilon receptor signaling; independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1 (PubMed:22068234). In macrophages enhances LPS-induced MAPK phosphorylation and NF-kappaB activation and modulates LPS-induced cytokine secretion; involving ITSM 2 (By similarity). Positively regulates macroautophagy in primary dendritic cells via stabilization of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8 (PubMed:29434592). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MMLGVYTLLLLWGLATPCLGLLETVGTLARIDKDELGKAIQNSLVGGPILQNVLGTVTSVNQGLLGAGGLLGGGGLLSYGGIFSLVEELSGLKIEELTLPKVSLKLLPGVGVQLNLHTKVSLHGSGPLVGLLQLAAEVNVSSKVALGMSPRGTPILVLKRCSTLLGHISLMSGLLPTPIFGLVEQTLCKVLPGLLCPVVDSVLSVVNELLGATLSLVPLGPLGSVEFTLATLPLISNQYIELDINPIVKSIAGDVIDFPKPRIPVKVPPKEDHTSQVTVPLYLFSTVFGLLQTNGALDLDITPEMVPRNVPLTTTDLAALAPEALGKLPPAQHLLLSLRVTKSPMVLLQNKKATVSIPVTIHVLSSVPQGTPVALFQLNGVMTLNAHLAPSSTKLHISLSLERLSVQLASSFPQPFDASRLEEWLSDVVRAAYMQRLNEHLEVGIPLPKILNVNFANSVVDIIENAVVLTVAP", "text": "FUNCTION: May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family."}
{"protein": "MSLQKHGLLFNNNKFSDCKLVLDDGNVQVTLNVHKCLLYMNSLYFQAMFDNFKEQEYSEIKIRVQNSQIATDVIKSFYEKSNVINADWQYQLDYAIETKFFGVEYVLDKNIIVPYIYFDLFVDKIELIGYNNTTLNMILNNLPLDYDLDKFPTDFLEGLLVSSTEYDIFLSNKHCFYVWSVTDNKFTYSKEIPLELYYSYLDNDKIYKFTEHNSLICFNKKTDRHKSILLYDNDKIIKFDTEGVIYYLPENNQIILSHVERTTTGCDYKISLFCLETKQLIRTFHSRNYFGNEIILQISVSHDKIIVFGDDVQVKNFSSGVCLFTINQNESGVCIACDPEWSYFAIGSEDYDTEDQKITIYDLSNGNKVKTLNHRDSIRDILWTSKYIIAHNNENIYFYETNNYELVKKLDYKNNGLIKKIDCFDDSEFLYVLTNNSKMFQINMDSLENTDSNNISTEICFTQIGRFCDFKTIKNSNYHKSKLIKKTLEQRRRMDKN", "text": "SIMILARITY: Belongs to the mimivirus BTB/WD family."}
{"protein": "MSLLSLPWLGLRPVATSPWLLLLLVVGSWLLARILAWTYAFYNNCRRLQCFPQPPKRNWFWGHLGLITPTEEGLKNSTQMSATYSQGFTVWLGPIIPFIVLCHPDTIRSITNASAAIAPKDNLFIRFLKPWLGEGILLSGGDKWSRHRRMLTPAFHFNILKSYITIFNKSANIMLDKWQHLASEGSSRLDMFEHISLMTLDSLQKCIFSFDSHCQERPSEYIATILELSALVEKRSQHILQHMDFLYYLSHDGRRFHRACRLVHDFTDAVIRERRRTLPTQGIDDFFKDKAKSKTLDFIDVLLLSKDEDGKALSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRDPKEIEWDDLAQLPFLTMCVKESLRLHPPAPFISRCCTQDIVLPDGRVIPKGITCLIDIIGVHHNPTVWPDPEVYDPFRFDPENSKGRSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALMLLHFRFLPDHTEPRRKLELIMRAEGGLWLRVEPLNVSLQ", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of endogenous polyunsaturated fatty acids (PUFAs). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon hydrogen bonds, with preference for omega-2 position. Metabolizes (5Z,8Z,11Z,14Z)- eicosatetraenoic acid (arachidonate) toward 18-hydroxy arachidonate (PubMed:11162607). Catalyzes the epoxidation of double bonds of PUFAs such as docosapentaenoic and docosahexaenoic acids (PubMed:16112640). Has low omega-hydroxylase activity toward leukotriene B4 and arachidonate (PubMed:11162645). Involved in the metabolism of xenobiotics. Catalyzes the hydroxylation of the antihistamine drug ebastine (PubMed:11162645). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane Microsome membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MMKTMRIAAIPGDGIGKEVLPEGIRVLQAAAERWGFALSFEQMEWASCEYYSHHGKMMPDDWHEQLSRFDAIYFGAVGWPDTVPDHISLWGSLLKFRREFDQYVNLRPVRLFPGVPCPLAGKQPGDIDFYVVRENTEGEYSSLGGRVNEGTEHEVVIQESVFTRRGVDRILRYAFELAQSRPRKTLTSATKSNGLAISMPYWDERVEAMAENYPEIRWDKQHIDILCARFVMQPERFDVVVASNLFGDILSDLGPACTGTIGIAPSANLNPERTFPSLFEPVHGSAPDIYGKNIANPIATIWAGAMMLDFLGNGDERFQQAHNGILAAIEEVIAHGPKTPDMKGNATTPQVADAICKIILR", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family."}
{"protein": "MPSSFDLLGEMIGLLQTEQLTSSWACPLPNALTKRQDLWRALINQRPALPLSKDYLNLEDAYLDDWRASFVPVSVKDCQKTNYTSLFLYHGDIRYLAVDAIVNAANSELLGCFSPNHGCIDNAIHTFAGSRLRLACQAIMTEQGRKEAIGQAKLTSAYHLPASYIIHTVGPRITKGHHVSPIRADLLARCYRSSLDLAVKAGLTSLAFCSISTGEFGFPKKEAAQIAIKTVLKWQAEHPESKTLTTIFNTFTSEDKALYDTYLQKENNCE", "text": "FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl- cysteine bonds (By similarity). Specifically reverses the SirTM- mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress."}
{"protein": "MSDSNDDRPFRPFQSQYRWPGVDLLAYKEEGSAPFRSVTRQVLFSGNGLTGELRYFEVGPGGHSTLERHQHAHGVMILKGRGHAMVGRAVSAVAPYDLVTIPGWSWHQFRAPADEALGFLCMVNAERDKPQLPTEADLAMLRADDAVAAFLDGLAG", "text": "FUNCTION: Catalyzes the formation of S-(methylsulfanyl)glutathione and 1-deoxy-D-xylulose 5-phosphate (DXP) from 1-methylthioxylulose 5- phosphate (MTXu-5P) (PubMed:23042035, PubMed:23035785). The S- (methylsulfanyl)glutathione is reductively cleaved to relase methanethiol in a second reaction. Involved in the MTA-isoprenoid shunt of the methionine salvage pathway (PubMed:23042035)."}
{"protein": "MENGLWEVLGSKGLLKKHEFIRILVQCLYSLGFKNSASCLEFESKILYKTADSEFLEKQVLSGNWDSCVQVLDRIFDNSMDDTRNTALYLVFKQCLLEYLKRGDVSLALNVLRKQAPLLRMGKEKIHRLACDIVYSKEMESGEVDNCLVLDLRRKLLVELEKLIPLPIVIPERRLEHLVETAVMDQIDTCMYHNSCDAVSLYKDHCCGRDQIPSETVQILVAHKNEVWFVQFSNSGKYLATASSDCTAIIWKVLDDNKVELKHTLESHQNPVSFVSWSPDDTKLLTCGNAEVLKLWDVDTGVLRHTFGNNNTGFTVSSCAWFPDSTRLVCGSSDPERGIVMWDTDGNEIKAWRGTRIPKVVDLAVTPDGESMITVFSDKEIRILNLETKVERVISEEQPITSLSISGDGKFFIVNLSCQEIHLWDLAGEWKQPLKFSGHRQSKYVIRSCFGGLDSSFIASGSEDSQVYIWNLKNTKPLEVLSGHSMTVNCVSWNPKNPRMLASASDDQTIRIWGPGKPNKPLN", "text": "SUBCELLULAR LOCATION: Cytoplasm Note=Associates predominantly in the form of large cytoplasmic complexes."}
{"protein": "MRFISASSLLLALAPTLNAVPVEVAGSAQGLDVTLSQVGNTRIKAVVKNTGSEDVTFVHLNFFKDAAPVQKVSLFRNGMLPNLNLATTEVQFQGIKQRLITEGLSDDALTTLAPGATIEDEFDIASTSDLSEGGTITINSNGLVPITTDNKVTGYIPFTSNELSIDVDAAEAASVTQAVKILERRTKVTSCSGSRLSALQTALRNTVSLARAAATAAQSGSSSRFQEYFKTTSSSTRSTVAARLNAVANEAASTSSGSTTYYCSDVYGYCSSNVLAYTLPSYNIIANCDLYYSYLPALTSTCHAQDQATTTLHEFTHAPGVYSPGTDDLGYGYSAATALSASQALLNADTYALFANGTYSSLLSFVNPLLTPDNSCQPQLLDARTCNRQFGRSTSCKVYWKAVE", "text": "FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M35 family."}
{"protein": "MGPRSRQRRTGTVQSTNDSSSLSKRSLAAQGYVSDAFAPLLVPGIVRRTPLIHRGYYVRARAVRHCVRAFLDLTGAIRSPTRAQILSLGSGSDSLYFRLKAAGLLTRTAVWEVDFPDVSRLKAKRIEETPELCAQTGPFKIGDSASTLCFESSDYRILGADLRELQRLGEALDSAGLDATSPTLILAEAVLTYLEPSRAAALIAWVAQRFPNALFVIYEQMKPGDAFGQIMLQHFRRLNSPLHGLELFPDVEAQRQRFLQAGWTTCSALDLNEFYRRLIPADERRRVETLEPFDEFEEWHLKCSHYFILAASRGDILSETPVFLPSEASFQIDPALPSGFLSASVVTSDHQHSSLQRYGHTSVLLSPGIIFSAGGFGEQEGRHCRVSRFHLLSRSCDSEWKGCQISTLGTEGQWDGRLYHTMTRLSDTRVLVLGGRLSPVNPASGALQLDIYKSEDNCPEGQNVVVTKAALEEGSMLSCWRHSTTEVYYQNQRYLFVYGGRSVTDPVLSDCRFLHVETMAWVRIPVQGSSPEGRHSHSACSWQGGALIAGGLGASEEPLSSVFFLRPVSSGFLWESIHIQPSITPRYSHTAHVFNGKLLLVGGVWIHSSSVPGVTVISLTTGLSSEYQIDTASVPWPLMLHNHSSALLPEEQQLLLIGGGGNCFSFGTYFNPHTVGLDLSSLGLGQ", "text": "FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity). May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues. SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family."}
{"protein": "MKLVLVVLAFIALVSSVSCTQTGGCSCGQQQSHEQQHHPQQHHPQKQQHQPPPQHHQQQQHQQQQVHMQPQKHQQQQEVHVQQQQQQPQHQQQQQQQQHQQQHQCEGQQQHHQQSQGHVQQHEQSHEQHQGQSHEQQHQQQFQGHDKQQQPQQPQQYQQGQEKSQQQQCHCQEQQQTTRCSYNYYSSSSNLKNCHEFLRQQCSPLVMPFLQSRLIQPSSCQVLQQQCCHDLRQIEPQYIHQAIYNMVQSIIQEEQQQQPCELCGSQQATQSAVAILTAAQYLPSMCGLYHSYYQNNPCSSNDISGVCN", "text": "FUNCTION: Zeins are major seed storage proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the gliadin/glutenin family."}
{"protein": "MNHSIKKTYLVFTMLLGFILLAGCNGDNNNDNSNNDNNGVLLTSIAVTPATPSMPLGLKQQFTAMGTYSDGTSSDITNSATWSSDDSTVATINGSGLAMGVIPGSVAITASLIDSSSNEQSATTTLTITDATLTALAITPVNPSLAKGLTKQFMATGTYSDGTSPDVTTSVTWSSANTLVATVNASGLASGVAIGSSIITASLGSDETTTELNITDAILSSIALTPVEPSIAKGITQQFTAIGTYSDGISVDITASSNWSSADTLVATMNTSGAAKGVSIGSSIITADFQAQSATSLLTVTDASLTSIMLTPANPHIPKGNTLQLTATGIYSDGISVDITSSAIWSSADTLIATVNADGVVSGITSGSAIITATSAALSATTTVTVTDTTLTSIAVTPGNQTIVKGSNKQLTATGTYSDGSLANITASVTWSSADTLVATVNNSGLASGIETGSSLISASSGALSGSTNLTITGAALNSIVVSPTNLSLVKGMNKQFAATATYSDGSVADISTSVTWSSADTLVATIDVNGLANGKAAGSSLITATSGAQSNSTNLTVTDATLNSIDVTPINPSIIKNSSQNFVATGHYSDGSTTNITSTVMWSSADTLVATLNPNEQLNSGRATAIEVGSSVIQASLSGVFADTTLNVTAALPNNPLAPELGEVARFAMLASQAITTTSGSAIVDGDLGILDQARSYYAGFTPGVNAGEFDELTNGLSYAGDDSTPPYVVPVPYASMVAFINQSRTDLGIAYNFLAADPNPNAATQVCPIELGNLTLTRGVYKTAADVTLQTGTLTLDGEGDPDSVFIFTIGGNLTSGAPGGDIVLINGAQAKNIYWRTAGKTVIGTNTNFSGNVFAWSEVNVRTGANVTGRLFAVTDQVTLDANAVTKAN", "text": "FUNCTION: Ice-binding adhesion protein that adsorbs this bacterium onto ice to maintain a favorable position in its aquatic habitat. Inhibits growth of the ice crystals. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point. The TH activity of this protein is approximately 1.4 degrees Celsius at 25 uM and little below 2 degrees Celsius at 80 uM. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Extracellular side. SIMILARITY: Belongs to the ice-binding protein family."}
{"protein": "MLWMLARAVAFRRPGRGLAGGRGLWTGRPQSDCDSMKPLEGVRILDLTRVLAGPFATMNLGDLGAEVIKVERPGAGDDTRSWGPPFVNTESTYFLSVNRNKKSIAVNIKDPRGVRIVKELAAICDVFVENYVPGKLSEMGLGYEDIDKIAPHIIYCSITGYGQTGPMSHRAGYDAIASAMSGLMHITGPEDGDPVRPGVAMTDLATGLFAYGAIMAGLLQRYRTGKGLFIDCNLLSSQVACLTQVAANYLIGQKEAKRWGTAHGSIVPYQAFKTKDGYLVIGAGNNQQFAVVCKILNLPELIDDCKYRTNHLRVQNRKELVKILSARFAEEVTAKWLCLFEGSGIPYGPINSLKDVFSEAQVLHNGLVMEMNHPTVGKISVPGPAVRYSKFKMSEAKPPPLLGQHTRHILKEVLRYDEGAIEKLLCSGVIEQHETK", "text": "FUNCTION: Catalyzes the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors, the preferred ones are glutarate, succinate, adipate, and 3- hydroxymethylglutarate (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the CoA-transferase III family."}
{"protein": "MKNNCTSLKSSIDEEDELKTDHEIDLEKGLLPEYDSKEEGALPLYSDHARLSNSPNTHRENNPSRSTDNSSPLLIKLLISFTSIILFNAPAVCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWTKAVKVTVIFLAQCVKACGKGIKHFLKKWENMPMAFSEVFLFNIFGGALRIISRHFFGKRWGLKCSLADHIIFAILSILVFIAETVKPGSIRVNLIRKMGHEAKQQVNEYTAIPLHEMNPESEA", "text": "FUNCTION: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons (By similarity). Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity). SUBCELLULAR LOCATION: Spore membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WTF family."}
{"protein": "MASIAIENAEPVPSDCKGDLKISKFDGDLPLKVLYCGVCSLPTEYCEYMPDVAKCRQWLEKNFPDEFSKLTLGISPKQETGTVEGQATSGEEEEKKKQKRGGRGQIKQKKKTVPQKVTIAKIPRAKKKYVTRVCGLATFEIELKDAQRFFAQKFSCGASVTGEDEIIIQGDFTDDIIDVIQEKWPEVDDDSIEDLGEVKK", "text": "FUNCTION: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits (By similarity). SIMILARITY: Belongs to the DENR family."}
{"protein": "MSPVASTCLLCEMRTVVWGWQPAVPQPWHFVRFASSARLARRKPARMALSPNVARSSDRFKDSKKKKPPPTFKNNPFGGMNQTRARLPDRPIPRSDAELKRSSSDLNNKEKDAADKKQDGSLFRALKMQIALSPIPYSRRNRIKEKIAAVTSFDQFPLLPQVREAVYANAFPTLTEISPTPIQRVAIPALLRPPISETEKNKRKKKPQEEEEEELFHFDQFLLAAETGTGKTLAYLLPIINWIKQAEMVEKDTELMDNGEKQQGVTEKSKENLFELEAPELATPEHSNVARPRAIILVPTAELVEQVGKLAKQLSHTAKFRSATISSVYTPRRITNSLFNPAGIDILISTPHLLTSIAKTNPYILSRVAHLVIDEADSLLDKSFSPLTYSIMEKTAPSLTQLILCSATIPRSLDSVMEKKFPEMKRLVTPNLHAIPRRVQLGVVDVDKDPSRGNKKLACADIIWSLGKAGEVAAFLSQKGIHTAALSRDTPDQRKDEILAEFTHVKPLPTPQEVKDAQRNKRNWFSDPVPFATGENSHLGPQRNLRDTKVLVTTDLGSRGIDTVAVRNVILFDVPHTTIDFIHRLGRTGRMGRRGRGIVLVSKKDRKDVVKEVREAMFRGQALI", "text": "FUNCTION: ATP-binding RNA helicase involved in mitochondrial RNA metabolism. Required for maintenance of mitochondrial DNA (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the DEAD box helicase family. MRH4 subfamily."}
{"protein": "MNSSTALMCFALLLISPLCLGYSDEDREADSRRIAEIIQNAQDDDSKINSTQELLDIYRRLYPTLSLEDRENIDKFVNEHTDAIVIDGVPIQGGRKAKIIGKIVSPAAKGLAVGFFEELGSKIAQLFTG", "text": "FUNCTION: A humoral factor that plays a role in stress tolerance; gives increased resistance to the lethal effects of bacterial challenge and stress. Regulated by the JAK/STAT pathway and NF-KB-like Relish pathway in the fat body, upd3 in the hemocytes and Mekk1 in response to septic injury and consequent immune response (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted from the fat body into the hemolymph. SIMILARITY: Belongs to the Turandot family."}
{"protein": "MSGRPRTSSFAEGNKQSPSLVLGGVKTCSRDGSKITTVVATPGQGTDRVQEVSYTDTKVIGNGSFGVVFQAKLCDTGELVAIKKVLQDRRFKNRELQIMRKLEHCNIVKLLYFFYSSGEKRDEVFLNLVLEYIPETVYKVARQYAKTKQTIPINFIRLYMYQLFRSLAYIHSLGICHRDIKPQNLLLDPETAVLKLCDFGSAKQLLHGEPNVSYICSRYYRAPELIFGAINYTTKIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEVIKVLGTPTREQIREMNPNYTEFKFPQIKSHPWQKVFRIRTPTEAINLVSLLLEYTPSARITPLKACAHPFFDELRMEGNHTLPNGRDMPPLFNFTEHELSIQPSLVPQLLPKHLQNASGPGGNRPSAGGAASIAASGSTSVSSTGSGASVEGSAQPQSQGTAAAAGSGSGGATAGTGGASAGGPGSGNNSSSGGASGAPSAVAAGGANAAVAGGAGGGGGAGAATAAATATGAIGATNAGGANVTDS", "text": "FUNCTION: Required for several developmental events such as syncytial blastoderm formation and embryonic segmentation. Is involved in transcriptional regulation. Required for arm phosphorylation. Wg signaling operates by inactivating the sgg repression of en autoactivation. Negatively controls the neuromuscular junction (NMJ) growth in presynaptic motoneurons. Plays a role in the regulation of microtubule dynamics and actin cytoskeleton during embryogenesis. Required for phosphorylation of sra in activated eggs. Essential for completion of meiosis, possibly by triggering calcineurin activation via sra phosphorylation. Phosphorylates microtubule-associated protein futsch in axons. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cell cortex. Synapse. Cell projection, axon. Note=In syncytial embryos, detected at the centrosomes throughout the cell cycle, and in the mitotic spindle and pseudocleavage furrows invaginating from the cell cortex during mitosis. Concentrated at the growing end of membranes during the cellularization process. After cellularization, localized to the centrosomes during mitosis and to the nucleus at the end of telophase. Enriched in the presynaptic side of the neuromuscular junction, with some signal detected also in axonal branches. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily."}
{"protein": "MSKGLFLIWLISSFHLISFSTSSKDTSFVFNGFGQSNLALDGSATLLPNGLLQLAKDSQHQMGHAFIKKPIDFSSSKPLSFSTHFVCALVPKPGFEGGHGITFVISPTVDFTRAQPTRYMGIFNASTNGSPSSHLFAVELDTVRNPDFRETNNNHIGIDVNNPISVESAPASYFSKTAQKNVSINLSSGKPIQVWVDYHGNVLNVSVAPLEAEKPSLPLLSRSMNLSEIFSRRRLFVGFAAATGTSISYHYLLGWSFSTNRELSQLLDFSKLPQVPRPRAEHKKVQFALIIALPVILAIVVMAVLAGVYYHRKKKYAEVSEPWEKKYGTHRFSYKSLYIATKGFHKDRFLGRGGFGEVYRGDLPLNKTVAVKRVSHDGEQGMKQFVAEVVSMKSLKHRNLVPLLGYCRRKGELLLVSEYMPNGSLDQHLFDDQSPVLSWSQRFVILKGIASALFYLHTEAEQVVLHRDIKASNVMLDAELNGRLGDFGMARFHDHGGNAATTAAVGTVGYMAPELITMGASTITDVYAFGVFLLEVACGRKPVEFGVQVEKRFLIKWVCECWKKDSLLDAKDPRLGEEFVPEEVELVMKLGLLCTNIVPESRPAMGQVVLYLSGNLPLPDFSPYTLGIGSFTPVVVDAASLTVSFTSRNWSAPSASSSSANNSKDHEQPLEFKS", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: In the N-terminal section; belongs to the leguminous lectin family. SIMILARITY: In the C-terminal section; belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MNTNRGRYPPGVGTGRGAPPNPDYHQSYRQQQPPQDQQYVQRGYSQNPQQMQLQQQHQQQQQQQQWSRRPQLPGNASNANEVVQQTTQPEASSDANGQDWKATLRLPPPDTRYQTADVTATKGNEFEDYFLKRDLLKGIYEKGFEKPSPIQEESIPIALTGSDILARAKNGTGKTGAFCIPVLEKIDPNNNVIQAMILVPTRELALQTSQVCKELSKYLNIQVMVTTGGTSLRDDIMRLHQPVHLLVGTPGRILDLTKKGVCVLKDCAMLVMDEADKLLSAEFQPSLEELIQFLPQNRQFLMFSATFPVTVKAFKDRHLRKPYVINLMDQLTLMGVTQYYAFVEERQKVHCLNTLFSKLQINQSIIFCNSVNRVELLAKKITELGYSCFYIHAKMVQDHRNRVFHEFRNGACRNLVCTDLFTRGIDIQAVNVVINFDFPRTSESYLHRVGRSGRFGHLGLAVNLVTYEDRFKMYQTEQELGTEIKPIPSNIDQAIYCQ", "text": "FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. SUBCELLULAR LOCATION: Cytoplasm, P-body Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily."}
{"protein": "MFNKINQIFNFHQQALNLCSQRQEILSANIANADTPGYKSIDFNFKNELNKTLYKNKKTIFLKKTSPNHLNEKHKNLFLLKTIPVLTNQIKQDGNTVNMDRERIEFLNNSIKYQSSLVFIKNEIKNMMYVLKG", "text": "FUNCTION: Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body (By similarity). SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the flagella basal body rod proteins family."}
{"protein": "MNNKEFNMEQFKKLAAVVSEDELDEMLDENVTGAASSIPCAKVVVKVTTVVVAATTGFDWCPTGACTTSCRF", "text": "FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) that is probably active on Gram-positive bacteria, since its analog [Del1]Flvbeta.e shows antibacterial activity against Gram-positive bacteria (PubMed:27028884). This activity is not synergistically enhanced by [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded by the same operon than Flvbeta.e (PubMed:27028884). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MENGDIPEDANEHCPGPQSESAGKSDSCAGCPNQEACATAPKGPDPDLVAIAERMSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVEDNLGVMSIGFMLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLLPTGIDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVENMSGLSQPLKDVKFMKLATETGSSINVTEDVIACLRKNAPELLDIVACSEVFDSSGGGAERMCREMGVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVVPSTVMTE", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. Functions as Fe-S scaffold, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Essential for embryo development. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily."}
{"protein": "MEHFDASLSTYFRAWLGPRDTRVEGWFLLDNYVPTLVCSILYLLIVWLGPKYMKTRQPFSCRGILVVYNLGLTLLSLYMFCELVTGVWEGQYNFFCQGTRSGGEADMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHASMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSSIPSMRPYLWWKKYITQGQLLQFVLTIIQTSCGVIWPCTFPLGWLYFQIGYMISLITLFTNFYIQTYNKKGVSRRREHQKDHQNGSVAAVNGHISSFSSLENNVKPRKQRKD", "text": "FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (By similarity). In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell projection, dendrite Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily."}
{"protein": "MVPTEATSLILNPSDDYGYDGTPPMEYDTNLTDYFCEKSHVRQFAGHFLPPLYWLVFIVGAVGNSLVILVYWYCTRVKTMTDMFLLNLAIADLLFLTTLPFWAIAAADQWKFQTFMCKVVNSMYKMNFYSCVLLIMCISVDRYIAIAQAMRAQMWRQKRLLYSKMVCFTIWVMAAALCLPELLYSQVKEEHGTAICTVVYSSNESTKLKSAVLTLKVTLGFFLPFVVMACCYAIIIHTLIRAKKSSKHKALKVTITVLTVFVLSQFPHNCVLLVQTIDAYATFISSCALSIKIDICFQVTQTVAFFHSCLNPVLYVFVGERFRRDLVKTLKNLGCISQAQWVSFTRREGSLKLSSMLLETTSGALSF", "text": "FUNCTION: Receptor for chemokine SCYA25/TECK. Subsequently transduces a signal by increasing the intracellular calcium ions level (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSTKKVYSFLSQAFIFSAIMLVSNIIATHLPIPMPSSVIGLVILFSLLCLKVIKLEQVESLGTALTGIIGFLFVPSGISVINSLGVMGQYFVQILTVIVVATIILLAVTGLFAQFILGKDDKEIEDTKELKVVNKGRKHGKVA", "text": "FUNCTION: Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgB, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CidA/LrgA family. LrgA subfamily."}
{"protein": "MAVDNNKAKQAYDNQTGVNEKEQEQRQEQQNQQPEFTNKLSFSDEVIEKIAGIAAREVSGILEMKGGFVDNISSSFGSNNNVSQGVSVEVGEKQAAVDLKVVLEYGESAPKIFRKVTDLVKEQVKYITGLDVVEVNMRVEDVMTKKEWSQKNEKSQSSNNEDKGLQ", "text": "FUNCTION: May play a key role in alkaline pH tolerance. SIMILARITY: Belongs to the asp23 family."}
{"protein": "MKAVIILGLVLLSVTVQGKIFERCELARTLKRLGLDGYRGISLANWVCLAKWESGYNTQATNYNPGDQSTDYGIFQINSHYWCNNGKTPGAVNACHISCNALLQDNIADAVTCAKRVVRDPQGIRAWVAWRNHCQNRDVSQYVQGCGV", "text": "FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. SIMILARITY: Belongs to the glycosyl hydrolase 22 family."}
{"protein": "MKLSKLLQLAVFSSLVTSKNIFDLESLKQGLQDEETVNNDKREPVNLLYLDRFKMGVSDEAKGNAKFKRDPKNVIDPASLKEGSAEEEQKDKREPKNLFNLQALHEGLKDEETKSKREAKNLPNLEALEEALKGGSLPKKDAKNLIDLVALKQSLEKEAAKRDAKNIPDLEALKTGIEEEEGQVAKRDAKNVINLSNFIETPSKREGKNLFDLTKFQQSGQPIKKRDQKILKQEKSLFVLNSVDCFNNLLQSILPQLSSISIFSSYIRQFASIDARTANPQKVMLIVAPDNDSLETKLSDLKPWEFPEQITPEQSEQEQDKTLKNNLLHFLNGHLINNFEENLVIDKSSTDAVTIISKLNNGKFLKIKQDQLSQKFSIRLLDSENWIDVETIKQVENGFVLIINDSLVKP", "text": "SUBCELLULAR LOCATION: Vacuole."}
{"protein": "MAFALLRPVGAHVLYPDVRLLSEDEENRSESDASDQSFGCCEGPEAARRGPGPGGGRRAGGGGGAGPVVVVRQRQAANARERDRTQSVNTAFTALRTLIPTEPVDRKLSKIETVRLASSYIAHLANVLLLGDSADDGQPCFRAAGSAKGAVPAAADGGRQPRSICTFCLSNQRKGGGRRDLGGSCLKVRGVAPLRGPRR", "text": "FUNCTION: Early transcription factor that plays a key role in somitogenesis, paraxial mesoderm development and regulation of stem cell pluripotency. Essential for the mesenchymal to epithelial transition associated with somite formation. Required for somite morphogenesis, thereby regulating patterning of the axial skeleton and skeletal muscles. Required for proper localization of somite epithelium markers during the mesenchymal to epithelial transition. Also plays a key role in regulation of stem cell pluripotency. Promotes pluripotency exit of embryonic stem cells (ESCs) by priming ESCs for differentiation. Acts as a key regulator of self-renewal of hematopoietic stem cells (HSCs) by mediating HSCs quiescence and long- term self-renewal. Together with MEOX2, regulates transcription in heart endothelial cells to regulate fatty acid transport across heart endothelial cells. Acts by forming a heterodimer with another helix- loop-helix (bHLH) protein, such as TCF3/E12, that binds DNA on E-box motifs (5'-CANNTG-3') and activates transcription of target genes. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKNTFILGIEGTAWNLSAAIVTETEIIAEVTETYKPTAGGIHPREAAQHHAKYAASVIKRLLAEAKEKGVKPSDIDGIAFSQGPGLGPCLRTVATAARMLSISLGIPLIGVNHCIAHIEIGIWRTPAMDPVVLYVSGANSQVISYMGGRYRVFGETLDIGLGNALDKFARGANLPHPGGPKIEAYAKNATKYIHLPYVIKGMDLSFSGLSTAASEALKKAPLEDVCYSYQETAFAMVVEVAERALAHTGKKEVLLAGGVGANTRLREMLNDMCEARGAKFYVPEKRFMGDNGTMIAYTGLLMYKSGNTLSLEDSRVNPSYRTDDVKVTWIQEEKMKRVPEISPGTSLKLGELLDNGAEAIVYLEEGPEGKKILVKERVPKAYRYKEIDERIRTERNRTEARLMSESRRHGVSTPIIYDVEDFKLKMQYIDGVPIKYLVTPELSEKVGELVGKLHSAGIVHGDLTTSNILLAGERLYLLDFGLAYYDKGLEARGVDVHVLFQTFESTHRNHEALIEAFKKGYRRTFIDSEDVLTRVEEIKKRARYA", "text": "FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily. SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD family."}
{"protein": "MMWIQKNPFLGLLLCSFLAFFQSTYAEVGKLVCFYDAQSFVREGPAQMSLAELEPALQFCNFLVYGYAGIDAVTYKIKSLDPSLTNDRQHYRHITALRKKYPHVRFLLSVGGDRDVNSEGVADSDKYLRLLEQSEHRKSFQASVLAELNNNGFDGIDLAWQFPKNRPKLQQGVFKRVWGSLRGWFSSSSVDEKSEEHREQFATLLEELQSDLRRGGQLLTVSMLPHVSAELFIDVPKVLSNVDFVNLGTYDFQTPERDPKVADLPTPLYAMYDRDPSHNVQYQVQYWMNQTSEISVHKLHVGVTSYGRAWNMTRNSGITGYPPIPAANGAAPPGRQTVTPGLLSWPEICDLLQQQPQDREVPHLRKVGDPTKRFGIYAYRAADDQGENGLWVGYEDPLTAAIKAGFVHAQGLGGVAFHDLSMDDFRGQCAGEKFPILRSIKFKL", "text": "FUNCTION: Probably required to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted in hemolymph. It is probably transported to target tissues via hemolymph. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. IDGF subfamily."}
{"protein": "MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTANEEEFLRTYAGVVNSQLSQLPQHSIDQGAEDVVMAFSRSETEDRRQ", "text": "FUNCTION: Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CTNNBIP1 family."}
{"protein": "MVINKVEICGVNTSKLPVLKEKEMRELLISMRNGNTTAREKFIKGNLRLVLSVIQRFNNRGENADDLFQVGCIGLIKSIDNFDLSQNVKFSTYAVPMIIGEIRRYLRDNNSIRVSRSLRDIAYRALQVRDRLISKNNKEPTVSQIAKELKIPREEVIFALDAIQDPISLFEPIYHDDGDAIYVMDQISDNKNLDDSWLQNISIKEAMKKLSDREKMILNMRFFDGRTQMEVADEIGISQAQVSRLEKTALKHMKKYV", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes. SIMILARITY: Belongs to the sigma-70 factor family."}
{"protein": "MVAHSSEGLSATAPVTGGDVLVDARASLEEKEAPRDVNANTKQATTEEPRIQLPTVDAFRRAIPAHCFERDLVKSIRYLVQDFAALTILYFALPAFEYFGLFGYLVWNIFMGVFGFALFVVGHDCLHGSFSDNQNLNDFIGHIAFSPLFSPYFPWQKSHKLHHAFTNHIDKDHGHVWIQDKDWEAMPSWKRWFNPIPFSGWLKWFPVYTLFGFCDGSHFWPYSSLFVRNSERVQCVISGICCCVCAYIALTIAGSYSNWFWYYWVPLSFFGLMLVIVTYLQHVDDVAEVYEADEWSFVRGQTQTIDRYYGLGLDTTMHHITDGHVAHHFFNKIPHYHLIEATEGVKKVLEPLSDTQYGYKSQVNYDFFARFLWFNYKLDYLVHKTAGIMQFRTTLEEKAKAK", "text": "FUNCTION: Omega-3 fatty acid desaturase that recognizes a range of 18- and 20-carbon omega-6 substrates. Introduces a double bond in the fatty acid chain three carbons away from terminal methyl group to biosynthesize n-3 (omega-3) polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Acts on a number of substrates like linoleoyl-CoA ((9Z,12Z)-octadecadienoyl-CoA, 18:2n-6), dihomo- gamma-linolenoyl-CoA ((8Z,11Z,14Z)-eicosatrienoyl-CoA, 20:3n-6), and arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA, 20:4n-6), to generate alpha-linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA, 18:3n-3), (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA (20:4n-3) and (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA (20:5n-3) respectively (PubMed:9037020, PubMed:11972048, PubMed:14765186, PubMed:22041902, PubMed:24391980, PubMed:26806391). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
{"protein": "MSTLSNFTQTLEDVFRRIFITYMDNWRQNTTAEQEALQAKVDAENFYYVILYLMVMIGMFSFIIVAILVSTVKSKRREHSNDPYHQYIVEDWQEKYKSQILNLEESKATIHENIGAAGFKMSP", "text": "FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with HCN1 and HCN2 and increase potassium current. Interacts with KCNQ1; forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (PubMed:11101505). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Apical cell membrane; Single-pass membrane protein Note=Colocalizes with KCNB1 at the plasma membrane. SIMILARITY: Belongs to the potassium channel KCNE family."}
{"protein": "MSEHVYNLVKKHHSVRKFKNKPLSEDVVKKLVEAGQSASTSSFLQAYSIIGIDDEKIKENLREVSGQPYVVENGYLFVFVIDYYRHHLVDQHAETDMENAYGSTEGLLVGAIDAALVAENIAVTAEDMGYGIVFLGSLRNDVERVREILDLPDYVFPVFGMAVGEPADDENGAAKPRLPFDHVFHHNKYHADKETQYAQMADYDQTISEYYDQRTNGNRKETWSQQIEMFLGNKARLDMLEQLQKSGLIQR", "text": "FUNCTION: Reduces FMN, organic nitro compounds and disulfide DTNB. Involved in maintenance of the cellular redox state and the disulfide stress response. FUNCTION: Reduces FMN, organic nitro compounds and disulfide DTNB. Involved in maintenance of the cellular redox state and the disulfide stress response (By similarity). SIMILARITY: Belongs to the flavin oxidoreductase frp family."}
{"protein": "MIFSTLEHILTHISFSIVSIVITIHLITFLVDEIVKLYDSSEKGIIVTFFCITGLLVTRWISSGHFPLSDLYESLIFLSWSFSLIHIIPYFKNNVLILSKITGPSAIFTQGFATSGILTEIHQSGILVPALQSEWLIMHVSMMILGYAALLCGSLLSVALLVITFRKNRKLFYKSNGFVNESFLLGENVLENTSFSAKNYYRSQLIQQLDYWSYRVISLGFTFLTIGILSGAVWANEAWGSYWNWDPKETWAFITWIVFAIYLHTRTNINLRGANSAIIATIGFLIIWICYFGVNLLGIGLHSYGSFTSTFN", "text": "FUNCTION: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family."}
{"protein": "MSDLGAVISLLLWGRQLFALYSGNDVTDISDDRFPKPPEIANGYVEHLFRYQCKNYYRLRTEGDGVYTLNDKKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYHQVDIGLIKLKQKVLVNERVMPICLPSKNYAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEGSTCPKWKAPKSPVGVQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDLEEDTWYAAGILSFDKSCAVAEYGVYVKVTSIQHWVQKTIAEN", "text": "FUNCTION: Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF-1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribute to the clearance of cell-free hemoglobin to allow hepatic recycling of heme iron. SUBCELLULAR LOCATION: Secreted Note=Secreted into blood plasma and associated with subtypes of high density lipoproteins (HDL). SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MVLSQRQRDELNRAIADYLRSNGYEAAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVEDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR", "text": "FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in the PAF inactivation (PubMed:10542206). Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (PubMed:10542206). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing (By similarity). Required for pronuclear migration during fertilization. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Nucleus membrane Note=Localizes to the plus end of microtubules and to the centrosome. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes (By similarity). May localize to the nuclear membrane. SIMILARITY: Belongs to the WD repeat LIS1/nudF family."}
{"protein": "MADYWKSQPKKFCDYCKCWIADNRPSVEFHERGKNHKENVAKRISEIKQKSLDKAKEEEKASKEFAAMEAAALKAYQEDLKRLGLESEILEPSITPVTSTIPPTSTSNQQKEKKEKKKRKKDPSKGRWVEGITSEGYHYYYDLISGASQWEKPEGFQGDLKKTAVKTVWVEGLSEDGFTYYYNTETGESRWEKPDDFIPHTSDLPSSKVNENSLGTLDESKSSDSHSDSDGEQEAEEGGVSTETEKPKIKFKEKNKNSDGGSDPETQKEKSIQKQNSLGSNEEKSKTLKKSNPYGEWQEIKQEVESHEEVDLELPSTENEYVSTSEADGGGEPKVVFKEKTVTSLGVMADGVAPVFKKRRTENGKSRNLRQRGDDQ", "text": "FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome (PubMed:9724750, PubMed:19592703, PubMed:28781166). May play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex (PubMed:9724750). SUBCELLULAR LOCATION: Nucleus Nucleus speckle."}
{"protein": "MSLFGTTSGFGTSGTSMFGSTTTDNHNPMKDIEVTSSPDDSIGCLSFSPPTLPGNFLIAGSWANDVRCWEVQDSGQTIPKAQQMHTGPVLDVCWSDDGSKVFTASCDKTAKMWDLNSNQAIQIAQHDAPVKTIHWIKAPNYSCVMTGSWDKTLKFWDTRSSNPMMVLQLPERCYCADVIYPMAVVATAERGLIVYQLENQPSEFRRIESPLKHQHRCVAIFKDKQNKPTGFALGSIEGRVAIHYINPPNPAKDNFTFKCHRSNGTNTSAPQDIYAVNGIAFHPVHGTLATVGSDGRFSFWDKDARTKLKTSEQLDQPISACCFNHNGNIFAYASSYDWSKGHEFYNPQKKNYIFLRNAAEELKPRNKK", "text": "FUNCTION: Plays a role in mitotic bipolar spindle formation. Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, spindle pole Note=Recruited from interphase nuclei to spindle MTs during mitosis. SIMILARITY: Belongs to the WD repeat rae1 family."}
{"protein": "KASSSAPKGWTHHGSRFTFHRGSM", "text": "FUNCTION: Able to depolarize frog skeletal muscle fibers, but has no effects on squid giant axons. Tetrodotoxin is able to partially antagonize the depolarization. Induces myonecrosis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the true venom lectin family."}
{"protein": "MATRNPPPQEYESDDDSYEVLDLTEYARRHHWWNRVFGHSSGPMVEKYSVATQIVMGGVSGWCAGFLFQKVGKLAATAVGGGFLLLQIASHSGYVQIDWKRVEKDVNKAKRQIKKRANKAAPEINNIIEEATEFVKQNIVISSGFVGGFLLGLAS", "text": "FUNCTION: Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FUN14 family."}
{"protein": "MKFSGIQVSILALLRVCLAEADSGEGNQEALPHANFDITYECLERDVGGLSSFMEFENGDNATLQYKFTNKEDLNVSVVGLGGRIYDVQKNEDAANISASAIGPLDVDVNGTTEFQHVIKLVLKEGDYVLSPDVYVQKENETMRVVTNPSLIRILPPPMSFFNPKFMLVQMVLGALIAAFSYFTFFKPSASYGRDAKKLKPDGSVSRMDSSWLPENHQKKK", "text": "FUNCTION: Is probably involved in a pathway contributing to genomic integrity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the IRC22 family."}
{"protein": "MTINPDDDNIEILTGAAGGADTEGEGEGEGKSLTDLVEQPAKVMRIGTMIKQLLEEVRAAPLDDASRNRLREIHQTSIRELEDGLAPELREELERLTLPFTDDNVPSDAELRIAQAQLVGWLEGLFHGIQTALFAQQMAARAQLEQMRQGALPPGIQVPGAQRGGATHPGTGQYL", "text": "FUNCTION: Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif) (PubMed:25469515). Interaction of Bpa with the proteasome stimulates proteasomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity). SIMILARITY: Belongs to the Bpa family."}
{"protein": "MKIKTGVGILALSALTTMMISAPALAKIEEGKLVIWINGDKGYNGLAEVGKKFEQDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLVPNPPKTWEEIPALDKELKVKGKSAIMFNLQEPYFTWPLIAADGGYAFKFENGKYDVKDVGVDNAGAKAGLTFLIDMIKNKNMSADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSKVNYGVTLLPTFKGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDQGLEAVNKDKPLGAVALKSFQEQLAKDPRIAATMDNAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALKDAQSRITK", "text": "FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
{"protein": "MRGPGVGSGFSGERGLLEQEAGADTEAVELLPFLVLGARADLQAAAAQHVLALTGAGSGRTLLAGQPELLRALVDLAVAPAPAPSRDASRALVNLAADPNVHWQLLAADPELPARLLRCVLDPQWPWAEEAAAVLANLSREPAPCAALMEKLMAAEPERLGLERLVNALCTPSYNAAAPLHYLGPLLSNLSQQAEVRAFLLDPDRCVVQRLLPLTQYTDSSVRRGGVVGTLRNCCFEHRHHKWLLGAQVDILPFLLLPLAGPEEFSEEEMDQLPVDLQYLSPDKQREPDADIRKMLIEAVMLLTATAPGRKQVRDQGAYLILRELHSWEPEPDVRMACEKLIQVLIGDEPEAGMENLLEVQVPEDVEQQLQELDQQEQQELAQELRGNGAPHT", "text": "SIMILARITY: Belongs to the HGH1 family."}
{"protein": "MKAYLALISAAVIGLAACSQEPAAPAAEATPAAEAPASEAPAAEAAPADAAEAPAAGNCAATVESNDNMQFNTKDIQVSKACKEFTITLKHTGTQPKASMGHNLVIAKAEDMDGVFKDGVGAADTDYVKPDDARVVAHTKLIGGGEESSLTLDPAKLADGDYKFACTFPGHGALMNGKVTLVD", "text": "SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
{"protein": "MHLGVEEPIRECQYNQICTHNSSPMDTPHIKKKKNKRKWQVFPGRNRFYCNGRIMMAKQTGVFYLTMVLILVTSGLFFAFDCPFLASNLTPAIPAIGGVLFVFVMGMLLRASFSDPGVLPRATPEEAADIERQIDANNGPSGPGYRPPPRTREVLINGQTVKLKYCFTCKIFRPPRASHCSLCDNCVDRFDHHCPWVGNCVGRRNYRFFYLFILSLSFLTIFIFAFVITHVILNALRKALALSTAADFEAVQKDPTGLAFLVLSKTALLDILEVVVCFFSVWSIVGLSGFHTYLISSNQTTNEDIKGSWSSKRGKGNYNPYSYGNFITNCCSALCGPLPPSLIDRRGFIQPDTPQPATQTNGTSACPPNQVQSHMCAQDQCIQSTKFVLQAATNPLLHSQPVILGGGPPLQAKTSLGGPCSTMGPPQPSLPSSIPGLSCGGELMALRDSEIHCHHHLHHQHFISPEETPSPPAPLPCATHLGHHVHPAQLFDPVSQDSLHEDSVRGLVKLSSV", "text": "FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily."}
{"protein": "MMDKRVVAVAAVLWNVQMLFAAGEVIVPEGYASYYAESFNGRPTASGEIFDMNAYTAAHRTLPFGTVVELTNLDNGKKVIVRINDRGPYAANREIDVSKAAAVALDMLNAGVARVSIHKADPNAHASQQRNDRQTSPGVLPQDSFGVPPTAPTSSAPVMYADPHNPPPAPVGRRAGTPGVPGVANTTDVPASEYGAPPVAYAAPGSTPSRVPYGTAVPGSAAPNSHAQPVPSSSSYAAAAPLPYAAGGGKVSGMKSVYTPTHSGETRGVLWRIQLGAFVREENALRLVVKCARRALILHMSEQSTRCAWCCRGYAPRT", "text": "FUNCTION: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. SIMILARITY: Belongs to the RlpA family."}
{"protein": "MDDDGDGSSSPTDDSAAAGLLPLFSRSPAEDLEEKLRRAMEENARLTRALDAILAGHHAHQRALLAPSLSPPPPSATARAPSVSTSCAAREDAAPAVAAAAASTACPSRQQPPTAEPRPKVRTVRVRADAADATDANSMAETVKDGYQWRKYGQKVTRDNPYPRAYFRCAFAPSCPVKKKLQRCAEDRSMLVATYEGEHNHALSTQTTEFVASGCTTSQHAGGSSSSPLPCSISINSSGRTITLDLTNQAGSGSIASCGVEAAAVSGELVTVLSPELRRHLVEEVVQVLKNDAEFVEAVTNAVAARVVDQIPHIPVHL", "text": "FUNCTION: Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Regulates, probably indirectly, the activation of defense-related genes during defense response (By similarity). Regulates negatively basal innate immunity and XA21-mediated defense against X.oryzae pv. oryzae (Xoo) (By similarity). FUNCTION: Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Regulates, probably indirectly, the activation of defense-related genes during defense response (By similarity). Regulates negatively basal innate immunity and XA21-mediated defense against X.oryzae pv. oryzae (Xoo) (PubMed:19825552, PubMed:21961049). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group II-a family."}
{"protein": "MKIIILLGFLGATLSAPLIPQRLMSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPLTGEASFAQGAQAGQVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMVLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPAISGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLQKEAINFRHDSAGVFMPSTSPKPSTTNVFTSAVDQTITPELPEEKDKTDSLREP", "text": "FUNCTION: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface. SUBCELLULAR LOCATION: Secreted Cytoplasm Nucleus. SIMILARITY: Belongs to the ODAM family."}
{"protein": "MYDAYTPCEVALRLPVEVTCLAFQESNQTLLAGGRAGHLYAYTISANRRGFELTNICKSFHKKAVMELKVCQREDLLLCVSDGQLMAHKLSDPEYKVETLIHKVKPVQTFARFSPKTSGDLYVIVSSRKKLYLFKWGEKDGHKEFIEVALDYNPVFLDTPTSIRCVGEMVFFSVRNEYFSMTMQKDKTTTSPSEGSTPEGWNGFVTRLLNFNCQPGIVPMIDRRRVAFVRNEIVVTTDIWGQRPANVLSDEYKFSEVPMQIVYDSPYLVGMLSKGRVEVRSIFDGQLVQTMSLPKAMTLCSGARGQVFVAALSDIWILDTSQNLRKNVSHLIQERHFELAIQLAENSNLFAEEQKLEIKKKAALNLFNQKKFDESFALFGEIKTDISEVLSIIRMFPELLPDGFQSMTGVVSDMPANDRMRALLALGSYLSEIRTEHAKHIELYNRLYSSGAAKKTDEDEKAKLLLTLRVVDTTLLKCYIKTKPMLVDSLIRLQSNACTFEDAKKILESEGRLRSLFILYETRKKHEMALDLFIDQSSRPDADPFFDDAIQQIVEYLQSLGNSNLPLILKYAKWVLAKNLEAGVQIFTSDETEMARNLNRKAVVEFLKSECPDALIPYLEHVIFKWEEPSSYFHETLLEFYVARVNTLFKDYVHAFPDAFSDENITRAGDEDGELGLYRKRLLKFLEVSHSYSPQTVLLQLAPHAFYEERALILGRLKQHEQALAIYVNTLKNVPAAEEYCRLYYNAHDETNSQVYLMLFRTLVHPNQQQLHSIPYHADSTPFGSYRDDVSEASTLVNSTSSYQPDVNTAIKILAKHADKIDTVGALNMLPATTPLRVVFSAINAVIQTTGRQASTRKMEKSVSQCAMSKKLERKNKAQSTKIIVNFSSECVVCEKKIAVSAFVRYPDGRLAHLYCHNDSQGGNRN", "text": "FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways (By similarity). Believed to act in part as a component of the putative HOPS endosomal tethering complex which is proposed to be involved in the rab-5-to-rab-7 endosome conversion probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion (PubMed:25273556). The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (PubMed:24374177). Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes (By similarity). Required for fusion of endosomes (By similarity). In association with lgg-2 mediates the tethering of autophagosomes with lysosomes to form autolysosomes (PubMed:25126728, PubMed:24374177). Within the HOPS complex, contributes to the normal development of gut granules in embryonic and adult intestinal cells (PubMed:24501423). SUBCELLULAR LOCATION: Cytoplasm Lysosome membrane; Peripheral membrane protein Late endosome membrane; Peripheral membrane protein Late endosome Lysosome. SIMILARITY: Belongs to the VAM6/VPS39 family."}
{"protein": "MFSWRRGDCESQKEENRSEERKGEETIRFPTRSPFHCVLFLLTDGFVLHKPTASPTVGFSPTIFSFYYSRWESSHRISHDESGFCTAKTPLQDSTFTRHPSTSVPSSPSTPRHSGMDYHQSSSVASSESTASTVAAAAAAAAAASLNQHHHPHLYCDDGLLSRSLTDMVSSGGYDSSSSSLSAAASMCYPTPDAYYYHAPPPPPPPQAQQGFSSTDAWLQMQMQPTYHNFGSTVVSTNSPLPSHLLSYGGQPAFADPFYTIGQSTPNTSSFLDTSNSSFGAPSTVVANPMTNYQLAFQAKLGSLHSLIGDSVQSLTSDRMIDFLSNKEKYECVISIFHAKVAQKSYGNEKRFFCPPPCIYLIGQGWKLKKDRVAQLYKTLKASAQKDAAIENDPIHEQQATELVAYIGIGSDTSERQQLDFSTGKVRHPGDQRQDPNIYDYCAAKTLYISDSDKRKYFDLNAQFFYGCGMEIGGFVSQRIKVISKPSKKKQSMKNTDCKYLCIASGTKVALFNRLRSQTVSTRYLHVEGNAFHASSTKWGAFTIHLFDDERGLQETDNFAVRDGFVYYGSVVKLVDSVTGIALPRLRIRKVDKQQVILDASCSEEPVSQLHKCAFQMIDNELVYLCLSHDKIIQHQATAINEHRHQINDGAAWTIISTDKAEYRFFEAMGQVANPISPCPVVGSLEVDGHGEASRVELHGRDFKPNLKVWFGATPVETTFRSEESLHCSIPPVSQVRNEQTHWMFTNRTTGDVEVPISLVRDDGVVYSSGLTFSYKSLERHGPCRIVSNY", "text": "FUNCTION: Transcriptional regulator that plays a central role in lin- 12/Notch and glp-1/Notch signaling pathways, involved in cell-cell communication that regulate a broad spectrum of cell-fate determinations (PubMed:8625826). Binds directly to the 5'-[A/G]TGGGAA- 3' DNA consensus sequence, which is present in the regulatory region of several genes (PubMed:8625826, PubMed:18706403, PubMed:23615264, PubMed:15297877, PubMed:32196486, PubMed:21737278). Acts as a transcriptional repressor when it is not associated with Notch proteins (By similarity). When in a complex with a Notch intracellular domain (NICD) product of lin-12/Notch or glp-1/Notch, and transcription regulator lag-3, it may act as a transcriptional activator that activates transcription of target genes(PubMed:18381292, PubMed:10830967, PubMed:32196486, PubMed:9003776). Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively (By similarity). Autonomously required in the germline for the stem cell fate, acting in the glp-1-dependent transcriptional activation of genes, including lst-1 and sygl-1 (PubMed:32196486). Involved in cell-fate specification during reproductive system development, by positively autoregulating its own expression, in response to lin-12/Notch signaling (PubMed:23615264, PubMed:32839181). Plays a role in Notch-dependent induction of left-right asymmetry in interneurons and motoneurons (PubMed:21737278). May repress expression of hlh-6, in a lin-12/Notch-independent manner (PubMed:18706403). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Su(H) family."}
{"protein": "MARAAPLLAVLATVLTTAAAGGDAPPGKIAVIGAGIGGSAVAHFLQQHFGPRVQIVVYEKGTVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREVVGRSAIFGGEHFVLEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGVEELLYSLGEATFVNMTQRSVAESLLQVGVTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTLHSTEGKALYQVAYESDKGNSSDFYDIVVIATPLHLDNSSNNNITFEGFTPPIEDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFANILTTDFPSFFCTLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPRFALHDQLFYLNALEWAASSVEVTAVAAKNVALLAYNRWYQDLDKIDQKDLIHKVKTEL", "text": "FUNCTION: Probable oxidoreductase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the prenylcysteine oxidase family."}
{"protein": "MSITAQSVYRDTGNFFRNQFMTILLVSLLCAFITVVLGHVFSPSDAQLAQLNDGVPVSGSSGLFDLVQNMSPEQQQILLQASAASTFSGLIGNAILAGGVILIIQLVSAGQRVSALRAIGASAPILPKLFILIFLTTLLVQIGIMLVVVPGIIMAILLALAPVMLVQDKMGIFASMRSSMRLTWANMRLVAPAVLSWLLAKTLLLLFASSFAALTPEIGAVLANTLSNLISAVLLIYLFRLYMLIRQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0259 family."}
{"protein": "MIMQSLFSNKYKFKDTEEKLNAYWDKIKLYKWKNLQGKQFIIDTPPPTISGQLHIGHVFSYCHTDFIARYQRMLGKDVLYPIGFDDNGLPTERLVEKIKKVRAADIDRKEFKALCNEVSAKFRMEFKILFQSLGISYDWDLEYHTISEEIQKLSQMSFIALYNMGKIYRKLQPIFWDCADRTAIARVEVEEKEMSSFMSTIAFSTEAGERINIATTRPELMPACVALFFNPLDIRYQHLQGQYAIVPIFGNKVPILSDEQVKIDKGTGLVMCCTFGDELDVYWWNKHNLNTQIIISKSGTLDLKHNIAETDTLSGKLHGVSIVEARKLVLETLSKCNLLIKKEEILHNVKCAERSGMPIEILLSNQWFIKVVEVKHELLEQVRKINWYPQSMRKQIEMWIDGLNWDWCISRQRYFGIPFPVWYSKRDNEEIIIPDVNELPIDPTETLPQGYSKEEVEADVDVMDTWATSSLSPQFNSIHTGINSIPLVPASLRAQSHEIIRSWAFYTILQAYYHHNSIPWENIMVSGWCLAADKSKMSKSKGNALIPNQLLQEYGADVIRYWAANSRLGSDTVFSDEVLQLGKRLVTKLWNASKFVSMFVSQCQIPDLNYVTETMDKWVLTKLYKVIVKATESFDVFEYCVALDYIESFFWKDFCDNYLELVKKRAYGESVTSKENLSAVNTLSFVLTTLLKMLAPFMPYITEEIYSTLYNNGSIHDHDNWPIVNTSLCNEMDEQLGEDFIEILNQVRKIKANAQLSVKCKIYKLIINSENYDFPTSWENDLKAVCNAEHIVRDKRTSYYDDKFLVSVQFAS", "text": "FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily."}
{"protein": "MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTSLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFDVGMSKESVRNDRNKKKKEAPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDKVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLDTLSGQSGGGTRDGGGLAPPPGSCSPSLSPSSHRSSPATQSP", "text": "FUNCTION: Receptor for retinoic acid (PubMed:17205979). Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes (PubMed:17205979). The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (PubMed:17205979). In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (By similarity). On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation (PubMed:17205979, PubMed:9230306, PubMed:19078967). Formation of heterocomplex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression (By similarity). Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2 (By similarity). RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis (PubMed:15901285). Has a role in the survival of early spermatocytes at the beginning prophase of meiosis (PubMed:15901285, PubMed:17905941). In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes (PubMed:10660575, PubMed:17905941). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (PubMed:19389355). Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (By similarity). In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nuclear localization depends on ligand binding, phosphorylation and sumoylation (PubMed:10660575, PubMed:12079996). Translocation to the nucleus is dependent on activation of PKC and the downstream MAPK phosphorylation (PubMed:10660575, PubMed:12079996). Increased nuclear localization upon pulsatile shear stress (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MVKSYTRYEPTEFFGVIASSGCNILGQPSSSAKSVGRAIVGGLESVLEWDLKTGQLLSKWKDSDCSAKVTCIANFDEMYAVGYADGSIRLWKDGELLITLNGHKSAVTTMDFDKMGTRLASGSMDTDIIVWDIVAETGLFRLRGHKDQITKLLFITPPSKNTAEETVVDTDIDSGDMDVDSKSSDSFLLSVGKDSFMKLWDLSIQHCVETHVDHQGEIWAMCVSPDAKRCLTAGTGSDVKVWEISFPDDNNFTPTTKAFQQLGTFTRQSRDRPITLAYDVSNRYVVFQAHDRLLEVFRLRSSAELEKILNRRRRRKKSEDVSITLKDEYEPFALIRTTARASSVAWIPGNRTPTLVTSLQNNSIEVYALDVKSEGSAAPLTERASRISAIEIPGHRADVRTLALSANHDVILSGANGSLKLWNKKTTSCIRTIECGYVLAASFINNDKCIVSAYKSGELEVYDIASSSLIERIQAHDGAIWDLAVGHDGTYFATASADHTVKLWSLKSSFDFVPGTTRKVTTLKLEQTRQIDFTDDVLAVKISPDGRFVAASLLDNTVKVYYLDSLKFFLNLYGHKLPVLSMDISYDSKLLVTCSADKNVKIWGLDFGDCHKSIFAHQDSIMEVTFQPDTYNFFTCSKDREVRYWDGKSFDLILKLRGHHSEVWALAVGPTFVVSGSHDHSIRLWEQGDDLVFLEEERERELEEQYESTLVSSYENAEADGEVKDGDVAAVTKQTIESLKDGEKILEAITIGIEDLDQEIQYRLDLLKSPGKARGPRNPILAHLGVSAEEYVLNTFKKIRSSHLDDALLVLPFEHVLSLFRFIDIWASRKWSIPLVSRIIFFLLRTYHRQLTTTVKMRPLLNNIRSSLRGSLQEERSLIGYNAAGLSYLRHEWELTHNTSLEDIDSTSLEVDGKKRAFSNIV", "text": "SIMILARITY: Belongs to the WD repeat WDR3/UTP12 family."}
{"protein": "MADQQTLDSSTPPPTQSDDLSHSHSTSSTTSASSSSDPSLLRSLSLSRLNAGAPEFVPGRTTPPLPQPPRMIIPPPPPHGMLHMYHHQPPFNTPVLGPVPIQPHLVPVQNHHPHHRFHQHHHHNRHQNQQYVPVRNHGEYQQRGGVGGEQEPDLVSKKNDRRDHSKRESKNDQVTETGASVSIDSKTGLPEDSIQKIVNQVEYYFSDLNLATTDHLMRFICKDPEGYVPIHVVASFKKIKAVINNNSQLAAVLQNSAKLFVSEDGKKVRRISPITESAIEELQSRIIVAENLPEDHCYQNLMKIFSTVGSVKNIRTCQPQNNGSGAPPAARSAAKSDGTLFSNKVHAFVEYEIVELAERAVTELSEAGNWRSGLKVRLMLKHQTKEPKQGQGRGRKGHDADVEHEEDDATTSEQQPIEKQSDDCSGEWDTHMQEQPIGEDQGNEKAAGQRKGRNRGRGKGRGRGQPHQNQNQNNNHSHNQNHNHNGRGNHHHHHHHQVGTQPSNNPMNNMEQPGMGKQQPPGPRMPDGTRGFSMGRGKPVMVQAE", "text": "FUNCTION: Transcriptional regulator. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSTITLLCIALAGVIMLLLLVIKAKVQPFVALLLVSLLVALAAGIPAGEVGKVMIAGMGGVLGSVTIIIGLGAMLGRMIEHSGGAESLANYFSRKLGDKRTIAALTLAAFFLGIPVFFDVGFIILAPIIYGFAKVAKISPLKFGLPVAGIMLTVHVAVPPHPGPVAAAGLLHADIGWLTIIGIAISIPVGVVGYFAAKIINKRQYAMSVEVLEQMQLAPASEEGATKLSDKINPPGVALVTSLIVIPIAIIMAGTVSATLMPPSHPLLGTLQLIGSPMVALMIALVLAFWLLALRRGWSLQHTSDIMGSALPTAAVVILVTGAGGVFGKVLVESGVGKALANMLQMIDLPLLPAAFIISLALRASQGSATVAILTTGGLLSEAVMGLNPIQCVLVTLAACFGGLGASHINDSGFWIVTKYLGLSVADGLKTWTVLTTILGFTGFLITWCVWAVI", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GntP permease family."}
{"protein": "MAVPKMVFSDVESFLDSHPELFEDYLNRKGSSSMVEKWLKNHQAGKSEAEPKEEKSSVCKDSWASKCDGLQRRASQKELRKTFARSKAINVNRTYDEHVNSRAQEPLTSMRRRALLRKASSLPPTTAHILSALLESRVNIPQYPSTAVDFKYYLKEHNEREFFLELVKDISNDLDLTSLSYKILVFVCIMVDADRCSLFLVEGTGNKKTLVSKFFDVHAGTTVLPSMNSGEVQVPWGKGIIGYVAEHGETVNIPDAYQDRRFSDEIDKLTGYKTKSLLCMPIQNSDGEIIGVAQAINKSSSGELFTEDDEKVLQMYLPFCGIAISNAQLFAASRKEYDRSRALLEVVNDLFEEQTDLEKIVRKIMHRAQTLLKCERCSVQLLEDIESPVVKFTKSFELLSPKCSADAESSFKDSMEKSSYSDWLINNSIAELVASTGLPVNISDAYQDPRFDAEADQFSDFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKTEVDKFKAANIPLVCELGIDKLSFDDFSLDVDAMITAALRMFIELGMVQKFKIDYETLCRWLLTVRKNYRMVLYHNWRHAFNVCQCMFAMLTTAGFQETLTDVEILALIVGCVCHDLDHRGTNNAFQAKTGSALSLLYGTSATLEHHHFNHAVMILQSEGHNIFCNLSSTEYSDLMQLLKQSILATDLTLYFENRNSFFELVSIGEYNWNVKTHRDMCRSMMMTACDLGAVTKPWDISRKVAELVTSEFFEQGDRERSELKLTPSAIFDRNRKDELPGLQLEWIDGICAPLYETLVKLNPKLQPMVDMINANRVKWEELDKKRQHDHGASVPASPCSAAEGSETGGVPCCSNNTPPTHVS", "text": "FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family."}
{"protein": "GDVAAGASVFSANCAACHMGGRNVIVANKTLSKSDLAKYLKGFDDDAVAAVAYQVTNGKNAMPGFNGRLSPKQIEDVAAYVVDQAEKGW", "text": "FUNCTION: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. SUBCELLULAR LOCATION: Cellular thylakoid lumen. SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily."}
{"protein": "MTDTVFSNSSNRWMYPSDRPLQSNDKEQLQAGWSVHPGGQPDRQRKQEELTDEEKEIINRVIARAEKMEEMEQERIGRLVDRLENMRKNVAGDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETNNRLHSVWLCKICIEQREVWKRSGAWFFKGFPKQVLPQPMPIKKTKPQQPVSEPAAPEQPAPEPKHPARAPARGDSEDRRGPGQKTGPDPASAPGRGNYGPPVRRASEARMSSSSRDSESWDHSGGAGDSSRSPAGLRRANSVQASRPAPGSVQSPAPPQPGQPGTPGGSRPGPGPAGRFPDQKPEVAPSDPGTTAPPREERTGGVGGYPAVGAREDRMSHPSGPYSQASAAAPQPAAARQPPPPEEEEEEANSYDSDEATTLGALEFSLLYDQDNSSLQCTIIKAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPIWNETLVYHGITDEDMQRKTLRISVCDEDKFGHNEFIGETRFSLKKLKPNQRKNFNICLERVIPMKRAGTTGSARGMALYEEEQVERVGDIEERGKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQLGISAKGERLKHWYECLKNKDKKIERWHQLQNENHVSSD", "text": "FUNCTION: Plays an essential role in docking and fusion steps of regulated exocytosis (By similarity). At the presynaptic level, RPH3A is recruited by RAB3A to the synaptic vesicle membrane in a GTP- dependent manner where it modulates synaptic vesicle trafficking and calcium-triggered neurotransmitter release (By similarity). In the post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4 and regulates NMDA receptor stability. Also plays a role in the exocytosis of arginine vasopressin hormone (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Cell projection, dendritic spine Postsynaptic cell membrane Membrane; Peripheral membrane protein."}
{"protein": "MAWIPLLLPLLILCTVSVASYELTQPSSVSVSPGQTARITCSGDVLAKKYARWFQQKPGQAPVLVIYKDSERPSGIPERFSGSSSGTTVTLTISGAQVEDEADYYCYSAADNN", "text": "FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins- secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). SUBCELLULAR LOCATION: Secreted Cell membrane."}
{"protein": "MQPHLDNNSNNDDVKLDTLGEQNVLSSAENITLPEDTFKSYMTYLLYEMAHYKPMIFSFLALSVSILIVVIFHNVKACDVVFGFSIFVTSILFLSTLIPFNVYISDEGFRIKLLLEVITHRPAVKGKEWRAITDNMNQYLLDNGLWSTRYYFYSSERCYKFFRFLVKEKPPGVNVNSSVKDATSTQIDAPANEASNEVIKCFSFSSDPIFEAYFVKAVEVEKQAQQEYWRKQYPDADIP", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DUP/COS family."}
{"protein": "MNKPIKNIVIVGGGTAGWMAASYLVRALQQQANITLIESAAIPRIGVGEATIPSLQKVFFDFLGIPEREWMPQVNGAFKAAIKFVNWRKSPDPSRDDHFYHLFGNVPNCDGVPLTHYWLRKREQGFQQPMEYACYPQPGALDGKLAPCLSDGTRQMSHAWHFDAHLVADFLKRWAVERGVNRVVDEVVDVRLNNRGYISNLLTKEGRTLEADLFIDCSGMRGLLINQALKEPFIDMSDYLLCDSAVASAVPNDDARDGVEPYTSSIAMNSGWTWKIPMLGRFGSGYVFSSHFTSRDQATADFLKLWGLSDNQPLNQIKFRVGRNKRAWVNNCVSIGLSSCFLEPLESTGIYFIYAALYQLVKHFPDTSFDPRLSDAFNAEIVHMFDDCRDFVQAHYFTTSRDDTPFWLANRHDLRLSDAIKEKVQRYKAGLPLTTTSFDDSTYYETFDYEFKNFWLNGNYYCIFAGLGMLPDRSLPLLQHRPESIEKAEAMFASIRREAERLRTSLPTNYDYLRSLRDGDAGLSRGQRGPKLAAQESL", "text": "FUNCTION: Involved in the biosynthesis of the antifungal antibiotic pyrrolnitrin. Catalyzes the chlorination of tryptophan (Trp) at C7 position to yield 7-chloro-L-tryptophan (7-CLT). The reaction between FADH2, Cl-, and O2 generates the powerful oxidant HOCl, which is presumed to carry out the chlorination reaction. The reaction of HOCl with the active site Lys-79 generates a lysine chloramine, which plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. It is also able to use bromide ions to generate monobrominated Trp. SIMILARITY: Belongs to the flavin-dependent halogenase family. Bacterial tryptophan halogenase subfamily."}
{"protein": "TSKISTTYEEEGRQSKIQPRAFVITRSGPTSRSSSYSARQSYGSRSSITPGVYQQLSSSGITDFRGTREKEKREMQNLNERLAGYIEKVHFLDAQVKKLEAENXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMDYAEFWKSELSKCVRDIQSAYDEKIDIIXXXXXXXXXXXXXXXXXXXXXXXMQLQHVQEEVKKLRTQAGEKNAAYAEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMELEIACYRKLLEGEESRVGLRSLVEQAIGVQGRGTASLKDTIQQSTASGSMTVQRSSKGPIAFNSVDQSGSNIVIENTTSGARAKTQSLKGWRVDKTVAGRVAASIELKNYDLPPNTKYTIWAKGAKDRATADNEQIADMFSLGVG", "text": "FUNCTION: Epithelial intermediate filament protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MENNIENFDPSLVYFGDRGQDFKKMIRSILSLGMSDEYIPYLTTPESLNTYNTAFTSRGADDKNNYEMFEQLGDVSVNKFIVNYMYKRFPQLRNPNGVDVVAKLKIKYASKNQLQMLSESLDMWRFITATYDERTNKKKPLLEDTFESFFGATEWLIDSFIEDIALKQGNNNTYVGVGYNIINGILTTLFDRINISLKYENLVDAKTRFNEVIAEQKSIIGDVKYEDEYKNGKHTSKIYRYPPNSNLKELLGIGTGTLKRDAQEQAASRALETLALKHNIIKEAPDRFKAFM", "text": "FUNCTION: Digests double-stranded RNA. SIMILARITY: Belongs to the IIV-6 142R family."}
{"protein": "MLNIPIIANSKRFLFSKDHEAQSTRDHDVELETREGPSSGYNPNFNAADAILKKNSDQVDLDVNKLTNVTSRVLNTPEASLIYDDDREFPDGGLKAWLVVFGAFMGLVPVFGLINSLGAIESYISKHQLANISSSTISWIFSLYLAISFLSCILSGGYFDRNGSIGLMCTGTVIYAGGLFALANCKSVWQFILAFSVCSGLGTGILMTPLIGTVATWFLKRRGIATSISTMGGSIGGIVFPIMLRKLYKEVGFQWAIRILSFICLTCLICASVLARERTKPVVQPFKSKAEVAKWYISSVFNWRYFLEGKFLFVAIGASFAESSLTSCATYLASYSMTRGNTENVAYTMITASNAVGILGRYIPGYFADKFIGRFNVEIITISMAALFNFVMWLPFGGNTKVLWAYVCLWGFSTGSILSLTPVCIGQISKTTDFGKRYATVYLLQALVTIPVLPIGGTLIGKGTVANYNHFIIFNSALMAAGAACYIISRHICVGAKLCKF", "text": "FUNCTION: Probable transporter. Does not act in the transport of monocarboxylic acids across the plasma membrane. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
{"protein": "MAIETVASTDAFKVLVAEVTAQEGYREPMAFGIARVDRGQKNAEKVLQANFPLINWKENFGSAAVFIKALQEAKCDVDFSGSEFVATINDNFVANAMAAFAPYLAEATGDSHKNVQVIKTLAKMEDIGKNFRIVFLFEDANPESVEAVYLKLYALSLRKAELRKVNLNGAFGILSNVAWVGNTPYELDYLRENEIEMKLNGTYPTVDSVDKFPRFLQHVIPDDNTRILEASKVRMGAQLAAGTTVMPGASYINFNAGTLGPVMVEGRISSSAIVGAGSDVGGGASILGVLSGTDGNPISIGENTLLGANSVTGLPLGDGCIVDAGITILAGTKIKIAPEELEKIKAANPDAKLDNKTTFKGEELQGLNGIHYRQNSLTGEIIARRSTREVKLNEDLH", "text": "FUNCTION: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N- succinyltransferase family."}
{"protein": "MGDDIMPISNLAKESEVRAVKDIPCKNIETDNHLEIGLSSGLSRSKDTSKFKKNSINTIKLIDDIIALHNDPKGNKLLWNDNWQDKIINRDLANIFEKIDESVSELGGLEMYQEMVGVNPYDPTEPVCGLSAQNIFKLMTEGEHAVDPVEMAQTGKIDGNEFAESVDQLSSAKNYVALVNDRRLGHMFLIDIPSNDQETVGYIYQSDLGQGALPPLKIADWLNSRGKDAVSLNKLKKLLSREFNLLSDDEKRALISETLDIHKDVSNVELDRIKRDRGVDIYLTEYDVNNFYENIETLKSKLSNYDKKLSKPK", "text": "FUNCTION: Protein-glutamine deamidase effector that inhibits the host cell cycle and other key cellular processes such as the actin network and programmed-cell death (PubMed:19308257, PubMed:19225106, PubMed:20870031). Acts by mediating the side chain deamidation of 'Gln- 40' of host NEDD8, converting it to glutamate, thereby abolishing the activity of cullin-RING-based E3 ubiquitin-protein ligase complexes (CRL complexes) (By similarity). Inactivation of CRL complexes prevents ubiquitination and subsequent degradation of the cyclin-dependent kinase inhibitors CDKN1A/p21 and CDKN1B/p27, leading to G1 and G2 cell cycle arrests in host cells (PubMed:19308257). Deamidation of 'Gln-40' of host NEDD8 also triggers macrophage-specific programmed cell death (By similarity). Also able to catalyze deamidation of 'Gln-40' of host ubiquitin in vitro; however, NEDD8 constitutes the preferred substrate in vivo (By similarity). SUBCELLULAR LOCATION: Secreted Host nucleus Note=Secreted via the type III secretion system (TTSS). SIMILARITY: Belongs to the Cif family."}
{"protein": "MKLPPRRKLKLFLLAWMLVLFSALIVLATLILVQHNNTELTEVKSELSPLNVVLHAEEDTVQIQGKPITEQAWFIPTVAGCFGFSALAIILGLAIGLPIVKRKEKRLLEEKERQEQLAEQLQRISAQQEEQQALEQQAAAEAHAEAEVEPAPQPVPVPPQPQVQINFGPRTGFPPQPGMAPRPGMPPHPGMAPRPGFPPQPGMAPRPGMPPHPGMAPRPGFPPQPGMAPRPGMPPHPGMAPRPGFPPQPGMAPRPGMQPPRPGMPPQPGFPPKR", "text": "FUNCTION: Adhesin necessary for successful cytadherence and virulence. SUBCELLULAR LOCATION: Cell projection, attachment organelle membrane; Multi-pass membrane protein. Note=Integral and surface exposed membrane protein that localizes to the membrane at the attachment organelle."}
{"protein": "MKVGIIGAMEQEVALLRSQMSNPTTLQLGGCEFYQGTLAGKEVILTRSGIGKVAASVATSLLLEKFAPDCVINTGSAGGFAQDLHIGDVVIASEMRFHDVDVTAFGYEMGQMAQQPAAFPCDETLIAVAQDCIAEQGKHQTKVGLICTGDQFMCKPDAIAKARADFPQMLAVEMEGAAIGQVCHMFKVPYLVVRAMSDIAGKEQVESFDAFIEVAGKHSAEVIIKMLGKL", "text": "FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN subfamily."}
{"protein": "MPDIRDVEIIAPNFKRRLSGVTSTIVQLIPCQIRLGIKIATLGPGLPEDLPKLKWRQLLGLWRPPARRRRRVWHARRNNEMAVGILLRHLTRMPLKLLFTSAAQRRHTAYTKWLIRRMDAVIATSDRSGSFLEVPHTVIQHGVDLALFHPPEAAEDGIAATGLPGRHLVGCFGRVRHQKGTDLFVRAMIELLPQHTEWTAVVSGRVTAEHVAFADKLKADVVAAGLSDRILFLGEVPDIKIWYRRLTLYVAPSRNEGFGLTPLEAMASRTAVVASDAGAYAELIVTGETGSVVAASDGEALTRAIAPYIADPALAVAHGENALRHVRANFALEREASAIGAVYNSLLGDNRS", "text": "FUNCTION: Acts at transfer of mannose group to a 3-deoxy-D-mono octulonic acid (KDO) via an alpha-1,5 linkage. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MAEGTDPLDDCGGFLDTEADCLDCDNLEEDLTELFDADTVSSLLDDTDQVQGNSLELFQHHEATETLKSIEHLKRKYVDSPDKSLGIDNSVNAESLQVESGFGSQQSVSDTPVTDILNANTARVKHLLLFRQAHSVSFSELTRTFQSDKTMSWDWVGGLADIHASVLESLQTSLRSHC", "text": "FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1- E2 complex binds to the replication origin which contains binding sites for both proteins. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the papillomaviridae E1 protein family."}
{"protein": "MFKFNEEKGQLKCSFCGKTQDQVRKLVAGPGVYICDECIELCTEIVEEELGTEEEVEFKDVPKPQEIREILNEYVIGQDQAKKSLAVAVYNHYKRINSNSKVDDVELSKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLKLIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNILFICGGAFDGIEQIIKRRLGQKVIGFGADNKAADLEKEDLLSKVLPEDLLRFGLIPEFIGRLPVIASLEKLDEEALVAILTKPKNALVKQFKKMLELDNVELEFEEEALSEIAKKAIERKTGARGLRSIIEGIMLDVMFELPSRDDIEKCVITGATVTHGEPPRLLLKDGTEVSQDKTSA", "text": "FUNCTION: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451). SIMILARITY: Belongs to the ClpX chaperone family."}
{"protein": "MKTLIRPLVVLFVVLTAVTGLAYPAVMTVFGQAVFPSQANGSLIEQNGKVVGSALIGQSFDAPKYFWGRLSATAPMPYNAAGSGGSNLGPLNPSLADQVKARIAALRDAGTDLSKPVPVDLVTASASGLDPEITPAAAAYQVERVAKARNLTPDAVAQLVAANTAGRQFGVLGEPRVNVLKLNLALDAAQAAH", "text": "FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the KdpC family."}
{"protein": "MATPRTLVPILPPVAALLLLLVAASSIPILAAAQPADACGGAPDQAAADGACHDVPRALRLKLIAIPTILVSSVVGVCLPLLSRSVPALRPDGGLFAVVKAFASGVILATGYMHVLPDAFNNLTSPCLPRKPWSEFPFAAFVAMLAAVSTLMADSLMLTYYNRSKPRPSSGGDVAAVADHGESPDQGHRHGHGHGHGHGMAVAKPDDVEATQVQLRRNRVVVQVLEIGIVVHSVVIGLGMGASQNVCTIRPLVAAMCFHQMFEGMGLGGCILQAEYGRRMRSVLVFFFSTTTPFGIALGLALTRVYRDNSPTALIVVGLLNAASAGLLHYMALVELLAADFMGPKLQGNVRLQLAAFLAVLLGAGGMSVMAKWA", "text": "FUNCTION: Iron transporter involved in the uptake of iron from the rhizosphere across the plasma membrane in the root epidermal layer. May also transport other divalent cations. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MSYKAQYTPGETQIAENRRKHMDPDYEFRKLREVSDEDLVKVLGHRNPGESYKSVHPPLDEMDFEEDIVRDMVEPIQGAKEGVRVRYIQFADSMYNAPAQPYDRARTYMWRYRGVDTGTLSGRQVIEMRELDLEGVSKELVETELFDPATTGIRGATVHGHSLRLDENGLMFDALQRYVFDEEKGHVVYVKDQVGRPLDEPVDMGQPLGEDELKKITTIYRKDNIAMRDDKEAIEVVENIHTGRTLGGFGMDVFKDDLRKRLGDD", "text": "FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. SIMILARITY: Belongs to the methyl-coenzyme M reductase gamma subunit family."}
{"protein": "MPLHHLTRFPRLELIGAPTPLEYLPRLSDYLGREIYIKRDDVTPIAMGGNKLRKLEFLVADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPDAQLQTLATRIEAQGFRPYVIPVGGSSALGAMGYVESALEIVQQCEEVVGLSSVVVASGSAGTHAGLAVGLEHLMPDVELIGVTVSRSVAEQKPKVIALQQAIAGQLALTATADIHLWDDYFAPGYGVPNDAGMEAVKLLANLEGVLLDPVYTGKAMAGLIDGISQKRFNDDGPILFIHTGGAPALFAYHPHV", "text": "FUNCTION: Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase family."}
{"protein": "MQAQAPVVVVTQPGVGPGPAPQNSNWQTGMCDCFSDCGVCLCGTFCFPCLGCQVAADMNECCLCGTSVAMRTLYRTRYGIPGSICDDYMATLCCPHCTLCQIKRDINRRRAMRTF", "text": "SIMILARITY: Belongs to the cornifelin family."}
{"protein": "MRLWLRGLACQALRSSWGVCRIHTQPPPPPIPEVVATWEAISLGRQPVPEYFNFAHDVLDVWSQLEKTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR", "text": "FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MALSMEFGFSIGSCFKAPNPPVLISASPNKINFTLRRRKKRFLLRVSAVSYKEFAESALEETRKRIVLEPSHLQEKYSSMTGLDGKTELQMLAFKSSKIRLLRSMAIENETMQVFDFAGFMEPEYDTPIFCANFFTSTNVNIVVLDLNPLHQLTDQTDYQDKYYNKIMSIYHKYAETFPWGGKLTGESIKFFSPLVMWTRFSSSKEKHKALFSAFLEYYQAWLEMTIQVREEMEPSHVRANCEAQHKYLTWRAQKDPGHGLLKRLVGEAKAKELLRDFLFNGVDELGTKTFIDYFPEYQTEDGTVSDKRSIIGKSYETRPWDLTGQFIG", "text": "FUNCTION: Catalyzes the two-electron reduction of biliverdin IX-alpha to the tetrapyrrole chromophore phytochromobilin (PPhiB). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the HY2 family."}
{"protein": "MIHLYKTSTPSTRNGAVDSQVKSNPRNNLIHGQHHCGKGRNARGIITAGHRGGGHKRLYRKIDFRRNEKDTSGRIVTIEYDPNRNAYICLIHYGDGEKRYILHPRGAIIGDTIVSGTEVPISMGNALPLSTDMPLGTAIHNIEITLGKGGQLARAAGAVAKLIAKEGKSATLRLPSGEVRLISKNCSATVGQVGNVGVNQKSLGRAGSKCWLGKRPVVRGVVMNPVDHPHGGGEGRAPIGRKKPTTPWGYPALGRRSRKRNKYSDSLILRRRK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
{"protein": "TESPIPVPAPAPAAKPKPKRVSKRPASHPPYSDMIAAA", "text": "FUNCTION: Histone H5 performs the same function as H1, being necessary for the condensation of nucleosome chains into higher order structures, and replaces histone H1 in certain cells. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H1/H5 family."}
{"protein": "MMKIKITKSTILLIISFLFILAIMAYIGLDKIIKVLINTNPEYVILAFILQILVSVILSARWKFIIKILGYSANFKNIFLLVLMGLFINNITPSMRGGGEAFRAYYLSKLEEIPKGLAFSTVVVERVLDTAIFLFFTLFVIGYFVVTGFKYLEYLILSWIFLFSLTAIIIYLIANKGLLIKTVTKISKFICKYCSYNYDETKILQSIEEFYNSMKFFKNKRGWEVVVAIFLSVMRYIFDILKLWLLFLSLSYVVSVICVSAVYLITLLSGVLSITPSGFGTADTVMILSFSAFNIPPSVAAAVTLLDRLVSYILPTILGYIAMLIIKREIDKKKGK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0104 family."}
{"protein": "MNALRGWLAALGSMLLASAAQLGMRWGMSRLPLPEAWAGQTPERAALLAVALAVTAYAASLLCWLAALRHLPLGRAYSLLSASYALVYLLAASLPAFDETFSTSKTLGVGLVVLGVLTVNARRTAAAPAHHPSRKAP", "text": "FUNCTION: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ArnF family."}
{"protein": "MNPNQKIICISATGMTLSVVSLLIGIANLGLNIGLHYKVGDTPDANTPNVNETNSTTTIINNNTQNNFTNITNIIVSKNEERTFLNLTKPLCEVNSWHILSKDNAIRIGEDAHILVTREPYLSCDPQGCRMFALSQGTTLRGRHANGTIHDRSPFRALISWEMGQAPSPYNVRVECIGWSSTSCHDGISRMSICMSGPNNNASAVVWYGGRPVTEIPSWAGNILRTQESECVCHRGICPVVMTDGPANNRAATKIIYFKEGKIQKIEELAGNAQHIEECSCYGAVGMIKCICRDNWKGANRPVITIDSEMMTHTSKYLCSKVLTDTSRPNDPTNGDCDAPITGGSPDPGVKGFAFLDGENSWLGRTISKDSRSGYEMLKVPNAETDTRSEPTSHQVIINNQNWSGYSGAFIDYWANKECFNPCFYVELIRGRPKESSVLWTSNSIVALCGSRERLGSWSWHDGAEIIYFK", "text": "FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. SUBCELLULAR LOCATION: Virion membrane Host apical cell membrane; Single-pass type II membrane protein Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. SIMILARITY: Belongs to the glycosyl hydrolase 34 family."}
{"protein": "MLFTVSCSKMSSIVDRDDSSIFDGLVEEDDKNKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNAREMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSVFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYMRFIGNFKSLNSVPTSAHNGFEGTIQRTHRLSYEDRVCSVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLENLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRRELGIEESLPDATADKGQDSGSDNRINTVSLKEALERFDHSPTPSASSRSSRKSSHTAVSDPSSTPTKIPTDTSTPPRQHLPAHEKMAQRRSSFSSQSMNSQSVGPSLTQPVISQAANLPVPQGMSQFQFSAQLGAMQHLKDQLEQRTRMIEANIHRQQEELRKIQEQLQMVHGQGLQMFLQQSNPGLNFGSVQLSSGNSSNIQQLTPINMQGQVVPTNQIQSGMNAGHIGTSQHLIQQQSLQSTSTQQSQQSVMSGHSQQTSLASQTQSTLTAPLYNTMVISQPAPGSMVQIPSSMPQNSTQSATVTTFTQDRQIRFSQGQQLVTKLVTAPVACGAVMVPSTMLMGQVVTAYPTFATQQQQAQTLSVTQQQPQQQQPQQQQPQQQQPQQQQQSSQEQQLPSVPQPSQAQLTQSPQQFLQTSRLLHGNPSTQLILSAAFPLQQSTFPPSHHQQHQSQQQQQLSRHRTDSLTDPSKVQPQ", "text": "FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post- translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking Ala residue in addition to the canonical 6-nucleotide E-box sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3'. The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (By similarity). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytosol Note=Localizes to sites of DNA damage in a H2AX-independent manner. Shuttling between the cytoplasm and the nucleus is under circadian regulation and is BMAL1-dependent. Sequestered to the cytoplasm in the presence of ID2."}
{"protein": "MYCTLNKKEIKAVKPTDAIPPQYPKEFFINGNGKKPTLRVPQGKLDLPTVRELVFGGLERGELVLSHVIRYLYLVGERITEKLEGDWISFGVNIGRRNQEINVWNFYEVIIEDDQTIDGRRANNVDENDDVWLTLALLAYYRLGRSANQNHRNNLLIKLNAQIKGYRKDAPNIIDDVAVHGSWVTNSEFCKIAAGFDMFMNRFKNNKYAHVRFGTVASRYKDAAGLMALGHACDVTGLTIGEILDWIFVSNVGEDVVKIMEEGNEIDDPYSYMPYMMDMGISNKSPYSSISCPHIYTFLHLVGTLLTSERSKHARMVSEHNLQNIKMNAFVVSYVKSNKAALTKAFLKSEDRDYEKRQEDGSNDDEDEDESGDDDDFGAMPKSSDPMEWFIFLESNHFILPEKVTEFCIRECKKIQNARPNTIGKYLASIV", "text": "FUNCTION: Encapsidates the genome, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non- specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the ephemerovirus nucleocapsid protein family."}
{"protein": "MSYGWYHGNITRSKAEDLLSQAGKDGSYLVRDSESVCRAYALCVLNQNCVHTYRILQNAEHQLSVQASEGVPMRFFTNLVELIEFYRRENVGLVTHLQYPIEKEEEGPEEPDEEQEPAPPNVPPRNFAFTPPSETKECQTAIERAPAANASLLLSETLLQRFQDTDSRCIPEEHLQAICDYFSLHIVSDCDMVRTGSQTLPQFKKLLMTLCTGLHRELTRTLPTLESLQVAIDPQLSPGFKQRSPLPGDSATNNMVNKLTHLTSMVSNLEEKVKTVLMEGAAVKHRRSLIPPIIFEVKADSIGISQKTHLKVDVETGKLIIKKSKDGPDDKFYPSKKILQLIKSQKFPHKLVIVLETEKEKTQRKEYVFADSKKREGFCQLLQQMKNKHSGQSEPDMLSIFIGTWNMGDAPPPKNITPWFQCKGQGKTRDDTADYIEHDIYVIGTQEDPLSEKEWTDTLIHSLREITSVEYKVITTQTLWNIRIVVLAKPEHAHRISHVCTNSVKTGIANTLGNKGAVGASFMFNGTSFGFINSHLTSGSEKKLRRNQNYFNILRFLVLGDKKLSPFNFTHRFNHLFWLGDLNYRLQLPNTEAENIIQKIKQQQHQELLPHDQLNLERRESLIFFQFHEEEITFPPTYRYERGSRERYCYTKQKATGIKYNLPSWCDRILWKSYPQMHILCQSYGCTDDITTSDHSPVFGTFQVGVTSQFVSKNNPGDSGDLEAQGHIELMNCKATLYTKSHTKFYIEFHSPCLENMVKSSEAEDQEGNNGTLVVKFGVLPKLTPIISDLEYLLDQHLLICIKSSDTDESYGEGCIALRKEDTEQQFPFCTILTHHGEETGLFCGEICLPASGGKQREKLYDFVKIEKDETVAQKQLKHPYSQSMEQSRIMKSISEKSAMIARMRAAPETQNSMDHTASVAAISSQAKQSPPTTPPGFRGSEPRQKPGSPVQGRGDTPITSPPRTTLSTQKFSHSNTNRTAPAARPQDSLQITVPSDPHEMVDNPLYGPVNNTLYPPTA", "text": "FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Able also to hydrolyzes the 5-phosphate of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P3) and inositol 1,3,4,5-tetrakisphosphate. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Membrane raft Cytoplasm, cytoskeleton Note=Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family."}
{"protein": "MYVCLCNAVTDKAIRNAVRQHNPHTMKQLRELVPIGTDCGKCIRQARQIMVEECGTIIPMHEVA", "text": "FUNCTION: Seems to associate with BFR; could be a general redox and/or regulatory component participating in the iron storage mobilization functions of BFR. Could participate in the release or the delivery of iron from/to bacterioferritin (or other iron complexes) (By similarity)."}
{"protein": "MSGARTAHALVFLLGCSALALGVCSASLEHGEAEYYVAAVYEHRSVLSPNPLELSSRQQALELMKQNLDVYEQQVMAAAQKGAHIIVFPEDGIHGFNFTRTSIYPFLDLMPSPRLVSWNPCLEPFRFNDTEVLQRLSCMAIKGKMFLVANLGTKQPCLGSDPGCPQDGRYQFNTNVAFSDNGTLVGRYRKHNLYFEEAFDSPADVDLTTFDTPFAGKFGMFTCFDILFFDPAVRLLRDFEVKHIAYPTAWMNQLPLLAAIEIQKAFATAFGVTVLAANIHHPTLGMTGSGIHTPLKSFWYHNMDDPEGHLIIARVATNPQGLVGTENTTSEMDPSHRKFLKVLSGDPYCEKDAQEVRCDEAAKWNLNAPPTFHSEMMYDNFTLVPVWGKEGHLQVCSNSLCCHLLFERPALSKELYALGVFDGLHTVHGTYYVQACALVKCGGAGFETCGQEISEAEGLFDFHLWGNFSTLYVFPLFLTSGMTLDTPDQLGWESDHYFLRKRGLSSGLVTAALYGRLYERN", "text": "FUNCTION: Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. BTD/VNN family."}
{"protein": "MGRYSREPEIAAKSCKARGSNLRVHFKNTCETANAIRKMPLKRAVAYLKNVIGHKECVPFRRFNGGVGRCAQAKQWGTTQGRWPKKSAEFLLQMLRNAESNADYSGLDVDRLVIEHIQVNRAACLRRRTYRAHGRINPYMSSPCHIEMWLTEAESTPEGAKKGKKKKGTKDAVEKSSKRVKTAATAAH", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL22 family."}
{"protein": "MTKLNAQVKGSLNVTTPGVQIWRIEAMQMVPVSSSTYGSFFDGDCYIVLAIHKTGSNLSYDIHYWIGQDSSQDEQGAAAIYTTLMDDFLKGRAVQHREVQGNESEAFRGYFKQGIVIRKGGVASGMKKVETNSYDIQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVGVVDGEDEKASPQLMEIMNYVLGQRKELKAAVPDTVVEPALKAALKLYHVSDSEGKVVVREVATRPLTQDLLSHEDCYILDQGGLKIYVWKGKNANPQEKKEAMNQALNFIKAKQYPPSTQVEVQNDGAESAVFQQLFQKWTVPNQTSGLGKTHTVGSVAKVEQVKFDATSMHVQPQVAAQQKMVDDGSGEVEIWRIENLDLVPVESKWVGHFYGGDCYLLLYTYLIGEKQHYLLYIWQGSQASQDEITASAYQAVILDQKYNNEPVQIRVPMGKEPPHLMSIFKGRMVVYQGGTSRANSTEPVPSTRLFQVRGTSVNNTKAFEVPARATSLNSNDIFVLKTQSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWVALGGKAPYASSKRLQEETLVITPRLFECSNQTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKNANEDEKKAAAVTAQEYLKTHPSGRDPETPIIVVKQGYEPPTFTGWFLAWDPFKWSDSKSYEDLKAELGNSGDWSQITAEIKNPKPDVFNANTNLSSGPLPIFPLEQLVNKPAEELPQGVDPSRREEHLSIEDFTKALGMTPAAFSALPRWKQQNLKKEKGLF", "text": "FUNCTION: Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell projection, ruffle Cell projection, microvillus Cell projection, filopodium tip Cell projection, filopodium Note=Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia (By similarity). SIMILARITY: Belongs to the villin/gelsolin family."}
{"protein": "MKILAVVLISVIVLNTANGENYYPQKYTNDYYGCQKQTDAFCDKVCKLHLADSGFCDQSWGLAKACKCVNVSYDNSFFFNALESQCPLLNKSAA", "text": "FUNCTION: The heterodimer non-edited LVP1 induces lipolysis in rat adipocytes. Induction of lipolysis by LVP1 appears to be mediated through the beta-2 adrenergic receptor pathway (ADRB2) (By similarity). FUNCTION: The homodimer inhibits HMG-CoA reductase (HMGCR) (32% of inhibition produced by 0.6 uM), a glycoprotein involved in the control of cholesterol biosynthesis. The inhibitory effects of bumarsin are seen at much lower concentrations (0.6 uM) than that for statins such as atorvastatin (5 mM) and simvastatin (10 uM). In addition to inhibition of HMG-CoA reductase, this protein lowers cholesterol levels by inducing steroid hormone synthesis via StAR, and by increasing reverse cholesterol transport mediated by the induction of ABCA1 and APOA1 (By similarity). FUNCTION: The monomer edited version, similar to alpha-toxins, may modulate voltage-gated sodium channels (Nav) and may block voltage- gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily."}
{"protein": "MLGKRTGSRHIAVVLLMCLFWYVISSSNNVIGKMVLNEFPFPMTVTLVQLCSITLYSGPFFNLWRIRKYQDIPRPYYYRLIVPLALGKLLASVTSHISLWKVPVSYAHTVKATMPLFTVVLTRVFFGEKQPTLVYLSLLPIITGVGIATVTEISFDMMGLISALISTMGFSMQNIFSKKVLKDTNIHHLRLLHLLGKLSLFIFLPLWLYMDSFAVFRHTAIKNLDYRVIALLFADGVLNWLQNIIAFSVLSLVTPLTYAVASASKRIFVIAVSLLILGNPVTWVNCVGMTLAIVGVLCYNRAKQLTRGREQPTLPLSQTSYVKYSPLEQQADPYYRGSVNGKLSNGLHRTPGNSLLANGSGMPSGTATRLLFV", "text": "FUNCTION: Putative transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35E subfamily."}
{"protein": "ALWKDMLSGIGKLAGQAALGAVKTLV", "text": "FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIQLGDTEFTLDPKDFPNLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLADYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNMMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAELGQNRVKPVIKDQYYNMAQIIEKDMSIIDIAKKAMENLDIAPIIEPIRGGTDGSKISFMGLPTPNLFAGGENMHGRFEFVSVQTMEKAVDTLLEIIRLNNEVAK", "text": "FUNCTION: Cleaves the N-terminal amino acid of tripeptides. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides (By similarity). FUNCTION: Cleaves the N-terminal amino acid of tripeptides. FUNCTION: Cleaves the N-terminal amino acid of tripeptides. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20B family. SIMILARITY: Belongs to the peptidase M20B family."}
{"protein": "MMSQATPSATPVRNADGQKKGKKLPLIVDVAIGNNGKQLYQVHESSKMVRKEMPRSTNFALNDDISDEGFFISQINEQRTPIRKTLGTLSPSSLNQKRIRHDVYDQGDDNSNDDNCQNDVYEQQQQQPQQQQQQQQQLHQPNMYENGNVGVISNDPVSSVGHYDNNPVSHVPTGAYSRVQDTDIWSDDVEEAFEEVLRLIPKSGLNKIKIAGRSCGRNELISDYIFAKTGKFRTRKQVSSHIQVIKNLGQKLDIIQLINDGPIFNSHEEQLESTKKFEDVFSKINLNKSLGFSDSMKRKSDSMPMHLPATKRIRRKHSGNPLNKIKFSNFFMSVNDQYGMNPIVLTIQQNGNDVKSLKLKDNANISSRFPGLSDFKSCPHIPIIHNMVKILLPQLPESYSIDDGFSSSYALKYEEPENASPTHTSIISSSRTYSLFTCVYSYGKEIVKFDEDGIQLNQDREFIPGFWKFFFSTFGDQSEGGLSAAFKGVTIKQILYESSPDSVKKEQDASKVNKSKVKLVLLWEFAKVSECKDALTTTTKLVLPPRASASSSKTTEEVFEYSEPALNSIGGTPTDTTSPNMDLNNQNLSAAATSIPGIRDTIHSASMPDINELPSSAKPQVRLQKTFQSMQHLQPHQMWQQQQQQQPSQGAYTSSVASQSLNTSLSSPYAQYGMPLPQQTIGTFVPPTSQTFGVSYTHNSQHPSANMDLMMLSSMNTGYGNITNNQDYQFGNIGYTEGFTSEF", "text": "FUNCTION: Transcription factor which regulates genes involved in hyphal development, cell adhesion, biofilm development, and virulence. Plays a role in the formation of 'finger' morphology, a unique multicellular morphology of C.albicans induced by carbon dioxide. Regulates gene expression during intestinal colonization. Required for the expression of the secreted aspartyl proteinases SAP4, SAP5, and SAP6; but also of BCR1, PGA4, and CDC24. Moreover, a positive feedback loop between CDC24 and TEC1 contributes to an increase in active CDC42 at the tip of the germ tube which is important for hyphae formation. Regulates also the pheromone response of the white cell phenotype. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TEC1 family."}
{"protein": "MQLQINVASHPLIQHWSGILENNNNPGTILRTACSELGKWITYEIMREWLVTETVSIKDNTTISLISNHYKYIIVIIMPYGFILAEGARALLPTANIALVSYNNSIDNISDKLDSFTKILVLDLFLDEIIMTSVLEELIKKGAILNNIKIACLECGSSQLNKLGQKWSTLEIYTTKVNSITDNSEATKEQVLKDKFFA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the UPRTase family."}
{"protein": "MRTLWIVAVLLLGVEGSLVQFEMMIIKVAKRSGLFWYGAYGCYCGWGGQGRPQDATDRCCFVHDCCYGKATDCNPKTVSYTYSVKNGEIICEDDDPCKKQVCECDRVAAVCFRDNIPSYNNNYKRFPAENCRGDPEPC", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that shows very low inhibition of ADP-induced platelet aggregation in platelet-rich plasma of human, rabbit and guinea pig. In vivo, shows efficient edema- inducing activities in rat paws. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
{"protein": "MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKAKTSPGTSVPSEASPTATPESSTSFPSAPASGMSHPPPTAREDKSPSEESAPTTSPESVSGSVPSSGSGGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPSTEAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELVDISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE", "text": "FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'- linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome (By similarity). FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, XPC:RAD23A dimer has NER activity. Can stabilize XPC (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RAD23 family."}
{"protein": "MTLPNDLLETLVKRKESPQANKVWPVTTFSLARNLSVSKFLPCLSKEQKLEILQFITSHFNHIEGFGEFIVLPLKDTPLWQKEFLLEHFLLPYDLVGNPEGEALVVSRSGDFLAAINFQDHLVLHGIDFQGNVEKTLDQLVQLDSYLHSKLSFAFSSEFGFLTTNPKNCGTGLKSQCFLHIPALLYSKEFTNLIDEEVEIITSSLLLGVTGFPGNIVVLSNRCSLGLTEELLLSSLRITASKLSVAEVAAKKRLSEENSGDLKNLILRSLGLLTHSCQLELKETLDALSWIQLGIDLGLIKVTENHPLWNPLFWQIRRAHLALQKQAEDSRDLQKDTISHLRASVLKELTKGLSPESF", "text": "FUNCTION: Catalyzes the specific phosphorylation of arginine residues in proteins. SIMILARITY: Belongs to the ATP:guanido phosphotransferase family."}
{"protein": "MELWRQCTHWLIQCRVLPPSHRVTWEGAQVCELAQALRDGVLLCQLLNNLLPHAINLREVNLRPQMSQFLCLKNIRTFLSTCCEKFGLKRSELFEAFDLFDVQDFGKVIYTLSALSWTPIAQNKGIMPFPTEDSALGDEDIYSGLSDQIDDTAEEDEDLYDCVENEEAEGDEIYEDLMRSESVPTPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFMKPLQRFLKPQDMETIFVNIEELLSVHTHFLKELKDALSGPGATMLYQVFIKYKERFLVYGRYCSQVESAIKHLDQVATAREDVQMKLEECSQRANNGRFTLRDLLMVPMQRVLKYHLLLQELVKHTQDTTEKENLRLALDAMRDLAQCVNEVKRDNETLRQITNFQLSIENLDQSLANYGRPKIDGELKITSVERRSKTDRYAFLLDKALLICKRRGDSYDLKASVNLHSFQVRDDSSGERDNKKWSHMFLLIEDQGAQGYELFFKTRELKKKWMEQFEMAISNIYPENATANGHDFQMFSFEETTSCKACQMLLRGTFYQGYRCYRCRAPAHKECLGRVPPCGRQDFSGTMKKDKLHRRAQDKKRNELGLPKMEVCQEYYGIPPPPGAFGPFLRLNPGDIVELTKAEAEHTWWEGRNTATNEVGWFPCNRVRPYVHGPPQDLSVHLWYAGPMERAGAEGILTNRSDGTYLVRQRVKDTAEFAISIKYNVEVKHIKIMTSEGLYRITEKKAFRGLPELVEFYQQNSLKDCFKSLDTTLQFPYKEPERRAINKPPVGSTKYFGTAKARYDFCARDRSELSLKEGDIIKILNKKGQQGWWRGEIYGRIGWFPSNYVEEDYSEYC", "text": "FUNCTION: Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation."}
{"protein": "QVHHQK", "text": "FUNCTION: Plays a role in attracting adult male S.mansoni to females in vitro."}
{"protein": "MKVAIIFLLSALALLNLAGNTTAKVIGKKANCPNTLVGCPRDYDPVCGTDGKTYANECILCFENRKFGTSIRIQRRGLC", "text": "FUNCTION: In the male reproductive tract, binds to sperm heads where it modulates sperm capacitance by inhibiting calcium uptake and nitrogen oxide (NO) production. FUNCTION: Serine protease inhibitor which exhibits anti-trypsin activity (PubMed:3202973, PubMed:2110056). In the pancreas, protects against trypsin-catalyzed premature activation of zymogens (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTGQPLLGDLLTLASDALPEVEALFETARSALKERVTTDGKVSSKALEEEQFAAHALSWLATYVESLRQMRAWAGRLETEGRFGEMEALILQIAFGEYLAQIRGGIPMSQTETARVQDIGIELGHPGEAVRRLIQAGNTPAARARLVALMRDNHGRATFGASGLDEELEMIRDQFRRFADERVAPHAHGWHMRDELIPMEIVEALAEMGVFGLTIPEEFGGFGLSKASMVVVSEELSRGYIGVGSLGTRSEIAAELILCGGTDAQKAAWLPKLASGEILPTAVFTEPNTGSDLGSLRTRAVKDGDEWVVHGNKTWITHAARTHVMTLLARTDLETTDYRGLSMFLAEKVPGTDADPFPTPGMTGGEIEVLGYRGMKEYEIGFDGFRVKAENLLGGVEGQGFKQLMQTFESARIQTAARAIGVAQNALEVGMQYAEERKQFGKALIEFPRVAGKLAMMAVEIMVARQLTYHSAWEKDHGQRCDLEAGMAKLLGARVAWAAADNALQIHGGNGFALEYQISRILCDARILNIFEGAAEIQAQVIARRLLD", "text": "FUNCTION: Involved in the ethylmalonyl-CoA pathway, a new acetyl-CoA assimilation strategy that operates in a number of bacteria and replaces the glyoxylate cycle. Catalyzes the oxidation of (2S)- methylsuccinyl-CoA to yield mesaconyl-(C1)-CoA. Highly specific for (S)-methylsuccinyl-CoA. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQTKTPVGNTAAICIYPRFIPIARKTLKEQGTPEIRIATVTNFPHGNDDIEIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSLLASLLKALGHGDGKSASSY", "text": "FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily."}
{"protein": "VTAAPAATAATAATPATAALNFAATAATPATPATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAAAAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATAATPATAACNFAATAATPATAATPALIFAATAATAATPATAACNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATAATPATPAFNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALHFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAAFNFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATAALNFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAAFNFAATAATAATPATAATPALIFAATAATAATPATPATPALIFAATAATAATPATPALNFAATAATAATTAARG", "text": "FUNCTION: Antifreeze proteins lower the blood freezing point. SUBCELLULAR LOCATION: Secreted."}
{"protein": "ADVPGNYPLDKDGNTYTCLELGENKDCQKVCKLHGVQYGYCYAFSCWCKEYLDDKDSV", "text": "FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). In mice, causes intense writhing. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MEYQILKMSSCLFILLFLTPGILCICPLQCTCTERHRHVDCSGRNLTTLPPGLQENIIHLNLSYNHFTDLHNQLTPYTNLRTLDISNNRLESLPAQLPRSLWNMSAANNNIKLLDKSDTAYQWNLKYLDVSKNMLEKVVLIKNTLRSLEVLNLSSNKLWTVPTNMPSKLHIVDLSNNSLTQILPGTLINLTNLTHLYLHNNKFTFIPEQSFDQLLQLQEITLHNNRWSCDHKQNITYLLKWVMETKAHVIGTPCSKQVSSLKEQSMYPTPPGFTSSLFTMSEMQTVDTINSLSMVTQPKVTKTPKQYRGKETTFGVTLSKDTTFSSTDRAVVAYPEDTPTEMTNSHEAAAATLTIHLQDGMSSNASLTSATKSPPSPVTLSIARGMPNNFSEMPRQSTTLNLRREETTANGNTRPPSAASAWKVNASLLLMLNAVVMLAG", "text": "FUNCTION: Cell adhesion molecule contributing to the interactive process required for myelination in the central nervous system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor."}
{"protein": "MAPPMTLQQWIIWKKMNKAHEALQNTTTVTEQQKEQIILDIQNEEVQPTRRDKFRYLLYTCCATSSRVLAWMFLVCILLIIVLVSCFVTISRIQWNKDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYVEVNMTSIPQGVYYEPHPEPIVVKERVLGLSQILMINSENIANNANLTQEVKKLLTEMVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFANCYLVKYKEPKPWPKEGLIADQCPLPGYHAGLTYNRQSIWDYYIKVESIRPANWTTKSKYGQARLGSFYIPSSLRQINVSHVLFCSDQLYSKWYNIENTIEQNERFLLNKLNNLTSGTSVLKKRALPKDWSSQGKNALFREINVLDICSKPESVILLNTSYYSFSLWEGDCNFTKDMISQLVPECDGFYNNSKWMHMHPYACRFWRSKKNEKEETKCRDGETKRCLYYPLWDSPESTYDFGYLAYQKNFPSPICIEQQKIRDQDYEVYSLYQERKIASKAYGIDTVLFSLKNFLNYTGTPVNEMPNARAFVGLIDPKFPPSYPNVTREHYTSCNNRKRRSVDNNYAKLRSMGYALTGAVQTLSQISDINDENLQQGIYLLRDHVITLMEATLHDISVMEGMFAVQHLHTHLNHLKTMLLERRIDWTYMSSTWLQQQLQKSDDEMKVIKRIARSLVYYVKQTHSSPTATAWEIGLYYELVIPKHIYLNNWNVVNIGHLVKSAGQLTHVTIAHPYEIINKECVETIYLHLEDCTRQDYVICDVVKIVQPCGNSSDTSDCPVWAEAVKEPFVQVNPLKNGSYLVLASSTDCQIPPYVPSIVTVNETTSCFGLDFKRPLVAEERLSFEPRLPNLQLRLPHLVGIIAKIKGIKIEVTSSGESIKEQIERAKAELLRLDIHEGDTPAWIQQLAAATKDVWPAAASALQGIGNFLSGTAQGIFGTAFSLLGYLKPILIGVGVILLVILIFKIVSWIPTKKKNQ", "text": "FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). FUNCTION: The leader peptide is a component of released, infectious virions and is required for particle budding. FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to the cell receptor. This interaction triggers the refolding of transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic reticulum membrane. Note=The polyprotein has a highly unusual biosynthesis for a retroviral glycoprotein. It is translated as a full- length precursor protein into the rough endoplasmic reticulum and initially has a type III protein configuration with both its N and C- termini located intracytoplasmically (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein Host endoplasmic reticulum membrane; Peripheral membrane protein. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane; Single-pass type II membrane protein Host endoplasmic reticulum membrane; Single-pass type II membrane protein Note=Its N-terminus is located inside the viral particle."}
{"protein": "MEPTPEMKRNRLPSMNFEAEILADPHDNSELYVIPSMRSLTAEEYVEAFQSFLDHSTEHQCMDEFNKEVMPHIMAGLGNGKSTINILGVGSGTGEQDLKMIQILQAAHPGVLINNEIIEPNPQHVAAYKELVNRAPDLQGVSFTWHQLTSSEYEQQVKEKNTHKKFDFIHMIQMLYRVEDIPNTIKFFHSCLNHQGKLLIIILSDSSGWASLWKKYRHCLPSTDSGHYITSDSITAVLRKLGIKYHVYEFPSGWDITECFIEGDPAGGHMMDFLTGTKNFLGTAPAALRSRLQEALCQPECSSRKDGRVIFCNNLSMIVAES", "text": "FUNCTION: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. HNMT family."}
{"protein": "MSAFDPQAHSPPRCGPQFPSIGQEPPEMNIYCESFLHPQTMPSPQRPSNFETGDYSTTANPYLWLNGPSITPPPYLPGSNSSHFMPQAYGMQRQLLPNMHGLGSSELGWLPIPSQEELMKLVRPPYSYSALIAMAIHGAPDKRLTLSQIYQYVADNFPFYNKSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRKRKSDVSPNGQLSSDKPEGSPLSESPTNGEHQDMLGNSSPGTDDSPEKRSPPPSITPCLNNFLSSMTAYVNSATPISRSVPLGLSNETSDKMGQNMVGFNSYTPLSNMPSHGGSDWSSTVSSNPFGYSSSVFNQFTPHFYNSMSTNNTLYNREGTEV", "text": "FUNCTION: Transcriptional activator. Activates ectoderm, in addition to inhibiting mesoderm and endoderm formation; required at the blastula stage for normal formation of both the central nervous system and epidermis, the two early derivatives of the ectoderm. In addition, also required to maintain the regional identity of the animal cells of the blastula, the cells that are precursors of ectodermal structures. Also plays a role in differential adhesion, which limits cell mixing as primary germ layers become specified. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL", "text": "FUNCTION: Selectively catalyzes the oxidative deamination of D- aspartate and its N-methylated derivative, N-methyl D-aspartate. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the DAMOX/DASOX family."}
{"protein": "MIEPSLKALASKYNCEKSICRKCYARLPPRATNCRKRKCGHTNQLRPKKKLK", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL40 family."}
{"protein": "MSHSVKIYDTCIGCTQCVRACPTDVLEMVPWGGCKAAQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGAETTRSMGLAY", "text": "FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side."}
{"protein": "MSVTTATSGALIFSGASLLVSLFAAASIYSQVSSIWTELDNEIDSFKLLTNDIWGDMINLGAGSASNRIRRQAYGGYGATGTNAPEPQFPQGDKGPLPVPGLPFGPNVSGGSDRCQCTVENTCPTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPSQGCFTCPQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGASGMKGDDAEKPVGRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGEEGPRGPSGLPGKDAEYCKCPTRDDGGNSHRAWRRKHKRVY", "text": "FUNCTION: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. Dose-dependent regulator of body length and shape. SIMILARITY: Belongs to the cuticular collagen family."}
{"protein": "MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDDSAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTATVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPATTTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQAPIGNPPVGPIGGMMPPQPGIPQQQGMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY", "text": "FUNCTION: Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly (PubMed:24462186, PubMed:24462187, PubMed:26388440). ZNF207/BuGZ is mainly composed of disordered low- complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks (PubMed:26388440). Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3 (PubMed:24462186, PubMed:24462187). Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3 (PubMed:24462186). According to another report, the stabilization is independent of the proteasome (PubMed:24462187). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Cytoplasm, cytoskeleton, spindle Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding."}
{"protein": "MKLKDLIGKASIHKNKTIAVAHAEDEEVIRAVKLAAEHLSARFLLTGDSKKLNELTSSMQGHQVEIVHANTPEESAKLAVRAVHHKTADVLMKGNVPTSVLLKAVLNRQEGLRSASVLSHVAVFDIPDFDRLMFVTDSAMNIAPSLEELRQILQNAVHVAHAVGNNMPKAAALAAVETVNPKMEATVNAAALAQMYKRGQIKGCIVDGPLALDNAVSQIAAAQKKISGDVAGNADILLVPTIEAGNILYKSLIYFAKASVAAVITGAKAPIALTSRADSAENKLYSIALAICASEEYTH", "text": "FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate. SIMILARITY: Belongs to the phosphate acetyltransferase and butyryltransferase family."}
{"protein": "MNAALDSANALNFQCETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDISAKLNDYEELKRLCLQIQRDRNPSVIVWIGTCTTEIIKMDLEGLAQKLEGEIGIPIVVARANGLDYAFTQGEDTVLASMAQRCPEQVRAEEQETRGGLQALFYGLRSGKKKEEEGFHKHPPLVIFGSVPDPVVTQLTLELKKHGIRVSGWLPAKRYGELPAIEPGTYVVGVNPFLSRTATTLVRRKKAKLITAPFPIGPDGTRAWIEAIARELGIPTQGLAEREAEVWNHPQVRDYRELLRGKSVFFMGDNLLEISLARFLVRCGMTVQEIGIPYMDKRYQAAELALLERTCEEMGVPKPTIVEKPDNYNQIQRIKALQPDLVITGMAHANPLEARGITTKWSVEFTFAQIHGFGNTQALLELVTRPLRRNAALKGLGWERLVREEAPI", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SIMILARITY: Belongs to the BchN/ChlN family."}
{"protein": "MGLFFDSPGSNLYLPCFTLVDAPKLVPLPGVSYKVSFERDSIIHVLSEFKRNNSFKNNHLLDKINTAIAQNEIVVDNSVVNSCKQFHKKYGSDNSNNDAEVQMYIVLLPFEAVNNSVGAASRITAIQVEDDTITITFKSVARVENKQPLLNMQHSLWKSSILEIDDRSELRTWDHKSINKSILSFVKIFYDTDKIIKDFKSKYSLASKRSGDIDSRVLYLSPLANTLFMQLNGSHFNKSWKLLKAYLEQLTVLERNYDTCFELVSMMDLVMSILPMSLKQRLDFLTAKKLKSRAILFSTCVQDFQQIFKKLDDSVDYVNNHFSNSSNNDKSKLIANQLRALRFYIDDIKRNNSSVILKANSEKERTDVTSPNKFLKTSSSHDEDSDSNDEMEQIKSFIDSLEEKNVHPDGIKLLQKDFKRFMKMTPQNADYQVLRNYFDIVMDIPFGKTVNISTIDLAKSRAKLNEDHYGLQSVKRRLVEYLSVLKISEISTNDPNLNTDLHPKKDRASINKPPILLLVGPPGVGKTSIAKSVADVLGRKFQRISLGGIHNEAEIRGHRRTYVGSMCGLIIGALRKAGTMNPLILLDEVDKVLSGGVGGFGNRVNGDPGAALLEVLDPEQNSTFSDHYVGFPVDLSQVLFFCTANDLEGISEPLLNRMELIELPGYTPDEKIMIGSKFLLPKQIKANGLDAIKELPKIYLTDEAWNCVVLEYTREPGVRGLERRIGAIVRGKVVEYVENKMIQGEVDKEHLYKYLGLAHHPISEEILAPTEHSEKFGVVNGLSYNSDGSGSVLLFEVIKIHTDESGATNGPYIKTTGNLGNILEESIKIATSFVKHILFRGLIPGVNEKDINEFLTSEYHLHVPMGAVSKDGPSAGAAISLAILSCALKRPVSPKLCMTGEITLRGKILPIGGIKEKLLGAQFYHMNHVLVPSANLSDVVQAVSTDNQEQYEIYMDRSRQPELQKLKDKTQLQLHYCSDFFDVVKYTWPELLNKEVSHSRPSL", "text": "FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. SUBCELLULAR LOCATION: Peroxisome matrix. SIMILARITY: Belongs to the peptidase S16 family."}
{"protein": "MIFTAPAYAPALPSPLPLQQTIGDFCLAKRRERQGASDSLFIEAAIDRKWTIDDIEARLGRMAAALSSAWNITPGQKWHKTVAILASNCVDTLILSWAVHRIGGGCLMLQPTSSADEMAAHMDRVPPFAMFLSQDLLTLGQEAFQKSSLSSNVPFYSFSGAEAPKPQQTAVPVASQDAPNISTLDDLMATGKELPLLEKTSFSEGEASRRVAYYCTTSGTSGFQRVVAITHENIIASILQAGLFIEATKGPASEVTLAFLPFNHIYGLLITHTFTWRGDSTVVHSGFNMMEILISIGKHRINTLYLVPPIINALSRNASILDRFDMSSVRYIVNGGGPLPKEAFLKMKAARPDWQIIPGWGQTEGCGIGSLSSPKDIFPGSSGVLLPGVRIRLRDDDGRIVQGLEEMGEIEIESPSGLFGYVDYADEALLSPPKEEEFWWPTGDVGLFRISPNGEQHLFIVDRIRDMIKVKGNQVAPGQIEDHLTKHAAVAETAVIGIADEVAGERALAFIVRESSHAREMSEADLRKIIQEHNDLELPEVCRLQDRIIFVDELPKSASGKILKRELRKQVATWSPPQK", "text": "FUNCTION: Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of the lipopeptides W493 A and B (PubMed:25412204). W493 A and B consist of six amino acid residues D-allo-thr, L-Ala, D-Ala, L- Gln, D-Tyr, and L-Val/L-Ile linked to a 3-hydroxy-4-methyltetradecanoic acid polyketide chain (PubMed:25412204). The biosynthesis starts with formation of the linear polyketide chain by the highly reducing polyketide synthase PKS40 (PubMed:25412204). The gene cluster contains a putative acyl-CoA ligase (FPSE_09184) for formation of a CoA thioester polyketide. The thiol bond could be hydrolyzed by the putative thioesterase (FPSE_09186) and then accepted by the first T domain in module 1 of NRPS32 (PubMed:25412204). The second T domain is responsible for accepting a threonine, which is adenylated by the A domain and epimerized to the D-allo-threonine formed by the E domain. The five successive modules incorporate Ala, Ala, Gln, Tyr, and Val/Ile into the final product, which is released by cyclization (PubMed:25412204). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "QECKCHGLSGSCTFTTCWKKMPHFREVGDRLLERFNGAFKVMGGNDGKTIIPVGHNIKPPDKQDLIYSAESPDFCQANRKTGSPGTRGRVCNSTALDVGGCDLLCCGRGQREETVVVEENCLCRFHWCC", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family."}
{"protein": "MSKEIKEYKKYSDVPKEYRFDLDYLLEGKTIDQLFDQFLEKSKKLIKIKDSKYQNIESYLESLKLEEDFNLLNNKIINYISNNISVNVVDSHFREISQKFEFMYYSFFNQIGDENQRILEHEEKITKWLLDPRLASYKKALDFVFKSKKHRLSKEVEDYLIKVSRGNIELYKVYGILTNSELDYGYALSSDGKRKIEINLSNRFNLLKDQDENIRKTTYLNWNKASAKHKETLSSLLYQHFSKLSADALARGYSSTVNSFLFEDQVDEKLLKNLYDKVSSNKKVFQKYYQNYKKFFEKKNSKQMEAWDIYLPLVVVDEKYSIEEAQDLVLKSLEPMGSEYISKVKEAFSSRWVDYLPVKNKRSGAYSIGSTHGIDKKFILMNFDGTLNSVSTLSHEMGHSMHSYFSDKTQPQSLSSYPIFLAEIASIFNELMLKDYLLEVSENLETKFHILNESILNFVGTVHRQTLWSEYEYTLYNKIDKGEPVGTYTKIDEIYEQISQKYKVSDLKNHHPEDEKNVIGVNVPHFYYHFYVYKYAIGMIVANVFYQKYKEEGKQALEFYINKFLSAGGRDWPVEILKDAGIDLYDSKIYDLAFKNFEQTIDQFVEIGNKLFK", "text": "SIMILARITY: Belongs to the peptidase M3B family."}
{"protein": "MAKPAKRVAVTGAAGQIAYSLLFRIANGDLLGKDQPVILQLLDLPQAQAAVKGVVMELDDCAFPLLAGVVITDDPKVAFKDADVALLVGARPRSKGMERKDLLSANAEIFTVQGAALNEVASRDVKVLVVGNPANTNAYIAMKSAPDLPKKNFTAMLRLDHNRALSQLAAKSGKPVASIEKLAVWGNHSPTMYPDFRFATAEGESLLKLINDDAWNRDTFIPTVGKRGAAIIEARGLSSAASAANAAIDHVRDWVLGTNGKWVTMGIPSDGSYGIPEDIIYGVPVTCENGEYKRVEGLEIDAFSREKMDGTLAELLEERDGVAHLLK", "text": "FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MRLPGVPLARPALLLLLPLLAPLLGTGAPAELRVRVRLPDGQVTEESLQADSDADSISLELRKPDGTLVSFTADFKKDVKVFRALILGELEKGQSQFQALCFVTQLQHNEIIPSEAMAKLRQKNPRAVRQAEEVRGLEHLHMDVAVNFSQGALLSPHLHNVCAEAVDAIYTRQEDVRFWLEQGVDSSVFEALPKASEQAELPRCRQVGDHGKPCVCRYGLSLAWYPCMLKYCHSRDRPTPYKCGIRSCQKSYSFDFYVPQRQLCLWDEDPYPG", "text": "SIMILARITY: Belongs to the OAF family."}
{"protein": "MNFKYIVAVSFLIASAYARSVKNDEQSLSQRDVLEEESLREIRGIGRKFLGGVKTTFRCGVKDFASKHLYGKRTAEEHEVMKRLEAIMRDLDSLDHPEEASERETRGFNQDEIANLFTKKEKRILGPVLGLVGNALGGLIKKIG", "text": "FUNCTION: Maximin-9 shows antimicrobial activity against bacteria and against the fungus C.albicans. It has little hemolytic activity (By similarity). FUNCTION: Maximin-H3 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
{"protein": "MACLKGAKGTVQDAPDFNDKEDAETLRHAMKGLGTDEDTILKLLISRSNKQRQQIALTYKTLFGRDLTDDLKSELSGKFETLLVALMVPAHLYDACELRNAIKGLGTLENVIIEIMASRTAAEVKNIKETYKKEFDSDLEKDIVGDTSGNFERLLVSLVQANRDPVGKVDEGQVENDAKALFDAGENKWGTDEETFISILSTRGVGHLRKVFDQYMTISGYQIEESIQSETGGHFEKLLLAVVKSIRSIQGYLAEVLYNSMKGAGTDDQTLIRVLVSRSEIDLFNIRQTFRKHYGKSLHAMIQSDTSGDYRNALLLLCGEIDD", "text": "FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. SIMILARITY: Belongs to the annexin family."}
{"protein": "MTEFGIRNMDQVAPVYNGHRGMLKRQLAFDNVQVPTSLYCGLFSAYEEEQAVPTGLDSYPHDSSSCELPLLTPCSKAVMSQALKDTFNGFAKERCRLGIPGNPWLWDENNVLQWLLWAAKEFSLENVNFQKFLMNGHELCSLGKERFLALAPDFVGDILWEHLEEMMKEYQEKAQEPYIDHSNRDSLNQWMNADSLNFTADPLQCGAQVHNYPKNGMYNDMCSVPTGQTLLNPKQEFQQYPSSCLKSRAVNYPPASQDFARSHMNVLLNSLNSGKLRDYDSGDSGTESFESTESLLHSWTSQSSLVDMQRVPSYDSFEEDGNQTLCLNKQPMSFKDYIQDRCEPAELGKPVIPASILAGFTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLADPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTSGKRYVYRFVCDLHNLLGYTPDELHAMLGVQPDTDE", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family."}
{"protein": "MKNRILRPALLCVAALFATTAQADAGHDHGSAHAGAHAHDADTPYGRPGDAAKAQRTVRVVMSDTMRFDPATITVRRGETVRFVAANGGRIEHEFVLGTTASLKAHAQEMRAMPDMQHADPGAVRVAAGASGEIVWQFTKAGSFEFACLIPGHFEAGMVGKVVVR", "text": "FUNCTION: Involved in copper tolerance (PubMed:26396241, PubMed:34791351). Required for copper resistance under both aerobic and anaerobic photosynthetic growth conditions (PubMed:26396241). Binds copper (PubMed:26396241, PubMed:34791351). Could be an important defense against copper in the periplasm and may protect not only c type cytochromes but also other proteins with cysteine residues from copper ions that may catalyze nonnative disulfide bond formation (PubMed:26396241). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the CopI family."}
{"protein": "MCSVCEGSAEGLVTRKRTHSGGGRSAGSKRKWHRRMGGLSFLIFFVIGSLFSGLMFALLSYAPSYRSRVTPHYLPDGRFLQIADEARVLEPYLSAAVRLPDSLNGTPAGKQQQTARSNEQEALSSLKVAVEMKLMGKDDKALRLFQHAMALSPRHPEILTKYGEFLEHSQQDIVTADHYYYQALTVNPSHSEALANRQRTASIVEHLDQKRFERLDKKRDALSSVHALDAGLKRAEKEAYIQHIYHSVGIEGNTMSLAQTRSILETKMAVDGKSIDEHNEILGLDAAMKYINATLVNKNDFITLKDLLEIHRRVLGHVDPVEGGEFRRTQVYVGGHIPPGPGDLSILMSRFEGWLNAEQSFLMHPVRYAAMAHYKLVHIHPFSDGNGRTSRLLMNTLLMRAGYPPVIIQKQHRHKYYDYLQVANEGDIRPFVRFIADCTERTLDLYLWATSELSHPVPLLAQEEMGGAIGEREHGFGREGGSTVHEGSGTGDSIRIGTMW", "text": "FUNCTION: Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-251 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). SUBCELLULAR LOCATION: Membrane; Single- pass membrane protein. SIMILARITY: Belongs to the fic family."}
{"protein": "MKNMLLLSSSKYKNTGYLEHTLPWLQNFLADYRGKTIAFVPYAGVSRTFDEYEKTVQNALSDLGMNIVSVHHGKQHRDIIEQADVISIGGGNTFCLLKQLYEHNLIDIIREKVNNGTPYFGWSAGANVAGASIMTTNDMPITYPPSFQALQLFPHQINPHFISGKMQGHNGESREERLAEFLLVNPTALVYALPEGSALHIQNEMATVLGENPILCFSENMECGTFDINTTFSY", "text": "FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S51 family."}
{"protein": "MEDIIYITGHKNPDTDSICSAIAYSELKNKLGFNTVPGRLGNISRETEFALNYFKANAPKLLENLSSNQDIIIVDHNERAQSVDNLEDLHLLEIIDHHRIADIQTSYPIFFRNEPVGCSSTIIGSMYFEKGIEPSKRAAGLMCSAIISDTLLFRSPTTTARDKEVLKKLAKIADIDPEKYASEMFKAGTSLKGKTVEEIFNSDYKAFNLGDKKIGVSQVTTMDIEGFDEYKKDMLAYMNKKVKDENFNAVLLLLTDIIKEGSLIIATGENTDLVNKAFNVELKDNAVYVPGILSRKKQVIPPLTSAIEGK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase class C family."}
{"protein": "MHRNNERINLEKSNDWANTNEPSIACFLNSLARESQSVQLLWGEDGKRVYRLPLANSDSINIPLSYFSSLGSHEYCLPALLHTQDSIKTLSVEQLIEHIVNEPALVGIVSEAKKAIFTKRVLESHRNTEQAIEHSPYQEQLFTEQLDFKTAEQGLLIGHSFHPAPKSREQFSLSDAKLYSPELGGQFKLFWLSVEQSLLTSGSSADIHFNQRFEALVAHDPKLVEALQNAQQQGHELLPVHPWQWHVMVENPSIKGYIATKQIQNLGQLGATWYPTSSTRSLYAPGLPYMLKFSLSVKLTNSIRNLSLKECDSWNDLNDLFQHPQLAQQLGNGRGFQLMQEPAYIGLKDLNGKIIDESLVAFRDNPLMNNPAEEAVVLATLTQQNPYGGSSLVAARIEHYATQQHLSLHQAASLWFDAYCRHAVVPLFHLQANFGIVFLAHQQNIVMQLEQGFPVGMYYRDCQGTGYTDLAFKLFGEQLGDRKEALENYWNQDKVRRYFAYYLIINSTFNLISAICANLDVEESELIEILYHNLNALLQSGVKDDLCLRYVLTSEALCCKGNFFCYLQNFNENSIPDPAVIYFDLPNPLARVEEIAHV", "text": "FUNCTION: Catalyzes the attachment of a first N-acetyl-N-hydroxylysine to a carboxylic group of citric acid to yield N-citryl-N-acetyl-N- hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions. SIMILARITY: Belongs to the IucA/IucC family."}
{"protein": "MLGQMMRNQLVIGSLVEHAARYHGAREVVSVETSGEVTRSCWKEVELRARKLASALGKMGLTPSDRCATIAWNNIRHLEVYYAVSGAGMVCHTINPRLFIEQITYVINHAEDKVVLLDDTFLPIIAEIHGSLPKVKAFVLMAHNNSNASAQMPGLIAYEDLIGQGDDNYIWPDVDENEASSLCYTSGTTGNPKGVLYSHRSTVLHSMTTAMPDTLNLSARDTILPVVPMFHVNAWGTPYSAAMVGAKLVLPGPALDGASLSKLIASEGVSIALGVPVVWQGLLAAQAGNGSKSQSLTRVVVGGSACPASMIREFNDIYGVEVIHAWGMTELSPFGTANTPLAHHVDLSPDEKLSLRKSQGRPPYGVELKIVNDEGIRLPEDGRSKGNLMARGHWVIKDYFHSDPGSTLSDGWFSTGDVATIDSDGFMTICDRAKDIIKSGGEWISTVELESIAIAHPHIVDAAVIAARHEKWDERPLLIAVKSPNSELTSGEVCNYFADKVARWQIPDAAIFVEELPRNGTGKILKNRLREKYGDILLRSSSSVCE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MPKLGMQSIRRRQLIDATLEAINEVGMHDATIAQIARRAGVSTGIISHYFRDKNGLLEATMRDITSQLRDAVLNRLHALPQGSAEQRLQAIVGGNFDETQVSSAAMKAWLAFWASSMHQPMLYRLQQVSSRRLLSNLVSEFRRELPREQAQEAGYGLAALIDGLWLRAALSGKPLDKTRANSLTRHFITQHLPTD", "text": "FUNCTION: Repressor involved in the biosynthesis of the osmoprotectant glycine betaine. It represses transcription of the choline transporter BetT and the genes of BetAB involved in the synthesis of glycine betaine (By similarity). FUNCTION: Repressor involved in the biosynthesis of the osmoprotectant glycine betaine. It represses transcription of the choline transporter BetT and the genes of BetAB involved in the synthesis of glycine betaine."}
{"protein": "MTAWRDTLGRIGVRAMPGAGGFWRWWQQSLLAWLPQRWQWQLGLSQSRLLLQLDGEALQLLRQRDQTSDTVASLPWPVQPQEVNALLPTALEGLPQHWLLPASHALRRPLRLPAAAAARLQDVARFEIDRQTPFTADQVYFDARVLDVREDGQLDAELVVVPRRMIDGPAGVPEAWSNALSGIDVADARGAPLGVNLLPPARRLRRSDPMQRWNLLLAVAALVLLAVAGWLLLDNRRQAADDLRAQVQANAGRARQVAAERQQLLELVEGAAFFQEQRATRPTSVEIWDELSRRLPSGTYLEKFSVEGGQLQLIGLSKEASSLVRRLEGSPLWHTPSLTGVLQSDAGRNVDRFTITAELAGPDAKEAADAAQR", "text": "FUNCTION: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits XpsM resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing XpsE protein in the cytoplasm and the rest of the T2SS machinery. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP L family."}
{"protein": "MNLKTHAFNDRGRIPSRYTCDGENISPPLSWDGVPGEAKSLALICDDPDAPSKVWTHWVIFNIPPDSTGLEENVPDAGRLPDGSVQGYNDSGTLGYRGPCPPSGVHRYFFRLYALDTVLDLEPGASKEDVLEAMEGHVLGEAKLIGLYRRG", "text": "SIMILARITY: Belongs to the UPF0098 family."}
{"protein": "MSRSVFSTLRPVIGQKTTLAPFAFSLRHASSSSSPFSTPTEPTSFHTQPSHSTPTGPLPLTWPSYLSLRRQRRLWSTLTSVPTTFLGLFLGGGYFASLEADPSQLIFGVEPMFVYGGATLGCMALGYLIGPSVGATLFSLTHPSIARGNPAPLEVMDREFYHRIRKNRADPRFQSVQNIVPDFYGEKIVSLSTYRRWLRDQAVYKRKAMHGVPGEDL", "text": "FUNCTION: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PAM17 family."}
{"protein": "MNQPTSRSGLTTFTVIIIGLLALFLLIGGIWLATLGGSIYYIIAGVLLLIVAWQLYKRASTALWFYAALMLGTIIWSVWEVGTDFWALAPRLDILGILGLWLLVPAVTRGINNLGSSKVALSSTLAIAIVLMVYSIFNDPQEINGEIKTPQPETAQAVPGVAESDWPAYGRTQAGVRYSPLKQINDQNVKDLKVAWTLRTGDLKTDNDSGETTNQVTPIKIGNNMFICTAHQQLIAIDPATGKEKWRFDPKLKTDKSFQHLTCRGVMYYDANNTTEFATSLQSKKSSSTQCPRKVFVPVNDGRLVAVNADTGKACTDFGQNGQVNLQEFMPYAYPGGYNPTSPGIVTGSTVVIAGSVTDNYSNKEPSGVIRGYDVNTGKLLWVFDTGAADPNAMPGEGTTFVHNSPNAWAPLAYDAKLDIVYVPTGVGTPDIWGGDRTELKERYANSMLAINASTGKLVWNFQTTHHDLWDMDVPSQPSLADIKNKAGQTVPAIYVLTKTGNAFVLDRRNGQPIVPVTEKPVPQTVKRGPQTKGEFYSKTQPFSDLNLAPQDKLTDKDMWGATMLDQLMCRVSFKRLNYDGIYTPPSENGTLVFPGNLGVFEWGGMSVNPDRQVAVMNPIGLPFVSRLIPADPNRAQTAKGAGTEQGVQPMYGVPYGVEISAFLSPLGLPCKQPAWGYVAGVDLKTHEVVWKKRIGTIRDSLPNLFQLPAVKIGVPGLGGSISTAGNVMFVGATQDNYLRAFNVTNGKKLWEARLPAGGQATPMTYEINGKQYVVIMAGGHGSFGTKMGDYLVAYALPDNK", "text": "FUNCTION: Catalyzes an exceptionally high rate of oxidation of a wide range of aldose sugars, including D-glucose, galactose, arabinose and xylose, and also the disaccharides lactose, cellobiose and maltose. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein; Periplasmic side. SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family."}
{"protein": "MMERFEKIEMKIPAKAEYVAIIRLTMAGVANRTGFAYDDIEDMKIAISEACTNIVQHAYKEDVGEIAIVFGLYEDRLEIMVADNGVSFDFNNLRSKVGPYDISKPVEHLPENGLGLYLINTLMDDIQIMHDEGMTVLMTKYIQREQVENDGNPISTYNSY", "text": "FUNCTION: Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). SIMILARITY: Belongs to the anti-sigma-factor family."}
{"protein": "MSETDRERPLLASEERAYEETEKVLIVGIDEEEDADYDDDPGNSPKFSWKKLWLFTGPGFLMSIAFLDPGNLESDLQAGAIAGYSLIWLLMWATAIGLLIQLLSARLGVATGRHLAELCREEYPTWARMVLWIMAEIALIGADIQEVIGSAIAIKILSNGLVPLWAGVVITALDCFIFLFLENYGIRKLEAVFAILIATMALAFAWMFGQTKPSGTELLVGALVPKLSSRTIKQAVGIVGCIIMPHNVFLHSALVQSREVDPKKRFRVKEALKYYSIESTGALAVSFIINVFVTTVFAKSFYGTEIADTIGLANAGQYLQDKYGGGFFPILYIWAIGVLAAGQSSTITGTYAGQFIMGGFLNLKMKKWVRALITRSCAIIPTMIVALVFDSSDSMLDELNEWLNVLQSVQIPFAVIPLLCLVSNEQIMGSFKIQPLVQTISWIVAALVIAINGYLMVDFFSGAATNLILLVPVIIFAIAYVVFVLYLISRGLTYTPWQLVASSHKEPQRDDE", "text": "FUNCTION: Vacuolar metal transporter involved in intracellular metal homeostasis. Can transport iron (Fe), manganese (Mn) and cadmium (Cd). Regulates metal accumulation under Fe starvation. Acts redundantly with NRAMP3 to mobilize vacuolar Fe and provide sufficient Fe during seed germination. In association with NRAMP3, required for optimal growth and photosynthesis under Mn deficiency. Exports Mn from vacuoles in leaf mesophyll cells, making Mn available for functional photosystem II in chloroplasts. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family."}
{"protein": "MAENPIYGPFFGVMGAASAIIFSALGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSLDAPSNNYTLYKGFIHLGAGLAVGFSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVAIYLYTKQ", "text": "FUNCTION: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family."}
{"protein": "MDERAVLEELKKYRKMDLKYEDGAILGSMCTKPHPITKKISDMFFETNLGDPGLFRGTKKLEDEVINNIGKFLNNPNPFGYIISGGTEANITAMRAINNIAKAKRKNHKTTVIMPETAHFSFEKAREMMDLNLITPPLTKYYTMDLKYINDFIEDRNNKNDISVDGIVGIAGCTELGAIDNIKELSKIAEQNNIFLHVDAAFGGFVIPFLDDKYKLDNYCYEFDFSLNGVKSMTVDPHKMGLAPIPAGGILFRDKSFKKYLDVEAPYLTDIHQATIIGTRSGVGVASTWGVMKLFGEEGYKNLASECMDKTHYLVKEAKKLGFKPVIDPVLNIVALEDDNPEETSLKLRKMGWFISICKCVKALRIIVMPHVEKEHIDKFLGALTEVKKN", "text": "FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine for methanofuran biosynthesis. Can also catalyze the decarboxylation of L-aspartate to produce beta-alanine for coenzyme A (CoA) biosynthesis. SIMILARITY: Belongs to the group II decarboxylase family. MfnA subfamily."}
{"protein": "MTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVLAGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIVGLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEEKKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDFFSMKGNGYKKATVEPLKDDDFYFEDEKEQI", "text": "FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small chain family."}
{"protein": "MDTRDDVTLAKVPAPVAVYCGSVPRTSVGLRAPPPGGIDSSLLAHDEASLQPVSSVLPSSEKPSQLSREHEDQSSLMLNAPLKGWQARNGYPRGLGVLPLGHHLGAAIPSLESEASSVARDTIQIKDKLKKRRLSEGMAASSQASLDPVGGPRGVPLRSTIPRTTSQRLLRVPRPMPPIQSIPTTPEANSAKEKDLDPPGGRQDLQDPGASAQEVQISRQYLHCADEKMHKSLGGLVIPPIPKARMPTGTSSCRPGSLPSPLCPSQDVLMGPKAPHTRLTCENGPLEKTPKSPASKPLVPVVKAKSAEAPETSLASSQSTFTLTAFSSHAKETRSLENEEDQKESSTKVQVTISKSAQEKMRLKQMKEMELLRRAKEPEWERELVSQGLGTRRTSAKEGLLPLRGSGALSEPAGMSSPRRNNMGALQRKRANRASLPSIPVSKQEPGFARHASANSLPAVLTLGSPEWEEEEEEMDLRALRELRPFSNPELGLTDALQCLNSNDWQMKEKGLVNIQRLAACHSEVLGTRLHDVSLAVTAEVTNLRSKVSRLAISTLGDLFRVLKKNMDQEAEEIVRCLLQKMGNTSEFIQRAANRALGAMVENVTPARALVALTSAGVYHRNPLVRKCTAKHLSAVLEQIGAEKLLSGSRDNTDMLVHNLVRLAQDSNQDTRFYGRKMVNILMANAKFDAFLKQSLPSHDLRKVMAAIKQRGIQDNHELQSAKGRKVSKSLVVCENGLPSHEGVETSEQLRELTRLLEAKEFQARMEGVGKLLEYCKAKPELVAANLVQVFDVFTPRLHDSNKKVNQWALESLAQMLPILKESIHPMLLSLIIAAADNLNSKNSGISTAASTVLDAMMGSLDHLCLLQAFAGRVRFLTGPAVLDITDRLSVLVASVYPRKPQAVERHILPVLWYFLNKMSGNGVLPGRGGNVRTAVCRLARSLQEQMGSRLQDFAASQPQQVLKALQGLLASESLGANDKVIGGRMAPDIQMTGTTCPQQLD", "text": "SIMILARITY: Belongs to the Crescerin family."}
{"protein": "MPALALVDTPVDAFSGDCSGVFIPPSPNSSSASLDWSPSLSSSLYRIDGWGAPYFAANSSGNISVRPHGSNTMPHQEIDLTKVVKKATDPKSSGGLALQFPLIVRFPDVLKNRLESLQSAFEFAIQTQGYESRYQGVYPVKCNQDRFIIEDIVEFGSSFRFGLEAGSKPEILLAMSCLCKGSPEAFLVCNGFKDAEYVSLALLGRKLQLNTVIVLEQEEELDLVIALSKKVNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQIIRVVRKLRDVGMLDCLQLLHFHIGSQIPSTALLSDGVSEAAQLYCELVRLGARMEVIDIGGGLGIDYDGSKSGESDLSVAYSLEEYAAAVVASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAGKRHETTPSDLQFLLEGYSEEARGDYENLYDAVMRGDRESCLLYVDQLKQRCVEEFKEGSLSIEQLAGVDGLCEWVTKEIGGSDPVLTYNVNLSVFHSIPDFWGIDQLFPIVPIHRLDQRPVARGILSDLTCDSDGKINKFIGGESSLPLHELDNNGYYLGMFLGGAYEEALGGVHNLFGGPSVVRVLQKDGPHGFAVTRAMMGQSSADVLRAMQHEPELMFQTLKHRAEELSLVHKPGGDKGNDKLVASCLARSFNNMPYLSVGTSTNALTAAINNLVYYSDEAAVGNGGGCGKNGKWSYSVD", "text": "SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily."}
{"protein": "MSSEQLQDPVEPDKILSAVTQRGLRLESILTTHHHLDHAGGNLDLVTKCRKQGLEGLKVYGGDDRIGGLTDTVSHGYKXRLVATSTFIAWLHHRHTTGHICYLVTEENSTKEGAVFTGDTLFLGGCGRFFEGTAEQMFKALIEVLSKLPTTTKVYCGHEYTVKNLEFGLTVEPKNEALKHRLEAVKRLRASNQASVPGTIGEELATNPLMRVSEPDVLAHAKTTDPIKAMKTIREEKDRF", "text": "FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family."}
{"protein": "MITLAVKVGMIQLCGCSGCHISLLDLHDKLLEVLPNLEIVYAPIIADPKEIPEGIDVFLVEGGIRNEHDEHLIHEIREKSKIVIAWGTCAAYGGIPGLGNLYKKEELLNYVYSTDSTENKGEIPSEEIPPLEEYVKPIKDFIKVDYTIPGCPPTPKMIADAIIALLNGEEPKLPTKIVCDECPRKKENVFPETFKRTHEGRPDPERCLFEQGYTCLGFATRAGCGAKCPSAGVPCRGCFGKTDKSLDLGANAANVLANAGEAALEIPDKVALLNRFTLPDALINRKAK", "text": "SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family."}
{"protein": "MLATKVCFVTVGATASFEELVRAALDPSFVTALEENGYSHLLVQYGKNAVIYENFLKQYPPERRPWRRINISGFSFHEHGLGGDFALAQADISKGRSGGLVISHAGSGTILEVLRMGIPLIVVPNPSLQDNHQEELARQLQKQGYVVASHYQNLCQALHQAEQLRARMLRWPPVRGPDQKNQPTLEQVMSDEMGFVD", "text": "FUNCTION: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 28 family."}
{"protein": "MKKRAIVAVIVLLLIGLDQLVKSYIVQQIPLGEVRSWIPNFVSLTYLQNRGAAFSILQDQQLLFAVITLVVVIGAIWYLHKHMEDSFWMVLGLTLIIAGGLGNFIDRVSQGFVVDMFHLDFINFAIFNVADSYLTVGVIILLIAMLKEEINGN", "text": "FUNCTION: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A8 family."}
{"protein": "MSAHKVQIGLSSGQFRVALQVPSVRLKGLGSFHTGSIVLPSQGSLREDQISLHNQDGLHKVMREVLGYERNSYKKFFLR", "text": "FUNCTION: Has antifungal activity against C.albicans. Has antibacterial activity against the Gram-positive bacterium S.aureus and the Gram- negative bacterium E.coli. Lacks hemolytic activity against rabbit erythrocytes."}
{"protein": "MNEQTYLLASAVEPVAAENMSWTQTLVLSVVQGLTEFLPISSSGHLRIISELFWGADAGASFTAVVQLGTEAAVLVYFAREIWQILTGWFAGVFNKDRRGRDYKMGWMIIVATIPVVVLGVLGKDLIRDALRNMWITATVLVLFSFVFILAEKVGKKDRGYDELNMRDALVMGFAQCLALIPGVSRSGGTISAGLFMGLNREVAAKFSFLLAIPAVLGSGLYSLPDAFDPSTGQAASGLQLTIGTLVAFLVGYASIAWLMKFVANHSFSWFAAYRIPAGLLVMLLLWLGYLNP", "text": "FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family."}
{"protein": "MALVAGLRAFGAKWPSWLRRSPWAPLSAGFCSPGSARPAGPESEPRLTSTRQQDGIRNIVLSNPRRRNALSLAMLKSLRSDILHEAESEDLKVIIISAEGPVFSSGHDLKELTGAQGRDYHTEVFQTCSEVMMLIRNHPVPIVAMVNGLATAAGCQLVASCDIAVASDKSSFATPGVNVGLFCSTPAVALGRAVPRKVALEMLFTGEPISAQEALRHGLISKVVPEEQLEEEATRIAKKIASLSRSVVALGKATFYKQLPQDLSTAYFLASQAMVDNLTLKDGQEGIEAFIQKRRPVWSH", "text": "FUNCTION: May play a role in fatty acid biosynthesis and insulin sensitivity. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MAWQVSLLELEDRLQCPICLEVFKESLMLQCGHSYCKGCLVSLSYHLDTKVRCPMCWQVVDGSSSLPNVSLAWVIEALRLPGDPEPKVCVHHRNPLSLFCEKDQELICGLCGLLGSHQHHPVTPVSTVCSRMKEELAALFSELKQEQKKVDELIAKLVKNRTRIVNESDVFSWVIRREFQELRHPVDEEKARCLEGIGGHTRGLVASLDMQLEQAQGTRERLAQAECVLEQFGNEDHHEFIWKFHSMASR", "text": "SIMILARITY: Belongs to the TRIM/RBCC family."}
{"protein": "MVAVPTSTASLQALPQYVVADIDLADFGRKELSIAETEMPGLIALRIKYGSEKPLKGARIAGSLHMTIQTGVLIETLVALGADVRWASCNIFSTQDHAAAAIAASGVPVFATKGETLDEYWAYTHRILEWGDGGTPNMILDDGGDATGLVMLGSKAESDSSVLDNPGNEEETALFASIRTKLAEDSSFYSRIKSSIQGVTEETTTGVARLYQMQKSGELPFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMVAGKVALVMGYGDVGKGSAQSLRGLGATVMIAEIDPICALQAAMEGYRVVRLDEVVQDVDIFVTSTGNFQVIRHEHLIRMKDEAIVCNIGHFDNEIDVASLKDYPWENIKPQVDHITLPSGNKIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFSKGDQYADQVYVLPKHLDEMVARLHLEKIGARLTELTKQQADYISVPVEGPYKPDHYRY", "text": "FUNCTION: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenosylhomocysteinase family."}
{"protein": "MRTSSMMKRMAAMSLAAAAAWATGAAAAADGAPAAQRTIQVLSVKGGDAASPQAAVWKKAPTGQVALQTAFPGHASIVGTALTQQMTAQAVRAGDRLFVRLAWRDATANTEIKDTDQFVDGAAVQFPVNGKDTTLAFMGDPDNPVNVWHWRADGRTRNLVAKGFGTATPVPAEGLRSTATRTRDGWEVVISRPLRVKAEEGADLQGRRTMPIAFAAWDGENQERDGLKAVTMEWWQLNF", "text": "FUNCTION: May transfer electrons to the iron-sulfur centers of SerB. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MMLPLQGAQMLQMLEKSLRKSLPASLKVYGTVFHINHGNPFNLKAVVDKWPDFNTVVVCPQEQDMTDDLDHYTNTYQIYSKDPQNCQEFLGSPELINWKQHLQIQSSQPSLNEAIQNLAAIKSFKVKQTQRILYMAAETAKELTPFLLKSKILSPNGGKPKAINQEMFKLSSMDVTHAHLVNKFWHFGGNERSQRFIERCIQTFPTCCLLGPEGTPVCWDLMDQTGEMRMAGTLPEYRLHGLVTYVIYSHAQKLGKLGFPVYSHVDYSNEAMQKMSYTLQHVPIPRSWNQWNCVPL", "text": "FUNCTION: Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate numerous substrates to form a variety of N- acylglycines, with a preference for benzoyl-CoA over phenylacetyl-CoA as acyl donors. Thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the glycine N-acyltransferase family."}
{"protein": "MDSVNDSLVILDIKYWTNHNNKKIFDKNLMKFLKKDYFRKIPSTKHKDLPAIPFPNYHVCSNVKCSRLFDLRDNFVMSDYLKGGPKCPDCSRKSYPARFVVSCQENHLDDFPWRWWAHGKQDTECKGKLRLWSTGNTSSLDSLYVECECKKKKSLRGAMQDSSFENYKCTGNHPHKLNEKSNCNEPVIPLQRGASNVYFPALRSAIVIPSNASEDNNLDDFFTSVKEVINTYADLIGENWHYKFYSDRLTGHSEFSDAEDFIAKWTSYLNSNDSEEEIEYNQIKEAEYRAFTAFDRKVKMGDFEAEVETVPDDFQPYFNRIVKAHRLKEILVLLGFMRNDSPEPDVNEPKKIVWLESDGYENWLPAIEVHGEGIFIEFNHTTISKWLEENSELPKRSEKFSSLYASWIESKGWEVRDEKDIVYVMLHTFAHLLIKQLSLQSGYSSVAIKERIYCGKNMAGVLLYTGSTDQEGSLGGLVEMGSIDKLRPLIVDALEEAIFCSNDPSCASLEPSEDNQLNGCACFACSMVAETSCETGNRLLDRSLLVKTIDSKYSPFFKGLL", "text": "FUNCTION: Component of antiviral defense system DISARM (defense island system associated with restriction-modification), composed of DrmE, DrmA, DrmB, DrmC and DrmMII. DISARM is probably a multi-gene restriction module, this subunit has an unknown function. Expression of DISARM in B.subtilis (strain BEST7003) confers resistance to phages Nf, phi29, phi105, phi3T, SPO1, SPR and SPP1. Protection is over 10(7)-fold against phi3T, 10(4)-10(5)-fold against Nf, phi29, phi105 and SPR, 100- fold against SPO1 and 10-fold against SPP1. DISARM does not interfere with phage adsorption, but instead interferes with (phi3T) DNA replication early in its cycle, preventing replication, circularization and lysogeny and probably causes phage DNA degradation (DNA is degraded in SPP1-infected cells). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MLCRSFNISQLAIPFVSVLISFLAYTSQLFFYYFEEAPLRSEEFWRLNIFAVCIWVCYYRACTVDPGRIPKDWTPPNLKQLEKDCAGGRQRWCRRCEAFKPPRAHHCKTCQRCIPKMDHHCPWTSNCVSHFTYPHFMRFLFYAVVGMGYLETLLFERASIVWASRHLPSYLGPGLGQLVHLFILLVVNSLTWLALFILLLRSIWSLALNTTTIESWEIERHETLLRRARHFGGYLSGPGGIQIRIKKQEFPYDIGIWSNIRAGMGGSANVLSWFWPFAATPDRSTGLEFEVNGFEDPNLSWPPPDPDRIPLPAKREDMSAAIAAADASYHRALQARNIQRSNDASHSGGHPIQRRKRFHDRFNENKAKERLSESESDFSDDEEVQDGEEGWKNSEGDRLRDFGVDEEAEFYDEEDIPLGILMQRRRQQ", "text": "FUNCTION: Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4 subfamily."}
{"protein": "MDSLGAVSTRLGFDLFKELKKTNDGNIFFSPVGILTAIGMVLLGTRGATASQLEEVFHSEKETKSSRIKAEEKEVIENTEAVHQQFQKFLTEISKLTNDYELNITNRLFGEKTYLFLQKYLDYVEKYYHASLEPVDFVNAADESRKKINSWVESKTNEKIKDLFPDGSISSSTKLVLVNMVYFKGQWDREFKKENTKEEKFWMNKSTSKSVQMMTQSHSFSFTFLEDLQAKILGIPYKNNDLSMFVLLPNDIDGLEKIIDKISPEKLVEWTSPGHMEERKVNLHLPRFEVEDGYDLEAVLAAMGMGDAFSEHKADYSGMSSGSGLYAQKFLHSSFVAVTEEGTEAAAATGIGFTVTSAPGHENVHCNHPFLFFIRHNESNSILFFGRFSSP", "text": "FUNCTION: May play a role in the proliferation or differentiation of keratinocytes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily."}
{"protein": "MLRGQQIWLSNLTQPQTSAGPVPAVESPPALCSTSLPQVCLDPASPALLPKPTWTLSWSRPGSCVMPGAAAASLLSPRTLRLESPRGAGLSLMRPRPFPLICCCSTCSGPPPSTFLATRIRSQPSILSTPGSFPPSGPIWPPPPGGMLPIAALRMYVS", "text": "FUNCTION: Acts by interacting with multiple viral and host proteins to enhance the activity of viral RNA-dependent RNA polymerase."}
{"protein": "MPLQVSDYSWQQTKTAVFLSLPLKGVCVRDTDVFCTENYLKVNFPPFLFEAFLYAPIDDESSKAKIGNDTIVFTLYKKEAAMWETLSVTGVDKEMMQRIREKSILQAQERAKEATEAKAAAKREDQKYALSVMMKIEEEERKKIEDMKENERIKATKALEAWKEYQRKAEEQKKIQREEKLCQKEKQIKEERKKIKYKSLTRNLASRNLAPKGRNSENIFTEKLKEDSIPAPRSVGSIKINFTPRVFPTALRESQVAEEEEWLHKQAEARRAMNTDIAELCDLKEEEKNPEWLKDKGNKLFATENYLAAINAYNLAIRLNNKMPLLYLNRAACHLKLKNLHKAIEDSSKALELLMPPVTDNANARMKAHVRRGTAFCQLELYVEGLQDYEAALKIDPSNKIVQIDAEKIRNVIQGTELKS", "text": "FUNCTION: Axonemal dynein assembly factor required for ciliary motility. Involved in neuronal migration during development of the cerebral neocortex. May regulate the stability and proteasomal degradation of the estrogen receptors that play an important role in neuronal differentiation, survival and plasticity. SUBCELLULAR LOCATION: Nucleus Cytoplasm Dynein axonemal particle Cell projection, neuron projection."}
{"protein": "MLILNGFSSATLALITPPFLPKGGKALSQSGPDGLASITLPLPISAERGFAPALALPYSSGGGNGPFGVGWSCATMSIARRTSHGVPQYNDSDEFLGPDGEVLVQTLSTGDAPNPVTCFAYGDVSFPQSYTVTRYQPRTESSFYRLEYWVGNSNGDDFWLLHDSNGILHLLGKTAAARLSDPQAASHTAQWLVEESVTPAGEHIYYSYLAENGDNVDLNGNEAGRDRSAMRYLSKVQYGNATPAADLYLWTSATPAVQWLFTLVFDYGERGVDPQVPPAFTAQNSWLARQDPFSLYNYGFEIRLLRLCRQVLMFHHFPDELGEADTLVSRLLLEYDENPIRTQLCAARTLAYEGDGYRRAPVNNMMPPPPPPPMMGGNSSRPKSKWAIVEESKQIQALRYYSAQGYSVINKYLRGDDYPETQAKETLLSRDYLSTNEPSDEEFKNAMSVYINDIAEGLSSLPETDHRVVYRGLKLDKPALSDVLKEYTTIVNIIIDKAFMSTSPDKAWINDTILNIYLEKGHKGRILGDVAHFKGEAEMLFPPNTKLKIESIVNCGSQDFASQLSKLRLSDDATADTNRIKRIINMRVLNS", "text": "FUNCTION: Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylates all actins tested, has more activity on nonmuscle beta/gamma-actin than on muscle alpha-actin. Prefers monomeric G-actin but can weakly ADP-ribosylate F-actin. ADP- ribosylation prevents the polymerization of G-actin to F-actin, causing actin filament depolymerization, destruction of the cytoskeleton and cytotoxicity. Does not possess NAD(+)-glycohydrolase activity, unlike most mART enzymes. SUBCELLULAR LOCATION: Secreted. Note=Secreted via the type III secretion system 1 (SPI-2 TTSS). SIMILARITY: Belongs to the SpvB family."}
{"protein": "MPSTPYDLVQDDQDLRVPLHAEQAFFHGITFQAKFVGWEEVPRPNTRAEIVQAMRRIRYECKVQNLKKRKVTIHISVNGVRVVLKKRRRKKKNWTNDPEDIELLNHPIYRIFYVSHDSSDLKIFSYIARDASTDTFKCSVFKSHKKSQAMRIVRTVGQAFEVCHKFNLHKNSLEPNDERSDISSSELLDVEQISEQQLSEDGERGGGDNETPKKEHLAITPDLNHTQPQRPNHLDIMPSHSSLRKSNSLLCDVDDKSPGSPSSPRSEITQLKDQLEAQALQTRQALGQLMLVREQLISETNARIEAQARTQQLLQQNRELLEHLASLGAYNEQQTAGLTSANIGMAPQQSQLQMLLQATSNNNNLATINQQISNLGSINQQLTSLSHQLSGLNQQSQHLQNLQQQQQQQQQQQQQQTQAAPTAATPPPAAGGSSPYPSMSALQSISNQLQQQQQQQQQDALSKDLFQVNQELLNRLQALNLNANPGQSQPTPSATAHNSFFYVNPLSCTPATPNNNAGGAGGFNFLTSPAATGTLTPSPLGTMNRNSFAGSSSLNEDIRLSIEQNLNNLEEQLKAAVSNGNLAGLACGGSTSTRDTSRSSSTLDSPSSPRLRSSNNNISPGSSNGNQNHNNNSNSNSSSSRETRFNTVLLRVTDEAGHQRKLSATPSFITRSTSEKVPNRSQMMSQVQRTTWARHTTK", "text": "FUNCTION: Putative adapter protein."}
{"protein": "MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H3 family."}
{"protein": "GLVGAPATLSTAPIAYGGYGGYGAYGGSLLRAAPIARVASPLAYAAPVARVAAPLAYAAPYARAAVAAPVAVAKTVVADEYDPNPQYSFGYDVQDGLTGDSKNQVESRSGDVVQGSYSLVDPDGTRRTVEYTADPINGFNAVVHREPLVAKAVVAAPAIAKVHAPLAYSGGYLH", "text": "FUNCTION: Component of the cuticle of the larva of Tenebrio molitor."}
{"protein": "MQMKKLLPILIGLSLSGFSTLSQAENLMQVYQQARLSNPELRKSAADRDAAFEKINEARSPLLPQLGLGADYTYSNGYRDANGINSNETSASLQLTQTLFDMSKWRGLTLQEKAAGIQDVTYQTDQQTLILNTANAYFKVLNAIDVLSYTQAQKEAIYRQLDQTTQRFNVGLVAITDVQNARAQYDTVLANEVTVRNNLDNAVEELRQVTGNYYPELASLNVEHFKTDKPKAVNALLKEAENRNLSLLQARLSQDLAREQIRQAQDGHLPTLNLTPSTGISDTSYSGSKTNAAQYDDSNMGQNKIGLNFSLPLYQGGMVNSQVKQAQYNFVGASEQLESAHRSVVQTVRSSFNNINASISSINAYKQAVVSAQSSLDAMEAGYSVGTRTIVDVLDATTTLYDAKQQLANARYTYLINQLNIKYALGTLNEQDLLALNSTLGKPIPTSPESVAPETPDQDCAADGYNAHSAAPAVQPTAARANSNNGNPFRH", "text": "FUNCTION: Outer membrane channel, which is required for the function of several efflux systems (By similarity). Required for virulence. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family."}
{"protein": "MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDHLQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP", "text": "FUNCTION: This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single- pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. SIMILARITY: Belongs to the glycosyltransferase 6 family."}
{"protein": "MAVPVVETNNILSHPEGGCPLQVGEGTYELKDDLHLATPPPHPSEAPIINPNPLATVPTPPTSGVKVSLVCVSPRSRTPSFISKQIVTAPPFGDGNPALVPAPVKDGLKRRKPKNNIIKSSSSFVSRVITHEVATKRLSERSPEGLFAFANINRAFQWLDLSSKQKEDPLAKILFTKAHMLCHDINEVTKSPSHIDVVMGSSAGDIIWYEPISQKYARINKNGVVCNSPVTHIKWIPGSENLFMASHANGQLVVYDKEKEDALFTPEIQDQSAEAVKASSTQPLQVLKSVNSRNQKTNPVALWKLANQRISHFAFSPDQRHLAVVLEDGSLRVMDYLKEDYYGGLICVCWSPDGKYIVTGGQDDLVTIWSFPERKIVARCQGHNSWVSAVAFDPWQCDERTYRFGSVGDDCRLLLWDFSVGMLHRPKVHQTSARQRTSMVAGSSQYGNRHRADSVGNRMRSDSQRTANTYESCDQAVRHPVEPRARTALLPPIMSKVVGTDPICWLGFQEDCIMTSSLEGHIRTWDRPREGINDKYNDQSSSTAVSASAAGSGSISGLAESTMGSL", "text": "FUNCTION: Component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Required to prevent the proteolysis of the CreB deubiquitinating enzyme in the absence of carbon catabolite repression. CreB deubiquitinating enzyme stabilized in a complex with the CreC leads to the expression of genes such as those in the proline and quinate pathways (By similarity). SIMILARITY: Belongs to the WD repeat creC family."}
{"protein": "MREALEADLRAVLNGALNMLGTVERMLPVAAEVLLHERADLLGEVRSLDREVDAQEAQLEAECLRIIALHQPVARDLRLVALILKSLSDIERMGDYVVHVAEDGAELAQAPALKKYVNLSRMLSRLTEMSQNLRTSLADRDVTRAENTTRMDDEVDELYEQIQRELVTYMLEDPRNISKALMLMRVGRSLERVGDHMENVAERVRYWVTGSRE", "text": "FUNCTION: Plays a role in the regulation of phosphate uptake. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PhoU family."}
{"protein": "MSFSERPRVTQNGPSMIHLFNVFSKFRKENDYDGLVNYLITNYSQNVKNRTFNFHNTGHIFHMLYAYVPSPSSKERKQIRLDCIENLLESTKNDFKLYEDLIKLMNGDDKCPCELITARLNDNIAYNESLKNKNFDSKPCKLKKEPIDSILFKYSINWKNSLNKKRSLPKSTTTKKSEEKENMDEIEVDASKISSQSSLSNLNGYTIASCVHDYVIEEHQLRAGDEMVSFIKFCKKCGHK", "text": "FUNCTION: Required for late and very late gene expression. SIMILARITY: Belongs to the baculoviridae LEF-5 family."}
{"protein": "MQIDVDPQEDPQNAPDVNYVVENPTLDLEQYAASYSGLMRIERLQFIADRCPPLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRELQNAPDAIPESGVEPPPLDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGDHYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLSYVSKAESTPEIAEQRGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCFLLASFDHCDFPELLSPSNVAVYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHKMAAAFNTTVAALEDELTQLILEGLINARIDSHSKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMILRAAVLRNQIHVKSPPREGSQGELTPANSQSRMSTNM", "text": "FUNCTION: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CSN1 family."}
{"protein": "MSKDSDYKRAEKHLSSIDNKWSSLVKKVGPCTLTPHPEHAPYEGIIRAITSQKLSDAATNSIINKFCTQCSDNDEFPTPKQIMETDVETLHECGFSKLKSQEIHIVAEAALNKQIPSKSEIEKMSEEELMESLSKIKGVKRWTIEMYSIFTLGRLDIMPADDSTLKNEAKEFFGLSSKPQTEEVEKLTKPCKPYRTIAAWYLWQIPKLHRKGQ", "text": "FUNCTION: Alkylbase DNA glycosidase-like protein that shows no DNA glycosylase activity for alkylated bases (PubMed:23273506, PubMed:23245849). The molecular role of mag2 appears to be abasic (AP) site recognition and protection, while possibly facilitating damage signaling by structurally sculpting the DNA substrate (PubMed:18270439, PubMed:23245849). Stimulates AP site binding to mismatch repair protein mutS (PubMed:23245849). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family."}
{"protein": "MCISEGKMDWRSWLRKKFQVRSQLLRGCMAEFLAVFVLMVFTEGCSASAIFTHRRNDLLFAAFGSGLAVTMAVYVAGGVTGAFLNPAIAVAFSVLGKLPWKNCFCYMIAQYLGAFLASLAIYAQYYDALNIFDGGHRQVLGDNGTAQIWSTYPQAFLSPQGAFVDQVFGTALLIIVVLSMVDKKNWKPQNGYFPIAIGLLIVVLDISLAYNAGAALNPSRDLAPRLFTYVAGYGTETFSVKGYTWFFVPVVGSHAGAIVGAVIYQLFIGAQWPQDDLDDSNSVSSMSIHEKNFSLAKRKNTRNFNLDITRDFKERNGISTVLY", "text": "FUNCTION: Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis (PubMed:23761966). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MTSQHSAKKSSKNTPKNNRTFKGFLLKFSFTALVLTIFYGGYLDWQIRSKMDGQIWHLPAEVYSRLESVKIADNLAFDEVIQILLDNEYRQTTMVAAPGDFKLEDDSIVVLRRAFPFPDKAEPQRVLRLRFSHNKLSRIEDLVTVKTVDEFRLAPKLIAMLQSDNEDRLAIPLQNYPRLLIDTLILTEDRRFYEHNGINPVGILRALIANIRAGQTVQGGSTLTQQLVKNLFLSRERTITRKANEALMSLVLDWRYDKNRILETYLNEIYLGQNGDTQIHGFELASQFYFGRSIREISLDQIALLVGMVKGPSLYNPWRNPQNALERRNIVLRLMLEHKMIGDELYQLLSQRPLGVQKKGQISRKYPAFIQTLQADLRRKLGEHKISSLLGARIFSTMDLKQQAQAENAVGNTVSQLQLKMKNPHLEGAMIITDYRTGEIRAVVGGLQTQYAGFNRALMAKRQIGSLVKPSIYLTALSNPEQFRLNTPINNQPITINVKGSPPWQPRNYDKKYSDSVMLMDALARSLNIPTVNIGMKVGLSKVIDTQKAMGWDNVEIPKVPAMLLGSYTISPYDVTKLYQTLANQGGRIALTTVDSIADRQGNLIFQHDKSAKQVVPQEAAFQTLFAMQQTVERGTARSLQKDYADLHLAGKTGTTNESRDTWFVGIDGKNISTVWLGRDDNGETKLTGASGALQIYKDYLNRTNIEKLAITPPTTVKWVGINQYGDWDCESYRTIPIWLNNGQNFCGETSSPSLTPTTETETPPQESLWDVLDNPNPPAQ", "text": "FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits) (By similarity). SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family."}
{"protein": "MGDSTEKLQANASLRQPKKRFVGRRTADTQAQSSTSVQDVESTSIQKATPRRTPRTLNQVPPEISQDPDILAAIDLLPKNYSFEIPKTIHRIRTSGAKRIALQFPEGLLLFATTISDILTQFCPGTETLIMGDVTYGACCIDDYTARALGCDLLVHYAHSCLIPVDVTKIKTLYIFVDISIDTSHLIATLERNFQPGKTIATVGTIQFNATLHGLKPVLERAGFNVVIPQITPLSKGEILGCTSPSLSAQQIDYLLYLGDGRFHLESAMIHNPSIPAYRYDPYSRTLSRESYDHTEMHTLRRDAIAAARTAKKWGIILGSLGRQGNPHTMAMIESHLNERGIPFVNLLLSEIFPGKLAAMSDVECWVQIACPRLSIDWGYAFPRPLLTPYEALIALGVRDDWEKTHEGVYPMDFYAKDGLGRTKPQAVQTV", "text": "FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post- translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily."}
{"protein": "MPPEPLSLPLDLAPGLVDGDTFLSIMGALPTGVTVVTTLGPDGEPYGLTCSAACSVSKAPPLLLVCINRDSRVLKALLERGEFAVNVLRGGGESTSARFAAPVDDRFRDVRWEPGSAGGVPVMSADVVAHAECRVAAALDAGDHTIVIGAVVAGGPRPEVPSPLMYWRRSYARWPVEEDPRTAALTLAAEG", "text": "FUNCTION: Catalyzes the reduction of flavin by NADH. Subsequently, the reduced flavins is transferred to the tetracycline 7-halogenase CtcP. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family."}
{"protein": "MQIKFLTTLATVLTSVAAMGDLAFNLGVKNDDGTCKDVSTFEGDLDFLKSHSKIIKTYAVSDCNTLQNLGPAAEAEGFQIQLGIWPNDDAHFEAEKEALQNYLPKISVSTIKIFLVGSEALYREDLTASELASKINDIKGLVKGIKGKNGKSYSSVPVGTVDSWDVLVDGASKPAIDAADVVYSNSFSYWQKNSQANASYSLFDDVMQALQTLQTAKGSTDIEFWVGETGWPTDGSSYGDSVPSVENAADQWQKGICALRAWGINVAVYEAFDEAWKPDTSGTSSVEKHWGVWQSDKTLKYSIDCKFN", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. Note=Tightly bound to cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
{"protein": "MKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNRWKEDIEIIEKIGAKAYRFSISWPRILPEGTGKVNQKGLDFYNRIIDTLLEKNITPFITIYHWDLPFSLQLKGGWANRDIADWFAEYSRVLFENFGDRVKHWITLNEPWVVAIVGHLYGVHAPGMKDIYVAFHTVHNLLRAHAKSVKVFRETVKDGKIGIVFNNGYFEPASEREEDIRAARFMHQFNNYPLFLNPIYRGEYPDLVLEFAREYLPRNYEDDMEEIKQEIDFVGLNYYSGHMVKYDPNSPARVSFVERNLPKTAMGWEIVPEGIYWILKGVKEEYNPQEVYITENGAAFDDVVSEGGKVHDQNRIDYLRAHIEQVWRAIQDGVPLKGYFVWSLLDNFEWAEGYSKRFGIVYVDYNTQKRIIKDSGYWYSNVIKNNGLTD", "text": "FUNCTION: Broad substrate specificity glycosidase. Releases glucose from soluble glucooligomers, with a preference for longer oligomers; acts more readily on cellotetraose than on cellobiose. Displays similar activities towards the disaccharides lactose and cellobiose. Is also able to hydrolyze various aryl-beta-glycosides in vitro. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MNTMKTTYIVLELIIAVLSIAGNVLVCWAVAINSTLKNATNYFLVSLAVADIAVGLLAIPFAITISIGFQVDFHSCLFFACFVLVLTQSSIFSLLAVAIDRYLAIKIPLRYNSLVTGKRARGLIAVLWLLSFVIGLTPLMGWNKAMSGCPNSTNETGADHGAGHHGCFISCLFENVVTMSYMVYFNFFGCVLLPLIIMLGIYIKIFMVACKQLHQIELMGNSRTTLQKEVHAAKSLAIIVGLFAFCWLPLHILNCITHFHEEFSKSKPEWVMYVAIILSHANSVINPIIYAYRIRDFRYTFHKIISKILCKTDDFPKCTTDNNQHLTVTNVNAPAASVTI", "text": "FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MLTFIELLIGVVVIVGVARYIIKGYSATGVLFVGGLLLLIISAIMGHKVLPSSQASTGYSATDIVEYVKILLMSRGGDLGMMIMMLCGFAAYMTHIGANDMVVKLASKPLQYINSPYLLMIAAYFVACLMSLAVSSATGLGVLLMATLFPVMVNVGISRGAAAAICASPAAIILAPTSGDVVLAAQASEMSLIDFAFKTTLPISIAAIIGMAIAHFFWQRYLDKKEHISHEMLDVSEITTTAPAFYAILPFTPIIGVLIFDGKWGPQLHIITILVICMLIASILEFLRSFNTQKVFSGLEVAYRGMADAFANVVMLLVAAGVFAQGLSTIGFIQSLISIATSFGSASIILMLVLVILTMLAAVTTGSGNAPFYAFVEMIPKLAHSSGINPAYLTIPMLQASNLGRTLSPVSGVVVAVAGMAKISPFEVVKRTSVPVLVGLVIVIVATELMVPGTAAAVTGK", "text": "FUNCTION: Responsible for the transport of C4-dicarboxylates during anaerobic growth. Catalyzes the uptake of fumarate coupled to the export of succinate. FUNCTION: Responsible for the transport of C4-dicarboxylates during anaerobic growth (PubMed:8955408, PubMed:10368146). Catalyzes the uptake of fumarate coupled to the export of succinate (PubMed:8955408). Can also catalyze the uptake of fumarate and the efflux of succinate, without exchange (PubMed:8955408, PubMed:10368146). Shows low rates of transport, which are sufficient for succinate export during fermentation but not for fumarate-succinate exchange in fumarate respiration, indicating that it may function in vivo as the succinate efflux carrier for glucose fermentation, even if it is also able to operate as a fumarate-succinate antiporter (PubMed:10368146). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DcuC/DcuD transporter (TC 2.A.61) family."}
{"protein": "MIGQITSGLFGGHDDSKKVKGTVVMMNKNVLDFTDLAGSLTGKIFDVLGQKVSFQLISSVQGDPTNGLQGKHSNPAYLENSLFTLTPLTAGSETAFGVTFDWNEEFGVPGAFIIKNMHINEFFLKSLTLEDVPNHGKVHFVCNSWVYPSLNYKSDRIFFANQPYLPSETPELLRKYRENELLTLRGDGTGKREAWDRIYDYDIYNDLGNPDQGKENVRTTLGGSAEYPYPRRGRTGRPPTRTDPKSESRIPLILSLDIYVPRDERFGHLKMSDFLTYALKSIVQFILPELHALFDGTPNEFDSFEDVLRLYEGGIKLPQGPLFKALTAAIPLEMIRELLRTDGEGILRFPTPLVIKDSKTAWRTDEEFAREMLAGVNPVIISRLQEFPPKSKLDPEAYGNQNSTITAEHIEDKLDGLTVDEAMNNNKLFILNHHDVIIPYLRRINTTITKAYASRTLLFLQDNGSLKPLAIELSFPHPDGDQFGVTSKVYTPSDQGVESSIWQLAKAYVAVNDVGVHQLISHWLNTHAVIEPFVIATNRQLSVLHPIHKLLYPHFRDTMNINASARQLLVNAGGVLESTVFQSKFAMEMSAVVYKDWVFPDQALPADLVKRGVAVEDSSSPHGVRLLIEDYPYAVDGLEIWSAIKSWVTDYCSFYYGSDEEILKDNELQAWWKELREVGHGDKKNEPWWPEMETPQELIDSCTTIIWIASALHAAVNFGQYPYAGYLPNRPTVSRRFMPEPGTPEYEELKRNPDKAFLKTITAQLQTLLGVSLVEILSRHTTDEIYLGQRESPEWTKDKEPLAAFDRFGKKLTDIEKQIIQRNGDNILTNRSGPVNAPYTLLFPTSEGGLTGKGIPNSVSI", "text": "FUNCTION: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lipoxygenase family."}
{"protein": "MNPHDLEWLNRIGERKDIMLAVLLLAVVFMMVLPLPPLVLDILIAVNMTISVVLLMIAIYINSPLQFSAFPAVLLVTTLFRLALSVSTTRMILLQADAGQIVYTFGNFVVGGNFIVGIVIFLIITIVQFLVITKGSERVAEVSARFSLDAMPGKQMSIDGDMRAGVIDVNEARERRATIEKESQMFGSMDGAMKFVKGDAIAGLIIIFVNILGGVTIGVTQKGLAAAEALQLYSILTVGDGMVSQVPALLIAITAGIIVTRVSSEDSSDLGSDIGKQVVAQPKAMLIGGVLLLLFGLIPGFPTVTFLILALLVGCGGYMLSRKQSRNDEANQDLQSLLTSGSGAPAARTKAKTSGANKGRLGEQEAFAMTVPLLIDVDSSQQEALEAIALNDELVRVRRALYLDLGVPFPGIHLRFNEGMGEGEYLISLQEVPVARGELKAGYLLVRESVSQLELLGIPYEKGEHLLPDQETFWVSVEYEERLEKSQLEFFSHSQVLTWHLSHVLREYAEDFIGIQETRYLLEQMEGGYGELIKEVQRIVPLQRMTEILQRLVGEDISIRNMRSILEAMVEWGQKEKDVVQLTEYIRSSLKRYICYKYANGNNILPAYLFDQEVEEKIRSGVRQTSAGSYLALDPAVTESLLEQVRKTIGDLSQIQSKPVLIVSMDIRRYVRKLIESEYYGLPVLSYQELTQQINIQPLGRVCL", "text": "FUNCTION: Could be involved in the secretion of the yop virulence proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family."}
{"protein": "MDSLRLISKSIKIEGTPFGSSHQRNQIFLKSVAFFLLIGLAYRFLITNSTVSPVPTVRSSPESLPPDPSGLTAITQTSASVDSPANITTIASQNVSTKCDIFIGNWVPDPSGPIYTNVSCRHIQDYQNCLKNGRPDVNYLRWRWQPRDCDLPRFNPEQFLDNMRNKWLAFIGDSISRNHVQSLLCILSQVEEVEDIFHDKEYKSRIWRFPSYNFTLSVIWSPFLVKAETFENGVPFSDIRVHLDKLDQKWTDQYINFDYVVISGGKWFLKTTIFHENNTVTGCHYCQGKNNMTELGYLYSYRKVLHLVLDFVAEPNHKAQVLFRTTTPDHFENGEWDSGGFCNRTMPFTEGSEGEMKSEDVSMRDIELEEFYKTTTTQQEGSNSNIVLLDTTSMSLLRPDGHPGPYRYPNPFAGLKNKELNQVQNDCLHWCLPGPIDSWNDLMVEVMLNRERQRRE", "text": "FUNCTION: May be involved in the O-acetylation of mannan (PubMed:22086088). May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily."}
{"protein": "MFDTRKKIYVSDVTLRDGMHAVRHQYSLADAERIARALDEAGVDSIEVAHGDGLQGSSFNYGFGAHTDLEWIERVAATVRRAKIATLLLPGIGTVHDLKNANAAGASVVRVATHCTEADISQQHIEYARKLGMDTVGFLMMSHMTTPTALAVEAKKMESYGAQCIYVVDSGGAMNMYDIADRFKALKDVLDPSTQTGMHAHHNLSLGVANSIVALEYGCDRIDASLTGMGAGAGNAPLEVFIAAVDRMGLKHGCDVRKLIDAAEEIVRPLQERPVRVDRETLALGYAGVYSSFLRHTEAAAHKYGLDAFEILVELGRRRMVGGQEDMIVDVALDMMSRKPQGTMRDVISH", "text": "FUNCTION: Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of p-cumate. SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family."}
{"protein": "METDPANSSSKSPAVVSEKDVLIPEPSENTVGVVQDPVSAEREAHEDSISTEASVAKVDDTQMPASSTGSEPLSKTDDIVPCPPGSSPRESPPSIFSSSGLSSWAKSFKFQQQDPNRTDSGMSAFTRFTSELGLHLPTKGSEEVGDSRSSNTQVGGAFESLTKAVVDSSRGAVKAMQVKARHIVSQNKRRYQEGEFDLDMTYITENIIAMGFPAGDISSGLFGFFEGLYRNHMEEVIKFFETHHKDKYKVYNLCSERLYDASRFEGKVASFPFDDHNCPPIQLIPSFCQSAYTWLKEDIQNVVVVHCKAGMARTGLMICCLLLYLKFFPTAEEAIDYYNQKRCLDGKALVLPSQIRYVKYYERVQNQFDGKVPPERRCMLRGFRLINCPYWIRPAITISNHTDILFSTKKHQKTKDLGPEDFWIKAPKKGVVVFAIPGEAGLTELAGDFKIHFQDSDGDFYCWLNTTLTDNRTMLKGSDFDGFDKRKLPAPGFHVEIVMIEPDNSQPTKSKSDSTQQQSQSSSSADSSKLKSNEKDDDVFSDSDGEEEGNSQSYSTNEKTASSMHTTSKPHQINEPPKRDDPSANRSVTSSSSSGHYNPIPNNSLAVSDIKAIAADASVFSFGDEEEDYESD", "text": "FUNCTION: Protein tyrosine phosphatase that exhibits also a weak lipid phosphatase activity towards PtdIns(3)P. SIMILARITY: Belongs to the PTEN phosphatase protein family."}
{"protein": "MEFMAATTSIADTDMEFDKNVPRICGVCGDKATGFHFNAMTCEGCKGFFRRSMKRKAMFTCPFNGDCRITKDNRRHCQSCRLKRCVDIGMMKEFILTDEEVQRKRQMINKRKSEEALKESMRPKISDEQQKMIDILLEAHRKTFDTTYSDFNKFRPPVRENVDPFRRITRSSSVHTQGSPSEDSDVFTSSPDSSEHGFFSASLFGQFEYSSMGGKSGELSMLPHIADLVSYSIQKIIGFAKMIPGFRDLIAEDQIALLKSSVIEVIMLRSNQSFSLDDMSWTCGSEDFKYKVDDVTQAGHNMELLEPLVKFQVGLKKLDLHEEEHVLLMAICILSPDRPGLQDKALVESIQDRLSSTLQTYILCKHPPPGSRLLYAKMIQKLADLRSLNEEHSKQYRSISFLPEHSMKLTPLMLEVFSDEIP", "text": "FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3- responsive target genes (By similarity). Plays a central role in calcium homeostasis (By similarity). Also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localizes mainly to the nucleus. Translocated into the nucleus via both ligand-dependent and ligand- independent pathways; ligand-independent nuclear translocation is mediated by IPO4. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDLRNDPKFTYTGTEMRTVAEKVDTVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESPRGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHVQELQQEKEELLQELSSLE", "text": "FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys- 63'-linked ubiquitin in various substrates. Mediates the specific 'Lys- 63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle pole Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. SIMILARITY: Belongs to the peptidase M67A family. BRCC36 subfamily."}
{"protein": "MGNSLRCISQEQDPNQKKPSSVVNGNSSEKHVRRLSLIPSFRRRTLLPSLSCSGSSTSSTSKKGGIKTKKKIRERHHQEQHHHDHEKDSLIQDQTLAATNILFSQTPRNSNSAPPFRRSTSVVYTQPPTAAVAASVGSVSGALTPKKSTYGYVRSSSNRQRSSTDPVLKPNQLLDKELKVEGAETKRFVLVHGGGFGAWCWYKTITLLEKHGFQVDAVDLTGSGVSSFDTNNITSLAQYVKPLLHFFDTLKPTEKVILVGHDFGGACMSYAMEMYPSKIAKAIFISAAMLANAQSTLDLFNQQPDSNYDLMEQVHLFLYANGKKNPPTAVDFDRSLLRDFFFNQSPPKDVALASVSMRPIPFAPVVEKLHVSEKNYGSIRRFYIKTMEDDYAVPVSLQDAMIKSNPPEQVFHLKGSDHAPFFSRPQSLNRILVEISQLPPKKSS", "text": "FUNCTION: Putative methylesterase. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase family."}
{"protein": "MLRKGCCVELLLLLLAGELPLGGGCPRDCVCYPAPMTVSCQAHNFAAIPEGIPEDSERIFLQNNRITFLQQGHFSPAMVTLWIYSNNITFIAPNTFEGFVHLEELDLGDNRQLRTLAPETFQGLVKLHALYLYKCGLSALPAGIFGGLHSLQYLYLQDNHIEYLQDDIFVDLVNLSHLFLHGNKLWSLGQGIFRGLVNLDRLLLHENQLQWVHHKAFHDLHRLTTLFLFNNSLTELQGDCLAPLVALEFLRLNGNAWDCGCRARSLWEWLRRFRGSSSAVPCATPELRQGQDLKLLRVEDFRNCTGPVSPHQIKSHTLTTSDRAARKEHHPSHGASRDKGHPHGHPPGSRSGYKKAGKNCTSHRNRNQISKVSSGKELTELQDYAPDYQHKFSFDIMPTARPKRKGKCARRTPIRAPSGVQQASSGTALGAPLLAWILGLAVTLR", "text": "FUNCTION: Cell surface receptor that plays a functionally redundant role in postnatal brain development and in regulating axon regeneration in the adult central nervous system (PubMed:22406547, PubMed:27339102). Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum (PubMed:27339102). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG (PubMed:26335717). Plays a role in inhibiting neurite outgrowth and axon regeneration via its binding to neuronal chondroitin sulfate proteoglycans (PubMed:22406547). Binds heparin (PubMed:22406547). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:22325200). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Membrane raft Perikaryon Cell projection Note=Localized to the surface of neurons, including axons. SIMILARITY: Belongs to the Nogo receptor family."}
{"protein": "MEPMLPEAGEAALLSSYAPQASGSMGVDPDPITGLVSTSAAPLVRVEEAPKFELESYIANYTGRTRFNRLYLIGTCSSYLAVDALKAAIAEAKSGKDVARYLRAVQALADVAPNEPEATIDSDWVERSQKVVKAETDRLEHELRGYKNNLIKESIRMGNEELGQHYHRIGDLTSAFKAYSRMRDFCTTPSHIASMLFKIINVAIERGDWLNVQSNVHRLRSQGGKPEEQAKHQPKISAAMGLSQLHSGSYLEAANSFIATDPSLGDTFNEVLTSNDVAVYGGLCALASMDRNELQRRVLDNSSFRNFLELEPHIRRAISFFCNSKFRPCLEILEAYRADYLLDIHLQRHVQVLYNRIRTKSIQQYLIPFNRVSLESMAKIFVLGNPTSQSSQSDSKSAFVQELISLIQDGTLDARIDLEKHVLVSTQGDKRIEVQEAVLDSLDNYVREAHLRLLRSNIIRAGLEVRPLGEDRRTKLEERGKKGHSAIGNLLRATGMKQ", "text": "FUNCTION: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin- protein ligase complexes (By similarity). The CSN complex seems to link protein degradation to sexual development. Required for fruit body formation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CSN1 family."}
{"protein": "METEPPPLEERRRLQEELSEFVESCCRTLEEVTASLGWSLDQLDPGDEAEAEDEIAICPYDSNHRMPKSSLTKHMESCRLRKLGYTKEEENEMYNPTFFYENLKIPSVTLNKDSQFQIIKQARTTAGKDGDCYSQRMYSSVPVEVPLNHKRSVCDLTQTDRLALYDFVIEETKKKRSGPQVIENDSDLFVDLAAKVNQDNSRKSPKSYLEILAEVRDYKRRRQSYRAKNVHITKKSYTEVIRDVIKVHMEELSSHWQEEQGRAGDAAEKNEERRSASVDSRQSGGSYLDVESSRHRRARSRSPHKRKRNKDKSSESRRRKERDGERHHSHKRRKQKI", "text": "FUNCTION: Likely involved in U12-type 5' splice site recognition. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MQSYKYDKAIVPESKNGGSPALNNNPRKGGSKRVLLICLDLFCLFMAALPFLIIETSTIKPYRRGFYCNDESIKYPLKVSETINDAVLCAVGIVIAILAIITGEFYRIYYLKEKSRSTTQNPYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCDPDFSQINCSEGYIQNYRCRGEDSKVQEARKSFFSGHASFSMFTMLYLVLYLQARFTWRGARLLRPLLQFTLLMMAFYTGLSRVSDYKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTSLSLPAPAIRREILSPVDIIDRNNHHNMV", "text": "FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1- phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z- octadecenoyl)-ethanolamine phosphate, a potential physiological compound. Has both an extracellular and an intracellular phosphatase activity, allowing the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes. Through the dephosphorylation of extracellular sphingosine-1-phosphate and the regulation of its extra- and intracellular availability, plays a role in vascular homeostasis, regulating endothelial cell migration, adhesion, survival, proliferation and the production of pro- inflammatory cytokines (By similarity). By maintaining the appropriate levels of this lipid in the cerebellum, also ensure its proper development and function (PubMed:21319224). Through its intracellular lipid phosphatase activity may act in early compartments of the secretory pathway, regulating the formation of Golgi to endoplasmic reticulum retrograde transport carriers (By similarity). FUNCTION: Independently of this phosphatase activity may also function in the Wnt signaling pathway and the stabilization of beta- catenin/CTNNB1, thereby regulating cell proliferation, migration and differentiation in angiogenesis or yet in tumor growth (PubMed:12925589, PubMed:27125875). Also plays a role in integrin- mediated cell-cell adhesion in angiogenesis (PubMed:16099422). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Membrane raft; Multi-pass membrane protein Note=Cycles between the endoplasmic reticulum and the Golgi. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
{"protein": "MKTMRMNSAFILAFALAAAMLILTEAANTAFVSSACNTQKIPSGSPFNRNLRAMLADLRQNTAFSGYDYKTSRAGSGGAPTAYGRATCKQSISQSDCTACLSNLVNRIFSICNNAIGARVQLVDCFIQYEQRSF", "text": "FUNCTION: Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity (PubMed:17338634). Exerts antifungal activity against S.cerevisiae and F.culmorum through its carbohydrate-binding specificity. Acts as a lectin that stricly recognizes alpha-1,2-linked mannose moieties and interacts with the yeast cell wall mannan polysaccharide (PubMed:25139159). Can interfere with the fungal actin remodeling resulting to the activation of an actin-dependent cell death (PubMed:26315821). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKWMCSICCAAVLLAGGAAQAEAVPNEPINWGFKRSVNHQPPDAGKQLNSLIEKYDAFYLGNTKEKTIYLTFDNGYENGYTPKVLDVLKKHRVTGTFFVTGHFVKDQPQLIKRMSDEGHIIGNHSFHHPDLTTKTADQIQDELDSVNEEVYKITGKQDNLYLRPPRGVFSEYVLKETKRLGYQTVFWSVAFVDWKINNQKGKKYAYDHMIKQAHPGAIYLLHTVSRDNAEALDDAITDLKKQGYTFKSIDDLMFEKEMRLPSL", "text": "FUNCTION: Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate. SIMILARITY: Belongs to the polysaccharide deacetylase family."}
{"protein": "MLSITILFLLIAEGSSQNYTGNPVICLGHHAVSNGTMVKTLTDDQVEVVTAQELVESQHLPELCPSPLRLVDGQTCDIVNGALGSPGCNHLNGAEWDVFIERPTAVDTCYPFDVPDYQSLRSILANNGKFEFIVEKFQWNTVKQNGKSGACKRANENDFFTNLNWLTKSDGNAYPLQNLTKVNNGDYARLYIWGVHHPSTDTEQTNLYENNPGRVTVSTKTSQTSVVPNIGSRPWVRGQSGRISFYWTIVEPGDIIVFNTIGNLIAPRGHYKLNSQKKSTILNTAVPIGSCVSKCHTDRGSITTTKPFQNISRISIGDCPKYVKQGSLKLATGMRNIPEKATRGLFGAIAGFIENGWQGLIDGWYGFRHQNAEGTGTAADLKSTQAAIDQINGKLNRLIEKTNEKYHQIEKEFEQVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDVTDSEMDKLFERVRRQLRENAEDKGNGCFEIFHQCDNNCIESIRNGTYDHDIYRDEAINNRFQIQGVKLTQGYKDIILWISFSISCFLLVALLLAFILWACQNGNIRCQICI", "text": "FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin- independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host apical cell membrane; Single-pass type I membrane protein Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. SIMILARITY: Belongs to the influenza viruses hemagglutinin family."}
{"protein": "MSGGYTSLESSIRTCKVNTGNADRIESDRFLGFPDKKTCPPFLGTDLTGRAICPDSFMTKSAGCNTPEDRIYIENTVSRPHYYEYINLSPRGMLNDETIEGFGFGQQESAYIREGFGTNGTSAQYGSNGNGGNGSCGLNNYRAPVNLNGWPRAGYGIGPEDIDDLPGDLRFNATQPGPFNNMPLWAFSVVPREYGMPYSQLYGQNAEDQRLKQALWARAEIMGQDPIVPGPSRYGYRMMGDY", "text": "SIMILARITY: Belongs to the IIV-6 415R family."}
{"protein": "MLRSELRDMVVAMVLWGILLPFCLSQTTSPSQDGKIKFRLAGYPRKHNEGRIEVFYNREWGTICDDDFTLANAHVLCRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDCTHQEDAGVICKDERLPGFAESNIIEMQVDEKRMEKIRLRPLKGAHAGRLPVTEGVVEVKFKEGWGHICNTGWTIKNSRVVCGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPCPGGGAAVVSCVPGLQFTQGRVRKAKLNPVPQMRLKGGARAGEGRVEVLKGSEWGTVCDDHWNLQSASVVCRELGFGTAKEALTGARMGQGMGPIYMNEVQCGGDEKSLWDCPHQSITAEDCKHTEDASVICNIPYMGFEKLMRLTGGRTRLEGRVELLLPAGGGVRDWGLICGDGWTSREAMVVCRQLGLGHASSGLRETWYWDSSNVTEMVMSGVKCKGDEMTLTDCQHHSVVSCKRAGAQFSAGVICSDMASDLVLNAPLVEQTVYIEDRPLHLLYCAAEENCLAKSAAQASWPYGHRRLLRFSSEIHNIGKADFRPRLGRHSWVWHECHRHYHSMDIFTYYDLLSLNGTKVADGHKASFCLEDTECHEGVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVSPGNYILQVIINPNFEVAESDFTNNAMRCNCKYDGHRVWLHKCHLGDSFSEEAEKEFEHYPGQLNNKIS", "text": "FUNCTION: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins. Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin. Can mediate oxidation of lysine residues that are acetylated. Also able to catalyze deacetylation of lysine residues (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space Cytoplasm Nucleus Note=It is unclear how loxl3a is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (loxl2) also has intracellular and extracellular localization despite the presence of a signal sequence. SIMILARITY: Belongs to the lysyl oxidase family."}
{"protein": "MIVFATILFGALSAEDPDVEKLDSQEFQRAVEERAFALGPEDHAPAGGEGQGAAGHRELRHPVGRAPSGGAGSDLEPGPLKVYDESQKVTGLLKPEGGGEPREFEYSYPEGYDIARVLNEANIPFTTDPQTAGPWARAIAVMAPFVLILLLFFLMTRTGRSASQSSRMTDFGKSRARRMTKDQPKVTFADVAGADEAVQELTEIKEFLENPQKFQKLGARIPKGALLVGPPGTGKTLLARAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFDSKSGIIMLAATNRPDILDPALLRPGRFDRQIVVDRPDLPGRIKILKVHTRGKPLGEDVDIETIARGTPGFTGADLANLVNEAALLAARHNKEQIEMAEMEEAIDRVIAGPERKTRLISEKEKEITAYHEAGHAIVGALLPEADPVHKVTIIPRGQALGVTMSLPEEDRFMMSRAQLMAQLSYMLGGRAAERVVFEEITTGASNDIERATKVARQMVTRYGMSEKLGLIALGQHDGQVFMGRDLHAQPDYSDEIAFQIDKEIRRLVDEAYDTAEDLLVRNRRLLEKLASDLIEYETVDAEHLRRLVEEYAVDEHPSRGRPAMSVNGHRG", "text": "FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family. SIMILARITY: In the central section; belongs to the AAA ATPase family."}
{"protein": "MSDPNLNDAVEPEAGASESAKDELDIVEAADSVDPDQAEAADLAAGEPAERAAVNVAGDDSDEDDAAAEEAVEADDESADEEEAEPAAPVDPVAALRDELRTLPGEWYVIHTYAGYEKRVKANLEQRAVSLNVEEFIYQAEVPEEEIVQIKNGERKNVRQNKLPGYVLVRMDLTNESWGVVRNTPGVTGFVGNAYDPYPLTLDEIVKMLAPEAEEKAAREAAEAEGKPAPARKVEVQVLDFEVGDSVTVTDGPFATLQATINEINADSKKVKGLVEIFGRETPVELSFDQIQKN", "text": "FUNCTION: Participates in transcription elongation, termination and antitermination. SIMILARITY: Belongs to the NusG family."}
{"protein": "MDRSRVLEQLIPELTGLLSLLDHEYLSDSTLEKKMAVASLLQSLQPLPAKEVSFLYVNTADLHSGPSFVESLFEEFDCDLGDLRDMSDDGEPSKGASPEPTKSPSLRSAAADVPPPLPNKPPPEDYYEEALPLGPGKSPEYISSHNGCSPAQSIVDGYYEDADNSYPTTRMNGELKNSYNDSDAMSSSYESYDEEEEEEKGRQPKHQWPSEEASMHLVRDCRICAFLLRKKRFGQWAKQLTVIKEEQLLCYKSSKDRQPHLRLALDVCTVIYVPKDSRHKRHELRFSQGATEVLVLALQSREQAEEWLKVIREVSRPIVGAEGLEVPRSPVILCKADQDKRLSQEKQNSDSDSLGMNDSGSTLGRREACEHGKGKKNSLAELKGSMSRAAGRKITRIISFSKKKALSEDLQTFSSEDEVPCCGYLNVLVNQGWKERWCRLRCNTLYFHKDRTDLHTHVNSIALRGCEVAPGFGPRHPFAFRILRNRQEVAILEASCSEDMGRWLGLLLVEMGSKVTPEALHYDYVDVETLTSIVSAGRNSFLYAQSCQDQWPEPRIYDEVPYEKVQDEEPQRPTGAQVKRHASSCSEKSHRADPQVKVKRHASSANQYKYGKNRAEEDARRYLVEKERLEKEKETIRTELTALRQEKKELKEAIRNNPGAKSKALEEAVATLEAQCRAKEEQRIDLELKLVAVKERLQQSLAGGPALGLSVSNKNKSQDTTNKPQSNAPEQSLPVNCVSELRKRSPSIVTSNQGRVLQKAKEWEMKKT", "text": "FUNCTION: May be involved in podosome and invadosome formation. SUBCELLULAR LOCATION: Cytoplasm Cell projection, podosome Cell projection, invadopodium Cytoplasm, cytoskeleton, stress fiber."}
{"protein": "MKAVVLTLAVLFLTGSQARHFWQQDDPQSPWDRVKDFATVYVDAIKDSGRDYVAQFEASALGKHLNLKLLDNWDSLGSTFTKVREQLGPVTQEFWDNLEKETEALRQEMSKDLEEVKKKVQPYLDDFQNKWQEEMETYRQKMAPLGAEFREGARQKVQELQEKLSPLAEELRDRLRAHVEALRQHVAPYSDDLRQRMAARFEALKEGGGSLAEYQAKAQEQLKALGEKAKPALEDLRQGLLPVLENLKVSILAAIDEASKKLNAQ", "text": "FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein A1/A4/E family."}
{"protein": "MGTVRSRRLWWPLPLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLAEALQHGATATFHRCAKDPWRLPGTYVVVLKEETQRLQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSYVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKNQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGTGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRVQPDQCMGHSGASTHASCCHAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVGTTGNISEEAVTAVAICCRSWHLAQASQELQ", "text": "FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)- mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). SUBCELLULAR LOCATION: Cytoplasm Secreted Endosome Lysosome Cell surface Endoplasmic reticulum Golgi apparatus Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MNASDFRRRGKEMVDYMADYLEGIEGRQVYPDVQPGYLRPLIPATAPQEPDTFEDILQDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLQLPEAFLAGEAGEGGGVIQGSASEATLVALLAARTKVVRRLQAASPGLTQGAVLEKLVAYASDQAHSSVERAGLIGGVKLKAIPSDGKFAMRASALQEALERDKAAGLIPFFVVATLGTTSCCSFDNLLEVGPICHEEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKRRTDLTGAFKLDPVYLKHSHQGSGLITDYRHWQLPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFEAFVLQDPRFEVCAEVTLGLVCFRLKGSDGLNEALLERINSARKIHLVPCRLRGQFVLRFAICSRKVESGHVRLAWEHIRGLAAELLAAEEGKAEIKS", "text": "FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin. SIMILARITY: Belongs to the group II decarboxylase family."}
{"protein": "MDIFSEFLNCLSSDGTLNESSIYKTYQILESLNPKDVDTKENYIKLSNTFSTLGSGVGFQDNLLIEMFKILTVLFFKTRSTDLGDLLIESFTSLEIEKLMRVKKTIGSIVLTKGIQELQEIELPKVGFNCMTYDESIFQGISLERLILQLMSIFIAKCEENKLWLVNNRKDLDLRVIGQRLLHRDFACRFLSGLFISRFSVSGDTDESKHQNGIRLQLFIDFSKFETRLTMQILKADRIFSTCVANTVHAYEGLFSSGSNIDSTIATLVLEPRDLIVYRKGFALLQIPWTSVTTIDKIKKVKSLKIITEVSSLDEFVFQCKDGDKFDELFSTSEEIMNKLLPAIIVSPKLTLRNRSIIQIKEGESKLPNTSKQASQNLPHLDDELAYQRFEDQVIDKSVCDDECTNTENTPSSNIPADVKDSLSADDYAYDTKRKTQIEDLEEDQNKSKIASKDGTNLKEINSVPEFSDENVINQTGPAKKTPVQRRKDGKFAKSTKRKKQKSLKPDTENQESSVKNKKAKSNVNLQYSPKTPICKINDETLKPPTIANIAGHKQMNHLTSENIETPVPVPNGNWYNGVKHETATDIFTTCHDGNNSLKSSVWKELLKEKHWKQESKPQLTGNSRQIDLSTFVKQANTPNITSLLDGTCSSPPNNECFNDKEPDSSSSTLISDRQELEYRNPNAETVKLEEIPYNKFFKTVEKNEAYNPSSKSATIDGLQRYTSMIGNQIYEGILQNEKELRSKLEAYHINCNKVIKEFSKRQTARYKIIEKELAQIEVNLVSQIDSLMFK", "text": "FUNCTION: Organizes linear element components on chromosomes and is thus required for meiotic DNA recombination. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to DNA double-strand break (DSB) hotspots."}
{"protein": "MGSNQLLRPRKVPKLFVFGDSYADTGNTKRDTEAWAIPYGITFPGKPSGRYCDGLIATDFLEKVLGAESPYLYRTHGRDKGLKRGMNFAFGGSKMLDSSPNSPFPNITAQVNFLVDLVLAGRVYGDITPSDVSLISYAGGDYIYYIDQNRPAAGLKALVEKVVDNLRVNMIVLGGLLFKKIAVTSLQPIGCLPSYTSASSFKSCNESQSALVELHNKLLKKVVAKLNEQSRVMKKEQHFFIIDIHNAFMTVMKNKGSKRFKNPMKSCCEGYCGRSSDGGKLYTLCDDPKSFFFWDAVHPTQEGWRSIYSVLGNPLTDFLTKP", "text": "SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family."}
{"protein": "MPYEIKKVFASLPQVERGVSKILGGDPKGDNFLYTNGKCVILRNIDNPAVADIYTEHAHQVVVAKYAPSGFYIASGDISGKLRIWDTTQKEHILKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDTGSSVGEITGHNKVINSVDIKQNRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIFIYDGKTGEKVCALGGSKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVNVNSVVSTFPMGSNVLDQQLGCLWQKDHLLSISLSGYINYLDKNNPSKPLRVIKGHSKSIQCLTVHKNGGKSYIYSGSHDGHINYWDSETGENDSFSGKGHTNQVSRMTVDESGQLVSCSMDDTVRYTNLTLRDYSGQGVVKLDVQPKCVAVGPGGYTVVVCIGQIVLLKDQKKCFSIDNPGYEPEVVAVHPGGDTVAVGGSDGNVRVYSILGATLKDEGKLLEAKGPVTDLAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETKVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY", "text": "FUNCTION: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Enhances cofilin-mediated actin severing. Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions. Involved in myocardium sarcomere organization. Required for cardiomyocyte growth and maintenance. Involved in megakaryocyte maturation and platelet shedding. Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP; the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension. Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, podosome. SIMILARITY: Belongs to the WD repeat AIP1 family."}
{"protein": "MAASTASHRPIKGILKNKTSSTSSRVASAEQPRGSVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMIGDDDDAYSDTETTEAMTPDTLAKKLAAAEGSEPKYRIREQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDEEDEEMSETADGESMNTEESNQGSTPSDQRQNKSQSS", "text": "FUNCTION: Inhibitor of protein-phosphatase 1. SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family."}
{"protein": "MEAPAAGLFLLLLLGTWAPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGGGSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITEQVLTLVNKRIGLYRHFDETVNRYKQSRDISTLNSGKKSLETEHKALTSEIALLQSRLKTEGSDLCDRVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKIDHILDAL", "text": "FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. SUBCELLULAR LOCATION: Endoplasmic reticulum Endoplasmic reticulum membrane; Single-pass type I membrane protein Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the OST1 family."}
{"protein": "MVDLARRCSGSTEGRFLMWECTKWCGPGNNAKCESDLGPLEADKCCRTHDHCDYIASGETKYGITNYAFFTKLNCKCEEAFDRCLTEAYNKEEKESAKSSTKRLQNFYFGTYSPECYVVTCNSKRSGRDAGCENGVATWKKSYKD", "text": "FUNCTION: Scorpion venom phospholipase A2 (PLA2) that contains enzymatic activity, but does not inhibit ryanodine receptors in contrary to imperatoxin-1, another heterodimer of P.imperator venom. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group III subfamily."}
{"protein": "MTKYKLEYIWLDGYTPTPNLRGKTQIKEFASFPTLEQLPLWGFDGSSTQQAEGHSSDCVLKPVAVFPDAARTNGVLVMCEVMMPDGKTPHASNKRATILDDAGAWFGFEQEYFFYKDGRPLGFPTSGYPAPQGPYYTGVGFSNVGDVARKIVEEHLDLCLAAGINHEGINAEVAKGQWEFQIFGKGSKKAADEMWMARYLMLRLTEKYGIDIEFHCKPLGDTDWNGSGMHANFSTEYMRTVGGKEYFEALMAAFDKNLMDHIAVYGPDNDKRLTGKHETAPWNKFSYGVADRGASIRVPHSFVNNGYKGYLEDRRPNSQGDPYQIASQILKTISSVPTEKKAVA", "text": "FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
{"protein": "MAEKFIKHTGLVVPLDAANVDTDAIIPKQFLQKVTRTGFGAHLFNDWRFLDEKGQQPNPDFVLNFPQYQGASILLARENFGCGSSREHAPWALTDYGFKVVIAPSFADIFYGNSFNNQLLPVKLSDAEVDELFALVKANPGIHFDVDLEAQEVKAGEKTYRFTIDAFRRHCMMNGLDSIGLTLQHDDAIAAYEAKQPAFMN", "text": "FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily. SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily."}
{"protein": "MNARLASSRAWVWCFLMVGLVCGATAKAESKINYRRISLRVTDKTTGDEYFRFITILRDYVSIGSFSNDIPLLRQSTIPVSDAQRFVLVELTNQWGDSITAAIDVTNLYVVAYQAAGQSYYLRDAPHGAERHLFTGTTRSSLPFNGSYADLERYAGHRDRIPLGREPLLRSVSALHYPGGSTRAQASSIIIVIQMISEAARFNPILWRARQYINRGVSFLPDVYMLELETSWGRQSTQVQQSTDGVFNNPIRLGISTGNFVTLSNVRDVIPSLAIMVFVCRDRSSSSDVHNWPLVIRPVMVDDVTCTTSEPTVRIVGRNGMCLDVRDSDYRDGSRIQLWPCKSNSDPNQLWTIRRDGTIRSNGSCLTTYGYTAGSYIMMYDCNRAGWDLTTWQIRGNGIIFNPRSKMVIGTPSGSRGTRGTTFTLQTLDDSLGQSWLASNDTAPREVTIYGFRDLCMETSGGRVWVESCVSSKQNQRWALYGDGSIRPKPYQDQCLTSQGDSVRSVINLFSCTAGSPRQRWVFTNKGTILNLKNGLALDVRESNPSLRQIIIFSVSGNPNQMWLPVP", "text": "FUNCTION: The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily."}
{"protein": "MDAGARQIRFTGEKNWMEVTMEEEEKGKRKGCIERQQDIQDLKYPNLPAGHSHHGNKSRRRRRQSGFWRWLRGIRRQRDKPKGDSEKGLGSCVGALAELTLEEAMAEEPADAASPTADDGHLDKWTAWRLPQK", "text": "FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre- mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs (By similarity). SUBCELLULAR LOCATION: Host nucleus, host nucleolus Host cytoplasm Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm."}
{"protein": "MEEYKGVWLKAGIIYALNLASNGFKPVEVGLGERDFYVDVESDTTLTLDEAKKFATYNQYSYQLKDGYIEFNGNKIKVLGEPSSLEPKYFEILNISVHHPSPNVQYVRIRGVGFEKKEELDQYLKWLEEVSEYDHRIIGERLDLFSFPDETAPGLALFHYKGQIIRKELMKFMEEINESMGYQEVFTAEIYRSILWKTSGHYDYYKDKMVLFKMEDEELGLKPMNCPAHILIYKSKTRSYKDLPIRFSEFGLVFRWEKRGELYGLLRVRGFVQDDGHIFLTEDQIKDEVKMLVKKTIDVLSIFGFKGDDVRINLSTRPDESIGSDELWEKATNALVSALNELGIKYIVKEKEGAFYGPKIDFDIRDSLGRWWQLSTIQVDFNLPERFKLEYIDKDGSRKRPVMIHRAIYGSIERFMAILLEHFRGKLPTWLSPVQVRILPISKDVEDYALNLLSKLKENKIRVELDMSDETLSKRIKKAYDEGVPYMIIVGKKEREEGKVTVRGRNNVEIRGVKFDDFLKALLEEIRNRDLNQSAINKLK", "text": "FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MGLDLLSTYAPGIFDSLLTWKGVAGLVVAITLGYLIISRLPGQKSRPKLLDLKTGGISFEKVAAVYDDYDKSYGEGDHGELHVKDKNKVFQLANTFYDFVTDGYEWAWGSSFHFSQRMPGLSHAASQMLHESRMASFLRLKPGMKCLDVGCGVGNPGRTVASCSGAEVTGITINEYQIKRAEYHNKRTGLVGYFKPVVGNFCAMPFKDKTFDAAFAMDSTCHAPKLEDVYSEVFRVLKPGGLFATYEWVSTKDYDPNNSRHVKVMNSIIFGNGLPNIRSWKQAEDAGKNVGFKLVTSFDLATAPPVGKPWYYVPELMVKYGLLTIQKALVRGACNVGLLPNEGWKVCNMVADMVPNLVEGGATNIFTPMHLLIFEKPK", "text": "FUNCTION: Converts squalene to mono- and dimethyl derivatives, but not to tri- and tetramethylated products. Unable to methylate cycloartenol, zymosterol or lanosterol. Methylates both C-3 and C22 positions, but only C-3 position in monomethylated products. Produces mainly dimethylated squalene. SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family."}
{"protein": "MTIADASKVNHELSSDDDDDVPLSQTLKKRKVASMNSASLQDEAEPYDSDEAISKISKKKTKKIKTEPVQSSSLPSPPAKKSATSKPKKIKKEDGDVKVKTTKKEEQENEKKKREEEEEEDKKAKEEEEEYKWWEKENEDDTIKWVTLKHNGVIFPPPYQPLPSHIKLYYDGKPVDLPPQAEEVAGFFAALLESDHAKNPVFQKNFFNDFLQVLKESGGPLNGIEIKEFSRCDFTKMFDYFQLQKEQKKQLTSQEKKQIRLEREKFEEDYKFCELDGRREQVGNFKVEPPDLFRGRGAHPKTGKLKRRVNPEDIVLNLSKDAPVPPAPEGHKWGEIRHDNTVQWLAMWRENIFNSFKYVRLAANSSLKGQSDYKKFEKARQLKSYIDAIRRDYTRNLKSKVMLERQKAVAIYLIDVFALRAGGEKSEDEADTVGCCSLRYEHVTLKPPNTVIFDFLGKDSIRFYQEVEVDKQVFKNLTIFKRPPKQPGHQLFDRLDPSILNKYLQNYMPGLTAKVFRTYNASKTMQDQLDLIPNKGSVAEKILKYNAANRTVAILCNHQRTVTKGHAQTVEKANNRIQELEWQKIRCKRAILQLDKDLLKKEPKYFEEIDDLTKEDEATIHKRIIDREIEKYQRKFVRENDKRKFEKEELLPESQLKEWLEKVDEKKQEFEKELKTGEVELKSSWNSVEKIKAQVEKLEQRIQTSSIQLKDKEENSQVSLGTSKINYIDPRLSVVFCKKYDVPIEKIFTKTLREKFKWAIESVDENWRF", "text": "FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)- enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli (By similarity). SIMILARITY: Belongs to the type IB topoisomerase family."}
{"protein": "MYDYAFVHLKFTVPAAVLLTAIAYPILNRIHLIQTGFLVVVAFTAALPWDAYLIKHKVWSYPPEAIVGPRLLGIPFEELFFFVIQTYITALVYILFNKPVLHALHLNNQQNPPAWMRVVKVTGQVVLVALSVWGWNAAQVHQETSYLGLILVWACPFLLAIWTLAGRFILSLPWYATVLPMFLPTFYLWAVDEFALHRGTWSIGSGTKLDFCLFGKLDIEEATFFLVTNMLIVGGMAAFDQYLAVIYAFPTLFPKVNRYPTTHMLLQSRLINTSRYDLERIEGLREAVERLRLKSRSFYLANSLFSGRLRIDLILLYSFCRLADDLVDDAKSRREVLSWTAKLNHFLDLHYKDADATEDPKKKAERIDAYIKTAFPPCAYQALHLLPTHILPPKPLYDLIKGFEMDSQFTFHGTSDSTDLQYPIADDKDLENYAIYVAGTVGELCIALIIYHCLPDMSDTQKRELETAACRMGIALQYVNIARDIVVDARIGRVYLPTTWLKKEGLTHKMVLENPEGPEVIERMRRRLLENAFELYGGARPEMQRIPSEARGPMIGAVENYMAIGRVLRERKEGTVFVRMEGRATVPKRRRLSTLLRALYEQ", "text": "FUNCTION: Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and from lycopene to beta-carotene via the intermediate gamma-carotene and from 3,4-didehydrolycopene to torulene (lycopene cyclase). Torulene is further processed to the acidic carotenoid neurosporaxanthin. The cyclase preferentially catalyzes single cyclizations at only one end of the substrate to produce monocyclic carotenoids (PubMed:11862485, PubMed:16928467). Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme al-2 first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase al-1 then introduces 5 desaturations to lead to 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene. Al-2 cyclase activity then converts 3,4- didehydrolycopene into torulene. Al-2 can also convet lycopene into gamma-carotene which in turn is converted to beta-carotene by an additional al-2 cyclization reaction. Torulene is the substrate of the dioxidase cao-2 that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase ylo-1 mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the lycopene beta- cyclase family. SIMILARITY: In the C-terminal section; belongs to the phytoene/squalene synthase family."}
{"protein": "MEETKTHELEVEAESGSRMEKVYIAVGNDVQEGYKTIHWALKKWNNIPISIVLLHLCNISQDFVYTPFGKLPASSVSEEKLQVLRKYEDQKIDKLLSKYITFCGKVCPLSVNFVLFGKSKSAISGSFYVYQNKPEFCEFYIICGGKMVSLKNDVNNNNSNIRSWIGKMFHDPGRNLDRSSGNNDDPTASGSSWDKNLQEIENYFQQLLSLNLAEEETENVVEEEQEDDDDVALNVLQHMDVAEKLEYVRRKVNEAKLMIDEKSREVKVNAERSNRAEWAISLCNSRIGEFEAWIKEESERREKLQATLDSDKECIEEAKNYVEKGKTKLHSLAELQEVLSSKVKTMMEAKSQAEVELERVVLQRGEMITEIEKLRSQRDVFNRRIEFCKEREVIGSVSKEEVKCGYREYVAEDIRLATETYSDRLRLKSGGNWTNVYRGRIKHTTVAVKVIGDSLSDEAFGAKVKLLNEIRHPNLVAIAGFCSQRPKCLLFEYMHNGNLRDNLFTSQRKSRRSKILKWHDRIRIAHQVCSGLGFLHSVKPKPIVHGRLTPSKILLDRNLVPKITGFGLIMHSDQSDTKPDVMAFGVLLLHLLTGRNWHGLLKAMSMNQTSILRDLDQTAGKWPLELAKEFGALAVKCSSVNRGGNMDFSTKEIMEELGKIREKADEFKTKGGYEEATNSNMDEGDPNDIPSVFMCPILQEVMKNPHVAADGFSYELEAIQEWLSMGHDTSPMTNLRLDYQMLTPNHTLRSLIQDWHSKRAAQASS", "text": "FUNCTION: Functions as an E3 ubiquitin ligase. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MEHIRTPKVENVRLVDRVSPKKAALGTLYLTATHVIFVENSPDPRKETWILHSQISTIEKQATTATGCPLLIRCKNFQIIQLIIPQERDCHDVYISLIRLARPVKYEELYCFSFNPMLDKEEREQGWVLIDLSEEYTRMGLPNHYWQLSDVNRDYRVCDSYPTELYVPKSATAHIIVGSSKFRSRRRFPVLSYYYKDNHASICRSSQPLSGFSARCLEDEQMLQAIRKANPGSDFVYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQLMEQFPCAFEFNERFLIHIQHHIYSCQFGNFLCNSQKERRELKIQERTYSLWAHLWKNRADYLNPLFRADHSQTQGTLHLPTTPCNFMYKFWSGMYNRFEKGMQPRQSVTDYLMAVKEETQQLEEELEALEERLEKIQKVQLNCTKVKSKQSEPSKHSGFSTSDNSIANTPQDYSGNMKSFPSRSPSQGDEDSALILTQDNLKSSDPDLSANSDQESGVEDLSCRSPSGGEHAPSEDSGKDRDSDEAVFLTA", "text": "FUNCTION: Phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and inositol 1,3- bisphosphate (Ins(1,3)P2). SUBCELLULAR LOCATION: Cytoplasm Endomembrane system; Peripheral membrane protein; Cytoplasmic side Note=May partially localize to endosomes and/or the Golgi apparatus. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily."}
{"protein": "MTLMHPHMIKLLSLSGLTLGLLAASQGVRADEIKAPTFTAEPCCSLCPAAHDAKNYTTRYQQNFTTLVQAQGDWLFRTQEDLRTEFDTTPSGYKRMQQLHDAFKAKGVELVVVYQPTRGLVNRNKLNPEEKAKFDFDKALGNYKTMLGRFAKMGYVVPDLSPLTNEQLPDELPAHDFYFRGDQHWTPYGAQRTAKIVAAKVKQMPEYAEIPKREFETKRSGRMGKTGTLHNMAGQLCGTSYAIQYMDQFTTEPKGEAGDGDLFSDSGNPQITLVGTSHSGKNYNFAGFLEEEIGADILNVAFPGGGLEGSMIQYLGSDEFQKSPPKILIWEFSPLYRLDQETIYRQMMALLDNGCEGKTAQMSASTTLKPGKNELLVNSSNKDLRNANHQVDIRFADPSVKTLQATLWYMNGRHEDIKIEKPETSDTDGRFAFELRTDEDWASQNLLAVEVQGPEAGAAAQKVEAKICTRNVFPAGGQQTAAAGQ", "text": "FUNCTION: Plays two roles in the biosynthesis of the exopolysaccharide alginate: protects alginate from degradation as the polymer traverses the periplasm, and also plays a role in its O-acetylation. Probably has acetyltransferase activity in vivo (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the AlgX family."}
{"protein": "MTPTLLSAFWTYTLITAMTPGPNNILALSSATSHGFRQSTRVLAGMSLGFLIVMLLCAGISFSLAVIDPAAVHLLSWAGAAYIVWLAWKIATSPTKEDGLQAKPISFWASFALQFVNVKIILYGVTALSTFVLPQTQALSWVVGVSVLLAMIGTFGNVCWALAGHLFQRLFRQYGRQLNIVLALLLVYCAVRIFY", "text": "FUNCTION: Exporter of O-acetylserine (OAS) and cysteine. FUNCTION: Exporter of O-acetylserine (OAS) and cysteine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Rht family."}
{"protein": "MGSKGLKGVMVCLLILGLVLEQVQVEGKSCCKSTLGRNCYNLCRARGAQKLCANVCRCKLTSGLSCPKDFPKLVLESNSDEPDTMEYCNLGCRSSLCDYIVNAAADDEEMKLYVEQCGDACVNFCNADAGLTSLDA", "text": "FUNCTION: Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant thionin (TC 1.C.44) family."}
{"protein": "MSLTTAAPLLALLKEKDAEVKAYALQSINEGVDQFWSEVSNDLPEIEALYDDNGFQDRKMAALIASKVYYNLGEYESAVKYALAAEEKFDIDEKTQYVETIVSKSIEMYIKLATEIYNKSGEQVNLDPKLTIVFEKMMTKCTQANEYKLALGIALEAFRLDVVKSILQERLGEDQEGGSMKLMSYVLTAATTTVFNSKFKDEILRLLFDLLMPLKNADYFITSKVVVNLNDPELATQLFEKLHDEEQIEVSYQIAFDLVSSASQHLLEKLHHNLSERSYDSGLLEILTGIPTCDYYNTFLLNKKNIDISLLNKSKSSLDGKFSLFHTAVSVSNGYMHAGTTDNSFIKANLSWLGKAQNWAKFSATASLGVIHKGNLIDGKKVMAPYLPGSRSSSRFIKGGSLYGLGLIYAGFGRDIVDYLKTHLIENSGTTGDEDVDVLLHGASLGVGLAAMGTANNEVYEALKDVLYNDVATSGEAAAFGIGLTLLGTGDETAINDLFTYAQETSHGNITRGLSMALALINYGRQEQADELIDKMLASENSLIRYGGAFSIALAYVGTGNNKVVKKLLHLAVSDSNDDVRRAAVTALGFVLLRDYTTVPRIVQLLAESHNAHDRCGAAFALGIACAGKGLQAAIDVLEPMTKDPADFVRQAAMISLSLVMIQQTEKMNPKVASINSHFLSVITNKHQEGLAKFGACVALGIMNAGGRNVTIQLENAETGTLDTKSVVGLAMFTQFWYWFPMAHFLSLSFTPTTIVGVRGSDLNIPKFDMNCYAREDVFSYPKMFEESADKEVEKVATAILSTTARAKARAKKTKKEKDTNEDDKKKKEKDLKKEETKKDDAKKESEAEEDFNKNRYSSKPYKIENMSRVLPQQLKYVQFIKEERFTPVRKFKGTNGVVVLKDNKPSEPASIIETVRQSKDVNAPLPTPFKVTEELDFEKI", "text": "FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. SIMILARITY: Belongs to the proteasome subunit S1 family."}
{"protein": "MLTNTNLFFFLSLLLLSCFLQVSSNGDAEILSRVKKTRLFDPDGNLQDWVITGDNRSPCNWTGITCHIRKGSSLAVTTIDLSGYNISGGFPYGFCRIRTLINITLSQNNLNGTIDSAPLSLCSKLQNLILNQNNFSGKLPEFSPEFRKLRVLELESNLFTGEIPQSYGRLTALQVLNLNGNPLSGIVPAFLGYLTELTRLDLAYISFDPSPIPSTLGNLSNLTDLRLTHSNLVGEIPDSIMNLVLLENLDLAMNSLTGEIPESIGRLESVYQIELYDNRLSGKLPESIGNLTELRNFDVSQNNLTGELPEKIAALQLISFNLNDNFFTGGLPDVVALNPNLVEFKIFNNSFTGTLPRNLGKFSEISEFDVSTNRFSGELPPYLCYRRKLQKIITFSNQLSGEIPESYGDCHSLNYIRMADNKLSGEVPARFWELPLTRLELANNNQLQGSIPPSISKARHLSQLEISANNFSGVIPVKLCDLRDLRVIDLSRNSFLGSIPSCINKLKNLERVEMQENMLDGEIPSSVSSCTELTELNLSNNRLRGGIPPELGDLPVLNYLDLSNNQLTGEIPAELLRLKLNQFNVSDNKLYGKIPSGFQQDIFRPSFLGNPNLCAPNLDPIRPCRSKRETRYILPISILCIVALTGALVWLFIKTKPLFKRKPKRTNKITIFQRVGFTEEDIYPQLTEDNIIGSGGSGLVYRVKLKSGQTLAVKKLWGETGQKTESESVFRSEVETLGRVRHGNIVKLLMCCNGEEFRFLVYEFMENGSLGDVLHSEKEHRAVSPLDWTTRFSIAVGAAQGLSYLHHDSVPPIVHRDVKSNNILLDHEMKPRVADFGLAKPLKREDNDGVSDVSMSCVAGSYGYIAPEYGYTSKVNEKSDVYSFGVVLLELITGKRPNDSSFGENKDIVKFAMEAALCYPSPSAEDGAMNQDSLGNYRDLSKLVDPKMKLSTREYEEIEKVLDVALLCTSSFPINRPTMRKVVELLKEKKSLE", "text": "FUNCTION: Receptor-like serine/threonine-kinase acting on substrates that controls floral organ abscission. Regulated by the 'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) family of ligands. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MTKHIIVIGGGLGGISAAIRMAQSGYSVSLYEQNNHIGGKVNRHESDGFGFDLGPSILTMPYIFEKLFEYSKKQMSDYVTIKRLPHQWRSFFPDGTTIDLYEGIKETGQHNAILSKQDIEELQNYLNYTRRIDRITEKGYFNYGLDTLSQIIKFHGPLNALINYDYVHTMQQAIDKRISNPYLRQMLGYFIKYVGSSSYDAPAVLSMLFHMQQEQGLWYVEGGIHHLANALEKLAREEGVTIHTGARVDNIKTYQRRVTGVRLDTGEFVKADYIISNMEVIPTYKYLIHLDTQRLNKLEREFEPASSGYVMHLGVACQYPQLAHHNFFFTENAYLNYQQVFHEKVLPDDPTIYLVNTNKTDHTQAPVGYENIKVLPHIPYIQDQPFTTEDYAKFRDKILDKLEKMGLTDLRKHIIYEDVWTPEDIEKNYRSNRGAIYGFVADKKKNKGFKFPKESQYFENLYFVGGSVNPGGGIPMVTLSGQQVADKINAREAKNRK", "text": "FUNCTION: Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the oxidation of the terminal methyl side group of 4,4'-diaponeurosporene to form 4,4'- diaponeurosporen-4-al. SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family. CrtP subfamily."}
{"protein": "MSSTAPLLTPYKMGRFDLSHRVVLAPLTRQRSYGNVPQPHAILYYQQRTTKGGLLIAEATGISDTAQGYKDTPGIWTKEQVEAWKPIVDGVHAKGGIFFCQIWHVGRVSNNTFQPNGQAPISSTNKSLKPAVRANGIDVATFSTPRRLETDEIPFVVNDYRVAARNAIEAGFDGVEIHGAHGYLIDQFLKDQVNDRSDKYGGSLENRCRFALEVVQAVTDEIGADKVGIRLSPFASYSEAADSNPEALGLYMANALNKFGILYCHMVEPRMVKLGEKFETPHSLRPIRDAFKGTFIAAGGYNKEDGNKAVSTGYTDLVAYGRLFLSNPDLPERFEIDAPLNKYNRETFYISDPVIGYTDYPFLPSDV", "text": "FUNCTION: Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules. SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family."}
{"protein": "MNFLLSWIHWGLAALLYFHNAKVLQAAPAQGDGDRQQGEVISFLTVYERSACRPVETMVDIFQEYPDEVEYIFKPSCVALMRCGGCCNDEALECVPTEVYNVTMEIMKLKPFQSQHIHPMSFQQHSKCECRPKKEVRIRQENHCEPCSERRKHLYKQDPLTCKCSCKFTDSRCKSKQLELNERTCRCEKPRR", "text": "FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the PDGF/VEGF growth factor family."}
{"protein": "MSNVKKHVSTINPVGEVLDVGSADEVQWSDASDVVVVGWGGAGASAAIEAREQGAEVLVIERFSGGGASVLSGGVVYAGAVPATRRKPASRFTEAMTAYLKHEVNGVVSDETLARFSRDSVTNLNWLEKQGATFASTMPGYKTSYPADGMYLYYSGNEVVPAYGNPQLLKKPPPRGHRVVAKGQSGAMFFAALQKSTLAHGARTLTQARVQRLVREKDSGRVLGVEVMVLPEGDPRTERHKKLDELVAKSACIRRRVPRRVAVNVRRSRARSARSATSVPAKVWCCPLAAISSIRNCWSMRRYKPGWLTGAAGCDGSGLRLGQSVGGIAQDLNNISAWRFITPPSVWPKGLVVNIQGERFCNEQVYGAKLGYEMMEKQGGQAWLIIDSNVRRQAAWQCLFGGLWAFQSMPALALMYKVAIKGKSVDDLAKKLRMDAAVLQLQFDRANAPARGEIEDPLGKSQDMRHEFKGGSLFAIDISISQKMFPLAVLSLGGLKVNEDNGAVIDGAGYDIPGLYAAGVPPLVWLPRVT", "text": "FUNCTION: Involved in the degradation of steroids having an A:B ring fusion in a trans configuration. Catalyzes the elimination of hydrogens located at positions 4 and 5 and the introduction of double bonds into ring A. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family."}
{"protein": "MLRSLLLRRSNARSLRPPFPPLRTLCTSGQTLTPAPPPPPPPPPPISSSASEKEFRKYAGYAALALFSGAATYFSFPFPENAKHKKAQIFRYAPLPEDLHTVSNWSGTHEVQTRNFNQPETLADLEALVKEAHEKKNRIRPVGSGLSPNGIGLSRSGMVNLALMDKVLEVDKEKKRVRVQAGIRVQQLVDAIQEYGLTLQNFASIREQQIGGIIQVGAHGTGARLPPIDEQVIGMKLVTPAKGTIELSKDNDPELFHLARCGLGGLGVVAEVTLQCVERQELLEHTYVSTLEEIKKNHKKLLSTNKHVKYLYIPYTDTVVVVTCNPVSKWSGAPKDKPKYTTEEALKHVRDLYRESIVKYRVQDSSKKTPDSREPDINELSFTELRDKLIALDPLNDVHVGKVNQAEAEFWKKSEGYRVGWSDEILGFDCGGQQWVSETCFPAGTLAKPSMKDLEYIEQLKELIQKEAIPAPSPIEQRWTGRSKSPMSPAFSTAEEDIFSWVGIIMYLPTADPRQRKDITDEFFHYRHLTQAKLWDQYSAYEHWAKIEIPKDKEELEALQERLRKRFPVDAYNKARRELDPNRILSNNMVEKLFPVSKTA", "text": "FUNCTION: Involved in the biosynthesis of ascorbic acid. Uses L- galactono-1,4-lactone as substrate, but not L-gulono-1,4-lactone, D- galactono-1,4-lactone, D-gulono-1,4-lactone, D-erythronic-1,4-lactone, D-xylonic-1,4-lactone, L-mannono-1,4-lactone, D-galactonic acid, D- glucuronic acid or D-gluconic acid. FAD, NAD, NADP and O(2) cannot act as electron acceptor. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein."}
{"protein": "MSEPESSVANNDGESTQAPQLAELTLKNVLGDIVNGVHFIIFDPLGNRFVVPVIILLTSIITKVIITKVPYTEIDFVTYMQQIQLVNQGEIDYAEISGDTGPIVYPAGFVQIYQWLYSQTNGGADIATGQSIFGYLMTATVVFVCVAYTMSPTTKPWVLFLLLGSKRLYSIYVLRLFNDCFTTAAMVGVTVFLQQGSYWYSTSSFISFLFAIVGADLFSIAISIKMNALLYLPAVVIIAYFLVGENILLFAIVLAIVPLVQILVGWKFLLPLFDDEAASQIRWNYINNAFNFGRKFLFKWTVNWRFIGEETFLSDKFSILLMGGHIVVLLFFIFTRFLNSKVTGKSIWQLIKDAFKPSSTISSNNKLIDYNVGPKLILLILATTNVIGVLFSRSLHYQFLSWYCWQLPFLLHSTGWNFIVCLVLWGAHEWTWNVYPSTVASSLVLVGILSSVLVGTWRNEAVWFEENNVVDDEKKNE", "text": "FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ALG3 family."}
{"protein": "MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVLKNVRIDPSSLSFNMWKEIPIPFYLSVYFFDVMNPSEILKGEKPQVRERGPYVYREFRHKSNITFNNNDTVSFLEYRTFQFQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNRTVGEIMWGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGLSKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYRFVAPKTLFANGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFLNADPVLAEAVTGLHPNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESGAMEGETLHTFYTQLVLMPKVMHYAQYVLLALGCVLLLVPVICQIRSQVGAGQRAARADSHSLACWGKGASDRTLWPTAAWSPPPAAVLRLCRSGSGHCWGLRSTLASFACRVATTLPVLEGLGPSLGGGTGS", "text": "FUNCTION: (Microbial infection) Mediates uptake of M.fortuitum, E.coli and S.aureus. FUNCTION: (Microbial infection) Facilitates the entry of human coronavirus SARS-CoV-2 by acting as an entry cofactor through HDL binding. FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes and appears to facilitate its cell entry (PubMed:12356718, PubMed:12913001, PubMed:18000990). Binding between SCARB1 and the hepatitis C virus glycoprotein E2 is independent of the genotype of the viral isolate (PubMed:12356718). FUNCTION: Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells (PubMed:12016218, PubMed:12519372, PubMed:21226579). Receptor for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux (PubMed:26965621). Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity (PubMed:12016218). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Membrane, caveola; Multi-pass membrane protein. Note=Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae. SIMILARITY: Belongs to the CD36 family."}
{"protein": "MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQLPAAPPTGPRDSDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSRSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTMVGIGKRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSSETFQISLKSKQGPIDVFLCPEESADGISPGKTSCQETSSGEDRTADSGPAGPPPSPPSTSPALDPSQSLLGLEQEAVLPRMGHLRVPMEEDQLSPLVAADSLLEHVKEDFSGLLPGEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF", "text": "FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication (PubMed:11672531, PubMed:20176812, PubMed:9674698). The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase (By similarity). E2F1 binds preferentially RB1 in a cell-cycle dependent manner (By similarity). It can mediate both cell proliferation and TP53/p53-dependent apoptosis (PubMed:9674698). Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:11672531, PubMed:20176812). Directly activates transcription of PEG10 (By similarity). Positively regulates transcription of RRP1B (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the E2F/DP family."}
{"protein": "MDSSSTKSKISHSRKTNKKSNKKHESNGKQQQQQDVDGGGGCLRSSWICKNASCRANVPKEDSFCKRCSCCVCHNFDENKDPSLWLVCEPEKSDDVEFCGLSCHIECAFREVKVGVIALGNLMKLDGCFCCYSCGKVSQILGCWKKQLVAAKEARRRDGLCYRIDLGYRLLNGTSRFSELHEIVRAAKSMLEDEVGPLDGPTARTDRGIVSRLPVAANVQELCTSAIKKAGELSANAGRDLVPAACRFHFEDIAPKQVTLRLIELPSAVEYDVKGYKLWYFKKGEMPEDDLFVDCSRTERRMVISDLEPCTEYTFRVVSYTEAGIFGHSNAMCFTKSVEILKPVDGKEKRTIDLVGNAQPSDREEKSSISSRFQIGQLGKYVQLAEAQEEGLLEAFYNVDTEKICEPPEEELPPRRPHGFDLNVVSVPDLNEEFTPPDSSGGEDNGVPLNSLAEADGGDHDDNCDDAVSNGRRKNNNDCLVISDGSGDDTGFDFLMTRKRKAISDSNDSENHECDSSSIDDTLEKCVKVIRWLEREGHIKTTFRVRFLTWFSMSSTAQEQSVVSTFVQTLEDDPGSLAGQLVDAFTDVVSTKRPNNGVMTSH", "text": "FUNCTION: Involved in both the vernalization and photoperiod pathways by regulating expression of the related floral repressors FLOWERING LOCUS C (FLC) and FLOWERING LOCUS M (FLM). Together with VIN3, required during vernalization for the modifications of FLC and FLM chromatin that are associated with an epigenetically silenced state (e.g. chromatin modifications, histone deacetylation, and trimethylated H3 'Lys-4' H3K4me3 and 'Lys-27' H3K27me3) and with acquisition of competence to flower. Promotes flowering in short days (SD=8 hours light/16 hours dark). Associates dynamically at FLC locus; during vernalization, binds to specific sites, but when in warm conditions, distributed along the whole locus. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Note=Probably DNA-associated."}
{"protein": "MPAKLGYWKIRGLQQPVRLFLEYLGEEYEEHLYGRNDREKWLGDKFNMGLDLPNLPYYIDDKCKLTQSVAIMRYIADKHGMLGSTPEERARISMIEGAAMDLRIGFGLTCYNPKFEELKGDYLKGLPTTLKMWSDFLGDRQYLIGSSVSHVDFMVYEALDCIRYLAPQCLDDFPKLKEFKSRIEDLPKIKEYMKSERFIKWPLHSWTSPFGGGDAPPA", "text": "FUNCTION: GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SIMILARITY: Belongs to the GST superfamily. Mu family."}
{"protein": "MNVTSPKDGNHSFSKKNRFNTNKPRFHKLNEQAQSINLPEDRDSIVSSNTTSIMTDDAFDYNEGIASRTKNINSDSDRSNDTIKQNNYNKRETGYNPFYNGSGINQRYTQFRKREFEPTLAENKAEEYISDEDNVKIDEDNIENELQFTPKIKEASILRSSLLGQRNVLNTRNPKSKESHIKVKPIINNKSSSQRKSSAALRKQLGKPLPLPYLNSPNSDSTPTLQRKEEVFTDEVLQKKRELIESKWHRLLFHDKKMVEKKLESLREYERKRMPPRGTDVSSSEQDNSFKISTPTKSYVSLEQKPLPNLSAMNNFNDVTDNKEKEETNNNILKFQAQRDPLQILQSEIEMHTKKLDTIIELLKDDTDSKEKRKVVTNDNAAPEQMVNKGWRKNVMMIYKKSGNIMKKYREYFLWTICILILLYCNIYVYYRF", "text": "FUNCTION: KAR1 is required for function of both intranuclear and extranuclear microtubules. KAR1 helps localize CDC31 to the spindle pole body (SPB), CDC31 then initiates SPB duplication via interaction with a downstream effector. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body."}
{"protein": "MAYSATQSKSGYQAGVKDYRLTYYTPDYTPKDTDVLACFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDLLTDLDRYKGRCYDIEPVPGEDNQYFCFVAYPLDLFEEGSVTNMLTSIVGNVFGFKALKALRLEDVRIPVAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYEALRGGLDFTKDDENINSQPFQRWRDRYLFVMEAVHKAQAETGEIKGHYLNVTAPTCEEMFKRAEFAKELGAPIIMHDYLTAGFTANTSLAKWCRDNGILLHIHRAMHAVIDRQKNHGIHFRVLAKCLRMSGGDHLHSGTVVGKLEGDRAITMGFVDLMRENYVEADRSRGIFFTQDWASMPGVMPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACIQARNEGRDLAREGNDIIREAAKWSPELAAACELWKEIKFEFKAVDTL", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Carboxysome. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
{"protein": "MKKWFPALLFSLCVSGESSAWNNIVFYSLGDVNSYQGGNVVITQRPQFITSWRPGIATVTWNQCNGPEFADGFWAYYREYIAWVVFPKKVMTQNGYPLFIEVHNKGSWSEENTGDNDSYFFLKGYKWDERAFDAGNLCQKPGEITRLTEKFDDIIFKVALPADLPLGDYSVKIPYTSGMQRHFASYLGARFKIPYNVAKTLPRENEMLFLFKNIGGCRPSAQSLEIKHGDLSINSANNHYAAQTLSVSCDVPANIRFMLLRNTTPTYSHGKKFSVGLGHGWDSIVSVNGVDTGETTMRWYKAGTQNLTIGSRLYGESSKIQPGVLSGSATLLMILP", "text": "FUNCTION: Tip adhesin component of type P pili that plays a critical role in kidney infection through targeted interaction with the globoseries glycolipids containing the Gal-alpha(1-4)-Gal disaccharide present on uroepithelial cells (PubMed:11440716, PubMed:31361021). In turn, transcriptionally regulates host gene expression in kidney cells, leading to inflammatory pathway activation and renal tissue damage. Acts thereby as key determinant of invasive uropathogenic E.coli (UPEC), which cause pyelonephritis and urinary-source bacteremia (By similarity). SUBCELLULAR LOCATION: Secreted Fimbrium Note=At the tip of P pili. SIMILARITY: Belongs to the adhesin PapG family."}
{"protein": "MGVDLGGLVEPREIELKELNNRTVAVDAYNTLYQFLSIIRQQDGAPLADDRGNVTSHLSGIIYRVTNLVEEGMKPVFVFDGKPPSFKAETIKARAEVREAARQMYEAAKAAGSAEAYKYAQASTSINRQIVDDAKVLLGYMGIPFIVAPSEGEAQAAYMVSRGAADYVGSQDYDSLLFGAPRVVRNIAITGKRKVPRKNIYMDVKPEVIELQEVLATLGLTREELIDMAILVGTDYNPGIFKVGPKTALKLVKKHGDNMPAILDELGQTIENWEAIKEFFLHPTVTDDYQVKWGKPEPAKIKEFLCEEHSFSVDRVDKVLERLTTAVSETTKQKTLSSWF", "text": "FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity). SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily."}
{"protein": "MATLYDVPPEELIEALTETLADEDDIEAPDWAEFTKTGVDRELPPEQEDFWTRRAASLLRKVAVDGPVGVNALRSEYGTSKQGTTRYRVRPHQKTKGSGNIIRTALQQLEDAGYVETSENDGRRVTGDGRSLLDDTAGDLLTELDRPELERYA", "text": "FUNCTION: May be involved in maturation of the 30S ribosomal subunit. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 family."}
{"protein": "MSVAASASRSASTLCSPQIQQGALKEAKVPPHIWAARHWNLGLRLVPGHASVRAGILVLLIFLPSTLCDLGSVYDSSYETVIPERLPGQGSDDPGGKVSYVLLMQGQKQLLHLEVKGHYSERNFPVYSYHHGILGQEVPLLSQACHYEGHIEGVPGSFVSVSICSGLRGVLIKEETAYGIEPLLFSTDFEHILYTMAHQPVVLCNVTPTDSLGDSSQRQGSSKTDELLALSDLWSHAKYVEMFVVVNHQRFQMWGSDVNTTVQAVVDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFNLWRQEKLMGRVRHDVAHLIVGHRPGANEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDRPGCTCGPKHLCLMHETISKTSGFSNCSSDHFLRFLHDHRGACLLDRPWHQSHKRRDAHCGNGVVEESEECDCGNACDSHPCCEPTCTLKVGAQCSEGLCCYKCTFKKKGTLCRPAEDVCDLPEYCNGITGECPANSYMQDGTQCDRIYYCSGGLCKNPDKQCARIYGYPARSAPEECYISVNTKANRFGNCGHPTSANLKYEACSNEDIFCGKLVCTDVRYLPQVKPLHSLLQIPYGDDWCWSMDAYNVTDIPDYGDVQGGTYCAPKKVCMESICTGHATLQYDCHPQEMCHGNGVCNNFKHCHCDAGFSPPDCSSGGNGGSVDSGPVGKPADRNLSLFGVGESPDSRMEDEEINLKVVVLVVPIFLIVLLCCLMLIAYLWSEVQEAVSPGSSSTTSSSESESD", "text": "FUNCTION: May be involved in sperm-egg fusion. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MLGAKPHWLPGPLHSPGLPLVLVLLALGAGWAQEGSEPVLLEGECLVVCEPGRAAAGGPGGAALGEAPPGRVAFAAVRSHHHEPAGETGNGTSGAIYFDQVLVNEGGGFDRASGSFVAPVRGVYSFRFHVVKVYNRQTVQVSLMLNTWPVISAFANDPDVTREAATSSVLLPLDPGDRVSLRLRRGNLLGGWKYSSFSGFLIFPL", "text": "FUNCTION: May be involved in synaptic functions in the CNS. SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus, cis-Golgi network Secreted Synapse Note=In the absence of CBLN1, remains in the endoplasmic reticulum/cis-Golgi apparatus. Partial secretion depends on an association with CBLN1 and maybe CBLN4, but not on CBLN2 (By similarity)."}
{"protein": "MAGINQTKCDLGFQITFNTVYRFSQFYTFSVSSFAVPGLIYFMFKRLFQLYFHGNLKTLLIAYFISILLYAVMLCFAFGYQFFVPFFIKSNCDLIINKTLFKYIHTSVIFLLTTPMMFPLGFSIERFTAMAMASRYENIRTLIGPVLVIFLIIPNCIIFYFLFQHETYDDTFISFLMLPNTTAVNFNTYLWFLLYLNIGNLALNVLLLLVHRKFKRRLLLHKTSLSTRYAIEEISQSSKFTLIITFTHLLFFGCNTICSILVRVLGEPFFGSFINHSVARGVNCAVPTYNLVIVVVGFVSLSKLNSRRQQEVQTTVQLKTTGKEGARNYDNITANQWATITQIGF", "text": "FUNCTION: G-protein coupled receptor that antagonizes the negative effects of the gcy-35 oxygen sensor on spermatogenesis (PubMed:28662030). This leads to the maintenance of mitochondrial function in developing spermatocytes and/or spermatids prior to testis maturation during the early larval stages (PubMed:28662030). Regulates the navigational capacity of sperm during hyperoxic conditions ensuring the proper targeting of sperm derived from males to the fertilization site in the uterus of hermaphrodites (PubMed:28662030). May act in the same signaling pathway as the neuropeptide flp-21 (PubMed:28662030). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Perikaryon Cell projection, dendrite Note=Detected in ciliated sensory neurons. SIMILARITY: Belongs to the nematode receptor-like protein srb family."}
{"protein": "MPDYMVTLESAWIIKDVKTMDDAISIAIGEAGKRLNPAAKYVEIETGMMVCPLCNKALNCAVVVANTALVGLTLQMKVFRAESEEHAVRIAKSVIGKALRDVPLNVQDVQEL", "text": "SIMILARITY: Belongs to the UPF0212 family."}
{"protein": "MAKWGSPFVFALACLALSWRVYGDDFDLYDALGDPTEKPKPKPPKPPKSPTHDSGDLDLSDFFDTPVKTTTKSPRLPPKQPDLRFSTTTKKPRTTKIPPKKSDPNDFDLSDALDGNNGKGDISDSDLDDILNDGYNPDKKKGGGGGGGGGGRATGQGDNDGSDTGFGSQAETGTIAGIASALAMALIGAVSSYISYQQKKFCFSIQEGLNAEYVKGEHMEAVVSEEPQVKYSVVESQSAIP", "text": "FUNCTION: May function as a homophilic adhesion molecule. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein; Extracellular side Cell junction. SIMILARITY: Belongs to the CD99 family."}
{"protein": "MEAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVINQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQKIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS", "text": "FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. SIMILARITY: Belongs to the eukaryotic AdoMetDC family."}
{"protein": "MLLLPFQLLAVLFPGGNSEHAFQGPTSFHVIQTSSFTNSTWAQTQGSGWLDDLQIHGWDSDSGTAIFLKPWSKGNFSDKEVAELEEIFRVYIFGFAREVQDFAGDFQMKYPFEIQGIAGCELHSGGAIVSFLRGALGGLDFLSVKNASCVPSPEGGSRAQKFCALIIQYQGIMETVRILLYETCPRYLLGVLNAGKADLQRQVKPEAWLSSGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGEQEQQGTQLGDILPNANWTWYLRATLDVADGEAAGLSCRVKHSSLEGQDIILYWRNPTSIGSIVLAIIVPSLLLLLCLALWYMRRRSYQNIP", "text": "FUNCTION: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endosome membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes."}
{"protein": "MRSLLLWIAVVVCLLCSVAAVVQSGSSDGFGKPRDTETAISFLEYKLMAPSVPMIPLTLIHGADSKGAVCLDGTLPGYHLDRGFGSGANSWLIQLEGGGWCNNHRSCVYRKTSRRGSSKFMEKALAFTGILSNRSEENPDFFNWNRIKLRYCDGASFSGDSQDESSQLFYRGQRIWQVAMEEFLSLGMKQANQALLSGCSAGGLASILHCDEFRELLPSSTKVKCLSDAGMFLDSVDVSGGHSLRNMFQGVVTVQNLQKDLSSTCTNHLDPTSCFFPQNLVSDIKTPMFLLNTAYDSWQIQESLAPPTADPGGIWKACKSDHSRCNSSQIQFFQEFRNQMLFAVNSFSNSDQNGLYINSCFAHCQTERQDTWFAQDSPQLNGKRVAESVGDWYFDRAKNVKAIDCPYPCDTTCHNLIFE", "text": "FUNCTION: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the pectinacetylesterase family."}
{"protein": "MKQKRLLRRDGFTFKQFFVGHDRCAMKVGTDGVLLGAWTPVSDKKAILDIGCGSGLIALMLAQRTDENTKIDAVELDTEAALQAQDNAEQSPWQRKIDVYQQDIGDFAEQYSQCYDLIVSNPPYFEPAVACRNEAREQARYTGSMTHQQLLQYAETLITADGLFCVVLPYAIGEEFETMACHQGWFSHHRVNIRDRQGKPLHRMLLAFSRKEKTGLISELTIRQPDGAYTQEFQQLVTDFYLYY", "text": "FUNCTION: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. tRNA (adenine-N(6)-)-methyltransferase family."}
{"protein": "MSSVAENIIQHATHNSTLHQLAKDQPSVGVTTAFSILDTLKSMSYLKIFATLICILLVWDQVAYQIKKGSIAGPKFKFWPIIGPFLESLDPKFEEYKAKWASGPLSCVSIFHKFVVIASTRDLARKILQSSKFVKPCVVDVAVKILRPCNWVFLDGKAHTDYRKSLNGLFTKQALAQYLPSLEQIMDKYMDKFVRLSKENNYEPQVFFHEMREILCALSLNSFCGNYITEDQVRKIADDYYLVTAALELVNFPIIIPYTKTWYGKKTADMAMKIFENCAQMAKDHIAAGGKPVCVMDAWCKLMHDAKNSNDDDSRIYHREFTNKEISEAVFTFLFASQDASSSLACWLFQIVADRPDVLAKIREEQLAVRNNDMSTELNLDLIEKMKYTNMVIKETLRYRPPVLMVPYVVKKNFPVSPNYTAPKGAMLIPTLYPALHDPEVYENPDEFIPERWVEGSKASEAKKNWLVFGCGPHVCLGQTYVMITFAALLGKFALYTDFHHTVTPLSEKIKVFATIFPKDDLLLTFKKRDPITGEVFE", "text": "FUNCTION: C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8635732, PubMed:8543054). ERG5 converts 5- dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (PubMed:8635732, PubMed:8543054). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4- dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3- beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron- containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C- methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl- methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen- 3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MPKNMAALQQSLYTGPSTPSHTQFSRSTEFPENLNFDVLNDSYETFSSVSLTTAEQDNQIDKILQESAAMNRDVNSELAQFTASEYVTGFRADTMEPEVIVETIGDSMKRKASELDSDSDSGESSKGKKRVIKPKMRQRYKKATIQNKTSLTEECNYNTEICTVAPTDQIAEYFKHDFSVYLEKQKSDCQMSANRFSDYISETGYYVFVVKKSEHKPFEVVFAKFVNNVTNEYTNNYYMVDNRVFVVSLNNVKFMVSYKLVREQGIDIPPHVNLCDDAQAERNPYDCYFEPVKNVFQTTLINHFHLDMYYSQTTFVTLMQSMGESKSGMLLNKLYQMFQDRSLFTLPIMLSRKEPTIENTPLSRNYTSSYVAQIIKYSKNVRFPENNPDNGVISRLEEIVTQKSSLTYKYSSVANLLFSRYGHQRDNNADSLKKVKKEDGNRLLVEQYMSQNENDETSHNFIVLQFGGVNDERLTIAKKGIEFFWIAAEIKDINVDDLVKKYTRNVHHVFRIINVNRRESTTWHNNLLKLLQLLLQNLIRIDDVQQYSNKGDSKFIYKRL", "text": "FUNCTION: Regulatory transcriptional protein, which trans-activates gene expression from early baculovirus promoters. Can also trans- activate its own promoter, suggesting that it is autoregulated during normal infection of insect cells. SIMILARITY: Belongs to the nucleopolyhedrovirus IE-1 protein family."}
{"protein": "MPNFFRNGCIALVGSVAAMGAAHAEGGIAEAAGKALDSAQSDVTITAPKVMMVVATVVGVGILINMMRKA", "text": "FUNCTION: Fimbriae (also called pili) are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs. Flexible pili possess hemagglutinating function. SUBCELLULAR LOCATION: Fimbrium."}
{"protein": "MMAPSIDTMAEELDTSITESTMALSVYLLATAFGPLIIGPVSEIYGRKSIFHITNIWFLVWNLVCGFAHSKGLLMAARLLAGFGASAVYSLGYGVLGDVWSAEQRGRSLSLYLLIPLTGSAVGPIVSGFIVKYSTWRWMFWSTAILQLTLDLSSLLFHESYAPLLLRRRAEELRSNTGGSRYHAAIEMREAGLSPPRKLSRSLSRPLRLLAFHPIIQMQAILEGIDYGLLYFALSSFSALHVAAYGESVEISGLHYIVICIGTVSGSQLCGPLMDYAYQRLSSNTGETQVPELRIPLLLPGALITPIGFLLYGWAAQYHLIWVVVDVGAALLSLGMQIFDTTLHAYVMDSYPEHVSSASAATQVLRSLLAFAFPLFSNSLYDSLGYGLGNSLLAFLSIGIALPATGILWRWGATLRGRQQSSY", "text": "FUNCTION: Probable efflux pump; part of the gene cluster 27 that mediates the biosynthesis of asparasone A, a sclerotium-specific anthraquinone pigment important for sclerotial survival (PubMed:24412484). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MNDLTLSPIAIIHTPYKEKFSVPRQPNLVEDGVGIVELLPPYNSPEAVRGLEQFSHLWLIFQFDQIQQGKWQPTVRPPRLGGNQRVGVFASRATHRPNPLGLSKVELRQVECINGNIFLHLGAVDLVDGTPIFDIKPYIAYADSEPNAQSSFAQEKLPVKLTVEFTEQAKSAVKKREEKRPHLSRFIRQVLEQDPRPAYQQGKPSDRIYGMSLYEFNVKWRIKAGTVNCVEVIEIEKDK", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability. Binds to tRNA. SIMILARITY: Belongs to the tRNA methyltransferase O family."}
{"protein": "MQDQQIINPISQSQIPQELSENVILSSVSDLYDWARLSSLWPLMYGTACCFIEIAAMIGSRFDFDRFGLVPRSSPRQADLIITAGTVTMKMAPALVRLYEQMPDPKYVIAMGACTITGGMFSSDSTTAVRGVDKLIPVDVYLPGCPPRPEAVMDAIVKLRKKIANEDVRERGNLMQTHRYYSTTHQMKVVPPIHTGVYLEAAARKSPAAALGAGVGEDMTPALVAEAEKEEA", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MARAAALLPSRSPPTPLLWPLLLLLLLETGAQDVRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDAPANHQNVAAFHPKMGPSFPSPKPGSERLSFVSAKQSTGQDTEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVIAKPKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPVTLSVRYPPEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQVIFVRETPNTAGAGATGGIIGGIIAAIIATAVAATGILICRQQRKEQTLQGAEEDEDLEGPPSYKPPTPKAKLEAQEMPSQLFTLGASEHSPLKTPYFDAGASCTEQEMPRYHELPTLEERSGPLHPGATSLGSPIPVPPGPPAVEDVSLDLEDEEGEEEEEYLDKINPIYDALSYSSPSDSYQGKGFVMSRAMYV", "text": "FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1 (HHV-1) mutant Rid1, herpes simplex virus 1 (HHV-2) and pseudorabies virus (PRV). FUNCTION: Modulator of T-cell signaling. Can be either a costimulator of T-cell function, or a coinhibitor, depending on the receptor it binds to. Upon binding to CD226, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell proliferation. These interactions are competitive (PubMed:26755705). Probable cell adhesion protein (PubMed:9657005). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the nectin family."}
{"protein": "MGAGQSTDSKALGTSPEEMSHILARRFASKCFTPLELAHLKDNFNSLALKQGDIRYWNEEVLSRFLGIPDGNGKFGDGDLDAGPVIFRMVSYLGAFPFQNTLAPSVLTFDALVKVIVLLTDRYGKVLRRGKKDRIKLLFGSLADVGRKEELPVPDNESKDKPDNTPNKSGTQSQTAGFSIDKPSNDNDDEEDNDDDDLALAALESLDAIEVFKHDQRIDRTVYEAHVSFDTFQRLLMLLVVLAPLRTNEETSQYFSQLNEDSMEAARRCVENILTSFDIGDRKSGIGYETFSWVISSSLPYIFDPLTPLFEHLLFSKNLDLSRRRDSGTSSPSEEKNAAPLSSLTPSKPSITLSGSFESCILDSAIISHLSFFLPTSSPIPNLLQNGTRLHGVFSSDTHGESLTSFSHNVLTWDAPSIMLVTGAKKDPSGDETESITIGAYIPRAWKSSTSASASHHDLSNQFQLPYLFQLSPNHVVMQGSPSINSLKANRPMVSFSTKSGIAIGCKIPPPTRTSLSSDSSRPTPAGGGSLLIDPALENAEFFMSNGLSHEEGVFLPAGAATWSPSHSSSTAASETIHISIYNIEVWGIVHTVTISKHSSSKHSRSSTANGAIPDAIMRQQAHWNFEAREAERRREIHLNVGGGDSEEQTGRALLEMAGIIGSSSRYR", "text": "FUNCTION: May be involved in a process influencing telomere capping. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RTC5 family."}
{"protein": "MTKLGWGRRVVWGAALAAVAMLGACNGDESAERNRLPGFVSGSVRTTAYDGASDDLLTAGLGKTGLAAATAPGFANPSRPTSAELRRLAIWSNYRALVDMSANGGYGRFWGPNVDLDGNDTLGEGKIPGTEYLAYADDGSGSKNVTLLVQVPASFNPAQPCIVTATSSGSRGVYGAISAAGEWALKRGCAVAYNDKGGGNGAHELGSDTVTLIDGTLANAVLAGTASLFTANVTSGDLAAFNSRFPNRYAFKHAHSQQNPEQDWGRVTLQSVEFAYWALNEQFGPVIDGARHGVRYRAGDITTIAASVSNGGGASLAAAEQDNRGWITAVVVGEPQINVRMAPNAVVRAGGQPVPSFGRPLADYATLANLLEPCAAASASLAGAPYLSALPATTTQSIRTQRCATLAAAGLVAGADTQSQAADALAQLHAAGYLADSDLLQAPMWDSQAIPAIAVTYANAYTRSRVTDNLCNFSFATTNPATGVVAAPAASPMPSVFGVGNGVPPTAGINLVFNDGAGTDHRLATPDASFAGALCLRQLWTNGMLGMPANVDAVRVNANLHGKPAIIVQGRSDALVPVNHASRAYVAQNGISEAGRSQLVFYEVTNGQHFDAFLSVPGFDTRFVPVHYYNVQALNLMWRHLKNGAPLPPSQVIRTVPRGGTPGAAPALTSANLPPISTAPGANAIATGVGTIDVPL", "text": "FUNCTION: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB- oligomers) into 3HB-monomers. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase family."}
{"protein": "MKAKPLSQDPGSKRYAYRINKEENRKELKHVKINESSLVQEGQKIDLPKKRYYRQRAHSNPFSDHQLEYPVSPQDMDWSKLYPYYKNAENGQMTKKVTIADIGCGFGGLMIDLSPAFPEDLILGMEIRVQVTNYVEDRIIALRNNTASKHGFQNINVLRGNAMKFLPNFFEKGQLSKMFFCFPDPHFKQRKHKARIITNTLLSEYAYVLKEGGVVYTITDVKDLHEWMVKHLEEHPLFERLSKEWEENDECVKIMRNATEEGKKVERKKGDKFVACFTRLPTPAIL", "text": "FUNCTION: Methyltransferase that catalyzes the formation of N(7)- methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity. FUNCTION: Methyltransferase that catalyzes the formation of N(7)- methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family."}
{"protein": "MTARLRPVLAGLPVYVPGKTVPGAIKLASNETVFGPLPSVRAAIEHATQSINRYPDNGCLAVKAALARHVSSLSAADFGPEHIAVGCGSVSLCQQLVQITASVGDEVIFGWRSFELYPPQVQVAGATAIQVPLTNHTFDLEAMLAAVTERTRLIIVCNPNNPTSTVVQPEALAEFVRSVPPHILVAIDEAYVEYLRDGTVPDSPHLVRTHSNVVVLRTFSKAYGLAGLRVGYAVGQPDVIAALDKVYVPFTVSSLAQAAAIASVQAADELLARTDAVVAERGRVSAELRAAGFTVPPSQANFVWLPLEDRTTDFVTQAAKAHIVVRPYGADGVRVTIAAPEENDALLRFARCWITHRDGAR", "text": "FUNCTION: May catalyze the transamination reaction in phenylalanine biosynthesis. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MTSLSRPRVEFISTILQTVLNLGLLCLGLILVVFLGKETVHLADVLFAPEQASKYELVEGLVVYFLYFEFIALIVKYFQSGFHFPLRYFVYIGITAIVRLIIVDHKSPLDVLIYSAAILLLVITLWLCNSKRLKRE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsiE family."}
{"protein": "MPPSLRKAVAAAIGGGAIAIASVLITGPSGNDGLEGVSYIPYKDIVGVWTVCHGHTGKDIMLGKTYTKAECKALLNKDLATVARQINPYIKVDIPETTRGALYSFVYNVGAGNFRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREVCLWGQQ", "text": "FUNCTION: Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Exhibits lytic activity against E.coli and S.typhi cell wall substrate. SIMILARITY: Belongs to the glycosyl hydrolase 24 family."}
{"protein": "MIVLLLLISYCFAGNGVNVKNQLLLMPYPTTVNAQFGSNDCVEATSNIKMVLSNNCQNDPNCLSFMTFNFNHTITYPLQRQRNLEDFRVSIFAPIDIEEMKGNVVYSANTVNIELTGNNIEEIYPPLKIGIDESYSLDVTKEGIKISATTVYGARLGLETLIQMLRPYQGKYIIKHIPIMIEDKPRLQWRGLMIDVARNSFSRSAFVKIINAMAAIKANVLHIHLSDAQTFMFESKEYPELSKKGAFFQNKVLTQSFIKQLVQYGAKRGVIVYPEIDTPAHTASWNAGYPGVVADIWDYIVSSSMRYGENVLALNPANEKTFSIIDALMKEMGEVFGNDYVHFGGDEVWTGAWSKAKEYPAILEWMNKKGINTLKELEAYFNKYAQEQIIKNGKTPVCWEEVYQKGSADKKTIIQVWNNVNLLKEAATAGYKVILSAGYYLDMQMPLCSDYVADSCTNPNHMWVWTNRDMYRNDPIKELDYATKQNVLGGEACSWDESVDEQNFFDRVFQRFSAVAERFWSSEDITDPESHEVRANYVRCLGLRRNFLKGTGPLYHSYCQLPEDI", "text": "FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates (PubMed:15555733). May contribute to amoebic pathogenicity and may be involved in the destruction of extracellular matrix components (Probable). SUBCELLULAR LOCATION: Cytoplasmic granule Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 20 family."}
{"protein": "MMMRVFIAMFFLLALVEAGWPRLYDKNCKKNILRTYCSNKICGEATKNTNGELQCTMYCRCANGCFRGQYIDWPNQQTNLLFC", "text": "FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin E superfamily."}
{"protein": "MAKVRLTTEEIMKIGFFEKIANVPILDCVLNDERVAFIVKEGDVGAAIGKGGENVKTAEEKFGKKVDIIEYSDDWRKFIRNIFAPIQLDDVWVKRVGKDVVAFIKINPKVRRAVFGEKGKNLERALKILKRHTKITKIKVIVENQKFKRKRAKRPVVKDQQQEQTETKQETDVQQDVKETVKE", "text": "FUNCTION: Participates in transcription termination. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NusA family."}
{"protein": "MATALPPRLQPVRGNETLREHYQYVGKLAGRLKEASEGSTLTTVLFLVICSFIVLENLMVLIAIWKNNKFHNRMYFFIGNLALCDLLAGIAYKVNILMSGKKTFSLSPTVWFLREGSMFVALGASTCSLLAIAIERHLTMIKMRPYDANKRHRVFLLIGMCWLIAFTLGALPILGWNCLHNLPDCSTILPLYSKKYIAFCISIFTAILVTIVILYARIYFLVKSSSRKVANHNNSERSMALLRTVVIVVSVFIACWSPLFILFLIDVACRVQACPILFKAQWFIVLAVLNSAMNPVIYTLASKEMRRAFFRLVCNCLVRGRGARASPIQPALDPSRSKSSSSNNSSHSPKVKEDLPHTAPSSCIMDKNAALQNGIFCN", "text": "FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSKAELAVLERRLRPIYDSLDSQQFKKALSDCDKVLKKHPNTSAAKVLKALTLIRLEKLADATEILEALDVPGAHHDELTLQAFVHCYRDSNQHMKVVTLYERIIQVDPSEHNLTQLFMAYSREKMYKEQQKIGMRLYKDFGNAPYYFWSVMSLIMQAQENPELGKKMLLPLADKMCQTQVEKSGYTEGSSAELDLQLLILEGQEKWKECAAFLDRPQASVLPMAPYNLVEKGMDFLMKDKQYKRVDQLAMEAVTKMPDNWNLWKIITESTICQIEQCLESDNKENIELAHNFVKRLGLLIEKVQKQVGYKSRAPFIATFFAYKQIGKLTKQIPDMDDMTSIFGEQVDKMLEYAKNFYKKPVCFADLQMFFCDLTSEQKSNFLKGIDLWIGEVSAKDDVEGDESKVWAIILTERCRRALGEYEKMDAAGHRSLFQQCIAQIAAPERTEHAQGVLCNLTVSHLWDAYRKENDLTKFYEMILLLEFVAASNKTDPMCKLALIRAYSALCATGRISALVKTLDIKVIQMDTLGHLTFPVYETSGRFNLAIIQNTQLSLMYEQAEKEIQDCIAQAYRNGKFSAIPRMTAASKHMKLSAQKTACDVMNRYLSSLFVLDDVDQITVTLWGDEDPIGEKRIDWKQLIDTRDFNAIPYTETEEYEALLDDMKKRTFKELIDISELRSTLCRALGAVGRVTHENMEPRLARLQLKMTVMEFKQHLEYCCREYPSFLIPSKLAQSPAPHHLSQWVHSGGLQMVLEYLEAAVKLVDILDSGEHPEKSLVGTRTEMATKLIKLIEIPPKRKEGEKLPPFWIVDPIIKSSRALQTIAAIQVVLRLIEKVVLKLVKNVPTAVPEPVGKGKGKKDKKAAEEAMTKALDECKAVVFLEHIRAMHVELRSAGNFLHTYLGQMLALEDEYIPSNIGEDLGGAKAALEGMHNPVASRLQRSFLNTCEDMHTTIKLRF", "text": "FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of proteins beginning with Met-Asp or Met-Glu (By similarity). Required for chromosome organization and arrangement; specifically for assembly of the central region components of the synaptonemal complex onto chromosomes during meiosis and for DNA double stranded break formation and repair (PubMed:18535664, PubMed:25768301). Acts downstream of xnd-1 to regulate levels of histone acetylation in germ and somatic cell nuclei by controlling acetyl-CoA production through antagonizing the acetyl- CoA hydrolase activity of acer-1 (PubMed:25768301). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome Note=Localizes to meiotic germline nuclei where it is first expressed in early prophase nuclei with expression increasing as nuclei progress into the pachytene stage. Expressed from interphase to prophase and at low levels from prometaphase to anaphase in mitotic nuclei. Highly expressed on autosomes during early to mid prophase. SIMILARITY: Belongs to the MDM20/NAA25 family."}
{"protein": "MAVSKITLHYAQTTGGSNEAAAAFPWNTPKKAVNPYLDPAEFAPESALSNLIALYAVDNEQEQLRRETLSDEVWERYFFNESRDPVQREMEQDRLISHAKTAREQQRFNPDLVIIANVGAQPAHISKPLLERIKYFHSLGRAKAYSRYLQKTIRPCLERLERVRDSQVSASFRFMASHDGLEGLLVLPEMNQDQVKRLSTLVAAHMSMCLDAACGDLFVSDDVKPEEIRQAWERVAAEAMRLEVIPPAFEQLRRKKRRRKPVPYELIPPSLARMLCADWWYRKLWQMRCEWREEQLRAVCLVNKKASPYVSYEAVIHKREQRRKSLEFFRSHELINEDGDTLDMEDVVNASNSNPAHRRNEMMACVKGLELIAEMRGDCAVFYTITCPSRFHATLNNGRPNPKWTSATVRQSSDYLVDTFAAFRKAMHKAGLRWYGVRVAEPHHDGTVHWHLLCFMRKKDRRSITALLRKFAIREDREELGANTGPRFKPELINPRKGTPTSYIAKYISKNIDGRGLAKEISKETGRSLRDSAEHVSAWASLHRVQQFRFFGIPGRQAYRELRLLAGQAARVQGERKAGAPVLDNPRLDAVLAAADAGCFATYIMKQGGVLVPRKHHLVRTAYELNDEPSAYGDHGIRIYGIWSPIAEGKICTHAVKWKKVRKAVDVQEAAADQGACAPWTRGNNCPPVENLNKSGGDLPDIKTMNEKELQDYLHNMGQKERRELTARLRLVKPKRKTVYKQNISEQQRLQLEAELTARGFEGSASEIDLLLRGGSIPSGAGLRIFYRNHRLQEDDKWRQ", "text": "FUNCTION: Possible endonuclease which induces a single-strand cut and initiates DNA replication. SIMILARITY: Belongs to the phage GPA family."}
{"protein": "MAQRRPAGKKIPFQKDSFLQQFEKLAQSRKHHVLLESARGGRYSIAGLDPIATVKGKDGITTIKHGDEMLFKEGDPLRAFHSWFKTLETETNHEFPDFQGGAIGFLSYDYARYIENFKMLSLDDLETPDIYFLVFDDIAVYDHQEESLWLITHVNGSDQETADVKLSELEQMWLTELPAVTSREMKPETAGSFAAPFTEDGFSQAVEKIKQYIASGDVFQVNLSIRQSQSLSVHPYQIYKTLREVNPSPYMAYLETPDFQIICGSPELLVSKKGKLLETRPIAGTRSRGKTNEEDEALANELIHNEKERAEHVMLVDLERNDLGRVSRYGSVRVNEFMAIEKYSHVMHIVSNVQGELQDGYDAVDIIHAVFPGGTITGAPKVRTMEIIEELEPTRRGLYTGSIGWFGYNHDLQFNIVIRTIYATGGQAFMQSGAGVVIDSVPKHEYKESFKKAFAMQRALELSEEETKIR", "text": "FUNCTION: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. SIMILARITY: Belongs to the anthranilate synthase component I family."}
{"protein": "MVRSRWKGIYVAKELQNYNTVTNPTIVTTERSSVIVPYYLTKTIYVYNGRKYVGVKITEKSLGRKLGEYVLTKKVEKYKASGKSKKK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS19 family."}
{"protein": "MARTDIARRVYNHTWKLDPIVRSLLDTDFYKLLMLQMIWGMYPKVDATFSLINRTTSVRLADEIDEGELREQLDHARTLRFSKKEMIWLGGNNFYGRKQIFEPEFLAWLEGFRLPDYELSKRDGQYELSFSGPWMYTTLWEIPALAIINELRSRAAMRAFGPFALDVLYARAKAKMWAKTERLKALPGIRISDFGTRRRHSFLWQRWCVEALKEGIGEAFTGTSNVLLAMDNDLEALGTNAHELPMVFAALANSEKELKQAPYKVLQDWQRYYGGNLLIVLPDAFGTASFLRDAPDWVADWTGFRPDSAPPIEGGEKILSWWRERGKDPKQKLLIFSDGLEVETIEETYRHFKGKVRMSFGWGTNLTNDFEGCAPTETNSLDAISLVCKVTEANGRPAVKLSDNPAKATGDEKEIERYLRIFGEKDRVEQLVKV", "text": "FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. SIMILARITY: Belongs to the NAPRTase family."}
{"protein": "MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGSVDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS", "text": "FUNCTION: (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300. FUNCTION: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:1871105, PubMed:11447121, PubMed:1986252, PubMed:7760831, PubMed:7623826, PubMed:8946918, PubMed:8940068, PubMed:9341107, PubMed:9121459, PubMed:9727490, PubMed:9499401, PubMed:9535852, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:25963659, PubMed:26754925, PubMed:18451878). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:9727490, PubMed:11583998, PubMed:16278218). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:1871105, PubMed:1986252, PubMed:8455624, PubMed:7935471, PubMed:7623826, PubMed:8940068, PubMed:9727490, PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:25963659, PubMed:26754925). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress- induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus, nucleoplasm Cytoplasm, perinuclear region Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome, centromere, kinetochore Note=The monomeric form is cytoplasmic in unstressed cells (PubMed:8455624, PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells (PubMed:10413683, PubMed:10359787). Translocates in the nucleus upon heat shock (PubMed:8455624). Nucleocytoplasmic shuttling protein (PubMed:26159920). Colocalizes with IER5 in the nucleus (PubMed:27354066). Colocalizes with BAG3 to the nucleus upon heat stress (PubMed:8455624, PubMed:26159920). Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock (PubMed:11447121, PubMed:11514557, PubMed:10359787, PubMed:25963659, PubMed:10747973, PubMed:24581496, PubMed:19229036). Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock (PubMed:11447121, PubMed:12665592, PubMed:11514557, PubMed:14707147, PubMed:10359787). Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock (PubMed:21085490). Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response (PubMed:26159920). Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner (PubMed:12917326). Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) (PubMed:26359349). Colocalizes with calcium- responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes (PubMed:18794143). Colocalizes with gamma tubulin at centrosome (PubMed:18794143). Localizes at spindle pole in metaphase (PubMed:18794143). Colocalizes with PLK1 at spindle poles during prometaphase (PubMed:18794143). SIMILARITY: Belongs to the HSF family."}
{"protein": "MGQKTALSNFLKPFNSNAGKVVPGWGTTPLMGLFMGLLFVFLLIILQIYNSTIVLDAFSVNVGG", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbH family."}
{"protein": "MSEKFSPTLRLGDLNDFIAPSQACVISLKDSKPIVKKSDRPQVVIAPKQQLEPVKISLKDCLACSGCITSAETVMLEKQSLDEFLSALSKGKDVVVSVSPQSRASLAVHYDISPLQVFKKLTTFLKSLGVKAVFDTSCSRDLVLIESCNEFVSRYKQANSDDGENSQSPLPVLSSACPGWICYAEKQLGSYVLPYVSSVKSPQQAIGAAIKHHLCQALGLRLHEVYHVTVMPCYDKKLEAARDDFVFDDGTQDNGDLKLTEVDSVLTTGEIMDLIKLKGVDFKDLEESPLDRVLTNVTEEGDLYGVAGSSGGYAETIFRHAAKALFGQTIEGPLEFKTLRNSDFREVTLQLEGKTVLKFALCYGFQNLQNIVRRVKTRKCDYQYVEIMACPAGCLNGGGQIKPKTGQSQKELIHSLEATYMNDTTLNTDPYQNPTAKRLFEEWLKEPGSNEAKKYLHTQYHPVVKSVTSQLNNW", "text": "FUNCTION: Essential component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery (PubMed:23104832). Required for the maturation of extramitochondrial Fe/S proteins (By similarity). Required for expression of the imprinted FWA gene, for seed development and is involved in the oxidative stress response in vegetative tissues (PubMed:23734982). Involved in the regulation of cell size, ploidy and cell cycle progression (PubMed:23639116). Required for growth under normoxic conditions and necessary for recovery after hypoxic treatment but its action is reactive oxygen species (ROS) independent (PubMed:23639116). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the NARF family."}
{"protein": "MSSIAQKNRNYFLYIFYGRIFNSSDKTFFIIKKQLVIAPNFFSVDQKLICSSELFCGTACSRSLVVLYENYKKIVILNSPQFFAGLDSGRENQSPDGSVQGNGLKWMLFLCQKSKRTIFSNHSNLFQCPSVAIVLVLALVILGVLAAIPLTLMLTSSAQKMSTDSTDLTDYSIRHPKFWPKTDKIHFDDLGGIPMSSMFPPNVSTCSGFGFACTGAVHMVIPSSKRCDGFKDCQDGSDEENCKECQSVFSCRSHIEEDSKKKRKTKVQPTLICLTAERLCNGVQDCLDGSDEAMCKSTCSKDQFKCNGSNACLPLSAKCDGVKDCSDGSDENNCNKCQKGAHVSLVSRNIKHLFASHVCDGVAQCADRSDEQQCDCKTCSGSDKALCDDGTCIKRSQVCDGKKDCSDGMDEENCPGTCSIEAFATKVKRVTCSDGKDYTESEACSGVEESCGGSCSKCHPKLTFTCPAAGNAQKKCIKRSKVCDGIFDCDDGADEKNCTPVKECGIDNASQFTCDRKCVDASRRCDGVWDCEDKSDEQNCSQCASGSIKCSADKKCLPAYTRCNGVAECSDGSDELKCSCEECLGAHSNTYMCSESNRCLKRDEVCSPYSMCPNATYTDKAYCAALVLKNSGRFPY", "text": "FUNCTION: Probable receptor which is required for the oocyte-to-zygote transition although its exact function is controversial (By similarity). Seems to be required for fertilization probably by promoting the interaction or fusion between sperm and oocyte (PubMed:16360684). Conversely, shown to be dispensable for fertilization but required for the formation of a continuous and cohesive eggshell chitin layer by maintaining a homogenous distribution of chitin synthase chs-1 at the unfertilized oocyte cell membrane (By similarity). Appears to recruit or maintain together to the unfertilized oocyte cortex several proteins including chs-1, kinase mbk-2 and pseudophosphatases egg-3, and possibly egg-4 and egg-5 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Note=Localizes to the cell membrane of developing oocytes. Plasma membrane localization requires extracellular matrix protein cbd-1. After fertilization, localizes to endosomes in zygotes."}
{"protein": "MISDKSPPRLSRPSYGSISSLPGPAPQPAPCRETYLSEKIPIPSADQGTFSLRKLWAFTGPGFLMSIAFLDPGNIESDLQAGAVAGFKLLWVLLWATVLGLLCQRLAARLGVVTGKDLGEVCHLYYPKVPRILLWLTIELAIVGSDMQEVIGTAISFNLLSAGRIPLWDGVLITIVDTFFFLFLDNYGLRKLEAFFGLLITIMALTFGYEYVVAHPSQGALLKGLVLPTCPGCGQPELLQAVGIVGAIIMPHNIYLHSALVKSREVDRTRRVDVREANMYFLIEATIALSVSFIINLFVMAVFGQAFYQQTNEEAFNICANSSLQNYAKIFPRDNNTVSVDIYQGGVILGCLFGPAALYIWAVGLLAAGQSSTMTGTYAGQFVMEGFLKLRWSRFARVLLTRSCAILPTVLVAVFRDLKDLSGLNDLLNVLQSLLLPFAVLPILTFTSMPAVMQEFANGRMSKAITSCIMALVCAINLYFVISYLPSLPHPAYFGLVALFAIGYLGLTAYLAWTCCIAHGATFLTHSSHKHFLYGLPNEEQGGVQGSG", "text": "FUNCTION: Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP family."}
{"protein": "MAGKRKRANAPDQTERRSSVRVQKVRQKALDEKARLVQERVKLLSDRKSEICVDDTELHEKEEENVDGSPKRRSPPKLTAMQKGKQKLSVSLNGKDVNLEPHLKVTKCLRLFNKQYLLCVQAKLSRPDLKGVTEMIKAKAILYPRKIIGDLPGIDVGHRFFSRAEMCAVGFHNHWLNGIDYMSMEYEKEYSNYKLPLAVSIVMSGQYEDDLDNADTVTYTGQGGHNLTGNKRQIKDQLLERGNLALKHCCEYNVPVRVTRGHNCKSSYTKRVYTYDGLYKVEKFWAQKGVSGFTVYKYRLKRLEGQPELTTDQVNFVAGRIPTSTSEIEGLVCEDISGGLEFKGIPATNRVDDSPVSPTSGFTYIKSLIIEPNVIIPKSSTGCNCRGSCTDSKKCACAKLNGGNFPYVDLNDGRLIESRDVVFECGPHCGCGPKCVNRTSQKRLRFNLEVFRSAKKGWAVRSWEYIPAGSPVCEYIGVVRRTADVDTISDNEYIFEIDCQQTMQGLGGRQRRLRDVAVPMNNGVSQSSEDENAPEFCIDAGSTGNFARFINHSCEPNLFVQCVLSSHQDIRLARVVLFAADNISPMQELTYDYGYALDSVHGPDGKVKQLACYCGALNCRKRLY", "text": "FUNCTION: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements. SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin and at a lower level with regions of euchromatin. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily."}
{"protein": "MPGIVELPTLEELKVEEVKVSSAVLKAAAHHYGAQCDKTNKEFMLCRWEEKDPRRCLKEGKLVNGCALNFFRQIKSHCAEPFTEYWTCLDYSNMQLFRHCRQQQAKFDQCVLDKLGWVRPDLGQLSKVTKVKTDRPLPENPYHSRARPEPNPVIEGDLKPAKHGTRFFFWTV", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein Mitochondrion intermembrane space Mitochondrion. SIMILARITY: Belongs to the complex I NDUFA8 subunit family."}
{"protein": "MVSINQNFKLPISMNSQPIQIQQQQFKQPQQQPQQKSNSCFSDQENYPANIQPSSSTSSSSSSSIHITKSMVIRPPLESNQPQPQQQQQQQQTLQQIHHQQVQLQQQQSLQMQQQQLQQQQQQQQQQQMPPPQSLPNKSNEPQEPIVVYETIRSGDSKRLKEYRQGEFLGKGGFAKCYLMTEVETNRIYAAKIIPKSTLQKTRARSKLKSEIKIHSSLSHENIVKFEHCFENEENVYILLELCNQKTVMDIHKKRKYLMEYETKYYVYQVIMAVQYLHNNNIIHRDLKLGNLFIDNMRIKLGDFGLSTKVEHGERKKTICGTPNYIAPEILDNSNGHSYEVDVWSIGIILYTLLIGKPPFETSDVKHTYQRIKQNQYSFPDEPIISHYGKSLIISILNPVPEQRPNLTQILEHDFFTYSPIPKYLPVSSLTTAPSQSTINQNMGRPLSEKTNIVNQQHLQLAGTTSPTKNNNHHYQQYQQQPQQQYNNNYQQSFSPKKQINNMNNNNNNNNNNNNNNNNNNNNNNNNLKQYNYSNNNINYNNNNNNINNQFANLSPNSQQKLSEVENDDFHYRKLRRLEKMKENDLKTQLLIKQQYTNMNENQQQQQQQQQQQQQQQQQQQRVNNNINNNGNTVTVTTGNNTVNVQIKELETKIANNHISDSPPVSSNNNYPQQIQKQQPNFNNEFYLGMPNNLVYISQYADFTNKYGLAYVLSNSYVGAYFNDSTKIVTLIESEIAYYMEHAKGTDGDGRRVLNVTQQHPHDTQKKVTLIKYFLNHFTNSDTTNLLINTGATSSSINNNNNNNVENVTNNNNNNSNNSSNINPIYVKKWIKFDNGIAFRLSDKTIQVNYLDKSRIIVSSKDMVTFVPYRGQIITGTLNYFKNGDKKISEKIKYIYGTLSNNLYSKKPESSFQQLPQQQYQQPQHYQQQTQQPQPQPQQQQLPQQLPQPQQSPAKQHQYQPNQIQYQQSIPQPQLINQ", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
{"protein": "MVDQVKVVADDQAPAEQSLRRNLTNRHIQLIAIGGAIGTGLFMGSGKTISLAGPSIIFVYMIIGFMLFFVMRAMGELLLSNLEYKSFSDFASDLLGPWAGYFTGWTYWFCWVVTGMADVVAITAYAQFWFPGLSDWVASLSVIILLLVLNLATVKMFGEMEFWFAMIKIVAIVSLIVVGLVMVAMHFQSPTGVEASFAHLWNDGGWFPKGLSGFFAGFQIAVFAFVGIELVGTTAAETKDPEKSLPRAINSIPIRIIMFYVFSLIVIMSVTPWSSVVPEKSPFVELFVLVGLPAAASVINFVVLTSAASSANSGVFSTSRMLFGLAQEGVAPKAFAKLSKRAVPAKGLTFSCICLLGGVVMLYVNPSVIGAFTMITTVSAILFMFVWTIILCSYLVYRKQRPHLHEKSIYKMPLGKLMCWVCMAFFVFVLVLLTLEDDTRQALLVTPLWFIALGLGWLFIGKKRAAELRK", "text": "FUNCTION: Permease that is involved in the transport across the cytoplasmic membrane of D-alanine, D-serine and glycine (PubMed:16952954, PubMed:23316042). Is the only transporter of D- alanine (PubMed:16952954). Transports D-serine less efficiently than DsdX (PubMed:16952954). In addition, in minimal media, transports the broad spectrum antibiotic D-cycloserine into the cell (PubMed:23316042). Transports D-cycloserine only in minimal media, and not in a complex medium, suggesting that CycA does not play a role in D-cycloserine transport when E.coli is grown in a complex or biologically relevant medium, probably due to competition from other CycA substrates present in the medium (PubMed:23316042). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family."}
{"protein": "MGAGALGVVAMVAAAVVVAMAGANSEGDALSALRRSLRDPGGVLQSWDPTLVNPCTWFHVTCDRDNRVTRLDLGNLNLSGHLVPELGKLDHLQYLELYKNNIQGTIPSELGNLKNLISLDLYKNNISGTIPPTLGKLTSLVFLRLNGNRLTGPIPRELAGISSLKVVDVSSNDLCGTIPTSGPFEHIPLSNFEKNPRLEGPELQGLAVYDTNC", "text": "FUNCTION: Involved in plant defense response. FUNCTION: Involved in plant defense response. SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein Late endosome membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein Late endosome membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein."}
{"protein": "MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLQQQQQQQQETSPRQQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSAPECHPERGCVPEPGAAVAAGKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSTDLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPVLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGAGEAGAVAPYGYTRPPQGLAGQEGDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETAQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ", "text": "FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily."}
{"protein": "MWSSWAWTWSWSGAAAVAVAAAAAWVAVYAAAARAAEALWWRPRRVERHFAAQGVRGPGYRFFVGSSIELVRLMVDAASRPMEPPTSHDILPRVLPFYHHWRKLYGPMHLIWFGRTPRLVVSEPELIREVLLTRADHFDRYEAHPMICQFEGYGLSNLHGERWARRRRVLTPAFHTENLRMIAPFVAGTVTRMLDELAERARAGGAGEAEVDVAEWFQRVPQEAITFAAFGRRNYDDGAAVFRLQDELAGYATEAHSKVYIPGYRFLPTRKNRRVWQLDREIRSHLAKFVTGLQSCSSSHGDDADDGGDGGGGMREFMSFMAPAMTAGEIIEESKNFFFAGKETLSNLLTWTTVALAMHPEWQERARREVVAVCGRGDLPTKDHLPKLKTLGMILNETLRLYPPAVAMIRTAKEDVELGGCVVPAGTEVMIPIMAVHHDAAAWGDDAAEFNPARFAADDDGGRRRHPMAFMPFGGGARVCIGQNMALMEAKVALAVVLRRFEFRLSPAYVHAPRVLMILSPQFGAPVIFRPLTSAAA", "text": "FUNCTION: Cytochrome P450 probably involved in brassinosteroids (BRs) inactivation and regulation of BRs homeostasis. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MQVSNVNDVKIYNLSCGKSLPEWLSDRKKRALQKKDVDVRRRIELIQDFEMPTVSTNIKVSRDGQYIMAAGTYKPRIRCYDTYQLSLKFERCLDSEVIKFDILSEDYSKIVFLQSDRYVELHSQHGRYYRLRIPKFGRDFAYHYPSCDLYFVGASSEVYRLNLEQGRYLNSLQTEASQINVCDINPTHHLFAAGTTEGRVECWDPRTRSRVGLLDCALSSVTADMEVEGLPSVSALKFNGPLHMAVGTSTGQVLLYDLRSNRPVIVKDHQYGLPIKSIQFHSALDLVISADSRIIKMWNKDNGKIFTSIEPEADVNDVCLYPNSGMLFTANEAPKMNVYYIPALGPAPRWCSFLDNLTEELEENPENTVYDDYKFVTRKELDELGLSHLIGSPMLRAYMHGFFMDIRLYHKVKAMVNPFAYEEYKKEKIRQKIEETRAQRVQIKKLPKVNKELALKLYEDEEEEKQLSKKKKKQKKMPNILTDDRFKVMFENPDFQVDQESEEYRLLNPLVSKISEKRKKKLKILEKLEAEGEEEEEEPEGKPSDAESSETSDDEKGWVEEVRKQRKLLRQEEKERRQERVREDQQTALKPQFYEIKAGEEFRSFQDAAKKQKLMRKTLEDRIKVEEKLGTLNVADTAVGSKQLTFTLKKSEQHRKRQEAEKQHQEERKKLRRSAGHLKSKQAKGRPFY", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the WD repeat NOL10/ENP2 family."}
{"protein": "MKFSYSFVQVVSLLLSLSPSVEGFTRSRNDACKPNHPFRPLPPSQPRTKTCHVVSNGHGKDDSKNIMQALHKCNNGGKVVFDANKVYTVGTALDMTFLKHIDLEVLGKIQFTNDTDYWQAHSFKHGFQNATTFFQLGGQDVNVYGGGTFDGNGQVWYDLYAEDALILRPILFGIIGLKGGTIGPLKLRYSPQWYQLVANSSDVIFDGIDISGYSSSKNEAKNTDGWDTYRSDNIVIQNSVINNGDDCVSFKPNSTNIIVQNLHCNGSHGISVGSLGQYKGEVDIVQNVLVYNISMYNASDGARIKVWPGVSSAMSEDLQGGGGLGSVKNITYNQMYIENVDWAIEVTQCYGQKNLTLCNEHPSNLTISDIHFKNFRGTTSGKRDPDVGTIVCSSPNVCSDIHAENINVKSPKGTDEFVCTNVDKSLLDVNCA", "text": "FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family."}
{"protein": "MINNTDNEYLEQKLSELSKKVPASIISKLRESITNSPIEITRDEIDKIIEIVMKDYLSSLVHPGEAIGVVAAQSIGEPGTQMTLRTFHFAGVRELNVTLGLPRLIEIVDARKVPSTPMMTIYLNEEYAKDRDMALEVARRIEYTRVEHVVETVNLDVGGMGIILKLDPVLLKDKGLSTEDVEKVIKKLKMGDYRVENSDEYTIAIYFENMETVTGLFKAREKILSTKIKGVKGIKRAIIRKKGDEYVIITDGSNLEGVLGVKGVDVSRIETNNLHEVESVLGVEAARELITREIKRVLEEQGLDVDIRHIELVSDIMTRTGEVRQIGRHGVTGEKTSVLARAAFEVTVKHLLDAAARGDMEEFKGVVENIIIGQPIKLGTGMVELLMRPANR", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA polymerase beta' chain family."}
{"protein": "MGFSDAGIYLSDPNNLCQTELGFFHEPSLGFSDQSDPQNEFHITPPIYQELQDQDLEPKSQETNNCSRKEGATVKKEEEEEDDYCKTPTRSDQILSAMPRICPPAPRKPKRVPSRSLKVRNSYRSKRMIILNVSREIDCLFNPTSLCNKIKKARYI", "text": "FUNCTION: Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle."}
{"protein": "MFSKFALTGSLLAGAVNAQGVGTQQTETHPQMTWQSCTSPSSCTTNQGEVVIDSNWRWVHDKDGYVNCYTGNTWNTTLCPDDKTCAANCVLDGADYSSTYGITTSGNALSLQFVTQSSGKNIGSRTYLMESSTKYHLFDLIGNEFAFDVDLSKLPCGLNGALYFVTMDADGGMAKYSTNTAGAEYGTGYCDSQCPRDLKFINGQGNVEGWTPSTNDANAGVGGLGSCCSEMDVWEANSMDMAYTPHPCETAAQHSCNADECGGTYSSSRYAGDCDPDGCDWNPFRMGNKDFYGSGDTVDTSQKFTVVTQFHGSGSSLTEISQYYIQGGTKIQQPNSTWPTLTGYNSITDDFCKAQKVEFNDTDVFSEKGGLAQMGAGMADGMVLVMSLWDDHYANMLWLDSTYPVDADASSPGKQRGTCATTSGVPADVESSDASATVIYSNIKFGPIGATY", "text": "FUNCTION: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family."}
{"protein": "MKINKLTLNERKNDILSYFSEINTPFRTSEVAEHLGVSAYQARHYLQCLEKEGKIKRSPVRRGASTLWEISAVTEPSVKTDRIAD", "text": "FUNCTION: May have a possible regulatory function on the expression of the other AFA-III genes. SIMILARITY: To E.coli PapI and DaaF."}
{"protein": "METAKDNTARTFMELMRVPVQFYRTIGEDIYAHRSTNPLKSLLFKIYLYAGFINFNLLVIGELVFFYNSIQDFETIRLAIAVAPCIGFSLVADFKQAAMIRGKKTLIMLLDDLENMHPKTLAKQMEYKLPDFEKTMKRVINIFTFLCLAYTTTFSFYPAIKASVKFNFLGYDTFDRNFGFLIWFPFDATRNNLIYWIMYWDIAHGAYLAGIAFLCADLLLVVVITQICMHFNYISMRLEDHPCNSNEDKENIEFLIGIIRYHDKCLKLCEHVNDLYSFSLLLNFLMASMQICFIAFQVTESTVEVIIIYCIFLMTSMVQVFMVCYYGDTLIAASLKVGDAAYNQKWFQCSKSYCTMLKLLIMRSQKPASIRPPTFPPISLVTYMKVISMSYQFFALLRTTYSNN", "text": "FUNCTION: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Heteromeric odorant receptor channel (TC 1.A.69) family. Or49a subfamily."}
{"protein": "MKPPSTQSSPAAVAAAAPAMDSAAAADLTDVLCEFDAVLADFASPFHERHFHYEEHLERMKRRSSASVSDSSGFSDSESADSLYRDSFTFSDEKLNSPTDSTPALLSSAVTPRKAKLGDTKELEDFIADLDRTLASM", "text": "FUNCTION: Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase (By similarity)."}
{"protein": "MGTRFLLALFLVLLVLGFEVQGAPLPQQEESAGPALLTQMRESLSGYWDSAKAAASSLYQKTYLPAVDEKLRDMYSKSTAAVSTYAGIFTDQVLSMLRGEE", "text": "FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C2 family."}
{"protein": "MNSKHSYVELKDKVIVPGWPTLMLEIDFVGGTSRNQFLNIPFLSVKEPLQLPREKKLTDYFTIDVEPAGHSLVNIYFQIDDFLLLTLNSLSVYKDPIRKYMFLRLNKEQSKHAINAAFNVFSYRLRNIGVGPLGPDIRSSGP", "text": "FUNCTION: Plays a crucial role in virion assembly and budding. SUBCELLULAR LOCATION: Virion Host cytoplasm Host cell membrane; Peripheral membrane protein Note=During viral budding, associates with the inner side of the plasma membrane of infected cells (PubMed:11711600). Found in nuclear punctate structures that have been proposed to be the sites of viral replication and transcription, also termed viral speckles of transcripts (vSPOTs) (By similarity)."}
{"protein": "MQNAESWFKKYWHLSVLVIAALISVKLRILNPWNSVFTWTVRLGGNDPWYYYRLIENTIHNFPHRIWFDPFTYYPYGSYTHFGPFLVYLGSIAGIIFSATSGESLRAVLAFIPAIGGVLAILPVYLLTREVFDKRAAVIAAFLIAIVPGQFLQRSILGFNDHHIWEAFWQVSALGTFLLAYNRWKGHDLSHNLTARQMAYPVIAGITIGLYVLSWGAGFIIAPIILAFMFFAFVLAGFVNADRKNLSLVAVVTFAVSALIYLPFAFNYPGFSTIFYSPFQLLVLLGSAVIAAAFYQIEKWNDVGFFERVGLGRKGMPLAVIVLTALIMGLFFVISPDFARNLLSVVRVVQPKGGALTIAEVYPFFFTHNGEFTLTNAVLHFGALFFFGMAGILYSAYRFLKRRSFPEMALLIWAIAMFIALWGQNRFAYYFAAVSAVYSALALSVVFDKLHLYRALENAIGARNKLSYFRVAFALLIALAAIYPTYILADAQSSYAGGPNKQWYDALTWMRENTPDGEKYDEYYLQLYPTPQSNKEPFSYPFETYGVISWWDYGHWIEAVAHRMPIANPFQAGIGNKYNNVPGASSFFTAENESYAEFVAEKLNVKYVVSDIEMETGKYYAMAVWAEGDLPLAEKYYGGYFYYSPTGTFGYANSQWDIPLNSIIIPLRIPSELYYSTMEAKLHLFDGSGLSHYRMIYESDYPAEWKSYSSQVNLNNESQVLQTALYEAVMRARYGVSPTMGTQEVLYKYAYTQLYEKKMGIPVKIAPSGYVKIFERVKGAVVTGKVSANVTEVSVNATIKTNQNRTFEYWQTVEVKNGTYTVVLPYSHNSDYPVKPITPYHIKAGNVVKEITIYESQVQNGEIIQLDL", "text": "FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a glucose-linked heptasaccharide composed of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the STT3 family."}
{"protein": "MHHRNDSQRLGKAGCPPEPSLQMANTNFLSTLSPEHCRPLAGECMNKLKCGAAEAEIMNLPERVGTFSAIPALGGISLPPGVIVMTALHSPAAASAAVTDSAFQIANLADCPQNHSSSSSSSSGGAGGANPAKKKRKRCGVCVPCKRLINCGVCSSCRNRKTGHQICKFRKCEELKKKPGTSLERTPVPSAEAFRWFF", "text": "FUNCTION: Acts as a negative regulator of the Wnt signaling pathway via its interaction with DVL1 (PubMed:11113207). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated- hydroxymethyl-CpG (By similarity). FUNCTION: Acts as a negative regulator of the Wnt signaling pathway via its interaction with DVL1 (By similarity). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl- CpG (By similarity). FUNCTION: Acts as a negative regulator of the Wnt signaling pathway via its interaction with DVL1 (By similarity). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl- CpG (PubMed:29276034). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGVKAAQTGIWASQGQSIRVVGFQAQTAHRAICLLGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDAIDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSNIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGQRDKQHFTTLIKEMRAEFIKEAQPGKKQLLLSAAVSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLEAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKERQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT", "text": "FUNCTION: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space Cytoplasm Cytoplasm, perinuclear region Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyl hydrolase 18 family."}
{"protein": "MEFKLEAHRIVSISLGKIYNSRVQRGGIKLHKNLLVSLVLRSARQVYLSDPCPGLYLAGPAGTPAVPPPQQPGEPVAGPPSGWGEPPPPVARAAWPEPEPQPQPQPQRPSVCHTPGAGSSEPVAAVAGSGEALRGGEEDSAAAAWGRVERPRAASSGGGSDACPEGPRAVRRPCGCPPAVEERSSEDGSPAPPAPCPRKRGAAGVGGGRASCSAPGSTPLKKPRRNSEEQPVTGEDDTDEEMETGNVANLISIFGSSFSGLLRKSPAGGREEEEAEEGGPEAAEPGQICCDKPVLRDMSPWSTAIVAF", "text": "FUNCTION: Plays a role as a transcription factor. Mediates positive transcriptional regulation of several chaperone gene during the heat shock response in a HSF1-dependent manner. Mediates negative transcriptional regulation of CDC25B expression. Plays a role in the dephosphorylation of the heat shock factor HSF1 and ribosomal protein S6 kinase (S6K) by the protein phosphatase PP2A. Involved in the regulation of cell proliferation and resistance to thermal stress. Involved in the cell cycle checkpoint and survival in response to ionizing radiation. Associates with chromatin to the CDC25B promoter. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Predominantly cytoplasmic. Translocated in the nucleus during heat shock. SIMILARITY: Belongs to the IER family."}
{"protein": "MPQCPTLESQEGENSEEKGDSSKEDPKETVALAFVRENPGAQNGLQNAQQQGKKKRKKKRLVINLSSCRYESVRRAAQQYGFREGGEDDDWTLYWTDYSVSLERVMEMKSYQKINHFPGMSEICRKDLLARNMSRMLKMFPKDFRFFPRTWCLPADWGDLQTYSRSRKNKTYICKPDSGCQGKGIFITRTVKEIKPGEDMICQLYISKPFIIDGFKFDLRIYVLVTSCDPLRIFVYNEGLARFATTSYSRPCTDNLDDICMHLTNYSINKHSSNFSRDAHSGSKRKLSTFSAYLEDHSYNVEQIWRDIEDVIIKTLISAHPIIRHNYHTCFPNHTLNSACFEILGFDILLDHKLKPWLLEVNHSPSFSTDSRLDKEVKDGLLYDTLVLINLESCDKKKVLEEERQRGQFLQQCCSREMRIEEAKGFRAVQLKKTETYEKENCGGFRLIYPSLNSEKYEKFFQDNNSLFQNTVASRAREEYARQLIQELRLKREKKPFQMKKKVEMQGESAGEQVRKKGMRGWQQKQQQKDKAATQASKQYIQPLTLVSYTPDLLLSVRGERKNETDSSLNQEAPTEEASSVFPKLTSAKPFSSLPDLRNINLSSSKLEPSKPNFSIKEAKSASAVNVFTGTVHLTSVETTPESTTQLSISPKSPPTLAVTASSEYSGPETDRVVSFKCKKQQTPPHLTQKKMLKSFLPTKSKSFWESPNTNWTLLKSDMNKPHLISELLTKLQLSGKLSFFPAHYNPKLGMNNLSQNPSLPGECHSRSDSSGEKRQLDVSSLLLQSPQSYNVTLRDLLVIATPAQLDPRPCRSHASAMRDPCMQDQEAYSHCLISGQKGCERS", "text": "FUNCTION: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins. Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction. Preferentially modifies the alpha-tubulin tail over a beta-tail. Promotes tubulin polyglutamylation which stimulates spastin/SPAST- mediated microtubule severing, thereby regulating microtubule functions. Mediates microtubule polyglutamylation in primary cilia axoneme, which is important for ciliary structural formation and motility. Mediates microtubule polyglutamylation in motile cilia, necessary for the regulation of ciliary coordinated beating. Polyglutamylates non-tubulin protein nucleotidyltransferase CGAS, leading to CGAS DNA-binding inhibition, thereby preventing antiviral defense response. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body Note=CEP41 is required for its transport between the basal body and the cilium axoneme. SIMILARITY: Belongs to the tubulin--tyrosine ligase family."}
{"protein": "MGKPRGLRTARKLKNHRREQRWHDKDYKKSHLGTRWKSNPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPRDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVASVSLLALYKQKKERPRS", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Rough endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
{"protein": "MNVTSNATAAGSFPLAFGLKTSFGFMHYAKAPAINLRPKESLLPEMSDGVLALVAPVVAYWALSGIFHVIDTFHLAEKYRIHPSEEVAKRNKASRMHVFLEVILQHIIQTIVGLIFMHFEPIYMTGFEENAMWKLRADLPRIIPDAAIYYGYMYGMSALKIFAGFLFVDTWQYFLHRLMHMNKTLYKWFHSVHHELYVPYAYGALFNNPVEGFLLDTLGTGIAMTLTHLTHREQIILFTFATMKTVDDHCGYALPLDPFQWLFPNNAVYHDIHHQQFGIKTNFAQPFFTFWDNLFQTNFKGFEEYQKKQRRVTIDKYKEFLQERELEKKEKLKNFKAMNAAENEVKKEK", "text": "FUNCTION: Required for hydroxylation of C-4 in the sphingoid moiety of ceramide. Catalyzes the conversion of sphinganine to phytosphingosine in sphingolipid biosynthesis. Involved in the response to syringomycin. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MSGFLEELLGEKLVTGGGEEVDVHSLGARGISLLGLYFGCSLSAPCAQLSASLAAFYGRLRGDAAAGPGPGAGAGAAAEPEPRRRLEIVFVSSDQDQRQWQDFVRDMPWLALPYKEKHRKLKLWNKYRISNIPSLIFLDATTGKVVCRNGLLVIRDDPEGLEFPWGPKPFREVIAGPLLRNNGQSLESSSLEGSHVGVYFSAHWCPPCRSLTRVLVESYRKIKEAGQNFEIIFVSADRSEESFKQYFSEMPWLAVPYTDEARRSRLNRLYGIQGIPTLIMLDPQGEVITRQGRVEVLNDEDCREFPWHPKPVLELSDSNAAQLNEGPCLVLFVDSEDDGESEAAKQLIQPIAEKIIAKYKAKEEEAPLLFFVAGEDDMTDSLRDYTNLPEAAPLLTILDMSARAKYVMDVEEITPAIVEAFVNDFLAEKLKPEPI", "text": "FUNCTION: Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A) (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the nucleoredoxin family."}
{"protein": "MAALSGGGGSSSGGGGGGGGGGGGGDGGGGAEQGQALFNGDMEPEAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLVFQTPTDASRNNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPVPQEEASFPETALPSGSSSAPPSDSTGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSSSEDRSRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGGFPVH", "text": "FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway. Phosphorylates PFKFB2 (By similarity). May play a role in the postsynaptic responses of hippocampal neurons. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane Note=Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily."}
{"protein": "MTKVLLSHPPRPASHNSSRAMVWVRKNLFSSWSNSLLTIGCIWLMWELIPPLLNWAFLQANWVGSTRADCTKAGACWVFIHERFGQFMYGLYPHDQRWRINLALLIGLVSIAPMFWKILPHRGRYIAAWAVIYPLIVWWLMYGGFFALERVETRQWGGLTLTLIIASVGIAGALPWGILLALGRRSHMPIVRILSVIFIEFWRGVPLITVLFMSSVMLPLFMAEGTSIDKLIRALVGVILFQSAYVAEVVRGGLQALPKGQYEAAESLALGYWKTQGLVILPQALKLVIPGLVNTIIALFKDTSLVIIIGLFDLFSSVQQATVDPAWLGMSTEGYVFAALIYWIFCFSMSRYSQYLEKRFNTGRTPH", "text": "FUNCTION: Probably part of the binding-protein-dependent transport system YdhWXYZ for an amino acid; probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily."}
{"protein": "MLDKSRLRIAMQKSGRLSKESQQLLEQCGIKINLQQQRLLAFAENMPIDIMRVRDDDIPGLVMDDVVDLGIIGENVLEEELLTRRAQGEDPRYFTLRQLDFGGCRLSIALLLDTPWTGPECLRGKRIATSYPHLLKQYLDKLDITFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREAEVIYRSKACLIQRDGELSVAKQSLVDKLLIRIQGVIQARESKYIMMHAPTERLDDIISLLTGAEQPTILPLAGDQHRVAMHMVSSETLFWETMENLKALGASSILVLPIEKMME", "text": "FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily."}
{"protein": "MKRQKRDQTERAFVKGYQAGIEGRSKSLCPHESGLARQQWLNGWRESRMDQWDGYSRLAQVQKITNLHPMSMSG", "text": "FUNCTION: During stationary phase, converts 70S ribosomes to an inactive dimeric form (100S ribosomes). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribosome modulation factor family."}
{"protein": "MIKLGIVMDPIAHINIKKDTSFAMLLEAQRRGYELHYMEMADLYLINGEARARTRTLSVEQNYDKWYEFGSEQEIKLADLDVILMRKDPPFDTEFIYATYILERAEEEGTLIVNKPQSLRDCNEKLYTAWFADLTPETLVTRNKAQLKAFWEKHGDIIMKPLDGMGGASIFRVKEGDPNIGVIAETLTELGNRYCMAQNYLPAIKDGDKRVLVVDGEPVPYCLARIPQGGETRGNLAAGGRGEPRPLSESDWEIARRVGPTLKAKGLIFVGLDIIGDRLTEINVTSPTCVREIEAEYPISITGMLMDAIEARLAK", "text": "SIMILARITY: Belongs to the prokaryotic GSH synthase family."}
{"protein": "MFERFTDRARRVVVLAQEEARMLNHNYIGTEHILLGLIHEGEGVAAKSLESLGISLEGVRSQVEEIIGQGQQAPSGHIPFTPRAKKVLELSLREALQLGHNYIGTEHILLGLIREGEGVAAQVLVKLGAELTRVRQQVIQLLSGYQGKEAAEAGTGGRGGESGNPSTSLVLDQFGRNLTAAAMEGKLDPVIGREKEIERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGEVPETLKDKQLYTLDLGSLVAGSRYRGDFEERLKKVLKEINTRGDIILFIDELHTLVGAGAAEGAIDAASILKPKLARGELQTIGATTLDEYRKYIEKDAALERRFQPVQVGEPTVEHTIEILKGLRDRYEAHHRVSITDSAMVAAATLADRYINDRFLPDKAIDLIDEAGARMRIRRMTAPPDLREFDEKIADARREKESAIDAQDFEKAAALRDKEKQLVAQRAEREKQWRSGDLDVVAEVDDEQIAEVLGNWTGIPVFKLTEEETTRLLRMEEELHKRIIGQEDAVKAVSKAIRRTRAGLKDPKRPSGSFIFAGPSGVGKTELSKALANFLFGDDDALIQIDMGEFHDRFTASRLFGAPPGYVGYEEGGQLTEKVRRKPFSVVLFDEIEKAHQEIYNSLLQVLEDGRLTDGQGRTVDFKNTVLIFTSNLGTSDISKAVGLGFSQGGSENNYERMKQKVHDELKKHFRPEFLNRIDDIIVFHQLTQDEIIQMVDLMIGRVSNQLKTKDMALELSDKAKALLAKRGFDPVLGARPLRRTIQREIEDQLSEKILFEEIGPGQLVTVDVEGWDGEGQGEDAKFTFSGGPKRAETAEPDLAGAGAAGAPTAGTE", "text": "FUNCTION: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2 (Probable). SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily."}
{"protein": "MKYELNGQVVLISGGSQGLGRAFAQKYIEESDSTVVIVSRSEEKLTRAGEAICGGARRLGAGGAGRLLYYACNLGDAAAVGGLFATLADAGLQVTQVLFCAGGAVPGLFAELSSAQLAAGVEMNYGTALHLAHGAVRHGARHLVFFSSAAAVYPFIGYSQYAPLKAALRALVAVLRQECDGVRVSCVYPGNFASEGYAEENRTKPAITAAIEGSSEAISCAACCDKIVRGLRSGYDDVTTDFVGWLLLACNMGFNYHSTTYFLWPLGWLLGALVNLLVVPIYMLLCRWDIHKWRTQREETHLAAKTD", "text": "FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MTPRRVAKLVQFSGSYLNTEWARKFILGSLLQRYNPQSLTTVGSSAAGNSGEDASLDKELLHLQRSLSEVWSLPAQPLDAVSEGRILRLLARYATGEGVMSIEALNELSHVLSCIRGSPQRVEGPIDMEELLLAIGYAKPGDNLRRVAFAGELQYPPSALAHMRAHLRDDMERDGSDPFDILRVVTHNPAYAIDSASTSEVDDAIGVHKDPVTGEECFVVYVSDATVYCPFDSPLEQLTARLLTTTTYLPEGVFFMLPKPIVDAATLREDRPCRTFDIRFQIDEVTGELKNYSVGVGWLHKLRRITYDEVQALYDEEAQVGNQHHHTERESTQASPAKREEGKKGMVASGGTSSCRPSWMTVEDESILRRIYRAAQKRYETRQLRAGDRFIHADLPEPLIKVGAGAQVLSVEDQIIGTRDARLAVAEMMIAANEVCSRVAQENHLSIPFRGTRELSLDHVAAKSYREPHGVVSVQSLDPQYVFFAEAMQRSIRQLSGVTRAVYFHTPIYHAGLDTHNYTHSTSPLRRYADMLVHHQLKVWLWRTSHCSSGGGVLHSAQKSSPVLIEQPIAEHTMATLCSMISSKQEQSSILQESSQRYWLLKHIKQNILTKSPHHRFICLVGDTRSVKCAPEYARFVVECSHDSPSQPDGGVHRTVPWAGRWKQRHHEYLYVSDIYITELQFAHVVLHSLPDVVVGAVVECEVREVHPTQGYLSLAIVKVWSGGDERRFEPLWKKCLLPSLDS", "text": "FUNCTION: 3'-5'exoribonuclease which is involved in the post- transcriptional processing, editing and degradation of mitochondrial RNAs, including mRNAs, rRNAs and guided RNAs (gRNA) (PubMed:15470249, PubMed:26833087). As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors by catalyzing the processive 3'-5' degradation of uridylated gRNA precursors (PubMed:26833087). Plays a role in the degradation of 12S rRNA processing intermediates and maturation by-products (PubMed:18032430). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RNR ribonuclease family."}
{"protein": "METFDPTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYIRYQSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVFDIDMTDYDDVRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHRLWVYSGRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKGGQDVKKKVHLSEKIHPFIRKSINIIKKYFEEYALVNQDILENKESWDKILALVPETIHDELQQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIMLQYCFPRLDINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICRELDAISTNEEEKEENEAESDVKHRTRDYKKTSLAPYVKVFEHFLENLDKSRKGELLKKSDLQKDF", "text": "FUNCTION: Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis (PubMed:9268648, PubMed:9705292, PubMed:17893144, PubMed:24043831, PubMed:26975377, PubMed:25550159, PubMed:31479243, PubMed:33060134). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (PubMed:17893144). These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity). In the primase complex, both subunits are necessary for the initial di-nucleotide formation, but the extension of the primer depends only on the catalytic subunit (PubMed:17893144). Synthesizes 9-mer RNA primers (also known as the 'unit length' RNA primers). Incorporates only ribonucleotides in the presence of ribo- and deoxy-nucleotide triphosphates (rNTPs, dNTPs) (PubMed:26975377). Requires template thymine or cytidine to start the RNA primer synthesis, with an adenine or guanine at its 5'-end (PubMed:25550159, PubMed:26975377). Binds single stranded DNA (By similarity). SIMILARITY: Belongs to the eukaryotic-type primase small subunit family."}
{"protein": "MDPTSRPAIVIDNGTGYTKMGFAGNVEPCFILPTVVAVNESFLNQSKSSSKATWQTQHNAGVAADLDFYIGDEALAKSRSSSTHNLHYPIEHGQVEDWDAMERYWQQCIFNYLRCDPEDHYFLLTESPLTPPESREYTGEILFETFNVPGLYIAVNSVLALAAGYTTSKCEMTGVVVDVGDGATHVVPVAEGYVIGSCIKSIPIAGKDVTLFIQQLMRERGENIPPEDSFDVARKVKEMYCYTCSDIVKEFNKHDKEPAKYIKQWKGVKPKTGAPYTCDVGYERFLGPEVFFNPEIYSNDFTTTLPAVIDKCIQSAPIDTRRALYKNIVLSGGSTMFKDFGRRLQRDLKKIVDARVLANNARTGGEITSQPVEVNVVSHPVQRFAVWFGGSVLSSTPEFFASCRTKEEYEEYGASICRTNPVFKGMY", "text": "FUNCTION: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity). Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development. Involved in the control of cell morphogenesis in leaf epidermal pavement cells, root hairs, hypocotyls epidermal cells and trichomes, especially during rapid cell expansion. Regulates the directionality of cell expansion by regulating the actin organization, and thus the microtubules distribution and the fusion of small vacuoles. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family. ARP3 subfamily."}
{"protein": "MDTLWDISPPLSPATPVWPGDTPLSVERVWRMEAGSPVNVARLTLSPHTGAHCDAPLHYDADGAPIGAVPLDAYLGPCRVIHCVGAAPRVQPADVEAALDRVPPRVLLRTCAHASVERWDSDFCAVAPETIDLLAARGVKLIGIDTPSLDPQESKTMDAHHRVRAHRMAILEGIVLDDVPAGDYELIALPLKFTTLDASPVRAVLRALPGHSS", "text": "FUNCTION: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family."}
{"protein": "MSIENSKEAALTAELSLAGAFFYTPECPDIEHLRSLSVANRWLDTDLPISDDLKDVAKLTPAEREFYRFLFAFLSAADDLVNLNLGDLSALFTQKDILHYYIEQESIEVTHSRVYSAIQLMLFGNDAAARARYVASIIGDAAIGRKVAWLQAKVRECGSVAEKYILMILIEGLFFASSFASIAYLRTHNLFVVTCQSNDLISRDEAIHTRASCCIYNNYLGGFEKPEPKRIYELFSEAVNIECEFLLSHAPQYSHLLDIGAIISYVRYSADRLLGEIGLSPLFNAPKPSPSFPLAFMTVEKHTNFFERRSTAYSGTLINDL", "text": "FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small chain family."}
{"protein": "MAIAIGLDFGSDSVRALAVDCASGEEIATSVEWYPRWQKGQFCDAPNNQFRHHPRDYIESMEAALKTVLAELSVEQRAAVVGIGVDTTGSTPAPIDANGNVLALRPEFAENPNAMFVLWKDHTAVEEAEEITRLCHAPGNVDYSRYIGGIYSSEWFWAKILHVTRQDSAVAQSAASWIELCDWVPALLSGTTRPQDIRRGRCSAGHKSLWHESWGGLPPASFFDELDPILNRHLPSPLFTDTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNALVKVIGTSTCDILIADKQSVGERAVKGICGQVDGSVVPGFIGLEAGQSAFGDIYAWFGRVLGWPLEQLAAQHPELKAQINASQKQLLPALTEAWAKNPSLDHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVEKTLQPRSEQAQRFEQLYRRYQQWAMSAEQHYLPTSAPAQAAQAVATL", "text": "SIMILARITY: Belongs to the ribulokinase family."}
{"protein": "MSHFAAIAPPFYSHVRALQNLAQELVARGHRVTFIQQYDIKHLIDSETIGFHSVGTDSHPPGALTRVLHLAAHPLGPSMLKLINEMARTTDMLCRELPQAFNDLAVDGVIVDQMEPAGALVAEALGLPFISVACALPLNREPDMPLAVMPFEYGTSDAARERYAASEKIYDWLMRRHDRVIAEHSHRMGLAPRQKLHQCFSPLAQISQLVPELDFPRKALPACFHAVGPLRETHAPSTSSSRYFTSSEKPRIFASLGTLQGHRYGLFKTIVKACEEIDGQLLLAHCGRLTDSQCEELARSRHTQVVDFADQSAALSQAQLAITHGGMNTVLDAINYRTPLLALPLAFDQPGVASRIVYHGIGKRASRFTTSHALARQMRSLLTNVDFQQRMAKIQTALRLAGGTMAAADIIEQVMCTGQPVLSGSGYATAL", "text": "FUNCTION: Catalyzes the glycosylation reaction which converts zeaxanthin to zeaxanthin bis(beta-D-glucoside). The reaction proceeds in two steps with the monoglucoside as an intermediate. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MQIIRNNSQDPISISNWRWACFLDETIKAFSTFQTRPYQIDNDFLFRESFFGSSSNPKKVILETWGLKMEKIRQARCACLQAGEITSVMNLVISPLNNYDLPFFGADFVTLPNGHLIALDLQPALKDDINHTQHVWNKLKPIHAHWQSKIPSGGDIPSDARQYFSPAFLWSRIPLGEEGDNLITQTIKPAFDEYLNCFFDLLRDAKITSKERSFQLLNGQKKYMRYRAEKDPARGMLRSFFGEVWTESYINNILFDLK", "text": "FUNCTION: Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin. SIMILARITY: Belongs to the HY2 family."}
{"protein": "MSLIGKLFGTGGKGAKGPSPQEAIQKLRDTEEMLTKKQEFLEKKIEQELVTAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGFAAKAMKAAHDNMDIEKVDELMQDIADQQELAQEISDAISKPVGFGEDFDEDELMAELEELEQEELDKNLLEVQGPETVPLPNVPAAVLPAKPVKKKQEEDDDDMRELENWATA", "text": "FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Late endosome membrane; Peripheral membrane protein Midbody. SIMILARITY: Belongs to the SNF7 family."}
{"protein": "MQNFKELGISDKTVQTLEAMGFKEPTPIQKDSIPYALEGDDILGQAQTGTGKTGAFGIPLIEKVVGQQGVQSLILAPTRELAMQVAEQLREFSKGQKVQVVTVFGGMPIERQIKVLKRGPQIVVGTPGRVIDHLNRRTLKTQGIHTLILDEADEMMNMGFIDDMRFIMDKIPAEQRQTMLFSATMPKAIQELVQQFMKAPKIIKTMNNEMSDPQIDEYYTIVKELEKFDTFTNFLDVHQPELAIVFGRTKRRVDELTSALLSKGYKAEGLHGDITQAKRLEVLKKFKNDQIDILVATDVAARGLDISGVSHVYNFDIPQDTESYTHRIGRTGRAGKEGIAVTFVNPIEMDYIRQIEDVNNRRMKALRPPHRKEVLKAREDDIKDRVQNWMSRENEPRLQRISSELLKEYDSTELVASLLQELVEANDEVEVQLTFEKPLARKNRSSKGGSRRSNHKRGNGKFDNKNRRSKGSKGQSSKKKNQKKFDRRDKQQKSGNQSLKGRTFADHQK", "text": "FUNCTION: DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily."}
{"protein": "MERTIGIDAGGTLTKIAYFNEKRLLTFEKFYSHEQHKIIDWIKNNNGIKQICITGGKSKLLQQLLTGSYKIIELNEFEATLAGVQYILKEEKHAIRNFILTNIGTGTSIHYVYNEQYIRAGGTGVGGGTIMGLSKLLTNIDHFEDVIPLTKVGSRKELDITVGDIYGGILSPIDNNLTASNFGKAAITESNNSSSDILATVQGLVGEVVTALSLQFAETKNIEHIIYIGSTLCNNVQLQHIISSYTEYQNKTPIFLQDGGNSGAIGALLHATK", "text": "FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II pantothenate kinase family."}
{"protein": "MGSPRSALSCLLLHLLVLCLQAQVRSAAQKRGPGAGNPADTLGQGHEDRPFGQRSRAGKNFTNPAPNYPEEGSKEQRDSVLPKVTQRHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR", "text": "FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. Required for normal brain, eye, ear and limb development during embryogenesis. Required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Plays a role in neurite outgrowth in hippocampal cells (By similarity). Cooperates with Wnt-1 in mouse mammary tumor virus-induced murine mammary tumorigenesis (PubMed:7884899). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the heparin-binding growth factors family."}
{"protein": "MGLTEQKQKHMEQLSDKNGIISALAFDQRGALKRLMAKYQSEEPTVSQIEALKVLVAEELTPYASSMLLDPEYGLPATKVLDDNAGLLLAYEKTGYDTSSTKRLPDCLDIWSAKRIKEEGADAVKFLLYYDVDSSDEVNEEKEAYIERIGSECVAEDIPFFLEILSYDEKITDSSGIEYAKIKPRKVIEAMKVFSNPRFNIDVLKVEVPVNMDYVEGFAQGETAYNKATAAAYFREQDQATLLPYIFLSAGVPAQLFQETLVFAKEAGAKFNGVLCGRATWAGSVKEYVEKGEAGARQWLRTIGFQNIDELNKILQKTATSWKER", "text": "SIMILARITY: Belongs to the aldolase LacD family."}
{"protein": "MGKQNSKLRPEVMQDLLESTDFTEHEIQEWYKGFLRDCPSGNLTMEEFKKIYGNFFPYGDASKFAEHVFRTFDANGDGTIDFREFIIALSVTSRGKLEQKLKWAFSMYDLDGNGYISKAEMLEIVQAIYKMVSSVMKMPEDESTPEKRTEKIFRQMDTNRDGKLSLEEFIRGAKSDPSIVRLLQCDPSSAGRF", "text": "FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds three calcium ions (By similarity). SIMILARITY: Belongs to the recoverin family."}
{"protein": "MVDGTLLLLLSEALALTQTWAGSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCDLGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISERKSNDACEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVDTRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWKPASQPTIPIVGIIAGLVLLGSVVSGAVVAAVMWRKKSSGGKGRSYSKAEWSDSA", "text": "FUNCTION: Preferably binds to a peptide derived from the signal sequence of most HLA-A, -B, -C and -G molecules. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class I family."}
{"protein": "VVGGDCIPQVPFLAFLYSEYFC", "text": "FUNCTION: Thrombin-like serine protease which cleaves specifically the Aalpha chain of human fibrinogen (FGA) to release fibrinopeptide A. Also cleaves rapidly the Bbeta chain of human fibrinogen (FGB). Is selective for Arg over Lys at position 1 of the tripeptide substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MQNNNDILKAQSPAALAEEYIVKSIWQDVFPSGSNLPSERDLADKIGVTRTTLREVLQRLARDGWLTIQHGKPTKVNNIWDAAGPNIIETLIALDMQSAPLIIDNMLSLRSKMSESYIYEAVKNSPQKSTALFAELEQLQNTAQDYTEFDYQLFRQFTVVANKPFYRLIFNSLKGVYQRIGLLFFKEKKHRELTKQFYLEMQQICLEGNADAVVDCIRKHNLRSSTYWKAILERLPQNLSD", "text": "FUNCTION: Multifunctional regulator of fatty acid metabolism. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW", "text": "FUNCTION: Antioxidant peptide has 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity. FUNCTION: Important role in the capacity of milk to transport calcium phosphate. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-casein family."}
{"protein": "MENATHPVPLIELRDIRKRYGGNGTPEVEVLKGVSLSIHAGEFVAIVGASGSGKSTLMNILGCLDRPSSGSYHFAGHDVAELDSDEQAWLRREAFGFVFQGYHLIPSASAQENVEMPAIYAGIPASERHTRARALLERLGLAERTANRPHQLSGGQQQRVSIARALMNGGHIILADEPTGALDSHSGAEVMALLDELASQGHVVILITHDRDVAARAKRIIEVRDGEIVSDSANDERPAQPSAGVERHLQADDLSQRLAEGSSEPSGAWRAELLEAVRAAWRVMWINRFRTALTLLGIIIGVASVVVMLAVGEGSKRQVMAQMGAFGSNIIYLSGYSPNPRAPMGIVSSDDVAAIATLPQVKKVMPVNGGELVVRYGNIDYHAYVGGNNTDFPEILNWPVAEGSYFTERDEDAATTVAVIGYKVRKKLFGSANPIGRYILIENVPFQVIGVLAEKGSSSGDKDADNRIAIPYSAASIRLFGTRNPEYVIIAAADAQRVHQAERAIDQLMLRLHRGQRDYELTNNAAMIQAEAKTQNTLSLMLGSIAAISLLVGGIGVMNIMLMTVRERTREIGIRMATGARQGDILRQFLTEAAMLSVVGGLAGIALALCIGGVLLLGQVAVAFSLSAIVGAFSCALVTGLVFGFMPARKAAQLDPVAALASQ", "text": "FUNCTION: Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide exporter (TC 3.A.1.122) family."}
{"protein": "MHQDTVRGKAFAMPLISPAYPAGPYRFRNREYLIITYRTDPQKLRDLVPEPLQVCEPMVKFEFIRMPDSTGFGDYTEGGQVIPVSFYGRRGSYTHCMFLDDHPPIAGGRELWGFPKKLASPTLRTETDTLVGTLDYGPVRVATGTMGYKHRAADLASVRASLAEPNFLLKIIPHVDGTPRICELVEYHLEDVHLRGAWTGPAALNLWSHALAPVAELPVLEVVSAVHLVADLTLALGKVVHDYLAKA", "text": "FUNCTION: Catalyzes the conversion of acetoacetate to acetone and carbon dioxide. SIMILARITY: Belongs to the ADC family."}
{"protein": "MVPLKISTLESQLQPLVKLVATETPGALVAYARGLSSADRSRLYRLLRSLEQAIPKLSSAVVSATTLAARGL", "text": "SUBCELLULAR LOCATION: Virion membrane."}
{"protein": "MIFVQQFEEVRSILEKAKKITVLTGAGASTESGIPDFRSANGLYADANVEMYLSRGYYNRSPKEFWKHYKEIFQINTFHQYKPNRGHRFLAELEEQGKDITILTQNIDGLHQLGGSKHVIDLHGTLQTAHCPKCKSGYDLQYMIDHEVPRCEKCNFILNPDVVLYGDTLPQYQNAIKRLYETDVLIVMGTSLKVQPVASFPQIAKREVGATTILVNEELTGQEYNFDFVFQNKIGEFVEGLSSMK", "text": "FUNCTION: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sirtuin family. Class U subfamily."}
{"protein": "MALKSTNGTHAGPTASAASLASLAANISEKAASLSTYLESQGHAQPSFLPGCADPPETEEYLALHTSLTSSLEDLQRLVDGPRRSLRPFIMIGNDLAALQVAFDFGFFQLIPPEGSMDVETLAHKVGIDADRTARVLRMLATHRIFVEPKPGFFAHTAASAVFHDDEELRCAGHYMLDECFKAATACSDCIKASPNDSDSTHSPFNTYFGVPMFSYYEQNPQFAARFAKAMAVDRQIAELRDCFPWGDIKGTVVDVGGGSGHISMALARNFPKLDFIVQDDSEKMLAQGRARNLSDIEGRISFMKHSFFHPQPIGGAGAFFIRQCTHNWCDRDVVKILKSFVPGLENSAPGTPLLINDTVLPVPGSKPLHEERALRQMDMLMFVVLGAKQRTAKEFEALLKEADARYEIRRVHADGSMGLVEVHLNI", "text": "FUNCTION: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phytotoxin solanapyrone, a causal agent of early blight disease of potato and tomato (PubMed:20486243). The prosolanapyrone synthase sol1 is a polyketide synthase that produces the octaketide desmethylprosolanapyrone I via sequential condensations of 7 malonyl-CoA units with one acetyl-CoA unit, and one methylation step (PubMed:20486243). The octaketide backbone is further methylated by the sol2 O-methyltransferase to yield prosolanapyrone I (PubMed:20486243). Prosolanapyrone I is hydroxylated to prosolanapyrone II by the cytochrome P450 monooxygenase sol6 (PubMed:20486243). The solanapyrone synthase sol5 then catalyzes the oxidation of prosolanapyrone II and the subsequent Diels Alder cycloisomerization of the product prosolanapyrone III to solanapyrones A and D (PubMed:9659400, PubMed:18256508). Solanapyrones A and D are then converted into solanapyrones B and E, respectively, by the sol3 dehydrogenase (PubMed:20486243). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
{"protein": "MGERARSPDIEQGKKGGKHPYSHYSSDLGSSPQSSGPSSPVNTTPCASTREKNPKRHLSDNQVHHPTVRKVSPKAVPSKKGIRVGFRSQSLNREPLRKDPDIVTKRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERKHVSCQSDFTDQCTKGVQTAEDFELEDFPFTAQTVLCYENRWDEPEYLSSYLEYQDLNKHGSEMLSSVLGQEGKYDEDEDPCSAKQEARKPESEWAREELDKVKGKSALLGRAEKLALEAGRFPTENYQAQSVDKFEDEAERLKTEMLLAKLNEINKELQDPQNLGRAPLPLLPNFESKLHSPDRSTRPYSFPESLDRSFNGQHLQDLSFLTPRGEGGSPGPIRSPGQIRSPAPLDEFSFGSYVPSFGKTLGKSNPPSQKSSLLDFQSNSSESPSKDSLDLMSRKEKKATLMEQLFGPSASNTSVSSKSTDPHFPAASRGDMDPLHFLSGDRNSRVREPGDEEEDLFLREGRSFNPNRHRLKHASNKPTVTAVDSVDEDIEEVTLR", "text": "FUNCTION: Involved in intraflagellar protein (IFT) transport in photoreceptor cilia. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body Cell projection, cilium Note=Localized to the region between the outer and inner photoreceptor segments, corresponding to the photoreceptor connecting cilium (PubMed:21606596, PubMed:17546029). Colocalizes with IFT complex A and B proteins in the connecting cilium of photoreceptors (PubMed:21606596). SIMILARITY: Belongs to the LCA5 family."}
{"protein": "MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMDHMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE", "text": "FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway. FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the p23/wos2 family. SIMILARITY: Belongs to the p23/wos2 family."}
{"protein": "MNGLISQACGSHRPRRPSSLGAVAILIAATLFATVVAGCGKKPTTASSPSPGSPSPEAQQILQDSSKATKGLHSVHVVVTVNNLSTLPFESVDADVTNQPQGNGQAVGNAKVRMKPNTPVVATEFLVTNKTMYTKRGGDYVSVGPAEKIYDPGIILDKDRGLGAVVGQVQNPTIQGRDAIDGLATVKVSGTIDAAVIDPIVPQLGKGGGRLPITLWIVDTNASTPAPAANLVRMVIDKDQGNVDITLSNWGAPVTIPNPAG", "text": "FUNCTION: Might be involved in transporting short diacylated glycolipids to the cell outer membrane (By similarity). FUNCTION: Might be involved in transporting short diacylated glycolipids to the cell outer membrane (By similarity). Overexpression induces expression of sensor protein kdpD gene at low K(+) concentrations (0 and 250 uM, tested in M.smegatis). FUNCTION: Might be involved in transporting short diacylated glycolipids to the cell outer membrane. Binds glycolipids that contain a diacylated glycerophosphate or a diacylated phosphatidylinositol moiety with C14 and C16 chains (upon overexpression in M.smegmatis; M.smegmatis does not encode this gene). Overexpression in M.smegmatis increases the cell wall glycolipid LAM/LM ratio (lipoarabinomannan/lipomannan), suggesting perhaps this protein is involved in the preferential translocation of diacylated LAM to the outer cell membrane. Overexpressing M.smegmatis cells adhere less well to hexadecane droplets, indicating decrease in the hydrophobicity of the cell surface, and have a slightly increased resistance to the antibiotic ethambutol. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Extracellular side. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family."}
{"protein": "MPEGPEIRRAADNLEAAIKGKPLTDVWFAFPQLKTYQSQLIGQHVTHVETRGKALLTHFSNDLTLYSHNQLYGVWRVVDTSEEPQTTRVLRVKLQTADKTILLYSASDIEMLRPEQLTTHPFLQRVGPDVLDPNLTPEVVKERLLSPRFRNRQFAGLLLDQAFLAGLGNYLRVEILWQVGLTGNHKAKDLNAAQLDALAHALLEIPRFSYATRGQVDENKHHGALFRFKVFHRDGELCERCGGIIEKTTLSSRPFYWCPGCQH", "text": "FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. SIMILARITY: Belongs to the FPG family."}
{"protein": "MKNKSLFEVIKIGKVEVXXKIXMAVMGAFG", "text": "FUNCTION: Involved in fermentation of amino acids (Stickland reaction) such as leucine, isoleucine, valine and phenylalanine."}
{"protein": "MARSGSCPHLLWDVRKRSLGLEDPSRLRSRYLGRREFIQRLKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRSGHRANIFSAKFLPCTDDKQIVSCSGDGVIFYTNIEQDAETNRQCQFTCHYGTTYEIMTVPNDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDILINCRRAATSVAICPPVPYYLAVGCSDSSVRIYDRRMLGTRATGNYAGRGTTGMVARFIPSHLSNKSCRVTSLCYSEDGQEILVSYSSDYIYLFDPKDDTARELKTPSAEERREELRQPPVKRLRLRGDWSDTGPRARPESERERDGEQSPNVSLMQRMSDMLSRWFEEASEVAQSNRGRGRPRPRGGTNQPDVSTLPTVPSSPNLEVCETAMDVDMPAALLQPSTSSTDPVQAQAATAAIESPRSSSLLSCPDSEPRQSVEASGHHAHHQSDNSNERLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSTASSSRGNGSHCKSEGQEECLVPPSSVQPPEGDSETRAPEELSEKGTLPENLTQNQIDTAQLDNFPAEPLDSNSGEKNNPSQDSPCGLPEEGTLSETDRETCEQASTESATRHASTKPELPSQTEAIEQASTESATRHTSANPELPSQTEAIAPLAHEDPSARDSALQDTDDSDDDPVLIPGARYRTGPGDRRSAVARIQEFFRRRKERKEMEELDTLNIRRPLVKMVYKGHRNSRTMIKEANFWGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSPLEESRIFNRKLADEVITRNELMLEETRNTITVPASFMLRMLASLNHIRADRLEGDRSEGSGQENENEDEE", "text": "FUNCTION: Ligand-dependent coactivator of nuclear receptors. Enhance transcriptional activity of the nuclear receptors NR3C1 and AR. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MFNWFRRQFGKDNTAPESAPPEGAEVSPELAPEVIQAETESPSEEDSQTTELAAPPPEEPSSDTANPDDYLQWAKAAYQNIQARKAETVSPPESAAAITVEAGIEETAEEIVVAPESDQATATEADLPSPETEITTGPAWLQKSDRLEALKETAVEEATVAGTLTAESMAMDDDFMWSAKVLAAQGRSAADVSAEEIDWLRKLRQGLSKTRVNLVNQLKSIVGQGPLNEAAVEEIEAILLQADVGVEATDYIITTLQDKLREEALPPEQAIEFLKEILRSILDRPLLSLPSAEFAPEAEGLNVWLLTGVNGAGKTTTIGKLAFMAKQSGYDCVIAAADTFRAAAVEQVKVWGERSGVPVIANPGQNTDPAAVVYDGISAAQSRNVNLLLVDTAGRLQNKKNLMDELAKIRRIIDKKAPNATVESLLVLDATLGQNGLRQAEVFAEAAKLSGVVLTKLDGSAKGGVALAVAQQLNLPIRFIGAGEGIEDLRPFSSYEFVEALLNG", "text": "FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily."}
{"protein": "MASVPRGENWTDGTVEVGTHTGNLSSALGVTEWLALQAGNFSSALGLPATTQAPSQVRANLTNQFVQPSWRIALWSLAYGLVVAVAVFGNLIVIWIILAHKRMRTVTNYFLVNLAFSDASVAAFNTLINFIYGLHSEWYFGANYCRFQNFFPITAVFASIYSMTAIAVDRYMAIIDPLKPRLSATATKIVIGSIWILAFLLAFPQCLYSKIKVMPGRTLCYVQWPEGPKQHFTYHIIVIILVYCFPLLIMGVTYTIVGITLWGGEIPGDTCDKYHEQLKAKRKVVKMMIIVVVTFAICWLPYHVYFILTAIYQQLNRWKYIQQVYLASFWLAMSSTMYNPIIYCCLNKRFRAGFKRAFRWCPFIQVSSYDELELKTTRFHPTRQSSLYTVSRMESVTVLFDPNDGDPTKSSRKKRAVPRDPSANGCSHRGSKSASTTSSFISSPYTSVDEYS", "text": "FUNCTION: This is a receptor for the tachykinin neuropeptide neuromedin-K (neurokinin B). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: neuromedin-K > substance K > substance P. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSSEKEYVEMLDRLYSKLPEKGRKEGTQALPNLIIFNIGNTTMIRNFAEYCDRIRREDKICMKYLLKELAAPGNVDDKGELIIQGKFSSQVINTLMERFLKAYVECSTCKSLDTVLKKEKKSWYIVCLACGAQTPVKPL", "text": "FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family."}
{"protein": "MTREQYILATQQNNLPRTENAQLYPVGIYGWRKRCLYFFVLLLLVTMIVNLAMTIWILKVMNFTVDGMGNLRVTKKGIRLEGISEFLLPLYVKEIHSRKDSPLVLQSDRNVTVNARNHMGQLTGQLTIGADAVEAQCKRFEVRASEDGRVLFSADEDEITIGAEKLKVTGTEGAVFGHSVETPHIRAEPSQDLRLESPTRSLIMEAPRGVQVSAAAGDFKATCRKELHLQSTEGEIFLNAETIKLGNLPTGSFSSSSPSSSSSRQTVYELCVCPNGKLYLSPAGVGSTCQSSSNICLWS", "text": "FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. May play a role in the maintenance of striated muscle membrane stability (By similarity). SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single- pass type II membrane protein Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family."}
{"protein": "MDYLKTVVPSQLMAERGANLVVINPGSSNVRIGFASQDVPFNIPHCIARHITQQKDDTPRLSVRDKMLNCHATPSQNAERERAYDIIASLLKIPFLDEDMPSANQALPPKMGRVDALSSQQNKDDSKFTWTDVMDRSIKSSTPIVDKDADVDPLQRSTPDDTEPNSEENMYKEIIFGEDALKIPPSESYCLSHPIRRGHFNISQDYSLHQVLEDLRTIWNWILTEKLHINPRDRHLYSAILVLGETFDNREIKEMLSIVLCDLGFSTAVIHQEALAAAFGNGLSTSCVVNIGAQVTQVVCVEDGVALPHTALALPYGGDDISRCLLWVQRRHCTWPNFQTDPVNKPIDMLMLNKLKESYSQIRSGSFDAVSVVHSYEHEKSVGHQKTKLSALNVPPMGLLYPRVLVPEEYPPPPRSWFQDYDDMLEDTWQTSDSLYSSGNGGFGMWDNYPMFPTRLKKFDNIGLVEAIVSSILSTGRIELQRKLFCSIQLVGGTASTAGLAPVLEQRVLNTIPSNQPIEKAEVLQSRSYPLFVPWKGGVILGVLDIGRDAWIHREDWAKNGVHIGSGRKYRDSYFLQAQAMCYYNS", "text": "SIMILARITY: Belongs to the actin family. ARP8 subfamily."}
{"protein": "MASLQTQMISFYLIFLSILLTTIFFFKVNSTETTSFSITKFSPDQQNLIFQGDGYTTKGKLTLTKAVKSTVGRALYSTPIHIWDRDTGNVANFVTSFTFVIDAPSSYNVADGFTFFIAPVDTKPQTGGGYLGVFNSKEYDKTSQTVAVEFDTFYNAAWDPSNKERHIGIDVNSIKSVSTKSWNLQNGERANVVIAFNAATNVLTVTLTYPNSLEEENVTSYTLNEVVPLKDVVPEWVRIGFSATTGAEFAAHEVHSWSFHSELGGTSSSKQAADA", "text": "FUNCTION: D-mannose specific lectin. SIMILARITY: Belongs to the leguminous lectin family."}
{"protein": "MAAPWASLRLVAPMWNGRIRGIHRLGAAVAPEGNQKKKRTILQFLTNYFYDVEALRDYLLQREMYKVHEKNRSYTWLEKQHGPYGAGAFFILKQGGAVKFRDKEWIRPDKYGHFSQEFWNFCEVPVEAVDAGDCDINYEGLDNLLRLKELQSLSLQRCCHVDDWCLSRLYPLADSLQELSLAGCPRISERGLACLHHLQNLRRLDISDLPAVSNPGLTQILVEEMLPNCEVVGVDWAEGLKSGPEEQPRDTASPVPA", "text": "FUNCTION: Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ATP synthase subunit s family."}
{"protein": "MTLPEKLLKITPKILVIMGSVRSKRLCPTIATWVGEMGKRETNFDYEKVDLTDWPLSMSDEPGLPIMGIDVYTQEHTKAWGSKIAGADGFVFVTPQYNGGYPAILKNALDHLYHEWNGKPLLIVSYGGHGGGDCASQLKHVAGFLKMRVAPTMPALTLPRDKIVQGVVDPAVEFTKHLGELKKAFGEFSQLFESNPERKP", "text": "FUNCTION: Has several reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor. May be involved in ferric iron assimilation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MSGSRKFFVGGNWKMNGSRDDNDKLLKLLSEAHFDDNTEVLIAPPSVFLHEIRKSLKKEIHVAAQNCYKVSKGAFTGEISPAMIRDIGCDWVILGHSERRNIFGESDELIAEKVQHALAEGLSVIACIGETLSERESNKTEEVCVRQLKAIANKIKSADEWKRVVVAYEPVWAIGTGKVATPQQAQEVHNFLRKWFKTNAPNGVDEKIRIIYGGSVTAANCKELAQQHDVDGFLVGGASLKPEFTEICKARQR", "text": "FUNCTION: Antigen to the host M.1 monoclonal antibody. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family."}
{"protein": "MYRDRGTVNSRPEVVDRKRINDALERPSPSTSRQVNGKGKGTVTAATTTANLIGKQQSNNINHRDSRSASLSKNNTVSDDESDTDSEESDVSGSDGEDTSWISWFCNLRGNEFFCEVDDDYIQDDFNLCGLSSLVPYYEYALDLILDVESSQGEMFTEEQNELIESAAEMLYGLIHARYILTSKGLAAMLDKYKNYDFGRCPRVYCCGQPCLPVGQSDLPRSSTVKIYCPKCEDIYYPRSKYQGNIDGAYFGTTFPHLFLMTYGHLKPAKATQNYVQRVFGFKLHKP", "text": "FUNCTION: Plays a complex role in regulating the basal catalytic activity of the alpha subunit. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor GBFl, resulting in stimulation of its DNA binding activity (PubMed:7696877). CK2 phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis (PubMed:21330376). CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation (PubMed:19509278, PubMed:19509420). Stimulates the binding of CCA1 to promoters (Probable). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the casein kinase 2 subunit beta family."}
{"protein": "MATLSDGLFDDMSVLGVIGYVLEQTRFIFLVPILKRLVNLCQVVSVLLFVDAAYMAIVVAIVKLLGRTPQKVLKWESFKSDDIELAPSSNHPMVLIQIPIFNEKEVCQLSIGAACKLSWPLDRMIIQVLDDSTEEESQKLVRLECKKWESEGITIKSEVRGGFREGFKAGALTAGMKHSYVDEYKCEFVVIFDADFQPEPDFLERTVPFLVHNPEIALVQAGWKYGNADECCMTRIQEMSLNYHFAVEQKSGSSILGFFGFNGTAGVWRIKALNEAEGWKDRTIVEDMDLAVRAYLRGSKFVYVDDVKVKNELPSSFQAYRFQQHRWSCGPANLFKKIAMEIIKNQNVSLWKKVYLIYNFFFLRKIVVHIFTFVFYCVILPATVIFPEIEVPKWTTIYIPATITILNAIATPKSFYLILYWILFENVMAMHRSIGTLIGLLETSRVKEWIVTQKLGESNNLRENLIFPDHYSFPERLRWREIMVGMYLFICGYYDFVFGRTYLYVYLFLQSIAFFVVGVGYVGMPVPSTPVQTSE", "text": "FUNCTION: Probable mannan synthase which consists of a 4-beta- mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4- mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like A subfamily."}
{"protein": "MAYVTSTQLYNWRFTQDELANQRQECNAAVRRRLSAQYRAKAEVKGGDVPAEPTFLTAEEEFIIVKRYIFAMKELFHQFSDSGLPVDVFGFAATYLKRFYLNNSVMDYFPREMMLTALYLACKAADYPLGLQTFAAHIPRNREHYSEIVVHSELFLMEKLQYDIWIHTPYRPLSGLLVDLLAYRKTQLGEPMTIEAGEVATADMMTSLKKEGYEIIHKWFQTDLCLTHSPSQFALAVLLELGQKHPDLGVEKFVKNSVCEYNSSDELMEQKWTALNEKMEQIQTMIGEFEFLSDLTYGSDLEAVLMQCRNPLYDPLSEEYAAAKEQAEKLMSFLD", "text": "FUNCTION: Regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily."}
{"protein": "MDRITGPFRKSKKSFRKPLPPIQSGDRIDYQNIDLLRRFISQQGKILSRRVTRLTLKQQRLLNLAIKQARILSFLPFTNTESLEKMKARIREARLKAEEVRLKNKEARFKKAKEARNQKKTTFRKIFINPKNSKLNTETNQI", "text": "SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family."}
{"protein": "MENMAEEELLPLEKEEVEVAQVQVPTPARDSAGVPAPAPDSALDSAPTPASAPAPAPALAQAPALSPSLASAPEEAKSKRHISIQRQLADLENLAFVTDGNFDSASSLNSDNLDAGNRQACPLCPKEKFRACNSHKLRRHLQNLHWKVSVEFEGYRMCICHLPCRPVKPNIIGEQITSKMGAHYHCIICSATITRRTDMLGHVRRHMNKGETKSSYIAASTAKPPKEILKEADTDVQVCPNYSIPQKTDSYFNPKMKLNRQLIFCTLAALAEERKPLECLDAFGATGIMGLQWAKHLGNAVKVTINDLNENSVTLIQENCHLNKLKVVVDSKEKEKSDDILEEGEKNLGNIKVTKMDANVLMHLRSFDFIHLDPFGTSVNYLDSAFRNIRNLGIVSVTSTDISSLYAKAQHVARRHYGCNIVRTEYYKELAARIVVAAVARAAARCNKGIEVLFAVALEHFVLVVVRVLRGPTSADETAKKIQYLIHCQWCEERIFQKDGNMVEENPYRQLPCNCHGSMPGKTAIELGPLWSSSLFNTGFLKRMLFESLHHGLDDIQTLIKTLIFESECTPQSQFSIHASSNVNKQEENGVFIKTTDDTTTDNYIAQGKRKSNEMITNLGKKQKTDVSTEHPPFYYNIHRHSIKGMNMPKLKKFLCYLSQAGFRVSRTHFDPMGVRTDAPLMQFKSILLKYSTPTYTGGQSESHVQSASEDTVTERVEMSVNDKAEASGCRRW", "text": "FUNCTION: May play a role in motor coordination and exploratory behavior. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family."}
{"protein": "MAALRAVCSLRGVGAQVLRAGSGIRLPSQPSRGARRWQPDIEWAEQFSGAVMYPSKETAHWKPPPWNDVDVLKEKVVTNVTLNFGPQHPAAHGVLRLVLELSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSLAVEKLLNIQPPPRAQWIRVLFGEITRILNHIMAVTTHALDIGAMTPFFWMFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLMDDIYEFSKNFSLRIDEVEEMLTNNRIWRNRTVDIGVVSAEDALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPIGSRGDCYDRYLCRVEEMRQSLRIIEQCLNKMPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEIDR", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:30922174). Essential for the catalytic activity of complex I (PubMed:30922174). Essential for the assembly of complex I (By similarity). Redox-sensitive, critical component of the oxygen- sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction (PubMed:30922174). Plays an important role in carotid body sensing of hypoxia (By similarity). Essential for glia-like neural stem and progenitor cell proliferation, differentiation and subsequent oligodendrocyte or neuronal maturation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 49 kDa subunit family."}
{"protein": "MARLLLRRGFFSSHIRMSSDQLGELGTGAGKGGGGGGSVRAAGGSFGRREAAEEERYFRQKEREQLAALKNHHEEEIDHHKKEIERLQREIDRHKGKIRKLKHDD", "text": "FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing fech to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (PubMed:23135403). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ATPase inhibitor family."}
{"protein": "MERFVLCIHWERRAESGAEQHRVPQGLAYAQDIYTQLKEYSTKYTSTFPACSLTGNPGTRKWFFALQSLYGSFQFCSSDWDDLCPAVTTEDNEEPVQTALDECLEALQFPDGEDDNSRDSISQTNLFEEAAELLHQLSDKLPAPGRALVDVLLFTPEAPKLKDCLSAIGAIKHLKEWHSAKITIVSKDCKGWQKIAKFLSANVVESACPKELIDSHELWRGNIEISERKFTSEVEFPEFCLRSVSDDKFPYFEHNGDDKNKAVLLPEVFHYYGTSLEYVQMVALSEIPSYFVSDSVFELSITRNALQGKSKLMLDQLCSLTDKVGAIFMLSCNVCSLPNPPALQRSSKKWREYMSRKPKDIKVPGVELKGEYCSYYFLIQGKGSGFCKATLLHSASQISGAASLVLLHQRLNNYQPGNMAEGTSEILDSVPHFRGEQIAVRERILARAQALAVNEYLKRHEALPHPSVSHVNNLRTLLAVTRERVIGDCESRLDGVSYKNLQNITVSTPTVSESEAMISNPADWPERNVLQNLENFEKVKQRLRASILSSSAEQLLGRKDGLKEGMTLLDAKELLKYFTPQGIAVGELQPLQVQRGDNAFLLTPKLTPKKLKGLPFEKAAECHYHGLEYCLDNRKALDRDVAFSELQSRLIRYETQTTCTRECCPVPFALSPLPSPAVLSEPGSVPDGESIQTELRGEPLLLKRRSRDLDGLYASKRLAKSGSSDSLVSLASEGSGHQPPTRATRLRPERAASSTSAVQPPSARVQMAPSVPAQSKQSTHPDLEQKESRSQKHNRMLKEVVSKTLQKYGIGVEHPCYAACNQRLFDISKFFLKDLKTSRGLLDEMKKAASNNAKQVIQWELDKLKKK", "text": "FUNCTION: May play a role in mdm2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of mdm2, thereby enhancing mdm2 stability. This promotes mdm2-mediated ubiquitination of p53/TP53 and its subsequent degradation (By similarity). SIMILARITY: Belongs to the MTBP family."}
{"protein": "MNAPLTLHRSGAGPSSYSSHRPLITQQRLVGASSSIPSQFIHNEFSFEQYIKDHLNVKLDNDAQICPDYSERLQCPRGASCPRRHVRPSHLNFLPAGSTALRDPNKRTVCKHWLRGLCKKDDQCDYLHEYDMRRIPECRFYATFGFCNSGDDCLYLHVDPAIKRRECERYNRGFCPKGPLCTKKHVRRVACPLYLAGFCPEGLDCPRGHVKSTPASSASRSNSPIQTHRPLTAAEAFGTGTGRGDEYGDGAGMRNQRAPAGRYGLPSGGAAGGAGAADIGASRGGMGYANNMQRRPNNVFGAPAQGAQEGGRGWRKDLSEVLCFKCGEMGHFANMCPNPALPGNRGGVERGPGGQARQARDRPRPY", "text": "FUNCTION: Component of the cleavage factor I (CF I) involved in pre- mRNA 3'-end processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CPSF4/YTH1 family."}
{"protein": "MTTLVLDNGAYNAKIGYSHENVSVIPNCQFRSKTARLKTFTANQIDEIKDPSGLFYILPFQKGYLVNWDVQRQVWDYLFGKEMYQVDFLDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGALSAHRYFRDNPSELCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYRDMDIAKLKGEENTVMIDYVLPDFSTIKKGFCKPREEMVLSGKYKSGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNSLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYAWEGGKLISENDDFEDMVVTREDYEENGHSVCEEKFDI", "text": "FUNCTION: Required for formation and/or maintenance of proper nucleolar structure and function (PubMed:26164235). Plays a dual role in the regulation of ribosomal DNA (rDNA) transcription (By similarity). In the presence of high glucose, maintains active rDNA transcription through H2A.Z deposition and under glucose starvation, is required for the repression of rDNA transcription, and this function may be independent of H2A.Z (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus Nucleus, nucleolus Note=Colocalizes with HP1 family proteins at pericentric heterochromatin. SIMILARITY: Belongs to the actin family. ARP6 subfamily."}
{"protein": "MTEHSFKQIDVFSNKGFRGNPVAVFFDADNLSQKEMQQIAKWTNLSETTFVQKPTIDKADYRLRIFTPECELSFAGHPTIGSCFAVVESGYCTPKNCKIIQECLAGLVELTIDGEKDEDTWISFKLPYYKILQTSETAISEVENALGIPLNYSSQVSPPVLIDDGPKWLVIQLPNATDVLNLVPKFQSLSQVCKNNDWIGVTVFGELGKDSFESRSFAPLIHVNEDPACGSGAGAVGVYIGSSQKTPTSLSFTISQGTKLSRQAISKVSVDVSSNKSIAVFVGGQAKTCISGKSFI", "text": "FUNCTION: May have isomerase activity (By similarity). Enhances target gene silencing when coexpressed with antisense RNA. SIMILARITY: Belongs to the PhzF family."}
{"protein": "MRRATYAFALLAILVLGVVASGCIGGGTTTPTQTSPATQPTTTQTPTQTETQAVECGSGKVVIWHAMQPNELEVFQSLAEEYMALCPEVEIVFEQKPNLEDALKAAIPTGQGPDLFIWAHDWIGKFAEAGLLEPIDEYVTEDLLNEFAPMAQDAMQYKGHYYALPFAAETVAIIYNKEMVSEPPKTFDEMKAIMEKYYDPANEKYGIAWPINAYFISAIAQAFGGYYFDDKTEQPGLDKPETIEGFKFFFTEIWPYMAPTGDYNTQQSIFLEGRAPMMVNGPWSINDVKKAGINFGVVPLPPIIKDGKEYWPRPYGGVKLIYFAAGIKNKDAAWKFAKWLTTSEESIKTLALELGYIPVLTKVLDDPEIKNDPVIYGFGQAVQHAYLMPKSPKMSAVWGGVDGAINEILQDPQNADIEGILKKYQQEILNNMQG", "text": "FUNCTION: Involved in an abc transport system for maltotriose. Binds maltotriose much more tightly than maltose. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
{"protein": "MNGTEGPNFYVPFSNKTGVVRSPFEFPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVGFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTLPAFFAKAASIYNPVIYIMMNKQFRTCMITTLCCGKNPLGDDEVSASASKTETSQVAPA", "text": "FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G- proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cell projection, cilium, photoreceptor outer segment Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEANAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE", "text": "FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAPPSRRECPFPSRRFPGLFLAALALLLSSRSDACGPPPTFVAMELTSRPKPYYKVGEQVEYDCKKGYHHFAPFLTHTVCDRNHTWLPISDAPCVKKVCHYIPNPAHGQAILANGTYSFGNQLHFICNDGYYLIGKAILYCELKGSDAVWSGRPPICQKILCKPPPTIKNGKHTFSEVDVFEYLDAVTYSCDPAPGPDPFSLVGESTIYCRDSLGWSGDPPECKVVKCRFPVIENGRQTAGFGIKFYYNAAVMFECYEGFHIIGSDTIVCNSNSTWDPPVPKCVK", "text": "FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein Note=Inner acrosomal membrane of spermatozoa."}
{"protein": "MGDSMHVLKLVSDLETPVSTFMKVSRGEEFAFLLESVELGSAFGRHSFIGIGKKDVLVFEKGILRTSNQQLDYTSSPLKAIKDWLEVYRYSVKHDELPSFRGGAVGFVSYDYISYIEKVKVKASVFPTFYFVVPEHLIIFDHLKNNVFIISDSPEELTSKVLSPFEEKPEKNVFVTEPESNFEREQFYKVVEKAKKYIVEGDIFQVVLSQAFTFKTTLDPFYIYRALRMINPSPYMFYLKFGDTVVLGSSPETMAKVEGDKATVKPIAGTRPRGRTVEEDLKLERELLNDEKEIAEHVMLVDLGRNDLGRVCKEGTVRVEKKMVIERYSHVMHIVSQVSGELKDDKDAVDVFEATFPAGTVSGAPKVRAMEIIEELEPTPRGPYAGAVGYFSFPDDKGRMNMDSAITIRSFFFKGKQGWLQAGAGIVYDSVPEREYQETLNKLRALFRSLEVAQKIQGGLF", "text": "FUNCTION: Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity). SIMILARITY: Belongs to the anthranilate synthase component I family."}
{"protein": "MSVDNLLDLLNDQQLAAVLNIDKPVRIIAGAGSGKTRVITTKIAYLIEKQNIDPSRILAVTFTNKAAKEMKERVLQITNNSFKSPFISTFHSWCSKVLRIDGKHIGLEDKFLIIDSDDQKRIIKSALKESNIELSENDKKTFDKKILYKIKEWKEELVDPSEAILNATSTLEKNFAVIYRLYQNTLLKNNSLDFDDLQIYVYRLFKQNNEILNKWRNAYDYVLVDEFQDTNELQFSLIKFLTINTNHLTVVGDPDQTIYSWRGAKLDIILNFNKTYSNAISIVLNQNYRSTKQILDISNSFIKNNKFREHKEIFTNNKSGKKVVLKECNSKTSEASYVSSKIKELVKQGYHYKDIFILYRMNAWSQEFEKELANKKIPFQLIGGIKFRERKVIKDAMAFLKMISIKDNLSSQRVLGLIPKIGNITIEKIINTANLNHLNIFDLITNEDKTLLHSITKNLDELIEVFKTAHQLYLDNTNIEEILKYLLIQSGYENKLKIRKEQDDLENINALYDQLKRFDEDFDPKYYSEENKLIAFLQEEALTSDIDEAEQIDKVSLLTVHAAKGLENKVVFITGLNQGIFPSRISETSINELEEERRALYVALTRAKDELFLTYVKGDYSHIMQSELKPSKFIHELDKDLYEFETQFLNTLLYDSNDYKQSSFYVSPKQHNLYNVGDHVEHKLFGKGVVVKIINDQLQISFTNSSYGIMMIATNNSALSKV", "text": "FUNCTION: Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair (By similarity). SIMILARITY: Belongs to the helicase family. UvrD subfamily."}
{"protein": "MADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTQSTFKNTEINFQLGIEFDEVTADDRKVKSLVTLDGGKLIHVQKWNGQETTLTRELVDGKLILTLTHGSVVSTRTYEKEA", "text": "FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MTNYPFFRQGTIFVDNSAIQRNSENKNSLSIENIFGRFPKEFFQFFSINVSKSTTKKSSVVIKPSTITAPWLENEYLDSNTSLLSVHSIQPSFIGMSDFAIGLDPSLKRILPEIRFRLDFQHLKSIAKGATSTIKVVTHRDKITDAKIYYAAKVYRKTKTSHKKRLNTMVYFLREWSIQPKLDHPNILKVICPCVTLTSVFNKSAGFCLVQEYCPQGDLFKQIEEKVLTLEDKCCYLKQILQAVAYLQSQRIAHRDLKPENILIGRDGLLKLTDFGTSEIVGNPGDNESIRFVSGAVGSLAYLAPEAFHENEYCGLLADRWSCGILLKVLFTGYFPFKTSVKTDLYYSKYMSILTDTCGISSTDESSFQTEVIKQIPTLQPLRYIPEGAKKIILSLLNPDSQNRPSLDSILGTAWVRKLDCCSNFSTDHENKSLQEVDFDASKPITRKSLIPRIHNHQTLV", "text": "FUNCTION: Has a role late in meiosis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MVSYRATTETISLALEANSSEAITILYQVLEDPSSSPEAIRIKEQAITNLCDRLTEEKRGEDLRKLLTKLRPFFSLIPKAKTAKIVRGIIDAVAKIPGTTDLQITLCKEMVEWTRAEKRTFLRQRVEARLAALLMENKEYVEALALLSTLVKEVRRLDDKLLLVDIDLLESKLHFSLRNLPKAKAALTAARTAANAIYVPPAQQGTIDLQSGILHAEEKDYKTGYSYFFEAFESFNALGDPRAVFSLKYMLLCKIMVSQADDVAGIISSKAGLQYVGPDLDAMKAVADAHSKRSLKLFENALRDYKAQLEDDPIVHRHLSSLYDTLLEQNLCRLIEPFSRVEIAHIAELIGLPLDHVEKKLSQMILDKKFAGTLDQGAGCLIIFEDPKADAIYSATLETIANMGKVVDSLYVRSAKIMS", "text": "FUNCTION: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6A is required for proteasome assembly (By similarity). SIMILARITY: Belongs to the proteasome subunit S9 family."}
{"protein": "MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKESLLAGHLQCSPEQAVELSALLAQTKFGDYNQNTAQYSYEDLCEKELSSSTLNSIVAKHKELEGISQASAEYQVLQIVSAMENYGIEWHAVRDSEGQKLLIGVGPEGISICKEDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRSDQSPPSSPLKSSDSSMSCSSCEGLSCQQTRVLQEKLRKLKEAMLCMACCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein."}
{"protein": "MSKVLKVGLLLLLVAVAASAYAVAEENGAPKENKQLPQIDDYGVTNKCPANQPFKWNCNYCTCGPEGKDASCTRMACPQH", "text": "FUNCTION: Parasitic wasp protein that may interfere with the host immune response. The recombinant protein inhibits trypsin activity and prophenoloxidase (PPO) activation, an enzyme essential for both clotting and insect innate immune responses. It does not inhibit activity of chymotrypsin and protease K, and has no effect on phenoloxidase (PO) activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I19 family."}
{"protein": "MADPQAFCVAEERSGHCAVVDGHFLYVWGGYVSIEDNEVYLPNDEMWTYDIDSGLWKMHLMEGELPPSMSGSCGACIHGRLYVFGGYDDKGYSNRLYFVNLRTRDGTYTWEKITKFDGQPPTPRDKLSCWVYKDRLIYFGGYGYRRHSELQECFDVHDASWEEQIFWGWHNDVHVFDTKTRTWSQPEIKGGVPPQPRAAHSCAVLGNKGYVFGGRVLQTRMNDLHYLNLDTWVWSGRISVNGESPKHRSWHTLTAITDDKLFLFGGLNADNIPLSDGWIHNITTNCWKQLRHLPYTRPRLWHTACLGKENEIMVFGGSKDNLLFLDTGHCNDLLIFQTQPYSLLRSCLDCIGKNAIILKSQISLLPPKLLQQVLKKITFWTAANYRKEQRIRKEETENNQPRVSSC", "text": "FUNCTION: Substrate-recognition component of a Cul5-RING (CRL5) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL5(KLHDC1) complex mediates ubiquitination and degradation of truncated SELENOS selenoprotein produced by failed UGA/Sec decoding, which ends with a glycine. SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
{"protein": "MTPWSLPQFAFHLVTFLSIAFIASIFVLPFLTFSFVLSSATVGLSFASRTSFEIGLFFYDRFVILLQGQLRGMIDQLPSNQPAKEEKKVKAQQQGDELFTQQEQAAPSQTLGSTIPLQSIEESLLDST", "text": "FUNCTION: Involved in spore wall assembly. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OSW5 family."}
{"protein": "MIPQTLEQLLSQAQSIAGLTFGELADELHIPVPPDLKRDKGWVGMLLERALGATAGSKAEQDFSHLGVELKTLPINAEGYPLETTFVSLAPLVQNSGVKWENSHVRHKLSCVLWMPIEGSRHIPLRERHIGAPIFWKPTAEQERQLKQDWEELMDLIVLGKLDQITARIGEVMQLRPKGANSKAITKGIGKNGEVIDTLPLGFYLRKEFTAQILNAFLETKPL", "text": "FUNCTION: Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MutH family."}
{"protein": "MLESIRLYKDLHDFELQGPTRVVEWIGDKSICVAGYDSAKRNEILQLLIPQKLHAKENPGLCPERDLKVEHGGFIDEPVYSLKHIPQSSLIVTSGPASCPLWVWQIGPEDRDVIQPISTLPSDAGKGTWTRIATTTSASPQILHGSQADSIRLTDIESTKQIHTLGVSGSDGVSTLCFLDSRTVFVCCMNGRQFIADIRMPGAASEGRVGEEGLSCVTWCSAVHPSKEDVCSTVASVSSEGHMCLTDPRNLSVPLKCATWCTPIPAASEQFLSICWAPALSDCISVSGFGGSVQIFDTKRWDSAMKEREAVFIHKGHSVMGTCEDGREPTVTAHAWHPWKERTVLSAASDGSLHVWNWSDLPVHDGTEL", "text": "FUNCTION: May play a role in the regulation of microtubule organization and dynamics. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Cleavage furrow Note=During interphase, located in the cytosol. During mitosis, accumulates at the spindle poles and microtubule asters and later in the cleavage furrow. SIMILARITY: Belongs to the WD repeat WDR73 family."}
{"protein": "MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS", "text": "FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. SIMILARITY: Belongs to the cycloisomerase 2 family."}
{"protein": "MDSEEEEEVPQPMPSIPEDLESQKAMVAFFNSAVASAEEEQARLCGQLKECTASAWLICWPRPRRNLRQQPQPQELGVIPCVGRPTRPCRGPWRSCGRVHRTVPEPEGSAEGGGVHQQAGPGQGRGEGEAAGAGVACGRLQQVA", "text": "SIMILARITY: Belongs to the GOLGA2 family."}
{"protein": "MEESNNNNFLFSPDYIWSQLLENNNNNYNNNYNNINNSINENLLNELNSFQNTGVFDLDTNIEQQQQQQPTEIQQQLQNYQEFQQKKYQERQEQYQIQYQQSYIEPLNFNETYNNETYCNIIPQPPQVEQQQEQEQEQEQQQKQQQQQYIEKQIQEIIKIPEKRQTLNQIPIEMMQHNFFNTPKLDQQLLSNYSDFFKTNPILPTTTTTTTTTAITIDQQQQNHIDNQSLNNSNTKTSKNQQKDNNLPKKKNLSYDITKITFNNNNIEKKRDQTESSKNFREKKKEYVKEIESKILALTLENDKLKKENDSLKTINGSNLMRPEPESINMIMECKKIIKKLEKALIDNDERSLIYLLYHYHSETSKRYSLVEIEVDKIANPYSQIKLKLAGYIQNPTTLDIFDGNFNNNNNNNGNKEEEEEISWFIKYKNEANLTIEQSNKLDLLRNQHGLIFETLLKERKQLDNEILKVFNEIIIASYDGSNANLISDKGFELKSKLKSLKMKIISSLNLNLDTFSSISSILLPKQEALLLVRAHLFGSSKLNPQMDFLNNVWTNIISSNSSCSVFEILNSLKEFSDLENLELNKNS", "text": "FUNCTION: Probable transcriptional regulator. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MATQRRDESPSGLSDIVEPDGLLGIGLTSRHIEAFGRKVTSTAGHLMGPITDSSNGSHYHTAMADIHRELRRPTTQRKVFSLTQTSPTDLVRSKLSTSEIQSRALSSVPDELLANIPEDSSSYSLFEGFKATQDDHEFRKAHRRRSSKGKKLLKDGEAAGALPSAPTDLKKERDLLSRRLDLMGVRKNMCSSEIHEIDNKIANLHNIRKIVLDRLAGLEMEEAELEHQLTEIDNKLEDIQEEAPKTPLTAATPKSSSVNDDSVVSEDAALDASFMSESIYQKLPSHSPRSLKQRSIRKRSMPILHEHFAPGSQIKEMQAHTDMVTAIDFDYPFGTMVSAALDDTVRVWDLNTGRCTGFLEGHNASVRCLQVEDNIVATGSMDASVKLWDLSRARTVTRDNRLNKPSEGEGEDDNASDAFSLFSATTLEDCYVFSLDAHVDEVTALHFRGNTLISGSADKTLRQWDLVKGRCVQTLDVLWAAAQASTLAADTQWRPSGRLPDASADFVGALQCFDAALACGTADGMVRLWDLRSGQVHRSLVGHTGPITCLQFDEVHLVTGSQDRSIRIWDLRMGSIFDAYAYDKPITSMMFDTKRIVAAAGENVVKVYDKADGHHWDCGAGVGADESGPAPATVERVRLKDGYLLEGRKDGTVAAWTC", "text": "FUNCTION: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family."}
{"protein": "MINTFNPEVRLAIHDLDKVGPAIPLENYEAALRAILTGKASPVETASFLASLHLTKAEEVPDILMQTVQILKSYSTPIANIEMVSPRFVDIVGTGGDGHNTFNVSTASAIVAAGAGLWVCKHGNKASTSASGSADLLMSFGCDLLNVTPKNIVSITEQCKFSFLFAPMCHPTLKNVAPIRKQLGLPTIFNLVGPLLNPIPTYARIIGVSKLSLGEVVAKTLLKLGAGRSLVVCGEEGLDEISPAGPTHTWLVRDGTITHEVYTPESFHLQSHPLSSVASGTPSANAILLEELLSNMLHANHPILDYVLMNTAALLHVAGMAESLREGVKIAQQSISSGAALRELSNFSTISQQP", "text": "SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase family."}
{"protein": "MSLSSLDAVLSLIATSSTLDQDSAKVPQCQVCKRKFANQKTLRTHMKHITCRPGRSNVVNHKFRCENCEKQFTNKPNLKRHQITHSGSKSKKCSTCQRTFFREDQLQRHLHNHLKERSHFDCPVLNCSMQFVFYEGVENHLVNHHHFSYSESAPCGKCHKLFGSPRHLLVHYHFDHKEALRSSAPAPTSSARLSPITVSTSGSPRAQLAISPQEKPPQKLSINLGTSPMIEEFCEQNSATLPNTDQQLSPTLSPNEPRFRNLITSEPTPSFECKHCTIKFHDATMSIMHNALHAPGSPFKCAICGAECGNKIVFTMHIITASHDFGGIGT", "text": "FUNCTION: Together with ehn-3, may play a role in gonadogenesis. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MSSLYTKLVKGATKIKMAPPKQKYVDPILSGTSSARGLQEITHALDIRLSDTAWTIVYKALIVLHLMIQQGEKDVTLRHYSHNLDVFQLRKISHTTKWSSNDMRALQRYDEYLKTRCEEYGRLGMDHLRDNYSSLKLGSKNQLSMDEELDHVESLEIQINALIRNKYSVSDLENHLLLYAFQLLVQDLLGLYNALNEGVITLLESFFELSIEHAKRTLDLYKDFVDMTEYVVRYLKIGKAVGLKIPVIKHITTKLINSLEEHLREETKRQRGEPSEPQQDRKPSTAISSTSSHNNNSNDKNKSIAQKKLEQIREQKRLLEQQLQNQQLLISPTVPQDAYNPFGSQQQDLNNDTFSFEPTQPQMTAQVPQPTANPFLIPQQQQQALQLTSASTMPQPSEIQITPNLNNQQTGMYASNLQYTPNFTGSGFGGYTTTENNAIMTGTLDPTKTGSNNPFSLENIAREQQQQNFQNSPNPFTLQQAQTTPILAHSQTGNPFQAQNVVTSPMGTYMTNPVAGQLQYASTGAQQQPQMMQGQQTGYVMVPTAFVPINQQQQQQQHQQENPNLIDI", "text": "FUNCTION: Involved in endocytosis and clathrin cage assembly. SUBCELLULAR LOCATION: Bud Bud neck Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm. SIMILARITY: Belongs to the AP180 family."}
{"protein": "MARIHLIIILLVISSTSSSSSSLREQEEDMIKALPGQPQVGFSQFSGYVTVNESHGRSLFYWLTESPSSSHTKPLLLWLNGGPGCSSIGYGASEEIGPFRINKTGSNLYLNKFTWNTEANILFLESPAGVGFSYTNTSSDLKDSGDERTAQENLIFLIKWMSRFPQYQYRDFYIVGESYAGHYVPQLAKKIHLYNKAFNNTPIINLKGFMVGNGDMDKHYDRLGAAMYAWSHAMISDKTYKSILKHCSFTADKTSDKCNWALYFAYREFGKVNGYSIYSPSCVHQTNQTKFLHGRLLVEEYEYDPCTESYAEIYYNRPDVQRAMHANLTSIPYKWTLCNMVVNNNWKDSEFSMLPIYKELTAAGLRIWVFSGDTDAVVPVTGTRLALSKLNLPVKTPWYPWYSEKQVGGWTEVYEGLTFATIRGAGHEVPVLQPERALTLLRSFLAGKELPRSY", "text": "FUNCTION: Probable carboxypeptidase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "PTHIKWGD", "text": "FUNCTION: Inhibits angiotensin-converting enzyme."}
{"protein": "MAEVAENVVETFEEPAAPMEAEVAETILETNVVSTTELPEIKLFGRWSCDDVTVNDISLQDYISVKEKFARYLPHSAGRYAAKRFRKAQCPIVERLTCSLMMKGRNNGKKLMACRIVKHSFEIIHLLTGENPLQILVSAIINSGPREDSTRIGRAGTVRRQAVDVSPLRRVNQAIWLLCTGAREAAFRNIKTIAECLADELINAAKGSSNSYAIKKKDELERVAKSNR", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MQQVIPAPRVQVTQPYAGQKPGTSGLRKKVTEATQPHYLENFVQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRLAYANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGIILTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHTTKIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVKVVDTVQDYTSLMQKLFDFDLLKGLFSNKDFTFSFDGMHGVAGPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTYAHDLVELLDIHKKKDVGAVPQFGAACDGDADRNMILGRQFFVTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVAAKNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNHIREKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQFGRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGNKADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGSVGATIRIYFEQFEQQEIQHETATALANIIKLGLEISDIAQFTGRNEPTVIT", "text": "FUNCTION: May be involved in membrane fusion in exocytosis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MNRFVIADSTLCIGCHTCEAACSETHRQHGLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEFSGSRPLDIPANANTPKAPPAPPAPARVSTLLDWVPGIRAIAVKCDLCSFDEQGPACVRMCPTKALHLVDNTDIARVSKRKRELTFNTDFGDLTLFQQAQSGEAK", "text": "FUNCTION: Probable electron transfer protein for hydrogenase 3. FUNCTION: Probable electron transfer protein for hydrogenase 3."}
{"protein": "MNPTTATDAHERTSLLSGRPQSAANSTAPYERQVQPSRKSQCFTPVTVITIITLIYRLATTMVITTNIRVLHTVACQLWYHVNDPDVFPGGNIPEKYCALPGVDKYYAIMVSMTTVIDGLGGILGTGIASYMSSRFGRKPVLMFLLSCTMIDHLAILTVQNVYGWKQLVTFGLIMIVETIGNENTTVFLVSMYVVDVTEAERRTAALSSITGWLVLGGALAYSIGGSITTFLHSNSAVYIVSFSVTGIVLTFTAFVLPESFPAEKRDLLRLERLAETRGHSQSWTQKIKAVATVALEPMELLKPTFNPITGKANWRLVYCALHSFIVTLADAYALPAMLIFFTTQYSYTPAQMGYVMTTYSVSSVFVLAIALPLFIRWFKPLYNNTQTKSVPDEGDGLRATDSGEAGVHTQEVVVSETSDRMDVHITVISWTIESLAYIVLGTVGSFYAQLLGRPLPLLALDLDAFQEFEA", "text": "FUNCTION: Major facilitator-type transporter; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product (PubMed:28763571). FUNCTION: Major facilitator-type transporter; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
{"protein": "MMADTEMQEQDVPSGTKGVVEEPSELEKDLNSIERPKSPVPEDTTHTLDSDVHLSDAPIANQIEANEEVGGQNSVDGRNGDVDQSEKKITSDGGQEETTLGESNPLKGDPSSPHVPEESVKKWKTWLLSDAEAREVDEAGAPQDQEAFIKEVEAFNKENFLEFKAPKFYGQPLNCLKLWRAVIKLGGYDVVTTSKLWRQVGESFHPPKTCTTVSWTFRIFYEKALLEYEKHLRQNGELNLPGSASLPSSGIEKEASSHQASGSGRTRRDAAARAMQGWHSQRLLGSGEVTEPIVKEKGLNSTPKQKNLKNIGVQKQKTTTGMDLVFSHESEKQSTAEVIDVGPPADWVKINVRETKDCFEIFALVPGLLREEVRVQSDPAGRLVIAGQPEQLDNPWGITPFKKVVNFPARIDPLHTSAVVSLHGRLFVRVPFEQ", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
{"protein": "MEPATVLSIALAAVCIGVTGYSIYLSFGPPSKELADPFDDHED", "text": "FUNCTION: May play a role in photosystem I and II biogenesis. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbN family."}
{"protein": "MNASEKLSQKAAQSVTRRFITWLKSPDFRKYLCSTHFWGPLSNFGIPIAAILDLKKDPRLISGRMTGALILYSSVFMRYAWMVSPRNYLLLGCHAFNTTVQTAQGIRFVNFWYGKEGASKQSVFENIMQAAKHPESGTRQK", "text": "FUNCTION: Mediates the uptake of pyruvate into mitochondria. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family."}
{"protein": "MEKLIITAAICGAEVTKEHNPNVPYTVEEIVREAKSAYDAGASVIHLHVREDDGTPTQSKERFKMCVDAIKEACPDAIIQPSTGGAVGMTDEERLQPVFLKPEMASLDCGTCNFGGDEIFVNTENMIINFSKYMIKNGVKPECEVFDKSMIDMAIRLAKKGHIQTPMHFNFVMGVNGGISATPRDLVFLIGSIPSESSFTVSAMGRNQFPMAAMAIITGGHVRVGFEDNVYIEKGVPAKSNGELVEKVVRLAKEFGRPVATPSEAREILGISK", "text": "FUNCTION: Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the CoA moiety. SIMILARITY: Belongs to the KCE family."}
{"protein": "MRAVLETADIAIVALYFILVMCIGFFAMWKSNRSTVSGYFLAGRSMTWVAIGASLFVSNIGSEHFIGLAGSGAASGFAVGAWEFNALLLLQLLGWVFIPIYIRSGVYTMPEYLSKRFGGHRIQVYFAALSLILYIFTKLSVDLYSGALFIQESLGWNLYVSVILLIGMTALLTVTGGLVAVIYTDTLQALLMIVGALTLMIISMMEIGGFEEVKRRYMLASPNVTSILLTYNLSNTNSCNVHPKKDALKMLRNPTDEDVPWPGFVLGQTPASVWYWCADQVIVQRVLAAKNIAHAKGSTLMAGFLKLLPMFIIVVPGMISRILFADDIACINPEHCMQVCGSRAGCSNIAYPRLVMKLVPVGLRGLMMAVMIAALMSDLDSIFNSASTIFTLDVYKLIRRSASSRELMIVGRIFVAFMVVISIAWVPIIVEMQGGQMYLYIQEVADYLTPPVAALFLLAIFWKRCNEQGAFYGGMAGFVLGAVRLTLAFAYRAPECDQPDNRPGFIKDIHYMYVATALFWVTGLITVIVSLLTPPPTKEQIRTTTFWSKKSLVVKESCSPKDEPYKMQEKSILRCSENSEATNHIIPNGKSEDSIKGLQPEDVNLLVTCREEGNPVASLGHSEAETPVDAYSNGQAALMGEKERKKETEDGGRYWKFIDWFCGFKSKSLSKRSLRDLMEEEAVCLQMLEEPPQVKLILNIGLFAVCSLGIFMFVYFSL", "text": "FUNCTION: Electrogenic Na(+)-coupled sugar symporter that actively transports myo-inositol and its stereoisomer scyllo-inositol across the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1 (PubMed:7537337, PubMed:1372904). Maintains myo-inositol concentration gradient that defines cell volume and fluid balance during osmotic stress, in particular in the fetoplacental unit and central nervous system (By similarity). Forms coregulatory complexes with voltage-gated K(+) ion channels, allosterically altering ion selectivity, voltage dependence and gating kinetics of the channel. In turn, K(+) efflux through the channel forms a local electrical gradient that modulates electrogenic Na(+)-coupled myo-inositol influx through the transporter (By similarity). Associates with KCNQ1-KCNE2 channel in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability (By similarity). Associates with KCNQ2-KCNQ3 channel altering ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (By similarity). Provides myo-inositol precursor for biosynthesis of phosphoinositides such as PI(4,5)P2, thus indirectly affecting the activity of phosphoinositide-dependent ion channels and Ca(2+) signaling upon osmotic stress (By similarity). Has very low affinity for sugars such as L-fucose and L-xylose, with an affinity about three orders of magnitude lower than myo-inositol (PubMed:7537337). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Note=Colocalizes with KCNQ1 at the apical membrane of choroid plexus epithelium. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
{"protein": "MIEAEEQQPCKTDFYSELPKVELHAHLNGSISSHTMKKLIAQKPDLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGPLVAKETVKLAEEFFLSTEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEGGSLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKKWNHLKPRVLHI", "text": "FUNCTION: Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine (PubMed:21755941, PubMed:29884623). Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A) (PubMed:21755941, PubMed:29884623). Catalyzes the removal of different alkyl groups not only from N6-substituted purine or 2-aminopurine nucleoside monophosphates but also from O6-substituted compounds in vitro (PubMed:21755941). SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family."}
{"protein": "MNRRHLFAWLFRHLSLNGHLQCHVHRHSHQLTQIPLDTRLWVFRRNRNHTVHRLLNKNCSRRYCHQDTSMLWKHKALQKYMEDLNKEYQTLDHCLHHISASEGDRRSLTRRHAELAPLAVIYKEIQEAEQAIEELESMCKSLNKQDEKQLQELALEERQTIAQKINMLYSELFQSLLPKEKYDKNDVILEVTSGRTTGGDICQQFTREIFDMYQNYSSYKHWRFELLNYTPADYGGLHHAAARISGDNVYKHLKYEGGIHRVQRIPEVGLSSRMQRIHTGTMSVIVLPHPDEVDVKVDPKDLRIDTFRAKGAGGQHVNTTDSAVRLVHIPTGLVVECQQERSQIKNKEIALRVLRARLYQQIIEKDKCQQRSARKLQVGTRAQSERIRTYNFTQDRVTDHRIAYEVRNIKEFLCGEKCLDQLIQRLLQSADEEAITEFLDENLKSVK", "text": "FUNCTION: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-cognate termination stop codons AGG and AGA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
{"protein": "MTDRAPHYGLLGLLQTPTQPPKDNPPKLPEKQRRRGRDTTRNRRLFASDGPTDEEGPEVPEIPPSDEEKENRPEPLPVVENGWHSFLRETLEHQLGRLQREVNQDFEDLYRRLGIHP", "text": "FUNCTION: Contributes to multiple aspects of the viral life cycle including viral genome amplification, suppression of suprabasal cell differentiation and egress of newly formed virions. Induces host cell cycle arrest at the G2 phase by associating with and preventing the nuclear entry of host CDK1/cyclin B1 complexes. Inhibits cellular DNA replication by preventing loading of host replication licensing proteins MCM2 and MCM7 onto chromatin. Within the cytoplasm, associates with host kinase SRPK1, a splicing factor regulator, and inhibits its activity. Therefore, E4 favors expression of late viral transcripts by inhibiting SRPK1-mediated phosphorylation of host serine-arginine (SR) proteins that have critical roles in mRNA metabolism. Late in the infectious cycle, E4 also acts to diminish the integrity of the keratinocyte by disrupting the keratin cytoskeleton and inducing apoptosis through alteration of mitochondrial function to facilitate egress of the newly formed virions. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the papillomaviridae E4 protein family."}
{"protein": "MNLASSACLLLLFLLGIAQALPVQNEEGHEEGNKEGHGEEGVEEGDEDDFVDFTTRILTSNNNTDQLLLEGDLVAPTNRNAMKCWYNSCFWKKASNGFVVIPYVISSQYSRGEVATIEGAMRAFNGRTCIRFVRRTNEYDFISVVSKNGCYSELGRKGGQQELSLNRGGCMYSGIIQHELNHALGFQHEQTRSDRDSYVRINWQNIIPASAYNFNKHDTNNLNTPYDYSSIMHYGRDAFSIAYGRDSITPIPNPNVPIGQRNGMSRWDITRSNVLYNCR", "text": "FUNCTION: Participates in the breakdown of the egg envelope, which is derived from the egg extracellular matrix, at the time of hatching. Thus allowing the newly hatched fish to swim free. HCE binds tightly to the egg envelope while it exerts the choriolytic swelling action. SUBCELLULAR LOCATION: Zymogen granule Note=Stored as proenzymes in the zymogen granules."}
{"protein": "TKSPDCGGILSPSGLSYFA", "text": "FUNCTION: May play a role in the developmental transition from cell proliferation to cell differentiation during neurogenesis."}
{"protein": "SKHSKPSKHSKHSKPSKHSKPSKHSKPEKCGSAMKRTEAAKCARKNGRFNSKRCTCTSVGKPSKPSKHSKPSKHSKPSKHSKPSKHSKPSKHSKPSKHSKPEKCGSAMKRTEAAKCARKNGRFNSKRCTCTSVGKPSKPSKHSKPSKHSKPSKHSKPSKHSKPSKHSKPEKCGSAMKRTEAAKCARKNGRFNSKRSTCNSVGKPSKPSKH", "text": "FUNCTION: Used by the larvae to construct a supramolecular structure, the larval tube. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MASKALVLLGLFAVLLVVSEVAAASSATVNSESKETVKPDQRGYGDNGGNYNNGGGYQGGGGNYQGGGGNYQGGGGNYQGGGGRYQGGGGRYQGGGGRYQGGGGRQGGGGSGGSYCRHGCCYRGYNGCSRCCSYAGEAVQTQPGH", "text": "FUNCTION: Regulates the function of the receptor protein kinase WAK1, and namely the phosphorylation of OEE2. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the GRP family."}
{"protein": "MSGVQSKAARLQKERKEKLSADRERKTATSLCLKHSEVPASMMKQFNALMEMQEVMFAEMRETYKNDIKEMLLKRTAPWVKHLEERIGQQEGDAISERPKPGEKVEELSSGTDEDTENLTVRSKKGKQDKAKPLNSSHVLKSSLERGGEALRGEHGRCGESSSLVDWKNANEKPAREASCQSEENRLKAPKESPPEGGAGATLRLAADFSAATLDVGRQWSQVFRLLKEKELEPELQCSVKLAFKCDGEANVFSDLHSLRQFTSRKPFLRELLKDVFPQNEGGRRNELRERLGKTLGDTKHEARRIASDSLSFLFIKEVEVASPEVKTYKEETLDRKNKGTLKKQEGEEEEISETQGEETSEGETSELGEEEGSESEEEEESSESEEEEESSESAEEIGFISLVVDSESEEEVNRKTASQTKKKETFHGLKELAFSYLVWDSKKKKLVRCQEGGAAAASTQRIGMPCLTLYLTSPSESLGAGSDGPKSHSCTKLSALSQVTPLLTNIEKGRYKVPQTEEPTAKEADLILETEENFKRGVISVIRQMQREVDKIKNIYVSDVLNMKSSLDDLNSLACTIEARVSEQEDAVEGLTKDTMQLAREIVDKERLREREDRFRSSNIRVIGIPEKENRENGAVDIIKEVIEENFAELEDQSLEIVSAHRVPNSVDEHRLTPRHILVKFGSASDKQRVLKASRAKQEITYRGSKIRLTADLSPGTIDARSQWCGIIKILQDEGFQPRILYPAKLAFDFKGKTKIFFDIEEFKKFISDIPYLKDLLNNIH", "text": "SIMILARITY: Belongs to the transposase 22 family."}
{"protein": "MYRPDHVFVILCAVFFTGQVTAVPAGTGITHPHSPQLGPFEPVGFASQTQTQLAPSRGPFTWLRDSVIERIWGIDKEKQSLSKPGPRPVPEKSWSRYGSDIVLRIEVHNAEEVEALAEAVNILFLDVWDSNENYVDIRLAKEVVPSLLGLLPQSLQKTHTLLIEDLSKMIYESQYPSRGFKHHKNDQTTRHTGFQSSDVGDLFFDNYQPFPVILQWMRLLVSMFPSHVQLINVGVTHEGRDIPAFRLGARPSGDQNEEPRKTVMIVGGSHAREWISTSTVAYIAFQLITEFGNSPPITKLLEDFDWILVPTINPDGYVYSWDMDRLWRKNRQQTGLPFCPGIDLDRSWGYEWDGQGTRANPCSESYAGNNAFDSMETRTIAEWAYNQTQNKQSDFVGFLDLHSYSQQILYPYSYSCSTVPPTLENLEELAFGIAKAIRMTNQETYVVKSACEGVVTTEKGTGQRVSTNVESTGGSALDWFYHQLHAKYSYQIKLRDKGMYGFLLPPENIVPTGREIFNSVLVLGHFLLGEGANGLEWSFLSGSGSAAGKEDDSSRTFDRLFFDNNEEQLEKSADDRDYFSVVEEDVYQDEGWGLW", "text": "FUNCTION: Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis. SUBCELLULAR LOCATION: Vacuole Secreted. SIMILARITY: Belongs to the peptidase M14 family."}
{"protein": "MNAERKFLFACLIFALVIYAIHAFGLFDLLTDLPHLQTLIRQSGFFGYSLYILLFIIATLLLLPGSILVIAGGIVFGPLLGTLLSLIAATLASSCSFLLARWLGRDLLLKYVGHSNTFQAIEKGIARNGIDFLILTRLIPLFPYNIQNYAYGLTTIAFWPYTLISALTTLPGIVIYTVMASDLANEGITLRFILQLCLAGLALFILVQLAKLYARHKHVDLSASRRSPLTHPKNEG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TVP38/TMEM64 family."}
{"protein": "MATLVELPDSVLLEIFSYLPVRDRIRISRVCHRWKRLVDDRWLWRHVDLTLYTMRPKVMWHLLRRYMASRLHSLRMGGYLFSGSQAPQLSPALLRALGQKCPNLKRLCLHVADLSMVPITSLPSTLRTLELHSCEISMAWLHKQQDPTVLPLLECIVLDRVPAFRDEHLQGLTRFRALRSLVLGGTYRVTETGLDAGLQELSYLQRLEVLGCTLSADSTLLAISRHLRDVRKIRLTVRGLSAPGLAVLEGMPALESLCLQGPLVTPEMPSPTEILSSCLTMPKLRVLELQGLGWEGQEAEKILCKGLPHCMVIVRACPKESMDWWM", "text": "FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia."}
{"protein": "MKLLNVINFVFLMFVSSSSFAQVIEMNNSPLRDFVTWYSKQSGESVIVSPDVKGTVTVYSSDVKPENLRNFFISVLRANNFDMVGSIPSIIQKYNPNNQDYIDELPSSDNQEYDDNSAPSGGFFVPQNDNVTQTFKINNVRAKDLIRVVELFVKSNTSKSSNVLSIDGSNLLVVSAPKDILDNLPQFLSTVDLPTDQILIEGLIFEVQQGDALDFSFAAGSQRGTVAGGVNTDRLTSVLSSAGGSFGIFNGDVLGLSVRALKTNSHSKILSVPRILTLSGQKGSISVGQNVPFITGRVTGESANVNNPFQTIERQNVGISMSVFPVAMAGGNIVLDITSKADSLSSSTQASDVITNQRSIATTVNLRDGQTLLLGGLTDYKNTSQDSGVPFLSKIPLIGLLFSSRSDSNEESTLYVLVKATIVRAL", "text": "FUNCTION: Acts in the assembly and extrusion of the bacteriophage by forming a channel across the host outer membrane. This channel is just large enough to allow a newly synthesized phage particle to pass through. Extrusion is a process of concomitant assembly and secretion and takes place at specific assembly sites where host inner and outer membranes are in close contacts (By similarity). SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the inovirus G4P protein family."}
{"protein": "MKRLETIRHMWSVVYDHFDIVNGKECCYVHTHLSNQNLIPSTVKTNLYMKTMGSCIQMDSMEALEYLSELKESGGWSPRPEMQEFEYPDGVEDTESIERLVEEFFNRSELQAGESVKFGNSINVKHTSVSAKQLRTRIRQQLPLYSHLLPTQRVDICSLELIIIHTK", "text": "SIMILARITY: Belongs to the Schlafen family. Subgroup poxviridae B3 subfamily."}
{"protein": "MTYRSIGSTAYPTIGVVLLGGIANPVTRTPLHTSAGIAYSDSCGSIRSETRIYADEATHIYFNGTESTDDNRSVRRVLDRYSSVFEEAFGTKTVSYSSQNFGILSGSSDAGAASIGAAILGLKPDLDPHDVENDLRAVSESAGRSLFGGLTITWSDGFHAYTEKILDPEAFSGYSIVAFAFDYQRNPSDVIHQNIVRSDLYPARKKHADEHAHMIKEYAKTNDIKGIFDLAQEDTEEYHSILRGVGVNVIRENMQKLISYLKLIRKDYWNAYIVTGGSNVYVAVESENADRLFSIENTFGSKKKMLRIVGGAWHRRPE", "text": "FUNCTION: Catalyzes the phosphorylation of mevalonate (MVA) to yield mevalonate-3-phosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5- phosphate. SIMILARITY: Belongs to the GHMP kinase family."}
{"protein": "MALRWGIVSVGLISSDFTAVLQTLPRSEHQVVAVAARDLSRAKEFAQKHDIPKAYGSYEELAKDPNVEVAYVGTQHPQHKAAVMLCLAAGKAVLCEKPMGVNAAEVREMVTEARSRGLFLMEAIWTRFFPASEALRSVLAQGTLGDLRVARAEFGKNLTHVPRAVDWAQAGGALLDLGIYCVQFISMVFGGQKPEKISVMGRRHETGVDDTVTVLLQYPGEVHGSFTCSITAQLSNTASVSGTKGMAQLLNPCWCPTELVVKGEHKEFLLPPVPKNCNFDNGAGMSYEAKHVRECLRKGLKESPVIPLVESELLADILEEVRRAIGVTFPQDKH", "text": "SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MRKNTYAMRYVAGQPAERILPPGSFASIGQALPPGEPLSTEERIRILVWNIYKQQRAEWLSVLKNYGKDAHLVLLQEAQTTPELVQFATANYLAADQVPAFVLPQHPSGVMTLSAAHPVYCCPLREREPILRLAKSALVTVYPLPDTRLLMVVNIHAVNFSLGVDVYSKQLLPIGDQIAHHSGPVIMAGDFNAWSRRRMNALYRFAREMSLRQVRFTDDQRRRAFGRPLDFVFYRGLNVSEASVLVTRASDHNPLLVEFSPGKPDK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0294 family. SIMILARITY: Belongs to the UPF0294 family."}
{"protein": "MKRQAEATKRKHQVSSDAPPAKRRSEISSVLAKKASDKETQRTFKGSTHKTFPPKKYLDSIGNGRQEEKPCIKTSSLFKNNPEIPELHSTVVKQAREQVFSPEAFQELDLHPHLISTINTVLKMSSMTSVQKQSIPVLLEGRDALVRSQTGSGKTLAYCVPVVQSLQALTSKIQRSDGPYALVLVPTRELALQSFDTVQKLLKPFTWIVPGVLMGGEKRKSEKARLRKGINILISTPGRLVDHIKSTKNLHFNRIRWLIVDEADRILDLGFEKDITVILNAVNAECQKRQNVLLSATLTEGVTRLVDISLHNPVSISVLDKNCNQPNPKEVASIQLNSFAIPESLDQHVVLVPSKLRLVCLAAFILQKCKFEKNQKMIVFFSSCELVEFHYSLFLHTLLCHSGTPTSEHLPSASWPLKFLRLHGNMEQEERTSVFHEFSHSETGVLLCTDVASRGLDLPQVTWIVQYSAPSSPAEYIHRIGRTARIGCHGSSLLILAPSEAEYVNSLASHKINVGEIKMEDILAVLAKDDCFKRRQRGAQKSRASGPQEIRERATVLQTVFEDYVHSSQRMVSWAKKALQSFIRAYATYPKELKSIFHVRALHLGHVAKSFGLRDAPRNLSVSAVKKASLKRPHPRRKTQRKQHLVPAEVLHSEHSSGLEGGATKCRKQGKQQGLQVAPSKPGPWRE", "text": "FUNCTION: Probable ATP-dependent RNA helicase (By similarity). Plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Note=Colocalized with NPM1 in the nucleoli. SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7 subfamily."}
{"protein": "MGSRPRGALSLLLLLLAPPSRPASGCPAPCRCSETRVDCGRRGLTWASLPAAFPPDTTELVLTDNNLTALPPGLLDTLPALRRVHLGANPWRCDCRLLPLRAWLAGRPEREFYRDLRCVAPLALRGRLLPYVAEDELRAACAPGLLCWGALVAQLALLVLGLLHALLLALLLSRLRRLRAQARARSTREFSLTAPLVAESAGGGAS", "text": "FUNCTION: Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MPIFVNTVYCKNILALYTTKKFKTIIEAIGGNIIVNSTILKKLSPYFRTHLRQKYTKNKDPVTRVCLDLDIHSLTSIVIYSYTGKVYIDSHNVVNLLRASILTSVEFIIYTCINFILRDFRKEYCIECYMMGIEYGLSNLLCHTKDFITKHFLELEDDIIDNFDYLSMKLILESDELNVPDEDYVVDFVIKWYMRRRNRLGNLLLLIKNVIRSNYLSPRGIHNVKWILDCNIIFHCDKQPRKSYKYPFIEYPMNMDQIIDIFHMCTSTHVGEVVYLIGGWMNNEIHNNAIAVNYISNNWIPIPPMNSPRLYASGIPANNKLYVVGGLPNPTSVERWFHGDAAWVNMPSLLKPRCNPAVASINNVIYVMGGHSETDTTTEYLLPNHDQWQFGPSTYYPHYKSCALVFGRRLFLVGRNAEFYCESSNTWTLIDDPIYPRDNPELIIVDNKLLLIGGFYRGSYIDTIEVYNNRTYSWNIWDGMEW", "text": "FUNCTION: Might have a role in the suppression of host immune response. SIMILARITY: Belongs to the orthopoxvirus OPG047 family."}
{"protein": "MRRSTIVPTSRTSSSSPSPSQMKSFQMNRLVDQLSKLQSNMSHLENHLHVTAIQAEAIRRLGALQASLLMASGRVMSEARIQKSSDAVEEDVPM", "text": "FUNCTION: May play a role in the progression of mitosis in an environment of high osmotic stress."}
{"protein": "MATARPSIVGPDSGPESPFPYKMEGKVISGFGRGSKELGIPTANLPVDATISPWISSISSGVYYGWASLQLPPSHPESPSSSSCSPYVVFPMVMSIGYNPFYNNTERSAEVHILHKFTADFYDAPMRLLILGFIRDEKNYDSLEALVKDINTDCDVARTSLDRKAWVPQGGLLHPAVDVREKQGDLDGSWLVRPNDSPSA", "text": "FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme. SIMILARITY: Belongs to the flavokinase family."}
{"protein": "MSRQSSVSFRSGGSRSFSAASAITPSVSRTSFSSVSRSGGGGGGRISLGGACGAGGYGSRSLYNVGGSKRISYSSGGGSFRNQFGAGGFGFGGGAGSGFGFGGGAGSGFGFGGGAGFGGGYGGAGFPVCPPGGIQEVTVNQNLLTPLNLQIDPTIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTIKQNLDPLFEQYINNLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRSEIDNVKKQCANLQNAIAEAEQRGELALKDARNKLTELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGVGPVNISVVTNSVSSGYGGGSSIGVGSGFGGGLGSGFAGGLGPRFTRGGGGLGLGSGLSVGGSGFSAGSSQGGMSFGSGGGSGSSVKFVSTTSSSRRSFKS", "text": "FUNCTION: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress (PubMed:11408584). Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage inflammatory cytokines and CTNND1 localization in keratinocytes (PubMed:19267394). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "APLLVELPNGKLRGRDNEGYYEAELIPKADPPVGDLAFKD", "text": "SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "MGDKKSPTRPKRQAKPTADNGFWDCSVCTFRNSAEAFKCSICDVRKGTSTRKPRINSQLVAQQVAQQYATPPPPKKEKKEKPERPEKDRAEEERPDINPPDEHPVEQRDKDKSEKEQPEKEKKDREKEIIPAITKKPNSKKNRPKSDIHQSPPSERNSIQSGKSTTKTKNSHNSRPKLKNIDRSTAQQLAITVGNVTVIITDFKEKTRTSSTSSSTVTSSASSEQQHQSSGSESMDKGSSRASTPKGDLSLGHDESF", "text": "FUNCTION: May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Primarily found in the nucleus."}
{"protein": "MGVCQSFVLTDEMKDQIKVNKEIEKQLEKKKNMQLEQTVLLLGPGESGKSTVMKQMRAMTGNYTKTELHERKVLIIQNLCQFSEMLLEYVREYILEMTEDDDKRYTVMCEELKMAVIHDGIMRPELADTLKEFWGNSAIQDAYSKRDTFHLTDSAKYFFDNIDRIKLPGFEPTNQDIVHIRVPTTGVAQVEVIMNNIKLMICDCGGQRSERRKWYHFFDEADAVLFVAAISEFDQKLAEDEETNRMHESIRLFWTVFNGKFFKKAAVILFLNKIDLFEEKVKHVKIKDYFPKFEGANTVSEGTKFFRRQFREGIHPDFKKRMYTHETCAISDQVQIIINTVIDTVIQDNLKDTGMI", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. SIMILARITY: Belongs to the G-alpha family."}
{"protein": "MELYLDTANVAEVERLARIFPIAGVTTNPSIVAASKESIWDVLPRLQNAIGEEGTLFAQTMSRDAKGMVEEAKRLNNAIPGIVVKIPVTAEGLAAIKQLKKEGIVTLGTAVYSASQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQTLLERHAPDSMVLAASFKTPRQALDCLLAGCQAITLPLDVAQQMLNTPAVESAIEKFEQDWKNAFGNLNL", "text": "FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily."}
{"protein": "MKVNHSISRFRPASWFEKTKIIPPQVYIFRNLEYGQVLYSQFPNFSQTQVDKLFVRPNWSNRKPSLRRDIWKCMCVVNLQNYKQSVHLYQNLCRLRYLRDVAQRKESDKLRKKDSNGHVWYSGQYRPTYCQEAVADLRESLLKVFENATPAEKQTVPAKKPSIYWEDPWRMGDKDKHWNYDVFNALGLEHKLIQRVGNIAREESVILKELAKLESHPTEQTEVSSQ", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:24675956). mL67/MHR1 also has extraribosomal functions, being involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells (PubMed:11121487, PubMed:12198175, PubMed:14565971, PubMed:16337661, PubMed:7664749, PubMed:9736700). mL67/MHR1 also acts as transcription factor involved in regulation of RNA polymerase II- dependent transcription (PubMed:12034822). SUBCELLULAR LOCATION: Nucleus Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL67 family."}
{"protein": "MAPTLYDFHHLPHVKTQNESKKALWVTLLLTMFFTAVEIIGGLISNSLALLSDSAHM", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To cation A.eutrophus efflux system protein CzcD."}
{"protein": "MLRNLLALRQIGQRTISTASRRHFKNKVPEKQKLFQEDDEIPLYLKGGVADALLYRATMILTVGGTAYAIYELAVASFPKKQE", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase VIIa family."}
{"protein": "MGWEYAQVHLKYTIPFGVVLAAVYRPLMSRLDVFKLVFLITVAVVSTIPWDSYLIKNRIWTYPPGVVVGLTAWDIPAEELFFFVIQTFNTSLLYMILSKPTFHPIYLSKKTGWGKIAGQILFASAIIFGLVSVSSGGEGMYMGLILIWACPFLLFLWSISYQFIVNLPWTNTALPIALPTLYLWVVDTFALRRGTWSITSGTKYGVVLWDGLEIEEAVFFLLTNTLIVFGLIACDNNLAILDTFPEHFPRTKGVPSLLTIIRTLILPKEKYDEERIQGLVSAVALLRKKSRSFYLASGTFEGRLRIDLIRLYAFCRAADDLVDEAPSVDDSRASIEKLRKFLDLAYEENQEEPSQRLREYVTSSIPEMFHMALLQLPTYYLPKQPLDDLLKGFDTDLLFDRKSGAFPIETTEDLDIYGSRVAGTVAELCNHLILYHTPEAVPEDIQREVVASGQEMGIALQYVNIARDIKTDAEIDRVYLPLSWLKEAQLTPEDVIQQPHGPTIEALRHKLLDRAFEKYNMAKGAIDKLPSEGKGPIRVAVESYMEIGRVLREKGPTMKKGRATVPKMRRIRVAWSALNK", "text": "FUNCTION: Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation (PubMed:12172798). CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene (PubMed:12172798). CarAR also converts part of gamma-carotene into beta-carotene (PubMed:12172798). Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the lycopene beta- cyclase family. SIMILARITY: In the C-terminal section; belongs to the phytoene/squalene synthase family."}
{"protein": "MPSASKNFRLQSKYVFLTYPKCSSQRDDLFQFLWEKLTPFLIFFLGVASELHQDGTTHYHALIQLDKKPCIRDPSFFDFEGNHPNIQPARNSKQVLDYISKDGDIKTRGDFRDHKVSPRKSDARWRTIIQTATSKEEYLDMIKEEFPHEWATKLQWLEYSANKLFPPQPEQYVSPFTESDLRCHEDLHNWRETHLYHDEGRTGVRHPSLYICGPTRTGKTTWARSLGRHNYWNGTIDFTNYDEHATYNIIDDIPFKFVPLWKQLIGCQSDFTVNPKYGKKKKIKGGIPSIILCNPDEDWMLSMTSQQKDYFEDNCVTHYMCDGETFFARESSSH", "text": "FUNCTION: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'- TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities (By similarity). Acts a an inhibitor of C-sense gene transcription. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the geminiviridae Rep protein family."}
{"protein": "MSIYRISTTRKMPEVQKLNALLASYVRFISADSSLRDVLAAKIPAEQERVKNFRKQHGSFKMGETTVDMMYGGMRGIKALVTETSVLDADEGIRFRGLSIPECQKVLPAADGGEEPLPEGLFWLLLTGEVPSKAQVKQVSREWAARAALPQHVVTMLNNFPTSLHPMSQFSAAITALNHDSKFAKAYSDGVHKSKYWEHVYEDSMDLIAKLPVVAATIYCNTYRNGKGSKSIDSSLDWSANFVKMLGYDDPKFTELMRLYLTIHSDHEGGNVSAHTVHLVGSALSDPYLSFAAGMNGLAGPLHGLANQEVLVWLRKLQKEAGSNPSEEQLKEYIWKTLKSGQVVPGYGHAVLRKTDPRYTCQREFALKHLPNDELFQLVSKIYKVVPPILQETGKVKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRALGVLASLVWDRALGLPIERPKSLSTDLLMKMVQK", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the citrate synthase family."}
{"protein": "MTHALPKVVKSQLVQDIGVALILGSIAGCFFKYGVDKKKQRERVAFYEKYDKEDL", "text": "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. SUBCELLULAR LOCATION: Mitochondrion inner membrane."}
{"protein": "MKKHISMLFVFLMAVMVLSACNSSESSSNSEVSSSKTRTVKHAMGTSDNIPANPKRIVVLTNEGTEALLALGIKPVGAVKSWKGDPWYDYLKDDMKGVKNVGLETEPNVEAIAELKPDLIIGNKVRQEKIYDQLNAIAPTVFAESLAGNWKDNLTLYANAVNKADKGKEVIADFDKRVSDLKNKLGDQTNKTVSVVRFLSGESRIYYTDSFPGIILDQLGFKRPEKQVELFKKQKDQFTFSTDSKESIPDMDADVLFYFTYKADNAKENEKWANQWTSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIKAANYLLDDIETYFLKTK", "text": "FUNCTION: Part of the ABC transporter complex YfiYZ/YfhA/YusV involved in import of the iron-hydroxamate siderophores schizokinen, arthrobactin and corprogen. Binds the siderophores and delivers them to the surface of YfiZ/YfhA (Probable). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Cytoplasm. Membrane raft; Lipid-anchor. Note=Present in detergent- resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. SIMILARITY: Belongs to the bacterial solute-binding protein 8 family."}
{"protein": "MKIEKLGKSSVASSIALLLLSNTVDAAQNITPKREKKVDDKITLYKTTATSDNDKLNIFQILTFNFIKDKSYDKDTLVLKAAGNINSGYKNSNPKDYNYSQFYWGGKYNVSVSSESNDAVNVVDYAPKNQNEEFQVQQTLGYSYGGDINISNGLSGGLNGSKSFSETINYKQESYRTTIDRKTNHKSIGWGVEAHKIMNNGWGPYGRDSYDPTYGNELFLGGDKSSSNAGQNFLPTHQIPLLARGNFNPEFISVLSHKLFDTKKSKIKVTYQREMDRYTNQWNRSHWVGNNYKNQNTVTFTSTYEVDWQNILLKLIGTDSKETNPGV", "text": "FUNCTION: Part of a bi-component leucotoxin that acts by forming pores in the membrane of the target cells. LukE-LukD is as effective as the Panton-Valentine leucocidin (PVL) for inducing dermonecrosis when injected in the rabbit skin, but not hemolytic and poorly leucotoxic on human blood cells compared to other leucotoxins expressed by S.aureus. HlgA-LukD is a Ca(2+) channel inducer. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the aerolysin family."}
{"protein": "MTHRYDVAIVGGGVIGAAIGFELAKRRHRVAIFEKGTMGSGASSAAAGMLGAQSEFSTSSPLVPLALQSRALMPALAEELRERTGIDIGLVEKGLIKLATTEEEADDLYRHYTFWRGIGEPVQWLTKGEALEMEPRLAAEALAGAMYIPGDGQVSAPDLAAALAYAAASAGACLYEYTEVFDIRSDSSGHVLDTTGGTFAAEAVVIASGAWAARLGARVGLSLSVYPVKGECVMVRAPVPLLQTTVFAKNGCYIVPKSGNRLLIGATSTPGTFDRRVSAGGVMNLLHRAAHLVPDIEQAEWVASWSGIRPQTEDGLPYLGEHPERRGLFVAAGHYRNGILLSPLTGLLVADLVERKETAFDLAPFSLTRHIGKVGVE", "text": "FUNCTION: Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes glycine, sarcosine (N- methylglycine), N-ethylglycine, D-proline, D-alanine, glycine-ethyl ester, and some other D-amino acids. Does not act on L-proline (PubMed:17894345). Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate (By similarity). SIMILARITY: Belongs to the DAO family. ThiO subfamily."}
{"protein": "MPTIKCVVVGDGAVGKTCLLISYTTNKFPSDYVPTVFDNYAVTVMIGDEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVTSPASFENVKEKWFPEVHHHCPGVPCLIVGTQIDLRDDPSVQQKLARQHQHPLTHEQGERLARELGAVKYVECSALTQKGLKNVFDEAIVAALDPPVPHKKKSKCLVL", "text": "FUNCTION: Involved in development of cell polarity during the cell division cycle. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily."}
{"protein": "MRLATDQLGRPPQRVAVLSVHTSPLAQPGTGDAGGMNVYVLQSALHMARRGVEVEIFTRATTSADPPVVRVAPGVLVRNVVAGPFEGLDKYDLPTQLCAFTAGVLRAEATHEPGYYDIVHSHYWLSGQVGWLARDRWAVPLVHTAHTLAAVKNAALAEGDSPEPPLRAVGEQQVVDEADRLIVNTELEAEQLVSLHNADPSRIDVVHPGVDLDTFTPGDRAAARAALGLDPRETVVAFVGRIQPLKAPDILLRAAAKLPDVRVLVAGGPSGSGLAAPDNLVALADELGISERVTFLPPQSREDLVRVYRAADLVAVPSYSESFGLVAVEAQACGTPVVAAAVGGLPVAVRDGVTGALVDGHDVGDWAHTIDSLLSRGPATMRRAAVEHAATFSWAHTVDDLLASYGRAISDYRDRHPHADETLSRRTARRFSRRRGVRA", "text": "FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2- deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway. SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA subfamily."}
{"protein": "MSLDYCLMVTGPAYGNQRASSALQFARALLECGHRLGTVFFYQDGVHNANRLSAPAGDEVDLVRAWHELAQQHQVALHVCAAAALRRGVTDALQASLLKRSGENLQPGFELSGLGSLVQAALGCDRFIQF", "text": "FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrE/TusD family."}
{"protein": "MGNCCWTQCFGLLRKEAGRLQRVGGGGGSKYFRTCSRGEHLTIEFENLVESDEGESPGSSHRPLTEEEIVDLRERHYDSIAEKQKDLDKKIQKELALQEEKLRLEEEALYAAQREAARAAKQRKLLEQERQRIVQQYHPSNNGEYQSSGPEDDFESCLRNMKSQYEVFRSSRLSSDATVLTPNTESSCDLMTKTKSTSGNDDSTSLDLEWEDEEGMNRMLPMRERSKTEEDILRAALKYSNKKTGSNPTSASDDSNGLEWENDFVSAEMDDNGNSEYSGFVNPVLELSDSGIRHSDTDQQTR", "text": "FUNCTION: Necessary for adaptor protein complex 1 (AP-1)-dependent transport between the trans-Golgi network and endosomes. Regulates the membrane association of AP1G1/gamma1-adaptin, one of the subunits of the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1- adaptin attenuates the release of the AP-1 complex from membranes. Regulates endosomal membrane traffic via association with AP-1 and KIF5B thus linking kinesin-based plus-end-directed microtubular transport to AP-1-dependent membrane traffic. May act as effector of AP-1 in calcium-induced endo-lysosome secretion. Inhibits Arp2/3 complex function; negatively regulates cell spreading, size and motility via intracellular sequestration of the Arp2/3 complex. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Late endosome. Early endosome. Note=Localizes to the juxta-nuclear Golgi region and to tubular structures throughout the cytoplasm, which are highly mobile and cycle between the juxta-nuclear area and the cell periphery."}
{"protein": "MDATAFHPSLWGDFFVKYKPPTAPKRGHMTERAELLKEEVRKTLKAAANQIKNALDLIITLQRLGLDHHYENEISELLRFVYSSSDYDDKDLYVVSLRFYLLRKHGHCVSSDVFTSFKDEEGNFVVDDTKCLLTLYNAAYLRTHGEKVLDEAITFTRRQLEASLLDPLEPALLADEVSLTLQTPLFRRLRILEAINYIPIYGKEAGRNEAILELAKLNFNLAQLIYCEELKEVTLWWKQLNVETNLSFIRDRIVECHFWMTGACCEPQYSLSRVIATKMTALITVLDDMMDTYSTTEEAMLLAEAIYGWEENAAELLPGYMKDFYLYLLKTIDSCGDELGPNRSFRTFYLKEMLKVLVRGSSQEIKWRNENYVPKTISEHLEHSGPSVGAFQVACSSFVGMGDSITKGSFEWLLTYPELAKSLMNIARLLNDTASTKREQNAGHHVSTVQCYMLMHGTTMDEACEKIKELTEDSWKDMMELYLTPTEHPKLIAQTIVDFARTADYMYKETDGFTFSHTIKDMIAKLFVDPISLF", "text": "FUNCTION: Sesquiterpene cyclase catalyzing the production of beta- farnesene and alpha-bergamotene in equal amounts from farnesyl diphosphate. Involved in indirect defense by producing volatile signals attracting natural enemies of herbivores. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MEGQAAETNHRAETVVRAELCLSAEQGPETTAYSQKRCLFLPMEVWQEAQQLLALAAPAFLSQLMIFLISIVSSIFCGHLGKVELDAVSLAITIINITGVAVGTGLAGACDTLISQTFGGSNLKLVGIILQRGILILLLFCFPCWALLINTESILLLFRQDPEVSKLTQIYVLIFLPALPAAFLYQLLAKYLQNQGIIYPQVLTGFIANIFNALFNYILLYVLGLGVMGSACANTVSQFIQMILLFLYIVWRRLYADTWGGWSQACFEEWGAFIRLAVASMLMLCIEWWAFEISMFLAGVLGMVDLAAQAIIYQVAIVVYLIPLGLCIAGSIRVGHGLGAGNTEQAKRSALVVLCMTELCALLSGILLATLKDVVAYIFTSDPNIVALVSYVLPVYSACLLFDACVAACGGILRGSGKLKVGAISHTVGYYVIGLPLGISLMFAAKLGIIGFWFGILACGIAQSIFLIIFVFKIDWKRASEEAQTRASERVEIPQKIDNKPSVYQEGCPTEQGDVDPGNVESIEFSQSSTSSEGTSPTPAGAAQHTRTLILTRGLALGCAVGTLIIGIVIRLSV", "text": "FUNCTION: Multidrug efflux pump that functions as a H(+)/organic cation antiporter. Mediates the secretion of cationic compounds including drugs, toxins and endogenous metabolites. Plays a role physiological role in the excretion of drugs, toxins and endogenous metabolites through the kidney and liver, into urine and bile respectively. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Note=Localizes to the plasma membrane; at the brush border membranes of the proximal tubules (kidney) and at the bile caniculi (liver). SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MLRALWLFWILVAITVLFSKRCSAQESLSCDASGVCDGRSRSFTSIPSGLTAAMKSLDLSFNKITYIGHGDLRACANLQVLILKSSRINTIEGDAFYSLGSLEHLDLSDNHLSSLSSSWFGPLSSLKYLNLMGNPYQTLGVTSLFPNLTNLQTLRIGNVETFSEIRRIDFAGLTSLNELEIKALSLRNYQSQSLKSIRDIHHLTLHLSESAFLLEIFADILSSVRYLELRDTNLARFQFSPLPVDEVSSPMKKLAFRGSVLTDESFNELLKLLRYILELSEVEFDDCTLNGLGDFNPSESDVVSELGKVETVTIRRLHIPQFYLFYDLSTVYSLLEKVKRITVENSKVFLVPCSFSQHLKSLEFLDLSENLMVEEYLKNSACKGAWPSLQTLVLSQNHLRSMQKTGEILLTLKNLTSLDISRNTFHPMPDSCQWPEKMRFLNLSSTGIRVVKTCIPQTLEVLDVSNNNLDSFSLFLPRLQELYISRNKLKTLPDASLFPVLLVMKIRENAVSTFSKDQLGSFPKLETLEAGDNHFVCSCELLSFTMETPALAQILVDWPDSYLCDSPPRLHGHRLQDARPSVLECHQAALVSGVCCALLLLILLVGALCHHFHGLWYLRMMWAWLQAKRKPKKAPCRDVCYDAFVSYSEQDSHWVENLMVQQLENSDPPFKLCLHKRDFVPGKWIIDNIIDSIEKSHKTVFVLSENFVRSEWCKYELDFSHFRLFDENNDAAILVLLEPIERKAIPQRFCKLRKIMNTKTYLEWPLDEGQQEVFWVNLRTAIKS", "text": "FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity) (PubMed:15690042). May also promote apoptosis in response to lipoproteins (By similarity). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (PubMed:17486091). Acts as the major receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PhoS1 (pstS1), in conjunction with TLR1 and for some but not all lipoproteins CD14 and/or CD36. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). Recombinant MPT83 from M.tuberculosis stimulates secretion of cytokines (TNF-alpha, IL-6 and IL-12p40) by mouse macrophage cell lines in a TLR2-dependent fashion, which leads to increased host innate immunity responses against the bacterium (PubMed:22174456). Lung macrophages which express low levels of TLR2 respond poorly to stimulation by M.tuberculosis LpqH (PubMed:19362712). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM (PubMed:27220037). Interacts with TICAM2 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cytoplasmic vesicle, phagosome membrane; Single-pass type I membrane protein Membrane raft Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. SIMILARITY: Belongs to the Toll-like receptor family."}
{"protein": "MKENDVVLRTVTKIVVFILLTFGFYVFFAGHNNPGGGFIGGLIFSSAFILMFLAFDVHEVLESLPIDFKKLMIVGAIISALTAIVPVFFGKSFLYQSEAYIHFPLLGELHVTTITLFELGILLTVVGVIVTIMLALSGGKS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit B family."}
{"protein": "MAAFPNLNSGSGLKKLDEHLLTRSYITGYQASKDDITVFTALSKPPTSEFVNVSRWFNHIDALLRISGVSAEGSGVIVEGSSPITEEAVATPPAADSKDTAAEEEDDDDVDLFGEETEEEKKAAEERAASVKASTKKKESGKSSVLMDIKPWDDETDMKKLEEAVRSIQMEGLFWGASKLVPVGYGIKKLHIMCTIVDDLVSIDTMIEEQLTVEPINEYVQSCDIVAFNKI", "text": "FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP. SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family."}
{"protein": "MASAVYFCDHNGKPLLSRRYRDDIPLSAIDKFPILLSDLEEQSNLIPPCLNHNGLEYLFIQHNDLYVVAIVTSLSANAAAIFTFLHKLVEVLSDYLKTVEEESIRDNFVIIYELLDEVMDYGIPQITETKMLKQYITQKSFKLVKSAKKKRNATRPPVALTNSVSWRPEGITHKKNEAFLDIVESINMLMTQKGQVLRSEIIGDVKVNSKLSGMPDLKLGINDKGIFSKYLDDDTNIPSASATTSDNNTETDKKPSITSSSATNKKKVNIELEDLKFHQCVRLSKFENEKIITFIPPDGKFDLMNYRLSTTIKPLIWCDVNVQVHSNSRIEIHCKAKAQIKRKSTATNVEILIPVPDDADTPTFKYSHGSLKYVPEKSAILWKIRSFPGGKEYSMSAELGLPSISNNEDGNRTMPKSNAEILKGPVQIKFQIPYFTTSGIQVRYLKINEPKLQYKSYPWVRYITQSGDDYTIRLT", "text": "FUNCTION: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin. AP57 is probably a subunit of the Golgi membrane adaptor. SUBCELLULAR LOCATION: Cytoplasmic vesicle. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Membrane, clathrin-coated pit; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the adaptor complexes medium subunit family."}
{"protein": "MQQIPMTVRGAEQLREELDFLKNVRRPEIIKAIAEAREHGDLKENAEYHAAREQQGFCEGRIQEIEGKLGNAQIIDVSKMPNNGKVIFGATVVLVNTNTDEEVTYRIVGDDEADIKSGLISVNSPIARGLIGKELDDTVNITTPGGVVEFDIIEVNYI", "text": "FUNCTION: Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides (By similarity). SIMILARITY: Belongs to the GreA/GreB family."}
{"protein": "MIVGYRSTIITLSHPKLGNGKTISSNAIFQRSCRVRCSHSTTSSMNGFEDARDRIRESFGKLELSPSSYDTAWVAMVPSRHSLNEPCFPQCLDWIIENQREDGSWGLNPTHPLLLKDSLSSTLACLLALTKWRVGDEQIKRGLGFIETYGWAVDNKDQISPLGFEVIFSSMIKSAEKLDLNLPLNLHLVNLVKCKRDSTIKRNVEYMGEGVGELCDWKEMIKLHQRQNGSLFDSPATTAAALIYHQHDQKCYQYLNSIFQQHKNWVPTMYPTKVHSLLCLVDTLQNLGVHRHFKSEIKKALDEIYRLWQQKNEQIFSNVTHCAMAFRLLRMSYYDVSSDELAEFVDEEHFFATNGKYKSHVEILELHKASQLAIDHEKDDILDKINNWTRAFMEQKLLNNGFIDRMSKKEVELALRKFYTTSHLAENRRYIKSYEENNFKILKAAYRSPNINNKDLLAFSIHDFELCQAQHREELQQLKRWFEDYRLDQLGLAERYIHASYLFGVTVIPEPELSDARLMYAKYVMLLTIVDDHFESFASKDECFNIIELVERWDDYASVGYKSEKVKVFFSVFYKSIEELATIAEIKQGRSVKNHLINLWLELMKLMLMERVEWCSGKTIPSIEEYLYVTSITFCAKLIPLSTQYFLGIKISKDLLESDEICGLWNCSGRVMRILNDLQDSKREQKEVSINLVTLLMKSMSEEEAIMKIKEILEMNRRELLKMVLVQKKGSQLPQLCKDIFWRTSKWAHFTYSQTDGYRIAEEMKNHIDEVFYKPLNH", "text": "FUNCTION: Monoterpene synthase catalyzing the production of beta- phellandrene from neryl diphosphate. Produces also lower amounts of delta-2-carene, alpha-phellandrene and limonene. When incubated in vitro with geranyl diphosphate, catalyzes the formation of acyclic myrcene and ocimene as major products in addition to beta-phellandrene. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpse subfamily."}
{"protein": "MIPLALKTTESTDWSRAIHRYIASSYGPDYAEQFREEISSFQRLRQDIRGAGRDATGRDILFRYFAQLDSLERRINAAESGMKPDFTWSDSLSQEKVTQHSISFEKANVLYQLGAILSCMGEEMSRDDSCDPKASFHAFQNAAGVFAFIADKFLHAPLPDIGQDVVRAFNKLMLAQAQEMFCQDSIAKSVSVLTDVNQEQAGKVSALTAKLCAGVGALYKAAFESFTAIQEEQKWGDKNWPLECQGKNKYFTALGSLLYAKSLQNKPSTQKFGESIGYIQKSINEFNEASMLPLPNGANKKDFNKWYRDLVSTALDLARSTLKSSEHDNDLIYHSLVPAPATLGAVEPKEVVTATPLQDMYKEEDHVRVVGRDLFTRLVPMHVLQQTSVYSEEKASLLRSEGERIEVADQKLNSALEYMGLPGELYALKKDLQSGRDSGSSAQVPAVVLGYASEVKTLDLSPLKTSRDQILTQIRDSQALIASEETESTKMKDYYKDGWTQAPSAQVNASLLSDIRRVQESLVAAGASDEKLQAQYDGVKPDIELLSRGINNPELEKLFDADSSSSKSSSGPSESLIDLDFSQGAASRDPAASSTLDKLLPSCETSFRKLQNCQKDRQAIFYEFKDKVHRDDISGVLVNSKGADDNLIFEQELEKFQPYQQRLTATINTQALLIKDLADSWEKITRDPVVKNKVTDRKRALDHSHVIVERFRKAFESWKQVKTGLDKGLEFYRDLQNMADKVNVSATQFVNARRQEGKSILSAIQSNTTNELQSQLGRLSFGSGSSSAAPTSGGAPTLPPKPQQHTGDNYGQPSTYDPSVYGPNSPFMQQPPQHQQYGQPPHHQQYGQNPPPPPQGANQNQFWNQYR", "text": "FUNCTION: Involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. SUBCELLULAR LOCATION: Cytoplasm Endosome. SIMILARITY: Belongs to the BRO1 family."}
{"protein": "MVHWSAEEKQLITGLWGKVNVEECGAEALARLLIVYPWTQRFFSSFGNLSSPTAIIGNPKVPPHGRKFFTSFGEPVKNLDNIKNTYAKLSELHCEKLQVEPENFRLLGDILIIVLASHFARDFTPACQFPWQKLVSVVAHALPRKYH", "text": "FUNCTION: Beta-type chain found in early embryos. SIMILARITY: Belongs to the globin family."}
{"protein": "MATRFKGLYNKSFKCFSDIFDVEEEEEMEIGYPTDVRHVSHIGWDSSSSSAPSWLHEFKTSNNVLEPNSSWPFQDLKSAMEAFGEVESSKEMERESTKQNLKKKLSSKASLLCNSWSPRFSRSSKVLA", "text": "FUNCTION: Functions as downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Is involved in pollen tube growth regulation through its interaction with ARAC11/ROP1. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein."}
{"protein": "MSEEKARVDNAATGDIQHQGKDIFFAAVETTRMPMIVTDPNRADNPIIFSNRAFLEMTGYSSEEIIGTNCRFLQGPETDRAVVQSIREAIDERVDISTEILNYRKDGSTFWNALFISPVYNDAGDLIYFFASQLDISRRRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMGGYIDLIGSAAEKPTIDVQRVQRSVHHAKSAVERASTLTKQLLAFARKQKLQGRVLNLNGLVSSTEPLIERTFGPHVTIETDLDPALKNCRIDPTQAEVALLNIFINARDALVGRPDPKISIETRNLVVDELANMSYDGLLPGRYVSIAITDNGIGMPSSIRDRVMDPFFTTKEEGKGSGLGLSMVYGFAKQSGGAARIYTEEGVGTTLRLYFPVDEAMLTHAEPPKAVDRRIGSCERILIVEDRPDVAELAKMVLDDYGYICEIVLNAREALKKFESGSRYDLLFTDLIMPGGMNGVMLAREVRRRYPKIKVLLTTGYAESSIERTDIGGSEFDVVSKPCMPQDLARKVRQVLDGPNGIA", "text": "FUNCTION: Photosensitive kinase and response regulator that is involved in increased bacterial virulence upon exposure to light."}
{"protein": "MVNVPKTRKTYCKGRECRKHSQHKVTQYKAGKSSLFAQGKRRYDRKQSGFGGQTKPVFHKKAKTTKKVVLRLECVVCKTKAQLALKRCKHFELGGDKKQKGQALQF", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family."}
{"protein": "NYLHDTVGRLWGPSRAGLLDGLDWMVGDVQSR", "text": "FUNCTION: Plasmin-like serine protease. Has fibrinolytic and fibrinogenolytic but not plasminogenolytic activity. Cleaves after Arg and Lys residues."}
{"protein": "MIEVVAELSRGPVFLAGEALECVVTVTNPLPPTATSASSEALAWASAQIHCQFHASESRVALPPPDSSQPDVQPDSQTVFLPHRGERGQCILSTPPKILFCDLRLDPGESKSYSYSEVLPTEGPPSFRGQSVKYVYKLTIGCQRVNSPITLLRVPLRVLVLTGLQDVHFPQDEAVAPSSPFLEEDDSGKKDSWLAELAGERLMAATSCRSLHLYNISDGRGKVGTFGIFKSVYRLGEDVVGTLNLGEGTVACLQFSVSLQTEERVQPEYQRRRGTGVAPSVSHVTHARHQESCLHTTRTSFSLPIPLCSTPGFCTAIVSLKWRLHFEFVTSREPGLVLLPPLEQPEPATWTGPEQVPVDTFSWDLPIKVLPTSPTLVSYAAPGPSTSSITI", "text": "FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP and may thereby required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors. SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane. SIMILARITY: Belongs to the RGP1 family."}
{"protein": "MTTLRSAVAKVSETWKMKIAQRSFFEKTIKDFNFNTGYYNQIGLRWHDIMPRNAVVEEAFRRLPREEREDMDFRLARATLLSANKTILSKEEWTKQEEDVPYLDPYIKLIERELRNKADWDNFISPRTYP", "text": "FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the UQCRB/QCR7 family."}
{"protein": "MKCKRLNEVIELLQPAWQKEPDLNLLQFLQKLAKESGFDGELADLTDDILIYHLKMRDSAKDAVIPGLQKDYEEDFKTALLRARGVIKE", "text": "SIMILARITY: To H.influenzae HI_0845."}
{"protein": "MSDNITRHKSQRWVSASKANYDGADWDAYSSNSEDEGLTNNIPQLPQVNIPESNNIAKSSSPDPSIGTCLRSDSLNTSVRSGNKSVNDDLDSLMHQISQEMTAKDEDVNNTSDPEDEDDAELKVSKTGYFAAYVNDEDTDDRESVKSDIESAKLAESATEINKTDNAKAESVSEVESVAESVKRAKVEVEPVQIVNVGEESFKGDDSEAESVKRADVEVEPFKIVSAEEEPLKGDDTEVELFKNAASEVETSQISVELQDEMIDPTTEIPSRIQGDVAISDDKGSKDAVDEDNWSKSDSHPESIGSQDKEEMPPSSINSLPSESQLSIQHSKEGDSNDSDSLLNGYGSEPSLMKDNASPVKLRKTSKTDLSYHDGYSSESSGEEKERAISEVSLGQYVVHSAESFKFRNPVRNSVLDSSDDDIDYTDEDGDLEVTKSGYFAAMVDEDKEIDDSDRHTLNNNDTDGLTADSDVNSITESVTKRLSQSSITQSDVPDQNSENDVGGYSDSSEDEEDGPQKLAFSTRESINLGKWKPDTDAFRSGFVTETIDINNPPEGYTVNEDGEIVEVNKNTTSNIQRNSSVASDGESQFNAFPHDVASDDDDLKTIADTKTIYDNQTIYNVPALIANNASAPALPTNIQITNESTDYVSSNDTIFKHVNGEAPKGESKLKEAFSSEGDEIPSVVHQSTVPNLDLVKLLSSNELHSQKLKKLNNYKEQLKEYDSGLQSWIQYALKSSTTSDKDFIFKDYKVNKHVQDAYAQADILSKKNSVANTVNQNVTHLKKKMFSSSMREKSKGLFSSIGKKL", "text": "FUNCTION: Involved in the resistance to unfolded protein response (UPR)-inducing agents. SIMILARITY: Belongs to the FYV8 family."}
{"protein": "MGLSLVLSCGVIAGISGFLFGYDSGIMTTTIAQEQFLQQFKPKESMVGTIVAIMQAGGFFGCLTAGKLSDLWGRRKAIMFGCVFVVVGGALQAAAYHTAMLLIGRLVTGFGVGSLTMTVPVYQAEISPPRWRGTIVGCQQLMLAIGSAIANWTGYGCSFVNSSFQWRMPLALQAVPGIVLFFGSYFLPESPRWLVEHDALDAALHVVQRLYPDKQNLDSAYAEFQEIVEQIKQEKAQASERSYLQIFRRKAWRKRLFLGAGIWLMLNLTGINVINYYLTQFFTSLGYKGRRAIFLSGVYGSVGAATTFLALFFVHRLSRKTPLMMANISQTATLIVMAGLTAASELGKSGQMGGVAMIFLFFVIYCSTWGPLSWVYASEIFPTQIRSKGYSMASAVNCEWRFYFLFVATNFISALVLLFLYPETSGKSLEAIDLLFDDHQTIHRSTLEENEVRRTSESVNAKH", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of echinulin family alkaloid. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MESGPAVCCQDPRAELVDRVAAINVAHLEEADEGPEPARNGVDPPPRARAASVIPGSASRPTPVRPSLSARKFSLQERPAGSCLGAQVGPYSTGPASHISPRSWRRPTIESHRVAISDTEDCVQLNQYKLQSEIGKGAYGVVRLAYNESEDRHYAMKVLSKKKLLKQYGFPRRPPPRGSQATQGGPAKQLLPLERVYQEIAILKKLDHVNVVKLIEVLDDPAEDNLYLVFDLLRKGPVMEVPCDKPFPEEQARLYLRDIILGLEYLHCQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDAQLSSTAGTPAFMAPEAISDSGQSFSGKALDVWATGVTLYCFVYGKCPFIDDYILTLHRKIKNEAVVFPEEPEVSEDLKDLILRMLDKNPETRIGVSDIKLHPWVTKHGEEPLPSEEEHCSVVEVTEEEVKNSVRLIPSWTTVILVKSMLRKRSFGNPFEPQARREERSMSAPGSLLMKEGCGEGCKSPELPGVQEDEAAS", "text": "FUNCTION: Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2- antagonist of cell death. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MEPAGPAPGRLGPLLLCLLLSASCFCTGATGKELKVTQPEKSVSVAAGDSTVLNCTLTSLLPVGPIRWYRGVGPSRLLIYSFAGEYVPRIRNVSDTTKRNNMDFSIRISNVTPADAGIYYCVKFQKGSSEPDTEIQSGGGTEVYVLAKPSPPEVSGPADRGIPDQKVNFTCKSHGFSPRNITLKWFKDGQELHPLETTVNPSGKNVSYNISSTVRVVLNSMDVNSKVICEVAHITLDRSPLRGIANLSNFIRVSPTVKVTQQSPTSMNQVNLTCRAERFYPEDLQLIWLENGNVSRNDTPKNLTKNTDGTYNYTSLFLVNSSAHREDVVFTCQVKHDQQPAITRNHTVLGFAHSSDQGSMQTFPDNNATHNWNVFIGVGVACALLVVLLMAALYLLRIKQKKAKGSTSSTRLHEPEKNAREITQVQSLIQDTNDINDITYADLNLPKEKKPAPRAPEPNNHTEYASIETGKVPRPEDTLTYADLDMVHLSRAQPAPKPEPSFSEYASVQVQRK", "text": "FUNCTION: Immunoglobulin-like cell surface receptor for CD47 (PubMed:18045614). Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells (By similarity). Plays a role in antiviral immunity and limits new world arenavirus infection by decreasing virus internalization (PubMed:30726215). Receptor for THBS1 (By similarity). Interaction with THBS1 stimulates phosphorylation of SIRPA (By similarity). In response to THBS1, involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "DPATCEKEAQFVKQELIGQPYTDAVANALQSNPIRVLHPGDMITMEYIASRLNIQVNENNEIISAHCA", "text": "FUNCTION: Elastase inhibitor. Inhibitor of A.flavus elastase with a Ki of 40 nM. Inhibitor of A.fumigatus elastase and human leukocyte elastase. Inhibits the fibrinogenase and collagenase activities of A.flavus elastase. Does not inhibit porcine pancreatic elastase, trypsin, chymotrypsin, thrombin or A.acutus AC1-proteinase. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MRGARLMGALLALAGLLQGALALRMAAFNIRTFGETKMSNATLSKYIVQILSRYDVAVVQEVRDSHLTAVGKLLDTLNQDDPNAYHYVVSEPLGRSSYKERYLFLFRPDRVSVLDSYQYDDGCEPCGNDTFSREPAIVRFHSPLTEVKEFAVVPLHAAPLDAVAEIDALYDVYLDVQHKWDLEDIVLMGDFNAGCSYVAASQWSSIRLRTNPAFQWLIPDTADTTSTSTHCAYDRIVVAGSQLQHAVVPESAAPFNFQVAYGLSSQLAQAISDHYPVEVTLKRA", "text": "FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:14688237). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:14688237). Binds specifically to G- actin and blocks actin polymerization (PubMed:14688237). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). SUBCELLULAR LOCATION: Secreted Zymogen granule Nucleus envelope Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. SIMILARITY: Belongs to the DNase I family."}
{"protein": "MAHGRNIRKRTFSDMDTLSDKNIGIHTNSLPKNLLCRRILFKGKISKYSIFNDSLAKDHSSNRSMSIDGLIGKKRPHDISFQNMNSSMPSSTQKKTRILDEEIKDQSSSNENDRDSPVIVTLKPSYMPKTSRITEIIHKMKELNMNRIEDGLSFNKKRSEHDAKNVLLHTMEMEEDCEIEEDIAIDSPYLNTSLSEDDTESIVETDYSEEEKESISETESSSDDESYSLYDSF", "text": "SIMILARITY: Belongs to the asfivirus DP238L family."}
{"protein": "MLFRSALLSNVLLLPACAHDVLFSRDLPLPIAANAESYTDCANAAWPPSNVGVELVPQPPDDELRAMVDEMSAENIEATITKLVSFGTRHTLSTFNSSTRGINAARDWIASEMRKYAAESNGTMTVEVQSYVQGVASRIPFPVTISNVLAKATGSEDPSRVYVMTGHYDSRVTDVLNYESDAPGANDDASGTAIAMELARVLAKHQPKSTIILGAVSGEEQGLYGSTYLAQTLKNTSTNVEGMLNCDIVGSSTGDRGQKDPFTIRAFAQGPPPLSAESSAKAAQRLQIGGENDSPARELARFSAEVAANNATGMKVAIIYRLDRFLRGGDHTGFLQAGYPAIRYTEPNENFAHQHQDIRTENGTVYGDLIEFVDFDFTARVGKVNLATLWSLAQAPAMPRNVTIDATILDNESRIKWIISNSTDVASYEVVWRSTIASLWTHMLDVGKVGYVVLPLSKDNVIFGIRAVGKNGYKSPAVYPFPG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily."}
{"protein": "MPQAPKSLSIDSDAAVVAAAAADDLVRASSPRPRTTTFTPSRPTVLLTKSWTSATVLPSTTSTRITVGANTSTATDAASSISQHEPSTSSNSTRASTPLPELSPSPFSPQTAVAEALTREQQPAGPSDDSQSRSILPHASDHSTPCNSDQATEVAFHDAADVEPEAVGTTVSSSIHALDLLHRVNDRAAAERASNSESLRSHLSRLSVSRASSKHRSRSNSRDASTQTRALPPAFLGTKQAAPSAASAVTQTSLRDEAKDGDRQLYDTSSAPSHEEEQYPDRKYYILSSAGKPIYISHASLSRRKRRREKRRRQRRAESNESDLNSNESDEEDESSTTQVGVMQALISIFADEDSDKLRFIRRGDLLITFLLRAPLYLVCVSSWNEEPSTLRQHLEYLYLQVISLVSASQLTRLFGRMPNFDLRRLLEGTEGIFDYLVNQLNANETEDDDAEQGQHQVATGGVEAKRAVTDWASCHQWWLQALQPIRITVPNLRDQLTAALQPPTAEAGSSTQPHRPKDLLYVLLCANGRIVTLLRPRKHSVHPIDLLLLTNMVMGSRSIKRSGGSEDAEIWLPLSMPKFAPHGFVHAYVKFLDPESWIGSRREGSEMVGDAKMTSSELAVIVVTGDKDAFPTVSAWISSLVAQPPAHWADNTADDAGDAGDAGSIRTTDIMAKRAASKKQAGKSAKPTQTELASWMTHFQRHILTLCRHLTDASNIEQGSPRVSAYTCAELGLAGLRHFVYRSNSTIQLTSPSLPDPYASDAVHRKRLLTLYSLVHHQIHHPLPASASHSESSSSSTTAPPTGMLNGVFGTPASSHPRLSADTRLKMHLVKSHHEQILGWITSPFELYLCLNPQLSKSAIVAVANSLTKWIKSNENDLFLVNAGSF", "text": "FUNCTION: Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. SUBCELLULAR LOCATION: Endosome, multivesicular body membrane; Peripheral membrane protein Prevacuolar compartment membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein. SIMILARITY: Belongs to the MON1/SAND family."}
{"protein": "MANSLDRLREHLKNGDKLVLKNNEGQSTDDITKATMVETLSSDGSTQDSFPLNEETEIEIDGSLVQLRIIVHCWMNKDSSAADYLADCQNKQLTNVSFLQRTDLINWLSGNTESSQYLKAPGQKGETSDKVDIENKTLAGELSTVKSTTSASLENDSEVSDPVVVETMKHERILVDHNSALRGAKPINFGYLIKDAELKLVQSIKGSLRGSKLPPGHKGAHGRISKTNGSSGGPRKDPIILIPSAASSILTVANIKQFLLESKYVNPRNLPSVPNGLVNIEKNFERISRPIRFIIVDNTRMFTKPEYWDRVVAIFTTGHTWQFNNYQWNSPQELFQRCKGYYFHFAGDSVPQHVQQWNVEKVELDKNKRFKDVEVVRYFWHSLEKELISRGYR", "text": "FUNCTION: The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the CDC73 family."}
{"protein": "MKLATEKKTTRQKLSIAGMLITMGVVYGDIGTSPLYVMKSIVEGNGGIRNISQDFVVGSISLVFWTLMLMTTVKYVLIALRADNNGEGGIFALYTLIRKQAKWLVIPAIIGGATLLADGMLTPAVTVTTAIEGLKGLPINGNVLVSNQREVIILTVTILSVLFFIQKFGTDLIGKSFGPIMLIWFTFIGAIGVMNLMGDLTMLKALNPYYAIHLLFSPENKVGILILGSVFLATTGAEALYSDMGHVGRHNIYGSWPYIAACLVLNYFGQGVWLLQHKEVAAYQNMTDFNPFFEAMPAQLKIPAILLATVAAIIASQALISGSYTLVSEAIKLRLLPRIKVDYPAKLKGQLYISIVNWILWAVCLAVVFYFKNSAHMEAAYGLAITITMLMTTILLFHYLGRREKRWFLAYVVLLFFGAIETIFFIASAAKFMHGGYVTVLIAFVILFIMFVWYRSNSIKESNTFKSSTVSLLAYKRQLHDLRNETSLPLYTTNLVYLSKPQAEPRGKNMVKKNILYSILDKRPKRAQVYWFVAVNVTDEPYTAEYTVDTLGTDYIVSVQLYLGFKMEQKVNIFIRQIIHEMIHNGELPAQPQHYTTIPNREVGDFSFVIIQEDLSPETQIRAMDKVIVQIRLWLEKFTDTPASWFGLEYSDVFVERIPLVLGRQKAINKYHLKRRQEES", "text": "FUNCTION: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family."}
{"protein": "MPKKNSPLLPKETTTTQSSVDTSGSSNLTWPVSEHTIRRPLWARLLGQILDPWLDLSIEPEHSVQYNDGRPIIYVLEDYGLCNTLILDKACRKTKLPSPLIPLSGNPLQRKRAYLALSRRSSSNSLIPNQRGGKTHSDSLANLLQAHRIRDTLDVHLVPVSIFIGRTPDRQSGWFAVLFSENWALVGRFRRILAILLNGRNTIVCFAPPISVRQTLNEGLPPERTLRKLQRVLRTHFRRIRETVIGPDLSTRRLLVDNVLATEAVREAIGAQAKRDGTDLSETWRKAQAYAWEIAADYSSPVIRSADFLFSHVWNRIYAGVLVHHVDSFKEISPGHEIVYVPSHRSHMDYLLLSYCLYKCSIGLPHIVAGINLNLPVVGTLLRKCGAFFIRRSIKGNMLYSVVLSEYVAQLVAGGYSLEYFIEGGRSRTGRLLQPKGGMIMMTVQAFLRQPRRPVLFQPIYIGYEKLMEGTSYLDELSGEPKKKESIWRVFWNIPKVLKQKYGQVVVNFGEPIALNDVLAELAPEWEGQALNENEKPAWLSSTVNHLARQIQTRINSAADVNPINLLALALLSTPKHAMGEADLIAQITLCKKILLELPYSNRVTITPHTPERIIAHAEQINILTRVHHPLGDVLRVDGDNAVLLSYFRNNVLHLFTASAWVACCFKNNRRMSRIALIRLGVGMYPFLQAELFLPWTEDQFAQHIQQVIELFVREGLLLSAGNEEEDPLTRNTSQTDEVFRLRAISHSLQQAFERYYITISILVKNGPGTLSASELESLCQLAAQRLSLLYASTAPEFFDKGLFRGFIQKLRELNLVWPDTYSKLLFDERLDTSAKDAQVILGRELRHTIERISPEATKPAPK", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family."}
{"protein": "MSHLWCWLFLVLCLACLVLSIEAKDSDGDGLLDVDEINVYFTDPYNADSDQDGLTDGLEVNRHQTHPQDKDTDDDSIGDGVEVNNLGTNPKDPDSDDDGLTDGAEVNLYRTDPLDADSTTTGCPMGGGAEVRHRPQNGDTDDDGLTDGAEVNVHRTNPQDGDSDDDGLSDGAEVNTYHSNPKDGDSDDDGVSDGAEVNPKLKDSDGDGLTDEEEIKLYRTDPFCADSDFDGLLDGEEVKVHKTNPLDGDSDDDGLGDGAEVTHFNTNPLDADSDNDGLDDGEEINVHGTDPEDPDSDNDGLNDGDEVNVYNTDPEEDDSDEDGVCDGAEVNVHHTNPKDEDSDNDGIPDGAEINTHKTDPNDEDSDDDGIADGAEVTLTDSDGDGLPDEDEVALYNTNPANADSDYDGLTDGAEVKRYQSNPLDKDTDDDGLGDGVEVTVGTDPHDATVTTTGSRTAVEINVHGSDPNDEDTDDDGLTDGAEVNLHRTDPEDADTDDDGLTDGAEVNTYRTNPKLADSDGDGLSDGAEVNTHKSDPNDGDSDDDGVPDAAEAKVKDSDGDGLSDTDEVRFRTNPKLADTDFDGLTDGAEILKHKTDPRNRDTDGDGVADGLEVNTYGSDPKDADTDDDGLTDGAEINVHDTNPTDADSDDDGLSDGAEVMTYHTNAKDGDSDDDGKADGAEVSASTDPWRSDHSV", "text": "FUNCTION: May function as a calcium-binding protein. SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum."}
{"protein": "MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNERAKASAESCSC", "text": "FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo- lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (By similarity). Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transporter-mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism (By similarity). Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes (By similarity). Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacteria (By similarity). Plays a role in the fusion of phagosomes with lysosomes (By similarity). Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses (By similarity). Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium) (By similarity). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts (PubMed:16040606). Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (PubMed:16306406). Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation (By similarity). Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway. Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). Required for vesicular trafficking and cell surface expression of ACE2 (By similarity). May play a role in PRPH neuronal intermediate filament assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane; Peripheral membrane protein; Cytoplasmic side Late endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Melanosome membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein; Cytoplasmic side Lipid droplet Endosome membrane Cytoplasmic vesicle Mitochondrion membrane; Peripheral membrane protein Note=Colocalizes with OSBPL1A at the late endosome. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts. Recruited to phagosomes containing S.aureus or Mycobacterium. Lipid droplet localization is increased upon ADRB2 stimulation. Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MSDLESSSSSSSDEEELERCREAALPAWGLEQRPRGPEKPGVDATNAKLPANQPSLMHKVDEHEQDGNELQTTPEFRAHVAKKLGALLDSSITISEIVKEPRKSEVQQGALEDDGFRLFFTSIPGGPEKEAAPQPCRKRLPSSSSSDDGDEELRRCREAAVSASDILQESAIHGHVSVEKKKKRKLKKKAKKEDSADVAATATSKAEVGRQEKESAQLNGDQAPPGTKKKKRKKKTKKASEASLSPPTKSAAAVPSN", "text": "FUNCTION: Plays a role in the regulation of Wnt signaling pathway during early development. SUBCELLULAR LOCATION: Nucleus envelope. SIMILARITY: Belongs to the CUSTOS family."}
{"protein": "MSTPSIHCLKPSPLHLPSGIPGSPGRQRRHTLPANEFRCLTPKDAAGVFEIEREAFISVSGNCPLNLDEVRHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLTLHRPGGRTAHLHALAVHHSFRQQGKGSVLLWRYLQHAGGQPAVRRAVLMCEDALVPFYQRFGFHPAGPCAVVVGSLTFTEMHCSLRGHAALRRNSDR", "text": "FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N- acetylserotonin, the penultimate step in the synthesis of melatonin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily."}
{"protein": "MAQETNHSQVPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQNSSNGRISPPATSVSSLSESLPVQCTDGSVPEAQSTLDSTSSSMQPSPVSNQSLLSESVASSQLDSTSVDKAVPETEDLQASVSDTAQQPSEEQSKSLEKPKQKKNRCFMCRKKVGLTGFECRCGNVYCGVHRYSDVHNCSYNYKADAAEKIRKENPVVVGEKIQKI", "text": "FUNCTION: Involved in regulation of TNF-alpha induced NF-kappa-B activation and apoptosis. Involved in modulation of 'Lys-48'-linked polyubiquitination status of TRAF2 and decreases association of TRAF2 with RIPK1. Required for PTS1 target sequence-dependent protein import into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro involved in PEX5 export from the cytosol to peroxisomes (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGHKYDVYGMGNALVDMEFEVTPEQLASLGIDKGVMTLVEEARENELIAQLAQQRGKQSSGGSAANTLVSLAQLGGTGFYACKVGKDEAGAFYLQDLNDCGLDTNPHHETAGEGITGKCLVFVTPDADRTMNAFLGISGSLSVTEMDWSALKQSQYLYLEGYLVTSPSAKAACIEAKAIAEQSGVKTCLSLSDPNMAKFFQDGLKEMLGSGVDLLFANEAEALEMAGTSDLNQAIAYCKSIAKNFALTRGGAGSLIFDGENLLTIGTPKVQPIDTVGAGDMYAGGFLYGLTHGMDYEKAGQLASETAAKVVTCYGPRLDTEILQEILQSVQAV", "text": "SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
{"protein": "MEAGAMGGSSFLSFSSGPSAETSPSSLSPPTSSSPSPSPQLVSDSVESLHAKRPLAQSSRSSSRTAASTCFCWQGEGQENEAAPTISQEERRGGSMTAASAGHLETAREEAARCLGCSYTGEERRGASSATSVLSLGGERGRPPSRSSSLWTFSGLLSPLAFRSRRCCPQFSSSSSPLSPLPHPRGAPASACGSAVITDRAGRPASPLSFSRLASPVSDPSGVCPPRVVAARVWRLLSSVLFSLVNCARLFPRRLSRRPDPLRKPRAQVWSASSRSLQALLLATVALFAACSSLHGSSLLGAQAASPTPPFLSLSSSPRSLASDSAKKGSNAPEQSREQRGEREGERQRPDKGEENGETEETFPAASGVVPAPGLKVADLPRTGPPVDLLGLPIRKKVFRARLYGSMFSYAYYFLDILVGTPPQRASVILDTGSSLLAFPCAGCSECGQHLDPAMDTSRSATGEWIDCKEQERCFGSCSGGTPLGGLGGGGVSSMRRCMYTQTYSEGSAIRGIYFSDVVALGEVEQKNPPVRYDFVGCHTQETNLFVTQKAAGIFGISFPKGHRQPTLLDVMFGHTNLVDKKMFSVCISEDGGLLTVGGYEPTLLVAPPESESTPATEALRPVAGESASRRISEKTSPHHAALLTWTSIISHSTYRVPLSGMEVEGLVLGSGVDDFGNTMVDSGTDLSSIFPPIKVSFGDEKNSQVWWWPEGYLYRRTGGYFCDGLDDNKVSASVLGLSFFKNKQVLFDREQDRVGFAAAKCPSFFLDQRPRGPDSGDGPKGRPTAPFTVPPLRVPVPMDGGGVPGDAKQPEGLPLSPQQLWVAAALVVVAILIAVTVILLHTIKRPSRSSAVVPAPSAPRLPFAQNSKSAGRFARGLGHGALGVGNPVYVQRTQRYREVQEAQPHTADAYYDVEEDRFTGEDDGDFFGDDSVPSAEEQETAPSLSLREESSPFSASQSTLLDLPLGGE", "text": "FUNCTION: In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence (PubMed:26576949, PubMed:26473595, PubMed:26270241, PubMed:30377279). However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24 (PubMed:26576949, PubMed:26473595, PubMed:26270241). Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu (PubMed:26576949). Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus (PubMed:26576949, PubMed:26473595, PubMed:26270241). Cleaves GRA19 and GRA20 (PubMed:26473595). Cleaves MYR1 (PubMed:26576949). Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2 (PubMed:30377279). By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response (PubMed:26576949, PubMed:26473595). At the bradyzoite stage, also involved in the formation of the cyst wall (PubMed:26473595). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MITPAFELSQDADFLIVVIRVPYTRTSDFDIYIQEEEFKFYAKPYFLRLTLPGRIVEDGREKASFDIDKGLFTLHVPKETAGQHFEGLEMLTSLLAPKGSRSAKPLVEDSEACGEGCEEEDEEFDWQIEQEVYTEAPADTLKEYHKYGFGNLRSGVFSRLQEELNEVIDMKDPDNTNAELRRRNRLDTETAVFCADHYLVNLYEDKEEIRNLLKFKPWWRKLNPDPSAGYDISMTFTEEEREQMRRFTNRSYLLDKKARFHVWLGLVDIILAYVYDVRTTEGEHNVESAWTIRKLSGTLSWLETYHSVQDVLVSFGRRTYCYPLYRHFSLVTLAVKDAACIFQAGKACILKCLLAIHKIFRENDPAYILNDLYITDYCIWIQRVKSKHVLALAEPLNNAKLQKNHLELELEIIEQAAELAVKEEEEKDTESDTDDSSSSSGDSDDEDDSDEECPEKAAEKKQTAFKAHAEAVTEAFCVELQRGDGRLIEELGKRLEEELTIEEDVPQERRSASEGEGERRREHYHPHAAESERDTTKAATGKELLDVCLQRKPLRILNTEELDSDDDDDDDDDGDLRITVVDERG", "text": "FUNCTION: Required for the quantitative accumulation of H/ACA ribonucleoproteins (RNPs). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus, nucleoplasm. SIMILARITY: Belongs to the SHQ1 family."}
{"protein": "MKVLWAALLVALLAGCWADVEPEPQLERELEPEAPWQASQPWEQALGRFRDYLRWVQTLSDQVQEEVLNTQVTQELTVLMEETMKEVKAYREELEEQLGPMASETQARVAKELQAAQARLGSDMEDVRNRLAQYRSEVQAMLGQSAEELRARLASHLRKLRKRLLRDAEDLHKRLAVYRAGVREGAERSVSSIRERFWPLVEQARARNANVAAVAAQPLRERAEALGQQLRGRLDEVREQVEEMRVKMEEQADQMRQQAEAFQARLKSWFEPLVQDMQRQWAGLVEKLQAAVGTSPTTAPVEKQ", "text": "FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE- containing lipoproteins by cells. SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Secreted, extracellular space, extracellular matrix Extracellular vesicle Endosome, multivesicular body Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans- dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. SIMILARITY: Belongs to the apolipoprotein A1/A4/E family."}
{"protein": "MNSGVAMKYGNDSSAELSELHSAALASLKGDIVELNKRLQQTERERDLLEKKLAKAQCEQSHLMREHEDVQERTTLRYEERITELHSVIAELNKKIDRLQGTTIREEDEYSELRSELSQSQHEVNEDSRSMDQDQTSVSIPENQSTMVTADMDNCSDLNSELQRVLTGLENVVCGRKKSSCSLSVAEVDKHIEQLTTASEHCDLAIKTVEEIEGVLGRDLYPNLAEERSRWEKELAGLREENESLTAMLCSKEEELNRTKATMNAIREERDRLRRRVRELQTRLQSVQATGPSSPGRLTSTNRPINPSTGELSTSSSSNDIPIAKIAERVKLSKTRSESSSSDRPVLGSEISSIGVSSSVAEHLAHSLQDCSNIQEIFQTLYSHGSAISESKIREFEVETERLNSRIEHLKSQNDLLTITLEECKSNAERMSMLVGKYESNATALRLALQYSEQCIEAYELLLALAESEQSLILGQFRAAGVGSSPGDQSGDENITQMLKRAHDCRKTAENAAKALLMKLDGSCGGAFAVAGCSVQPWESLSSNSHTSTTSSTASSCDTEFTKEDEQRLKDYIQQLKNDRAAVKLTMLELESIHIDPLSYDVKPRGDSQRLDLENAVLMQELMAMKEEMAELKAQLYLLEKEKKALELKLSTREAQEQAYLVHIEHLKSEVEEQKEQRMRSLSSTSSGSKDKPGKECADAASPALSLAELRTTCSENELAAEFTNAIRREKKLKARVQELVSALERLTKSSEIRHQQSAEFVNDLKRANSNLVAAYEKAKKKHQNKLKKLESQMMAMVERHETQVRMLKQRIALLEEENSRPHTNETSL", "text": "FUNCTION: Candidate for the putative colorectal tumor suppressor gene located at 5q21. Suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells. Inhibits DNA binding of b- catenin/TCF/LEF transcription factors. Involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2- dependent manner by sequestering CCAR2 to the cytoplasm, thereby impairing its ability to inhibit SIRT1 which is involved in the deacetylation and negative regulation of beta-catenin (CTNB1) transcriptional activity (PubMed:24824780). SUBCELLULAR LOCATION: Cell membrane. Cell projection, lamellipodium. Nucleus Cytoplasm Note=Colocalizes with actin at the leading edge of polarized cells. SIMILARITY: Belongs to the MCC family."}
{"protein": "MDSSPPNTIIEEAPPRFSELKPPLSEDIIEALDRSGFEVCTPVQAETIPFLCSHKDVVVDAATGSGKTLAFLLPFIEIIRRSNSYPPKPHQVMGVIISPTRELSAQIHKVARAVRLDFAKCREVEADMNTLEEEGANLLIGTPGRLSDMMKRMEFLDFRNLEILILDEADRLLDMGFQKQVNYIISRLPKQRRTGLFSATQTQAVADLAKAGLRNPYLKCEADQKSSQLVHLLIENKNKKLVVFFMTCACVDYWGLVISKIPSLKSISFFPTHGKMDQKGRDTALASFTEASSGVLLCTDVAARGLDIPGIVYIRSLAIKDREVLEKGLKAFVSFVRAYKEHQCSYIFSWKGLEIGKLAMGYGILSFPYISEVKQDRIGIVGFTPVQGITFEDIKFKNKSREKQRQQNLLARKDKLQQEKRGKRKKSSKEAVDDSNKASRKRKLTGRQRQTIQTAQDEEEMNLRL", "text": "SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4 subfamily."}
{"protein": "MWKIHNKLLIYILWIMEIRLVSSFTSVMLCGRIPGLTPGQRNMCREMPDALIALGEGHQLGAQECQHQFRGHRWNCSEVWQRNVFAHVIPTASREAAYTYAIASAGAAYAVTAACARGNISTCGCDVRHKATPTGGGTPDEPWKWGGCSADVDFGMRYARRFMDARELERDSRTLMNLHNNRAGRTLVKKMLRTDCKCHGVSGSCVMKTCWKSLPPFRLVGDRLMLKYQKAKTVQAVKGKRGLRLVLSRKKHAGTARAQKPVLDWPKRMELIYLEASPNYCERSLQTGSQGTSGRTCQRTGHGPQSCDLLCCGRGHNTQHIRRTTQCRCQFRWCCEVKCDECDESYEEFTCK", "text": "FUNCTION: Binds as a ligand to a family of frizzled seven-transmembrane receptors and acts through a cascade of genes on the nucleus. Segment polarity protein. May function in gonadogenesis and limb development. Wg and Wnt2 have a role in the developing trachea and together are responsible for all dorsal trunk formation. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family."}
{"protein": "MTLSRAKHANRNHLPHLLAKVPEEHQEPIKNMCLKMMSHDAYGQPYDWSPRDFEMGAHLGRGKFGRVYLARERHSHYLVAMKVMFKEELRKGCVQRQVLREIEIQSRLKHPHILRLLTWFHDESRIYLALEIASEGELFKHLRGAPNHRFDEPRSAKYTYQVANALNYCHLNNVIHRDLKPENILLTSTDDLKLADFGWSAHTPNNKRRTLCGTLDYLPPEMVDGNSYDDSVDQWCLGILCYEFVVGCPPFESNSTESTYSKIRRMEISYPSHLSKGCKELIGGLLRKESKGRITLVDVMTHYWVKAGMAERELQLQKRERGKENTARN", "text": "FUNCTION: Serine/threonine-protein kinase which mediates both meiotic and mitotic chromosome segregation. Required for histone H3 'Ser-10' phosphorylation. Phosphorylates mei-S332 within residues 124-126 and stabilizes its association with centromeres during meiosis. SUBCELLULAR LOCATION: Chromosome. Cytoplasm, cytoskeleton. Midbody. Note=Meiotic and mitotic chromosomes. During each division, relocates to the midbody microtubules. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily."}
{"protein": "MSVNEDLSHLGVFSVDQENLERDVTNTASEYIAHESREIEKKRLQKVRKEISSVKEKIRRLDERIDSRLTKISVKENFRKQLSKFRDTLQSLQSDENDIKRRLNNEDSANAPGIGAFSTEELERQELIRTGKVTPFRNLSGLQKEVDFDDESSIREAVIKSEGTYYETAPHLSSEPSNIDHGIIPRDEKDEYVTVDAVTEKVVTAAIDDGDDLVYRQRLNAWCANRKELRDQASASENNKDRGEFEGKDEWLLPHPSKKGQTFEGGFTIPGDIRPHLFRYQVTCVQWLWELYCQEAGGIIGDEMGLGKTIQIVSFLSSLHHSGKFQKPALIVCPATLMKQWVNEFHTWWAPLRVVVLHATGSGQRASREKRQYESDASESEAEESKTSIKLRGASSSFHRYAKNLVESVFTRGHILITTYAGLRIYGDLILPREWGYCVLDEGHKIRNPDSEISISCKQIRTVNRIILSGTPIQNNLTELWNLFDFVFPGRLGTLPVFQNQFALPINIGGYANASNVQVQTAYKCACMLRDLISPYLLRRMKLDVAADLPKKSEQVLFCKLTPLQRKAYQDFLQGSDMQKILNGKRQMLYGIDILRKICNHPDLVTREYLLHKEDYNYGDPEKSGKLKVIRALLTLWKKQGHRTLLFSQTRQMLDILEIGLKDLPDVHYCRMDGSTSIALRQDLVDNFNKNEYFDVFLLTTRVGGLGVNLTGADRVILFDPDWNPSTDAQARERAWRLGQKKDVVVYRLMTAGTIEEKIYHRQIFKQFLTNKILKDPKQRRFFKMTDLHDLFTLGDNKTEGTETGSMFLGSERVLRKDNSSRNGNEAEDIPARDRKKHKIHDKGKKVNSSKVFEKMGIASMEKYKPPQESNVTKTNSDSTLGDDSVLDDIFASAGIQSTLKHDDIMEASQTESILVEKEATRVANEALRAVSSFRRPPRQLIPPQQSTNVPGTSKPSGPITSSTLLARLKQRR", "text": "FUNCTION: Involved in transcription-coupled repair (TCR). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MEFFISMSETIKYNDDDHKTVFLKTLNEQRLEGEFCDIAIVVEDVKFRAHRCVLAACSTYFKKLFKKLEVDSSSVIEIDFLRSDIFEEVLNYMYTAKISVKKEDVNLMMSSGQILGIRFLDKLCSQKRDVSSPEENTQSKSKYCLKINRPIGEPNDTQDDEVEEIGDHDDSPSDVTVEGTPPSQEDGKSPTTTLRVQEAILKELGSEEVRKVNCYGQEVESMETTESKDLGSQTPQALTFNDGISEVKDEQTPGWTTAAGDMKFEYLLYGHREHIVCQACGKTFSDEARLRKHEKLHTADRPFVCEMCTKGFTTQAHLKEHLKIHTGYKPYSCEVCGKSFIRAPDLKKHERVHSNERPFACHMCDKAFKHKSHLKDHERRHRGEKPFVCGSCTKAFAKASDLKRHENNMHSERKQVTTANSIQSETEQLQAAAMAREAEQQLETIACS", "text": "FUNCTION: Transcriptional activator of the dopamine transporter (DAT), binding it's promoter at the consensus sequence 5'-CCTGCACAGTTCACGGA- 3'. Binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions and acts as a repressor of the FMR1 gene. Transcriptional repressor of MYC and thymidine kinase promoters (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MEWPWSAIAASSSSSSSCFFASPNSCLSITRRTNLSCVNTSVKSLRHSRFDSKHNLVKRRINGDSVVRRSTTSNNSTEETESSSSSSSVDCVGMGSDVECVNNGEDEENRSSGILSGGEGTFLEWTVLISPFFFWGTAMVAMKEVLPITGPFFVAAFRLIPAGLLLVAFAVYKGRPLPEGINAWFSIALFALVDATCFQGFLAQGLQRTSAGLGSVIIDSQPLTVAVLASFLFGESIGIVRAGGLLLGVAGLLLLEVPSVTSDGNNFSLWGSGEWWMLLAAQSMAIGTVMVRWVSKYSDPIMATGWHMVIGGLPLLAISVINHDPVFNGSLQDLSTNDVIALLYTSIFGSAVSYGVYFYSATKGSLTKLSSLTFLTPMFASIFGYLYLNETFSSLQLVGAAVTLVAIYLVNFPEGND", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Plant drug/metabolite exporter (P-DME) (TC 2.A.7.4) family."}
{"protein": "MEEQPECREEKRGSLHVWKSELVEVEDDVYLRHSSSLTYRL", "text": "FUNCTION: Precursor of the histocomplatibility antigen HB-1. More generally, minor histocomplatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocomplatibility antigen in HLA-matched sibling marrow transplants. HB-1 is presented on the cell surface by MHC class I HLA-B44. This complex specifically elicits donor-cytotoxic T lymphocyte (CTL) reactivity in B-cell acute lymphoblastic leukemia (B- ALL) after treatment by HLA-identical allogenic bone marrow transplantation (BMT). It induces cell recognition and lysis by CTL. However, HB-1 restricted expression in B-ALL cells and not in normal tissues may allow a specific CTL reactivity against B-ALL without the risk of evoking graft-versus-host disease."}
{"protein": "ADPDPLQDFXVADLXDNAVXV", "text": "FUNCTION: May subsume the role of germin at the low water potentials during embryogenesis. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. Secreted, cell wall. Note=Component of the walls of the mature, ungerminated embryos. SIMILARITY: Belongs to the germin family."}
{"protein": "MSALSRWLLIPPVSARLSERYQGYRRHGASPFSAALGCLWTILAWIVFPLEHPRWQRIRDGHKALYPHINAARPRPLDPARYLIQTLWLVMISSTKERHEPRWRSFARLKDVRGRYHQWMDTLPERVRQKTTHLEKEKELGHLSNGARRFILGVIVTFSLILALICITQPFNPLSQFIFLLLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVSLVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKEMSQWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIWILDDGGRESFRQFARHVGVHYIARATHEHAKAGNINNALKHAKGEFVAIFDCDHVPTRSFLQMTMGWFLKEKQLAMMQTPHHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQSAGLATESLSAHIGQRIRWARGMVQIFRLDNPLFGKGLKLAQRLCYLNAMFHFLSGIPRLIFLTAPLAFLLLHAYIIYAPALMIALFVIPHMVHASLTNSKIQGKYRHSFWSEIYETVLAWYIAPPTLVALINPHKGKFNVTAKGGLVEEKYVDWVISRPYIFLVLLNLLGVAAGVWRYYYGPENETLTVIVSLVWVFYNLVILGGAVAVSVESKQVRRAHRVEIAMPGAIAREDGHLFSCTVHDFSDGGLGIKINGQAQVLEGQKVNLLLKRGQQEYVFPTQVVRVTGNEVGLQLMPLTTKQHIDFVQCTFARADTWALWQDSFPEDKPLESLLDILKLGFRGYRHLAEFAPPSVKVIFRSLTALIAWIVSFIPRRPERQAAIQPSDRVMAQAQQ", "text": "FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cellulose and thin aggregative fimbriae leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MGNAATKESRSSQEHSARHSRGGSTASTAAYDHYRPSDGIHASSSRALRGGRSDFALLGLGAEREPVEHRRETRQEREARKREKENAARIKERQRSMKEEHVDGGYLVTQGVYVGTEDFNKAIVRQLMIERRLAPFWRGLNDFSESWTEHQLMAAARGMPIPAPDEVPPELEYKIPSKSSAEKQPPERNLNTLMVPITSRSQSYNSDTSSINRTISPARSPGALSPTNSFLRGRAKTLASLTTSSKTPASDMAPRELQLPKDPFVNGQPIEAYLYKDASECPICFLYYPPYLNKTRCCDQPICSECFVQIKRPDPHPPEHHDPNNSETTHPDEPEGQLVSEPAACPFCVQPEFGVMYTPPPFRRGLAYAASPGVHALANSSAASSASSLVSGGANPGTRRRAVSISADSPSVITTDRVRPDWATKLAAARAQAARRSAAATALHTAAYMMNNPGGPGEPRRRGMLRRTAGQDSPGGRTAPSHVNAMAYLAERRVVTDRDNASPVDSTTNLAPPRASSRRSRIDELEEMMMMEAIRLSLAAEEERRKKEEKETRKEAKRREKEAKKAEKSAKKAGLDSQNPSNLTSSTSSANSAVQTAGGANSELDMSANKGKGVDRSEPRPGVSTEAGSSTEPPKITIKDLKGEQFSSMLEGSSKNMHLRHVSSASSSNSSLVESAFGESIGSGTPHNGSSSSLAAIHGFRSLAAMIDDTPSGDSGESMNRPGSTNEQVQGAPAVKEPSENSAPNEPDQVTLLSSSPSLEQKDTLGKEVHMSSAEVLPQSSLGTAS", "text": "FUNCTION: May negatively regulate the SNF1 kinase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIP5 family."}
{"protein": "IVYGTVTTPGKYPWMVSIHERVKDVMKQACGGAILNENWIVTAAHCFDQPIILKDYEVYVGIVSWLHKNAPTVQKFQLSKIIIHDKYVKDGFANDIALIKTATPIDIKGSKYGVNGICFPSGATDPSGEATVIGWGMIRGGGPISAELRQVTLPLVPWQKCKQIYGHPDSEFEYIQVVPSMLCAGGNGKDACQFDSGGPLFQYDKKGVATLIGTVANGADCAYAHYPGMYMKVSAFRSWMDKVMT", "text": "FUNCTION: Protease. Hydrolyzes gelatin and succinyl casein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MEISLVPLENGSAMTLRGGGEAGASCVQTPRGECGCPPTSGLNNQSKETLLRGRTTLEDANQGGRPLPPMAQELPQPRRLSAEDEEGEGDPGLGTVEEDQAPQDAGSLHHQRVLINISGLRFETQLGTLAQFPNTLLGDPAKRLHYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIFEYPESSGSARAIAIVSVLVILISIITFCLETLPEFRDERELLRHPPVPPQPPAPAPGINGSVSGALSSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAEFSRNIMNIIDVVAIFPYFITLGTELAEQQPGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNHGSHFSSIPDAFWWAVVTMTTVGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEQAALKEEQGNQRRESGLDTGGQRKVSCSKASFCKTGGSLESSDSIRRGSCPLEKCHLKAKSNVDLRRSLYALCLDTSRETDL", "text": "FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:2361015, PubMed:15618540). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:15618540). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (PubMed:15618540). Homotetrameric channels display rapid activation and slow inactivation. May play a role in regulating the secretion of insulin in normal pancreatic islets (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily."}
{"protein": "MPELYTEDFIQGCDVGELQEPGLPGVLSYVGAQERALDHRKPSTSSKKTKRVEIDQRCENRLECNGAISAHCNLRLPDSNDSPASASRVAGITDLSRNCVIKELAPQQEGNPGEVFHTVTLEQHEKHDIEEFCFREIKKKIHDFDCQWRDDERNCNKVTTAPKENLTCRRDQRDRRGIGNKSIKHQLGLSFLPHPHELQQFQAEGKIYECNHVEKSVNHGSSVSPPQIISSTIKTHVSNKYGTDFICSSLLTQEQKSCIREKPYRYIECDKALNHGSHMTVRQVSHSGEKGYKCDLCGKVFSQKSNLARHWRVHTGEKPYKCNECDRSFSRNSCLALHRRVHTGEKPYKCYECDKVFSRNSCLALHQKTHIGEKPYTCKECGKAFSVRSTLTNHQVIHSGKKPYKCNECGKVFSQTSSLATHQRIHTGEKPYKCNECGKVFSQTSSLARHWRIHTGEKPYKCNECGKVFSYNSHLASHRRVHTGEKPYKCNECGKAFSVHSNLTTHQVIHTGEKPYKCNQCGKGFSVHSSLTTHQVIHTGEKPYKCNECGKSFSVRPNLTRHQIIHTGKKPYKCSDCGKSFSVRPNLFRHQIIHTKEKPYKRN", "text": "FUNCTION: Involved in transcriptional regulation. Transcriptional activity differed among the various isoforms. All isoforms except isoform 3 seem to suppresses the transcriptional activities of AP-1 and p53/TP53. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Isoforms 1, isoform 2, isoform 4 and isoform 5 showed both nuclear and cytoplasm localization. Isoform 3 localized only to nucleus."}
{"protein": "MTLVQHVVTIKSTYWVIPWELASYDNPNLFTAMILMSPLVNADAVSKLNLLAAKLMGTITLNAPVGKLCPESVSRDMDKVYKYQYDPLINHEKIKAGFASQVLKATNKVRKIISKINTPRLSYSREQTIRLAMF", "text": "SIMILARITY: Belongs to the poxviridae K5 protein family."}
{"protein": "MANNNSNSPTGPHFLFVTFPAQGHINPSLELAKRLAGTISGARVTFAASISAYNRRMFSTENVPETLIFATYSDGHDDGFKSSAYSDKSRQDATGNFMSEMRRRGKETLTELIEDNRKQNRPFTCVVYTILLTWVAELAREFHLPSALLWVQPVTVFSIFYHYFNGYEDAISEMANTPSSSIKLPSLPLLTVRDIPSFIVSSNVYAFLLPAFREQIDSLKEEINPKILINTFQELEPEAMSSVPDNFKIVPVGPLLTLRTDFSSRGEYIEWLDTKADSSVLYVSFGTLAVLSKKQLVELCKALIQSRRPFLWVITDKSYRNKEDEQEKEEDCISSFREELDEIGMVVSWCDQFRVLNHRSIGCFVTHCGWNSTLESLVSGVPVVAFPQWNDQMMNAKLLEDCWKTGVRVMEKKEEEGVVVVDSEEIRRCIEEVMEDKAEEFRGNATRWKDLAAEAVREGGSSFNHLKAFVDEHM", "text": "FUNCTION: Glucosyltransferase that glucosylates kaempferol. Can glucosylate the phytotoxic xenobiotic compound 2,4,5-trichlorophenol (TCP). SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MIKRYLQFVKPYKYRIFATIIVGIIKFGIPMLIPLLIKYAIDGVINNHALTTDEKVHHLTIAIGIALFIFVIVRPPIEFIRQYLAQWTSNKILYDIRKKLYNHLQALSARFYANNQVGQVISRVINDVEQTKDFILTGLMNIWLDCITIIIALSIMFFLDVKLTLAALFIFPFYILTVYVFFGRLRKLTRERSQALAEVQGFLHERVQGISVVKSFAIEDNEAKNFDKKNTNFLTRALKHTRWNAYSFAAINTVTDIGPIIVIGVGAYLAISGSITVGTLAAFVGYLELLFGPLRRLVASFTTLTQSFASMDRVFQLIDEDYDIKNGVGAQPIEIKQGRIDIDHVSFQYNDNEAPILKDINLSIEKGETVAFVGMSGGGKSTLINLIPRFYDVTSGQILIDGHNIKDFLTGSLRNQIGLVQQDNILFSDTVKENILLGRPTATDEEVVEAAKMANAHDFIMNLPQGYDTEVGERGVKLSGGQKQRLSIARIFLNNPPILILDEATSALDLESESIIQEALDVLSKDRTTLIVAHRLSTITHADKIVVIENGHIVETGTHRELIAKQGAYEHLYSIQNL", "text": "FUNCTION: May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation. FUNCTION: May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MARELSQEALLDFLCQAGGRVTNAALLSHFKSFLRDPDASPSQHQHRRELFKGFVNSVAAVRQDPDGTKYVVLKRRYRDLLGEEGLQRPREPPAAAPSAGGAAPCSPRGARRGEPPQQQPRRRRREKEPEEEPAGAAARAADAACNGLPGSDSRRAPGKGGGSKGSPGQRPPVPAAAAAGAQARASCAAAKTQGRCCWECLQNNLAVLPGELGALPHSATAEEKPARALPAQDDRGASREREEGALAEPAPVPAVAHSPPATVEAATSRASPPALLPGPAPRGDRPELLTPSSLHYSTLQQQQQRTREWVARHPQVPEARDQGPIRAWSVLPDNFLQLPLEPGSTEPNSEPPDPCLSSHSLFPVVPDESWESWAGNPSLTVFRSIRCQLSLQDLDDFVDQESDGSEESSSGPKDSPGASEEGLQVVLGTPDRGKLRNPAGGLSVSRKEGSPSRSPQGLRNRGDGHISQQVPAGANGLAGHPLKPLPWPVPKLRRSLRRSSLAGRAKLSSSDEEYLDEGLLKRSRRPPRSRKPSKAGTAPSPRVDAGLSLKLAEVKAVVAERGWRHSLWVPSGEGSAALAPHRTSEHKSSLVPLDAREHEWIVKLASGSWIQVWTLFWEDPQLALHKDFLTGYTALHWIAKHGDLRALQDLVSGAKKAGIVLDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASRVNVRDSSGKKPWQYLTSNTSGEIWQLLGAPRGKPIFPVYPLVGSSSPTRKAKSKEISRSVTRKTSFAALLKSQHNKWKLANQYEKFHSPREREEYSD", "text": "SIMILARITY: Belongs to the SOWAH family."}
{"protein": "MYKRLFISHVILIFALILVISTPNVLAESQPDPKPDELHKSSKFTGLMENMKVLYDDNHVSAINVKSIDQFLYFDLIYSIKDTKLGNYDNVRVEFKNKDLADKYKDKYVDVFGANYYYQCYFSKKTNDINSHQTDKRKTCMYGGVTEHNGNQLDKYRSITVRVFEDGKNLLSFDVQTNKKKVTAQELDYLTRHYLVKNKKLYEFNNSPYETGYIKFIENENSFWYDMMPAPGDKFDQSKYLMMYNDNKMVDSKDVKIEVYLTTKKK", "text": "FUNCTION: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines (PubMed:2303780, PubMed:25015819). Causes also the intoxication staphylococcal food poisoning syndrome (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family."}
{"protein": "MLLLGILTLAFAGRTAGGSEPEREVVVPIRLDPDINGRRYYWRGPEDSGDQGLIFQITAFQEDFYLHLTPDAQFLAPAFSTEHLGVPLQGLTGGSSDLRRCFYSGDVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNASAPAAQRNSQGAHLLQRRGVPGGPSGDPTSRCGVASGWNPAILRALDPYKPRRAGFGESRSRRRSGRAKRFVSIPRYVETLVVADESMVKFHGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLRDRDSGPKVTGNAALTLRNFCAWQKKLNKVSDKHPEYWDTAILFTRQDLCGATTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNVKVCEEVFGKLRANHMMSPTLIQIDRANPWSACSAAIITDFLDSGHGDCLLDQPSKPISLPEDLPGASYTLSQQCELAFGVGSKPCPYMQYCTKLWCTGKAKGQMVCQTRHFPWADGTSCGEGKLCLKGACVERHNLNKHRVDGSWAKWDPYGPCSRTCGGGVQLARRQCTNPTPANGGKYCEGVRVKYRSCNLEPCPSSASGKSFREEQCEAFNGYNHSTNRLTLAVAWVPKYSGVSPRDKCKLICRANGTGYFYVLAPKVVDGTLCSPDSTSVCVQGKCIKAGCDGNLGSKKRFDKCGVCGGDNKSCKKVTGLFTKPMHGYNFVVAIPAGASSIDIRQRGYKGLIGDDNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSLLRYSGTGTAVESLQASRPILEPLTVEVLSVGKMTPPRVRYSFYLPKEPREDKSSHPKDPRGPSVLHNSVLSLSNQVEQPDDRPPARWVAGSWGPCSASCGSGLQKRAVDCRGSAGQRTVPACDAAHRPVETQACGEPCPTWELSAWSPCSKSCGRGFQRRSLKCVGHGGRLLARDQCNLHRKPQELDFCVLRPC", "text": "FUNCTION: Metalloprotease which has proteolytic activity against the proteoglycan VCAN, cleaving it at the 'Glu-1428-|-1429-Ala' site. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Cell surface."}
{"protein": "MIISAASDYRAAAQRTLPPFLFHYIDGGAYAEYTLRRNVEDLSQVALRQRVLKNMSDLSLETTLFNETLSMPVALAPVGLCGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYWQAVMHPKWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWIREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAYLYALATAGKAGVANLLDLIEKEMKVAMTLTGAKSISEISGDSLVQELGKSLPAALAPMSKGDAA", "text": "FUNCTION: Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
{"protein": "MAVGKNKRTSKGKKGGKKKVTDVFTKKEWYDLKAPKMFLVRNFGKTLVTKTIGKKLATDSLKGRIYEVNLADLNNDEDQAHKKIKLSCDHIINRDCYTDFCGLSITRDKLCSLIRKGYTLIEGHTDVKTLDNYHLRMFCIAFTKKRQNQTKSTCYAQTSQIKKIRKKMVDIMTAEASKVLLKDLVKKFIPESIGKEIEKQCKKIYPLQNVLIRKVKILKRPKLDISKLMELHTDPKEESGKNVNALPESKEATNILTAELKH", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (Probable). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (Probable). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (Probable). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family."}
{"protein": "MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAELEELTSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKMTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLLLQLEATKNTKGAGSGGKTTSGSPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQSKVHQLYETIQRWSPIASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMIACSLKDNATLLTQVQTTMRENLSTVEGNFANIDERMKKLGK", "text": "FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (PubMed:25814576, PubMed:33734450, PubMed:36071160, PubMed:29420470). Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the dynactin subunit 2 family."}
{"protein": "MIGFSFSIVTSWSALSGVLVVGVESGGPPVMIWSWVGVCAVSLAVAYSMAEMCSAYPVAGGQYSWVAILAPKKWARGLSYVCGWFMLIGILSMGAVNNFIAGNFVLGMANLTYPEYTIERWHAVLVAYLICIVAALSSIFLPHLLNRISKAILIWNICSFFICFITILATNDHKQPASFVFADFQNSTGFNKAYAAIIGILQSAFGMCCYDAPAHMTEEIKDARKQAPRAIVMSVWLGFLTGFVFLISLCFCMGGIDETASTPTGVPLIAIFHNSTGSVAGTCALTSLITVVALVCANSLMTEGGRAVYAFARDRGLPFSRALSRVHPTLGVPVAGILATAAVQAAFNSIYFGTVTGFNTVISIATEGFYVSYAIPLLVRILSRVSGDKRERLDGPYSLGRWGLLANVVGFTYLAFAVITFNFPTVDPVDKENMNYTSAASFKFIQDISNQAE", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily."}
{"protein": "MERVVVSMQDPDQGVKMRSQRLLITVIPHAVAGRDLVEWLVQKFCILEDEALHLGTLLAQHGYIYPLRESRDLTLRPDETPYRFQTPYFWTSTMWPAAELDYAIYLAKKNIQKQGALVDYEKEHYALLHKKINHAWDLVLMQAREQLRAAKQRRKGDRMVISCQEQTYWLVNKPPPGAPNILEQGPERGSYNPSHMQMSSDFYKCEIECFRKALGRNRVKSSACLEAYLKFSSQHGPHDPIMSGCLPSNPWITDDVTYWAMNAPNVAAPTKLRVERWSFSFRELLDDPVGRAHFMDFLQKEFSAENLSFWEACEELRFGGQAQVPTLVDSVYQQFLAPGAARWINIDSRTMERTLEGLRQPHRYVLDAAQLHIYMLMKKDSYPRFLKSDIYKGLLEEAVIPLETKRWPFPFLRKPLHSSPSPALQSTPREPAATSSPEGADGE", "text": "FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form."}
{"protein": "MTENNRLSVKLPGLDLKNPIIPASGCFGFGEEYAKYYDLNKLGSIMVKATTLHPRFGNPTPRVAETASGMLNAIGLQNPGLEVIMTEKLPWLNENFPELPIIANVAGSEEADYVAVCAKIGDAANVKAIELNISCPNVKHGGQAFGTDPEVAAALVKACKAVSKVPLYVKLSPNVTDIVPIAKAVEAAGADGLTMINTLMGVRFDLKTRQPILANITGGLSGPAIKPVALKLIHQVAQVVDIPIIGMGGVANAQDVLEMYMAGASAVAVGTANFADPFVCPKIIDKLPELMDQYRIESLESLIQEVKEGKK", "text": "FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. Cannot use fumarate as an electron acceptor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily."}
{"protein": "MTRVLLLGGTAEGRALAKELHPHVEIVSSLAGRVPNPALPIGPVRIGGFGGVEGLRGWLREERIDAVVDATHPFAVTITAHAAQVCGELGLPYLVLARPPWDPGTAIIAVSDIEAADVVAEQGYSRVFLTTGRSGIAAFANSDAWFLIRVVTAPDGTALPRRHKLVLSRGPYGYHDEFALLREQRIDALVTKNSGGKMTRAKLDAAAALGISVVMIARPLLPAGVAAVDSVHRAAMWVAGLPSR", "text": "FUNCTION: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y. SIMILARITY: Belongs to the precorrin-6x reductase family."}
{"protein": "MSRNLFLSITNFIRNLESLFLPHGGHPPALALAGFQHDHSPKSSQEFSLKQLIGDGLLWAVPKHRRSVEKRLKRKFGYPEYNWKPLREKRNLRSCLQCGHDHEMGVLCPFCYQKVLKETELMQSKIQETLGLDPVDKEVIVLYEGEKAEQSTDDLKNKRIVEMKKPRPMWFTKNLLQKSTQQLSETKEVKPSDLA", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
{"protein": "MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGAARFGHEGRTWGDAGAAAGGGTPSKGVNFAEEPMRSDSENGEEEEAAEAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVRITMKRKGKSDIEENGAVEIARCLRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA", "text": "FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Colocalizes with PJA2 in the cytoplasm and at the cell membrane. SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain family."}
{"protein": "MKLLAKAPLNLLRAFEAAGRTGAFALAASELELSPSAISHAIRKLENLLDVRLFQRSTREITLTKEGEILLEHIQRGFNELQQGLALVTADESRPLRLHTAPSFAHQWLLPRLGKFIRENPSIDLRLSASTEYARFEQDDFDLDIVYGEPRPSPYEKIPLAVEELTPLCSPQLAERLKKPEDLYALTLIQCDVQLYQWKGWFEANKMTPPNNYGLRFDRSFMAIAAAVDGLGVVLESKLLAEREIASGKLVCPLVNSTSEIHYIGHYLVFPQHQHMHSALDVFKTWLLNELNLGKIR", "text": "FUNCTION: Apparent regulatory gene involved in peroxide resistance in stationary phase. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MSVFSNILDENSRNLRNEIPCDDGIASPINDDDEEFLTKSNRVLLVGADSNSSLKNLMTQYSYQVTKYESGEEAMAFLMKNKHEIDLVIWDFHMPDINGLDALNIIGKQMDLPVVIMSHEYKKETVMESIKYGACDFLVKPVSKEVIAVLWRHVYRKRMSKSGLDKPGESGTVESDPDEYDDLEQDNLYESNEEGSKNTCDHKEEKSPTKKPRMQWTPELHHKFEVAVEKMGSLEKAFPKTILKYMQEELNVQGLTRNNVASHLQKYRQSSKKTCTPQEPQEDFVWGNAGPDVTLAASKTLLSSHATPSYLINNQAAPRGSYFMNNIPYPSTSCLPVNNNNCFMTNPSTYIDQFQHQLQQQQQHQQYQSTLNSISAMLTKQESRHVPSSAMENSEPLMIYNSNLPFGIDECFPPAGFNIFDQIGHN", "text": "FUNCTION: Putative transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Could directly activate some type-A response regulators in response to cytokinins (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARR family. Type-B subfamily."}
{"protein": "MFVFTKNLFTTKFSSSLLNWRFLRTMADSLVDINERITSQGNLVRSLKSQGASKEDIDKEVAKLLQLKNLKLGGSEVSGKKKDTSFTLKTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFARWLAMNPKVTSIKRFHIAKVYRRDQPAMTKGRMREFYQCDFDIAGNYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTVCGVPDDKIRTISSAVDKLDKLPWEDVRREMVVEKGLKEEVADKIKEYVLLKGDRSLLDKLEADSLLSSNSSAVAAFNDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEASAPKIKSSAEKKKSADPEADRSNDDSIGVGSIAAGGRYDNLVGMFAAKKNAKIPCVGISLGLERIFSILRSKIPDEDIRANDVDVFVMAFGGGKEWTGFLKERMSVCKDLWANGIKAEFLYKVKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMGLKENSDEGQLVPREEMVSVLKKLLKYD", "text": "FUNCTION: Catalyzes the aminoacylation of histidyl-tRNA in both the cytoplasm and the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MARWGAARMAACGPWGRNRRVGAGDAFEASEVRRDGRSRMMPACGPWGAGHGGGDPALERELSRDGSHYSISSAILPSLGARSNRRIKLRRFIISPYDRRYRIWETFLIVLVVYSAWVSPFEFGFIPKPTGALATADNVVNAFFAVDIILTFFVAYLDKMSYMLEDDPKKIAWRYSTTWLVLDVASTIPSEFARRILPSKLRSYGFFNMLRLWRLRRVSSLFSRLEKDRHFNYFWVRCAKLICVTLFAVHCAACFYYLLADRYPVPTSTWIGNYMADFHERSLWIRYVTSVYWSITTLTTVGYGDLHAENTREMIFNIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNYRDTIQAATSFGVRNQLPPRLQDQMISHISLKYRTDSEGLQQQEILDSLPKAIKSSISQYLFFHLVQNVYLFQGVSNDLIFQLVSEMKAEYFPPREDVILQNEAPTDFYILVSGSVELVEQQNGADQVIQVATSGEVVGEIGVLCYRPQLFTVRTRSLCQLLRLNRTAFLSIVQSNVGDGTIIMNNLIQFLKEQKENSVMAGVVKEIESMLARGNLDLPITLCFAVTRGDDFLLHQLLKRGMDPNESDNDGHTALHIAASKGNEQCVRLLLEYGADPNARDSEGKVPLWEALCEKHAAVVQLLVEGGADLSSGDTGLYACIAVEESDTELLNDIIHYGGDVNRARRDGTTALHRAVCDGNVQMAELLLEHGADIDKQDGNGWTPRALAEQQGHDDIQLLFRSRKAATASGHHHVPSSTTTRVAPAAAAASLIGRFNSEPMMKNMIHEDADLPSRVLPEKLRRKRVTFQNSLFGVISSSQAQRETDHPLSRGGLAATGSPNPSSGSRNAVIRVTISCPEKGNTAGKLVLLPQTLDMLLELGAKKFDFAPTKVLTVEGAEVDEVELIRDGDHLVLVSDEWDAEKMKGKS", "text": "FUNCTION: Highly selective inward-rectifying potassium channel that mediates potassium uptake by plant roots. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4) subfamily."}
{"protein": "MAPFNMDIPTLAIPGDRNQSQAIELSQQAQQPQQPQQSQQAYTGHLQRKQADEGSAEYYFDKGCEWMGNHPWMTGMGVLGVAYFASGFVKSKQPGINGKAFVKGPFGQKMTPKEALQILNLKETNLSQAKLKEQHRKLMMANHPDKGGSSYLATKVNEAKDILEKRGGLKKK", "text": "FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM14 family."}
{"protein": "MSAPMEVSFSAPPPPDAASAAAAAPSLVPAVSAAAVAATTVSCSPQPPTGSPSADDRILVSVEVLLHATSTARAEDVCAAVERMLEARSLSYVDGPVPIPNDDPFLLANVKRIQICDTDEWTENHKVLLFWQVRPVVHVFQLSEDGPGEEPGEDDTLSSFNEWALPAKEFDGLWESLLYEVGLKQRLLRYAASALLFTEKGVDPCLVSWNRIVLLHGPPGTGKTSLCKALAQKLSIRFKSRYSMCQLIEVNAHSLFSKWFSESGKLVAKLFQKIQEMVEEESNLVFVLIDEVESLAAARQAAISGSEPSDSIRVVNALLTQMDKLKSWPNVIILTTSNITTAIDIAFVDRADIKAYVGPPTLQARYEILRSCLQELLRVGILTHTQGGNSLCLLSYFSLMENQHCPEVADPHGSVHLSGLLHKAAEICEGLSGRTLRKLPFLAHASVANPSCCDASAFLHALIQTAQRELSESRG", "text": "FUNCTION: Plays a key role in chromosome recombination during meiosis. Required for the initiation of meiotic recombination and the recruitment of PAIR2 onto meiotic chromosomes. Essential for meiotic DNA double-strand break (DSB) formation. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Appears as punctuate foci on chromosomes at leptotene. Colocalizes with ZEP1 to the central region of the synaptonemal complex. SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily."}
{"protein": "MLVLCSRSRLTSSLIRRLKDQIANVSNHRSFATSEGHRLAIVNKRSLDILQDPWFNKGTAFSMTERDRLDLRGLLPPNVMTTEQQIERFTADLRVLELTTKDGPSDTYDLAKWRILNRLHDRNETMFFKVLIENIEEYAPIVSTPTVGLVCQKFSGLYRRPRGMYFSSDDRGEMMSMVYNWPAEQVDMIVVTDGSRILGLGDLGVHGIGVAIGKLDLYVAAAGINPQRVLPVMIDVGTNNEDLLKNPLYLGLQKKRLDGEEYLAVMDEFMEAVFTRWPNVIVQFEDIQNKWALTLLQRYRHKYRTFNVDVQGTSGVAIAGLLGAVRAQGRPMIDFPKQKIVVAGAGSSGVGVLNAARKTMARMLGNDESAFDRARSQFWVVDDKGLITEKRANLDPEVQPFAWKENEISLQGLNEGAKLVEVVRQVKPDVLLGLSAYGGLFSKEVLEALKDSTSTRPAIFAMSNPTKNAECTPEEAFSIVGDHVVYASGSPFKDVDLGNGKIGHVNQGNNMYLFPGIGLGVLLSGSRIISDSMFQAAAERLAGYMTDEEVINGVIYPSISRIRDITKEVAAAVIKEAVEEDLAEGYRDMDARELQKLNEEQILEYIEKNMWNPEYPTLVYKKR", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the malic enzymes family."}
{"protein": "MVIFTDLDGTLLNHEDYSFKDAIPSLERIKKKGIPLVIVTSKTKKEVELIQKELGIEEPFIVENGAAVFFPKGYRGFNIRCDQENRYCIIKLGRDYREIRDFIEKIKDKFKIKGFGDMTVEEIVRLTDLPYDRAELAKERDFTEPFIIEDEKDIKDLEEIAEKEGFKITKGGRFYHLIGKGQDKGRAVQIVKKVFEENYGEVPLTVGLGDSRNDIPMLREVDIPILIPHINKKYESVNLPGIIKAEYPGSKGWNESIWRILNEIERGCC", "text": "FUNCTION: Involved in the biosynthesis of glucosylglycerate. Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and mannosylglycerate (MG), respectively. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MPGP family."}
{"protein": "MDPKGWCEKLNDGHVIPVLGFGTYAPEEVPKSRTVEVTKLAIDAGFRHIDSAYSYNNEKEVGQAIRSKIEDGTVKREDIFYTSKLWLTFLRPELVRPALEKSLTNLQLDYVDLYIIHFPIALKPGEELFPEDEHGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYGALGTQRLKRWLAPNSPVLLEDPVLCAMAKKYKRTPALIALRYLLQRGVVVLAKSYNEKRIKENMQVFEFQLTSEDMKDLDGLNRNHRFLPLQIAVDHPEYPFADEY", "text": "FUNCTION: NADP-dependent oxidoreductase involved in steroid metabolism. May act on various hydroxysteroids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MRSLLKQFAFSRRLLKVESCRITESASLILLPWASLIQKLNRVPVIFLLDQRKRFSTMPEIETNHRDSELFSPPSEVRGMTELDRTAFKKTVTIPVLKVRKEVVNKLMRSLKRAALQRPGIKRVIEDPEDGEGRLIMLDPYKMFTVDSFEKEELSILKQLNVNPQISKYNLDLTYENFKSEEILRAVLPEGQDVTSGFSRVGHIAHLNLRDHQLPYKHLIGQVMIDKNPGITSAVNKINNIDNTYRNFEMEVLSGEENMMTKVRENNYTYEFDFSKVYWNPRLSTEHSRITELLKPGDVLFDVFAGVGPFAIPAAKKKCTVFANDLNPESHKWLLHNCKLNKVDQKVKVFNLDGRDFLQGPVREELMQQLGPLSKERKHSVHIVMNLPAKAIEFLSAFKALLEGQPCGSELLPIVHCYSFSKDANPAKDVQQRAATVLGISLEAYSSVHLVRNVAPNKEMLCITFRIPAAILYKNQTVNRDNHEGPPLKRQRTDKDF", "text": "FUNCTION: Involved in mitochondrial tRNA methylation (By similarity). Specifically methylates the N1 position of guanosine-37 in various tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Cytoplasm Note=Predominantly in the mitochondria and in the nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family."}
{"protein": "MMRLVIILIVLLLISFSAY", "text": "FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system. Overexpression causes cessation of growth and rapid membrane depolarization. Overexpression induces stress-response, the psp phage shock and a number of membrane protein genes. SIMILARITY: Belongs to the Ibs toxic protein family."}
{"protein": "MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPPFVRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLGRCCHVGKGYSG", "text": "FUNCTION: Antibacterial activity against M.luteus and E.coli bacteria. Antifungal activity against N.crassa and F.oxysporum. Presents chitin- binding activity. SUBCELLULAR LOCATION: Cytoplasmic granule Note=Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. SIMILARITY: Belongs to the penaeidin family."}
{"protein": "MSAREERYQRGSKRPAARRENESDNGSWEQADLGNEERKQKFLRLMGAGKKEHTGRLVIGDHKSTSHFRSGVEDKKISDQLEHQYQQSMDSSMSGRNRRHCGLGFSESETTQEKAPPPPPEHPPERESESESSNEVSSEEESESESVSEEETAADKQKPTKPNEKDSFPDSRDGKSNYKMLFVKSTGS", "text": "SIMILARITY: Belongs to the SMAP family."}
{"protein": "MAKEISSELLNTILTRVGGPGNIASCGNCMTRLRLGVHDSSLVDPDIKTLEGVKGVILTSDQVQVVFGPGKAHRAAKAMSELLGEAPVQDAAEIAAQNKRQLKARQTSGVQQFLAKFATIFTPLIPGFIAAGLLLGIATLIATVMHVTADAQGTLPDALNFMKVFSKGLFTFLVILVGYNAAQAFGGTGVNGAIIAALFLLGYNPTATTGYYAGFHDFFGLPIDPRGNIIGVLIAAWACARIEGMVRRFMPDDLDMLLTSLITLLITATLAYLIIMPLGGWLFEGMSWLFMHLNSNPLGCAVLAGLFLIAVVFGVHQGFIPVYLALMDSQGFNSLFPILSMAGAGQVGAALALYWRAQPHSALRSQVRGAIIPGLLGVGEPLIYGVTLPRMKPFVTACLGGAAGGLFIGLIAWWGLPMGLNSAFGPSGLVALPLMTSAQGILPAMAVYAGGILVAWVSGFIFTTLFGCRNVNLD", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6-anhydro ring. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MGSKAKKRVLLPTRPAPPTVEQILEDVRGAPAEDPVFTILAPEDPPVPFRMMEDAEAPGEQLYQQSRAYVAANQRLQQAGNVLRQRCELLQRAGEDLEREVAQMKQAALPAAEAASSG", "text": "SIMILARITY: Belongs to the UPF0449 family."}
{"protein": "MDLFISSQLLLLLVFCLFLFWNFKPSSQNKLPPGKTGWPIIGETLEFISCGQKGNPEKFVTQRMNKYSPDVFTTSLAGEKMVVFCGASGNKFIFSNENKLVVSWWPPAISKILTATIPSVEKSKALRSLIVEFLKPEALHKFISVMDRTTRQHFEDKWNGSTEVKAFAMSESLTFELACWLLFSINDPVQVQKLSHLFEKVKAGLLSLPLNFPGTAFNRGIKAANLIRKELSVVIKQRRSDKLQTRKDLLSHVMLSNGEGEKFFSEMDIADVVLNLLIASHDTTSSAMGSVVYFLADHPHIYAKVLTEQMEIAKSKGAEELLSWEDIKRMKYSRNVINEAMRLVPPSQGGFKVVTSKFSYANFIIPKGWKIFWSVYSTHKDPKYFKNPEEFDPSRFEGDGPMPFTFIPFGGGPRMCPGSEFARLEVLIFMHHLVTNFKWEKVFPNEKIIYTPFPFPENGLPIRLSPCTL", "text": "FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPT-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:27746309, PubMed:29378087). Catalyzes the formation of protopanaxatriol from protopanaxadiol during ginsenoside biosynthesis, a class of tetracyclic triterpenoid saponins. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MDRLELIKRNVQEIVTEEELEGLLNKKETPRAYVGYEPSGKIHMGHVLTVNKLIDLQKAGFKITVLLADVHAYLNRKGTLEEVRKIADYNRRCFIALGLDEEQTDFVYGSDFQLGAEYMLNVLKLSRAVTLNRAKRSMDEVGRAMDDPTVSQMVYPLMQAIDIALLEVDVAVGGIDQRKIHMLARENLKSLGFETPICIHTPILLGLDGTKMASSKDNFISVDDTEEEIYRKFKKAFCKMGDVEENPILALFRYHIFPRYETIVIERPEKFGGNLVYNSYSEMESGFAEEKVHPMDLKNSAAKYINEILDPVRKVLL", "text": "FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily."}
{"protein": "MRMIDIIEKKRDGKSLTKEEIEFFVNGYTHGEVPDYQASSLAMAIFFQDMNDEERAALTMSMVNSGEKIDLSDINGIKVDKHSTGGVGDTTTLVLAPLVAAVGVPVAKMSGRGLGHTGGTIDKLESVKGFNVEISEKDFIKLVNDNQVAVIGQSGNLTPADKKLYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGSGAFMKTLDDAEALAHAMVRIGNNVGRNTMAIISDMSQPLGNAIGNALELKEAIATLKGNGPKDLTELVLTLGSQMVVLAEQATSLDEARQMLIDAIKTGKALNKFKTFLSNQGGDDSIVDSPEKLPSAKYQVEFKAKKDGYITEIIANEIGVASMMLGAGRQTKEDVIDLGVGIVLNKKVGEHVEKGENILTIHTNTKEIDDILYKLDNSITIESKGEAPTLIHKIITE", "text": "FUNCTION: Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate. SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family."}
{"protein": "MASCSTSGTCGSSCCQPSCCETSCCQPSCCQTSSCGTGCGIGGGIGYGQEGSGGSVSTRIRWCHPDCHVEGTCLPPCYLVSCTPPSCCQLHHAEASCCRPSYCGQSCCRPACCCHCCEPTC", "text": "FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SIMILARITY: Belongs to the KRTAP type 1 family."}
{"protein": "MDAIRKQASRLREQVARQQQAVFKQFGGGGYGSGLADEAELNQHQKLEKLYISTRAAKHYQRDIVRGVEGYIVTGSKQVEIGTKLSEDSRKYGSENTCTNGNVLTRAALNYGRARAQMEKERGNMLKALGTQVAEPLRAMVLGAPLEDARHLAQRYDRMRQEAEAQATEVARRQAKARESQGNPDILMKLESAEAKLHDLKSNMTILGKEAASALASVEDQQQKLTLERLLSMVESERAYHQRVLQILDQLEGEMVSERQRIEAPSTPSSADSMPPPPSYEEANGVFASQMHDTSTDSMGYFLGEVLFPYHGVTDVELSLSTGEYVVVRKVTGSGWAEGECKGKAGWFPYGYIERRERVLASKVSEVF", "text": "FUNCTION: Regulator for autophaosome formation and/or maturation (PubMed:24249832, Ref.9). Binds phosphatidylinositol-phosphate; highest affinity for vesicles containing PtdIns(3,4,5)P(3), followed by those containing PtdIns(4,5)P(2) and PtdIns(3,4)P(2), with minimal binding to phosphatidylinositol monophosphates, including PtdIns(3)P (PubMed:24249832, PubMed:28584166). Together with DRP1A, converts the fused vesicles to tubular structures at the cell plate during cytokinesis (PubMed:28584166). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, clathrin-coated vesicle Cell membrane Late endosome Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein Note=Transolcate from the cytosol to the phagophore assembly site/preautophagosome structure upon autophagy induction (PubMed:24249832). Localized at the leading edge of the cell plate in dividing cells, especially in constricted or curved regions (PubMed:28584166). Observed at the plasma membrane and in endosomal compartments in non-dividing cells (PubMed:28584166)."}
{"protein": "MARTKQTARKSTGGKAPRKQLATKAARKSAPAAGGVKKPHRYKPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAAEAYLVSLFEDTNLAAIHAKRVTIQPKDIALARRLRGERS", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H3 family."}
{"protein": "MGSRFLLALFLVLLVLGCEVQAAQQLQQDDPGSPALLDKVQESISSYWDTAKAAAQGLYQKTYLTSVDEKLRDMYSKSSAAMTTYASIFTDQIFTLLKGE", "text": "FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C2 family."}
{"protein": "MSEEQLKAFIAKVQADTSLQEQLKVEGADVVAIAKASGFAITTEDLKAHQANSQKNLSDAELEGVAGGTIGGTIVSITCETCDLLVGKMC", "text": "FUNCTION: Lanthionine-containing peptide (lantipeptide) with unknown function (Probable). Does not show antibiotic activity against Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria (By similarity). Organisms that produce this peptide live in oligotrophic environments at very dilute concentrations, suggesting this peptide is not secreted to influence other bacteria (Probable). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MSQIMYNYPAMLAHAAEMNTYSGALHAVGADIAAEQHALASAWQGDTGMTYQAWQAQWNQAMEELVRAYRAMATTHEQNTMAMSARDQAEGAKWG", "text": "SUBCELLULAR LOCATION: Secreted Note=Secreted via the ESX-3 / type VII secretion system (T7SS). SIMILARITY: Belongs to the WXG100 family. ESAT-6 subfamily."}
{"protein": "MLEHFPWLTTMIALPLVAALFIPLIPDKDGKQVRWYALGVGLADFVLMSYVFWTNYDISSTGFQLQEKFSWIPQFGLSWSVSVDGISMPLVLLAGLVTTLSIFAAWQVDHKPRLFYFLMLVLYAAQIGVFVAQDMLLLFIMWELELVPVYLLVCIWGGQKRQYAAMKFLLYTAAASVFILVAALGLAFYGDVTTFDIAELGLKDYPIALELFLYAGLLIAFGVKLAIFPFHTWLPDAHGEASAPVSMILAGVLLKMGGYGLIRLNLGLLEDAHVYFAPILVILGVVNIIYGGFSSFAQDNMKRRLAYSSVSHMGFVLLGIASFTDLGISGAMLQMLSHGLIAAVLFFLAGVTYDRTHTLSLAQMGNIGKVMPTVFALFTMGAMASLALPGMSGFVSELAVFVGVSSSDIYSTPFKTVTVFLAAVGLVLTPIYLLSMLRQLFYGNNIPPSCNLEQDNLSANSDQEAVCFGTSCVLPGNAIYDDARPREVFIAACFLLPIIAVGLYPKLATQTYDATTVAVNSQVRQSYVQIAETNPRVYAEALTAPHIPTTDFATVKVQP", "text": "FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family."}
{"protein": "MKLYNLKNHNEQVNFETAVKLGLGQKQGLFFPVKLPIMTPVELSKILKMDFITRSTEILSKFISSEISKEVLHEHVKKAFSFSKPLKICINKNISCFELFHGPTLAFKDFGARFMAQMILCLNKKNESFTILTATSGDTGAAVAHAFYGMKNIRVIILYPKGKITLLQEQLFCTLGKNIKTISINGSFDDCQKLVKKAFDDKKLKESIGLNSANSINISRLLAQICYYFEAFSLISEEKRKNLVIAVPCGNFGNLTAGLLAKSLGLPIQSFIACTNSNDTVPRFLNSGKWNPKKTVSTISNAMDISCPNNWPRIEELFRRKKWDLKELRFGSVSDNVTKETLKELFRMGYVSEPHAAIAYRLLHDQLKKEEFGLFLGTAHPSKFKDTVEKILENSISLPKELKNRNNLPLLSHNINPDFNKLKEFLLEK", "text": "FUNCTION: Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. SIMILARITY: Belongs to the threonine synthase family."}
{"protein": "MAAMLGDAIMVAKGLAKLTQAAVETHLQNLGLGGELLLAARALQSTAVEQFSMVFGKVQGQDKHEDSYATENFEDLEAEVQFSTPQAAGTSLDFSAASSLDQSLSPSHSQGPAPAYASSGPFREAGLPGQATSPMGRVNGRLFVDHRDLFLANGIQRRSFHQDQSSVGGLTAEDIEKARQAKARPESKPHKQMLSERARERKVPVTRIGRLANFGGLAVGLGIGALAEVAKKSLRSENSTGKKAVLDSSPFLSEANAERIVSTLCKVRGAALKLGQMLSIQDDAFINPHLAKIFERVRQSADFMPLKQMTKTLNSDLGPHWRDKLEYFEERPFAAASIGQVHLARMKGGREVAMKIQYPGVAQSINSDVNNLMAVLNMSNMLPEGLFPEHLIDVLRRELTLECDYQREAAYAKKFRELLKDHPFFYVPEIVDELCSPHVLTTELISGFPLDQAEGLSQEVRNEICYNILVLCLRELFEFHVMQTDPNWSNFFYDPQQHKVALLDFGATREYDRSFTDLYIQVIRAAADQDREAVLKKSIEMKFLTGYEVKAMEDAHLDAILILGEAFASEEPFDFGTQSTTEKIHNLIPVMLKHRLIPPPEETYSLHRKMGGSFLICSKLKARFPCKAMFEEAYSNYCRMKSGLQ", "text": "FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:27499294). Its substrate specificity is unclear: does not show any protein kinase activity (PubMed:27499294). Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (By similarity). Shows an unusual selectivity for binding ADP over ATP (By similarity). SUBCELLULAR LOCATION: Mitochondrion Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein kinase family."}
{"protein": "MTLRCLEPSGNGAEGTQSQWGTSGSAEEPSPEAARLAKALRELSHTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPPLQHLCRLTINKCTGTIWGLPLPTRLKDYLEEYKFQV", "text": "FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway (By similarity). Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity)."}
{"protein": "GVLSLLKKLPMILKHLHGK", "text": "FUNCTION: Antimicrobial and mast cell degranulating peptide which probably acts by forming pores in membranes (By similarity). Active against both Gram-negative and Gram-positive bacterial strains as well as against yeasts (By similarity). Has little hemolytic activity (By similarity). In the context of inflammation and cancer tests, is weakly cytotoxic to normal cells, induces calcium signaling but does not impact cAMP production (PubMed:36548715). In addition, prevents LPS- induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells (PubMed:36548715). Does not show significant antiproliferative activity on the breast cancer cell line MDA-MB-231 (PubMed:36548715). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Assumes an amphipathic alpha-helical conformation in a lipid environment. SIMILARITY: Belongs to the xylopin-like family."}
{"protein": "MKALAKLERGPGLTLTRVKKPEVGHNDVLIKIRRTAICGTDIHIWKWDDWAQKTIPVPMHVGHEYVGEIVEMGQEVRGFSIGDRVSGEGHITCGFCRNCRAGRRHLCRNTVGVGVNREGAFAEYLAIPAFNAFKIPPEISDDLAAIFDPFGNATHTALSFNLVGEDVLITGAGPIGVMAVAIAKHVGARNVVITDINDYRLDLARRMGATRAVNVSRESLRDVMADLHMTEGFDVGLEMSGVPSAFTSLLESMNHGGKVALLGIPPAQTAIDWNQVIFKGLEIKGIYGREMFETWYKMVAMLQSGLDLSPIITHRFAVDDYEKGFAAMLSGESGKVILDWAAA", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFSSPMDIFDMFFGGGGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVEKCPLCKGRGMQIHIQQIGPGMVQQIQTVCIECKGQGERINPKDRCESCSGAKVIREKKIIEVHVEKGMKDGQKILFHGEGDQEPELEPGDVIIVLDQKDHSVFQRRGHDLIMKMKIQLSEALCGFKKTIKTLDNRILVITSKAGEVIKHGDLRCVRDEGMPIYKAPLEKGILIIQFLVIFPEKHWLSLEKLPQLEALLPPRQKVRITDDMDQVELKEFCPNEQNWRQHREAYEEDEDGPQAGVQCQTA", "text": "SUBCELLULAR LOCATION: Membrane; Lipid-anchor."}
{"protein": "MVCARAALGPGALWAAAWGVLLLTAPAGAQRGRKKVVHVLEGESGSVVVQTAPGQVVSHRGGTIVLPCRYHYEAAAHGHDGVRLKWTKVVDPLAFTDVFVALGPQHRAFGSYRGRAELQGDGPGDASLVLRNVTLQDYGRYECEVTNELEDDAGMVKLDLEGVVFPYHPRGGRYKLTFAEAQRACAEQDGILASAEQLHAAWRDGLDWCNAGWLRDGSVQYPVNRPREPCGGLGGTGSAGGGGDANGGLRNYGYRHNAEERYDAFCFTSNLPGRVFFLKPLRPVPFSGAARACAARGAAVAKVGQLFAAWKLQLLDRCTAGWLADGSARYPIVNPRARCGGRRPGVRSLGFPDATRRLFGVYCYRAPGAPDPAPGGWGWGWAGGGGWAGGARDPAAWTPLHV", "text": "FUNCTION: Essential for the proper localization of brevican (BCAN), mainly as a perineuronal nets (PNNs)-type deposition in the brainstem and cerebellum thereby playing a key role in the formation and structural organization of PNNs (By similarity). Contributes to the formation and transmission of inhibitory GABAergic synapses between Purkinje cells and deep cerebellar nuclei neurons (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the HAPLN family."}
{"protein": "MESLLNRLYDALGLDAPEDEPLLIIDDGIQVYFNESDHTLEMCCPFMPLPDDTLTLQHFLRLNYASAVTIGADADNTALVALYRLPQTSTEEEALTGFELFISNVKQLKEHYA", "text": "FUNCTION: Molecular chaperone required for SopB/SigD stabilization and secretion. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IpgE/SigE chaperone family."}
{"protein": "MSLIRKKGFYKQDVNKXXXELXKTYVSPTHVGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFHDFYLVMXFMQTDLQKIMXMEFSEEKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDXAAKSYIQSLPQTPRKDFTQLFPRASPQAADLLEKMLELDVDKRLTAAQALTHPFFEPFRDPEEETEAQQPFDDSLEHEKLTVDEWKQHIYKEIVNFSPIARKDSRRRXGXKL", "text": "FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up- regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down- regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
{"protein": "MKLRRERFERRNGSGKNSQSSSSWMVTFTDLITLILVFFILLFSMSQIDLQKFKAAVDSIQKEGNGLQPDQTSIEKKNTSPSDTKKQEDQQDQLLKKVNTYIKDNHLKAQMTAKRDERGVVLVLQEAVLFDTGEAKVLKNAETLLHQIAVLLQTIPNDIQVEGHTDSRNISTYRYPSNWELSAARASGVIQYFTSKEKLPSKRFIAVGYADTKPVKDNKTNEHMKENRRVEIVIKKSKTTSS", "text": "FUNCTION: May be involved in some transport function. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the MotB family."}
{"protein": "MTHLLTVFLVALMGLPVAQALECHVCAYNGDNCFKPMRCPAMATYCMTTRTYFTPYRMKVRKSCVPSCFETVYDGYSKHASATSCCQYYLCNGAGFATPVTLALVPALLATFWSLL", "text": "FUNCTION: Acts in different tissues through interaction to nicotinic acetylcholine receptors (nAChRs) (PubMed:10402197). The proposed role as modulator of nAChR activity seems to be dependent on the nAChR subtype and stoichiometry, and to involve an effect on nAChR trafficking and its cell surface expression, and on single channel properties of the nAChR inserted in the plasma membrane.Modulates functional properties of nicotinic acetylcholine receptors (nAChRs) to prevent excessive excitation, and hence neurodegeneration. Enhances desensitization by increasing both the rate and extent of desensitization of alpha-4:beta-2-containing nAChRs and slowing recovery from desensitization. Promotes large amplitude ACh-evoked currents through alpha-4:beta-2 nAChRs (PubMed:10402197, PubMed:11906696). Is involved in regulation of the nAChR pentameric assembly in the endoplasmic reticulum. Shifts stoichiometry from high sensitivity alpha-4(2):beta-2(3) to low sensitivity alpha-4(3):beta- 2(2) nAChR (PubMed:25193667). In vitro modulates alpha-3:beta-4- containing nAChRs. Reduces cell surface expression of (alpha-3:beta- 4)(2):beta-4 and (alpha-3:beta-4)(2):alpha-5 nAChRs suggesting an interaction with nAChR alpha-3(-):(+)beta-4 subunit interfaces and an allosteric mode. Corresponding single channel effects characterized by decreased unitary conductance, altered burst proportions and enhanced desensitization/inactivation seem to depend on nAChR alpha:alpha subunit interfaces and are greater in (alpha-3:beta-2)(2):alpha-3 when compared to (alpha-3:beta-2)(2):alpha-5 nAChRs (By similarity). Prevents plasticity in the primary visual cortex late in life (PubMed:21071629). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Cell projection, dendrite Endoplasmic reticulum Note=Detected in Purkinje cells soma and proximal dendrites."}
{"protein": "MTVDSKPQLQRLAADADVDRMCRLLEEDGAFILKGLLPFDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVATTCPTFRNTILINPVIHAICEAYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHYQPLEAPPISLSVIFPLTEFTEENGATEVILGSHRWTEVGTPERDQAVLATMDPGDVLIVRQRVVHAGGGNRTTAGKPRRVVLAYFNSVQLTPFETYRTMPREMVESMTVLGQRMLGWRTMKPSDPNIVGINLIDDKRLENVLQLKAADSPA", "text": "FUNCTION: Verruculogen synthase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:19763315, PubMed:23649274). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13- dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable). SIMILARITY: Belongs to the PhyH family."}
{"protein": "MTYSITLRVFQRNPGRGFFSIVEKTVFHYANGGTWSEAKGTHTLTMGGSGTSGVLRFMSDKGELITVAVGVHNYKRWCDVVTGLKPEETALVINPQYYNNGPRAYTREKQLAEYNVTSVVGTRFEVKYTVVEGNNLEANVIFS", "text": "FUNCTION: Lectin that recognizes O-linked galactose-beta-1,3-N- acetylgalactosamine, a disaccharide (Thomsen-Friedenreich antigen or T- disaccharide), present on cell surface glycoproteins. Can also bind chitin, N,N'-diacetylchitobiose, N-acetylgalactosamine and N- acetylglucosamine. Inhibits proliferation of colon, breast and liver cancer cell lines (in vitro). SIMILARITY: Belongs to the fungal fruit body lectin family."}
{"protein": "MSKARVYTDVNVVRPKEYWDYESLVVQWGHQDDYEVVRKVGRGKYSEVFEGKNVNTNERCVIKILKPVKKKKIKREIKILQNLCGGPNIVKLYDIVRDEHSKTPSLVFEFVNSVDFKVLYPTLTDYDIRYYIYELLKALDFCHSQGIMHRDVKPHNVMIDHQLRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTNELDHYLNKYQLDLDPQLEALVGRHVPKPWSKFINADNQHLVSPEAIDFLDKLLQYDHQDRLTAREAMDHPYFAQVKAAESSRLRTQ", "text": "FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site. The tetrameric holoenzyme CK2 is composed of two alpha and two beta subunits (By similarity). Acts as circadian clock component that maintains the correct period length through phosphorylation of CCA1 (PubMed:21900482). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily."}
{"protein": "MAIATTKTALTTIMNWMTFTDDSKEQLKIVEGRLFQSCEVSYEAKYVPVRFKRGEVYTVTVRPREAENLNGEAIVFIPGLGAGVAMFTANFNSCAKNHAVHSFDPLGFGRSSRSRFSDDNAIAELEMVEVMEDWRKAMGIEKMYIIGHAFGGYLASAYALENPSRVAHLILVDPWGFAEKVETTEKLIKPYAWMSFLGGVAGYFNPFSPMRWMGPYAPAIVKKLRPDLLLRFPGLHDYDIYKYVYYLNLPNPTGETAFMNMTLPVGWAKRPMIKRFNGIDKNVGVSFIYGSKSWIDPGPAIDIQSTRENAYVDIKIVRGAGTHVYADDPAAFNEIVSDVVEGRLSNPSNDFEIEECCHSD", "text": "FUNCTION: Acts coordinately with atgl-1 within the lipolytic cascade to distribute stored energy to tissues during nutritional deprivation. SUBCELLULAR LOCATION: Lipid droplet Note=Forms ring-like structures on the surface of lipid droplets. SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily."}
{"protein": "MIDIVRWRYAFYLLSLLIIIPGTIYLLLFGLRLGIDFEGGTFWQIQFEKPVRIEDVRSALAQAGYNEAFVQSFGQQSNTAQGTVTRGVSMRLPEIKENSPEKAKLEQILKSRFGNYEELVFTSVGPAVGREIRNRSIVAIALASLGILGYIAFAFRKVSHPFRYGICAIIAMLHDVLVVVGIFAILGKHFGVEIDALFVTALLTVIGFSVHDTIVVFDRIRENQLRRYGESFEQIVNISLLQTLVRSVNTSMTVIFTLLALYFFGGTTIKHFVLALLIGIVSGTYSSIFNASLLLVSWENKDFLRIFRRTEPEAAAT", "text": "FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily."}
{"protein": "MRSRSNLIGLINFFTFLLSIPILGGGIWLSSRANSTDCLRFLQWPLIIIGISIMVISLAGIAGACYQNKFLMWLYLFTMFFVIAALIGFTIFAYVVTDKGSGRFVMNRRYLDYYLNDYSGWLKDRVTDNGYWRDIGSCVRDSGVCKKIGRDLNGVPETAHMFYFRNLSPVESGCCKPPTDCGYTYVNETVWIPGGEMVGPNPDCMLWNNDQRLLCYQCSSCKAGVLGSLKKSWRKVSVINIVVVIILVIFYVIACAAYQNVKRMYNDEPVGEARMTNLILVIFKFKEILVQFFFGIVFLLLFNGLMVCCCNDKFAFSVFFFGYVTYA", "text": "FUNCTION: May be involved in the regulation of cell differentiation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
{"protein": "MNNKSISPIILMILDGWGHSTNAKGNAIHEANTPIIDKLWDNYPKTLLSASGEHVGLPHKQMGNSEVGHTTIGAGRIINQDLVKISKSIKNKEFFNNYQLHNIYKYSCEKNSKVHIVGLCSNGGVHSHINHLKALIQISKQYKVMTCLHLITDGRDTLPKQAKLFVKEIIDIIDENYNTEICTISGRYYSMDRDCRWSRTEKAYKAMVENSCNQNSSSDILSIIDKYYEQNISDEFLPPTKISMHNIVHNDSLIFFNFRPDRIRQLLHSFAKPNFKGFQRKTIKNLMLTTFTEYDSTLSIPTVFPNEPKKNFLGQIISNSGLKQLRLAETEKYAHVTYFFNGGIEEPFPGENRELIASPKVETYDLPPEMSAYQLTNSLIEAINKQLYQFIVINYANPDMIGHTGNMNATIEAIEIVDQCIEKVLHTIEDTNNILIITSDHGNADYMLTDENKPCTSHSINPVPFILINNRQKKQTNLHSHGSLADIAPTILDILNINIPNEMNGKSLIT", "text": "FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family."}
{"protein": "MLSTMAPGSTVGTLVANMTSVNATEDACTKSYSAFLSGMTSLLLVLLILLTLAGILFIIFVRKLVHRMDVWLIALLIELLLWVLGKMIQEFSSTGLCLLTQNMMFLGLMCSVWTHLGMALEKTLALFSRTPKRTSHRNVCLYLMGVFCLVLLLIIILLITMGPDANLNRGPNMCREGPTKGMHTAVQGLKAGCYLLAAVLIVLLTVIIIWKLLRTKFGRKPRLICNVTFTGLICAFSWFMLSLPLLFLGEAGSLGFDCTESLVARYYPGPAACLALLLIILYAWSFSHFMDSLKNQVTVTARYFRRVPSQST", "text": "FUNCTION: Constitutively active, ligand-independent G protein-coupled receptor that has immunoevasive and oncogenic activities (PubMed:34216564, PubMed:15596846, PubMed:15596837, PubMed:30647152). Couples with the host inhibitory G protein (Gi) in order to disrupt the host chemokine signaling (PubMed:34216564). As a consequence of its constitutive activity, mediates host CXCR4 inhibition (PubMed:20622011). Enhances degradation of host major histocompatibility complex class I antigens via lysosomes, thereby modulating the antigen presentation to cytotoxic T cells (PubMed:19119421, PubMed:21123379, PubMed:23315076). Targets selectively HLA-A, HLA-Band HLA-E molecules (PubMed:23315076). Targets also newly synthesized MHC-I/peptide complexes en route to the host cell surface (PubMed:21123379). Inhibits the host EIF2AK2/PKR phosphorylation (PubMed:15596837). Displays tranforming activity (PubMed:20543866). SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Epstein-Barr virus BILF1 protein family."}
{"protein": "MEELSQALASSFSVSQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYVNHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQEWIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCTPESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTKPDYAGHQLQQIMEHKKSQKEGMKEKLTHKASENGHYELEHLSTPKLKGSSHSPDHPGCLMEN", "text": "FUNCTION: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta (PubMed:10209022, PubMed:12095920). It is re-exported to the cytoplasm by the XPO1- dependent nuclear export receptor pathway (PubMed:10209022). SIMILARITY: Belongs to the snurportin family."}
{"protein": "MTSHAANPKEEQDQRLPFKSDISGPIAPSQAPAHTVQAHDSQPKPSDDSSDEHLSFYEAKARIVRAFAASRAPQPAAPAAKALEGDASVIVPGKLILSSCEVEESSELLTKLGVTHILQVGEELKPSHPGRFTYLSLPILDMEGQDIVALLPSCFQFLQQAQASGGVCLVHCLAGISRSASVVIAYLMWTQGMPYTEARAMVRRARSKVYPNTGFTLQLQELDRLRESGAIQWGDTPSLASSLEQHRQPWNLIRYLEVKEKQAQEEGWTWGRTLVI", "text": "FUNCTION: Could be involved in tyrosine phosphatase signalling pathways, having MAP-kinases as substrates. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "MYGNYSHFMKFPAGYGGSPGHTGSTSMSPSAALSTGKPMDSHPSYTDTPVSAPRTLSAVGTPLNALGSPYRVITSAMGPPSGALAAPPGINLVAPPSSQLNVVNSVSSSEDIKPLPGLPGIGNMNYPSTSPGSLVKHICAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLIYTCRDNKDCLIDKRQRNRCQYCRYQKCLVMGMKREAVQEERQRSRERAESEAECASSGHEDMPVERILEAELAVEPKTESYGDMNMENSTNDPVTNICHAADKQLFTLVEWAKRIPHFSDLTLEDQVILLRAGWNELLIASFSHRSVSVQDGILLATGLHVHRSSAHSAGVGSIFDRVLTELVSKMKDMQMDKSELGCLRAIVLFNPDAKGLSNPSEVETLREKVYATLEAYTKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLETPLQIT", "text": "FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily."}
{"protein": "MNKQIFVLYFNIFLIFLGIGLVIPVLPVYLKDLGLTGSDLGLLVAAFALSQMIISPFGGTLADKLGKKLIICIGLILFSVSEFMFAVGHNFSVLMLSRVIGGMSAGMVMPGVTGLIADISPSHQKAKNFGYMSAIINSGFILGPGIGGFMAEVSHRMPFYFAGALGILAFIMSIVLIHDPKKSTTSGFQKLEPQLLTKINWKVFITPVILTLVLSFGLSAFETLYSLYTADKVNYSPKDISIAITGGGIFGALFQIYFFDKFMKYFSELTFIAWSLLYSVVVLILLVFANDYWSIMLISFVVFIGFDMIRPAITNYFSNIAGERQGFAGGLNSTFTSMGNFIGPLIAGALFDVHIEAPIYMAIGVSLAGVVIVLIEKQHRAKLKEQNM", "text": "FUNCTION: Involved in quinolone resistance. May constitute a membrane- associated active efflux pump of hydrophilic quinolones (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
{"protein": "MSKIVSCEDDRPVRRTLEPIIVTRQGKVARLESSLTPHEAQIEDLIFLRKALNRADIPFLFIRNHKNRPVLAINIKLRPAVERALVTACASEPMYAKTIDERGLSPVLVAKGQLSQSIDPRIVRLYRRRIAPGGFRFGSRFGVELQFWSFEETLIRCPVENSLTRKVLPRKEVTPATIKLYGYKWHTIEGMFTPHASDVTFDIDLVFSWVDGSDPEFRARRAAEMSHHVVGEGDDADARIRQIDELKYALRSVNMFAPWIRRIFIATDSIPPSWLADHPMITIVPAEDHFSDRSALPTYNSHAVESQLHRIPDLSEHFLYSNDDMFFGRPLKASMFFSPGGVTRFIEAKTRIGLGTNDPTRSGFENAARVNRQLLLRRFGQLITRHLEHTTVPLRKSVLFEMEQEFPEEFARTQESVFRSGTDISVTNSLYHYYALITGRAVQQEKAKVLYVDTTSYTGLNLLPELRKRRNYDFFCLNDGSFPEVPATERAERVVSFLERYFPIPAPWEKVATDFNRQDFASPTVSAPLEDGQTANPAQTAR", "text": "SIMILARITY: Belongs to the stealth family."}
{"protein": "MALAVRVVYCGAUGYKPKYLQLKEKLEHEFPGCLDICGEGTPQVTGFFEVTVAGKLVHSKKRGDGYVDTESKFRKLVTAIKAALAQCQ", "text": "FUNCTION: Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency. FUNCTION: Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SelWTH family. Selenoprotein W subfamily."}
{"protein": "MTAPWRRLRSLVWEYWAGLLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQYLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWSMERLQAAPRSESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFVYKLRKTAEREQRSFCSTVADEIRFSLTCQRRVKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMACSTSLAPVFP", "text": "FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK3 subfamily."}
{"protein": "MSMGLEITGTSLAVLGWLCTIVCCALPMWRVSAFIGSSIITAQITWEGLWMNCVVQSTGQMQCKMYDSLLALPQDLQAARALIVVSILLAAFGLLVALVGAQCTNCVQDETAKAKITIVAGVLFLLAAVLTLVPVSWSANTIIRDFYNPLVPEAQKREMGTGLYVGWAAAALQLLGGALLCCSCPPREKYAPTKILYSAPRSTGPGTGTGTAYDRKDYV", "text": "FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the claudin family."}
{"protein": "MNDEINEPPPNICEQCLGDEANIRMTKIPQGSECKICTLPFTLYHFKTSKRSNNIIKTLICVRCATQRNICQCCMLDSRWHIPIQLRDHLISLVNEENVMTEEAKNDMMKRFLSLKNVKLGGAQITSDPSEADNIVDKLKNILLRATSDGPSTPLIKNTTALYKNEKGANEVKNLEKYASVDISHILKKLPLNESFLKNPSTKSFFLYNIDASIPEWKITDTVSQLLGIKKWKDGNSLSLIVNHKAKCGGLRFQSSELGERFVSKISETLVTPKGLKRGVLLIDRFRIFIIPWSSGFSAASFGTNTAENIKLSLSLNKLIQLELGLSFPTKSTDNAKNDKKKTSKKVHKDRSKKSKPRANKLTI", "text": "FUNCTION: Involved in pre-mRNA splicing. Facilitates the cooperative formation of U2/U6 helix II in association with stem II in the spliceosome. Binds to RNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLT11 family."}
{"protein": "MDILKSEILRKRQLVEDRNLLVENKKYFKRSELAKKEEEAYFERCGYKIQPKEEDQKPLTSSNPVLELELAEEKLPMTLSRQEVIRRLRERGEPIRLFGETDYDAFQRLRKIEILTPEVNKGLRNDLKAALDKIDQQYLNEIVGGQEPGEEDTQNDLKVHEENTTIEELEALGESLGKGDDHKDMDIITKFLKFLLGVWAKELNAREDYVKRSVQGKLNSATQKQTESYLRPLFRKLRKRNLPADIKESITDIIKFMLQREYVKANDAYLQMAIGNAPWPIGVTMVGIHARTGREKIFSKHVAHVLNDETQRKYIQGLKRLMTICQKHFPTDPSKCVEYNAL", "text": "FUNCTION: Participates in the second step of pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus speckle Note=Colocalizes with spliceosomal snRNPs. SIMILARITY: Belongs to the PRP18 family."}
{"protein": "MSDSNSRLVYSTQTGRIEEPKTAPVRPKGDGIVRIQRQTSGRKGKGVCLITGIEMNDAELTKLAAELKKKCGCGGAVKEGIIEIQGDKRDLIKSLLEAKGMKVKLAGG", "text": "SIMILARITY: Belongs to the SUI1 family."}
{"protein": "MNFKYIVAVSFLIASAYARSEENDEQSLSQRDVLEEESLREIRGIGTKIIGGLKTAVKGALKELASTYVNGKRTAEDHEVMKRLEAVMRDLDSLDYPEEASERETRGFNQEEIANLFTKKEKRILGPVISTIGGVLGGLLKNLG", "text": "FUNCTION: Maximin-H1 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity. FUNCTION: Maximin-11 shows antimicrobial activity against bacteria and against the fungus C.albicans. It has little hemolytic activity (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family."}
{"protein": "MTPPIKSPSSSSVDYGKLSEQLMIAYTKDVLQRNLQKFHGEQHRQQFKQLLNQPVIKSIHSLSGIIVRYRHNNSELDKALDTIDLPKIFERLEIREKTNKDKNLDYDDLLVLELLNYFKNDFFKWVNSPDCPSCGSNEDVQGLGAINPSSSKTISQSQAIIDQVSVIEVHECKKCKQKIEFPRINNPVTLLTTRRGRCGEWVNCFMLILQALIGGGDDDSDRIRYVWNQEDHVWCEYYSLSSKRWIHLDPCEGVYDEPLLYCNNWGKRMSYVIGFNYNYMIDLSDKYIVPEKQIPKNSIVNVQNVNFVISYSNGINQLKHFKRIEQQQQQQEVDVNEQRNLAFLKLYHNFLVPYNKEINQLKPELTKTTPSTDLPSGRQSGSTEWTKSRGENGES", "text": "FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase family."}
{"protein": "MRKNWTDEEIRVLQNNYEYVDTEIIANFLNRSYHSIKNKAVRLGISKNSVWTEDEDIYLEYFVYENDDNISKAAEFLGRTKDAVINRLAKLRKRDSSVSFIRRPWTKKEDEILKNNYIIMSNDQLAERLRRTKASVAARKVLLGLTNKHMSKKDDKMIRHLGNQGYTIKEISAEMNLPYCLIKNYIRNHRINYRRESKNEMNGWRKEADATYSHYINSKKIKEEQA", "text": "SIMILARITY: To L.innocua lin1255, lin1742 and lin2408."}
{"protein": "MKNVDNYRRGYFMPPVKSLKWAEKEYITTPPTWCSVDLRDGNQALVVPMSLEEKLEYYHMLLKIGFKEIEVGFPAASETEYAFLRTLIEQNLIPEDVTIQVLTQSRDHIIEKTFKALVGVKKAVVHLYNSTSVAQREQVFKMSREEIVEIAVSGARLLKKYAAETEGNFQFEYSPESFTGTEMEFALEICNQVLDVFEPTPENKVIINLPATVSLSMPHVYASQIEYMSEHLKYRDNVILSLHPHNDRGTAVADAELGLLAGGQRIEGTLFGNGERTGNVDIVTLALNLFSHGVDPGLNFASMLEITAKYEALTRMKVHDRQPYGGKLVFAAFSGSHQDAITKGIKWREEHECHYWNVPYLLIDPQDIGREYEGDVIRINSQSGKGGIAYMLEQHYALDLPAKMREAFGYKVKNVSDNLHKELMPEEIKDIFFKEYVNIENPIKFLNFHFLNHDDFQTTVTLEFKGEIQELSGEGDGRLDAISNALQARLGLSYSNLIYKEHALELGSKSQAVSYVGVTGPDGVIHWGCGIHTDIFTSSVKALISAINTMIKDSAAV", "text": "FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily."}
{"protein": "MESGSGSGAALNSTPFPTYSTPNFTDDYDWNSSDWYGLTNQCQAVSFSKLIVVPCLVILLVFCLIGNLWLLFKLLEKTVKKVSTFILILMCLNSFWGCLCMIFSIVENFAEFSTSVCKLRMVVFWVYVFFDMFLICWLCFDTWCAVWFSVRRTEANQKCWVFCTVALIILAFILSMQKALHVEAIKEYGQVRSSCQFHKETHSTLKVFNVAVSVNVLGFLLPLLFLCIFYGMCLWKLYKAVFKTKTKVIKTMLLFVFMFLLTWGPYYILSFIDGLLSAGYISESCSLKKTLGLMLPLLGLWGMAHGGLQVFIYILCNSHFNKSLFSCFKK", "text": "SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTLQSDLPATVRPLGPVMLDVAGFALTEEERERLLDPLVGGVILFARNFRDSEQLQALTAEIHALRSPALIIAVDHEGGRVQRFRTDGFTRIPSMRCLGRLWERDHVAALESARCAGYVLAAELLAHGVDLSFTPVLDLDYGCSRVVGDRAFHRDPLVVAALAQSLVSGMADAGMGCVGKHFPGHGYAEADSHVEIPVDEREFDAIWTEDIAPYRHRLGRQLAGVMPAHVIYPRVDPNPAGFSRFWLQDILRGRVGFGGVIFSDDLTMEGATVVGDILARARAAFGAGCDVVLVCNRPDLAVDLLDRWAPDIAPESRARIEALRSRPQAADPFALELHPVYRQARDVVAGLVEDTA", "text": "FUNCTION: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide- linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N- acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily."}
{"protein": "MKSAKTKDHAKMKAAEEKAIHSTGADSKSLDEVNGSVRVPKDASFWRTLIAYTGPGALVAVGYMDPGNWITSIAGGSQYKYALLSVILLSSLIAMLLQAMAARLGIVTGKDLAQLTRERTSKGMGIFLWIITELAIMATDVAEIIGSGIALKLLFGFPLIVGILITTADVLILLLLMKLGFRKIEAIVATLVAVILFVFLYEVIISQPNIPEMLKGYVPTSRIVSNRSMLFLALGIVGATVMPHNLYLGSSISQTRQVDRSDEKEVAKAVKFTTIDSNIQLSVAFVVNSLLLILGAALFFGTKGDLGRFVDLYNALGDSKVVGSIASPLLSMLFAIALLSSGQSSTITGTLSGQIIMEGFIRLKMPLWAQRLLTRLISVTPVLAFAIYYHGNEAKIEDLLTMSQVFLSIALPFAMIPLVMFTSNRALMGNFTNRVWVKWTAWIVTVILIILNIYLILQTVGLVK", "text": "FUNCTION: H(+)-stimulated, divalent metal cation uptake system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP family."}
{"protein": "MAKRSSLYIRIVEGKNLPAKDITGSSDPYCIVKVDNEPIIRTATVWKTLCPFWGEEYQVHLPPTFHAVAFYVMDEDALSRDDVIGKVCLTRDTIASHPKGFSGWAHLTEVDPDEEVQGEIHLRLEVWPGARACRLRCSVLEARDLAPKDRNGTSDPFVRVRYKGRTRETSIVKKSCYPRWNETFEFELQEGAMEALCVEAWDWDLVSRNDFLGKVVIDVQRLRVVQQEEGWFRLQPDQSKSRRHDEGNLGSLQLEVRLRDETVLPSSYYQPLVHLLCHEVKLGMQGPGQLIPLIEETTSTECRQDVATNLLKLFLGQGLAKDFLDLLFQLELSRTSETNTLFRSNSLASKSMESFLKVAGMQYLHGVLGPIINKVFEEKKYVELDPSKVEVKDVGCSGLHRPQTEAEVLEQSAQTLRAHLGALLSALSRSVRACPAVVRATFRQLFRRVRERFPGAQHENVPFIAVTSFLCLRFFSPAIMSPKLFHLRERHADARTSRTLLLLAKAVQNVGNMDTPASRAKEAWMEPLQPTVRQGVAQLKDFITKLVDIEEKDELDLQRTLSLQAPPVKEGPLFIHRTKGKGPLMSSSFKKLYFSLTTEALSFAKTPSSKKSALIKLANIRAAEKVEEKSFGGSHVMQVIYTDDAGRPQTAYLQCKCVNELNQWLSALRKVSINNTGLLGSYHPGVFRGDKWSCCHQKEKTGQGCDKTRSRVTLQEWNDPLDHDLEAQLIYRHLLGVEAMLWERHRELSGGAEAGTVPTSPGKVPEDSLARLLRVLQDLREAHSSSPAGSPPSEPNCLLELQT", "text": "FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium. Functions as an adaptor for Cdc42 and Rac1 during FcR-mediated phagocytosis. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane; Peripheral membrane protein Note=Localized to the cytosol as a result of its lack of phosphoinositide binding activity. Upon agonist-stimulated calcium mobilization, utilizes the C2A and C2B domains to associate with the plasma membrane."}
{"protein": "MSDTSFVRTEMLAPRPAPVSQVGAIKWMRENLFSGPLNTALTVFGLLATVWLVQAAAPWLLHGVWNANSLTECRAIIAERWGPEATGACWAVIRVRWNQFLFGFYPVDQYWRLFVTFAGLFLALAPVLFDALPRKLIWGTLLYPLAAFWLLWGGPIWGPVSVLAGFAILGLLFTALAPKLGVPVSAGIGLVVAALFWLYAAAPIEAALQSALPLALPEVDSDQFGGFLLALVIGVTAIVVSLPLGILLALGRQSDMLIVKSLSVGIIEFVRGVPLITLLFTASLLLQYFLPPGTNFDLILRVVILVTLFAAAYIAEVIRGGLAALPRGQYEAADALGLDYWQAQRLIIMPQALKISIPGIVSSFIGLFKDTTLVAFVGLFDPLKGISNVVRSDMAWKGTYWEPYIFVALIFFLFNFSMSRYSMYLERKLKRDHR", "text": "FUNCTION: Part of a binding-protein-dependent transport system for glutamate, glutamine, aspartate and asparagine. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily."}
{"protein": "MASPIHATDDSATFQETDVISGNLLSNDSSDNGHLFLRAFDGASVGAKSGNSQVTEIQGDYGTFFVKPDGSYTYVLSDAAKIGFANGESFQEKVSYKISDGSGHTDVGLFTLNIQGVTQVKPIAVDDHYSFNEGDAIGGNVLDNDIAGDNGHLFLRQFDGTNVSAKSGPDAVTDIVGDYGVFHVKPNGEFTYELTDDLAAGQTVTETVQYYKISDGEGHTDAGVLTLNITGTDALV", "text": "FUNCTION: Interacts specifically in a calcium-dependent manner with the acidic exopolysaccharide (EPS) and capsular polysaccharide produced by R.leguminosarum. Could be involved in the development of the biofilm matrix made of EPS. SUBCELLULAR LOCATION: Secreted Note=Secreted by the type I secretion system PrsDE."}
{"protein": "MEADYYSPEHSDADDGGATPVQDERDSASDDEGNEREQRSEPGSPERQSEDEHSDIEDNKHRSDSGSDNEEGAEHNDSEDEHRPHNSSDLENHDASDSENEESRNHIASDSEDDVRRQKGSDSEGSPVKDAASDSDEEPIRHSASDSEDDGPRKEQANDSEDERHKKNTASDSEDEAPAKHQGSDSEDEAPAKHVASDSEDEAPAKRAASDSEDEAPAKRAASDSEDEAPAKRAASDSEDEAPAKRAASDSEDEAPAKRAASDSEDEAPPKRAASDSEDEAPPKRAASDSEDEAPPKRAASDSEDEAPAKRKVSSSEDEAPSKQAFSASKKSSKKSSGDSEDKARGKRAIIDSDDEDEDVPVKRAASDSEEETHPKGKASDSEDEAPSKQQPSDSEEETPAKAAANNSEDEFPRMKRKIVSSDDSDDEIDRKPLQKKKKKSPRRSSESDSSDKVDSKKRKASESDEEEEKASKKKSAILSDSEDEDAANKSGNKKSRILSDGDDSDSDAGSDRPKQKKKLASSDSEEEDELKSKTEAKNADKLFGSESDSGNEEENLIADIFGESGDEEEEEFTGFNQEDLEGEKTVTSANKQHAAAADSDSDDDDVKPGKMGDFKSDFEIMLERKKSMSGKRRRNRDGGTFISDADDVVNAMIMKMNEAAEEDRNLNSSKKPALKKLTLLPTVVMHLKKQDLKETFIDSGVMSAIKEWLTPLPDRSLPALKIREELLKILQELPSVSQETLKHSGIGRAVMYLYKHPKESRPNKDIAGKLINEWSRPIFGLTSNYKGMTREEREQRDLEQMPQRRRMSSSGGQTPRRDLEKVLTGEEKALRPGDPGFCARARVPLPSNKDYVVRPKWNVEMESARYQGSSKKGVSRLDKQMRKFVDIKKKNRFGHAVKISIEGNKMPL", "text": "FUNCTION: Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IWS1 family."}
{"protein": "MNVPATRKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPVLGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNAPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFRERELLYDLFEAATGMRMMHNYFRIGGVAADLPHGWIDKCLDFCDYFLTGVVEYQKLITRNPIFLERVEGVGIIGGEEAINWGLSGPMLRASGIQWDLRKVDHYECYDEFDWQVQWQKEGDSLARYLVRISEMTESIKILQQALEGIPGGPYENLEGRRFDRESDSEWNDFDYRFISKKPSPTFELSKQELYVRVEAPKGELGIFLIGDNSVFPWRWKIRPPGFINLQILPHLVKRMKLADIMTILGSIDIIMGEVDR", "text": "FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the complex I 49 kDa subunit family."}
{"protein": "MSKHKHEWTESVANSGPASILSYCASSILMTVTNKFVVNLDNFNMNFVMLFVQSLVCTVTLCILRIVGVANF", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily."}
{"protein": "MDDRLSSQLEHYASQVTASATLIIRHLKSLKDEPSTLPSQTSVPTAVGTAQLRLAEAAFQLLHFTRDPGNVLTQLTVDLQVISAVRWLLHFEIFSLVPLEGSISYHELSSVANVPENLLRSHIRLAMTCHLFQESGPIGMVAHSPVSRQLASDPSLVSWGQYFANSVFPTATKNVNATAAWPGSKALNETAHNLAFNHHGSFFDYVSQDPARTVEFANSMKAVSTTSLFDTCHLCKSFDWSSLGDGVVVDMGGSTGHVSIALAESFPSLRFVVQDLPDVVSNSIRQLEERQLPLSVTTRIQFQGHSLLHMQPVKGAAVYLLRQILHDWPDREAVQILRSIVPALGPSSKIFIADIVLPEAGSIPATEEQVMRCNDLLLHQFTNTLERTLEDWQAIVSRVSDNLRIQHVYRDPGSILSLLVIETV", "text": "FUNCTION: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of aurasperone B, a dimeric gamma-naphthopyrone (PubMed:31067027). The first step in the biosynthesis of aurasperone B is the production of gamma-naphthopyrone precursor YWA1 by the non- reducing polyketide synthase albA, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:31067027). YWA1 is then methylated by aunE at position C-6 to yield foncesin which is further methylated at position C-8 by aunD to produce fonsecin B (Probable). A key enzyme in the biosynthetic pathway is the cytochrome P450 monooxygenase aunB which catalyzes the oxidative dimerization of fonsecin B to aurasperone B (PubMed:31067027). AunB also catalyzes the oxidative dimerization of rubrofusarin B into aurasperone A (PubMed:31067027). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MTATLSLKPAATVRGLRKSYGTKEVLQGIDLTINCGEVTALIGRSGSGKSTILRVLAGLSKEHSGSVEISGNPAVAFQEPRLLPWKTVLDNVTFGLNRTDISWSEAQERASALLAEVKLPDSDAAWPLTLSGGQAQRVSLARALISEPELLLLDEPFGALDALTRLTAQDLLLKTVNTRNLGVLLVTHDVSEAIALADHVLLLDDGAITHSLTVDIPGDRRTHPSFASYTAQLLEWLEITTPA", "text": "FUNCTION: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system (Probable). Is also involved in taurine transport. Seems to not be involved in long chain aliphatic sulfonates transport (chain length of eight carbon atoms or more). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Aliphatic sulfonates importer (TC 3.A.1.17.2) family."}
{"protein": "MTKVGLRIDVDTLRGTREGVPRLLATLHRHGVQASFFFSVGPDNMGRHLWRLIRPRFLWKMLRSNAASLYGWDILLAGTAWPGKNIGNANAGIIRETATYHETGLHAWDHHAWQTHSGHWSIRQLEEDIARGITALEAIIGKPVTCSAAAGWRADGRVVRAKEPFNLRYNSDCRGTTLFRPLLMPGQTGTPQIPVTLPTWDEVIGPAVQAQSFNTWIISRMLQDKGTPVYTIHAEVEGIVHQPLFEDLLVRARDAGITFCPLGELLPASPESLPLGQIVRGHIPGREGWLGCQQAASAS", "text": "FUNCTION: Catalyzes the deformylation of 4-deoxy-4-formamido-L- arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose- phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily."}
{"protein": "MFSIPVSSKTVRLILVSLLLITLINILAAFQRSTLSSWFPSSRHIINKFTDLRLALSSQESVLRDEEGEIYSLVGYHHDFDSNLVVVQKQYLLEKTPNEDTTEHFWNFLQSNFETKSEYDLNLIDGYNYKKLIKHLNEQNELQLSHSFVEQYKMENQFIQSFQNFFVQLIDTIEDCKPDLDPINNDNHYPNGDKIVKYYELRNKIPSENMKQFNIERLIHRNGRIPIYGGHLREQYKDELIRNKEFLSMYLTLSDSEISALKKSHTKFLETMMENWPENLFKFNKFNNFMKGDGIVYLGGGKYNQLVLLSIKILRENGSRLPVEVIIPYKNDYDIQFCDRVLPTLNGKCKLMTDYLPQTFVDKISGFQLKNIALLISSFERILYLDADNIPIRNPDVLFTNAPFTTKHLVVWPDLWRRSTSPHYYTIAGIEVDPNFKVRNSYVDGDERGKYTDSMYYSYHDCKGSIPEASSETGQLLINKKIHFQTLILAMYYNYYGPDYYYPLFSQGAAGEGDKETFIAAAHKLDLPYYQVGEFNREFGPINDNTRKHEFYGMGQYDPIIDYYMSTITTTQKDTKKKINYNSPLPEKYAANDEDDTCSNYDFHLFQSSSLFFLHANWPKYYIEKLFLYSYDEDRGPVTNDGDKRRLYGNELKKELGGYDFELNIMKNLHWCFCEEPLIDLIGIPVVGSKTRTDVCIAIKNHIEFLEIS", "text": "FUNCTION: Alpha-1,2-mannosyltransferase required for cell wall integrity. Responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides. Addition of alpha-1,2-mannose is required for stabilization of the alpha-1,6-mannose backbone and hence regulates mannan fibril length; and is important for both immune recognition and virulence. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the MNN1/MNT family."}
{"protein": "MEKCSVGGLELTEQTPALLGNMAMATSLMDIGDSFGHPACPLVSRSRNSPVEDDDDDDDVVFIESIQPPSISAPAIADQRNFIFASSKNEKPQGNYSVIPPSSRDLASQKGNISETIVIDDEEDIETNGGAEKKSSCFIEWGLPGTKNKTNDLDFSTSSLSRSKTKTGVRPFNPGRMNVAGDLFQNGEFATHHSPDSWISQSASFPSNQKQPGVDSLSPVALLRKQNFQPTAQQQLTKPAKITCANCKKPLQKGQTAYQRKGSAHLFCSTTCLSSFSHKRTQNTRSIICKKDASTKKANVILPVESSKSFQEFYSTSCLSPCENNWNLKKGVFNKSRCTICSKLAEIRHEVSVNNVTHKLCSNHCFNKYRLANGLIMNCCEHCGEYMPSKSTGNNILVIGGQQKRFCCQSCINEYKQMMETKSKKLTASENRKRNAFREENEKQLYGSSNTLLKKIEGIPEKKEKTSQLQLSVECGTDTLLIQENVNLPPSSTSTIADTFQEQLEEKNFEDSIVPVVLSADPGTWPRILNIKQRDTLVENVPPQVRNFNFPKDNTGRKFSETYYTRILPNGEKTTRSWLLYSTSKDSVFCLYCKLFGEGKNQLKNENGCKDWQHLSHILSKHEESEMHVNNSVKYSKLKSDLKKNKAIDAAEHRLYENEKNDGVLLLYT", "text": "FUNCTION: Functions as a transcriptional regulator. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDKLVDNFLSGQSRTMSEDLLSASSPQLCYENLNGSCIRSPYSPGPRLILYAVFGFGAVLAVCGNLLVMTSILHFRQLHSPANFLVASLACADFLVGLTVMPFSTVRSVEGCWYFGDTYCKFHSCFEGSFCYSSIFHLCFISVDRYIAVSDPLIYPTRFTASVSGKCITFSWLLSIIYSFSLLYTGANEAGLEDLVSALTCVGGCQIAVNQSWVFINFLLFLVPTLVMMTVYSKIFLIAKQQAQNIEKMSKQTTRASESYKDRVAKRERKAAKTLGIAVAAFLLSWLPYFIDSIIDAFLGFITPTYVYEILVWIAYYNSAMNPLIYAFFYPWFRKAIKLIVTGKILRQNSSVTNLFPE", "text": "FUNCTION: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MALYIIFLLIASSFILFSFIFSQKPKGKLPPGPPKLPIIGNIHQTVGGLPHYVFRDLAKKYGPIMHLQLGQVSIMVVSSPRLAEEVLKTNDIVVANRPYSLVGDIVLYGSSDVAFGSYGDYWRQMKKIMTVEVLSAKKVAAISGTRQQEVNNLMEYIRSTCGKPFHVREHVMQRNNNIICKSLFGDNCKQQHVLIESLDEMMKLSTGFNVSDLFPNWGFLPVISGYKSTLTRIHKNIDSILSEIFEERKIKRQKGGASDEDMLDVLLNIKERGGLEFPVADNNIKAIFVNMFVGGTDTSVATIEWAMTELMRNPKVMSKAQAEVRQLFKGKNTILDKDLQDLVYLKYIIKETLRLHPVVPILLPRECRGPCKIGGYDIPMNTVLFVNAFACSTDPEYWDDAESFKPERFENSSLDLNGRACEYLPFGAGRRMCPGITFGMSVVEIILAQLLYYFNWELPNGLSPNDIDLTPNFGAVADKKVPLQIVPTLNSLK", "text": "FUNCTION: Probably involved in the biosynthesis of germacrene-derived sesquiterpene lactones. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MRLQRQCIVVNMRSAIVLIMIFVLTGIRNSETASGGNQMDLSDSKGDHKDNSNASNGNGNANDNEVYVPPLVSSMVAKSGGGAGGLLDNITAYSSSSSSSSSNGNNNMLCPYDKETPCDRLQFPCIRCNYNHGCIYGRDLNVTCEVINNVQCLGERSFQRQMNCRYCYQTEMWQQSCGQRSSCNSATDKLFRTNCTVHHDVLCLGNRSFTRNLRCNWTQGYRWSTALLISLTLGGFGADRFYLGHWQEGIGKLFSFGGLGVWTIIDVLLISMHYLGPADGSLYI", "text": "FUNCTION: Involved in the control of cell fates in the neurectoderm. Acts as a positive regulator of Notch pathway and is required at different levels during development. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TM2 family."}
{"protein": "MGSTSSLYAAIDLGSNSFHMLVVREVAGSIQTLTRIKRKVRLAAGLNSENALSNEAMERGWQCLRLFAERLQDIPPSQIRVVATATLRLAVNAGDFIAKAQEILGCPVQVISGEEEARLIYQGVAHTTGGADQRLVVDIGGASTELVTGTGAQTTSLFSLSMGCVTWLERYFADRNLGQENFDAAEKAAREVLRPVADELRYHGWKVCVGASGTVQALQEIMMAQGMDERITLEKLQQLKQRAIHCGRLEELEIDGLTLERALVFPSGLAILIAIFTELNIQCMTLAGGALREGLVYGMLHLAVEQDIRSRTLRNIQRRFMIDIDQAQRVAKVAANFFDQVEKEWHLEAISRDLLISACQLHEIGLSVDFKQAPQHAAYLVRNLDLPGFTPAQKKLLATLLLNQTNPVDLSSLHQQNAVPPRVAEQLCRLLRLAIIFASRRRDDLVPEMTLQANHELLTLTLPQGWLTQHPLGKEIIAQESQWQSYVHWPLEVH", "text": "FUNCTION: Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily."}
{"protein": "MTEPTLNFHIQTHQNQFKIPHELIKKNFKLIQKLIEKQRKQLIDDISKIKKCKTTSPSFKLELIQKLIKNFESFMKKLQNFINKDEEFRSRLIARLENLTELQQYVITNNDNQEGQNHEESTENNNNNRNNNNNSTTTDDDKLLDFHNPNLINWYRDQTNLLIVDYLIKSNTRTRFEDNGEDNPGNIGLLLLKNLTKTNPKLLKLIDYDLLENFNKVFVSIINNHDLSLIVGWFNENKNLLNKINSNLEFEINYCKFLTLIEKGDINEAINYSRENLSGYGNKENYQQTNNNNNNTFSNGDTTSTNHLTNLERLKGLGGLLVFRSMENNNKNNNDLNSNDTPLSSKLMLNSTPFKEYQKLLSNERWESLAQCFIENFTKLYGISKNFPIYIYLSAGLSSLKTKSCYHNVENTIFKHSTGNGIDYDNGNDDYDDDDDDDDEGGVIDSNLSFISAETTTNTNTTSNSGKSLLNDPKYRGPNHYYKLLNKINNCPICSPELFKLSQNLPYAQLITSIFNNPFKLPNGNIYPFDKLLAPTDKYLSEKNTLLRANKVKDPLTREIFTIDSCIRVFPA", "text": "FUNCTION: Involved in the proteasome-dependent degradation of fructose- 1,6-bisphosphatase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the FYV10 family."}
{"protein": "MCDLVARTGRLQQRYEDGSRLVAGCIPFRYVNSDKDGNSESGKVIQVLMISSSSGPGLLFPKGGWENDETVREAAAREAVEEAGVRGILMDFLGNYEFKSKSHQDEFSPEGLCKAAMYALYVKEELATWPEHETRTRKWLTIEEAVESCRHPWMKDALVEGFCKWHKEKMVKGEEITGEH", "text": "FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MKFTLSTVTKCSGRLGVLGGLDRLPNLSLQTPAFIFHTKGGSIPHLSKEAMQHVSGDPSCFLHLSISNTLHMQEAIKASRITIAEFIAQSNCATLLFVRDPSEPPIPGLPEKDSLPIYTRNGRRNITLEQYMTLVETFRPDAYVPLYDGDTDASSSKKRDQKSLDRTEKFVEQCLEWHRKSDALQSSCLIGPVVGGYNEKLREQSVAFLRQSDDAFAGYLIEGLHMHGPSVARMDGSAALGIVANVCKQLPEAKVRLCFGSYDPALVLEMVAAGVDVFDTSYVYLKAAQEHRALVFSFDVTSTEQEHVTELDTTDARWAEDFGPLLPGCKCYTCQKHSRAYVHHLHNTREMLGPILLMMHNLHHYVEFFKAIRHHVANDSLPELRNHLAGQKSLPPYEPPKEEKLPMPAAQKAELMEPMEDLGEKQNKKQRA", "text": "FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily."}
{"protein": "MSADGIGMASRRSSGPWLVLVLALLVLQAAILFAMGRLPICACGTVKLWHGVVQSSENSQHLTDWYTFSHIIHGFLFYALTALVVPLLPWQGRLIIAMLIEGAWELVENSSFIIERYRAATISLDYFGDSVVNSIGDTLAMITGFLLARVLPIWLTVLIAIAFEIGVGLHIRDNLTLNILMLIYPTEAIRQWQAGPPLL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0314 family."}
{"protein": "MEAVLTKLDQEEKRALQDFHRCAWEETKNIINDFLEIPEERCTYKFNPYTKKMELLFTPEFHTAWQEVPECREFILNFLRLISGHRVVLKGPIIVFTKEVKNLGIPSTINVDFQANIENMDDLQKGNLIGKMNIKES", "text": "FUNCTION: Plays a role in the inhibition of the host innate immune response. Mechanistically, promotes the autophagy-mediated lysosomal degradation of host TBK1 and affects IRF3 nuclear translocation to block type I IFN production. SUBCELLULAR LOCATION: Virion Host cytoplasm. SIMILARITY: Belongs to the asfivirus A137R family."}
{"protein": "MKRGSVALFAISFFAFGWMTHALYNDAYKMIKESTLKKIKKSGALNVVLLNAPSTYYIGSDGPKGFEYDLLESYANHLGVKLNITTANTIKEALELSKNPDIHITSASLTKTPEREKEFNFGPSYFEAQEQVVCNKSLLLDGRFPSDADSLSGLRVVVGDSTSYSETIESLKKEGFDINATYTAEYSTEELISQVDTHEIDCTIIDSNIYALNQRYFKNIVLAFDISNRRQQAWILTPDSKMLKNDMYSWLNTVNQSGEMARLKDHYYSYVLFFDYYDTVMFYKRIKTRLPKYESYFKEAAVKYEIPYSALAALSYQESHWNPNAVSYTGVRGLMMLTQDTASMLGVKNRIDPQESIFGGAKHLDQMIKSVHADVTGEDRLKFALAAYNVGLGHVADAQKLAQQLGLNQNSWADLKKVLPMLSQKKYYRTLKHGYARGNEAVKYVDAIYDYRDILQKNDVEVSLTTK", "text": "FUNCTION: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein. Note=Attached to the inner leaflet of the outer membrane. SIMILARITY: In the C-terminal section; belongs to the transglycosylase Slt family. SIMILARITY: In the N-terminal section; belongs to the bacterial solute- binding protein 3 family."}
{"protein": "GYKVTYFAIRGLAEPIXLLL", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SIMILARITY: Belongs to the GST superfamily. Sigma family."}
{"protein": "MFNWAKQQLANVAGTQEPIYGPSAIKSVAIEAEKTPYTEVTRDGLKWKAMDSTSVETESFYITADNGYIALAQVIYSNVAGIRTTCQFNCKVFDKDPTKPHLWASTPLNNQDFNEDKTSFYADDCAVELSEDGTYYTIKSMNSQDAIVNLKITRSTPGFQAGTTGTTLYGTDHNNPWGSIRHAFWPRCVSEGTITTKEGPIDLKGKALFVYALQGMKPHHAAGRWNFVNFQGPTYSAIMMEFTSTPSYGSTLVNVGGIVKDGEIIHAGAMSTATHTQVKKDSENEWPEPSEVKYTWSGATKDAKPVEASIEGPLGERVDRVDVMAEVPGFVKTIVAAAAGTKPYIYQYHPKLSLKLKIGDEEIVEEGVMFTEATFIS", "text": "FUNCTION: Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein Endoplasmic reticulum membrane; Peripheral membrane protein Cytoplasm Nucleus Note=Localizes to the interface between the cis-Golgi network and endoplasmic reticulum exit sites. SIMILARITY: Belongs to the SVF1 family."}
{"protein": "MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPSGLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFIDKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYATRDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVAAKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPGSEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL", "text": "FUNCTION: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the paraoxonase family."}
{"protein": "MDFEDDYTHSACRNTYQGFNGMDRDYGPGSYGGMDRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGGGSRFGPYESYDSRSSLGGRDLYRSGYGFNEPEQSRFGGSYGGRFESSYRNSLDSFGGRNQGGSSWEAPYSRSKLRPGFMEDRGRENYSSYSSFSSPHMKPAPVGSRGRGTPAYPESTFGSRNYDAFGGPSTGRGRGRGHMGDFGSIHRPGIVVDYQNKSTNVTVAAARGIKRKMMQPFNKPSGTFIKKPKLAKPMEKISLSKSPTKTDPKNEEEEKRRIEARREKQRRRREKNSEKYGDGYRMAFTCSFCKFRTFEEKDIELHLESSSHQETLDHIQKQTKFDKVVMEFLHECMVNKFKKTSIRKQQTNNQTEVVKIIEKDVMEGVTADDHMMKVETVHCSACSVYIPALHSSVQQHLKSPDHIKGKQAYKEQIKRESVLTATSILNNPIVKARYERFVKGENPFEIQDHSQDQQIEGDEEDEEKIDEPIEEEEDEDEEEEAEEVGEVEEVEEVEEVREGGIEGEGNIEGVGEGGEVGVVGEVEGVGKVEEVEEETAKEEPADFPVEQPEEN", "text": "FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus matrix. SIMILARITY: Belongs to the AKAP95 family."}
{"protein": "MGEPEPVVALTEDAPLSVYNPNYRSDNALIADGDSSPIGGDCCPAEAVAAAEEVATAALASEEIYEMHIKSCISSTTCGDHNNSIGVTSGLTVRAAECHPPSPEAVGIEDVVVVQTAATTNGPSDTVPASAAASVISDDNGCVPLLGSRLELENYDLESGCYYSESDNETASLFIQRVGRRQARRHRRRRVALTVAGVVLVAVLCAISGIVGAFLARVFQ", "text": "FUNCTION: Essential for the anterograde spread of the infection throughout the host nervous system. Together with the gE/gI heterodimer, US9 is involved in the sorting and transport of viral structural components toward axon tips (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Host Golgi apparatus membrane; Single-pass type II membrane protein Host smooth endoplasmic reticulum membrane; Single-pass type II membrane protein Host cell membrane; Single-pass type II membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN), maybe through an interaction with PACS-1 sorting protein. SIMILARITY: Belongs to the alphaherpesvirinae envelope protein US9 family."}
{"protein": "MSLQMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPSPQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSREAMHMPTTMEDFEMALKKISKSVSAADIERYEKWIVEFGSC", "text": "FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. SUBCELLULAR LOCATION: Cytoplasm Midbody Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, spindle Note=Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily."}
{"protein": "MTAPWVALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLPPKESSI", "text": "FUNCTION: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin- A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily."}
{"protein": "MEEPAAKRPKLSDRSEPLTQRDVVLFQKEALFRQLNRYRAEARAGQVQVEELRRAHGQVGERLAAVCGVVRSVARAVADARGDGDARALCERVAGGDDDEVVARAAEFAAVVAGGLGRGAAAGEGWHRLEAVNSRLAAENAQLAAELGAVRGFYAELLRRYDRDESETVRRVFKVEESEPPRAATPVEESSAKGAASDGEAATAVVEREMQIEELQTEIRVLEDTVAQLTDWKRLNEQELTKLRQMASSAELSQRHPTPPSSSNLSADLQVLRSKVEKLSHENKELAQLNEAYLGKFQQLSADREIFNNRLSAEFQTAQETLKKHNSNLEKDLVRIRTARDELLSKVAVLEAQKSKSDMLEDLEKMLALQQEQLKALSEHKPEPARDAVMKELQDLEKAFKELSQYSNKKYSEYVNQESLMSKLTVEKTKADQKYFAAMRSKDSILIENKNLSKNLSKSNELIQQLKDIEKSLQAKIENLNKQLHISRINEKRLLDSNKTTSLKIMDLTSQLSKANKSSTLVQQECNKLIEEKAKMESKLNDLEIETKNLATKLTYQENKSKKLHKTLVSNGGDNGALAEELENFRTVVYCSLCSKNWKDTVIKTCGHVFCADCCKERLAARMRKCPTCNKGFSSNDLLVVHL", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BRE1 family."}
{"protein": "MEKKIIFLCFLVALLTFPEFISSEVIRDSVIHDEEKFANRSYCIKTCATEFTGGDESRIKDVRPRHYKCVCWYYSD", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-15 family."}
{"protein": "MVSEMTPTRRVMAAVLGGRVDYVPPANPLAQTTTELMQICNASWPKAHFDSKMMADLAAAPYEICGIEAARPQFDISLEAEVLGCKLDWNKPDRPPVTGPAYTDPADITWPDNLEEAGRIPVVLGAIEELRKRYDGMLPVIPVLTSPFTVAGHIAGVENLVRWTKTDPEKAHAFIEAATDFVIAYGKLQTAYGAHILFPADPSASGDLISGETYKEFVLPAHKRMAKEISCPLILHICGDTSKLLPYIKQSGIDCFSFDAVPVWYCRQVMGNEMSILGSLDVIDLMPNGTPEQVYNRTRECILQGADIVGTACDVSFGTSLENLRAYVRACKETPIPKYDDVEDIIRQIGVGIGRNMKENVLGGMQK", "text": "FUNCTION: Methyltransferase involved in methanogenesis from methylated- thiols. Catalyzes two successive steps: mediates the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated- thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to coenzyme M. SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family."}
{"protein": "MSIHEELVKVRESVWEVPTSYKKGMRVPGRIFLREEALRDLEKGAIDQVANVACLPGIQKFSIGLPDIHFGYGFSIGGVGAFSARTGVISPGGVGFDINCGVRMVRTNLDHEDVRPKIKELINTLFTNVPSGVGSKGKIRLKPGEIDEVLENGAEWAVENGYGWDQDLRRLEENGKMEDASSEKVSEKAKKRGIPQLGSLGSGNHFLEVQMVDEIFDEEAARVYGVSPGKVAVMIHSGSRGCGHQICSDYLRLMDKAYRRYKINIPDRQLACAPVDSDEALDYFQAMAAAANYAWANRQMIVHWVRESFEAVFGMTAEDMEMEIVYDVAHNIAKKEVHTIKGRETEVFVHRKGATRAFGPGRDEIPQEYRKIGQPVIIPGTMGTSSYLLHGTEVAMEETFGSTAHGAGRKMSRAGAKKTYRGEEVQRKLESEGIYVRATSMPVVAEEAPGAYKDVDVVVRTAHETGISRLVARMLPLGVAKG", "text": "FUNCTION: Essential for tRNA splicing and maturation. Acts by directly joining spliced tRNA halves to mature-sized tRNAs. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. SIMILARITY: Belongs to the RtcB family."}
{"protein": "MLSEASDFNSSGSRSEGSVFSRTEHSVIAAYLIVAGITSILSNVVVLGIFIKYKELRTPTNAVIINLAFTDIGVSSIGYPMSAASDLHGSWKFGHAGCQIYAGLNIFFGMVSIGLLTVVAMDRYLTISCPDVGRRMTTNTYLSMILGAWINGLFWALMPIIGWASYAPDPTGATCTINWRNNDTSFVSYTMMVIVVNFIVPLTVMFYCYYHVSRSLRLYAASDCTAHLHRDWADQADVTKMSVIMILMFLLAWSPYSIVCLWACFGNPKKIPPSMAIIAPLFAKSSTFYNPCIYVAAHKKFRKAMLAMFKCQPHLAVPEPSTLPMDMPQSSLAPVRI", "text": "FUNCTION: May play a role in rpe physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MGFWKFLPFLVLSFLVVYQAGMFQAAPFRSALENDFDPAILTEKEMCLLLAAVMNDYVQMKTSELKQEAEHFHITAQKRSCNRATCVTHKMAGSLSRSGSEIKRNFMSTNVGSKAFGQRSRDLQK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calcitonin family."}
{"protein": "MSEKQTIKALPAHNPTQVKKLGPVSGFLSGGLAACGAVTLTNPFEVIKTRFQLQGQLTKLDPSKRIYKSVGQAFSLIARHEGIRGLQRGLGTAYVYQICLNGCRLGFYEPIRRTLNTWFLDDPKGNKLAINVASGAGSGLCGALFGSPFFLVKTRMQSYSPKFPVGQQYGYKHIFNAFSRIIKENGVKGLFVGADAAILRTVSGSSVQLPIYNWAKRMIEHYNLLEEGMIKHLTASAVSGFGVCCTMQIFDTVMTRMYNQKNKELYKNPIDCILKTIRSEGFFALYKGFGAHLARIAPHTIFCLTFVEQTNKLFLKFQKD", "text": "FUNCTION: Transports oxaloacetate and sulfate. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MDTARVYFGLKPPRTPGAWHESPPSLPPDACRCPRSHRLALKLSCAGLILLVVTLIGMSVLVRVLIQKPSIEKCYVLIQENLNKTTDCSAKLECPQDWLSHRDKCFHVSHVSNTWEEGLVDCDGKGATLMLIQDQEELRFLLDSIKEKYNSFWIGLRYTLPDMNWKWINGSTLNSDVLKITDDTENDSCAAISGDKVTFESCNSDNRWICQKELYHETLSNYVGYGH", "text": "FUNCTION: Plays a stimulatory role on natural killer (NK) cell cytotoxicity. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein."}
{"protein": "MAALCRTRAVTAESHFLRVFLFSRSCRGAGTESGSGSESSNSTEPRPRPGGFASALERHSELQRKAELARTRGSPKNVESFASMLRHSPLTQMGPAKDKIVIGRIFHIVENDLYIDFGGKFHCVCKRPEVDGEKYQKGTRVRLRLLDLELTSRFLGATTDTTILEAEAVLLGLQESKDSKSKEERRENK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family."}
{"protein": "MGGIIKLSFLFCSLISLVNSENTGKLPTAISDHSVPKATATTDPSVFVLSNDFEITDVPTTREYTFNLTEALASPDGYERLVYAVNNMLPGPVIEANTGDTVIVHVNNYLHEGQGIHWHGLRQNGTALMDGVPGITQCSIPPGGSFTYQFTVSHQSGTFWWHSHYSNSMADGIWGPLIVHSPNEPLQRGRDYDEDRIVAVTDWMHDESETIVEALISSEGYRGRPFPPQGDAILINGRGQTNCTATGSPSCTYPPPPEIHVPVNCRVRLRFISAASHPMYRISIDNHSMEIVETDGTAVYGPTIHEISISSGERYSVIINTTEGKEGDAFWLRTSVALDCMAQGVTQVGLAVVRYTGNGSITTAEPRTEAWTDLARPDTPCVGLDEMYHLSPRELVNASQTALESRVLDSKLGKFVDVYGNSFEGYGFNNVTYQNQINDPLLYVVQRGGTCNSSLIANATFADIGPVNIIINNLDSHIGHPYHMHGTEFQLMGRGTGALTLDDLPNTNLTLDNPTRKDTIWMQGGSWALLRIISDNPGVWALHCHIGWHLAKGKMAVVVVQPEAIKKIQWPESWMDLCANTDPNAFGPARRSVS", "text": "FUNCTION: Laccase that catalyzes the oxidation of certain aromatic compounds, including L-dopa, to quinones, which then polymerize to melanin (By similarity). Able to oxidize a wide variety of aromatic diphenol and diamino groups in the ortho, meta, and para positions but not monophenolic groups such as in phenol, tyramine, or tyrosine (By similarity). Plays an important role in virulence (By similarity). Plays a role in dissemination to extrapulmonary sites but is not involved in pulmonary growth or in elicitation of cellular immune responses in the lung (By similarity). SUBCELLULAR LOCATION: Secreted Secreted, cell wall. SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MTHPVISLKPSYNSVIRGCPGLPDTLPRIECQLRVRSNNSLPFKLVKIEIVLKTIEIYFNKNLYSSNNSSFTPFNRPSDPSNGHSDTSNQNISIHYKKNIVLSHPTHDGDDLNNDLIGIDIPLTIGLPDDIKETNYNPKFGKTQTFLDCTVFYTEVGGGSSNKKRNFLYPVNVERYTYLPSPSYFRPINRSNITSPDQKFLISYSIENPCVSMNNDTLKLSISIRLNPFPNNATTPSSNDFDVSTPTLFSTKKKFKSKLKLKSITTQILEYLEILKNQSEFSSTQTTNILQTSVRQVDQIISMNSMIFQFNLKIFTKDKILQSFRSSESSCPETKVLINKIDDIPLQYHSSITTIGQHFNVSHYLSIRFKFNKSLKNFEINHPLIISFWSVSQLPLIENLILQERQTAKFAKKFYKNFGRIKNTSNNNNSSNCLEYPSLPPIIYNFNDPETNNRFNILYSQKDPSRTDPSKLRRVPVIQ", "text": "FUNCTION: Regulator of RHO1 signaling that acts as a cofactor required for the efficient localization of the TUS1 GTP exchange factor (GEF) for RHO1 to the bud neck during all phases of cytokinesis (PubMed:22344253). RHO1 is a key, essential hub protein in the cell wall integrity (CWI) pathway in which activated RHO1-GTP binds directly to and activates multiple different downstream effectors required for cell wall synthesis and actin assembly during cytokinesis (Probable)."}
{"protein": "MAKQYDVLFRLLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGVDFKMKTIDVDGIKVRIQIWDTAGQERYQTITKQYYRRAQGIFLVYDISSERSYQHIMKWVSDVDEYAPEGVQKILIGNKADEEQKRQVGREQGQQLAKEYGMDFYETSACTNLNIKESFTRLTELVLQAHRKELDGLRTRASNELALAELEEDEGKPEGPANSSKTCWC", "text": "FUNCTION: May act in concert with RAB3A in regulating aspects of synaptic vesicle membrane flow within the nerve terminal. EHBP1L1. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MASWEAQEELRELLHHLPEDDPPADLTHLLELDEMEPKVLCGENPGDEKLKKQVIKTPPMHPSTVTWHFGYKQKEDQQDNIKMRDWVPDPSKMSKSTCKRLILLGLYQACKAQEIIKMDYDVHWEKSVVNEQYFEVEYNCKMCRTVLHEPMPIMYDPETELWVKPGRLRGPLGSAVYTLKKHYERCLLTLPSLKGTRLPKRRCNPSRRYETFREHPPTRKRRSKEGIPTDQQPSTSNGDPMALLSGPCGPHSIQPPSCLLQELPKPEVGSPEMAVAMSGGPFWEEVYGDSIFATPLGSSEDQLLSQFD", "text": "FUNCTION: Transcriptional transactivator that activates the viral internal promoter (IP), thereby enhancing its own expression. This transactivation is repressed by nuclear factor I. Also transactivates the long terminal repeat (LTR) promoter, thereby inducing structural gene expression, initiating the late phase of infection. It is therefore a key regulator of viral gene expression. It directly binds to and activates DNA target sites of viral promoters and those of distinct cellular genes. Required for viral replication (By similarity). SUBCELLULAR LOCATION: Host nucleus."}
{"protein": "MIATGGVITGLAALKRQDSARSQQHINLSPLPATQDQKPVRRRPRADVVVVRGKIRLYSPSGFFLILGVLVSIIGIAMAVLGYWPQKEHFIDAETTLSTNETQVVRNQGGVVVRFFEQHLHSDKMKMLGPFTMGIGIFIFICANAILHENRDKETKIIHMRDIYSTVIDIHTLRLKEQKQANGLYAGLLGDTEVKQNGSPCASRLAATTLASFSGMRNSFRVDSSVEEDELMLTESKSLGHLMPPLLSDSAVSVFGLYPPPAKATDDKASSSKKCDTKSIVSSSISAFTLPVIKLNNCVIDEPSIDSITEVADNLKTRSRNLSMDSLVVPLPSSGESFQPAVTLLPRNNSVGESLSSQYKSSVALGPGTGQLLSPGAARRQFGSNTSLHLLSSHSKSLDLDRGPSTLTVHAEQRKHPSWPRLDRSNSKGYMRLENKEDPMDRLLVPQTAIKKDFTNKEKLLMISRSHNNLSFEHDEFLSNNLKRGTSETRF", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM200 family."}
{"protein": "MSRLNIFLLIIVMGCALSVVNSTNQQRQIFIQLQRAQSQEHQLQQDYAQLQYQQSALSKTSRIEQLATSSLKMQPITTGRTQYLTLSPGAAKAVDVPLPASAAPTGGAR", "text": "FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum where it forms a ring structure. SIMILARITY: Belongs to the FtsL family."}
{"protein": "MILEMLNPMHYNLTSMVPEVMPVATLPILLLTGFLFFVWNHEETSSIPGPGYCMGIGPLISHLRFLWMGLGSACNYYNKMYGEFVRVWISGEETLVISKSSSTFHIMKHDHYSSRFGSTFGLQYMGMHENGVIFNNNPAVWKALRPFFVKALSGPSLARMVTVCVESVNNHLDRLDEVTNALGHVNVLTLMRRTMLDASNTLFLRIPLDEKNIVLKIQGYFDAWQALLIKPNIFFKISWLSRKHQKSIKELRDAVGILAEEKRHRIFTAEKLEDHVDFATDLILAEKRGELTKENVNQCILEMMIAAPDTLSVTVFFMLCLIAQHPKVEEALMKEIQTVLGERDLKNDDMQKLKVMENFINESMRYQPVVDIVMRKALEDDVIDGYPVKKGTNIILNIGRMHKLEFFPKPNEFTLENFEKNVPYRYFQPFGFGPRSCAGKFIAMVMMKVMLVSLLRRFHVKTLQGNCLENMQKTNDLALHPDESRSLPAMIFTPRNSEKCLEH", "text": "FUNCTION: A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19- aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid. Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Converts dihydrotestosterone to delta1,10-dehydro 19- nordihydrotestosterone and may play a role in homeostasis of this potent androgen. Also displays 2-hydroxylase activity toward estrone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH- ferrihemoprotein reductase). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Microsome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MATTTGAKRGIWPMIRRIAASDRISGLIMLGFALAGLVLANLPLTAHAFEAVAETHVFIPHTNLDLPIGHWAQDGLLTIFFLTVGLELKQELTTGSLANPKAAAVPMLCAVGGMITPPILFLATTALFSQFGPGEPGSLILATTGSSIPFAEMSHGWAVPTATDIAFSLAVLALFAKALPGSIRAFLMTLATVDDLLAIILIAVFFSSVNAWYWFIGIAVCAVVWAHLVRLKKVPWIAVGVVGILAWIMMFEAGIHPTLAGVLVGLLTPARVMHGEYSPRAERYADKLKPFSALLALPIFALFATGVHFESMSPLLLLSPLVIALIVALVVGKPLGIIVTAWLATHVGGLKMAKGLRVRDMIPAAVACGIGFTVSFLIASLAYTNQELSAEARFGVLVASLIAAAISGVLLSRQSKRFEQAAAVAAAEADAESDVNTHSDELAEHSITLADGTESVEIDFRR", "text": "FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family."}
{"protein": "MDKSSGLDFINQMFPVEASLSCVESFMQKICDEIRRVDATILAVVSQQGNSGTRAKENLNDAICAAEELSHKIQEIKSKAEQTEAMVQDICSDIKKLDFAKKNITTAVTALSRLTMLVSAVQQLQVMTSKRQYKEAATQLEAINELCNHFKAYMDLPKIMELREKLKNIKQILKFHVFSDFSSLGTGTETEELFLLKKLSDSCLVVDALEPSVREELINNFCSRELTSYEQIYVGAELKTLDEIELIYNQLSCLIRKNQGKWTIFPASWHVPYRLCIQLSRKTRVQVESILVNLKEKSDVEKLLLELKRTLEFERELEMKFGGGGSIGDDIIGGGGNNSQKFNFRGMISSCFEPHLTIYIEKEEMELMQLLEKVVQEETWDIEEELGCHSENSVYLMLLDAHDMKMILLKVPSLARQPEASALLVKTATASYVKLVNHQMKRAEAVLKVIASPIVTVIDTYRALFPEETPMEFQRILVLKGLTKAEQQSILDDFNNHSSRITQLSVAAKTPEAHALPLALTNVAPAVRFKANSEEVLTRAASAATTSFMKLYALTGAAKDRPFRKLFNP", "text": "FUNCTION: Involved in retrograde transport from early and late endosomes to late Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the VPS53 family."}
{"protein": "MFSLRTAQPAQSLFRAATNTYSTSLPRSAIAARSFATVQSDIFKPTKYGGKYTVTLIPGDGIGTEVAESVKTIFKADNVPIEWEQVDVSGLDAGNKHSEDLFKESIASLKRNKLGLKGILHTPVERSGHQSFNVALRQELDIYASIVLIKNIPGYKTRHDNVDLCIIRENTEGEYSGLEHQSVSGVVESLKIITRAKSERIAKFAFSFALANNRKKVTCIHKANIMKLADGLFRSTFHKVAESYPTLETNDMIVDNASMQAVARPQQFDVMVMPNLYGGILSNVGAALVGGPGIVPGCNMGRDVAVFEPGCRHVGLDIKGKDQANPTALILSGSMLLRHLGLDEHANRISKAVYDVIGEGVTRTRDMGGQASTHEFTRAVLDKMESAL", "text": "FUNCTION: Performs an essential role in the oxidative function of the citric acid cycle. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family."}
{"protein": "MASLIYRQLLANSYAVDLSDEIQSVGSEKNQRVTVDPGPFAQTGYAPVNRGPGEVNDSTVVQPVLDGPYQPAPFDLPVGNRMLLAPTGPGVVVEGTDNSGRWLSVILIEPGVTSETRTYTMFGSSKQVLVSNVSDTKWKLFEMMKTAVDGDYAEWGTLLSDIKIYGMMKYGERLFIYEGETPNARTKGYIVTNYTSVEVRPYSDFYIISRSQESACTEYINNGLPPIQNTRNVVPLAISSRSIKPRKVQPNEDIVVSKTSLWKELQYNRDIIIRFRFDNSIIKAGGLGYKWAEISFKAANYQYNYISDGEEVTAHTTCSVNGVNDFSFNGGSLPTDFAISRYEVIKENSYVYVHYWDDSQAFRNMVYVRSLAANLNDVMCSGGDYSFALLVGQWPVMKGGAVTLHTAGVTLSTQFTDFVSLNSLRFRFRLSVEEPSFTITRTRVSKLYGLPAANPNGGREYYEVAGRFSLISLVPSNDDYQTPIMNSVTVRQDLERRLNELREEFNNLSQEIAVSQLIDLAILPLDMFSMFSGIEGTVNAAKSMATNVIRKFKSSKLASSVSMLTDSLSDAASSISRSTSIRSIGSTASAWTNISKQTQDAVNEVATISSQLSQISGKLRLKEITTQTEGMSFDDISAAVLKANIDRSIQVDKNALPDVITEASEKFIRNRAYRVIDGDEAFEASTDGRFFAYKVETLEEMPFDIEKFADLVTRSPVISAIIDFKTLKNLNDNYGITREQAFNLLRSNPKVLRGFMDQNNPIIKNRIEQLIMQCRL", "text": "FUNCTION: [Outer capsid protein VP8*]: Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. In some other strains, VP8* mediates the attachment to histo- blood group antigens (HBGAs) for viral entry. FUNCTION: [Outer capsid protein VP4]: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts. FUNCTION: [Outer capsid protein VP5*]: Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment. SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion Host rough endoplasmic reticulum Host cell membrane Host cytoplasm, host cytoskeleton Host endoplasmic reticulum-Golgi intermediate compartment Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple- layered particles. VP4 also seems to associate with lipid rafts of the host cell membrane probably for the exit of the virus from the infected cell by an alternate pathway. SUBCELLULAR LOCATION: [Outer capsid protein VP8*]: Virion Note=Outer capsid protein. SUBCELLULAR LOCATION: [Outer capsid protein VP5*]: Virion Note=Outer capsid protein. SIMILARITY: Belongs to the rotavirus VP4 family."}
{"protein": "MAKILTIVMLVFVSMAGWMFGADTGSIGGITNMRDFQSRYADRYDPVTDTYSYSSARQGLLVGMVNTGTTVGCLLSSPLGDRFGKRKCIMGWTLVYITGVIVQLTTIPSWVQMMVAKIWTGLGIGALSVIAPGYQSESSPPHIRGAIVTTYQLFITLGIFIAACINMGTHKYTTHPEAQWRVPIGINLLWGILMFFGMLFLPESPRYLAVKGRNEECMKILTRNAGLPADHPIMQKEYNAIQADVEAELAGGPCSWPQIFSNEIRYRTLLGMGVMAFQQLTGNNYFFYYGTQVFRGTGLNSPFLAALILDAVNFGCTFGAIFVLEYFGRRGPLIVGGVWQSICFFIYASVGDRALTRPNGTSNHRAGAVMIVFSCLFIFSFAQTWAPAAYVIVGESYPIRYRSKCAAVATASNWFWNFMISFFTPFISNSIGFKYGYVFAACNLCAAIIIFLFAKETKGLTLEEINQLYLSNIKPWNTGAYQRDREDIKQSDSEKERGPTSKLHEYVEHAPNSYASTHSTESENYPQQVTNPVGL", "text": "FUNCTION: High-affinity fructose transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MRAWIFFLLCLAGRALAAPQQTEVAEEIVEEETVVEETGVPVGANPVQVEMGEFEDGAEETVEEVVADNPCQNHHCKHGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI", "text": "FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane Note=In or around the basement membrane. SIMILARITY: Belongs to the SPARC family."}
{"protein": "MSGTLEKVLCLRNNTIFKQAFSLLRFRTSGEKPIYSVGGILLSISRPYKTKPTHGIGKYKHLIKAEEPKKKKGKVEVRAINLGTDYEYGVLNIHLTAYDMTLAESYAQYVHNLCNSLSIKVEESYAMPTKTIEVLQLQDQGSKMLLDSVLTTHERVVQISGLSATFAEIFLEIIQSSLPEGVRLSVKEHTEEDFKGRFKARPELEELLAKLK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL48 family."}
{"protein": "MAIHLVIIDALNLIRRVHSAQPDPTDIANTIQNTCRTLQRIISESHPTHIVAVFDHLGSDRGWRAEILPEYKQGRKPMPEPLLNGLEKIQDAWWQLGIDSLLSEGDEADDLVATLACKVAQHGEKVTIISTDKGYCQLLSPTLQIRDYFQHRWLDQPFIEQEFGVKPQQLSDYWGLTGISSSQVTGIPGIGPKAAKEILSQFDDIEQAFLSPDLPKKYRTKFDQHIELARRCKRVSALKTDIELGFNLQDLRFTANETH", "text": "FUNCTION: Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. SIMILARITY: Belongs to the Xni family."}
{"protein": "MKFGFIAHPTSLGLKRYVKMLDLLQRNSTEQHSGYTRELWERQNLVPFMNFARITSATGATCEGVIKYMPLVADEMLADARGIAARVVQGIEELAGDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLEIRPEEEPVAIVGYPGSICLALSRLLLAHGFSLHLLHRAGNHDRSELLSHLPEEYHSRVTLTSDPEDLYPRCKLFAAATSAGGVIDPARLQPGSIFIDVALPRDIASETRPARDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLAPEKVLEIGEIAERHGFFAYPLASYGERIDRQSVTNLKRYYHHDIYAGESADAALPASRLAFIDAVIAQTPAREDTLDRYHQYINPMMVDFLKLQRCDNVFRSAAGTQLYDDAGEAFLDMVAGYGCLNLGHNPQPVVNALKNYLDAQGPNFIQYISIPEQTAKLAEVLCRLAPGNMGRVFFSNSGTEAVEAAMKIAKASTGKPGIAYLRNSYHGKTLGALSITGRDKHRRYFTPLLDAMVEVPFGDLAALREALNREDVGALMIEPIQGEGGVHIPPAGYLQAVQQLCRETGVLLMVDEVQTGLGRTGKLFACEWDGIEPDVLMLSKSLSGGLIPIGATLCRADLWQKAYGTADRFLVHSSTYGGGNLASVVALSALREILAQDLVGHAERMGAYFKQALSEIAARYPFVSEVRGRGLMLGIQFDQAFTGAVNASAREFATRLPGDWHTTWKFLPDPVQAHLRAAMDRMEQALGEMFCMKFVTKLCQDHKILTFITANSSTVIRIQPPLIISKAEIDRFVGAFATVCEELSTFLD", "text": "FUNCTION: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transamination to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to yield the dihydro form of MAP (H2MAP). SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG", "text": "FUNCTION: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (PubMed:16118205, PubMed:17402747). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency (PubMed:16118205, PubMed:17402747). Cannot use triazofurin monophosphate (TrMP) as substrate (PubMed:16118205, PubMed:17402747). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (PubMed:16118205, PubMed:17402747). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively (PubMed:16118205, PubMed:17402747). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (PubMed:16118205, PubMed:17402747). Also acts as an activator of ADP- ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16 (PubMed:34314702). SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor Cytoplasmic vesicle membrane; Lipid-anchor Cytoplasm Cell projection, axon Note=Delivered to axons with Golgi- derived cytoplasmic vesicles. SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family."}
{"protein": "MAHSLGEQYDLGKPTEEHHESHPPAHQAPHAGGELGAGQKTSQLARSNSSSSSSSEDDGQGGRRKKPIKEKVKEKLPGGAGGKQTGECGTTTTTAAGGHEEKKGVMEKIKEKLPGQH", "text": "SIMILARITY: Belongs to the plant dehydrin family."}
{"protein": "MARMDFNNIVGDPFALIAWLLSFATCVISDIQGAFPNFAWWAVGYMLCAIIGISLVLASQTSHVYGVAIVGYLAAGLTFTTLAVNSLIYDDQASKQAGAAGFILQSMVTIVWIFYFGSSSQTSSRPYLDSMGAGKEHPSYRNSKPLSTNYGARPETVVSGNQPPQMYTSAQLNGFETSSPVSGYPPTAANGAENGTQNRFVGPAIGSQSNLGGGSTLGADHPSTPNEVSQPTVYPYRAKAIYSYEANPDDANEISFSKHEILDVSDVSGRWWQAKKASGETGIAPSNYLILI", "text": "FUNCTION: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SHO1 family."}
{"protein": "LPEQIDWRKKGAVTPVKNQGSCGSCWAFSTVSTVESINQIRTGNLISLSEQELVDCDKKNHGCLGGAFVFAYQYIINNGGIDTQANYPYKAVQGPCQAASKVVSIDGYNGVPFCNEXALKQAVAVQPSTVAIDASSAQFQQYSSGIFSGPCGTKLNHGVTIVGYQANYWIVRNSWGRYWGEKGYIRMLRVGGCGLCGIARLPYYPTKA", "text": "FUNCTION: Cysteine proteinase (PubMed:9836431). Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity (PubMed:9836431). Has little or no activity against synthetic substrates (PubMed:9836431). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MSLVACECLPSPGLEPEPCSRARSQACVYLEQIRNRVALGVPDMTKRDYLVDAATQIRLALERDVSEDYEAAFNHYQNGVDVLLRGIHVDPNKERREAVKLKITKYLRRAEEIFNCHLQRPLSSGASPSTGFSSLRLRPIRTLGSAVEQLRGCRVVGVIEKVQLVQDSATGGTFVVKSLPRCHMVSRERLTIIPHGVPYMTKLLRYFMSEDSIFLHLEHVQGGTLWSHLLSQAHPRHSGLSSGSTQERMKAQLNPHLNLLTPARLPSGHAPGKDRIALEPPRTSPSLPLAGEAPSIRPQREAEGEPTARTSTSGSSDLPKAPGGHLHLQARRAGQNSDAGPPRGLTWVPEGAGPVLGGCGRGMDQSCLSADGAGRGCGRATWSVREEQVKQWAAETLVALEALHEQGVLCRDLHPGNLLLDQAGHIRLTYFGQWSEVEPQCCGEAVDNLYSAPEVGGISELTEACDWWSFGSLLYELLTGMALSQSHPSGIQAHTQLQLPEWLSRPAASLLTELLQFEPTRRLGMGEGGVSKLKSHPFFSTIQWSKLVG", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. S6 kinase subfamily."}
{"protein": "MVKEKKKADKKGDKSARSPSSISDNPEASKQDSNASKQEVAPSAVVPVVETPLKQAPKRDSVQMEQSEEETQYEEPILTKLIVESYEGEKVRGLYEGEGFAVFQGGNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVYTWPDGSTYEGEVTNGMRNGFGMFKCGTQPVSYIGHWCHGKRHGKGSIYYNQEGTSWYEGDWVYNIKKGWGIRCYKSGNIYEGQWENNMRHGEGRMRWLTTNEEYTGHWEKGIQNGFGTHTWFLKRIPNSQYPLRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHIAQFFETEMDYSQSLDRWSDASQRSRQPRGSSVSAVREPETLRKLDGSESRSVLGTSIELDLTLLLDMYPEESQEEEKKQVEYAVLRNITELRRIYCFYSGLGCDHSLDNTFLMTKLHFWRFLKDCRFHHHNITLADMDRVLSVYNGIPIEEIHSPFRTILLRTFLNYLLQLAYYIHHKEFQNRSPSLFLCFTKLMSENIHPHACQVKGHLFSEQQRTLYSMNYIDKCWEIYTAYCRPNEAPPYELTMKMRYFLWMLKDFRMINKDLTATKFMTVIAEDNPFVYDGTDSNFELELVFLEFFEALLCFSLCCMFDQMTRSYLKVPYDDITTNRYGSTQTILNQSIHRSPSAITSHDSEVHFSSTKSSLDKIGALPDGKIRQSEPKLKKSLSEDKVSKMNFKTQGRGLVFMSPQGEKYEKPKDEQKEKLNIWVNNLYVFFVSVLFSAYKREEMLKEKVKENQLQEAELAQQRQIENEELEARLNILREEEARKQDFELDITVLKEPSEIPASQPLTPSPPKEDLASIQTSKASPGKKKKK", "text": "FUNCTION: May function as part of the axonemal radial spoke complex 3 (RS3) (Probable). Radial spoke complexes are important for ciliary motility (PubMed:34871179). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme."}
{"protein": "MDAEALRNLYLSSILPNESKTGNESPEKKFSSPVLLQRAKVIPLRLEYEERKLLHLLTAALDVSDYTDSVDTLSFSSPAKRLAQQLKGITAVLSGIMVAYDYKVGQELLEHKNFEQHAEFFKKIFEIGRRYKVLNPNRLGSTYGKLMYFVQDSMRPEIQDALGFNLFKPILTVYEFLNERDALNALEDPYAEIATMEIVAENRSRSAIQKDIKAKERAVEHIAKKYYSSKITKEKVRWCLYSIADSNSYLRYNRDPIAKLIGLVEAYFSPDTVDDEFTLAIDAINGSRLKHSHYKQYHYVVQSLHLWLLIMGEIFSLWALSDLELTNPDMEYKLIDNNQGIHRMQPCPNIRIAMERILRTAQEQSETWIGSSTIHLGDTAVPNALLFIDKYMQVPRILTPLVLLFKELDSLNDHSLLNYIDTAFGGREYLKKTILTDFMRFGFDGSGADNWFDAGSCIDGRLTSAWNWANNIHTKDYYRVLLMSGFLSFNGE", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the UPF0652 family."}
{"protein": "MSIREKLLMKKIVKREKMKKELSQKKGNKNAQKQEPPKQNGNKPSKKPEKLSKKHVAKDEDDDLEEDFQEAPLPKKKQQKQPPKKQQIQVANSDSESDDDEQEDEADEDSDLDEVAEVDEEDVDSGSEDDDQQEDEDEEEPVPAKKTKLLPNKSKAQNGKPAKDDEPFTVESSLAALDYRDSDDRSFASLKGAVSEATLRAIKEMGFTEMTEIQSKSLTPLLKGRDLVGAAQTGSGKTLAFLIPAVELINKLRFMPRNGTGVIIISPTRELSMQTFGVLKELMAHHHHTYGLVMGGSNRQVESEKLGKGINILVATPGRLLDHLQNSPDFLYKNLQCLIIDEVDRILEIGFEEELKQIINLLPKRRQTMLFSATQTARIEALSKLALKSEPIYVGVHDNQDTATVDGLEQGYIVCPSEKRLLVLFTFLKKNRKKKVMVFFSSCMSVKYHHELFNYIDLPVTSIHGKQKQTKRTTTFFQFCNAESGILLCTDVAARGLDIPQVDWIVQYDPPDDPREYIHRVGRTARGSGTSGHALLLMRPEELGFLRYLKAAKVPLNEFEFSWQKIADIQLQLEKLIAKNYFLNQSAKEAFKSYVRAYDSHQLKQIFNVNTLDLQAVAKSFGFLVPPVVDLKVGAAKRERPEKRVGGGGFGFYKKMNEGSASKQRHFKQVNRDQAKKFMR", "text": "FUNCTION: Probable RNA-dependent helicase. Functions in cell growth and proliferation. May have a role in ribosome biogenesis and, consequently, in protein biosynthesis. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily."}
{"protein": "MNINVDVKQNENDIQVNIAGEIDVYSAPVLREKLVPLAEQGADLRICLKDVSYMDSTGLGVFVGTFKMVKKQGGSLKLENLSERLIRLFDITGLKDIIDISAKSEGGVQ", "text": "FUNCTION: Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B. SIMILARITY: Belongs to the anti-sigma-factor antagonist family."}
{"protein": "MTTIVKRALVAAGMVLAIGGAAQANEGGVSLHKQDWSWKGIFGRYDQPQLQRGFQVFHEVCSTCHGMKRVAYRNLSALGFSEDGIKELAAEKEFPAGPDDNGDMFTRPGTPADHIPSPFANDKAAAAANGGAAPPDLSLLAKARPGGPNYIYSLLEGYASDSPGEPAEWWVKQQQEKGLEVAFNEAKYFNDYFPGHAISMPPPLMDDLITYEDGTAATKDQMAQDVVAYLNWAAEPELDARKSLGLKVLLFLGVLTAMLLALKLAIWRDVKH", "text": "FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MSSAPASGGLRLLVCFLGVFVCYFYYGILQETITRRTYGEGEKQEKFRFALSLVFVQCIVNALFAKLLIQCFDSGKTDRTQSWLYSACSLSYLGAMVSSNSALQFVNYPTQVLGKSCKPIPVMLLGVTLLRKKYPLTKYLCVLLIVFGVALFMYKPKTGSGDGDHTVGYGELLLLLSLTLDGLTGVSQDYMRAHFQTGSNHMMLSINLWSSLFLGAGIVLTGELWDFLSFTERYPSIVYNIVLFSLTSALGQTFIFMTVVYFGPLTCSIITTTRKFFTILASVILFSNPISSIQWVGTLLVFLGLGLDATYGKGSKKPSH", "text": "FUNCTION: Probable sugar transporter. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily."}
{"protein": "MTIEAAMGEEAIKENLEQFLIVLSVSLGVATLSQISSFFRQIPYTLLLVIVGLGLAFVDIRLVNLSPELILEIFLPPLLFEAAWNIRWRNLKKNLFPVVLLAIIGVVISVVGIGFSLNYFSGLSLPIALLVGAILAATDPVSVIALFRELGVGERLTVLMEGESLFNDGVAVVAFSLLVGIPLGTQEFSVTNTLIQFVTLQGIGIGCGGVIGFGISYLTQRFDLPLVEQSLTLVSAYGTYLITEELGGSGVIGVVTVGLILGNFGSRIGMNPRTRLLVSEFWEFIAFFVNSIVFLLIGDQINIRGLADNGQLILITIIALVIIRAISIYGLGTISNLITKQDISWQEETVLWWGGLRGSVSIALALSVPVMLDGRQDIIEAVFGVVLFTLLVQGLTMQTVIEKLGLIGDRAQRRTYSELIARRSALERVLAHLNAVPPSPSIRMKSLKTTKEASKGQLESRQTKKLRSYNNSYPQLRSLEQEQLRELTFKVEADTYAELIRAGKLNNNLSPLLQEVLAKPE", "text": "FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Shows also high Ca(2+)/H(+) antiporter activity at alkaline pH. Does not catalyze exchange between Li(+) and H(+). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family."}
{"protein": "HREEQARYIVKNKPVTMSCAASPATQIYFKCNGEWLHQKAHHIEEREDETTGRSVREVQTDVSRQQVEELFGLEDYWCQCVAWSAAGTSKSRKAYVRLAYLRKNFEQKPLGKYALLDHEVLLHCRPPDAIPQAEVEWLKSEEIIDPVIDQNFYITVDHNLIIKQTRLADSANYTCVAKNLVAKRRSSTATITVYVNGGW", "text": "FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the unc-5 family."}
{"protein": "MYESVDVVGLTPSPNPFLSMDYYHQNRGCLIPDKGLVSGAARGFRNPHWSGSNHSVETQSTSSEEIVPSPPSPPPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHREKSCIINKVTRNRCQYCRLQKCLEVGMSKESVRNDRNKRKKDDKKQECLENYVLSPDTEKMIEQVRKAHQETFPSLCQLGKYTTNNSADHRVALDVDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPDQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLLCGDRQDLEQSDKVDELQEPLLEALKIYVRNRRPHKPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLEGGGSKGAGGGGGGGGGKGAPPGSCSPSLSPSSAHSSPSAHSP", "text": "FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain development and, in lateral plate mesoderm, for specification of the pectoral fins. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MIIKPKIRGFICTTTHPVGCEANVKEQIAYTKAQGPIKNAPKRVLVVGSSSGYGLSSRIAAAFGGGAATIGVFFEKPGTDKKPGTAGFYNAAAFDKLAHEAGLYAKSLNGDAFSNEAKQKAIELIKQDLGQIDLVVYSLASPVRKMPDTGELVRSALKPIGETYTSTAVDTNKDVIIEASVEPATEQEIADTVTVMGGQDWELWIQALEEAGVLAEGCKTVAYSYIGTELTWPIYWDGALGRAKMDLDRAATALNEKLAAKGGTANVAVLKSVVTQASSAIPVMPLYIAMVFKKMREQGVHEGCMEQIYRMFSQRLYKEDGSAPEVDDHNRLRLDDWELRDDIQQHCRDLWPQITTENLRELTDYDMYKEEFIKLFGFGIEGIDYDADVNPEVEFDVIDIE", "text": "FUNCTION: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the NADH-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It can use both crotonyl-CoA and crotonyl-ACP. SIMILARITY: Belongs to the TER reductase family."}
{"protein": "MKKLLALAVIAPLLISCSSSTKKGETYNEAWVKDTNGFDILMGQFANNIENLWGYKEVLIAGPKDYVKYTDQFQTRSHINFDDGAITVETIAGTEPTAHLRRAIIKTLLMGDDPTSVDLYSDVDDIKISKEPFLYGQVLDNTGQPIRWEGRATTFADYLLKTRLKSRSNGLSIIYSVTINLVPNHLDKRAHKYIGMVRQASRKYGVDESLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGKDVFRSQGKSGTPSRNFLFDPASNIDTGTAYLAMLNNVYLSGIENPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANMINRMSPGDVYQILTTRHPSAESRRYLYKVNSAQRSYRRR", "text": "FUNCTION: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the transglycosylase Slt family."}
{"protein": "MWRSIISFLFFSVALCQPFLFQKRSSNISDFISFNASLPNVTIFAMGGTIAGYASSSTETVDYAAGSVGIATLVDAVPAIKNFSNIRGVQVTNVGSEELTPANVLNLTQLILAEVAKPDVHGIVVTHGTDSLEETAMFLDMTVNTTKPIVVVGAMRPSTAISADGPMNLLNAVVVAASNRSIGRGTMILLNDRIGSAFYTTKTNGNMLDTFKSYEAGFLGMILDQRPHFFYSPATPTGKVHFDVSNTTELPAVEILYGYQGLNPNLAKAAVDLGAKGLVLAGMGAASWTDPGNEVIDGLISNQSIPVVYSHRTMDGFSDYYYNGIPSYFQNPQKARYMLMLSINAGYSIQNITDIFSLEY", "text": "SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the asparaginase 1 family."}
{"protein": "MTTLIHVLGSDIPHHNQTVLRFFNDVLAKRLPSDQTRHFMVAAKDAAALGPFPELNLECHPDKKSLAMAVIARAQADRDQRFFFHGQFNPTLWLALLSGKIKAHQVSWHIWGADLYENATSWKFRLFYLLRRIAQGRVGRVFATRGDVIHYQQRHARVPASLLYFPTRMDPALTGISVEKNLAGPMTILVGNSGDRTNRHVEALKAIHQQFGADVRVILPMGYPANNEAYIEQVRTAGLALFSASNLQVLTQQVAFDDYLNILRECDLGYFIFNRQQGIGTLCLLIQFGVPFVLSRQNPFWQDLAEQHLPVLFYGDSLDEAVVREAQRQLASVDKQEIAFFNPNYVDGWQQALALAAGDNS", "text": "FUNCTION: Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (Lipid III), the third lipid-linked intermediate involved in ECA synthesis. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the glycosyltransferase 56 family."}
{"protein": "MEGVLAANWSAEAVNSSAAPPEAEGNRTAGPPQRNEALARVEVAVLCLILFLALSGNACVLLALRTTRHKHSRLFFFMKHLSIADLVVAVFQVLPQLLWDITFRFYGPDLLCRLVKYLQVVGMFASTYLLLLMSLDRCLAICQPLRALRRPADRLAVLATWLGCLVASAPQVHIFSLREVADGVFDCWAVFIQPWGPKAYITWITLAVYIVPVIVLAACYGLISFKIWQNLRLKTAAEAAEAIAGTEGAAAGSRGRAALARVSSVKLISKAKIRTVKMTFIIVLAFIVCWTPFFFVQMWSVWDADAPKEASAFIIAMLLASLNSCCNPWIYMLFTGHLFHELVQRFLCCSSSHLKTSRPGETSVSKKSNSSTFVLSQHSSSQKSCS", "text": "FUNCTION: Receptor for oxytocin. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Vasopressin/oxytocin receptor subfamily."}
{"protein": "MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVITTKDVQKALCADFNKMKMKLDIVCIPDEADMGTADSLRHIYQKLKTDVLVLSCDLITDVALHEVVDLFRAHDASLAMLMRKGQESLEPVPGQKGKKKAVEQRDFVGVDSTGKRLLFMANEADLDEELIIKGSILQKHPRIRFHTGLVDAHLYCLKKYVVDFLMENKSITSIRSELIPYLVRKQFSSASSQQGQEEKEEDLKKKELKSLDIYSFIKEANTLTLAPYDTCWNACRGDSWEGLSRSQVRCYVHIMKEGLCSRVSTLGLYMEANRQVSKLLPVICPEESLIHSSAQIVSKHMVGADSLIGPDTQVGEKSSIKHSVIGSSCVIRDRVTVTNCLLMNSVTVEEGSNIQSSIICNDAVIEKGADIKNCLIGSGQRIEAKAKRVNVIVGNDQFLEI", "text": "FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2- bound GDP for GTP. SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family."}
{"protein": "MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPSRADDARQLFALSCTAEEQGVLPDDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITHSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta- adrenergic stimuli. May play a role in cell division. FUNCTION: [Isoform sGi2]: Regulates the cell surface density of dopamine receptors DRD2 by sequestrating them as an intracellular pool. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell membrane Membrane; Lipid-anchor Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily."}
{"protein": "MGSVALILKVMPESPDVDLEALKAAMRAKVPSIQDIQEEPIGFGLKALKVMAVVSDQGGETDALEEALSSIEGVERAEIAELTLT", "text": "FUNCTION: Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA. SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family."}
{"protein": "MNRQSWLLNLSLLKTHPAFRAVFLARFISIVSLGLLGVAVPVQIQMMTHSTWQVGLSVTLTGGAMFIGLMVGGVLADRYERKKVILLARGTCGIGFIGLCVNALLPEPSLLAIYLLGLWDGFFASLGVTALLAATPALVGRENLMQAGAITMLTVRLGSVISPMLGGILLASGGVAWNYGLAAAGTFITLLPLLTLPRLPVPPQPRENPFLALLAAFRFLLACPLIGGIALLGGLVTMASAVRVLYPALAMSWQMSAAQIGLLYAAIPLGAAIGALTSGQLAHSVRPGLIMLVSTVGSFLAVGLFAIMPVWIAGVICLALFGWLSAISSLLQYTLLQTQTPENMLGRMNGLWTAQNVTGDAIGAALLGGLGAMMTPVASASVSGFGLVIIGLLLLLVLGELRRFRQTSPVSDAG", "text": "FUNCTION: Component of an export pathway for enterobactin. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. EntS (TC 2.A.1.38) family."}
{"protein": "MSHAVKIYDTCIGCTQCVRACPLDVLEMVPWDGCKAGQIASSPRTEDCVGCKRCETACPTDFLSIRVYLGDETTRSMGLAY", "text": "FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MSLDIDQIALHQLVKRDEQTLDVVLRDSLLPANAVVEEMMAELHRVYSAKSKAYGLFNEQSELADALKRSRKGDEDFLSFSRAATGRLRDELAKYPFAEGGVVLFCQYRYLAVEYLLISVLSSCNSMRVNEQLDLSTTHYLDINRADIVARIDLTEWENNPESTRYLTFLKGRVGRKVSDFFMDFLAASEGLDTKAQNRGLLQAVADYCADAELGKNERQAYRQQVYSYCNEQLQAGEEIALQELAQELPKLGEKDFQQFSVEQGYALEESFPADRGTLRQLTKFAGSGGGLSINFDALLLGERIFWDAATDTLTIKGTPPNLRDQLQRNSGK", "text": "SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the YejK family."}
{"protein": "MDQFNQQQQSQMNKGIPGKPHKNHGGHEMFDMHEVLSGTLTVLDQFMMLRQFCKDQELLNILDRQHQFITSQYNITAECFKTGSEPSQKTATYMMKEDNQTVYGMQPSQPKKPVQSMNDIDDSIISRQMLCAIKAQASMLTMASLEMTNPAVRRVLSAQIQEYVEMAFEIFLYQNKHGYYQVPQLDAQDMEQLRNSFAPAQGQMPPTQGGMGQQGLH", "text": "SUBCELLULAR LOCATION: Spore coat. SIMILARITY: Belongs to the CotF family."}
{"protein": "MKSVLYSYILFLSCIIINGRDVTPYAPSNGKCKDNEYKRHNLCCLSCPPGTYASRLCDSKTNTQCTPCGSGTFTSRNNHLPACLSCNGRCDSNQVETRSCNTTHNRICECSPGYYCILKGSSGCKACVSQTKCGIGYGVSGHTSAGDVICSPCGLGTYSRTVSSADKCEPVPSNTFNYIDVEINLYPVNDTSCTRTTTTGISESISTSELTITMNHKDCDPVFREEYFSVLNKVATSGFFTGENRYQNISKVCTLNFEIKCNNKGSSSKQLTKAKNDDGIMPHSETVTLVGDCLSSVDIYILYSNTNTQDYETDTISYHAGNVLDVDSHMPGSCDIHKLITNSKPTHFL", "text": "FUNCTION: Inhibits host immune defense by binding to host TNF and various chemokines in the extracellular space. Binds host CC chemokines (beta chemokines) and CXC chemokines (alpha chemokines). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the orthopoxvirus OPG002 family."}
{"protein": "MVKERKTELVEGFRHSVPYINTHRGKTFVIMLGGEAIEHENFSSIVNDIGLLHSLGIRLVVVYGARPQIDANLAAHHHEPLYHKNIRVTDAKTLELVKQAAGTLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEDALHRQLESGAIVLMGPVAVSVTGESFNLTSEEIATQLAIKLKAEKMIGFCSSQGVTNDDGDIVSELFPNEAQARVEAQEEKGDYNSGTVRFLRGAVKACRSGVRRCHLISYQEDGALLQELFSRDGIGTQIVMESAEQIRRATINDIGGILELIRPLEQQGILVRRSREQLEMEIDKFTIIQRDNTTIACAALYPFPEEKIGEMACVAVHPDYRSSSRGEVLLERIAAQAKQSGLSKLFVLTTRSIHWFQERGFTPVDIDLLPESKKQLYNYQRKSKVLMADLG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily."}
{"protein": "MAPFPDEVDVFTGPHWRMKQLVGLYSEKLSNTNFSNNRDFRSFLQSLLDTFTEFKKHEQIENECIMELLQERSHTVYHVHADNKLSDMLTLFQKGLRSVTSEFEQLNYAQQLKERLEAFTQDFIPHMKEEEEVYQPMLMEYFSYEELKAIKQQVMLQHCSSQCQSSCSDTHTLLKGLSLWSHAELQKAFKYSDHEKTGDERVLERVSVSSLPQELLLRIFRFLGPQDLCRCAQVCSVWTQVTRTGSLWRHLYPVRWARGEYYSGPPGDLDLEPDDDWIKSLQDDGRAYQEWDEDADVDESEEASAERSSISALQREKLLLNGIIQKLLPAVGSSVRSLSLAYSSTLSSKMVRQMLSLCPNLTHLDLTQTDVSDSAFDSWCALGACGTLQHLDLSGCDKITDRTLKILSVGLGDSSTPSPAHKLLQAPPSPIRIEEPRLQPMGRSCQDLIFKRRPGGRGSGCGPTHIWVLDPVKLADIEDAADWSRRGGVASQEIGCGGISEALSASCCCRRSQRRGFRTGLSSSPWQYGDALCGHSSCCSSDAAAIRTQSDLQATGGSAELRTKCWFEGQSCAEHHNRTDQSGAQRALRFLSLSGCHQITDLGLRCVCLRGGLPLLEHLNLSGCPLITGAGLQEVVSASPALNIEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE", "text": "FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of ireb2/irp2. Upon high iron and oxygen level, it specifically recognizes and binds ireb2/irp2, promoting its ubiquitination and degradation by the proteasome (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region."}
{"protein": "MESIGVLLTCPMNPYLEQELDKRFKLFRFWDFPSANDLFREHSNSIRAVVGNSFIGADAQMIEALPKMEIVSSFSVGLDKIDLVRCKEKGIRVTNTPDVLTEDVADLALALILATLRRICESDRYVRSGSWKKGDFKLTTKFTGKSVGIIGLGRIGSAIAKRAEGFSCPISYHSRTEKPGTNYKYYPSVVELASNCQILVVACALTPETRHIINREVINALGPKGVVINIGRGLHVDEPELVSALVEGRLGGAGLDVFENEPNVPEELLAMDNVVLLPHVGSGTVETRKDMADLVLGNLEAHFLNKPLLTPVV", "text": "FUNCTION: Involved in the biosynthesis of L-tartarate from L-ascorbate (PubMed:31488549). Catalyzes the NAD(P)H-dependent reduction of 2- dehydro-L-idonate (2-keto-L-gulonate) to L-idonate (PubMed:31488549). Can also reduce hydroxypyruvate to glycerate, glyoxylate to glycolate and pyruvate to D-lactate (PubMed:31488549). Prefers NADPH to NADH as proton donor (PubMed:31488549). SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family."}
{"protein": "MAETSGPQSSHISSSSVGEKGSGCAVRDLLYWRDVKQSGMVFGGTMVLLLSLAAFSIISVISYLVLSLLTVTISYRVYKSVLQAVQKTDEGHPFKPLLEKDITLSSDSFQKALTASLAHVNHALKYIVRLFLVDDLVDSLKLALLMWLMTYVGAVFNGITLLILGVLLTFTAPIVYEKYKVQIDHYVSLVHSQVKSITEKIQAKLPGALKKKSE", "text": "FUNCTION: May be involved in membrane trafficking in the early secretory pathway. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein."}
{"protein": "MYSNNRVEVFHGDGRLGELEIYPSRELNQQQDDVMKQRKKKQREVMELAKMGIRISHFSQSGERCPPLAILTTISSCGLCFKLEASPSPAQESLSLFYSSCLRDNKTAVMLLGGEELHLVAMYSENIKNDRPCFWAFSVAPGIYDSCLVMLNLRCLGIVFDLDETLVVANTMRSFEDKIDGFQRRINNEMDPQRLAVIVAEMKRYQDDKNLLKQYIESDQVVENGEVIKVQSEIVPALSDNHQPLVRPLIRLQEKNIILTRINPMIRDTSVLVRMRPSWEELRSYLTAKGRKRFEVYVCTMAERDYALEMWRLLDPEGNLINTNDLLARIVCVKSGFKKSLFNVFLDGTCHPKMALVIDDRLKVWDEKDQPRVHVVPAFAPYYSPQAEAAATPVLCVARNVACGVRGGFFRDFDDSLLPRIAEISYENDAEDIPSPPDVSHYLVSEDDTSGLNGNKDPLSFDGMADTEVERRLKEAISASSAVLPAANIDPRIAAPVQFPMASASSVSVPVPVQVVQQAIQPSAMAFPSIPFQQPQQPTSIAKHLVPSEPSLQSSPAREEGEVPESELDPDTRRRLLILQHGQDTRDPAPSEPSFPQRPPVQAPPSHVQSRNGWFPVEEEMDPAQIRRAVSKEYPLDSEMIHMEKHRPRHPSFFSKIDNSTQSDRMLHENRRPPKESLRRDEQLRSNNNLPDSHPFYGEDASWNQSSSRNSDLDFLPERSVSATETSADVLHGIAIKCGAKVEYKPSLVSSTDLRFSVEAWLSNQKIGEGIGKSRREALHKAAEASIQNLADGYMRANGDPGPSHRDATPFTNENISMGNANALNNQPFARDETALPVSSRPTDPRLEGSMRHTGSITALRELCASEGLEMAFQSQRQLPSDMVHRDELHAQVEIDGRVVGEGVGSTWDEARMQAAERALSSVRSMLGQPLHKRQGSPRSFGGMSNKRLKPDFQRSLQRMPSSGRYS", "text": "FUNCTION: Processively dephosphorylates 'Ser-5' but not 'Ser-2' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II. Together with CPL2, required for male gametes fertility. Multifunctional regulator that modulates plant growth, stress, and phytohormones responses. Negative regulator of stress gene transcription involved in abscisic acid (ABA) mediated and jasmonic acid (JA) mediated signaling pathways, NaCl, osmotic stress, wounding, and cold resistance. Regulates negatively the expression of jasmonic acid (JA) biosynthetic genes in response to wounding (PubMed:11874572, PubMed:12149434, PubMed:12149453, PubMed:15388846, PubMed:18506580, PubMed:18764923). Forms a complex with RCF3 that modulates co- transcriptional processes such as mRNA capping and polyadenylation, and functions to repress stress-inducible gene expression (PubMed:23874224). Dephosphorylates RCF3 (PubMed:26227967). Involved in the dephosphorylation of EIF4A3. This dephosphorylation retains EIF4A3 in the nucleus and limits its accumulation in the cytoplasm. Is essential for the degradation of the nonsense-mediated mRNA decay (NMD) transcripts (PubMed:26887918). SUBCELLULAR LOCATION: Nucleus Nucleus speckle."}
{"protein": "MSDISCKKRDDYLEWPEYFMAVAFLSAQRSKDPSSQVGACIVNTENKIVGIGYNGMPNGCSDDLLPWRRTAENKLDTKYPYVCHAELNAIMNKNSADVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSEETTAARLLFKLAGVTFRKFTPKYSKIVIDFDSINSRPSQKPQ", "text": "FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MDSLLMNRRKFLYQFKNVRWAKGRRETYLCYVVKRRDSATSFSLDFGYLRNKNGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVADFLRGNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIAIMTFKDYFYCWNTFVENHERTFKAWEGLHENSVRLSRQLRRILLPLYEVDDLRDAFRTLGL", "text": "FUNCTION: Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses (PubMed:18722174, PubMed:21385873, PubMed:21518874, PubMed:27716525). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (PubMed:21496894). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Predominantly cytosolic (PubMed:21385873). In the presence of MCM3AP/GANP, relocalizes to the nucleus (By similarity). SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "VLIIAVLFLTACQLTTAETYPRGQQRHHALRSTDKNSKLTRGCTPRNGACGYHSHCCSNFCHTWANVCL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
{"protein": "METLFHTLLRLLLFVAISHTLSPLAGSFRISNDFPAVFNFGDSNSDTGELSSGLGFLPQPSYEITFFRSPTSGRFCNGRLIVDFLMEAIDRPYLRPYLDSISRQTYRRGCNFAAAASTIQKANAASYSPFGFGVQVSQFITFKSKVLQLIQQDEELQRYLPSEYFFSNGLYMFDIGQNDIAGAFYTKTVDQVLALVPIILDIFQDGIKRLYAEGARNYWIHNTGPLGCLAQVVSIFGEDKSKLDEFGCVSDHNQAAKLFNLQLHGLFKKLPQQYPNSRFTYVDIFSIKSDLILNHSKYGFDHSIMVCCGTGGPPLNYDDQVGCGKTARSNGTIITAKPCYDSSKYVNWDGIHYTEAANRFVALHILTGKYSETASSLNL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family."}
{"protein": "MSLNLPNPSLIGILLVISTHSGPQLIYKYPFDLSNDPSRDESKYALDDNEDDELYDHEESEDENEVNENEMYGVNSRNWDSKHIDYYMGTKSDLLKFLDEQDSRRRKITTTSPSEEKHTKEKHGLTKTISKSSTMASSSTTSPPESSIQGEIFGTDAAYICEMLAPPKQMCNTRFEMTIQDKLFLGLPVHRSDNGQWRSIGHNNEHDEEETHTAKNSLNMFHLVFVMNPPVIESNYRVDEMFHYVISRLSLVLRYEQQKHDYVSQQVKNILALRESLEGNESLLTEKSSLSRVIRDCFEGISTSTIANLSINGKLRSFQIPIKTEFHSLPDPSVPFLPASYLSSTVELLGDTSFINVGETSRYGHAFNSVQDEENSAEKIIVYFALLLLDDPESIIKDMKTETDSTLAKFIRMIEPTESLLKLSARNSKLDISQIKDFAFHLIYWRRARVILPLSSRSVYIVSPMAPITIKLYDDISFFNRRFPTLPSLPHFLKLLSPQSRKPQQFATVIPSKDHRDRYLQALGWLIKHGYVTQLQTFIWLKISRKIKIKVEEDIENENLAKKKKKQKNGSVTVATANSSKTEAPIMPTDNTSKQVSDSKDSDKPEDDEYASKPRLDGLHEHIDGTPIVTLVQGDDTIILDPGRATTLERRWINKIIYEECKLSPELTAVFYKLLKYMNGKNSLELLLLKENISRSELRKLLLSIEEHIISVRHW", "text": "FUNCTION: Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division (By similarity). SIMILARITY: Belongs to the NPR3 family."}
{"protein": "MLRFTGARAIRKYSTRYALEHLKEGAPLKGLFSIEGLQKAWFDRVKYLDAKLNDCTNEAQQKPLETLIHENSKSASKKHIVNYASSLYNLKFSMSSLQGCIRTPPEECPRLGPEALLQTPDFNRTISNEPLTTGNERLQAALISSFGSLMEFRTLLINSNLAISGDGFTWLVARRQLDKRAMRNDMPNRDIEYDKLFILNTYNAGTPFNFSTSGVMNELNNQYTNMEKQRAKEAGNLEDSEMTAKQAKTKFIYETQQKGFSGKEVSYIPLLAIDASPKTWLTDYGVFGKREYLERVWDSIEWKIVESRLPQRTKIQAFNTL", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS43 family."}
{"protein": "MNGNHSAPAIAIAVIDGCDGLWREVLLGIEEEGIPFRLQHHPAGEVVDSAWQAARSSPLLVGIACDRHMLVVHYKNLPASAPLFTLMHHQDSQAHRNTGNNAARLVKGIPFRDLNSEATGEQQDE", "text": "FUNCTION: Small subunit of the diol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin- dependent diol dehydratase (DD, pddA, pddB, pddC). DDR acts as a chaperone, reactivates inactivated DD holoenzyme in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one (PubMed:9405397, PubMed:9920879, PubMed:10529189, PubMed:17916188, PubMed:18586770, PubMed:21040475). Reactivation takes place in two steps: ADP-dependent cobalamin release, and ATP-dependent dissociation of the DD apoenzyme-DDR complex. DDR has weak ATPase activity which is required for DD reactivation (PubMed:10529189, PubMed:17916188, PubMed:21040475). Activates glycerol-inactivated, O2-inactivated holoenzyme and inactivated enzyme-cyanocobalamin complex (PubMed:9920879). Also reactivates glycerol-inactivated hologlycerol dehydratase, a DD isozyme (PubMed:17916188). SIMILARITY: Belongs to the DdrB/PduH family."}
{"protein": "MTVKIAQKKVLPVIGRAAALCGSCYPCSCM", "text": "FUNCTION: Chalkophore involved in scavenging, uptake and suppression of toxicity of copper. Each apo-methanobactin (apo-mb) complexes 1 Cu(2+) or Cu(1+) ion to form Cu(1+)-mb (Cu-mb) which is then taken up by the cell. Enhances growth rate in the presence of copper and reduces growth lag upon exposition to elevated levels of copper. Cu-mb contributes to the switchover from soluble methane monooxygenase (sMMO) to the membrane-bound particulate MMO (pMMO) by inducing transcription of pMMO subunit A. It also stimulates the enzymatic activity of pMMO. In the absence of copper, binds other metal ions, like Zn(2+), Ag(1+), Au(3+), Co(2+), Cd(2+), Fe(3+), Hg(2+), Mn(2+), Ni(2+), Pb(2+) or U(6+), but not Ba(2+), Ca(2+), La(2+), Mg(2+) or Sr(2+). Uptake is an active process, which may involve TonB-dependent transporters, and as such does not involve porins. Cu-Mb can be taken up by other methanotrophic bacteria but not by E.coli. Has Cu-dependent superoxide dismutase-like activity. Shows reductant-dependent oxidase and hydrogen peroxide reductase activities. Reduces copper-levels in liver in a rat model of Wilson disease. SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Secreted as apo-mb, uptake into the cytoplasm in complex with copper as Cu-mb. In the cytoplasm, Cu-mb is associated with the cell membrane."}
{"protein": "MVSRWEKLKNNPQTKSIGISIFLMMITRVIDFSRPSLLWPLRILYATVNIVQIGIFLYTKIIIEKKNDLTVLKYVEPATPMSGREHSKFVATTVRDYDLSKLLTSFKQMLVTIATTLFMHLYMGYAPPLLLQSVSAARGLFDNSEVQIHVQNKPAIDELRRPFKSSGGLLGSFGQVLTDKKSVDEAELTKLKPT", "text": "FUNCTION: May function in a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. Involved in inorganic phosphate uptake. Also involved in telomere length regulation and maintenance (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PHO88 family."}
{"protein": "MRCGCLACDGVLCANGPGRPRRPALTCTAVATRTLHSLATNAELVESADLTVTEDICSRIVSLPVHDHMAIADVARVVAPFGEGLARGG", "text": "SIMILARITY: To M.tuberculosis Rv3402c."}
{"protein": "MACVSTCLILSPRLTQVGLSSKKPFLIRLRSPVDRYSFPRMLTERCLSTRRKFNRHGIAVVKAASLDKVSGAIKPGGLVESDKLPTDVRKRAMDAVDECGRRVTVGDVASRGGLKVTEAQTALQAIAADTDGFLEVSDEGDVLYVFPRDYRTKLAAKSLRIQIEPFLEKAKGAVDYLARVSFGTALIASIVIVYTSIIALLSSKSEDDNRQRRRGRSYDSGFNFYINPVDLLWYWDPNYYNRRRAREDEGKGMNFIESVFSFVFGDGDPNQGIEEERWQMIGQYITSRGGVVAADELAPYLDVPSSKSAMNDESYILPVLLRFDGQPELDEEGNILYCFPSLQRTASGSSRRKEYVGKWFDWVADMEKFFKEKKWQFSKTSTSERALVIGLGAVNLFGVIVLNTLLNEMSVRPGGFLTFVKNIYPLLQIYAGSFFTIPLIRWFSIKRKNNQIENRNKARLQFARALESPDIALRRKLLSARDMAQKTVIGKDRIVYSTDRDMMEQNYETDEWDRRFKELEKSD", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein."}
{"protein": "MPPKKHSGFMMFVNEWRDNNPEGRNLSIAQAVSRCGSIWEKMTAQQRGPYNSGAKNADVLTRVKKERLNCHGQVLSQVELEEREMAESQINMKRCTERIVMDAKRSHDLENTKFVFVAFNYFTKALTTDVYVPAEFSASEYSFNEGIMSVYSTLIDPGQIIFGQGSDAQHHSSTTHNLPLPPNALGEKNMGKLYRNILEYLSKIQEGKDATKPFVVFTKTDMVPVVKSCFRYLACENQDGSYENGDQIQVLDIQYLLFILKKEVLDIAGVSDEKINLYVTDAYFLKDFFEFTPEISCQYHEENDRSKYCTQSLVMRWAYTFSDYMCSDLAISVQPGKHIPPKTKPNYRFYRQPPAGDHLHHPLTCQQTILRLLATLTRKTNFHLSVGGEPPTVALVPSDLTLWDPGIYPLTPVPFMTFLTTTLV", "text": "FUNCTION: Involved both in the piRNA and miRNA metabolic processes. As a component of the meiotic nuage, plays a central role during oogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Repression of transposable elements is mediated via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the repression of transposons. As a nuclear component, it is required for proper differentiation in the germline stem cell (GSC) lineage by repressing microRNA-7 (miR-7), thereby acting as an indirect regulator of bag-of-marbles (Bam). Acts by binding to the promoter of miR-7 gene and repressing its expression; miR-7 repression alleviates the Bam repression by miR-7, thereby allowing differentiation in the germline stem cell (GSC) lineage (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. SIMILARITY: Belongs to the maelstrom family."}
{"protein": "MALLTAKTFSLQFNNKRRVNKPYYPRKALLCYQLTPQNGSTPTRGHLKNKKKDHAEIRFINKIKSMGLDETQCYQVTCYLTWSPCPSCAGELVDFIKAHRHLNLRIFASRLYYHWRPNYQEGLLLLCGSQVPVEVMGLPEFTDCWENFVDHKEPPSFNPSEKLEELDKNSQAIKRRLERIKSRSVDVLENGLRSLQLGPVTPSSSIRNSR", "text": "FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase- dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MLALLGATTLMLVAGRWVLPAASGEANLKPENVEIHIIDDNFFLKWNSSSESVKNVTFSADYQILGTDNWKKLSGCQHITSTKCNFSSVELENVFEKIELRIRAEEGNNTSTWYEVEPFVPFLEAQIGPPDVHLEAEDKAIILSISPPGTKDSIMWAMDRSSFRYSVVIWKNSSSLEERTETVYPEDKIYKLSPEITYCLKVKAELRLQSRVGCYSPVYCINTTERHKVPSPENIQINADNQIYVLKWDYPYENATFQAQWLRAFFKKIPGNHSDKWKQIPNCENVTSTHCVFPREVSSRGIYYVRVRASNGNGTSFWSEEKEFNTEMKTIIFPPVISVKSVTDDSLHVSVGASEESENMSVNQLYPLIYEVIFWENTSNAERKVLEKRTNFIFPDLKPLTVYCVKARALIENDRRNKGSSFSDTVCEKTKPGNTSKTWLIVGTCTALFSIPVVIYVVSVFLRCVKYVFFPSSKPPSSVDEYFSDQPLRNLLLSTSEEQTERCFIIENASIITEIEETDEIDEVHKKYSSQTSQDSGNYSNEDENSGSKISEEFPQQDSV", "text": "FUNCTION: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:8318540). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response (By similarity). Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross- phosphorylate one another (By similarity). The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (By similarity). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (By similarity). Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Late endosome Lysosome Note=Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes. SIMILARITY: Belongs to the type II cytokine receptor family."}
{"protein": "MKPWAAFHLIFLVASSLEGEVSNYGTGGTQDTEPTCRTEHQCTRDKIILQSQPGIPGIPGVPGTNGSEGLKGDPGPQGPPGIRGPDGIRGEAGPKGDKGDQGDKGDKGDKGDKGEDCNLDGCLPTEVRNCQDLLEHGEILNGWYTIYPTKENPMVVFCDMETDGGGWLVFQRRQDGSVDFYLDWESYKKGFGKQESEFWLGNDKIHLLTSSGTQQLRIDLEDFEGSRTFAKYSSFSIGDENEKYRLIVGSYLDGSMNDSFRIHNGHSFSTKDRDNDTNKGNCAMMYKGAWWYFHCHHANLNGLYYKGKHANYADGINWRSGKGYYYSYKYADMKIRPQQSETTVS", "text": "FUNCTION: Initiates complement activation and/or interferes in platelet aggregation and/or blood coagulation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ficolin lectin family. Veficolin subfamily."}
{"protein": "MEPMSNKQDSNSSEGDEKGWPDVPKRKRKNSQCSMKSMSALSVSVPGYIPSYLEKDEPCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPAYSCKYEGCCIIDKITRNQCQLCRFKKCISVGMAMDLVLDDSKRVAKRRLIEENREKRKREEMVRTLQVRPEPDTAEWELIRMATDAHRHTNAQGSSWKQKRKFLSDDIGQGPMVPTSDGDKVDLEAFSEFTKIMTPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVKREQLKNGGLGVVSDAIFDLGKSLAQFNLDDTEVALMQAVLLMSSDRSGLTSLEKIEQCQEAYLLAFEHYINYRKHNIPHFWPKLLMKVTDLRMIGACHASRFLHMKVECSSELFPPLFLEVFEDQEV", "text": "FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "GCIPYGKTCEFWSGPWCCAGKCKLNVWSMTLSCTRNF", "text": "FUNCTION: Blocks the Nav1.2/SCN2A, Nav1.4/SCN4A, and Nav1.6/SCN8A sodium channels. Reduces the peak amplitude of the sodium current and negatively shifts the steady-state inactivation process. Does not shift the threshold potential of activation or the voltage corresponding to maximal current. Does not change the reversal potential of the sodium current. May act on site 1 of the receptor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 01 (U2-agtx) family."}
{"protein": "MTPSLANFLWSLVYGAVVLGLLFGAIVFVSQRDRVRRR", "text": "FUNCTION: Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbX family. Type 1 subfamily."}
{"protein": "SVAGRAQGM", "text": "FUNCTION: Has antimicrobial activity against Gram-positive bacteria B.subtilis (MIC=76 ug/ml) and S.aureus (MIC=80 ug/ml), and against Gram-negative bacteria E.coli (MIC=82 ug/ml) and P.aeruginosa (MIC=79 ug/ml). SUBCELLULAR LOCATION: Secreted, extracellular space."}
{"protein": "MDDIEDSLDQWKFAQCFGDKGDVEDITEADIISAVEFDHTGDYLATGDKGGRVVLFERNHSKKGCEYKFFTEFQSHEPEFDYLKSLEIEEKINKIRWCKRTNRAHFLLSTNDKTIKLWKLYEKNLKVVAENNLSDSFHSPMQGPLTTPSQLRLPRLNHHDMIIAAYPRRVYANAHAYHINSISVNSDAETYISADDLRINLWNLSISDHSFNIVDIKPENMEELTEVITSAEFHPINCNHLMYSSSKGNIKLLDLRQSALCDNPCKLFEDQEDQDSKSFFSEIISSISDVKFSQNGRYILSRDYLTLKIWDVNMEKAPVKTIPLHDVLRSKLCDLYENDCIFDKFECTFSGDDKHVLSGSYSNNFGIYPTDSSLPGDRGQIVLQADKAAFRARKSAANNVPKLNAVKNNDWRSQPQAAMGSASVGLDPDNLDYNKKILHASWHPFEDSVAIAATNNLFVFSKL", "text": "FUNCTION: Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family."}
{"protein": "MGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATTGDGLYEGLTWLTSNYKS", "text": "FUNCTION: GTP-binding protein involved in protein trafficking; regulates endocytic recycling and cytoskeleton remodeling. May modulate vesicle budding and uncoating within the Golgi apparatus. May contribute to the regulation of dendritic branching, filopodia extension and dendritic spine development (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane; Lipid-anchor Endosome membrane; Lipid-anchor Recycling endosome membrane; Lipid-anchor Cell projection, filopodium membrane; Lipid-anchor Cell projection, ruffle Cleavage furrow Midbody, Midbody ring Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression. In late stages of cytokinesis, concentrates at the midbody ring/Flemming body. After abscission of the intercellular bridge, incorporated into one of the daughter cells as a midbody remnant and localizes to punctate structures beneath the plasma membrane (By similarity). Recruited to the cell membrane in association with CYTH2 and ARL4C. Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles. Myristoylation is required for proper localization to membranes (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
{"protein": "MNGTEGDMFYVPMSNATGIVRSPYDYPQYYLVAPWAYACLAAYMFFLIITGFPVNFLTLYVTIEHKKLRTPLNYILLNLAISDLFMVFGGFTTTMYTSLHGYFVFGRVGCNPEGFFATLGGEMGLWSLVVLAFERWMVVCKPVSNFRFGENHAIMGVVFTWFMACTCAVPPLVGWSRYIPEGMQCSCGVDYYTRPQAYNNESFVIYMFIVHFIIPLIVIFFCYGRLVCTVKEAAAQHEESETTQRAEREVTRMVVIMVIGFLICWIPYASVAWYIFTHQGSEFGPVFMTLPAFFAKTAAVYNPCIYICMNKQFRHCMITTLCCGKNPFEEEEGASTTASKTEASSVSSSSVSPA", "text": "FUNCTION: Photoreceptor required for image-forming vision at low light intensity. While most salt water fish species use retinal as chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of retinal and 3-dehydroretinal (PubMed:18422881). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cell projection, cilium, photoreceptor outer segment Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MANITVFYNEDFQGKQVDLPPGNYTRAQLAALGIENNTISSVKVPPGVKAILYQNDGFAGDQIEVVANAEELGPLNNNVSSIRVISVPVQPRARFFYKEQFDGKEVDLPPGQYTQAELERYGIDNNTISSVKPQGLAVVLFKNDNFSGDTLPVNSDAPTLGAMNNNTSSIRIS", "text": "FUNCTION: Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions. SIMILARITY: Belongs to the beta/gamma-crystallin family."}
{"protein": "MSQVTEQSVRFQTALASIKLIQASAVLDLTEDDFDFLTSNKVWIATDRSRARRCVEACVYGTLDFVGYPRFPAPVEFIAAVIAYYVHPVNIQTACLIMEGAEFTENIINGVERPVKAAELFAFTLRVRAGNTDVLTDAEENVRQKLRAEGVM", "text": "FUNCTION: Assembles the procapsid by joining twelve 12S pre-assembly complex into a T=1 icosahedral particle, called 108S procapsid. Ten proteins D bind each 12S complex, which are formed by three pentamers of F, G, B protein and a H protein. The scaffolding protein is released from the provirion after genome packaging to form the mature virion. FUNCTION: Assembles the procapsid by joining twelve 12S pre-assembly complex into a T=1 icosahedral particle, called 108S procapsid. Ten proteins D bind each 12S complex, which are formed by three pentamers of F, G, B protein and a H protein. The scaffolding protein is released from the provirion after genome packaging to form the mature virion. SUBCELLULAR LOCATION: Host cytoplasm. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the microvirus D protein family."}
{"protein": "MAWFALYLLSLLWATAGTSTQTQSSCSVPSAQEPLVNGIQVLMENSVTSSAYPNPSILIAMNLAGAYNLKAQKLLTYQLMSSDNNDLTIGQLGLTIMALTSSCRDPGDKVSILQRQMENWAPSSPNAEASAFYGPSLAILALCQKNSEATLPIAVRFAKTLLANSSPFNVDTGAMATLALTCMYNKIPVGSEEGYRSLFGQVLKDIVEKISMKIKDNGIIGDIYSTGLAMQALSVTPEPSKKEWNCKKTTDMILNEIKQGKFHNPMSIAQILPSLKGKTYLDVPQVTCSPDHEVQPTLPSNPGPGPTSASNITVIYTINNQLRGVELLFNETINVSVKSGSVLLVVLEEAQRKNPMFKFETTMTSWGLVVSSINNIAENVNHKTYWQFLSGVTPLNEGVADYIPFNHEHITANFTQY", "text": "FUNCTION: Promotes absorption of the essential vitamin cobalamin (Cbl) in the ileum. After interaction with CUBN, the CBLIF-cobalamin complex is internalized via receptor-mediated endocytosis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins family."}
{"protein": "MSFRSIVRDVRDSFGSLSRRSFEVRISGLPGLSGHHRGKSLGSLSELRDRPVVVDQSRWVGLPPELLRDVMKRLEEGESNWPSRKDVVACAAVCRTWREICKDIVQSPEICGKLTFPVSLKQPGPRDGLIQCFIKRDKSKLTYYLYLCLSPAVLSENGKFLLAAKRNRRATSTEYIISVDSKNISRSSNGYVGKMRSNFLGTKFVVYDTQPPYNAGSLMSCQHGSRRISSRRVSPKLPTGSYPIAHVKYELNVLGTRGPRRMQCTMHSIPASAVDPEGVVPGQPEQLLPGPFEESFRSTNTSSRFSFMDRSLDFSSSRFSEISGSANQQGEDDIPEAKERPLVLRNKVPRWHEQLQCWCLNFRGRVTVASVKNFQLIAAASSESSQLEQQQQQQQQNHASSSSSASDHGKVILQFGKVGKDMFTMDYRYPLSAFQAFAICLTSFDTKLACE", "text": "SIMILARITY: Belongs to the TUB family."}
{"protein": "MKASMFLALAGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRRCKYEIGK", "text": "FUNCTION: Neurotoxin. Selectively blocks neuronal tetrodotoxin- sensitive voltage-gated sodium channels (Nav). Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 22 (Htx-4) subfamily."}
{"protein": "MADASIQIEVVYASVQRQVLKTVDVPTGSSVRQALALSGIDKEFPELDLSQCAVGIFGKVVTDPAARVLEAGERIEIYRLLVADPMEIRRLRAARAREKRGLPG", "text": "SIMILARITY: Belongs to the UPF0125 (RnfH) family."}
{"protein": "MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIMKNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKDYKDQKASRNESTF", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family."}
{"protein": "MKRLTLVCSIVFILFILFYDLKIGTIPIQDLPVYEASAKTAVQEPAYKTVKVKPGDTVMSIVGSAGSPDDIVKDFEALNPNVKANAIQAGTAYKFPVYP", "text": "SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Single-pass membrane protein."}
{"protein": "MVISPSLIISSLNLGILTILLGSIFFFSKSYFSKGNVNFPLIKTTSACLSVNNDKEETIEYNSGPFAMAILKVLAFLSVLSLLVTCNNSIQSINITLSLWLSNTPLNISLNFIYDQYFLVFLSVALIVTWSIMEFSFYYMTEDPNSSAFFRLLTIFLLNMLILTCSNSLFLIFLGWEGGGFLSFLLISWWTTRNDASSSALEAVITNRIGNIGLITFMALSALNFNSSNLTNILSSNENLTPLLPFLLFGLILAAAGKSAQFGLHPWLPALLEGPTPVSALLHSSTMVVAGVFLLVRTSELFSSPLITHSLVLILGGTTALFAASTAIAQHDIKKIIAYSTTSQLGLMVTAIGIGQPALAFFHICTHAFFKAMLFLCSGSVIHSLSDEQDLRKMGGLSKLLPVTSSCLILGSLALMAPLLAGFYSKDLILEATSASVLNLLGIVLSIVATMLTAVYSFRIIFFCFSLSPSCSSPFSHSEENFNLNNALLRLATGTIASGWFFSNLLFAPPSFNVTSLAKGTPLIVPIIGVAALFMSLISSTSNSIGSNAHSATTSQWFFVDAVHLSIITMSLALSFFSSRTLDRGWQENIGPQGIAPTSTALSKISQAGQIGLIKRYILSSMASVLVILALSLLILS", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 5 family."}
{"protein": "MFGTPSRRTFLTASALSAMALAASPTVTDAIAAPGPDSWSALCERWIDIITGRRAARTSDPRARAIIAKTDRKVAEILTDLVSGSSRQTVLISADLRKEQSPFITKTARAIESMACGWATPGSSYHKDPEILSACIEGLRDFCRLRYNPSQDEYGNWWDWEDGASRAVADVMCILHDVLPPEVMSAAAAGIDHFIPDPWFQQPGSVKPTANPVQPVVSTGANRMDLTRAVMCRSIATGDEKRLRHAVDGLPDAWRVTTEGDGFRADGGFIQHSHIPYTGGYGDVLFSGLAMLFPLVSGMRFDIDESARKAFHDQVERGFIPVMYNGQILDDVRGRSISRINESAAMHGISIARAMLMMADALPTHRAEQWRGIVHGWMARNTFDHLSEPSTLVDISLFDAAAKAPRPGVVDAELLRVHGPSRPATADWLITVSNCSDRIAWYEYGNGENEWAYRTSQGMRYLLLPGDMGQYEDGYWATVDYSAPTGTTVDSTPLKRAVGASWAAKTPTNEWSGGLASGSWSAAASHITSQDSALKARRLWVGLKDAMVELTTDVTTDASRAITVVEHRKVASSSTKLLVDGNRVSSATSFQNPRWAHLDGVGGYVFATDTDLSADVATRKGTWIDVNPSRKVKGADEVIERAYASLHGHPPRSSSPWALLPTASRSHTMALATRPGVEPFTVLRNDGNRPGRASAGALLTKDPTVVTTLAFWKPATCGGVAVNRPALVQTRESANQMEVVIVEPTQKRGSLTVTIEGSWKVKTADSHVDVSCENAAGTLHVDTAGLGGQSVRVTLARQVTQTPSGGGRHDRA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 8 family."}
{"protein": "MIGTIAVLVIAILVIFAFKKSPSNIPPIVETIPFIGCFYQFAKNPLQLVRNSYDRLGEIFTLHLMGFKMTFVLGPEAQALFFRGTDEELSPKEAYRFVTPVFGKGVVYDSETEIMYEQLRFVKNGLVLSQLKKAVGIIQEETEKYFETKWGDSGEIDLLYEMNKLTILTASRCLMGKSINKSLGQSGQLADLYHELEEGLNPISFFFPNLPLPSFKKRDAARAKVAAIFHSIIQERRRSTDDSVDDVLYTLMNSKYKDGSVLEDEQIVGLMIGLLFAGQHTSSITLTYTIFYLLNNLEYFDETQKDINDIVQKENQGEINFDGLKRMNRLETVIREVLRLHPPLIFLMRKVMTPMEYKGKTIPAGHILAVSPQVGMRLPTVYKNPDSFEPKRFDVEDKTPFSFIAFGGGKHGCPGENFGILQIKTIWTVLSTKYNLEVGPVPPTDFTSLVAGPKGPCMVKYSKKQK", "text": "FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in cell membranes that participates in a variety of functions. Starting from lanosterol (lanosta-8,24-dien-3beta-ol), it catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of the sterol in the form of formate, and converts the sterol to 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, which is critical for ergosterol biosynthesis. Can demethylate susbtrates not intrinsic to yeast, such as eburicol (24-methylene-24,25-dihydrolanosterol) at a similar rate to lanosterol, and at a lower rate the 24,25- dihydrolanosterol (DHL) to 4,4-dimethyl-8,14-cholestadien-3beta-ol. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSANDFKPETWTSSANEALRVSIVGENAVQFSPLFTYPIYGDSEKIYGYKDLIIHLAFDSVTFKPYVNVKYSAKLGDDNIVDVEKKLLSFLPKDDVIVRDEAKWVDCFAEERKTHNLSDVFEKVSEYSLNGEEFVVYKSSLVDDFARRMHRRVQIFSLLFIEAANYIDETDPSWQIYWLLNKKTKELIGFVTTYKYWHYLGAKSFDEDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAIIQSWLEDKSITEITVEDPNEAFDDLRDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSLKLEERQFNRLVEMLLLLNNSPSFELKVKNRLYIKNYDALDQTDPEKAREALQNSFILVKDDYRRIIESINKSQG", "text": "FUNCTION: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the HAT1 family."}
{"protein": "MALASQLSVTDDSAYGFITTNAEIVSKKRKLAQNDDRFEVVMSVYSPKADSMDVGVSVLKLKTLELTLMSFCDSSTFVRTVNQIQVYEPTSIILPEAQSHSQIEKLKYIIHSNISDKVRERFMKAKVFNAFDGMNSLKLYTDINESTLGQVISNRKLSLAAANACIDYCVSTKMFRVTNKIRLKYCMCENTMLIDTCTVRDLELVDSLSETGTTLYSFLNCCLTKMGMRILRTSILQPSTHENSIILRSESLQELINDEDALISIRSSLKHTCDLEKVFSTFLEPRGLLSQEQEINNIILLKTVLQNTFVIRKSIQNVSSHLLVQVKQILEHENVQHLLAIINEYIRNDCQWANNSTELANQRANAVKSGVNGLLDVSRRIRETLLEEVSELVAKLSEELEIFMEYRFEISRGFFIKIKGNNTDINSLPEVLINRVKKRKTIECTTIELMKQSSRYNDIVSEITTLNSTIIHDMYTSINSYTPILLMVSEAIGTLDLLCSFAYFTSLQKDSYTCPEFAKEVTIMRSLHPILGGNNSNFVANNYSCNHELSRIHVITGANMSGKSVYLRQIAYLVIMAQMGCFVPAEYARMRIFNSLYSRISSDNVDINASSFSKEMSETAVILNDSDGDSLILIDELGRGSSLTDGFSICLAILEDLICKEATVITTTHFRDIAQVLANKSCVVTAHMQTVETNGQLEMKYNLVLGRNDIVGYGIRFAEVSNLLPQELIEDSKVVANILRSRKPVHGDKELKLLSRRRKLVLELYFALNYISKLNCDMNYKMQLLQTLQSKFVEEINITPNTE", "text": "FUNCTION: Involved in meiotic recombination. Facilitate crossovers between homologs during meiosis (By similarity). SIMILARITY: Belongs to the DNA mismatch repair MutS family."}
{"protein": "MGKKKFVNKNKAQTFHLVHRSQRDPQYHDENATERVLVSAETLNKTARRLNRQTLDEEYGSTIRPNEGEAANYGIYFDDTEYDYMQHLRNIGNEDATWVEAPATRKTQDKQKKQQIQLRDQPSILPQEVLPSEVELERTYQDQQSVPDAISGFQPDMDPRLREVLEQLEHSDINDEETSDFDEEFEKLVASGKADESEFYAQPFVEEGEKDYDEAAAAKAGKSEWEIEFEKFKLEQKKQPDVASSDGDFSDEPESEERDEVPELVSSSKSKSKTKRKARTALSSVSMSSSALFRNEGLTLLDDRFDKVEEEYTPIKDERELIDPDQKDVFDLVNDNQFNDIMDEFLVSYGPTLGRKKAPSRMSNSKKKSSLEELDNVRKMLGRARI", "text": "FUNCTION: Involved in protein transport. Non-ribosomal factor required for efficient nuclear export of the ribosomal 40S subunit. May participate in intracellular sorting of GAP1 out of the endosome (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the LTV1 family."}
{"protein": "MAVNQSHTENRRGVLIPNGESLLKQSLNVELSFPRQSEGSNVFNGTKTGTLFLTSYRVIFITSHSINGPMLSFMMPFDLITNLTVEQPVFAANFIKGTIQAAPYGGWEGQATFKLVFRNGGAIEFAQLMVKAASSVIAYGAPPAGYGAPPAGYGAPPPGYGAPPAGYGAPPPGYGAPPAGYGAQPAGNEGPPVGYRASPAGYGAPPLGYEAPPAGNEGLPAGYRASPAGSGARPHESAAAQAPENEASLPSASSS", "text": "FUNCTION: May play a role in meiotic resumption and pronuclear formation, mediated by a WW domain-signaling pathway during fertilization."}
{"protein": "RLRSKGKK", "text": "FUNCTION: [Venom peptide 7.1]: Has a weak inhibitory effect on voltage- gated sodium channel Nav1.5/SCN5A. Inhibits acetylcholine esterase in vitro. Increases interleukin-6 secretion from macrophages in vitro. Has no antifungal, antiviral or cytotoxic activity. FUNCTION: [Venom peptide 7.2]: Strongly inhibits acetylcholine esterase in vitro. Increases Il-6 secretion from macrophages in vitro. Has no antifungal, antiviral or cytotoxic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
{"protein": "MRVKVLSRNPDDYVRETKLDLQRVPRNYDPALHPFEVAREYVRALNATKLERVFAKPFLSSLDGHRDGVNCMAKHPKSLSTVLSGACDGEVRIWNLTKRQCIRALQAHEGFVRGMCARFCGTSFFTVGDDKTVKQWKMESPGYGEEEEPIHTILGKTVYTGIDHHWKDAVFATCGQQVDIWDEQRTSPMCSLTWGFDSISSVKFNPIETYLLGSCASDRNIVLYDMRQSTPLKKVILNMRTNTLCWNPMEAFIFTAANEDYNLYTFDMRFLTSPVMVHMDHVSAVLDVDYSPTGKEFVSASFDKSVRIFPVDKGHSREVYHTKRMQHVITVKWTSDSRYILCGSDEMNIRLWKANASEKLGVLAPREKAAMNYNQKLKEKFQHHPQIKRIARHRHLPKSIYCQIKEQRIMREARRRKELNRRKHSKPGSVPVVSEKKKHIVAVVQ", "text": "FUNCTION: Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre- rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre- ribosomal RNA by the RNA exosome. FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex. SUBCELLULAR LOCATION: Nucleus, nucleolus Note=In the nucleolus, localizes predominantly in the granular component, but also detected in the fibrillar center and dense fibrillar component. SIMILARITY: Belongs to the WD repeat DCAF13/WDSOF1 family."}
{"protein": "MTTFSEKEKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEHRANIVAEIGNGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDGLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELKKHDTKHELDVAPMFKSLIGKEISEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNKLSLDIPSNHRPVTSDKNSKLITTIKDVASSYVEQDEIFVSALVGATDASSFLGDNKDNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEASIQYLKEK", "text": "SIMILARITY: Belongs to the peptidase M20A family."}
{"protein": "MKPPMDLDSLLTQTPAKDNAALERVLAAARGELALRRPVRRWRTQAVGLMAASAGLGLLAAVVLLAVGAVTGPLLLARAPLLAMLVGTSAVCAWGALSPKGRWMRRLGVGLAVVSAAALVLARGAPHSPPSFPGWVCTVSHLAIGVVPLVVALFALRGAFFQPLRAVVAGLSVGSTGALLGELACEQDWRHVLSHHLLAWVVITVVLVVISKSLKPRSYAP", "text": "FUNCTION: Negative regulator of the carotenoid synthesis regulon. It is probably inactivated by protoporphyrin IX in the presence of blue light. Inactivation of CarR leads to loss of negative control over the carotenogenesis protein CarQ. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MVKNYSFYQFIMTVRGRKDDKGVFAEQIFEDLAFPKHEDDFNTLSEYIETHSEFTLPMSVFDDLYDDYTEWLKF", "text": "SIMILARITY: Belongs to the UPF0346 family."}
{"protein": "MSGGLDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTEWS", "text": "FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA. SUBCELLULAR LOCATION: Cell membrane Cytoplasm Nucleus Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Colocalizes with PPP1R16B in the cell membrane (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQGGKQ", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 2 family."}
{"protein": "MAISRGDLVRVKRPESYWYNEIGKVASVDTSGIKYNCVVRFDKVNYAGISGTEGGANTNNFAESELEKA", "text": "FUNCTION: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the PsaE family."}
{"protein": "MRIASSSGILMDANGKANGSAPSALVAYFLGMGFSREMVFRAIKEIGNDNNNTFPHLLQLLPFLSGDTDSEQILELLLTYQILEEEDEEEDVNWDEDDTVDNFDRATYSDGSGDEDFLQEMSEKDEKIKSLVSMGFPEDEAMRAITRCGLDASVDLLVESIYAPASAGNVYFTNLSDYEDTEFSSFGGRKKTKLIDGTKKKRERYRSRPQWNQVPFDGSHEEPMPLPNPMVGFSLPNDGLRSVHRNLPDHALGPPFFYYENVALAPKGVWTTISRFLYDIYPEFVDSKYFCAAARKRGYIHNLPIENRSPVLPIPPKTISEAFPSTKMWWPSWDPRRQFNCLQTYVASAKHTERIRCALGRFGDALPPAVQKSVLEECRKWNLVWVGKNKVATLEPDEMEFLLGYPRNHTRGVSRKRDIELLGIHSKLIQLHTTSLC", "text": "FUNCTION: Involved in de novo DNA methylation. Involved in RNA-directed DNA methylation (RdDM). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. DRM-methyltransferase family."}
{"protein": "MTQYFRALAFFLLLVPATAMACDDWPSWARGACQRVDQIWNEGGNDLYLTGYSWHNRAMYSSDKIRSFNELAWGGGLGKSIYDEDGDWQGLYAMAFLDSHSDIEPIAGYGFQKIGRIGADTRLGIGYTVFLTSRSDIMSRVPFPGILPLVSAGYRDATLYATYIPGGKGNGNVLFMFGRWEF", "text": "FUNCTION: Transfers a fatty acid residue from the sn-1 position of a phospholipid to the N-linked hydroxyfatty acid chain on the proximal unit of lipid A or its precursors. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the lipid A palmitoyltransferase family."}
{"protein": "MVYRRRRSRSADGTYTRRRRSSGYRRRPGRPRTYRRSRSATRRSGYRRRRY", "text": "FUNCTION: Thought to be responsible for DNA condensation during packaging of the nucleocapsids. SUBCELLULAR LOCATION: Virion."}
{"protein": "MSQDPYTPPPLPKPFTNTTPPPTLLTQGAEAHLYKTIHLNTNTPAALKIRPSKPYRHPILDRRLTRQRILQEARCLVKLVREGVNVPAVLALDWEGQGGENGNGGAWLLMEWIEGLVVRVVFERWEAFIKASGGSLGEKELRREEEKVRGLMRGIGGVVGGLHKAGVIHGDLTTSNLILRTGDVDIKDGESPAMVGDVVLIDFGLAGQSSSEEDRAVDLYVLERAFGSTHPQAEKFFEEVLEGYKDSYKGAAVTLKRLQDVRMRGRKRSMIG", "text": "FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, telomere. SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family."}
{"protein": "MPAIEIGRICVKTRGREAGKKCVIVDIIDENFVLVTGPKDVNKVKRRRVNILHLEPTDKKIDINKGASDDEVKKKLEEAGLIEFMKQDVKPKIPVI", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL14 family."}
{"protein": "MSVQPVAVYALKVPAGGALIPAVPDAAAMFRVSMAAIDPDEEPDFDGHDTNQRPRATLRIVRAPPGLDLEDDSDDDYEDVDSDEESDDEEPNGGPSDKEKARKLKELAALKEMEEAMDEDDEDEDEDEDGEFDLKAAISKLVKGKGPATDSDEDDEEDEGLELDEMVVCTLDTEKNLQQPLDITVSEDERVFFKVTGTHTVYLTGNYVMPIDPHFHGEDEDEEDEDDYDLSPDEDELALDLMGDDDNESDELDGLENPRITEVDSDEEPPKLVDTKGKNKRSAPADEEKPAKQANGEESLSKKQQKKLKKNNGDAAAVEQKKEAKEGKEAKKVQFAKNLEQGPTPSGQDKKPAEQTTGTLGVKEVKGVKIDDKKLGKGPAAKAGNTVAMRYIGKLEDGKVFDANKKGKPFTFKLGKGEVIKGWDIGVAGMAVGGERRISIPPHLAYGKKALPGIPGNSKLIFDVKLLEIK", "text": "FUNCTION: PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily."}
{"protein": "MYPRVMHAVCFLALSLVSYVAVCAETKVATNCLVKSENTHLTCKCSPNNTSSNTGNGSKCHAMCKCRITEPITMLGAYSAWGAGSFVATLIVLLVVFFVIYAREEEKNNTGTEVDQCLAYRSLTRKKLEQHAAKKQNIYERIPYRPSRQKDNSPLIEPTGTDDEEDEDDNV", "text": "SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HHV-5 RL10 protein family."}
{"protein": "MSSGNSSTGTHTNGNFATLGSSPPSAVGGKGRAIPPKVTHEDASVELKTMNPERGAARGSIPLGEDIMQIARIGEVPAMQRLFDEKKFSANHKDEEGITPLHWAAINNQYAMCKFLLDSGADVNAKGGESVATPAMWAAQRCHYYIVHLLLQRGADPLLTDVQGYNILHLATIDGNAFLLVLLLHQEIPVDVVDQQGHTGLMWAAYKGYPALVDLFLRWGAHANAVDEGGLTPLHWALVKGSLPCVLKLIEYGADKFAKTRDGKTPAVVAGEMNTTRVWYRALDEYGYDLDGNAKVSSSGLASWVRNKSLMSKFFFLWPFAIVFAAVWILSNMVVYAAIPMMLVTVFGLQWVAQKAASQGPSEYRILQKTPYLSGVFAGSLFWVGFRYVFYVLPVTYSTSPILNGLFAIFFSLTTYFYIYSMVEDPGFVPKLGSRNQQRAVITELFEQWKFDEENFCVSCMVRRPLRSKHCKRCARCVAKHDHHCPWIDNCVGANNLRHFVLYITCLEVGIVLFVQLTFNYINSLPAPAQPQCNIINETLCDFVLRDTFTLVLDLWVCIQLVWITMLVAVQMIQISRNQTTYENMRGHSVDRSYPSSRAFASAVAAGTTSLNAAGLTSSGQGPNPALAQGAPRHRKHGCLQQWSSLLGIDTFFATARDGLRDGPRAVRPKNPFSRGVVTNCRDFWCDPAPYFGKREPGAAMLGGEVINYNRMYETPSRMHSGGGYQSLSVEDPEQGV", "text": "FUNCTION: Palmitoyltransferase specific for casein kinase 1. SUBCELLULAR LOCATION: Early endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily."}
{"protein": "MASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY", "text": "FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition (PubMed:25361978). FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase. SIMILARITY: Belongs to the PA28 family."}
{"protein": "MPIKPVGWICGQVLKNFSGRIEGIQKVIMDLIDEFKDEFPTILRLSQSNQKREPMQKPSKIRMAIALAKINRGTLIQGLNSISRSSKSVAKLLQPQLACRLLELRAISHRLLKEVNAPRQPLYNIQVRKGSLFEIISFPAKTALTSIMCASYAALIYLTVCVNAVLEKIMKIFQEEESIRQNREESENFRNAFSEPVLSEPLFPEGEIKAKPYRSLPEKPDSISDRPKLPANKLSNKIQVLHSVFDQSAEMNE", "text": "FUNCTION: May play at role in testicular development/spermatogenesis and may be an important factor in male infertility. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MQLRKLLLPGLLSVTLLSGCSLFNSEEDVVKMSPLPTVENQFTPTTAWSTSVGSGIGNFYSNLHPALADNVVYAADRAGLVKALNADDGKEIWSVSLAEKDGWFSKEPALLSGGVTVSGGHVYIGSEKAQVYALNTSDGTVAWQTKVAGEALSRPVVSDGLVLIHTSNGQLQALNEADGAVKWTVNLDMPSLSLRGESAPATAFGAAVVGGDNGRVSAVLMEQGQMIWQQRISQATGSTEIDRLSDVDTTPVVVNGVVFALAYNGNLTALDLRSGQIMWKRELGSVNDFIVDGNRIYLVDQNDRVMALTIDGGVTLWTQSDLLHRLLTSPVLYNGNLVVGDSEGYLHWINVEDGRFVAQQKVDSSGFQTEPVAADGKLLIQAKDGTVYSITR", "text": "FUNCTION: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the BamB family."}
{"protein": "MYKNQLQELAQRSCFNLPAYTCLREGPDHAPRFKAAVNFNGEQFESPGFFTTLRQAEHAAAEVALAALARRGPSYSLAARILDETGVYKNLLQEVAQRVGAPLPSYTTERSGLGHLPVFTCTVELAGITFTGDPAKNKKQAEKNAASAAWSSLRQLVRQEASSSNEPESNDEQEQIRIARALLNYRLKEKMAMANNPHASPFPKKFPMQPERRTAFPQSSHSSYSKILPLFRPKSNSRSRPESPAASDAASQTPFRPTESPNPRSRFPAAEAAPYVPVGHFRMPCHSMAPPVTVRTSIPVFSAPPLPPPGARTQQLPPLMSHPPPIRMASPVRIRPAPPLFTPSAVQGPKPMMPVQIKDVQHQQIKETRSPVMPVQVKDAQNQLLKGSLSPVIPVQIKDVQSQPPKEALSPAIPVQIKDVQLQPRNEPVSIGKGVVPLPAIRPPVKVEAPAEVKEASQPVAGSSVVQCKADTSPDSLPKTQLKTANADNADAKDDHLPVDAEEVEDIIRHLELK", "text": "FUNCTION: Binds double-stranded RNA."}
{"protein": "MESVIFSINGEIIQVNKEIITASPYNFFKRIQDHHLKDEAIILNGINYHAFESLLDYMRWKKINITINNVEMILVAAIIIDVPPVVDLCVKTMIHNINSTNCIRMFNFSKRYGIKKLYNASMSEIINNITAVTSDPEFGKLSKDELTTILSHEDVNVNHEDVTAMILLKWIHKNPNDVDIINILHPKFMTNTMRNAISLLGLTISKSTKPVTRNGIKHNIVVIKNSDYISTITHYSPRTEYWTIVGNTDRQFYNANVLHNCLYIIGGMINNRHVYSVSRVDLKTKKWKTVTNMSSLKSEVSTCVNDGKLYVIGGLEFSISTGVAEYLKHGTSKWIRLPNLITPRYSGASVFVNDDIYVMGGVYTTYEKYVVLNDVECFTKNRWIKKSPMPRHHSIVYAVEYDGDIYAITGITHETRNYLYKYIVKEDKWIELYMYFNHVGKMFVCSCGDYILIIADAKYEYYPKSNTWNLFDMSTRNIEYYDMFTKDETPKCNVTHKSLPSFLSNCEKQFLQ", "text": "SIMILARITY: Belongs to the poxviruses Kelch family."}
{"protein": "MVSQSTVRQDSPVEPWEGISDHSGIIDGSPRLLNTDHPPCQLDIRLMRHKAVWINPQDVQQQPQDLQSQVPAAGNSGTHFVTDAASPSGPSPSCLGDSLAETTLSEDTTDSVGSASPHGSSEKSSSFSLSSTEVHMVRPGYSHRVSLPTSPGILATSPYPETDSAFFEPSHLTSAADEGAVQVSRRTISSNSFSPEVFVLPVDVEKENAHFYVADMIISAMEKMKCNILSQQQTESWSKEVSGLLGSDQPDSEMTFDTNIKQESGSSTSSYSGYEGCAVLQVSPVTETRTYHDVKEICKCDVDEFVILELGDFNDITETCSCSCSSSKSVTYEPDFNSAELLAKELYRVFQKCWILSVVNSQLAGSLSAAGSIVVNEECVRKDFESSMNVVQEIKFKSRIRGTEDWAPPRFQIIFNIHPPLKRDLVVAAQNFFCAGCGTPVEPKFVKRLRYCEYLGKYFCDCCHSYAESCIPARILMMWDFKKYYVSNFSKQLLDSIWHQPIFNLLSIGQSLYAKAKELDRVKEIQEQLFHIKKLLKTCRFANSALKEFEQVPGHLTDELHLFSLEDLVRIKKGLLAPLLKDILKASLAHVAGCELCQGKGFICEFCQNTTVIFPFQTATCRRCSACRACFHKQCFQSSECPRCARITARRKLLESVASAAT", "text": "FUNCTION: Regulator of autophagy that promotes autophagosome maturation by facilitating the biogenesis of phosphatidylinositol 3-phosphate (PtdIns(3)P) in late steps of autophagy (PubMed:28306502, PubMed:30704899). Acts by antagonizing RUBCN, thereby stimulating phosphatidylinositol 3-kinase activity of the PI3K/PI3KC3 complex (PubMed:28306502). Following anchorage to the autophagosomal SNARE STX17, promotes the recruitment of PI3K/PI3KC3 and HOPS complexes to the autophagosome to regulate the fusion specificity of autophagosomes with late endosomes/lysosomes (PubMed:28306502). Binds phosphoinositides phosphatidylinositol 3-phosphate (PtdIns(3)P), 4- phosphate (PtdIns(4)P) and 5-phosphate (PtdIns(5)P) (PubMed:28306502). In addition to its role in autophagy, acts as a regulator of lipid and glycogen homeostasis (By similarity). May act as a tumor suppressor (Probable). SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein Note=Associates with late autophagic structure (PubMed:28306502). Recruitment to autophagosome membrane is promoted by autophagic stimuli (PubMed:28306502)."}
{"protein": "MPSELAMNNDELHVVMFPFLAFGHISPFVQLSNKLFSHGVHVTFLSAASNIPRIRSTLNLNPAINVISLKFPNGITNTAELPPHLAGNLIHALDLTQDQVKSLLLELKPHYVFFDFAQHWLPKLASEVGIKSVHFSVYSAISDAYITVPSRFADVEGRNITFEDLKKPPPGYPQNSNISLKAFEAMDFMFLFTRFGEKNLTGYERVLQSLGECSFIVFKTCKEIEGPYLDYIETQFRKPVLLSGPLVPEPSTDVLEEKWSKWLDGFPAKSVILCSFGSETFLSDYQIKELASGLELTGLPFILVLNFPSNLCQS", "text": "FUNCTION: Has no flavonol 3-O-glucoside (1->6) rhamnosyltransferase activity in vitro."}
{"protein": "MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFSIPMLDLDDDDDREESLMMNRLASVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPERPPPIPPDNRLSRHFHHGESVPSRDQPMPLEAWCPRDAFGTNQVMGCRILGDGSPKPGVTANSSLNGRHSRMGSEQVLMRKHRRHDLPSEGAKVFSNGHLATEEYDVPPRLSPPPPVTTLLPSIKCTGPLANCLSEKTRDTVEDDDDEYKIPSSHPVSLNSQPSHCHNVKAPVRSCDNGHCILNGTHGAPSEMKKSNIPDLGIYLKGGGSDSASDPVPLPPARPPPRDSPKHGSSVNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFFDPTSGQVPLPPARRAAGDSGKANRASQDYDQLPSSSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL", "text": "FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (PubMed:29237719). SUBCELLULAR LOCATION: Cytoplasm Note=In adipocytes, translocates to the plasma membrane upon insulin stimulation."}
{"protein": "MDIIIKNGTIVTADGISRADLGIKDGKITQIGGALGPAERTIDAAGRYVFPGGIDVHTHVETVSFNTQSADTFATATVAAACGGTTTIVDFCQQDRGHSLAEAVAKWDGMAGGKSAIDYGYHIIVLDPTDSVIEELEVLPDLGITSFKVFMAYRGMNMIDDVTLLKTLDKAVKTGSLVMVHAENGDAADYLRDKFVAEGKTAPIYHALSRPPRVEAEATARALALAEIVNAPIYIVHVTCEESLEEVMRAKSRGVRALAETCTHYLYLTKEDLERPDFEGAKYVFTPPARAKKDHDVLWNALRNGVFETVSSDHCSWLFKGHKDRGRNDFRAIPNGAPGVEERLMMVYQGVNEGRISLTQFVELVATRPAKVFGMFPQKGTIAVGSDADIVLWDPEAEMVIEQTAMHNAMDYSSYEGHKVKGVPKTVLLRGKVIVDEGSYVGEPTDGKFLKRRKYKQ", "text": "FUNCTION: Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family."}
{"protein": "MAGYEYVSPEQLAGFDKHKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLLVVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPLGELFDHGLDNWSYVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGILFLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLLNFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAFANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIHYGVRVVKQLSSHFQIYPFSLRKPNSDULGMEEKNIGL", "text": "FUNCTION: Ethanolaminephosphotransferase that catalyzes the transfer of phosphoethanolamine/PE from CDP-ethanolamine to lipid acceptors, the final step in the synthesis of PE via the 'Kennedy' pathway. PE is the second most abundant phospholipid of membranes in mammals and is involved in various membrane-related cellular processes. The enzyme is critical for the synthesis of several PE species and could also catalyze the synthesis of ether-linked phospholipids like plasmanyl- and plasmenyl-PE which could explain it is required for proper myelination and neurodevelopment. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family."}
{"protein": "MKPDETPMFDPSLLKEVDWSQNTAIFSPAISPTHPGEGLVLRPLCTADLNKGFFKVLGQLTETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVEDVVVSDECRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFDYTVSEENYMCRRFLK", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily."}
{"protein": "MVEELLSLLHALLDRHQALCMENHQLLKQLRLLVCERARLLRQVCPPSCPVPYPSRFSGESGRLPEFIMQTMSYMLANEEHFCNDAMKVAFLISLLSGEAEEWVMPYIESNSYVLGDYQAFVDEMKQYFGWGTDDEDDGDDDEEEEMEEDH", "text": "FUNCTION: May have an important role in the development and/or progression of some cancers. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the LDOC1 family."}
{"protein": "NQFDILLCSNLFGDIISDECAVITGSIGMLPSASFNEKNFGLYEPAGGSAPDIAGKNIANPIAQILSLSMLVRYGMKLKKIADKIDKSVASALKAGYRTADISNNNSYLKTNEMGDVISDFLINGK", "text": "FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily."}
{"protein": "MAETQTVNPMRKLRLEKVTVNIGVGEAGERLQKAYQLLQELTGVKPVYTIAKRTIREFGVRKGAPIGVKVTLRGKKAEEFLNKVLAAVGHRIKASSFDEYGNVSFGIAEHVLIPGTRYDPEIGIFGMDVAITLVRPGFRVARRRRKKAHIPKRHRTVSKEEAMEFLKQNFNVTIVEG", "text": "FUNCTION: This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
{"protein": "MENMENDENIVYGPEPFYPIEEGSAGAQLRKYMDRYAKLGAIAFTNALTGVDYTYAEYLEKSCCLGEALKNYGLVVDGRIALCSENCEEFFIPVLAGLFIGVGVAPTNEIYTLRELVHSLGISKPTIVFSSKKGLDKVITVQKTVTAIKTIVILDSKVDYRGYQSMDNFIKKNTPQGFKGSSFKTVEVNRKEQVALIMNSSGSTGLPKGVQLTHENAVTRFSHARDPIYGNQVSPGTAILTVVPFHHGFGMFTTLGYLTCGFRIVMLTKFDEETFLKTLQDYKCSSVILVPTLFAILNRSELLDKYDLSNLVEIASGGAPLSKEIGEAVARRFNLPGVRQGYGLTETTSAIIITPEGDDKPGASGKVVPLFKAKVIDLDTKKTLGPNRRGEVCVKGPMLMKGYVDNPEATREIIDEEGWLHTGDIGYYDEEKHFFIVDRLKSLIKYKGYQVPPAELESVLLQHPNIFDAGVAGVPDPIAGELPGAVVVLEKGKSMTEKEVMDYVASQVSNAKRLRGGVRFVDEVPKGLTGKIDGKAIREILKKPVAKM", "text": "FUNCTION: Produces green light. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MTIQAKPSSSISYDSTTYGTAPGLDIKEFQIIEDWNGRPASAWSVQRIGLLQSKIERYTYNIYHNNKYGKHNLSKLIPGHALIQFANETFGYDGWRMDVIDVEARECQPFTAVNNGENTNTSEVKYTVVAEAQVKVTLKDGTNTQCGGLGRITLSSRGECYNRSKKEAVGDALKKALLSFEKIILDYETKITNNYYVDGLYGSKKIKNEANTNYNLLSATNSKPTFIKLEDAKGTHIK", "text": "FUNCTION: Involved in the repair of double-strand breaks in DNA during vegetative growth via recombination and single-strand annealing. Anneals complementary single-stranded DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RAD52 family."}
{"protein": "MTGGQVKVFGKAIQTLSRVSDELWLDPSEKGLALRSVNSCHSTYGYVLFSSVFFQHYQWSPSATITDSDIPLNLNCKLAIKSILPIFRCLNYLERSIEKCTMVARSDRCRVVIQFFGRHGIKRTHNVYFQDCQPLKILFEKSLCANILMIKPRLLAEAIALLTSNQEEVTFSVTPENFCLKSSSGESLDLTSSVYSEMSFGPEEFDFFQVGLDTEITFCFKELKGILTFSEVMHAPIAIYFDFPGKPVVLSVEDMLLEASFILATLLDYPSRTSSPQSLRLSQARRSDPTLSGAQEGKSRVSQTPESISRAAPKRLFPKDPPDSSSAAETRRASASQDDISEVPESVVSDMEEGQSPSPLRKFSCMFFGAVSCEQQEHANHPLGSLAVASDSEQDASG", "text": "SIMILARITY: Belongs to the rad9 family."}
{"protein": "MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQLLEGPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVPSTETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQTTSMRDVYRKFDLGQDVIDFTGHALALYRTDDYLDQPCLETVNRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVRKAGQVIRIICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETTDPEKEVEPALELLEPIDQKFVAISDLYEPIDDGCESQVFCSCSYDATTHFETTCNDIKDIYKRMAGTAFDFENMKRKQNDVFGEAEQ", "text": "FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes (By similarity). FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus, trans-Golgi network. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus, trans- Golgi network. SIMILARITY: Belongs to the Rab GDI family."}
{"protein": "MNEAILSRNHVKVKGSGKASIMFAPGFGCDQSVWNAVAPAFEEDHRVILFDYVGSGHSDLRAYDLNRYQTLDGYAQDVLDVCEALDLKETVFVGHSVGALIGMLASIRRPELFSHLVMVGPSPCYLNDPPEYYGGFEEEQLLGLLEMMEKNYIGWATVFAATVLNQPDRPEIKEELESRFCSTDPVIARQFAKAAFFSDHREDLSKVTVPSLILQCADDIIAPATVGKYMHQHLPYSSLKQMEARGHCPHMSHPDETIQLIGDYLKAHV", "text": "FUNCTION: Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity. SIMILARITY: Belongs to the AB hydrolase superfamily."}
{"protein": "MRFDTIIMGGGLAGLLCGLQLQKHGLRCAIVTRGQSALHFSSGSLDLLSHLPDGQAVTDIHSGLESLRQQAPAHPYSLLGPQRVLDLACQAQALIAESGAQLQGSVELPHQRITPLGTLRSTWLSSPEVPVWPLPAKKICVVGISGLMDFQAHLAAASLRELDLAVETAEIELPELDVLRNNATEFRAVNIARFLDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVLGIRLQNQLQRQFVRQGGVWMPGDEVKKVTCKNGVVNEIWTRNHADIPLRPRFAVLASGSFFSGGLVAERNGIREPILGLDVLQTATRGEWYKGDFFAPQPWQQFGVTTDQTLRPSQAGQTIENLFTIGSVLGGFDPIAQGCGGGVCAVSALHAAQQIAQRAGGQQ", "text": "FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein Note=Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase. SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B family."}
{"protein": "MAHRRRCLLLLLAVLLPAMAARGDPDAVQDFCVPDAGRGRPVELAMLPAYPCRSPANLTAGDFAFSGVRAAGNFSPETGFAGVSVTPAQFPGLHTLGMSFARADLSAAGGVNPPHYHPRATETALVLAGRVYAGFVDSGGRLFAKVLEQGEVMVFPRAMVHFQLNVGDTPATVYGAFNSENPGIVRIPATVFGSGIREAVLERAFGLTPAELRRLEKRFGPPKKAEMED", "text": "FUNCTION: May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the germin family."}
{"protein": "MATVIQNPLKALGDQFYREAIEHCRSYNARLCAERSVRMPFLDSQTGVAQNNCYIWMEKRHRGPGMAAGQMYTYPARCWRKKRRLHTPLDPQLRLCELRLEAELMAKREAPQTEATALEALLRGDGILDKRNNNAKEEETLLEIQRVLEADENGDGFHDDEDFEVDTPKRKHRNKGRGRGSGRRRTEAVANDDQDKPYVCDNRYKQKHNSKTADSVCGKRYKNRPGLSYHYAHTHLAEEEGEEERETEIPQSPPVHHENHKPQKAPDGSIIPNDYCDFCLGDSGSNRKTGQAEELVSCSDCGRSGHPSCLQFTDNMMQAVRTYQWQCIECKSCSLCGTSENDDQLLFCDDCDRGYHMYCLKPPMTQPPEGSWSCHLCQNLLKDKASGVEDP", "text": "FUNCTION: Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4. In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex) and may play a role in neural development (By similarity). Plays an essential role in heart and skeletal muscle development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MVDYYEVLGVQKHASAEDIKKAYRKLALKWHPDKNPENKEEAEQQFKQVAEAYEVLSDAKKRDIYDRFGKEGLINGGGGGSHHDNPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGGRRGPRGSRSRAGGSFLSAFGGFPAFGNAFPSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSVSTSTKIVNGRKITTKRIVENGQERVEVEEDGQLRSLTINGEANEEAFAEECRRRGQHALPFQPTNTRLLKPHKPASSPRYAYHYNSDEVEEQEKSRVASSLETPFYLSGYKEGSKRRKQKQREEQKKKKSTKGSY", "text": "FUNCTION: Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co- chaperone of HSP70. Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Also reduces cellular toxicity and caspase-3 activity. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Nucleus."}
{"protein": "MTEEHVVYIGKKPVMNYVLAVITQFHEGAKEVSIKARGRAISRAVDVAEIVRNRFLKDDVDVKEIKIGTEELPTADGRTTNTSTIEIVLARKT", "text": "FUNCTION: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes. SUBCELLULAR LOCATION: Cytoplasm Chromosome. SIMILARITY: Belongs to the histone-like Alba family."}
{"protein": "MNAIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEAVMLKIAELLNVEPQPLDGEAPELTPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQPVAETPDSWKWDLNTIPVRIIPVEHHA", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily."}
{"protein": "MTVQRLVAAAVLVALVSLILNNVAAFTSNWVCQTLEDGRRRSVGLWRSCWLVDRTRGGPSPGARAGQVDAHDCEALGWGSEAAGFQESRGTVKLQFDMMRACNLVATAALTAGQLTFLLGLVGLPLLSPDAPCWEEAMAAAFQLASFVLVIGLVTFYRIGPYTNLSWSCYLNIGACLLATLAAAMLIWNILHKREDCMAPRVIVISRSLTARFRRGLDNDYVESPC", "text": "FUNCTION: Can influence paracellular permeability. Appears to be involved in cell-cell interactions through adherens. SUBCELLULAR LOCATION: Cell junction, adherens junction Cell membrane; Multi-pass membrane protein Note=Colocalizes with the beta-catenin adherins."}
{"protein": "MVTLYLHVPILLLVVITARAAPKPDTHNPFDELSSVAEKQDLHYGDRSRKDPFIAQNDVGNNFRDGTQENLTKVRSKVNQYDQPFTFKCPLGETIKSIGSIHDNHYEDRQWDIDCKPAGYTMGISTWSPYANDYDGSMNFECNEGSVVTGMSSIHDNYYEDRRYQLMCSYLNNWKRGSCAWTSYTTYDASFVELTPTGKFLVGMKSQHNNYYEDRKFKMLYC", "text": "FUNCTION: Is potently cytotoxic (EC(50) value 79 ng/mL) towards L1210 mouse leukemia cells, has hemagglutination activity on sheep erythrocytes, and is lethal in crayfish. Has no phospholipase A2 activity. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the dermatopontin family."}
{"protein": "MKYPLDCEENFEKSFLFWLAKYVKFKLNSLSNKELKNPQALAEVNFALTKGVKNIDELDALAKKARNAGLSGVNTYFNPLKKVFEYLNFYKLYSLKQIDEELIVEVLASITGALSDASKKNYRIAVINFFDFLDKQNEEDEKAHIFDINLKNWAGIAGSKGVKLPEFMSKEELKKFLDAIENADFKNNTIRNKLIIKIIIFTGIRVSEAINIKMGDISEENDLYIIRIRAKGNKYRVVMIKKELIYDLLKNVSINYISKDALLFVNKKGTPLTQSYVSRIVEQLLFRAGIRKQKNGAHMLRHTFATLLYKKQKDLVLVQEALGHASLNTSRIYTHFDNDKLKLAAQVAKELSDS", "text": "FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds to the complete atypical dif motif (difH) site and to both halves separately. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerH subfamily."}
{"protein": "MPQRTFLMMLIVVCVTILCFVWMVRDSLCGFRIEQGNTVLVATLAYEVKR", "text": "FUNCTION: When overexpressed kill the cells from the inside by interfering with a vital function in the cell membrane. FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system (By similarity). Toxic component of a type I toxin-antitoxin (TA) system (By similarity). When expressed is involved in cellular Mg(2+) release and degradation of stable RNA (PubMed:2465777). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Hok/Gef family."}
{"protein": "MPTISVAMIIKNEAQDLANCLDTVKDWVDEIIILDSGSTDNTKEIALSYGAKFYENSDWQGFGKQRQLAQQYVTSDYVLWLDADERVTPKLQQAILSAVKNDRENTVYEIPRVSEVFGREIRHSGWYPDYVVRLYRTNYAQYNDSLVHEKVEFPAGTKVEKLTGDLEHFTYKSIHHYLVKSAGYAKAWADQRQAKGKKATLWQGISHALGCFVKMYLLKAGFLDGKQGFLLAVLSAHSTFVKYADLWERDQHKH", "text": "SIMILARITY: Belongs to the glycosyltransferase 2 family. WaaE/KdtX subfamily."}
{"protein": "MFFLYTDFFLSLVAVPAAAPVCQPKSATNGQPPAPAPTPTPRLSISSRATVVARMEGTSQGGLQTVMKWKTVVAIFVVVVVYLVTGGLVFRALEQPFESSQKNTIALEKAEFLRDHVCVSPQELETLIQHALDADNAGVSPIGNSSNNSSHWDLGSAFFFAGTVITTIGYGNIAPSTEGGKIFCILYAIFGIPLFGFLLAGIGDQLGTIFGKSIARVEKVFRKKQVSQTKIRVISTILFILAGCIVFVTIPAVIFKYIEGWTALESIYFVVVTLTTVGFGDFVAGGNAGINYREWYKPLVWFWILVGLAYFAAVLSMIGDWLRVLSKKTKEEVGEIKAHAAEWKANVTAEFRETRRRLSVEIHDKLQRAATIRSMERRRLGLDQRAHSLDMLSPEKRSVFAALDTGRFKASSQESINNRPNNLRLKGPEQLNKHGQGASEDNIINKFGSTSRLTKRKNKDLKKTLPEDVQKIYKTFRNYSLDEEKKEEETEKMCNSDNSSTAMLTDCIQQHAELENGMIPTDTKDREPENNSLLEDRN", "text": "FUNCTION: Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K(+) currents. Activated by arachidonic acid and other naturally occurring unsaturated free fatty acids. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the two pore domain potassium channel (TC 1.A.1.8) family."}
{"protein": "MTSTRKLSVSCLIVFMVSSLIAVSSGWLSSTGKSPLKIGKCDPKNGNLYAIGRKWYNDEDCFEITCIQGDKGSVAQQVASCPVHAVKPGCELVFPGGTYPKCCPYYECPNS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-16 family."}
{"protein": "MLATGATVSTAGLAQVDREKIYQWINELSSPETRENALLELSKKRESVTDLAPMLWHSCGTIAALLQEIVNIYPSINPPTLTAHQSNRVCNALALLQCVASHVETRSAFLAAHIPLFLYPFLHTVSKTRPFEYLRLTSLGVIGALVKTDEQEVINFLLTTEIIPLCLRIMESGSELSKTVATFILQKILLDDTGLAYICQTYERFSHVAMILGKMVLQLSKEPSARLLKHVVRCYLRLSDNSRAREALRQCLPDQLKDTTFAQVLKDDSTTKRWLAQLVKNLQEGQVTDPRGIPLPTQ", "text": "FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down- regulation of MYB- and JUN-dependent transcription. Enhances ligand- dependent transcriptional activity of nuclear hormone receptors. May play a role in cell differentiation. SUBCELLULAR LOCATION: Nucleus Cytoplasm, P-body. SIMILARITY: Belongs to the CNOT9 family."}
{"protein": "MSPSDVPINWKRNLTVTWLGCFLTGAAFSLVMPFLPLYVEQLGVTGHSALNMWSGLVFSITFLFSAIASPFWGGLADRKGRKIMLLRSALGMAIVMLLMGMAQNIWQFLILRALLGLLGGFIPNANALIATQVPRHKSGWALGTLSTGGVSGALLGPLAGGLLAGHYGLRPVFFITASVLFICFLLTFFFIRENFLPVSKKEILHVREVVASLKNPRLVLSLFVTTLIIQVATGSIAPILTLYVRELAGNVSNIAFISGMIASVPGVAALLSAPRLGKLGDRIGPEKILIVALIISVLLLIPMSFVQTPWQLALLRFLLGAADGALLPAVQTLLVYNSTNQIAGRIFSYNQSFRDIGNVTGPLMGAAISASYGFRAVFCVTAGVVLFNAIYSWNSLRRRRLAIE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. MdtG (TC 2.A.1.2.20) subfamily."}
{"protein": "MTEFPVVLVINCGSSSIKFSVLDAASCDCLLNGVAEGINAERAFLSLNGGEPVALAPRGYEGALQAIAGALAQRDLIDSVALIGHRVAHGGDLFTESVIISEEVINNIRQVSSLAPLHNYASLSGIASAQRLFPQVMQVAVFDTSFHQTLAPEAFLYGLPWEYYQNLGVRRYGFHGTSHRYVSRRALALLGLPEQESGLVIAHLGNGASICAVRNGRSVDTSMGMTPLEGLMMGTRSGDVDFGAMAWIAGETRQTLSDLERVANTASGLLGISGLSSDLRVLEQAWHEGHARARLAIKTFVHRIARHIAGHAAALQRLDGIIFTGGIGENSVLIRRLVSERLAVFGLEMDVARNQQPNSVGERLISADASRVRCAVIPTNEERMIALDAIRLGRIHTAALA", "text": "FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. SIMILARITY: Belongs to the acetokinase family. TdcD subfamily."}
{"protein": "MTASGGGSTAATGRMPTWKERENNKKRERRRRAIAAKIFTGLRSQGNYKLPKHCDNNEVLKALCLEAGWIVHEDGTTYRKGSRPTETTVPCSSIQLSPQSSAFQSPIPSYQASPSSSSYPSPTRFDPNQSSTYLIPYLQNLASSGNLAPLRISNSAPVTPPISSPRRSNPRLPRWQSSNFPVSAPSSPTRRLHHYTSIPECDESDVSTVDSCRWGNFQSVNVSQTCPPSPTFNLVGKSVSSVGVDVSVKPWEGEKIHDVGIDDLELTLGHNTKGRG", "text": "SIMILARITY: Belongs to the BZR/LAT61 family."}
{"protein": "MDMMGLAGTSKHITFLLLCQLGASGPGDGCCVEKTSFPEGASGSPLGPRNLSCYRVSKTDYECSWQYDGPEDNVSHVLWCCFVPPNHTHTGQERCRYFSSGPDRTVQFWEQDGIPVLSKVNFWVESRLGNRTMKSQKISQYLYNWTKTTPPLGHIKVSQSHRQLRMDWNVSEEAGAEVQFRRRMPTTNWTLGDCGPQVNSGSGVLGDIRGSMSESCLCPSENMAQEIQIRRRRRLSSGAPGGPWSDWSMPVCVPPEVLPQAKIKFLVEPLNQGGRRRLTMQGQSPQLAVPEGCRGRPGAQVKKHLVLVRMLSCRCQAQTSKTVPLGKKLNLSGATYDLNVLAKTRFGRSTIQKWHLPAQELTETRALNVSVGGNMTSMQWAAQAPGTTYCLEWQPWFQHRNHTHCTLIVPEEEDPAKMVTHSWSSKPTLEQEECYRITVFASKNPKNPMLWATVLSSYYFGGNASRAGTPRHVSVRNQTGDSVSVEWTASQLSTCPGVLTQYVVRCEAEDGAWESEWLVPPTKTQVTLDGLRSRVMYKVQVRADTARLPGAWSHPQRFSFEVQISRLSIIFASLGSFASVLLVGSLGYIGLNRAAWHLCPPLPTPCGSTAVEFPGSQGKQAWQWCNPEDFPEVLYPRDALVVEMPGDRGDGTESPQAAPECALDTRRPLETQRQRQVQALSEARRLGLAREDCPRGDLAHVTLPLLLGGVTQGASVLDDLWRTHKTAEPGPPTLGQEA", "text": "FUNCTION: Functions as an interleukin receptor which binds interleukin- 12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily."}
{"protein": "MIETYSQTAPRSVATGPPVSMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLYEDFVFMKTLQKCNKGEGSLSLLNCEEIKSQFEAFLKEIMLNNEMKKEENIAMQKGDQDPRIAAHVISEASSNPASVLRWAPKGYYTISSNLVSLENGKQLAVKRQGLYYVYAQVTFCSNRAASSQAPFVASLCLHSPSGTERVLLRAASSRGSSKPCGQQSIHLGGVFELHPGASVFVNVTDPSQVSHGTGFTSFGLLKL", "text": "FUNCTION: Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation (By similarity). Induces the activation of NF-kappa-B (By similarity). Induces the activation of kinases MAPK8 and PAK2 in T-cells (By similarity). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (By similarity). Involved in immunoglobulin class switching (By similarity). FUNCTION: [CD40 ligand, soluble form]: Acts as a ligand for integrins, specifically ITGA5:ITGB1 and ITGAV:ITGB3; both integrins and the CD40 receptor are required for activation of CD40-CD40LG signaling, which have cell-type dependent effects, such as B-cell activation, NF-kappa-B signaling and anti-apoptotic signaling. SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted Note=Release of soluble CD40L from platelets is partially regulated by GP IIb/IIIa, actin polymerization, and a matrix metalloproteinases (MMP) inhibitor-sensitive pathway. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Cell surface. SIMILARITY: Belongs to the tumor necrosis factor family."}
{"protein": "MYIVAISLLSHTIWIQGVFFLFGLALGVISAFKIFTKTLAQKNEVIRNLEHDKAILQMSLDARRNQEQLIEEFSHKLTSVSQAFARDIKTESQEFFSEKTQAIHSVLAPMHNTLSVFKQNLENFETKQAEDRGALREQLSQLLTAEKKLERETQALTNILKHPGSRGRWGEIQLERILEISGMLKYCDYSVQTVDANDSSSRADIVIRLPQNRSLVIDAKTPFSEEYLTDSHADPTDLVKKIKDHIKTLKTKSYWDKFDQSPEFVILFLPGESLFNDAIRCAPELMDYAGQSNVILSSPVTLMALLKTVTYVWKQENLQNQIREIGQLGKDLYQRMHKLFDHFHKVGKHLGQAVHSYNDMSSSLSARVLPILRTFDKLEISSSHNKIEGLSQISTLPHSPKVPCQEPPLSECFSHQDTSSSDPLS", "text": "FUNCTION: Involved in DNA recombination. SIMILARITY: Belongs to the RmuC family."}
{"protein": "METEAADESGFTSVASKRGRRKRRAAGAEPMEAAESAEAAGPQPSKRPAFPPLPAAALGVGKGEVRKVPVPANRYTPLKENWMKIFTPIVEHLQLQIRFNLKTRNVEIKTCSETKDLSALTKAADFVKAFILGFQVEDALALIRLDDLFLESFEVTDVKPLKGDHLSRAIGRIAGKGGKTKFTIENVTRTRIVLADSKIHILGSFQNIKMARTAICNLILGSPPSKVYGNIRAVASRAAERF", "text": "FUNCTION: Positively regulates dimethylation of two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the PNO1 family."}
{"protein": "MAAQCVRLARRSLPALALSLRPSPRLLCTATKQKNSGQNLEEDMGQSEQKADPPATEKTLLEEKVKLEEQLKETVEKYKRALADTENLRQRSQKLVEEAKLYGIQAFCKDLLEVADVLEKATQCVPKEEIKDDNPHLKNLYEGLVMTEVQIQKVFTKHGLLKLNPVGAKFDPYEHEALFHTPVEGKEPGTVALVSKVGYKLHGRTLRPALVGVVKEA", "text": "FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity). FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner (By similarity). Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (PubMed:11311562). SUBCELLULAR LOCATION: Mitochondrion matrix. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the GrpE family."}
{"protein": "MAKKKEFRQAEVNIGMVGHVDHGKTTLTKALTGIWTDTHSEELRRGITIKIGFADAEIRKCPSCGRYSTSPICPYCGHETEFERRVSFIDAPGHEALMTTMLAGASLMDGAVLVIAANEGVMPQTREHLMALQIVGNKNIVIALNKIELVDREKVIERYQEIKEFVKGTVAENAPIIPISALHGANVDVLLAAIEEFIPTPEHDPNKPPKMLVLRSFDVNKPGTKPEKLVGGVIGGSIVQGKLKVGDEIEIRPGVPYEEHGRIKYEPITTEIVSLQAGGRFVEEAYPGGLVGVGTKLDPYLTKGDLMAGNVVGKPGQLPPVWDELRLEVHLLERVVGTEEELKVEPIKRREVLLLNVGTARTMGLVTGLGKDEIELKLQIPICAEVGDRVAISRQVGSRWRLIGYGFIRE", "text": "FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily."}
{"protein": "MWIIIASYGVLIIVLAIGIGVGVGVIRKVLKKGMKAEMTIGERMLCFGYYLLPVLECMTHCGPDVLNGWMKGLYKRSLGDLVVVYSTYPILGFMIFFMSYFLLVRGILQVRKKVRFHVSQALIIYLLTSIIGSLLNALPEMILMGWFGSTCLDILFILTMGSVIYASYQVWNGELTRLPLISEAAKLQVQDGEGEKK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tic20 family."}
{"protein": "MTKNQDRMKSHTMELPRQIVVGEKNINEFGEFLHNLTKPKKVSLISGIHVKKVLRQRIEKSLKTKRIKFVWHTSKDNQISTLNRIEKEVKKDRSDMIAGIGGGRSVDTAKLISFNLDIPFVSVPTAASHDGVSSPFVSVKSDKPHSIVATAPLGVFVDIDIIKKAPSRLLASGCGDLVANIIAVKDWQLGHQKTGEYYGTYSAELAMMSAMMVLDNSSKYAKNGLDARVIVEALISAGVASCIAGSSRPCSGAEHLFSHALDKIAPGKGLHGEKCGIGSIMIAKLQGQDWKKIVKTLKDVGAPTTAKQIGLTEDQIIDALIIAQDLRPERYTILKEVEMTDRKAKSLAKSTKVI", "text": "FUNCTION: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1- phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family."}
{"protein": "MATIKDVARLAGVSTTTVSHVINKTRFVAETTQEKVMKAVDELNYAPSAVARSLKCNSTRTIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELKEMLDRHSDIPKVVMDWGPESSQADKIIDNSEEGGYIATKYLIDNGHTDIACLSGHFEKAACQERIAGYRRAMAEANLAVNEDWVLEGNFECDTAVLAADNITAMEKRPTAVFCFNDTMALGLMSRLQQNGLKVPDDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHEKRVFEMQPEIVVRNTVKKLN", "text": "FUNCTION: Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression."}
{"protein": "MRTVVLTMKASVIEMFLVLLVTGVHSNKETAKKIKRPKFTVPQINCDVKAGKIIDPEFIVKCPAGCQDPKYHVYGTDVYASYSSVCGAAVHSGVLDNSGGKILVRKVAGQSGYKGSYSNGVQSLSLPRWRESFIVLESKPKKGVTYPSALTYSSSKSPAAQAGETTKAYQRPPIPGTTAQPVTLMQLLAVTVAVATPTTLPRPSPSAASTTSIPRPQSVGHRSQEMDLWSTATYTSSQNRPRADPGIQRQDPSGAAFQKPVGADVSLGLVPKEELSTQSLEPVSLGDPNCKIDLSFLIDGSTSIGKRRFRIQKQLLADVAQALDIGPAGPLMGVVQYGDNPATHFNLKTHTNSRDLKTAIEKITQRGGLSNVGRAISFVTKNFFSKANGNRSGAPNVVVVMVDGWPTDKVEEASRLARESGINIFFITIEGAAENEKQYVVEPNFANKAVCRTNGFYSLHVQSWFGLHKTLQPLVKRVCDTDRLACSKTCLNSADIGFVIDGSSSVGTGNFRTVLQFVTNLTKEFEISDTDTRIGAVQYTYEQRLEFGFDKYSSKPDILNAIKRVGYWSGGTSTGAAINFALEQLFKKSKPNKRKLMILITDGRSYDDVRIPAMAAHLKGVITYAIGVAWAAQEELEVIATHPARDHSFFVDEFDNLHQYVPRIIQNICTEFNSQPRN", "text": "FUNCTION: Promotes matrix assembly and cell adhesiveness. Plays a role in spinal cord formation by regulating the proliferation and differentiation of neural stem cells. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
{"protein": "MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETPEGCLQIIEQIQPAIKTGTEELKSLFNLVAVLYCVHRKIDVKDTKEALDKIEEIQNKSQQKTQQAAADKEKDNKVSQNYPIVQNAQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNAMLNTVGGHQAAMQMLKDTINEEAAEWDRVHPVHAGPIPPGQMREPRGSDIAGTTSTLQEQIAWMTGNPAIPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTETLLVQNANPDCKTILRALGQGASIEEMMTACQGVGGPSHKARVLAEAMSQVTNTNTAIMMQKGNFKGQRKFVKCFNCGKEGHIARNCRAPRKKGCWKCGREGHQMKDCTERQANFLGKIWPSSKGRPGNFLQSRPEPTAPPAESFGFGEEMTPSPKQEQLKDKEPPLASLRSLFGSDPLLQ", "text": "FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion. SUBCELLULAR LOCATION: [Capsid protein p24]: Virion. SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-anchor Host nucleus Host cytoplasm. SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane; Lipid-anchor Host endosome, host multivesicular body Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. SIMILARITY: Belongs to the primate lentivirus group gag polyprotein family."}
{"protein": "MLPQHSDIEIAWYASIQQEPNGWKTVTTQFYIQEFSEYIAPLQDAVDLEIATEEERSLLEA", "text": "FUNCTION: Might play a role in cell growth during glycolysis. SIMILARITY: Belongs to the tfa family."}
{"protein": "MDNGIFIVATIFIVNILYVTIYTVRLLLTMKGYRYLAALSSVFEMIIYVVALSLVLDNLNNIANVLAYAIGFGVGIIVGMKIEERIALGYITVNVITKEYNLDLPNQIRDLGYGVTSWLASGRDGERMMLEILTQRKNERKLYKHIIEIDNGAFIVSSEPKQIHGGFWVKQVRK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0316 family."}
{"protein": "MSPVSPRSLTLIGAGLAGCLLAILLSRRGWQVTVYERRGDPRIKGYESGRSINLALAERGRHALRQAGAEDAVMAKAVMMRGRMVHPIIGQPQLQRYGRDDSEVIWSIHRAALNVALLDLAEQAGARVHFYRRLHTVGFDAGYARFIDDRDDQPHEIHFQSLIGSDGAGSALRAAMQRKSPLGERTEFLDHSYKELEIPPQPGGGFRIEGNALHLWPRGRYMCIALPNDGGTFTVTLFLPNAGEPSFATTRTGDEALALFARDFPDALPLIPQLREHWEEHPPGLLGTLTLDRWHLDGRALLIGDAAHAMVPFHGQGMNCAFEDCVALADQLDAHDDLASAFAAFEAARRDDAAAIQQMALENYLEMRDRVDDPDFLLQRELEQKLQARWPTRFVPHYTMVTFLRTRYSIALARSEIQRQILVEATRGHRDLSRIDWAALEAVVHARLEPLDGAH", "text": "FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO subfamily."}
{"protein": "MYPAHLLVLLAVCVSLLGAASIPARPLNLYQFGNMIQCANHGRRPTRHYMDYGCYCGKGGSGTPVDELDRCCQTHDDCYGEAEKLPACNYMMSGPYYNTYSYECNDGELTCKDNNDECKAFICNCDRTAAICFARAPYNDANWNIDTKTRC", "text": "FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
{"protein": "MDVIKKKHWWQSDQLKWSVIGLLGLLVGYLVVLMYVQGEYLFAIMTLILSSAGLYIFANRKTYAWRYVYPGLAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQQVLMDRSYQAGKTYNFGLYPTGDEWQLALTDGETGKHYLSDAFSFGGEQKLQLKETDALPGGERANLRIITQNRLALNQITAVLPDESKVIMSSLRQFSGTRPLYTLADDGLLTNNQSGVKYRPNNDSGYYQSINADGSWGDEKLSPGYTVTIGAKNFTRVFTDEGIQKPFFAIFVWTVVFSVLTVVLTVAVGMVLACLVQWEALKGKAIYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGIKPAWFSDPNTARAMVIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVSYTYRIAFEGGGGQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD", "text": "FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. MalFG subfamily."}
{"protein": "MEIIEGKMPFMGYETHYRIVGRRSEKSPLVLLHGGPGSTHNYFEVLDKLAKIDDRRIIMYDQLGCGNSSIPDDHPELYTKETWVKELKTLREHLALRKIHLLGQSWGGMLAIIYMCDYHPEGIQSLILSSTLSSASLWSKELHRMIKYLPIEEQAAIHRAELTDTFTEPDYLKANEHFMNQHAIDMKKKWPECVMREKKGGTVAYETAWGPNEYTPEGNLHDYEYTDQLSKIKVPTLITSGTDDLCTPYVAKTMHDHIAGSQWKLFENCSHMSFVQKTDEYIAMLKKWLDAND", "text": "FUNCTION: Releases the N-terminal proline from various substrates. SUBCELLULAR LOCATION: Cell envelope. SIMILARITY: Belongs to the peptidase S33 family."}
{"protein": "MLADVFEKIMGD", "text": "FUNCTION: Possesses weak insulin-releasing activity. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MSKSDHFLVINGKNCCVFRDENIAKVLPPVLGLEFVFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFLTDNYVHNWDWRFGGIPCRVMLFMLAMNRQGSIIFLTVVAVDRYFRVVHPHHFLNKISNRTAAIISCFLWGLTIGLTVHLLYTNMMTKNGEAYLCSSFSICYNFRWHDAMFLLEFFLPLAIILFCSGRIIWSLRQRQMDRHAKIKRAINFIMVVAIVFIICFLPSVAVRIRIFWLLYKYNVRNCDIYSSVDLAFFTTLSFTYMNSMLDPVVYYFSSPSFPNFFSTCINRCLRKKTLGEPDNNRSTSVELTGDPSTTRSIPGALMADPSEPGSPPYLASTSR", "text": "FUNCTION: Acts as a high affinity receptor for both nicotinic acid (also known as niacin) and (D)-beta-hydroxybutyrate and mediates increased adiponectin secretion and decreased lipolysis through G(i)- protein-mediated inhibition of adenylyl cyclase. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. Mediates nicotinic acid-induced apoptosis in mature neutrophils. Receptor activation by nicotinic acid results in reduced cAMP levels which may affect activity of cAMP-dependent protein kinase A and phosphorylation of target proteins, leading to neutrophil apoptosis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MKTQTALFSFFLVLLLVATQTEGGILDAITGLLGKRALRNQNFVDYAFDPSLSAADWRALETLLEEY", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
{"protein": "MKSLSMLIKPASSNCNLRCTYCFYYDICNNREIKSFGMMKLNLLETIVKRAFNEAEQNCTFAFQGGEPTLVGIDFYREFINFVKKYNTRNINVFYSIQTNGTTINEDWAKFFKENNFLVGISLDGTKEIHDKYRLDANKKGSFNKIMTNIKILNRYKVEYNILTVVNKNTSRHIDKIYKFFKKQDFRFLQFIPCLDPINDPRESHPYSLNPKDYETFLNKLFDLWFKDFLDGRFVSIRYFDDLLSILLGNNPKSCCMNGFCSCEFVIESDGSVYPCDFYVLDEYKIGYIEEKTFSELFNSNVTKNFIDSSLNHDVKCKNCNWYPLCRSGCRRNKEPNFPNGTNDNIFCESFKSFFEKNISKLTYVAKTLAYRQH", "text": "FUNCTION: Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family."}
{"protein": "MDRPDEGPPAKTRRLSSSESPQRDPPPPPPPPPLLRLPLPPPQQRPRLQEETEAAQVLADMRGVGLGPALPPPPPYVILEEGGVRAYFTLGAECPGWDSTIESGYGEAPPPTESLEALPTPEVSGGSLEIDFEVVQPSSFGGEGALETCSAVGWGPQRLIDPKSKEEAIIIVEDEDEDEQESMRSSRRRRRRRRRKQRKVKRESRQRNAERMESILQALEDIQLDLEAVNIKAGKAFLRLKRKFIQMRRPFLERRDLIIQHIPGFWVKAFLNHPRIPILINRRDEDIFRYLTNLQVQDLRHISMGYKMKLYFQTNPYFTNMVIVKEFQRNRSGRLVSHSTPIRWHRGQEPQARRHGNQDASHSFFSWFSNHSLPEADRIAEIIKNDLWVNPLRYYLRERGSRIKRKKQEMKKRKTRGRCEVVIMEDAPDYYAVEDIFSEISDIDETIHDIKISDFMETTDYFETTDNEITDINENICDSESPDHDEVRNETTDNNESADDNETTDNNESADDNNENPEDNNKNADDNKENPDNNKHTYGNNFFNGGFWGSHGNNQDSSDSDNEADEASDDEDNDGNEGDNEGSDDDGNEGDNEGSDDDDRDIEYYEKVIEDPFDRDQDDYEDVIEIISDESVEEEEGIVEGIEQDEDVYQEEGNYEGEGNEDVWEEGEDSDDSDLEDVLQVPNGWANPGKRGKTG", "text": "FUNCTION: Part of the CASK/TBR1/TSPYL2 transcriptional complex which modulates gene expression in response to neuronal synaptic activity, probably by facilitating nucleosome assembly. May inhibit cell proliferation by inducing p53-dependent CDKN1A expression (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Enriched in transcriptionally active regions of chromatin in neurons. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
{"protein": "MACGATLKRSMEFEALMSPQSPKRRRCAPLPGSPATPSPQRCAIRPEMQQGQQQPLSQLGGDRRLTPEQILQNIKQEYTRYQRRRQLEGAFNQCEAGALNEVQASCSSLTAPSSPGSLVKKDQPTFSLRQVGILCERLLKDHEDKIREEYEQILNIKLAEQYESFVKFTHDQIMRRYGARPASYVS", "text": "FUNCTION: Molecular adapter that acts as a bridge between proteins, and which is involved skeletal muscle development. Functions as signal transducer for MSTN during skeletal muscle regeneration and myogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the akirin family."}
{"protein": "MYTEGFIDVTGGRVSFQKFDENGGGTPVIVLHGGPGSSCYSLLGLKALAKDRPVILYDQLGCGKSDRPMDTTLWRLDRFVEELAQIRQALNLDEVHILGHSWGTTLAAAYCLTKPSGVKSVIFSSPCLSAPLWEQDQKRNLKKLPLDVQETINRCEENGTTDSEEFAAAIEVFGKHFVNRLEKQPEWLEQKPSGYRNADIYNIMWGPSEFTVLGNLKNFDCTTQLKEITCPSLYTCGRFDEATPETTEYYSSLTPKSKFHVFEKSAHMPYIEEPEEYLAVIGDFLNSI", "text": "FUNCTION: Releases the N-terminal proline from various substrates including at least dipeptides Pro-Pro, Pro-Gln, Pro-Trp and Pro-Tyr. Acts also on amides (Pro-beta NA) and oligopeptides including Pro-Leu- GlyNH2, Pro-Leu-Gly, Pro-Phe-Gly-Lys, Pro-Pro-Ala-OBut and Pro-Pro-Gly- (Pro-Pro-Gly)(4). Higher activity toward small peptides (up to three residues), but very low activity for longer peptides. Has no activity against p-nitrophenyl acetate, poly_L-proline, Met-Pro or amino acyl amides other than Pro-betaNA (Pyr-betaNA, Phe-betaNA, Cys-betaNA, Met- betaNA, Leu-betaNA, Ala-betaNA and Z-Gly-Pro-betaNA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S33 family."}
{"protein": "MSIPKQLPCMVRALYAWPGEREGDLKFTEGDLIECLSIGDGKWWIGRHINTNTQGIFPSNFVHCLDIPTVRPGSSMSRTSASSFRYSSPQKSSIDTPITSSDQGLTPDLVGSSNALNKPTRESDSLKHQKSHPMLNSLGSSLSLKKSVSRPPSSMSRTNLDVSSRWDNTADNDSQIDAQDLSRSTPSPLRSAMENVLQSLNAMGKKSFSRANSPLLRLTKSTTTSKETDFIPVPPAHGSTSMTSRSKLDDSTDNSSKPRTSLQPGESPMKSSRDISRKPSMASSVLSPSDYFPQHRRFQSAPAPIPRPVSTLIPLTQVRTTASNVIKPRPQTTERPSTAQSFRKGGGFLKKTFKKLLRRGSSKRKPSLQPTPPVSYPAHNVPQKGVRPASPHTLKSVKDDLKRTKTYTKAEFAAKREEIFNKLSMPVYEPLKDLSECIGNVLADGEPVQFSVGTNIHNMNFSAIDKQIRSIIPQRVQVSPAVLAKNYLAPGQTTALAQMRAVFIYISERITFTNQTLDNDELRTSTQVISEGQGTPFEVALLVKEMLQALDLWCEVIEGYLKSPDDIYYTRDININHAWNVVTFDNEVRLIDASFASPTHPQQALKSSSSNDFYFLMKPNECIFTHVPENPDQQFIMPDLSMPIVMALPWVSSVYFTLGLKLRKFNTSILHLNDLEVLQIEFLAPKDIECVAEVDALSALAPTADVSQCYKYTLTQAFWETPDIRVMRVKAVMPANNRAAVLRIYAGRLGVSSPVRTAPHPMAMSLPFVHHGKNKALEFVTRHPVPHCPSVDLYINSPQCGTLHSGVEYKFNVSAYACQPSTSISNTRLAIQTPTGNIVRLREERSGNGVIFFSLSLTINETGEYRALILAEKIGRWVVYATWQAV", "text": "FUNCTION: Involved in cytokinesis. SUBCELLULAR LOCATION: Cell tip Cell septum. SIMILARITY: Belongs to the CYK3 family."}
{"protein": "MVKSKRNVVVNMTKVTKNPGEKKKKLVSTIKDIVDQYKFIYLFTFENMRNNKLKSVRTEWSTSKFLFGKNKVLSVGLGKSEEDELKPNLHKLTEHLEGECGLFFTNEPKDKVFEYFTNYSEKDFPRSGFVSEETITIKEGPIVGMTHSMETYLRGLGLPTTLKNGVIFVDREYTLCEAGVAVTPEQSQLLKLFNHEISEFKFHIKGFWNEDEFTLCEEESQEE", "text": "FUNCTION: Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes. SUBCELLULAR LOCATION: Nucleus, nucleolus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL10 family."}
{"protein": "MDQLRQSLLDAPIIEKGEYQYFVHPISDGVPMLKPELLREIVIRIIRKAELENVDKIVTPAAMGIHISTALSLMTDIPLVVIRKRQYGLDGEVPLFQETGYSESEMYINDVEEGDRVLVLDDVLSTGGTMKAILDALTDEVGAEVVDVVAVIKKAGENELDDTDYNVKTLINVTVEDGEVVIVDAKGDD", "text": "FUNCTION: May catalyze a purine salvage reaction, the substrate is unknown. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. Archaeal HPRT subfamily."}
{"protein": "MIMSLPQCSHLRLSILAATAAMLMVITTAQIGGQVIQVELWCVAKNNAEDSSLQTAIEWACGQGGADCGPIQQGGPCNDPTDVQKMASFVFNNYYLKNGEEDEACNFNNNAALTSLNPSQGTCKYPSSKGANNGRLADDTSMGAGQADMSRGGRPISSSWMVTFIGFGSLLTMTWIIHHL", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Cell junction, plasmodesma."}
{"protein": "MRHFTYHSDVVVWQYIFESGAATNYITRGRALKKLQLSLKDFRRLCILKGVYPHEPLHKKKVNKGSTENRVYYYAKDINFLASEPIIRKFREYKIFLRKLTTAKAKRDEERIKTLYENRPEYQLDHIVKERYPTFESALRDLDDALCLLFAFAVLPHTKIITSSLVASSRRLTAEFNHYIIESNSLNKVFVSIKGIYYEAEVMGERVTWIVGHDRGMGHVSEVDFSVMATFAEFYVTMLEFVNFRLYQSVGLFYPPKLAFKSDKLEDDDQAEEGRVYSLACPLSKFENYEEQIDASIGDEVDNVLNEKLCDVEKRKQLFANYRFWLNREVPKDVLAIIIRSCGGLVSWENCPAAQYYENDAQITHQIVDRPLLDSHKNISRCYVQPQWVFDSFNRRSCLSIKKYLPGAILPPHLSPFSSDYDTYEEQLNQLRLLSKASANVTNRMETEAENKVQERKKIQKEKEVPIINVNKGRMHKENLQKKLNEKGHELKLREMLIPKKRRRVYSKIKRGIKRRVHEEKKLNEKRLKMLKAAD", "text": "FUNCTION: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the pescadillo family."}
{"protein": "MHALGRTLALMLLIFITILVPESSCSVKGREEIPPDDSFPFSDDNIFPDGVGVTMEIEIITPVSVQIGIKAQLFCHPSPSKEATLRIWEITPRDWPSCRLPYRAELQQISKKICTERGTTRVPAHHQSSDLPIKSMALKHDGHYSCRIETTDGIFQERHSIQVPGENRTVVCEAIASKPAMQILWTPDEDCVTKSKSHNDTMIVRSKCHREKNNGHSVFCFISHLTDNWILSMEQNRGTTSILPSLLSILYVKLAVTVLIVGFAFFQKRNYFSSRDLVFMKERRSKRSVWQREALG", "text": "FUNCTION: According to PubMed:15187158 isoform 4 is a receptor for the CD200 cell surface glycoprotein. According to PubMed:16081818 isoform 4 is not a receptor for the CD200/OX2 cell surface glycoprotein. Isoform 1, isoform 2 and isoform 3 are involved in the recruitment or surface expression of the TYROBP receptor. Isoform 6, isoform 7 and isoform 8 are not involved in the recruitment or surface expression of the TYROBP receptor. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the CD200R family."}
{"protein": "MNIKILKILVGGLFFLSLNAHLWGKQDNSFLGIGERAYKSGNYSKAASYFKKACNDGVSEGCTQLGIIYENGQGTRIDYKKALEYYKTACQADDREGCFGLGGLYDEGLGTAQNYQEAIDAYAKACVLKHPESCYNLGIIYDRKIKGNAAQAVTYYQKSCNFDMAKGCYILGTAYEKGFLEVKQSNHKAVIYYLKACRLNEGQACRALGSLFENGDAGLDEDFEVAFDYLQKACALNNSGGCASLGSMYMLGRYVKKDPQKAFNYFKQACDMGSAVSCSRMGFMYSQGDTVSKDLRKALDNYERGCDMGDEVGCFALAGMYYNMKDKENAIMIYDKGCKLGMKQACENLTKLRGY", "text": "FUNCTION: May hydrolyze 6-aminopenicillinic acid and 7- aminocephalosporanic acid (ACA) derivatives. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the hcp beta-lactamase family."}
{"protein": "MASREDELRNCVVCGDQATGYHFNALTCEGCKGFFRRTVSKSIGPTCPFAGSCEVSKTQRRHCPACRLQKCLDAGMRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRRPRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS", "text": "FUNCTION: Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton Note=Recruited to the cytoplasm by DNAJC7. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MLYRIPVSTVGYWHSPWQIHQFLLPIERFIHRNPMLQLDPISKTTHQHSGHKGLVMAIGGAEDKVRGRQILTTFCQRAGGLDAVIGVIPSASREPDAMGRLYHDIFRDIGVREVDILLVGDRADAEQEEMLARLSRCTGIFMSGGDQLRLSALLDETPLLYQLRHQVWEGKSILGGTSAGAAVLGECMIASGGSNEAPNRSLVDLATGLGILPDVLVDQHFHNRNRLARLISAISAHPDKLGVGIDEDTCAMFEADGTLRVLGRGSVTIVDPRDVSYTNYAHVDVNEPLSIYNLRLHILSDGDCYNLRTHQVQHKCILPPLN", "text": "FUNCTION: Exopeptidase that catalyzes the hydrolytic cleavage of multi- L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides. FUNCTION: Exopeptidase that catalyzes the hydrolytic cleavage of multi- L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides. SIMILARITY: Belongs to the peptidase S51 family."}
{"protein": "MTLVLFATEYDSAHIVANVLSQTPTDHCVFPLLVKHQVSRRVYFCLQTQKCSDSRRVAPVFAVNNETLQLSRYLAARQPIPLSALIASLDEAETQPLYRHLFRTPVLSPEHGGEVREFKHLVYFHHAAVLRHLNQVFLCPTSPSWFISVFGHTEGQVLLTMAYYLFEGQYSTISTVEEYVRSFCTRDLGTIIPTHASMGEFARLLLGSPFRQRVSAFVAYAVARNRRDYTELEQVDTQINAFRERARLPDTVCVHYVYLAYRTALARARLLEYRRVVAYDADAAPEAQCTREPGFLGRRLSTELLDVMQKYFSLDNFLHDYVETHLLRLDESPHSATSPHGLGLAGYGGRIDGTHLAGFFGTSTQLARQLERINTLSESVFSPLERSLSGLLRLCASLRTAQTYTTGTLTRYSQRRYLLPEPALAPLLERPLPVYRVHLPNDQHVFCAVASETWHRSLFPRDLLRHVPDSRFSDEALTETVWLHDDDVASTSPETQFYYTRHEVFNERLPVFNFVADFDLRLRDGVSGLARHTVFELCRGLRRVWMTVWASLFGYTHPDRHPVYFFKSACPPNSVPVDAAGAPFDDDDYLDYRDERDTEEDEDGKENKNNVPDNGVFQKTTSSVDTSPPYCRCKGKLGLRIITPFPACTVAVHPSVLRAVAQVLNHAVCLDAELHTLLDPISHPESSLDTGIYHHGRSVRLPYMYKMDQDDGYFMHRRLLPLFIVPDAYREHPLGFVRAQLDLRNLLHHHPPHDLPALPLSPPPRVILSVRDKICPSTEANFIETRSLNVTRYRRRGLTEVLAYHLYGGDGATAAAISDTDLQRLVVTRVWPPLLEHLTQHYEPHVSEQFTAPHVLLFQPHGACCVAVKRRDGARTRDFRCLNYTHRNPQETVQVFIDLRTEHSYALWASLWSRCFTKKCHSNAKNVHISIKIRPPDAPMPPATAV", "text": "FUNCTION: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs. SUBCELLULAR LOCATION: Host nucleus Note=Requires the presence of the primase associated factor to properly localize in the host cell nucleus. SIMILARITY: Belongs to the herpesviridae DNA primase family."}
{"protein": "MSSSTRVGLKEQLHPLIRDLATGIEATWQRWLNLEPYAAMPADLGYIEGKLEGERLQIENRCYQSREFRKLHLELARVGNNLDILHCVLFPRTTFDLPMFGADLVGGRGQISAAIVDLSPTTIARELSNDYIAGLTALPNPTFQGLRELPTWGDIFSSFCLFIRPGSPEEEAAFLDRALGFLQVHCQQAAAATALTDPEAIATVLEQQRYYCEQQRRNDKTRRVLEKAFGDDWADRYMTTMLFDLPSD", "text": "FUNCTION: Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. SIMILARITY: Belongs to the HY2 family."}
{"protein": "MKPSIILYKTLPDDLLHRLEAHFTVTQVPNLHPETVARHAQAFASAQGLLGASETVNRALLEKMPALRAASTISVGYDNVEVDALTARKIVLMHTPTVLTETVADTVMALMLATARRVVDVAERVKAGEWTESIGPAWFGVDVHHKTLGIVGMGRIGMALAQRAHFGFTMPVLYHARRRHQEAEDRFNARYCDLDTLLQEADFVCVILPLTAETRHLFGATQFARMKSSAIFINAGRGPVVDENALIAALQNGEIYAAGLDVFEQEPLSVDSPLLNMSNVVAVPHIGSATHETRYNMMACAVDNLIDALQGKIEKNCVNPQAAG", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily."}
{"protein": "MEVMNLIEQPIKVTEWQQTYTYDSGIHSGVNTCVPSVSSKGIMDEDDACGRQYTLKKTTTYTQGVPQNQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQTTNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQGLVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYADDMDATYRPMYSSDVPLDPLDMHMDLDGDYPMDTYSDGLRPPYPTADHMLA", "text": "FUNCTION: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE- cadherin function in endothelial cells. Can replace beta-catenin in E- cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton. SUBCELLULAR LOCATION: Cell junction, adherens junction Cell junction, desmosome Cytoplasm, cytoskeleton Membrane; Peripheral membrane protein Note=Cytoplasmic in a soluble and membrane-associated form. SIMILARITY: Belongs to the beta-catenin family."}
{"protein": "MLASPALAGARAFAATVSGSLGIPIPAISAPSPSQARRRASLVVVAKVKVSTPQADRIARHVRLRKKVSGTTERPRLSVFRSNKHLYAQVIDDTKSCTLVSASTMHKSLSKDLEYSAGPTVEVAQKIGEVIAKSCLEKGITKVVFDRGGFLYHGRIKALADAARENGLDF", "text": "FUNCTION: Binds 5S rRNA, forms part of the central protuberance of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL18 family."}
{"protein": "MANSRNKSSNELAVHGAQQAIDQMKYEIASEFGVTLGPDTTARANGSVGGEITKRLVQMAEQQLGGGRSKSLS", "text": "FUNCTION: SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. SIMILARITY: Belongs to the alpha/beta-type SASP family."}
{"protein": "MSKIHTDLKKIDPITVQVVLGSLENVAVEMGHKLARMSYSSIIRESEDFGCALVDVRGQQLCESSHSTPLQSGPIPGYIKGIREIMEDRNDTFNQGDVIMHNSPYHGASHGPDVGFCIPVFYKDELIGFSVTTAHHLDIGSSTPGSCGIVDAVDAYAEGLQFKAIKVYDQGVKNRYVWDILKDNIRAPKLVVGDMEAQIAAARIGAQRYIEIIEKYGLDTVQAASEELMNYSEKMMRDAIKKLPDGEYTAEGFLDGYLDSDDPAKKDLRINVTVKVDGSDLTVDLTGTSPQVTDKPINMPLLGTVDIAIYLTLRSILLDSTVYGNFPQNSGLIRPIKIVAPKGTLCNPIFPAPTIARFNSGNAVADTLMKALAQVVPHQVSAGVGNLQVVAFSGQSNENYWVYMDIMEGSYGGRYGKDGMDAVDTLYANTRNNPIEDIESHYPLRVNRYELRDNDSAPGKWRGGIGSIREVSFLADGSFSVEADGHKYAPWGFDDGQDGYVGSLSIRDNETNELVQLPSKLPNRHAQSGSTIQLVGPCGGGYGNPLEREPEKVLSDYLDGFITKEKALVEYGVTITDSEEIDYEKTNELRKV", "text": "FUNCTION: Involved in the asymmetric conversion of racemic 5- substituted hydantoins to the corresponding L-amino acids. HyuA and HyuB are both required for the conversion of D- and L-5-substituted hydantoins to corresponding N-carbamoyl-D- and N-carbamoyl-L-amino acids, respectively. SIMILARITY: Belongs to the HyuB family."}
{"protein": "MEAPEGGGGGPAARGPEGQPAPEARVHFRVARFIMEAGVKLGMRSIPIATACTIYHKFFCETNLDAYDPYLIAMSSIYLAGKVEEQHLRTRDIINVSNRYFNPSGEPLELDSRFWELRDSIVQCELLMLRVLRFQVSFQHPHKYLLHYLVSLQNWLNRHSWQRTPVAVTAWALLRDSYHGALCLRFQAQHIAVAVLYLALQVYGVEVPAEVEAEKPWWQVFNDDLTKPIIDNIVSDLIQIYTMDTEIP", "text": "FUNCTION: Activating cyclin for the cyclin-associated kinase CDK10. SIMILARITY: Belongs to the cyclin family. Cyclin-like FAM58 subfamily."}
{"protein": "MRFELEGRIIFSKDVSEETQKDIIEVLENGDIFLKGVPEGKENEASKIEGYEFEGKDLKLNMTSGTYTRAHEGIVRLKKPIMEKVGRKHQIGIRDVAIDTYVVTITATPSKVAELKGLKVPECEVELDNEKIKILFKNLGDGELKRNIIDRAIKFVKTELDKQEQDLTFEVCKIAPGTIVSDYKATREITFDKDPTELAEPYGWVKRFPGRGQWFYTAPMAKLFRAFESLIVEECIEKVGFDECLFPKLIPLDVMYKMRYLEGLPEGMYYVCPPKREPEMFRDFVNEMMIKKEIPIDKLKTLLRDPGYVLAPAQCEPFYTFFDHELVDVDSPSKFFDKSGWTYRWEGGGAKGLDRVNEFLRGECVWMGSPEFVEKVRDDTLKYAEKLAEKLDLEYWTEVGDDPFYLEGRKNEDRGIEFPDVPKYEMRLWLPHVKDERKGVAVTSANIHGTHFVEGFGIKDYKDRKVWTGCTGYGLSRWLIGFLAQYGYNYEDWPEIIQKKVGKLPEIPKLITWP", "text": "FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily."}
{"protein": "MSYSIVRVSKVKSGTNTTGIQKHVQRENNNYENEDIDHSKTYLNYDLVNANKQNFNNLIDEKIEQNYTGKRKIRTDAIKHIDGLITSDNDFFDNQTPEDTKQFFEYAKEFLEQEYGKDNLLYATVHMDEKTPHMHYGVVPITDDGRLSAKEVVGNKKALTAFQDRFNEHVKQRGYDLERGQSRQVTNAKHEQISQYKQKTEYHKQEYERESQKTDHIKQKNDKLMQEYQKSLNTLKKPINVPYEQETEKVGGLFSKEIQETGNVVISQKDFNEFQKQIKAAQDISEDYEYIKSGRALDDKDKEIREKDDLLNKAVERIENADDNFNQLYENAKPLKENIEIALKLLKILLKELERVLGRNTFAERVNKLTEDEPKLNGLAGNLDKKMNPELYSEQEQQQEQQKNQKRDRGMHL", "text": "FUNCTION: The interaction of the RSA site and the PRE protein may not only serves a function in plasmid maintenance, but may also contributes to the distribution of small antibiotic resistance plasmids among Gram- positive bacteria. SIMILARITY: Belongs to the plasmid mobilization pre family."}
{"protein": "MEVLPGLLRLLAALVVAERWARDTSGAESLGLWPLPFAVDISPRSLHLSPNNFFFGHSPTSKAGSSCEILQEAFRRYYDFIFGFYKWHQGSYQLCFGTELQQLQVHVESECDTFPSISSNESYVLHVKGPEALLRANTVWGALRGLETFSQLIYQDSYGTFTVNESEIIDFPRFPHRGILIDTGRHFLSVKTIFKTLDAMAFNKFNVLHWHIVDDQSFPYQSINFGVLSSKGSYSLSHVYTPNDVRMVIEYARIRGIRVMPEFDTPGHSRSWGKGQKDLLTPCYRKQVLSGTFGPINPILNTTYNFLSKFFKEISTVFPDEFIHIGGDEVDFDCWASNSEILQFMQEKGFSQISLNSNLCTVFKISNMISAMKKRPIVWQEAFDGRDKFMPGTVVQVWKIEDYKWEQSLITKAGFPVILSAPWYLDLISYGQDWKNYYEVEPQDFPGSDKERKRVLGGEACLWGEYVDATNLTPRLWPRASAVGERLWSHKDVRDIHDAYSRLTIHRCRMVRRGIAAEPLFTGYCNHEHRM", "text": "FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (By similarity). During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity). SUBCELLULAR LOCATION: Lysosome Cytoplasmic vesicle, secretory vesicle, Cortical granule. SIMILARITY: Belongs to the glycosyl hydrolase 20 family."}
{"protein": "MDRVASQIYSGALPYITTMDMEDRLRNRIAAKAGAKFFKACFEAVVADKSGLFVLSGGAATACHIGDDRNVLKCLDFDYYNATQEWLQLARLQQRLQACVQDNLEILSRLAQSVRMQDDLFVVKCFQNGAFCFNGPVQARLVPCVETVRTSFNGEFDLLRFALQVELKALNGVDEYVDQKVIVDRGAAVFNVFFVNIRAMKGPLTMERCVRTLAVFGDAYRVVVSPLQSVINDQIMCLLKDIFTDKPEFRVARPKALICALFAKLPREAYDECINSHHGAEPTRRRDETVTSFCRRTLHIHGPALGCRKLVYAYFKTDSFARQMPDYVANRAIYPHTDCEMKWKEFIHFFVVAKV", "text": "FUNCTION: This protein is required for viral late gene expression."}
{"protein": "MNRYRYESIFFRYISSTRMILIICLLLGIGDMSAMGLKKDNSPIIPTLHPKGNENLRATLNEYKIPSPLFDTLDNSYETKHVIYTDNCSFAVLNPFGDPKYTLLSLLLMGRRKYDALVAWFVLGRACGRPIYLREYANCSTNEPFGTCKLKSLGWWDRRYAMTSYIDRDELKLIIAAPSRELSGLYTRLIIINGEPISSDILLTVKETCSFSRRGIKDNKLCKPFSFFVNGTTRLLDMVGTGTPRAHEENVKQWLERIGGKHLPIVVETSMQQVSNLPRSFRDSYFKSPDDDKYDDVKMTSATTNNITTSVDGYTGLTNRPEDFEKAPYITKRPIISVEEASSQSPKISTEKKSRTQIIISLVVLCVMFCFIVIGSGIWILRKHRKTVMYDRRRPSRRAYSRL", "text": "FUNCTION: Envelope glycoprotein that binds to host cell entry receptors. May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. SIMILARITY: Belongs to the herpesviridae glycoprotein D family."}
{"protein": "MASRRGALIVLEGVDRAGKTTQGLKLVTALCASGHRAELLRFPERSTEIGKLLNSYLEKKTELEDHSVHLLFSANRWEQVPLIKAKLNQGVTLVLDRYAFSGVAFTGAKENFSLDWCKQPDVGLPKPDLILFLQLQLLDAAARGEFGLERYETGTFQKQVLLCFQQLMEEKNLNWKVVDASKSIEEVHKEIRAHSEDAIRNAAQRPLGELWK", "text": "FUNCTION: Catalyzes the phosphorylation of thymidine monophosphate (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the DNA building block dTTP, with ATP as the preferred phosphoryl donor in the presence of Mg(2+). SIMILARITY: Belongs to the thymidylate kinase family."}
{"protein": "MIFYLHGFDATSPGNHEKMRQLQFIDPDVRLVSYSTLHPKHDMQHLLKEVAKQMKHSDDPAPLMVGVGLGAYWAERIGFLNGLKSVLINPNLHPEDNMQGKIDRPEEYADIANKCVSQFREKNTHKAMCIFSVNDEMFDNQQLASELSAYYSIDWDDVQPHKFPQLAAHLPKIKAFKLA", "text": "SIMILARITY: Belongs to the UPF0227 family."}
{"protein": "MFKIEYNVSRNSTSVRRGQFYLNAFQLKKECNNYVVSKNKNTFFRDMILKMQQTIKFKDNMKSINDDYIYLKNNYCHSYGIKNKNFCSFDYFIFSKLFIIKKTSSFSNLFVLPKISEFFVQKKCLFIGLNKSKYTNFSLGHNISSWFYDDKLCCLFSILNFLADTSLNSIFSLNRKRYYSIIYSLDRDKIFKFGKIYKLFDIFKKKFILSCDYKFWKKFVFKKMLVFLNNKTKCITFILNSKHLGSVFIYFKIINNKSIILDLVTCRNEIKKIFQSHIIYLKNVLKDCGIEVSSINVSSREEFLNAVRTNYDRKFDSKILNHYNTVISKTKSHALRFYELDKNDYQYNYNNINMYV", "text": "FUNCTION: Controls the length of the flagellar hook. SIMILARITY: Belongs to the FliK family."}
{"protein": "MKLLLLLALLVGAVSTRHLNVDTSSLQSLQGEESLAQDGETAEGATREAASGVLMPLREEVKEEMEGGSGSEDDPEEEEEEKEMESSSELDMGPEDVQCPKEEDIVKFEGSPGCKICRYVVLSVPKTFKQAQSVCQRCFRGNLASIHSYNINLQVQRSSRILNVAQVWIGGQLRGKGHHKHFHWVDGTLWNFWYWAAGQPWRGNNSGRCVTLCARGGHWRRSHCGVRRAFSCSY", "text": "FUNCTION: MBP may play some important roles in the allergic reactions and inflammations, since MBP is capable of releasing histamine from mast cells and damaging the epithelial cells of bronchial tubes. Antiparasitic and antibiotic. SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule (crystalloid core)."}
{"protein": "MKPNFSLRLRIFNLNCWGIPYLSKHRADRMRRLGDFLNQESFDLALLEEVWSEQDFQYLRQKLSPTYPAAHHFRSGIIGSGLCVFSKHPIQELTQHIYTLNGYPYMIHHGDWFSGKAVGLLVLHLSGMVLNAYVTHLHAEYNRQKDIYLAHRVAQAWELAQFIHHTSKKADVVLLCGDLNMHPEDLGCCLLKEWTGLHDAYLETRDFKGSEEGNTMVPKNCYVSQQELKPFPFGVRIDYVLYKAVSGFYISCKSFETTTGFDPHRGTPLSDHEALMATLFVRHSPPQQNPSSTHGPAERSPLMCVLKEAWTELGLGMAQARWWATFASYVIGLGLLLLALLCVLAAGGGAGEAAILLWTPSVGLVLWAGAFYLFHVQEVNGLYRAQAELQHVLGRAREAQDLGPEPQPALLLGQQEGDRTKEQ", "text": "FUNCTION: Catalyzes, at least in vitro, the hydrolysis of sphingomyelin to form ceramide and phosphocholine (PubMed:10608884). Also hydrolyzes 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (lyso-platelet-activating factor) in vivo (PubMed:10608884). Also acts on 1-acyl-2-lyso-sn- glycero-3-phosphocholine (lyso-PC) and sphingosylphosphocholine (PubMed:10608884, PubMed:14741383). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the neutral sphingomyelinase family."}
{"protein": "MEFPDLGAHCSEPSCQRLDFLPLKCDACSGIFCADHVAYAQHHCGSAYQKDIQVPVCPLCNVPVPVARGEPPDRAVGEHIDRDCRSDPAQQKRKIFTNKCERAGCRQREMMKLTCERCSRNFCIKHRHPLDHDCSGEGHPTSRAGLAAISRAQAVASTSTVPSPSQTMPSCTSPSRATTRSPSWTAPPVIALQNGLSEDEALQRALEMSLAETKPQVPSCQEEEDLALAQALSASEAEYQRQQAQSRSSKPSNCSLC", "text": "FUNCTION: Plays a role in protein homeostasis by regulating both the translocation and the ubiquitin-mediated proteasomal degradation of nascent proteins at the endoplasmic reticulum. It is involved in the regulation of signal-mediated translocation of proteins into the endoplasmic reticulum. It also plays a role in the ubiquitin-mediated proteasomal degradation of proteins for which signal-mediated translocation to the endoplasmic reticulum has failed. May therefore function in the endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Lipid-anchor."}
{"protein": "MTGGLIAAGLGLAAVGFGARYVLRNQALIKKGMEALPVAGGLNSYYRGGFDQKMSRSEAAKILGITPSAKPAKIKDAHKKVMIVNHPDRGGSPYLAAKINEAKDLMESTKS", "text": "FUNCTION: Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM14 family."}
{"protein": "MKFAVVGTGVIGSGWITRMLAHGHEVIATDPSEGAYERMLTQVKQNWPYAEQMGLAENASIQNLTFTPHLEEAVKDADHIQENVPEVEEIKDAVLKEIDFYAKPEATIGSSTSGIMPSELQANLSHPERLVVAHPFHPVYILPLVEIVPGKQTSEETTVKAEQIYESIGMDVLHVRHEIEGHIADRLMEALWRESLHIVNDGIATTEEVDKAFTHAAGLRYAQYGPFMTFHLAGGEGGMRHMLKQFGPALKKPWTKLIAPELTDDLYHKVVSGSEASSQGYTMSELDQKRNEFLIKVKELAEQYWPSDSKAMKKSNGAELQ", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3- dehydrocarnitine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. L- carnitine dehydrogenase subfamily."}
{"protein": "MARPPPLPGLVGRRSGRAVDRAIGWRLFLLLWHPALGAQARPPRRAPGGRWRSRRVFLLVRRTRAAAYAFAIRRGVVRVVGGGGQLRPAPGEAAGEAGVAGAGLEAWRHPSGPARTQLEGQEGAGGWLVVGFLLCLFLLMPP", "text": "SUBCELLULAR LOCATION: Nucleus membrane; Single-pass type I membrane protein Mitochondrion membrane; Single-pass type I membrane protein Cytoplasm."}
{"protein": "MSDLDKQIEQLKRCEALKESEVKALCLKAMEILVEESNVQRVDAPVTICGDIHGQFYDMKELFKVGGDCPKTNYLFLGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVNVWRYCTDIFDYLSLSALVENKIFCVHGGLSPAIMTLDQIRAIDRKQEVPHDGAMCDLLWSDPEDIVDGWGLSPRGAGFLFGGSVVTSFNHSNNIDYICRAHQLVMEGYKWMFNSQIVTVWSAPNYCYRCGNVAAILELDENLNKEFRVFDAAPQESRGALAKKPAPDYFL", "text": "SUBCELLULAR LOCATION: Plastid stroma. SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily."}
{"protein": "MDNKLGLEIIEVVEQAAIAAARWMGKGDNKTADQVAVEAMREKLNQIPMRGRIVIGEGTRDEAPMLYIGEEVGICTRPDAEQFCRVEELVEIDIAVDPCEGTNLVAKGQNGSMAVLAISEKGGLLHAPDIYMQKLAAPPQAKGKVHIDYPPEKNLKIIAESLDREISDLTVVVMDRKRHLDLIRQIREAGARVKLITDGDISAALSAGFNGTGIHALMGIGAAPEGVISAAALRCLGAHFQGRLIYDPEVVQAGTYLPPVEETRRELKEKGIEDPDKVWECEELASGKEVLFAATGITDGDLMRGVRFFGGGARTETLVISSQSRTVRFVDTIHMKDGQQPRGLQLR", "text": "FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6- phosphate and sedoheptulose 7-phosphate, respectively. SIMILARITY: Belongs to the FBPase class 2 family."}
{"protein": "MDPRTSLRHLFLVLQLVMLPAGTQGKKVVLGKAGELAELPCKASQNKSLFFSWKNSYQTKILGRHGYFWHKGASNLHSRVESKINLWDQGSFPLVIKDLEVPDSGTYICEVEDKKIEVELQVFRLTASSDTRLLLGQSLTLTLEGPSGSNPSVQWKGPGNKRKNEAKSLSLPQVGLQDSGTWTCTVSQAQQTLVFNKHILVLAFQEVSSTVYAKEGEQMNFSFPLTFGDENLSGELSWLQAKGNSSPESWITFKLNNGKVTVGKARKDLKLRMSKALPLHLTLPQALPQYAGSGNLTLNLTKGKLYQEVNLVVMRVTKSPNSLTCEVLGPTSPRLILSLKKENQSMRVSDQQKLVTVLGPEAGMWQCLLSDKGKVLLESKVKILPPVLAHAWPKLLAVVLGGITSLLLLAGFCIFSAKCWHRRRRAERTSQIKRLLSEKKTCHCSHRLQKTCSLT", "text": "FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T- helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Localizes to lipid rafts."}
{"protein": "MLWHLVFILIAILLLTFSPKIESLFKSFTINKPTKTTCYQYTTREQLKSILESDTHETNFCIEKPSISPPKTNSTLLMLCRNSDVFSVLETIQNIQDRFNDKYNYDYTFLNDVPFNYEFIYLVSSIIPHGKINFGLIPIEHWSYPSHINISLATEIRQNYANVPYGDSESYRHMCRFYSGFFYKHELVKQYQYYWRIEPGIKIYCDIDYDVFEYMIINDKKYGFVISLFEYSETIPTLWNHVVQYINDNEIKSELLPLLTNKYNWYNLCHFWSNFEIANLDIFNNDDYENFFQYLDNLGGFYYERWGDAPIHSIAIALFLQKKDIHWFENIGYYHVPYLQCPQDIDLYVKNKCTCNPDEDFTWSDLSCTNHFLNILHN", "text": "FUNCTION: Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D- mannose linkage. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 15 family."}
{"protein": "MADGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPKNTVFDAKRLIGRRFDEESVQNDMKTWPFKVVDVDGAPVIEVEYLGENKQFSPQEISSMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSDKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKGEFKKKTGLDISNDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFEGEDFEASLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDYFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDIFGVVVPRNTTVPTIKRRTFTTVGDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPPMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAVGRLSSEDIEKMVNQAEEFKAADEAFAKRHEAKQRLESYVASIEQTVTDPVLSSKLKRGSKTKIEAALADALSALQIEDGSAEEYRKAEVGLKRVVTKAMSSR", "text": "FUNCTION: Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome- associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with translating ribosomes. SIMILARITY: Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily."}
{"protein": "MERVRGLVELLRPGNAVAAGGLTFIGAFVAGGLSSPQSMAFAVVATVLATGAGNAINDYFDRDIDAINEPDRPIPRGAVSPRGALVYSVALFAVAVVLTLLLPWLAIAIAAINLVALVAYTEVFKGLPGVGNALVAYLTGSTFLYGGAAVGGDLAAVVVLFALAACATMAREIVKDVEDIDGDRAEGLRTLPIVIGERRSLYVAAGFVVVAVLSSPLPYLLGLFGWVYLVVLVPALCGLAAATWRSFSDPTTGQAWLKASMFAAAVAFVIGRLAVVA", "text": "FUNCTION: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily."}
{"protein": "MCSSVTGKLWFLTDRRIREDYPQKEILRALKAKCCEEELDFRAVVMDEMVLTVEQGNLGLRISGELISAYPQVVVVRVPTPWVQSDSDITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEVLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRHEAPYLFQKYIKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGTDVCGIDLLMKDDGSFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPAGRLTRRMSLLSVVSTASETSEPELGPPASAAVDNMSASSSSVDSDPESTTEREMLTKLPGGLFNMNQLLANEIKLLVE", "text": "FUNCTION: Catalyzes the synthesis of beta-citryl-L-glutamate and N- acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimK family."}
{"protein": "MLLFLLITLLSAIFIFAKRHYTQWQRLGLVSDEAVIPFGSLAKVFRKERPFGLVMYDLYEKFQEQVVGIYLFFKPALLIRDAELARQILTSDFNSFHDRGIYVDEKNDPMSANLFALEGQSWRTLRMKLTPSFSSGKLKGMFETVDDVGNKLLEYLNNQLKDGQTHVLDIKSILTTYAIDIIGSVIFGLEIDSFTNPDNEFRVLSDRSFDNESRSFLSKLQNLTNFVCPPIAKLLTRLGTKEPVVYRLRDIVKRTIEFREENNVVRKDLLHLLIQLRNTGKISDDNDNLWNKVESTATNLKAMSIDMIASNSFLFYIAGSETTASSTSFTIYELAMNPEALKKAQNEVDECLKKHGIKPDGRITYEAIQDMKYLDLCVKETTRKYPGLPFLNRQCTQDFKVPNSKFTIKKDTNVIISLLGLHRDAKYFPEPLAYKPERFADETKDYDAAAYMPFGEGPRHCIAQRMGVMNTKVALAKILANFNIEPMPHKEAEFQFNTAPVLVPVNGLRVGLSKRSFNRR", "text": "FUNCTION: Metabolizes pyrethroid insecticides and other xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MVEIGMGRTARRTYELEDVTIVPSRRTRSSKDVSTAWQLDAYRFEIPVIAHPTDALVSPEFAIEMGRLGGLGVLNGEGLIGRHADVEEKIAQVVEVAAKEPEPSAAIRLLQQLHAAPLDPDLLGAAVARIREAGVTTAVRVSPQNAQALTPTLVAAGIDLLVIQGTIISAERVASDGEPLNLKTFISELDVPVVAGGVLDHRTALHLMRTGAAGVIVGYGSTSGVTTSDEVLGISVPMATAIADAAAARREYLDETGGRYVHVLADGDIHSSGDLAKAIACGADAVVLGTPLATSAEALGNGWFWPAAAAHPSLPRGALLQVALGERPSLEQVLTGPSDDPFGSLNLVGGLRRSMAKAGYCDLKEFQKVGLTVGS", "text": "SIMILARITY: Belongs to the IMPDH/GMPR family."}
{"protein": "MEYGKCRGIERGMGRRDFLKAATLLGATAAGAGMLAGCAPKSASEAQAQTAPAATGGLDPADVDWKYETDVVIVGSGSGGTCAAIEAAEAGADVVVFEKDKAMYGGNSALCGGYMLAAGWSTQEEITGYAGDTGEAFANQMLRWSQGLGNQDMIREACLRSGEAVDWMMDTGRTYEGASPLPPVWSCGDTEADVVPRSVYNHNAYGATEGHMATLKKRAESLSNIEIEMGCEVAHILKNAEGSVIGVQLADGSFAKARKGVVMACASVDNNLEMSKDLGLMQNVWGLTLEGAGLLAPGNPDMDSNTGDGVRMLREIGAELCMQQAVCMNDSIYVGGISDWGMSEILGKDVNIHDSSNIDAILVDKTGRRFCQDDAEWGYVMHECAQAAWKQGFTPDDPTTGYIFYVYDATGAPFFEMKGHTPDTCDTTFSADSVDGLAEFIGCDPTALASEVERWNSFCEAGLDADFGRRANMAPIATPPFYCDVVRPGPMGTFAGAKSNVEAEIIGLDGNPIPRLYGAGCIIGGNVSGAFYFGCGWSITNTVVWGREAGRNVAALEPWE", "text": "FUNCTION: Involved in the inactivation of the cardiac medication and plant natural product digoxin, thus decreasing drug efficacy and toxicity. Catalyzes the reduction of the alpha,beta-unsaturated butyrolactone ring of digoxin to the inactive metabolite dihydrodigoxin. Likely uses the cytochrome Cgr1 as the physiological electron donor, encoded by the adjacent gene in the locus. Only reduces digoxin and other cardenolide toxins, such as digitoxin, digoxigenin, ouabain and ouabagenin. Therefore is a specialized enzyme present in some gut bacteria E.lenta that protects their human host against ingested plant toxins. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family."}
{"protein": "MMATKEEISMVGFALVAYAGDARTAAVHALDAAEAGDFDKANELVEKAQQDINEAHNQQTQLLSQEAGGAEMDVTFIMVHGQDTLMTTMLLIDETRYMIRMFKRIKELENKQ", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LacEF PTS system is involved in lactose transport. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAGVCDRVPNFLSPSEDQALGPALGSAVALNCTAWVFSRPQCPQPSVQWLKDGLALGNGSHFSLHQDFWVSDNFSEIVSSVLVFNLTKAEDYGTFTCSAWNVSSHSFTLWRAGPAGHVAAVLASLLVLVVLLLVALLYVKCRLNVLLWYQDTYGEVEMNDGKLYDAYVSYSDRPEDRKFVNFILKPQLERRRGYKLFLEDRDLLPRAEPSADLLVNLSRCRRLIVVLSDAFLRRPWCSQSFREGLCRLLELTRRPIFITFEGQRREPIHPALRLLRQHRHLVTLLLWKPGSVTPSSDFWKELQLALPRKVQYRPVEGDPQTRLQDDKDPMLIVRGRAAQGRAMESELDPDPEGDLGVRGPVFGEPPTPLHESKVSIGEGHASEMDVSDLGSRNYSARTDFYCLVSEDDV", "text": "FUNCTION: Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor- proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the interleukin-1 receptor family."}
{"protein": "MDLATLRAQQIELASNVVREDRLNVDPPTIIGGADVGFEQGGEVTRAAMVLLKYPSLELLEYQVARIPTTMPYIPGFLSFREYPALLTAWEMLSRKPDLLFVDGHGISHPRRLGVASHFGMLVDVPTIGVAKKRLCGKFEPLSDEPGAVSPLMDKGEQLAWVWRSKARCNPLFVSTGHRVSIDTALGWVQRCTKGYRLPEPTRWADAVASGRPAFLRWQEIQG", "text": "FUNCTION: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endonuclease V family."}
{"protein": "MEVNATLIDCCDPQKPSRVLFHFLILDAPSPSNLPTYIKELQHRGVRHLVRVCGPTYDATLVKSRGIDVHSWPFDDGAPPTRAVLDSWLKLLDTELARQQEDPSVPPPTIGVHCVAGLGRAPILVALALVEYGNVSALDAIALIREKRKGAINQTQMHWITKYKRRHQGAGCVIM", "text": "FUNCTION: Has protein tyrosine phosphatase activity and may act as a virulence factor to support intracellular survival in host macrophages. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion matrix, kinetoplast Secreted, extracellular exosome Secreted Note=Enriched around the kinetoplast. SIMILARITY: Belongs to the protein-tyrosine phosphatase family."}
{"protein": "MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRPMSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVGEEEESQPEACVIDDRSPDT", "text": "FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. SUBCELLULAR LOCATION: Apical cell membrane Cytoplasm Membrane Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome (By similarity). Colocalized with SHANK2 to the apical membrane of colonic crypt cells. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily."}
{"protein": "MATPLGWSQGGSGSVCLAFDQLRDVIESQEELIHQLRNVMVLQDENFVSKEEFHEIEKKLVEEKAAHAKTKALLAKEEEKLQFALGEVEVLSKQLEKEKMAFEKALSSVKSRVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQNFRNHISDFRIQKQQETYMAQVLDQKRKKATGMRRARSRQCSREK", "text": "FUNCTION: Binds DNA with high affinity but does not bind to TATA boxes. Synergises with GMNN and TBP in activation of TATA box-containing promoters and with GMNN and TBPL1 in activation of the NF1 TATA-less promoter. May play a role in cytoplasm movement and removal during spermiogenesis. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Associated with chromatin. SIMILARITY: Belongs to the SPATA24 family."}
{"protein": "MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL", "text": "FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30- fold greater affinity than it does norepinephrine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome Golgi apparatus Note=Colocalizes with VHL at the cell membrane (PubMed:19584355). Activated receptors are internalized into endosomes prior to their degradation in lysosomes (PubMed:20559325). Activated receptors are also detected within the Golgi apparatus (PubMed:27481942). SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily."}
{"protein": "MAAADTCGAGTLSSRSVASEAGQGGTSSFQRKGKASGGPGGGPRLLSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTLLLIEEDKYNIYSPLLFKYFMAEGIINGHTLLVASAKENPAKILQELPAPLLDDNSKKELEDVHSAKTPEPNVNMKIAWRYQLQPKMEVGPVSSSRFGHYYDLSKRIPWELLQSSKWHGFFLPEHISPDLKGESCFLSCGYMRLLEFIQKSVYAEGFDGANPQKKQKNILRIGIQNLGSPLWGDDICCKENCDNNHRLTKFLYILRGLLRSSLSACIITMPAHLVQNKSITTRVRNLSDTVVGLESFIGSERETNPLYKDYHGLIHIRKIPRLNNLTCDESDVKDLAFKLKRKLFTIERLHLPPDLSDTVGRSSKQDLAASTARLGAGCSSMAEGKKHLDF", "text": "FUNCTION: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ELP4 family."}
{"protein": "MAKAKISPVANTGAKPPYTFRTGWALLLLAVNFLVAAYYFHIIQ", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaX family."}
{"protein": "MSIRTSIALIGILFAISIYTVLLVVYVSTLSQNGSGCIYATLVDSSLYDAKNFTWEQYNSTLIYTALGNKLPLDGGFDDFSDVCRTYLVNLTSISGLASHVSTKPKIRSVVGTRNCVTYLWRIHIQSLSSSLGLYTIFYVIREWRRMFGVVRFEDDAISTARYTKNYAARVISSVLLNTTYTKMSRFMCEIMIYKNALSRTFKDDPISFLFHHPIAAVLIITEGLVRLGAQCLCLATLSMYFVPCEKVLSKWFLSITGIFIGIIICIELSLLLAPGPVDGAAMLGETKQVKKDECALETSPSGVHVFCSNCCASLISNILIKVLYILFMIILIVTIVRYERTLQIALFGRAYLP", "text": "FUNCTION: Glycoprotein that probably modulates membrane fusion events during secondary envelopment of cytoplasmic capsids that bud into specific trans-Golgi network (TGN)-derived membranes. SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein. Host endosome membrane; Multi-pass membrane protein Host Golgi apparatus membrane; Multi-pass membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with UL20 to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). Cell surface expression of gK is required for virus-induced cell-to-cell fusion. Likely not present in extracellular virions (By similarity). SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein K family."}
{"protein": "MPKIIEAIYENGVFKPLQKVDLKEGERVRIKLEKVEEVVDEVFGILKGKDTLKALRELEEWGFC", "text": "FUNCTION: Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. SIMILARITY: Belongs to the UPF0165 family."}
{"protein": "MRSSKNVIKEFMRFKVRMEGTVNGHEFEIEGEGEGRPYEGHNTVKLKVTKGGPLPFAWDILSPQFQYGSKVYVKHPADIPDYKKLSFPEGFKWERVMNFEDGGVVTVTQDSSLQDGCFIYKVKFIGVNFPSDGPVMQKKTMGWEASTERLYPRDGVLKGEIHKALKLKDGGHYLVEFKSIYMAKKPVQLPGYYYVDSKLDITSHNEDYTIVEQYERTEGRHHLFL", "text": "FUNCTION: Thought to play a role in photoprotection of the coral's resident symbiont microalgae's photosystems from photoinhibition caused by high light levels found near the surface of coral reefs. In deeper water, the fluorescence may be to convert blue light into longer wavelengths more suitable for use in photosynthesis by the microalgal symbionts. SIMILARITY: Belongs to the GFP family."}
{"protein": "MSDDNSHSSDTVNSKKGFFSLLLSQLFHGEPKNRDELLALIRDSGQNELIDEDTRDMLEGVMDIADQRVRDIMIPRSQMITLKRNQTLDECLDVIIESAHSRFPVISEDKDHIEGILMAKDLLPFMRSDAEAFSMDKVLRTAVVVPESKRVDRMLKEFRSQRYHMAIVIDEFGGVSGLVTIEDILELIVGEIEDEYDEEDDIDFRQLSRHTWTIRALASIEDFNDAFGTHFSDEEVDTIGGLVMQAFGHLPARGETIDIDGYQFKVAMADSRRIIQVHVRIPDDSPQPKLDE", "text": "FUNCTION: Plays a role in the transport of magnesium and cobalt ions. FUNCTION: Plays a role in the transport of magnesium and cobalt ions. SIMILARITY: Belongs to the UPF0053 family."}
{"protein": "MDNRSRSSSLASNVRIKSYSSLSSHSNSNSNSNGRSIEAPAVRRPSDNLLASESKKNELDQDYLNAINLQNHTKSSSCIGSALTGHVVPVKERPISNDSISTRNTDLFSSTSIYTKNSSSEDIFNDGDSNGTDDTSNITSKPENCNYLLNRKESIISEGQITNSTPTPAPTPIPGSNNIYTHHFAPSNPLLRSKTALTPSQQYKLHRVRSDSLLRNIINTNDRNLFNSSNLILQEHDDEDDDNEEVQIDVNNNSLNWNVPMASVSTTSFINSVTNDTDIPTHVKKSKRKNHPTGLYRASTYTSSYTTINGRHTPSYVPESPYDIALPTTPIPGISNVSDLEYMRDTSKSLSALYLQSSGKLSESRLAQRTRSSSLLPLEFKEASDHGMENLLLVSNHKRSFTTTTRPCWLPPKDPMEIKSHEKQISQHLDEVSVFELQRNNSFQDHVHNNKVNQDRLQTIIDRGLTRNSSLKILKEIIWENSLPDDLRLSIWNEILQSSDNLISNNYIESFDSINEIYSNLQFPRSKELEIMKLIDKNIKSKYGDNLEISENLLYLLKLKSLSQQGLVTGDELLFHHFIYDKSFKFSLNDVWTMVNLIQKTCFNDICKDFYDHQIVNGNKVFAQYIGNNEEFSKENNSTCLNYGTLWNILERMDHNIFMWILDIIIIHNSQNFKNSSISKSNINNEITWDIYRTKNVVVNYKILLSFTLLILLKYHFGFNNLSELSLLNDKQFCIPVASKNVQDEWHFTSMFIRKWNYYYKKF", "text": "FUNCTION: With SBE22, is involved in cell wall integrity and polarity processes like bud growth. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the SBE2 family."}
{"protein": "MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK", "text": "FUNCTION: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:14622290). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (By similarity). FUNCTION: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. SIMILARITY: Belongs to the eIF-5A family."}
{"protein": "MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDSFLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATGVTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPHSSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLHEAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPLPGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEKPVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALASRLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMGPDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPLSFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLARGRLHPDLQSNLLQVDSEFTEEEIEFLEARGHHVEKVDVLSWVHGSRRTNNFIIAVKDPRSPDAAGATIL", "text": "FUNCTION: Hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors. SUBCELLULAR LOCATION: Membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the gamma-glutamyltransferase family."}
{"protein": "MNKNRQLAVNSNILFRKWLNGTREMVQDTIFHSRLHKVNQKIRSKRMFFEQDVHSNYFSFYKKKDFFKENPVSYVRNKDFTNVLKKLKKGKYYPDIFLDLHGLNQYQARKKLGQLIAICQKEKMFCAHIMHGYGKNILKKQIPFWLSQHPDIVAFHQAPKMFGNDAAIMVIIEIHS", "text": "SIMILARITY: Belongs to the UPF0115 family."}
{"protein": "MSNFRLILETEGGKRVLCESIVLHFAFMFQTEIVPVCNDEFTLSSCVPTLDFDVDVLSAAYGDGLEISSPGLRCCIAWPPMYALTLGEFYHFHTHRWVSAYDWSSLLDTDEFLSAIGYAHPIYRDPNPDYDPYVMHSSTGKTIAVDTVTEKVYIIAESLVQFFNIGLRQFPPFAEAELDPEQEKMWFGETKCGREEFILLQRNLPAMKDYVAKHCGKRIRVDAFQDFDFSFCSLSDIYYLTGPGILEKITEKDYAIIGTCARSQAEPNCRAAIVMGSNCHIYIYVENRISKVSKSLRTFIRRGFDELLYKEKYSLDWNDDTLFYISDTETENLNRMLNGELPVLRSKPRHMCVRKDRLVKDRSKILFAVRLDEEDSLTVKFITKFLTPVFVGRLPATSRFVVPVSCARLTNGLQGTAAARFGIKGLHPSSDCVVWNRLIDYEYETYKYPSTYVRADQIADMVKNLKFMDNFDEKWQCITKLAFIGLYAGASLFNFASKPTLGYWCRYLCEYASMLLFQFESKLKELTKESTRQLGGYNLCHWGQELKDCLENKSDVFFRYDFFERIESCLIEHFMLLCGCVECRRMFIMYNKRGRKCDFGHCVRIQCFPMIGSIRLPAFLHLGEPYSVSLSSLIAKDLGLSMIEGQIEHSRLPISLQISVTPDKKALLTFLTNIVFIVFVVNTLYRVINAELDIYYDLFTEEVGKLCVTMEEEMKLGRNGCLGDLCYFSSMKQMKEIVRCPGEKSQFILKCWEALRIGFSVPAYKDYDETRFMEMFFLHHLHIKRFHEHNDRDLVSSDNLIPGFFIVNTHEENFLQRLQRVVLPVAEDYLTNTRCINGTMAFFFSGLKYFGSGNHRGVQISPEKDVRAIGYKLGSLDVLRDDYKYYEYAPDCAGELNGHDGDE", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the herpesviridae US22 family."}
{"protein": "MDRRHRVYRVFNQEMYVEPNFKVVKELGQGAYGIVCAARNVASKDQEAVAIKKITNVFSKSILTKRALREIKLLIHFRNHRNITCIYDLDIINPYNFNEVYIYEELMEADLNAIIKSGQPLTDAHFQSFIYQILCGLKYIHSANVIHRDLKPGNLLVNADCELKICDFGLARGCSENPEENPGFMTEYVATRWYRAPEIMLSFSSYHKGIDVWSVGCILAELLGGTPLFKGKDFVHQLNLILHQLGTPDEETLSHISSSRAQEYVRSLPKQRPIPFETNFPKANPLALDLLAKLLAFDPNRRISVDDALEHPYLAVWHDPSDEPVCDSVFDFSFEYIEDANELRRVILDEVLNFRQKVRRRSHPTNPTVNIPQPAQTVPSNDNGSFNVSSSSSSQTSNKKRHDHSYNETAAIDHKSDDNRHN", "text": "FUNCTION: Regulates cell integrity and functions coordinately with the protein kinase C pathway (pck1 and pck2). Involved the regulation of wall architecture, cell shape, cytokinesis in exponential and stationary phase, and metabolism of ions. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
{"protein": "MDKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKMQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN", "text": "FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 14-3-3 family."}
{"protein": "MALFSAQSPYINPIIPFTGPIQGGLQEGLQVTLQGTTKSFAQRFVVNFQNSFNGNDIAFHFNPRFEEGGYVVCNTKQNGQWGPEERKMQMPFQKGMPFELCFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFITFQNSAAPVQHVFSTLQFSQPVQFPRTPKGRKQKTQNFRPAHQAPMAQTTIHMVHSTPGQMFSTPGIPPVVYPTPAYTIPFYTPIPNGLYPSKSIMISGNVLPDATRFHINLRCGGDIAFHLNPRFNENAVVRNTQINNSWGQEERSLLGRMPFSRGQSFSVWIICEGHCFKVAVNGQHMCEYYHRLKNLQDINTLEVAGDIQLTHVQT", "text": "FUNCTION: [Isoform 2]: Acts as an eosinophil chemoattractant (By similarity). It also inhibits angiogenesis (By similarity). Suppresses IFNG production by natural killer cells. FUNCTION: Binds galactosides (By similarity). Has high affinity for the Forssman pentasaccharide (By similarity). Ligand for HAVCR2/TIM3 (By similarity). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (By similarity). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (PubMed:20937702). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (PubMed:25065622). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (By similarity). Expands regulatory T- cells and induces cytotoxic T-cell apoptosis following virus infection (By similarity). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (By similarity). Inhibits degranulation and induces apoptosis of mast cells (By similarity). Induces maturation and migration of dendritic cells (By similarity). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (By similarity). Astrocyte derived galectin-9 enhances microglial TNF production (PubMed:25158758). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Secreted Note=May also be secreted by a non-classical secretory pathway (PubMed:9038233). Secreted by mesenchymal stromal cells upon IFNG stimulation (By similarity)."}
{"protein": "MSTLEQKLTEMITAPVEALGFELVGIEFIRGRTSTLRIYIDSEDGINVDDCADVSHQVSAVLDVEDPITVAYNLEVSSPGLDRPLFTAEHYARFVGEEVTLVLRMAVQNRRKWQGVIKAVDGEMITVTVEGKDEVFALSNIQKANLVPHF", "text": "FUNCTION: Required for maturation of 30S ribosomal subunits, probably at a late stage of ribosomal protein binding, while Era is associated and after RimM (PubMed:20188109). FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family. SIMILARITY: Belongs to the RimP family."}
{"protein": "MGSTAEDFVIKPMKGEHGFGAEIYGLDVNNITDEQVDRLRDTIQRYLLVVLKHQHDETPQKNWELLNRLSPDAPKFTPEEWALMYNPDPQGAGILPKLGYLVLPGTERLFLMGKGYQGEDHWGLKDIDIPEVFADAYYSKPLPHEDYHNGVARFQSWHIDGPSYKIDHPMFTSFRIIKFPEGEQTVDWADGSGLTKKVKAGRTAFFSSAKLYDMLTKEEQAIADYSWAEYMYFPYEWILRCRGNPQGLLVACEGREVPDEQMDAMPRNPEDQLVLPLVWVNPVTGGKHFHVQPNIVRRVFVRSGPDEEPKIIDDVKEVRDFFTKFQYRIIRPENIYVGPEEEGDQLLFFNWGVMHSKIDYPIEMGTRTTHQGWLAGDRPPKGPVPIPDPRARSSIYYQK", "text": "FUNCTION: Alpha-ketoglutarate-dependent dioxygenase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker (PubMed:21299202, PubMed:22870285). The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H (PubMed:17360612). The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca- 2,10(14)-diene-8-beta-ol (PubMed:22870285). The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol (PubMed:22870285). The dioxygenase fc-dox then catalyzes the 16- oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al) (PubMed:21299202, PubMed:22870285). The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol (PubMed:21299202, PubMed:22870285). The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O- glycosyltransferase PaGT (PubMed:22870285). Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O- methyltransferase PaMT to yield fusicoccin P (PubMed:22870285). Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT (PubMed:22287087). Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2 (PubMed:22870285). Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A (PubMed:22870285). SIMILARITY: Belongs to the TfdA dioxygenase family."}
{"protein": "MGAYKYLEELQRKKQSDVLRFLQRVRVWEYRQKNVIHRAARPTRPDKARRLGYKAKQGFVIYRVRVRRGNRKRPVPKGATYGKPTNQGVNELKYQRSLRATAEERVGRRAANLRVLNSYWVNQDSTYKYFEVILVDPQHKAIRRDARYNWICDPVHKHREARGLTATGKKSRGINKGHKFNNTKAGRRKTWKRQNTLSLWRYRK", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family."}
{"protein": "MAANSQGNFDGKFEALDLAELTKKQPWWRKLFGQESGPSAEKYSVATQLVIGGVTGWCTGFVFQKVGKLAATAVGGGFFLLQLANHTGYIKVDWQRVEKDMKKAKEQLKIRKNKQIPTEVKSKAEEVVSFVKKNVLVTGGFFGGFLLGMAS", "text": "FUNCTION: Binds directly and specifically 1,2-Diacyl-sn-glycero-3- phospho-(1'-myo-inositol-3',4',5'-bisphosphate) (PIP3) leading to the recruitment of PIP3 to mitochondria and may play a role in the regulation of the platelet activation via AKT/GSK3B/cGMP signaling pathways (PubMed:30576423, PubMed:29786068). May act as transcription factor that regulates SREBP1 (isoform SREBP-1C) expression in order to modulate triglyceride (TG) homeostasis in hepatocytes (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Nucleus. SIMILARITY: Belongs to the FUN14 family."}
{"protein": "MASGTAANAAALAAFNAGKKRDDGWKQNNEGNNKSSKYVCAPAVKSQNNKVKPAAPAAPAALAGAVNTNTTNTTNTVTTTSASTTPKPKSNHAVHRDTTPTSMVNQQYSQNNDRIMTKSPRPVLNVNTDSSKQGSYSSAASKNNHDNKGLDYFNLGSATSGRSDTFKLPRYLPHTPKDMINNVKSSIEAKNIANDPSSRRLSANYSPQQMLKNLKTSLNEKSKAPAPPKASENDKGRQILSDMRERLDTSRKIAADQAATRGLAPGFDFEEDGDKEDKGYEDYTWNLTDRKKPVSSNRSAKSFKSFKSVKSTNSNKTVNSIAKNVVTKAGENDQLGTTELNISTPERHGICIDVTYHDSDVEDDCLKNENGNKCANGIGHENGHGTQNENNVENGIRNENQHDNESDIGDQVMVPIKLYNSDKSSISSKSKVRRKPPPSLSQEEYGSSSTELLSTDLKHIMALHAKSSDTFSSGDNFNQSDDQISIAENDAGQPNVGTTAAATLVRRGDTKFPQFPEIKKKHYHSRNIFGLKRHDHRNQNSVIWLDPDSDVEAEGEGLGGEAKYVRGVNRKSAGEDDELEEEEEEEQDGEEEEEEEEEGNEVEENEESEFSDASAIANNFNHGNTKNGVRRLGPQSRPQQAHVQQQQPQQSQQQPVQFRTTMRTTNKRKDRKSKFDEYKPWKNHSDLNYLTDQERKRYEGVWVSNKGNYTNLVVVKLHGVDYSTVKDGKVNLEHIDDSMRAALISTNAYPSSKQEEQESMKSNNGTGIKVNSDGSVYNSAIEVPSQANNQSRPERVELSQLILGAVVKRIWSRSGLPDETLEQIWNLVDFRRDGTLTKNEFIVGMWLVDQCLYGRKLPKKVESIVWESLGGIGVNINTKKMR", "text": "FUNCTION: Positive regulator of phosphatidylinositol 4,5-bisphosphate turnover and negatively regulates signaling through the cell integrity pathway. Involved in rDNA silencing (By similarity). SIMILARITY: Belongs to the IRS4 family."}
{"protein": "MDTHRADASQRSQAPAARPRHAVHSIDHYALEVPDLAVAERFLDAFGLTVARTPECLEVYAADQRCWARFYEGERKRLAYLSFSCFEGDFAGIRQQLAASGATLVEDPRYGDESGVWFFDPDGNLVQVKIGPKTSPSSKSPARLEGAPGGQRGAVVRSQVQRVLPRRLSHVLLFTPSVQRALDFYRDALGLRLSDRSDDVIAFTHAPYGSDHHLLALVKSSARGWHHAAWDVADVNEVGQGASQMAKAGYTQGWGTGRHVLGSNYFFYVLDPWGSFCEYSADIDYIPAGQAWPAGDFAAEDSLYQWGPDVPEYFVRNTEA", "text": "SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family."}
{"protein": "MLREQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPIGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNE", "text": "FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane- associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R (By similarity). Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MNTSDPPAVLRIAAITLLCTASESVEQNPLIPFENAVLGSYAKMASEKRCDGWMAKCPDRDDCCETFHCTRFNARGN", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 65 (Jztx-21) subfamily."}
{"protein": "MSQWSLSQLLSSLHEDIQQRLSVVRKTFGHPGTKGDASENVWIDMLDTYLPKRYQAAKAHVVDSLGNFSQQIDVVVFDRQYSPFIFTYENETIIPAESVYAVFEAKQTADAGLVAYAQEKVASVRRLHRTSLPIPHAGGTYPAKPLIPILGGLLTFESEWSPALGPSMDKALNANLTEGRLDIGCVAAHGHFFYDQASGAYSYTNENKPATAFLFKLIAQLQFSGTVPMIDVEAYGQWLTK", "text": "FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system (PubMed:32839535). FUNCTION: A cyclic nucleotide-activated dsDNase. In the presence of 3',3',3'-cyclic AMP-AMP-AMP (cAAA) and to a lesser extent cyclic-di-AMP (c-di-AMP), endonucleolytically degrades dsDNA (Probable). Binds one cAAA in a pocket on one surface of the trimer; cAAA binding promotes hexamerization which is probably necessary for nuclease activation (PubMed:31932164). The nuclease digests dsDNA to about 50 bp lengths. DNA has been modeled to contact a pair of juxtaposed active sites (one from each layer of the hexamer), accounting for cleavage on both strands (By similarity). SIMILARITY: Belongs to the NucC endonuclease family."}
{"protein": "TSTTLVKCACEPCLCNVDPSKAIDRNGLYYCCEACADGHTGGSKGCGHTGCNC", "text": "FUNCTION: This protein complexes cadmium, zinc and copper. SIMILARITY: Belongs to the metallothionein superfamily. Type 14 family."}
{"protein": "MGASARLLRAAIMGAPGSGKGTVSSRITKHFELKHLSSGDLLRDNMLRGTEIGVLAKTFIDQGKLIPDDVMTRLVLHELKNLTQYNWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVIKQRLTARWIHPGSGRVYNIEFNPPKTMGIDDLTGEPLVQREDDRPETVVKRLKAYEAQTEPVLEYYRKKGVLETFSGTETNKIWPHVYAFLQTKLPQRSQETSVTP", "text": "FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily."}
{"protein": "MKTRIHVVQGDITKLAVDVIVNAANPSLMGGGGVDGAIHRAAGPALLDACLKVRQQQGDCPTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAYLNSLRLVAANSYTSVAFPAISTGVYSYPRAAAAEIAVKTVSEFITRHALPEQVYFVCYDEENAHLYERLLTQQGDE", "text": "FUNCTION: Deacetylates O-acetyl-ADP ribose to yield ADP-ribose and free acetate. Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation. SIMILARITY: Belongs to the YmdB family."}
{"protein": "MTTLEAIKFDRTNVTLQILDQLLIPYSTEYLNIEGVDDAYDAIKSMQVRGAPAIAIVGSFAIVVEIKNRHISSIDELAAKIDYLESSRPTAVNLSNACNEIRALLGNSESLDEVYKRVFDFAVALYDDDLSNNHKIGSNGVDYLVESLRSQNFEGPFSIITYCNTGSLATSGHGTALGIVRSAYKALSKENSKEKFWLEQIYPCETRPYNQGAKLTTFELKYEKIPFTLICDNMVTSLISRTHNKKQVKDIVAPVKFAIVGADRIVQNGDTANKIGTFQLAAIFDSFNRRNTGPRDSLKMIVAAPRTTIDLKTTTGDDIIIEERPANELTTLKGPILRKDVAGEKQIVGVATPGIQVWNPAFDVTPHELIDSIVTEEKVYAKDKEGNYHL", "text": "FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily."}
{"protein": "MNKAQLVEAIADKLGGRQQAADAVDAVLDALVRAVVAGDRVSVTGFGSFEKVDRPARYARNPQTGERVRVKKTSVPRFRAGQGFKDLVSGSKKLPKNDIAVKKAPKGSLSGPPPTISKAAGKKAAAKKATGAAKKTTGAAKKTSAAAKKTTAKKTTGAAKTTAKKTTAKKSAAKTTTAAAKKTAAKKAPAKKATAKKAPAKKSTARKTTAKKATARKK", "text": "FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. SIMILARITY: Belongs to the bacterial histone-like protein family."}
{"protein": "MKELARLESPEILDQYTAGQNDWMEIDQSAVWPKLTEMQGEFCAYCECRLNRRHIEHFRPRGKFPALTFIWSNLFGSCGDSKKSGGWSRCGIYKDNGAGAYNADDLIKPDEENPDDYLLFLTTGEVVPAIGLTGRALKKAQETIRVFNLNGDIKLLGSRRTAVQAIMPNVEYLYSLLEEFEEDDWNEMLRDELEKIESDEFKTALKHAWTSNQEFA", "text": "FUNCTION: Putative HNH endonuclease component of antiviral defense system retron Ec78, composed of a non-coding RNA (ncRNA), a reverse transcriptase (RT), a probable ATPase and this protein. Expression of retron Ec78 confers protection against bacteriophage T5. At multiplicity of infection (MOI) of 0.02 cultures slow growth when infected with T5 but do not collapse, at MOI 2 cultures enter growth stasis."}
{"protein": "MLTLSKFHVILIPILFFITLLSPLFSIALPINIWPKPRFLSWPQHKAIALSPNFTILAPEHQYLSASVTRYHNLIRSENYSPLISYPVKLMKRYTLRNLVVTVTDFSLPLHHGVDESYKLSIPIGSFSAHLLAHSAWGAMRGLETFSQMIWGTSPDLCLPVGIYIQDSPLFGHRGVLLDTSRNYYGVDDIMRTIKAMSANKLNVFHWHITDSQSFPLVLPSEPSLAAKGSLGPDMVYTPEDVSKIVQYGFEHGVRVLPEIDTPGHTGSWGEAYPEIVTCANMFWWPAGKSWEERLASEPGTGQLNPLSPKTYEVVKNVIQDIVNQFPESFFHGGGDEVIPGCWKTDPAINSFLSSGGTLSQLLEKYINSTLPYIVSQNRTVVYWEDVLLDAQIKADPSVLPKEHTILQTWNNGPENTKRIVAAGYRVIVSSSEFYYLDCGHGGFLGNDSIYDQKESGGGSWCAPFKTWQSIYNYDIADGLLNEEERKLVLGGEVALWSEQADSTVLDSRLWPRASALAESLWSGNRDERGVKRCGEAVDRLNLWRYRMVKRGIGAEPIQPLWCLKNPGMCNTVHGALQDQ", "text": "FUNCTION: Has a broad substrate specificity. Can use synthetic substrates such as p-nitrophenyl-beta-N-acetylglucosaminide, p- nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p- nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU- GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D- glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the glycosyl hydrolase 20 family."}
{"protein": "MRKHPQTATKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRNLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQPDADGNRPDVVITEIGGTVGDIESQPFLEAARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVISTPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGGFKHRAKVEICWVASDGCETTSGAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSVGLTNANSAEFDPDTPDPVIATMPDQEEIVAGEADLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDKIAESGLRFSGTSPDGHLVEFVEYPPDRHPFVVGTQAHPELKSRPTRPHPLFVAFVGAAIDYKAGELLPVEIPEIPEHTPNGSSHRDGVGQPLPEPASRG", "text": "FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Is essential for M.tuberculosis growth in vitro and ex vivo (PubMed:26097035). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity). SIMILARITY: Belongs to the CTP synthase family."}
{"protein": "MADKSTEVEKAIDPIIDLGNLLFIDREPLQGDAEEGLEERARKNTQLLFNNIWQLEQKRVEEAIIVTLPAATYRLPREKKLPEKKEPTKWEKYAKEKGIEKRKKDKKVFDEATKEWKPTYGYRRGNDNTKDWLIEIPDNAEDPNKDFFAERREKKKERVAKNEMQRMKNLARQMKTTVKTGPSTDKMIGVGIDAKDKSKQDVRFAVDRAKLATASAGKFQEGLKGEKANIKTGKKRKFESNEAPVSAEKERALQILQRMKSKKAKIVEEKASAVAGPLREKKEKQEKKGAKEATRQKSQIHRQQWFKNKVDSKKKGTGGAKKKGANKRK", "text": "FUNCTION: Involved in ribosomal large subunit assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRS1 family."}
{"protein": "MSRGPSSAVLPSALGSRKLGPRSLSCLSDLDGGVALEPRACRPPGSPGRAPPPTPAPSGCDPRLRPIILRRARSLPSSPERRQKAAGAPGAACRPGCSQKLRVRFADALGLELAQVKVFNAGDDPSVPLHVLSRLAINSDLCCSSQDLEFTLHCLVPDFPPPVEAADFGERLQRQLVCLERVTCSDLGISGTVRVCNVAFEKQVAVRYTFSGWRSTHEAVARWRGPAGPEGTEDVFTFGFPVPPFLLELGSRVHFAVRYQVAGAEYWDNNDHRDYSLTCRNHALHMPRGECEESWIHFI", "text": "FUNCTION: Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis."}
{"protein": "MMSRLNSVVIKLWLTIILIVTTVLILLSIALITFMQYYFTQETENAIREDARRISSLVEQSHNKEEAIKYSQTLIENPGGLMIINNKHRQSTASLSNIKKQMLNEVVNNDHFDDVFDKGKSVTRNVTIKEKGSSQTYILLGYPTKAQKNSHSKYSGVFIYKDLKSIEDTNNAITIITIITAVIFLTITTVFAFFLSSRITKPLRRLRDQATRVSEGDYSYKPSVTTKDEIGQLSQAFNQMSTEIEEHVDALSTSKNIRDSLINSMVEGVLGINESRQIILSNKMANDIMDNIDEDAKAFLLRQIEDTFKSKQTEMRDLEMNARFFVVTTSYIDKIEQGGKSGVVVTVRDMTNEHNLDQMKKDFIANVSHELRTPISLLQGYTESIVDGIVTEPDEIKESLAIVLDESKRLNRLVNELLNVARMDAEGLSVNKEVQPIAALLDKMKIKYRQQADDLGLNMTFNYCKKRVWSYDMDRMDQVLTNLIDNASRYTKPGDEIAITCDENESEDILYIKDTGTGIAPEHLQQVFDRFYKVDAARTRGKQGTGLGLFICKMIIEEHGGSIDVKSELGKGTTFIIKLPKPE", "text": "FUNCTION: Member of the two-component regulatory system SrrA/SrrB, which is involved in the global regulation of staphylococcal virulence factors in response to environmental oxygen levels as well as biofilm formation. Also plays an essential role in host-derived nitric oxide resistance by regulating hmp/flavohemoglobin, an enzyme that detoxifies nitric oxide by converting it to nitrate. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to SrrA. In turn, SrrA binds to the upstream promoter regions of the target genes to positively and negatively regulate their expression. FUNCTION: Member of the two-component regulatory system SrrA/SrrB, which is involved in the global regulation of staphylococcal virulence factors in response to environmental oxygen levels as well as biofilm formation (PubMed:24222487). Also plays an essential role in host- derived nitric oxide resistance by regulating hmp/flavohemoglobin, an enzyme that detoxifies nitric oxide by converting it to nitrate (PubMed:16859493, PubMed:24222487). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to SrrA. In turn, SrrA binds to the upstream promoter regions of the target genes to positively and negatively regulate their expression (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MARGERRRRAAAAEGARPLERARGAGRRDGRAGGARGSAGGAALAVVVLALAFGLSGRWVLAWLGVRRALTLHPAPSALPPDSSSPAVAPEFFWGTYRPHVYFGMKTRSPKPLLTGLMWAQQGATPGTPPKLRHTCEQGDGVGPYGWEFHDGLSFGRQHIYDGALRLTTEFVKRSGGHHGGDWSWRVTVEPQASGTPSFPLVSLFFYVVTDGQEVLLPEVGAKGQLKFISGHTSELGDFRLTLLPPTTPGDTVPKHGSYNVFWSSNPGLPLLTDMVKSHLNSWFHHRPPGASPERYLGLPGSLKWEERGPSGQGQFLVQQVTLKAPFSVEFVFESGSARTGRDQASEQLVGGQLTRALESHAAAFKERFERTFQLKEKGLSPEEQALGQVALSGLLGGIGYFYGQGLVLPDTGMEGSEQKMDPSLFPPVPLFSGVPSRSFFPRGFLWDEGFHQLVVQRWDPHLTREALGHWLGLLNADGWIGREQILGDEARARVPPEFLVQRAAHANPPTLLLPVIHMLEGRAPEDLAFLRRAFPRLHAWFSWLHQSQAGPVPLSYRWRGRDLALPTLLNPKTLPSGLDDYPRASHPSAAERHLDLRCWVTLGARVLSQLAEELGETEAAAELGPLAASLEAAGSLDELHWAPELGVFADFGNHTKAVQLKSRPPQGLVRVVGRPPARLQYVDALGYVSLFPLLLQLLEPSSPRLGPLLDVLADSRHLWSPFGLRSLSASSLFYKQRNTEHDPPYWRGAVWLNINYLALGALHHYGRVEGPHKVQAAKLYRELRANVVSNVRQQYQATGFLWEQYSDQDGRGMGCRPFQGWTSLVLLIMAEEY", "text": "FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 63 family."}
{"protein": "MEQNLPSRITKLIKKSESGDFASSYQLYKVFGSKEYGVEPDEKMSDYFKELSAKQLEGGQLRVADIHLENYKGFESLIMDFSMKKNSTILVGNNGCGKSTILDAIQKGLTHLSSRLSTRSHNGDGIEKHELRKGQNYASIAINYDYMGIRFPMIIATTEPGYEDRAKSNYSGINELGSIFKTAHSINPNVSFPLIAMYTVERANDVSTRDIENSEEIKEAQIWDKFKAYNKSLTGKADFKLFFRWFKELIEIENSDNADITALRAEIRAKEKDLDNPLLKALLAENKNSETTKKLLEDHQNSLKVLKEKLNSYYSVNSKTLHTVEDAMYSFLPGFSNLKLQRAPLDLIVDKNNVSLSVLQLSQGEKTILALIADIARRLTLLNPNSVNPLDGTGIVLIDEIDLHLHPSWQQNIIPRLEKTFKNIQFIVTTHSPQVCHTIDSQNIWLLKNGQKFKAPKGVRGAISSWVLENLFEVAQRPPEDKYTKLLQEYKNLVFSEKYASEDARKLGATLSQHFGPDDETLVELKLEIEKRIWEDDFEKDQ", "text": "FUNCTION: Probable ATPase component of antiviral defense system retron Ec83, composed of a non-coding RNA (ncRNA), a reverse transcriptase (RT), this protein and a putative HNH endonuclease. Expression of retron Ec83 confers protection against bacteriophage T2, T4 and T6. At multiplicity of infection (MOI) of 0.02 cultures slow growth when infected with T4 but do not collapse, at MOI 2 cultures enter growth stasis."}
{"protein": "MTKQSADSNAKSGVTSEICHWASNLATDDIPSDVLERAKYLILDGIACAWVGARVPWSEKYVQATMSFEPPGACRVIGYGQKLGPVAAAMTNSAFIQATELDDYHSEAPLHSASIVLPAVFAASEVLAEQGKTISGIDVILAAIVGFESGPRIGKAIYGSDLLNNGWHCGAVYGAPAGALATGKLLGLTPDSMEDALGIACTQACGLMSAQYGGMVKRVQHGFAARNGLLGGLLAHGGYEAMKGVLERSYGGFLKMFTKGNGREPPYKEEEVVAGLGSFWHTFTIRIKLYACCGLVHGPVEAIENLQGRYPELLNRANLSNIRHVHVQLSTASNSHCGWIPEERPISSIAGQMSVAYILAVQLVDQQCLLSQFSEFDDNLERPEVWDLARKVTSSQSEEFDQDGNCLSAGRVRIEFNDGSSITESVEKPLGVKEPMPNERILHKYRTLAGSVTDESRVKEIEDLVLGLDRLTDISPLLELLNCPVKSPLV", "text": "FUNCTION: Involved in the production of itaconic acid, a soluble unsaturated dicarboxylic acid mainly produced from sugars. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PrpD family."}
{"protein": "MAVKTYQAGVTQYRQSYWQPDYVPLDTDILACFKITPQPGVDREEAAAAVAAESSCGTWTTVWTDLLTDLDYYKGRAYRLEDVPGDDTCYYAFIAYPIDLFEEGSVVNVFTSLVGNVFGFKAVRALRLEDLRFPIAYVKTCGGPPHGIQVERDRLNKYGRPMLGCTIKPKLGLSAKNYGRACYEALRGGLDFTKDDENINSQPFMRWRDRFDFVMEAVQKAEQETGERKGHYLNVTAPTPEEMYKRAEHAKEIGAPIIMHDYLAGGLCANAGLANWCRDNGILLHIHRAMHAVIDRNPHHGIHFRVLTKILRLSGGDHLHTGTVVGKLEGDRASTLGWIDLLRESFVPEDRSRGIFFDQDWGSMPGCFAVASGGIHVWHMPALVTIFGDDSVLQFGGGTLGHPWGNAAGAHANRVALEACVQARAEGRQLEKEGKDILTAAAAHSPELKIAMETWKEIKFEFEAVDQLAIANK", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
{"protein": "MSKKYDAGVKEYRDTYWTPDYVPLDTDLLACFKCTGQEGVPREEVAAAVAAESSTGTWSTVWSELLTDLEFYKGRCYRIEDVPGDKESFYAFIAYPLDLFEEGSITNVLTSLVGNVFGFKALRHLRLEDIRFPMAFIKTCGGPPNGIVVERDRLNKYGRPLLGCTIKPKLGLSGKNYGRVVYECLRGGLDLTKDDENINSQPFQRWRERFEFVAEAVKLAQQETGEVKGHYLNCTATTPEEMYERAEFAKELDMPIIMHDYITGGFTANTGLANWCRKNGMLLHIHRAMHAVIDRHPKHGIHFRVLAKCLRLSGGDQLHTGTVVGKLEGDRQTTLGYIDNLRESFVPEDRSRGNFFDQDWGSMPGVFAVASGGIHVWHMPALLAIFGDDSCLQFGGGTHGHPWGSAAGAAANRVALEACVKARNAGREIEKESRDILMEAAKHSPELAIALETWKEIKFEFDTVDKLDVQ", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Carboxysome Note=This bacterium makes alpha-type carboxysomes. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
{"protein": "MVRSGKKAVVLATVAFCATSVVQKTCGFVPSPLRQRAAAAGAAASVATMFAPAAFADEIGDAAKTLGDASYAFAKEVDWNNGIFLQAPGKLQPLAALKAIDKMIVMGAAADPQLLKAAAEAHHKAITTVSGANGVTSRADWDNVNAALGRVISAVPEKMVMDVYNSVAKITDPKVPAYMNSLVNGADAEKAYAGFLAFKDVVKKNQVTSAAGPATVPSGDTIGVAAQKLSDASYPFLKQIDWLSDVYLKPLPGVSAQQSLKAIDRMIVMGAQADGNALKAAAEAHHKAIGSIDAKGVTSAADYAEVNAAIGRVVASVPKSTVMDVYKAMASVTDTGIPLNMFSKVNPLDANAAAKAFYTFKDVVLAAQR", "text": "FUNCTION: Water-soluble antenna for capture of solar energy in the blue-green range. Peridinin is an asymmetric carotenoid. SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MSVNLSKNGAALQAAYKDVLDEKTKTDWALYTYEGNSNDIRLAETGDGGLEELVEELSSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVKDARKGMCANHVSTMASFLKGAHVTINARAEEDVEPESIMEKVAKASGANYNFHKESNRGNEGPQGPVGSVYQKTNAMSEIKRVGKENFWAKAEKDEEERRIEEHRRANVEKDRLERERKEREQREAEERERRFRERSKEIDGHRKQQEEVEKQQTVPASQRSVNPREMFLQKERSLPESGSVSAQPEQFTASQQEEENIYQDATENQNIYEDTPQEDPVYETGVAEDSGMCARALYDYQAADDTEISFDPDDVIIQIEMIDDGWWRGVAPSGHFGMFPANYVELLE", "text": "FUNCTION: Adapter protein that binds F-actin and dynamin, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation. Does not bind G-actin and promote actin polymerization by itself, but excerts its functions by interaction with other proteins. Required for the formation of organized podosome rosettes (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell projection, ruffle Cytoplasm, cell cortex Cytoplasm, cytosol Synapse Perikaryon Cell projection, neuron projection Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, podosome Early endosome Cell projection, dendrite Postsynaptic density. SIMILARITY: Belongs to the ABP1 family."}
{"protein": "MNTNLLFIPLKQSSVLDLGDELRQVITNNYFQPASSFNSDLIYITQLRNQVAQIKNVNDELGKTSQDDSILLEYLQVLNTLQNKFSDDCVEFAWFDTLAYGPQGPYRYRSLKIEKLNVIYQIGSLYSQIAISESRHTDIGLKRACHYFQLSAGCFMFINNFLIETIKNKNDPLVLSIPLSMQSSTIQCLEYLMLAQAQETIWQKAINNNSMKDSVVARLSIQTSEYYSKALDFGNSSDLIKLEWINHMKVKKLHFLAAAHLRSSTIAADSFQYGEQVAHLRVASQAVDQALKSKKYVNSLVLEDLQGLADVIKVRLRTAEKDNDLVYLKIVPQEKELKTIIGVSMVKSIIPEAFEQKPESNTEIFKELLPYVIIHVAQAMRERQDEYVQTKFHTPISSLNNMLVKFLIDRDLPSSIDSIQQPENIPDSVIHHSQEILKTGGVDFIDKAFKELDKLKLECNHLLQECETRIDLDRSEDDMLRRKQGSTRWTRKSTDDAAQELIKKVDKMKQYLLQANNGDGFVLKKFYDIKPALDVYSSGYKALSQYIPNSQYIELPEQLSIVISDLRSCLARANTLESERKEFLQTLEIRSRDNSILPKLITEYNSNRSKYQTENGEFNFNAFESVYEKHMKLFDSDIKYIARTRDSQMTLEHEIDSINQKFVQEFKSLQNSSNEKRQQVLQYLETAYEKFLEIINNLTEGSKFYTDFIEKGSAVLQECEEYLYRRRVESRDLELAISNSFQQQQQVQEQNEQLSVPRNYSNDKLISPKTSKPGLWNPNSDIQFS", "text": "FUNCTION: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. May act as a scaffold protein that recruits the calpain-like protease RIM13 via SNF7 to its substrate RIM101 (By similarity). Required for filamentation. SIMILARITY: Belongs to the palA/RIM20 family."}
{"protein": "MKPDTVSLTRAFSKATSTSSKAALSWLKKYNFDYDVAYTKWIQQKSREEAEKQLNNVFSQFSSKEDKDLIELDGSVQLFTALDISLEDPETLLVSYFLKSPRMGEFHRESFVEGALNLSTTSLDQLKLAIKEKVQVWRSDASLQKAIYIYTYPLACDKGKKTLSTSIAIEFFQILLKDTFPLLDDWIAFLKVSPIIEKSLPKDTWNELWDFSVFVKSDPNCSNYDFEGAWPTLIDEFVSYYREHGYKNSSS", "text": "FUNCTION: May contribute to neddylation of cullin components of SCF- type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity)."}
{"protein": "MTGVAVPHRAELARQLIDARNRTLRLVDFDDAELRRQYDPLMSPLVWDLAHIGQQEELWLLRGGDPRRPGLLEPAVEQLYDAFVHPRASRVHLPLLSPAQARRFCATVRSAVLDALDRLPEDADTFAFGMVVSHEHQHDETMLQALNLRSGEPLLGSGTALPPGRPGVAGTSVLVPGGPFVLGVDLADEPYALDNERPAHVVDVPAFRIGRVPVTNAEWRAFIDDGGYRQRRWWSDAGWAYRCEAGLTAPQFWNPDGTRTRFGHVEDIPPDEPVQHVTYFEAEAYAAWAGARLPTEIEWEKACAWDPATGRRRRYPWGDAAPTAALANLGGDALRPAPVGAYPAGASACGAEQMLGDVWEWTSSPLRPWPGFTPMIYQRYSQPFFEGAGSGDYRVLRGGSWAVAADILRPSFRNWDHPIRRQIFAGVRLAWDVDRQTARPGPVGGC", "text": "FUNCTION: Catalyzes the oxidative sulfurization of hercynine (N- alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-L- glutamyl-L-cysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine. SIMILARITY: Belongs to the EgtB family."}
{"protein": "MDHAPERFDATPPAGEPDRPALGVLELTSIARGITVADAALKRAPSLLLMSRPVSSGKHLLMMRGQVAEVEESMIAAREIAGAGSGALLDELELPYAHEQLWRFLDAPVVADAWEEDTESVIIVETATVCAAIDSADAALKTAPVVLRDMRLAIGIAGKAFFTLTGELADVEAAAEVVRERCGARLLELACIARPVDELRGRLFF", "text": "FUNCTION: A minor component of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm artificial BMCs with a molecular mass of 6.5 MDa. This protein does not form stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of BMC-T trimers protruding to the exterior. SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the bacterial microcompartments protein family."}
{"protein": "MQEYCELVRRLYAEIASGDLGYIPDSLGCVLKTLDGIAANDALPSSVREQAAFAAANLLVSDYVNE", "text": "SIMILARITY: Belongs to the UPF0253 family."}
{"protein": "MSFEVPSPYVWDDSFRVAYDNLDSEHQALFKCIAKCAENRADAAALADLVKVTVDHFADEERMMAKTNFSGLPEHNKIHSEFVAKIKSLSAPLDDATVAFAKQWLVNHIKGIDFKYKGNL", "text": "FUNCTION: Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms (By similarity). SIMILARITY: Belongs to the hemerythrin family."}
{"protein": "MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGAMSLADMAEVVLRQAPDKAIWLGWSLGGLVASQIALTHPERVQAIVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPKVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPDEFCHLLVALKQRV", "text": "FUNCTION: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family."}
{"protein": "MQNNNPCGLDGFAFLEFSGPDRNKLHQQFSEMGFQAVAHHKNQDITLFKQGEIQFIVNAASHCQAEAHASTHGPGACAMGFKVKDAKAAFQHAIAHGGIAFQDAPHANHGLPAIQAIGGSVIYFVDEEHQPFSHEWNITSSEPVVGNGLTAIDHLTHNVYRGNMDKWASFYASIFNFQEIRFFNIKGKMTGLVSRALGSPCGKIKIPLNESKDDLSQIEEFLHEYHGEGIQHIALNTNDIYKTVNGLRKQGVKFLDVPDTYYEMINDRLPWHKEPLNQLHAEKILIDGEADPKDGLLLQIFTENIFGPVFFEIIQRKGNQGFGEGNFQALFEAIERDQVRRGTLKELT", "text": "FUNCTION: Catalyzes the transformation of p-hydroxyphenylpyruvate into HGA. Has hemolytic and brown pigment production activity. SIMILARITY: Belongs to the 4HPPD family."}
{"protein": "MVNDFNEKNGIKKRLLDFFPVVLEGIREILESMQYFPEETEKLLYSIKRNTLGGKNNRGLAVLQSLTSLINRELEEAEFRDAALLGWLIEILQGCFLMADDIMDQSIKRRGLDCWYLVVGVRRAINESQLLEACIPLLIRKYFRNMPYYVDLLDTFREVTFLTELGQQEDLLSSRDGEASLRSFDLMKYDFIITYKTSFYSFYLPIKCALLLSRNSNQKAYDTTIKLSKLLGYYFQVQDDYLDCFGDYTVLGKVGMDIQDNKCTWLVCYAEKFASADQLNLLRAHYGKAGSENIAVIKQLYHELQIPELYHKFEDDMVDSISKEIDLIDESTGLKKCIFTKFFQLIYKRSR", "text": "FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of ypt7 and rhb1. May be involved in vesicle trafficking and protein sorting. Required for forespore membrane formation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
{"protein": "MALSKRELDELKPWIEKTVKRVLGFSEPTVVTAALNCVGKGMDKKKAADHLKPFLDDSTLRFVDKLFEAVEEGRSSRHSKSSSDRSRKRELKEVFGDDSEISKESSGVKKRRIPRFEEVEEEPEVIPGPPSESPGMLTKLQIKQMMEAATRQIEERKKQLSFISPPAPQPKTPSSSQPERLPIGNTIQPSQAATFMNDAIEKARKAAELQARIQAQLALKPGLIGNANMVGLANLHAMGIAPPKVELKDQTKPTPLILDEQGRTVDATGKEVELTHRMPTLKANIRAVKREQFKQQLKEKPSEDMESNTFFDPRVSIAPSQRQRRTFKFHDKGKFEKIAQRLRTKAQLEKLQAEISQAARKTGIHTSTRLALIAPKKELKEGDIPEIEWWDSYIIPNGFDLTEENPKREDYFGITNLVEHPAQLNPPVDNDTPVTLGVYLTKKEQKKLRRQTRREAQKELQEKVRLGLTPPPEPKVRISNLMRVLGTEAVQDPTKVEAHVRAQMAKRQKAHEEANAARKLTAEQRKVKKIKKLKEDISQGVHISVYRVRNLSNPAKKFKIEANAGQLYLTGVVVLHKDVNVVVVEGGPKAQKKFKRLMLHRIKWDEQTSNTKGDDDEESDEEAVKKTNKCVLVWEGTAKDRSFGEMKFKQCPTENMAREHFKKHGAEHYWDLALSESVLESTD", "text": "FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). SUBCELLULAR LOCATION: Nucleus Nucleus speckle."}
{"protein": "MSRYDSRTGDSTSYRDRRSDSGFGGTSSYGSSGSHTSSKKDNDGNESPRKLDLDGLTPFEKNFYVESPAVAAMTDTEVEEYRKLREITVEGKDIPKPVKSFRDVGFPDYVLEEVKKAGFTEPTPIQSQGWPMAMKGRDLIGIAETGSGKTLSYLLPAIVHVNAQPMLAHGDGPIVLVLAPTRELAVQIQQEASKFGSSSKIKTTCIYGGVPKGPQVRDLQKGVEIVIATPGRLIDMMESNNTNLRRVTYLVLDEADRMLDMGFDPQIRKIVSHIRPDRQTLYWSATWPKEVEQLSKKFLYNPYKVIIGSSDLKANRAIRQIVDVISESQKYNKLVKLLEDIMDGSRILVFLDTKKGCDQITRQLRMDGWPALSIHGDKSQAERDWVLSEFRSGKSPIMTATDVAARGLDVKDVKYVINYDFPGSLEDYVHRIGRTGRAGAKGTAYTFFTVANARFAKELTNILQEAGQKVSPELASMGRSTAPPPPGLGGFRDRGSRRGWS", "text": "FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily."}
{"protein": "MELHGEEQPPPPQEPWGRLLRLGAEEDEPQILLWKREWTIGRRRGCDLSFPSNKLVSGDHCKLTVDEISGEVTLEDTSTNGTVINKLQVVKKQTYPLQSGDIIYLVYRKNEPEHNVAYLYESLSGKQSLTQDSLEANKENMFHVTKDCSGPGQGDDPQVPLLSPMAQTCLEEPQPSTSTSDLLPTASTSSTEPELTSAGQKHSSSSGPGNTSISPKGRSSLVANGELSSLSPVFQDKEASFSLLESKDHEELEPAKKKMKGDGELDTNLQLLVSGQRGNAQTSSEDVKDASVKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVRSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYIVCRQCPEYRRQAVQSLPCPVPESELGATLALGGEAPSTSASLPTAAPDYMCPLQGSHAICTCCFQPMPDRRAEREQDPRVAPQQCAVCLQPFCHLYWGCTRTGCFGCLAPFCELNLGDKCLDGVLNNNNYESDILKNYLATRGLTWKSVLTESLLALQRGVFMLSDYRITGNTVLCYCCGLRSFRELTYQYRQNIPASELPVTVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN", "text": "FUNCTION: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys- 48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'- linked polyubiquitin chains and functions with the specific ubiquitin- conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress (By similarity). SUBCELLULAR LOCATION: Nucleus, PML body. SIMILARITY: Belongs to the CHFR family."}
{"protein": "MQPRRPDRFDGLEYRGTSWGRGDGDVPPYQHGFPARSFSSSGDLSQHWVTTPPDIPGSRNLHWGEKSPQYGADSNAGPAAVGEESSSSSSGGEHLNRFAGFGIGLASLFTENVLAHPCIVLRRQCQVNYHARNYQLSPFSIVNIMYSFTKTQGFRALWKGMGSTFIVQGISLGAEGMLSEFTHLPRELNHKWNPKQIGGHLLLKGLVYVIVTPFYSASLIETVQSEIIHDNPGILDCLKEGIGRVLNLGVPYSKRLLPLLVLTFPTVLHGILHYIISSTIQKCVLFFIKKKSPAQLPGDGSNAVQNKLEDYFPELIANFAASLCADVLLYPLETVLHRLHIQGTRTIIDNTDLGHEVVPINSQYEGLKDCINTIKREEGGLGFYKGFGAVVVQYTLHAIVLQITKIIYSSVVQTAS", "text": "FUNCTION: May play a role in mitochondrial dynamics by controlling mitochondrial membrane fission. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MAAAQPKYPAGATARRLARGCWSALWDYETPKVIVVRNRRLGVLYRAVQLLILLYFVWYVFIVQKSYQESETGPESSIITKVKGITTSEHKVWDVEEYVKPPEGGSVFSIITRVEATHSQTQGTCPESIRVHNATCLSDADCVAGELDMLGNGLRTGRCVPYYQGPSKTCEVFGWCPVEDGASVSQFLGTMAPNFTILIKNSIHYPKFHFSKGNIADRTDGYLKRCTFHEASDLYCPIFKLGFIVEKAGESFTELAHKGGVIGVIINWDCDLDLPASECNPKYSFRRLDPKHVPASSGYNFRFAKYYKINGTTTRTLIKAYGIRIDVIVHGQAGKFSLIPTIINLATALTSVGVGSFLCDWILLTFMNKNKVYSHKKFDKVCTPSHPSGSWPVTLARVLGQAPPEPGHRSEDQHPSPPSGQEGQQGAECGPAFPPLRPCPISAPSEQMVDTPASEPAQASTPTDPKGLAQL", "text": "FUNCTION: Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes to the apical membranes of hair cells in the organ of Corti. SIMILARITY: Belongs to the P2X receptor family."}
{"protein": "MEKGTRQRNNTAKNHPDRGSDTSPEAEASSGGGGVALKKEIGLVSACGIIVGNIIGSGIFVSPKGVLENAGSVGLALIVWIVTGVITAVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGFLRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSVRWATRVQDIFTAGKLLALALIIIMGVVQICKGEFFWLEPKNAFENFQEPDIGLVALAFLQGSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANIAYVTAMSPQELLASNAVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVKRCTPIPALLFTCLSTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPIKISLLFPIIYLLFWAFLLIFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFNDFIESLTLVSQKMCVVVYPQEGDSGTEETIDDVEEQHKPIFQPTPVKDPDSEEQP", "text": "FUNCTION: Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney. SUBCELLULAR LOCATION: Cytoplasm Basolateral cell membrane; Multi-pass membrane protein Note=Localized to the cytoplasm when expressed alone (By similarity). When coexpressed with SLC3A2/4F2hc, is localized to the plasma membrane. Colocalized with SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal tubules and small intestine epithelia of the villi (By similarity). SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family."}
{"protein": "ADKAKAAEEAKKKQDDIDRKKAEVRKRLEEQSLKKQKKGFMTPERKKKLRLLLRKKAAEELKKEQERKAGERRKIIDQRCGQPKNLDGANEEQLRAIIKEYFDHTAQIESDKYDVELEIIRKDYEINELNIQVNDLRGKFIKPTLKKVSKYENKFAKLQKKAAEFNFRNQLKTVKKKEFELEDDKGATEGDGPAAEEVAAE", "text": "FUNCTION: Troponin I is the actomyosin ATPase inhibitory subunit present in the thin filament regulatory complex. SIMILARITY: Belongs to the troponin I family."}
{"protein": "MSNKSNDNGRAYEFAFINELGRIATQNQNINIEKNSSYYVVEKSWSTLSDLEKEKYTKSAIAGINLITSLEPIIEDGNGVLNLKIQADNKGELGDIRDILIQRENINWEIGLSLKHNHFAVKHSRLSHKIDFSEKWFQLPSSQNYWDNILPIFEKLEIYKKDKIKWRELSNKEDCIYYPILKSFIAEIKEKYDKYNSIVPQRMVEYLLGYFDFYKIISQDNKKLTSIQSFNLRGTLNKPSKKRKADIFIPVANLPTRIIDIDFKPNSKNTVELYLDKGWQFSFRIHNASTIIEPSLKFDIKLIGVPATIICLETPWEE", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGCC-3' and cleaves after G-2."}
{"protein": "MEGPSLRGPALRLAGLPTQQDCNIQEKIDLEIRMREGIWKLLSLSTQKDQVLHAVKNLMVCNARLMAYTSELQKLEEQIANQTGRCDVKFESKERTACKGKIAISDIRIPLMWKDSDHFSNKERSRRYAIFCLFKMGANVFDTDVVNVDKTITDICFENVTIFNEAGPDFQIKVEVYSCCTEESSITNTPKKLAKKLKTSISKATGKKISSVLQEEDDEMCLLLSSAVFGVKYNLLAHTTLTLESAEDSFKTHNLSINGNEESSFWLPLYGNMCCRLVAQPACMAEDAFAGFLNQQQMVEGLISWRRLYCVLRGGKLYCFYSPEEIEAKVEPALVVPINKETRIRAMDKDAKKRIHNFSVINPVPGQAITQIFAVDNREDLQKWMEAFWQHFFDLSQWKHCCEELMKIEIMSPRKPPLFLTKEATSVYHDMSIDSPMKLESLTDIIQKKIEETNGQFLIGQHEESLPPPWATLFDGNHQMVIQKKVLYPASEPLHDEKGKKRQAPLPPSDKLPFSLKSQSNTDQLVKDNWGKTSVSQTSSLDTKLSTLMHHLQKPMAAPRKLLPARRNRLSDGEHTDTKTNFEAKPVPAPRQKSIKDILDPRSWLQAQV", "text": "FUNCTION: May play an important role in lymphopoiesis."}
{"protein": "MKIKTLAMIVVSALALSSTAALADTTTVNGGTVHFKGEVVNAACAVDAGSIDQTVQLGQVRSAKLATAGSTSSAVGFNIQLDDCDTTVATKASVAFAGTAIDSSNTTVLALQNSAAGSATNVGVQILDNTGTPLALNGATFSAATTLNDDPNIIPFQARYYATGAATAGIANADATFKVQYE", "text": "SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the fimbrial protein family."}
{"protein": "FCGSKPRCRPRCKPRCRSRSKKRCRRCRRRCSRIVKKCCRRRSKCCRRRRRCPCPCPRKKLRCCKRRPKRRCPKRKKKRCRRKC", "text": "FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. This protamine condenses spermiogenic chromatin in a pattern which comprises fibers with a progressively larger diameter and lamellae that finally undergo definitive coalescence. SUBCELLULAR LOCATION: Nucleus Chromosome."}
{"protein": "MITIKRGLDLPIAGTPSQVINDGKTITKVALLGEEYVGMRPTMHVRVGDEVKKAQILFEDKKNPGVKFTSPASGKVIEVNRGAKRVLQSVVIEVAGDEQITFDSFEASQLASIDRQTVKTQLVESGLWTALRTRPFSKVPAIESSTQAIFVTAMDTNPLAAKPETIINEQSEAFVAGLDILSTLTEGKVYVCKSGTSLPRSSQPNVEEHVFDGPHPAGLVGTHMHFLYPVNAVNVAWSINYQDVIAFGQLFLTGELYTQRVVSLAGPVVNKPRLVRTQIGASLEELTDNELMPGEVRVISGSVLSGVKAAGPVAYLGRYHLQVSVLREGRDKDFLGWAMPGKNKFSVTRSFLGHLFTGQLFNMTTTTNGSDRAMVPIGNYEKVLPLDMEPTLLLRDLCAGDIDSAQRLGALELDEEDLALCTFVCPGKYEYGQLLRECLDKIEKEG", "text": "FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. SIMILARITY: Belongs to the NqrA family."}
{"protein": "MATSHPDPTTSRHVAVIGAGAAGLVAARELRREGHSVVVLERGSQIGGVWAYTSQVEPDPLSLDPTRPVVHSSLYRSLRTNIPRECMGFTDFPFATRPHDGSRDPRRHPAHTEVLAYLRDFAKEFDIEEMVRFETEVVKAEQVAAEGEERGKWRVESRSSDGVVDEIYDAVVVCNGHYTEPRHALITGIDSWPGKQIHSHNYRVPDQFKDQVVIVIGSSASGVDICRDIAQVAKEVHVSSRSTSPDTYEKLTGYENLWLHSTIQIAREDGSVVFENGKTIYADTIMHCTGYKYYFPFLDTKGEVTVDDNRVGPLYKHVFPPALAPSLSFIGLPWQITPFPMFELQSKWVAAVLSGRVSLPSQDEMMEDTKAFYDKLEASGIPKRYTHLMPDDSQFEYDNWLADQCEYPRIEKWREQMFYIGFKRIYAQSSTYRDNWDDDHLIVEAYDDFVKFMSSYQELLPMLKT", "text": "FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates of any chain length into methylsulfinylalkyl glucosinolates. SIMILARITY: Belongs to the FMO family."}
{"protein": "MSKDMSYSGVMSRRNEIMKNAIGIDYTTFESGSLSFDYEKMMRETGYTLEEMQKIQYSTGVGRTPVLELRNITALARKYAAPGKGARIFIKDEAGNPSGSFKARRAANAVYHAKKLGYKGVIAATSGNYGAAVASQAAMAGLKCIIVQECYDSKGVGQPEIIEKARKCEALGAEVVQLSVGPELFYKFLSLLEETGYFNASLYTPFGIAGVETLGYELAVEFREAYGKDPDVVVCSNAGGGNLTGTARGLIKAGAQSEVVAASVNLQGLHMASDTQFNKKSFTTSHTGFGMPFATWPDRSDVPRSAARPLRYMDRYVTVNQGEVFYITETLASLEGLEKGPAGNTALAAAFSLAQEMDKDQIIVVQETEYTGAGKHIQPQLAFARDNGIDIKFGNPKEEVAGINIILPENPGMIKAVDHEMNKLRKSLIKNALANYPDAKLDDSDIDFLVKETKSDTEFVKATIKEIKG", "text": "FUNCTION: Involved in the ornithine fermentation pathway. Catalyzes the thiolytic cleavage of 2-amino-4-ketopentanoate (AKP) with coenzyme A (CoA) to form acetyl-CoA and alanine. It is strictly specific for AKP. SIMILARITY: Belongs to the threonine synthase family."}
{"protein": "MYSTVFYTSVHPSTSVLSRKQLPLLISKDFSAELYHSLPCRSLENGHINKVKGVKVKATIAEAPVTPTEKTDSGANGDLKVPQKKLKVLVAGGGIGGLVFALAAKKRGFDVLVFERDLSAIRGEGQYRGPIQIQSNALAALEAIDLDVAEDIMNAGCITGQRINGLVDGISGNWYCKFDTFTPAVERGLPVTRVISRMTLQQILARAVGEEIIMNESNVVDFEDDGEKVTVVLENGQRFTGDLLVGADGIRSKVRTNLFGPSEATYSGYTCYTGIADFVPADIDTVGYRVFLGHKQYFVSSDVGGGKMQWYAFYNEPAGGADAPNGKKERLLKIFGGWCDNVIDLLVATDEDAILRRDIYDRPPTFSWGRGRVTLLGDSVHAMQPNLGQGGCMAIEDSYQLALELEKACSRSAEFGSPVDIISSLRSYESARKLRVGVIHGLARMAAIMASTYKAYLGVGLGPLSFLTQYRIPHPGRVGGRVFIDLGMPLMLSWVLGGNGDKLEGRIKHCRLSEKANDQLRKWFEDDDALERATDAEWLLLPAGNGSSGLEAIVLSRDEDVPCTVGSISHTNIPGKSIVLPLPQVSEMHARISCKDGAFFVTDLRSEHGTWVTDNEGRRYRTSPNFPTRFHPSDVIEFGSDKAAFRVKAMKFPLKTSERKEEREAVEAA", "text": "FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Involved in the epoxidation of zeaxanthin. Plays an important role in resistance to stresses, seed development and dormancy. SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MISPSFRKGMLKERVMDLASQTTILPLLFGCLGIFSLFRLLQRIRSKAYLRNAVVVVTGATSGLGRECAKVFHAAGAKLVLCGRNVKALEELSRELAGSSQGQTHQPFVVTFDLADPGTIAAAAAEILQCFGYVDVLINNAGISYRGTISDTIVDVDRKVMEINYFGPVALTKALLPSMVERKQGHIVAISSIQGKISIPFRSAYSASKHATQAFFDCLRAEMEEANIKVTVISPGYIHTNLSVNAVTADGSRYGALDKNTAQGRSAAEVAQDVFDAVGKKKKDVLLTDFVPSMAVYIRTLAPGLFFRIMASRARKERKSKSS", "text": "FUNCTION: Putative oxidoreductase. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MFPSRRKAAQLPWEDGRSGLLSGGLPRKCSVFHLFVACLSLGFFSLLWLQLSCSGDVARAVRGQGQETSGPPRACPPEPPPEHWEEDASWGPHRLAVLVPFRERFEELLVFVPHMRRFLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSNSTDYIAMHDVDLLPLNEELDYGFPEAGPFHVASPELHPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPAWRKRDQKRIAAQKQEQFKVDREGGLNTVKYHVASRTALSVGGAPCTVLNIMLDCDKTATPWCTFS", "text": "FUNCTION: Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single- pass type II membrane protein. Note=Cis cisternae of Golgi stack. SIMILARITY: Belongs to the glycosyltransferase 7 family."}
{"protein": "MDKPYGYASVSMSGIDRSAGKDIDLEMGVGEATLYPGLSYGENQLRWGFIRKVYGILSAQLLLTTLISAVVVLNPPVNDLLTGSPGILLFLCIVPFILIWPLHIYHQKHPVNLILLALFTVSLSFTVGVSCAMTEGRIVLQALILTLSVVGSLTAYTFWAAKKGKDFSFLGPILFTSLIILVVTSFIQMFFPLGPTSVAVYGGFSALVFCGYIVYDTDNLIKRFTYDEYILASVALYLDILNLFLTILRILRQGDN", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family."}
{"protein": "MQSIKRTLLLLGALLPAALAAPAREPHPSSNIIPGKYIITFKSGIDTAAIESHTAWASNIHKRNLERRGLVGGEFPAGIERKFKIKDFAAYAGSFDPATIEEIRNSEDVAHVEEDQIWYLDALTTQSGAPWGLGSISHKGQASTNYVYDTSAGAGTYAYVVDSGINVDHIEFQGRATKAYNAVGGDHVDTLGHGTHVAGTIGGKTYGVAKQTNLLSVKVFEGRTGSTSVILDGFNWAANDIVSKGRKGKAAINMSLGGGYSYAFNNAVESAYEQGVLSVVAAGNEGVDASNSSPASAPNALTVGATNKSNARASFSNYGKVLDIFAPGQDILSAWIGSTTATNTISGTSMATPHVVGLAVYLMGLEGVSGPAAVTQRILQLATSGVISDVKGSPNKLAYNGAA", "text": "FUNCTION: Secreted alkaline protease that allows assimilation of proteinaceous substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MSVLTPLLLRGLTGSARRLPVPRAQVHSMPPEQKLGVLELAIGFTSCLVTFLLPAGWILSHLDSYKKRG", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase VIII family."}
{"protein": "MPLPDFHVSEPFTLGIELEMQVVNPPGYDLSQDSSMLIDAVKNKITAGEVKHDITESMLELATDVCRDINQAAGQFSAMQKVVLQAATDHHLEICGGGTHPFQKWQRQEVCDNERYQRTLENFGYLIQQATVFGQHVHVGCASGDDAIYLLHGLSRFVPHFIALSAASPYMQGTDTRFASSRPNIFSAFPDNGPMPWVSNWQQFEALFRCLSYTTMIDSIKDLHWDIRPSPHFGTVEVRVMDTPLTLSHAVNMAGLIQATAHWLLTERPFKHQEKDYLLYKFNRFQACRYGLEGVITDPHTGDRRPLTEDTLRLLEKIAPSAHKIGASSAIEALHRQVVSGLNEAQLMRDFVADGGSLIGLVKKHCEIWAGD", "text": "FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate. SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily."}
{"protein": "MSDSDLGEDEGLLSLTGKRKRRGNLPKESVKILRDWLYLHRYNAYPSEQEKLSLSGQTNLSVLQICNWFINARRRLLPDMLRKDGKDPNQFTISRRGGKASDVALPRGSSPSLLAVSVPAPTNMLSLSVCSMPLHSGQGEKPAAPFPQVELESPKALVTPASTLTLLTRAEAGSPTGGLFNTPPPTPPEQDKDDFSSFQLLVEVALQRAAEMELQKQQEPAPPLLHTPLPFVSENAK", "text": "FUNCTION: Transcriptional repressor, which probably repress transcription by binding directly the 5'-CTGTCAA-3' DNA sequence or by interacting with TGF-beta activated SMAD proteins. Probably represses transcription via the recruitment of histone deacetylase proteins (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Excluded from nucleoli. SIMILARITY: Belongs to the TALE/TGIF homeobox family."}
{"protein": "MSRPFSSGVYVSRGVALLLAALTAVLLLVLVALASLYGSCAHVQPSEQGNSRVKNTSLWPPGGQEWALPTPAQEPTVGTSQDLGPPSGPWDHLRLPPWLVPLHYDLELWPWLQPDKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGPLAQDTRNATVGRVQVEKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGQVLQVGLEGLFLNLYHDEDELRALVATQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNMPQLGQSERIDVNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRTERGKEIRVWARKDDIANGYLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENFTETSEINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVIVPFRHFLAEH", "text": "FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys- LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. SUBCELLULAR LOCATION: Membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the peptidase M1 family."}
{"protein": "DCLGWFKSCDPKNDKCCKNYTCSRRDRWCKYYL", "text": "FUNCTION: Inhibits several voltage-gated sodium channels and only one voltage-gated calcium channel (Cav2.2/CACNA1B (IC(50)=1.1 uM) and Nav1.2/SCN2A (IC(50)=3.7-80 nM), Nav1.3/SCN3A (IC(50)=88-5570 nM), Nav1.1/SCN1A (IC(50)=170-407 nM), Nav1.7/SCN9A (IC(50)=95.5-230 nM), Nav1.6/SCN6A (IC(50)=49.9-3990 nM), Nav1.4/SCN4A (IC(50)=113-400 nM or >10 uM), Nav1.5/SCN5A (IC(50)=1524-1634 nM or >10 uM)) (PubMed:16267209, PubMed:28880874, PubMed:29703751). The toxin acts by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current (PubMed:16267209). It shows moderate affinity for lipid bilayers without cholesterol and high affinity for lipid bilayers containing cholesterol (PubMed:29703751). In vivo, this toxin causes general ataxia, lack of response to stimuli, and semiparalysis (PubMed:16267209). After a few minutes, the mice are unable to stand, and breathing is reduced in rhythm and intensity (PubMed:16267209). Symptoms gradually increase with progressive slowing of breathing and flaccid paralysis; death occurred within 10 to 20 minutes post injection (PubMed:16267209). Animals remain totally flaccid, and no symptoms of excitatory neurotoxicity are observed (PubMed:16267209). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 04 (CcoTx1) subfamily."}
{"protein": "MRYVKLPKENTYEFLERLKDWGKLYAPVKISDKFYDFREIDDVRKIEFHYNRTIMPPKKFFFKPREKLFEFDISKPEYREVIEEVEPFIIFGVHACDIYGLKILDTVYLDEFPDKYYKVRREKGIIIGISCMPDEYCFCNLRETDFADDGFDLFFHELPDGWLVRVGTPTGHRLVDKNIKLFEEVTDKDICAFRDFEKRRQQAFKYHEDWGNLRYLLELEMEHPMWDEEADKCLACGICNTTCPTCRCYEVQDIVNLDGVTGYRERRWDSCQFRSHGLVAGGHNFRPTKKDRFRNRYLCKNAYNEKLGLSYCVGCGRCTAFCPANISFVGNLRRILGLEENKCPPTVSEEIPKRGFAYSSNIRGDGV", "text": "FUNCTION: Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The beta and gamma subunits form the sulfur reducing component that catalyzes the cytoplasmic production of hydrogen sulfide in the presence of elemental sulfur. Not active in the presence of sodium sulfate, sodium sulfite, sodium thiosulfate or cysteine. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGSCCSSQDGDGNGKATAGSTVDSHELSQSVKGKIKQPEPKPKPPPQVPPAQDVKYPIYVGKYDYDSRTDDDLSFKKGDLMYIISTDEGDWWFARSKDTAGKEGYIPSNYVAEYKSLDAEEWFFGQVKRVDAEKQLMMPFNNLGSFLIRDSDTTPGDFSLSVRDIDRVRHYRIKKLENGTYFVTRRLTFQSIQELVAYYTQQADGLCVNLKGPCMVMEKPQTAGLSKQANEEWEIEKKQIKLLRGLGAGQFGEVWEGLWNGTTSVAVKTLKPGTMSIEEFLEEASIMKQLRHPKLIQLYAVCTKEEPIYIVTELMKHGSLLEYLRGDGRSLKLPDLVDMCSQVASGMSYLEQQNYIHRDLAARNILVGEHKICKVADFGLARVIDEEIYEAKLGAKFPIKWTAPEAAMYSRFTIKSDVWSFGIVLYEVITYGRFPYPGMTNAQVLEQIQQSYRMPRPMGCPEKLYAIMMDCWREDPASRPTFETLSWQLEEFFTTGDDAGYKDMER", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family."}
{"protein": "MWETKINPNKVFELRCKNTTYFGIGSIKKIKDILEVLKNKGINNVILVTGKGSYKASGAWDVVKPALETLGFKYSLYDKVGPNPTVDMIDEAAKIGRETGAKAVIGIGGGSPIDTAKSVAVLLEYTDKNARELYEQKFIPEKAAPIIAINLTHGTGTEVDRFAVATIPEKNYKPAIAYDCLYPMYAIDDPSLMTKLDKKQTIAVTIDALNHVTEAATTLVASPYSVLMAKETVRLIVRYLPAAVNDPENLVARYYLLYASALAGISFDNGLLHLTHALEHPLSAVKPEIAHGLGLGAILPAVVKAIYPSVAEVLAEVYSPIVPGLKGLPAEAEYVAKKVEEWLFKVGCTQKLSDFGFTKEDIPTLVRLAKTTPSLDGLLSNAPVEATEAVIAKIYEESF", "text": "FUNCTION: Alcohol dehydrogenase active against primary long-chain alcohols. Pentan-1-ol is the optimum substrate in vitro, but also shows efficient dehydrogenase activity on propanol, hexanol, and ethanol. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family."}
{"protein": "MGSDKRVSRTERSGRYGSIIDRDDRDERESRSRRRDSDYKRSSDDRRGDRYDDYRDYDSPERERERRNSDRSEDGYHSDGDYGEHDYRHDISDERESKTIMLRGLPITITESDIREMMESFEGPQPADVRLMKRKTGVSRGFAFVEFYHLQDATSWMEANQKKLVIQGKHIAMHYSNPRPKFEDWLCNKCCLNNFRKRLKCFRCGADKFDSEQEVPPGTTESVQSVDYYCDTIILRNIAPHTVVDSIMTALSPYASLAVNNIRLIKDKQTQQNRGFAFVQLSSAMDASQLLQILQSLHPPLKIDGKTIGVDFAKSARKDLVLPDGNRVSAFSVASTAIAAAQWSSTQSQSGEGGSVDYSYLQPGQDGYAQYAQYSQDYQQFYQQQAGGLESDASSASGTAVTTTSAAVVSQSPQLYNQTSNPPSSPTEEAQPSTSTSTQAPAASPTGVVPGTKYAVPDTSTYQYDESSGYYYDPTTGLYYDPNSQYYYNSLTQQYLYWDGEKETYMLAAESNSHQQTGLPPAKEGKEKKEKPKSKTAQQIAKDMERWAKSLNKQKENFKNSFQPVNSLREEERRESAAADAGFALFEKKGALAERQQLIPELVRNGDEDNPLKRGLVAAYSGDSDNEEELVERLESEEEKLADWKKMACLLCRRQFPNKDALVRHQQLSDLHKQNMDIYRRSRLSEQELEALELREREMKYRDRAAERREKYGIPEPPEPKRKKQFDAGTVNYEQPTKDGIDHSNIGNKMLQAMGWREGSGLGRKCQGITAPIEAQVRLKGAGLGAKGSAYGLSGADSYKDAVRKAMFARFTEME", "text": "FUNCTION: Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes production of a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes production of a catalytically active form of CASP2/Caspase-2 that induces apoptosis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RBM5/RBM10 family."}
{"protein": "MAASMARLWWPFLARQGLRSRGRCVCSQNPRRSFATEKRVRNLLYEHAREGYSELPYLDMESVCACPEKAARSLELRKGELRPADLPAIISTWQELRQLREQIRSLEAEKEAVAEAVRALLANQDSDQVQKDPQYQGLRARGREIRKQLTPLYPQETQLEEQLYQQALRLPNQTHPDTPVGDESQARVVRVVGEKPAFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTLSKLVSRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPSRFEDLNLAGTAEVGLAGYFMDHSVAFRDLPVRMVCASTCYRAETDTGKEPWGLYRVHHFTKVEMFGVTGPGLEQSSQLLDEFLSLQVEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRYGEVTSASNCTDFQSRRLYIMFETETGELQFAHTVNATACAVPRVLIALLESNQQKDGSVLVPAALQPYLGTDRITAPTHVPLQYIGPNQPQKPRLPGQSATR", "text": "FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily."}
{"protein": "MKQQKAMLIALIVICLTVIVTALVTRKDLCEVRIRTGQTEVAVFTAYEPEE", "text": "FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system (Probable). When overexpressed kills cells within 2 minutes; causes collapse of the transmembrane potential and arrest of respiration (PubMed:3019679). FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system (By similarity). When overexpressed kills cells within minutes; causes collapse of the transmembrane potential and arrest of respiration (By similarity). Its toxic effect is probably neutralized by an antisense antitoxin Sok RNA (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Hok/Gef family."}
{"protein": "MAMAAAAAVASQGLVAASTQQQKKTSAKLSCNAAPVFSGKSFLRVKSGSNGAVRVRNVGVRCEAQAIERESVKADTGSGREEDAFSGLKQVCAVLGTQWGDEGKGKLVDILAQRFDVVARCQGGANAGHTIYNDKGEKFALHLVPSGILNEKTTCVVGNGVVIHLPGFFKEIDNLESKGVNTSGRLLVSDRAHLLFNLHQEVDGLREAELAGQMIGTTKRGIGPCYASKAIRNGIRVGDLRHLDTFREKLDILFRDAAARFKGFEYSAAAVDAEMEMYVKYAERLEHYIVDTVDYVNTAYAEGKRILIEGGQATMLDIDFGTYPFVTSSNPSVGGICTGLGMAPNRLGDIVGVAKAYTTRVGSGPYPTELFGEEGEELRKAGFEWGTTTGRPRRCGWLDIVALNFACTINGFTAINLTKLDVLSGLPEVKLGVAYRTQSGEKLRSFPADLSILEQVEVEYETLEAWKEDITKVRSYAELPVAAQKYVERIEELIGLPCQYIGVGPGRDALIVKQ", "text": "FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the adenylosuccinate synthetase family."}
{"protein": "MSTLYHTCDKIEQRIIWIDCEMTGLDVEKQTLCEIALIVTDSELNTIATGPDIVIHQPKEVLDNMEEWPRNTFHENGLMEKIIASKYSMADAENEVIDFLKLHALPGKSPIAGNSIYMDRLFIKKYMPKLDKFAHYRCIDVSTIKGLVQRWYPDYKHPKKQCTHRAFDDIMESIAELKNYRESIFVKSTASSF", "text": "FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SIMILARITY: Belongs to the oligoribonuclease family."}
{"protein": "MSSSDESGSSSSESEKKVKKTPVKKPKKEPKVSKKGKKEGKKTKKKPKDENAPRRYLSPFIFFSKDHRSVIKNSHPNCSFGEIGSLLGQEWAKISAEDKKKYEKLAAEDKKRWELEKKNYDEKLKTQSQAESSSDSSDESD", "text": "FUNCTION: DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the NHP6 family."}
{"protein": "MERPDKAALNALQPPEFRNESSLASTLKTLLFFTALMITVPIGLYFTTKSYIFEGALGMSNRDSYFYAAIVAVVAVHVVLALFVYVAWNEGSRQWREGKQD", "text": "FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the VMA21 family."}
{"protein": "MLRQNLLDQLKHFIETVSNGHSCPQLLTSPNLIKLALGFLEELPATRDIVFEYFALLAEISVQLYVSPEMADPKTGMPVSQVKLAGNRQQQQRAPEYEAFNLVKTALQSLVWKGPPAWSPLIANWSLELVAKLSDKYTQRRMTITASCNYWLECSAMHGLMTLINSCFRKLTQPEEEACVEIMLNAFHRFPMTFDWIVARLGGCFPYKIIMQILQCGIKRFVDDYRCHLDSEAGILDYMTSCHEQHLRAAFREMLREGFAPKKPLDVAVVPFLLITTNYSDTILQSLVNVLVEIYTEDMCEVIVQKAPLWLSNKMFAGMQPTLNNAVLRLNERGATLLLTAAKMAEKYVWCQDFLDNSMQELEQWVLNQRNFPLLADLAYEETKYMLWKSCLSTNLFEQQTAVRLLLVVSSQHPNIYYQTISQLLKKSYAQNPNGIGALIRLLGGQSGMVNFPGFTPGFKMVLEDITLDVQVNNRLPVPPGTPTEAFNTFSNLNILARMHKSKNVAPYIKAQHLNQALNECLPKILQIFDCTVNKLVLRIDRDAAERIADKFRAQQSKNSNNNNELCNGKDYGKRTKLEPGEDKVDDEDATRMRLAHLIVDLLNNIEAGSRTTVLRTPLVLKLATLSVKYFFVGLTEKTVIRRAAASHRSYTLLQRQCSARKIARTVCLRELVERALFYHGHLLGQLEVYQLDELEIPEHEHLILQNLHTSSGANSNRSVLHSGIIGRGLRPVLPPSERNCDAEKQALYLKALNACCADLEKPNNVEGYSLVSLLLVELVSTDVMYNGLPFPDEEFTRVTMERDMLIRRAFINSPVLWAVLGLIAGHRPALCYSSVLLRALCATCLHHWRGKNVNRFQPTAANDELMLCTKKMLQLLAMSQLIPPPLTNLHLIIEHFESAEIALLLRECIWNYLKDHVPSPALFHVDNNGLHWRNTNTQLAKVPPQYVDPLRHLMQRKLSTLGPHYHQMFIMGELMEGDSEPDPTARLQIVEID", "text": "FUNCTION: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein Nucleus Cytoplasm. SIMILARITY: Belongs to the Integrator subunit 5 family."}
{"protein": "MENNEEFQDELLALESIYPSCLLPISEQSFTYTLSIPDSSVRLNIQFPLDYPNSAPTVLDAYGIDKTLAEDVLLSVATGDVCIFSYMDLLKELVDIDAEQAAAERESKLQEESDKETPVMLNKSHYVAKTPEIQDEPWKPKFDWKESEPITDRKSTFMAHATRVYSTEEVREALEDLYMDKKVAKANHNMVAYRIISPNGNVIQDNDDDGESAAGSRMSHLLTMMSAENVFVCVSRWFGGVHIGPDRFKHINSSAREAVLLTDAAPSQKKGTEHGKKKKK", "text": "FUNCTION: Translational regulator that ensures constant high levels of translation under amino acid starvation. Plays a role as a negative regulator of the gcn2 kinase activity; impairs gcn1-mediated gcn2 activation, and hence gcn2-mediated eIF-2-alpha phosphorylation in amino acid-starved cells and subsequent down-regulation of protein synthesis. In normal conditions, it resides in a actin complex and has no activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the IMPACT family."}
{"protein": "MQPPPRKVKVTQELKNIQVEQMTKLQAKHQAECDLLEDMRTFSQKKAAIEREYAQGMQKLASQYLKRDWPGVKADDRNDYRSMYPVWKSFLEGTMQVAQSRMNICENYKNFISEPARTVRSLKEQQLKRCVDQLTKIQTELQETVKDLAKGKKKYFETEQMAHAVREKADIEAKSKLSLFQSRISLQKASVKLKARRSECNSKATHARNDYLLTLAAANAHQDRYYQTDLVNIMKALDGNVYDHLKDYLIAFSRTELETCQAVQNTFQFLLENSSKVVRDYNLQLFLQENAVFHKPQPFQFQPCDSDTSRQLESETGTTEEHSLNKEARKWATRVAREHKNIVHQQRVLNDLECHGAAVSEQSRAELEQKIDEARENIRKAEIIKLKAEARLDLLKQIGVSVDTWLKSAMNQVMEELENERWARPPAVTSNGTLHSLNADTEREEGEEFEDNMDVFDDSSSSPSGTLRNYPLTCKVVYSYKASQPDELTIEEHEVLEVIEDGDMEDWVKARNKVGQVGYVPEKYLQFPTSNSLLSMLQSLAALDSRSHTSSNSTEAELVSGSLNGDASVCFVKALYDYEGQTDDELSFPEGAIIRILNKENQDDDGFWEGEFNGRIGVFPSVLVEELSASENGDTPWMREIQISPSPKPHASLPPLPLYDQPPSSPYPSPDKRSSLYFPRSPSANEKSLHAESPGFSQASRHTPETSYGKLRPVRAAPPPPTQNHRRPAEKIEDVEITLV", "text": "FUNCTION: Adapter protein that plays a role in endocytosis via clathrin-coated pits. Contributes to the internalization of cell surface receptors, such as integrin ITGB1 and transferrin receptor (PubMed:29887380). Promotes endocytosis of EGFR in cancer cells, and thereby contributes to the down-regulation of EGFR signaling (PubMed:30249660). Recruited to clathrin-coated pits during a mid-to- late stage of assembly, where it is required for normal progress from U-shaped intermediate stage pits to terminal, omega-shaped pits (PubMed:29887380). Binds to membranes enriched in phosphatidylinositol 3,4-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate (PubMed:29887380). When bound to membranes, promotes actin polymerization via its interaction with WAS and/or WASL which leads to the activation of the Arp2/3 complex. Does not promote actin polymerisation in the absence of membranes (PubMed:29887380). SUBCELLULAR LOCATION: Cytoplasm Cell junction Membrane, clathrin-coated pit Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, stereocilium Note=Partially localized at clathrin-coated pits at the cell membrane (PubMed:30249660). Detected at the cell membrane at sites around clathrin-coated pits, very close to the clathrin-coated pits but not an intrinsic part of the clathrin-coated pits (PubMed:29887380). Colocalizes at cell-cell contacts with CDH1, but is not detected at tight junctions (PubMed:14627983)."}
{"protein": "MQKYHFTGLDCPDCANKLESALNKQSYVQEARVVFNTNTLYLKTQDMPKALALIKQLEPDMELSEQVQSEAKPSAIPLLLSVVLYLIAVATIHFSAQNWALHLSYALLAGVYLVAGKDVFLGALRAIRNKQFFDENTLMLSATIAAFGVGAHEEAVSIMVFYSAGEFLQQLAIARSKQSLHALLDVAPNHAVRKVGQELQEVEPSALAIGDVVIVKVGEKIPTDGVVLRGESLLDQKALTGESLPVNVKEHSAVLGGSINLKGVLEIQVSKLYADSSVAKIVDLVSNAVSQKSQTEKFITTFARYYTPAVFAIALLIALVPPLLGHGDFDTWIYRGLFALMVSCPCALVISVPLGYFGGVGAASRAGILIKSVQTLEALSQVKNIAFDKTGTLSKGEFNVIDVVPIAPFSKEDVLQHATCAQILSTHPIAISIQKAYKRQCQHEVKDYQEIGGLGVQASCHSHLIIAGNDKMLHKYNIPHDTCSLEGTIVHVAVDGKHIGYIVVADTLKDNAKECLDGLKHAGIEHMCILSGDHEYSTKRVAKELDCPYYANLLPEDKLNAFKDFQAQHAHKSMFVGDGINDAPTLARADVSMSMGSASQISKESADIVITNNSLESVLKVFKIAKKTKRIIIENIIFALAIKAMFIVLGLSGDASLWEAVLGDVGVTLIALANSMRTMRI", "text": "FUNCTION: Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily."}
{"protein": "MVLEGNPDVGSPRTSDLQHPGSQGSCILSCPGEEALAGEEPIKYGELIVLGYNGCLASGDKGRRRSRLALSRRPHANGVKPDVMHHISTPLVSKALSNRGQHSISFTLSRSHSVIVEYTHDSDKDMFQIGRSTENMIDFVVTDTSPGGGATEGPSAQSTISRYACRILCDRRPPYTARIYAAGFDASSNIFLGERAAKWRTPDGLMDGLTTNGVLVMHPAGGFSEDSAPGVWREISVCGNVYTLRDSRSAQQRGKLVENESNVLQDGSLIDLCGATLLWRTPAGLLRAPTLKQLEAQRQEANAARPQCPVGLSTLAFPSPARGRTAPDKQQPWVYVRCGHVHGYHGWGCRRERGPQERECPLCRLVGPYVPLWLGQEAGLCLDPGPPSHAFAPCGHVCSEKTARYWAQTPLPHGTHAFHAACPFCGAWLTGELGCVRLIFQGPLD", "text": "FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:23892723). Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6 (By similarity). Mediates 'Lys-63'- linked polyubiquitination of IRAK1. Can activate AP1/JUN and ELK1 (By similarity). Acts as a regulator of innate immunity by mediating 'Lys- 63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (PubMed:23892723). Catalyzes 'Lys-63'-linked polyubiquitination of RIPK2 in parallel of XIAP (PubMed:23892723). SIMILARITY: Belongs to the pellino family."}
{"protein": "MTRKKTNPFVAHHLLAKIEKVNMKEEKETIVTWSRASSILPAMVGHTIAIHNGKEHIPIYITNPMVGRKLGEFVPTRHFTSYESARKDTKSRR", "text": "FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS19 family. SIMILARITY: Belongs to the universal ribosomal protein uS19 family."}
{"protein": "MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQEAAQSKVTATQDSTNLRCIFCGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERMERERLERERLERERLERERLEQEQLERQRQEREHVERLERERLERLERERQERERERLEQLEREQVEWERERRMSNAAPSSDSSLSSAPLPEYSSCQPPSAPPPSYAKVISAPVSDATPDYAVVTALPPTSTPPTPPLRHAATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPVNTPSSQPPAAKSCAWPTSNFSPLPPSPPIMISSPPGKATGPRPVLPVCVSSPVPQMPPSPTAPNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPLPPPPLPPLASLSHCGSQASPPPGTPLASTPSSKPSVLPSPSAGAPASAETPLNPELGDSSASEPGLQAASQPAESPTPQGLVLGPPAPPPPPPLPSGPAYASALPPPPGPPPPPPLPSTGPPPPPPPPPPLPNQAPPPPPPPPAPPLPASGIFSGSTSEDNRPLTGLAAAIAGAKLRKVSRVEDGSFPGGGNTGSVSLASSKADAGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDRNEDAEPITAKAPSTSTPEPTRKPWERTNTMNGSKSPVISRPKSTPSSQPSANGVQTEGLDYDRLKQDILDEMRKELAKLKEELIDAIRQELSKSNTA", "text": "FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell projection, filopodium Synapse Cell junction, focal adhesion Note=Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses (By similarity). SIMILARITY: Belongs to the Ena/VASP family."}
{"protein": "MSVSHSSRLNKGVREQYMKLPQGEKVQVTYVWIDGTGEGVRCKTRTLDQEPKTIDEIPEWNFDGSSTHQAEGSNSDMYLIPVQMFRDPFCLDPNKLVMCEVLKYNRKSAETNLRHTCKKIMEMVNDHRPWFGMEQEYTLLGINGHPYGWPENGFPGPQGPYYCGVGADKVYGRDVVESHYKACLYAGIKICGTNAEVMPSQWEFQVGPCEGIDMGDHLWMARFILHRVCEDFGVVATLDPKPMTGNWNGAGCHTNYSTESMRVEGGLKHIEDAIEKLGKRHDYHICVYDPRGGKDNSRRLTGQHETSSIHEFSAGVANRGASIRIPRQVGQEGYGYFEDRRPAANCDPYAVTEALVRTTILNETGSETKDYKNGAGFSRAIGMASPRDAAVF", "text": "FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. SUBCELLULAR LOCATION: Cytoplasm, cytosol Microsome Mitochondrion. SIMILARITY: Belongs to the glutamine synthetase family."}
{"protein": "MAALVRPARFVVRPLLQVVQAWDLDARRWVRALRRSPVKVVFPSGEVVEQKRAPGKQPRKAPSEASAQEQREKQPLEESASRAPSTWEESGLRYDKAYPGDRRLSSVMTIVKSRPFREKQGKILLEGRRLISDALKAGAVPKMFFFSRLEYLKELPVDKLKGVSLIKVKFEDIKDWSDLVTPQGIMGIFAKPDHVKMTYPKTQLQHSLPLLLICDNLRDPGNLGTILRSAAGAGCSKVLLTKGCVDAWEPKVLRAGMGAHFRMPIINNLEWETVPNYLPPDTRVYVADNCGLYAQAEMSNKASDHGWVCDQRVMKFHKYEEEEDVETGASQDWLPHVEVQSYDSDWTEAPAAVVIGGETYGVSLESLQLAESTGGKRLLIPVVPGVDSLNSAMAASILLFEGKRQLRGRAEDLSRDRSYH", "text": "FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase domain of the mtLSU rRNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family."}
{"protein": "MSGGTAATTAGSKVTFKITLTSDPKLPFKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGVGVNPAQPAGNIFLKHGSELRLIPRDRVGH", "text": "FUNCTION: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine- linked polymer (By similarity). The so-called ufmylation requires the ufm-1-activating E1 enzyme uba-5, the ufm-1-conjugating E2 enzyme ufc- 1, and probably the ufm-1-ligase E3 enzyme ufl-1 (PubMed:23449979). SIMILARITY: Belongs to the UFM1 family."}
{"protein": "MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEPADLTGVTVQSPGEAQCLLGPAEAEGSQRRRLLVPANGADPTETLMLFFDKFANIVPFDSWDQLMRQLDLTKNEIDVVRAGTAGPGDALYAMLMKWVNKTGRNASIHTLLDALERMEERHAREKIQDLLVDSGKFIYLEDGTGSAVSLE", "text": "FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:26457518). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (PubMed:19090789). Promotes the activation of NF- kappa-B (PubMed:9430227). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane raft Cytoplasm, cytosol Note=Palmitoylation is required for association with membranes."}
{"protein": "MSFDAEKQLAIAAVRRASYLTEKVFNQLIKEKSAAGALTKDDKSPVTIGDFGAQAIVISMLKDAFPNDPIVGEEDSDFLRENTQTCSRVWELVQETIQHATEYKELGQIKSAEEMMSIIDQGSYHGGRNGRMWTLDPIDGTKGFLRGAQYAICLALIENGKPVVSAIGCPNLPYDFNQPETSPKGIIMSAVRNHGCFQYSLHNEKLEPVQVHMQDVQNTKDSKFCEGVEAGHSMQGTQEEIAKYLGITRGPTKMDSQAKYASLARGDGDIYLRLPTKMTFEEKIWDHAGGSLLVEEAGGVVSDMFGKPLDFGVGRTLKNNNGVIAAYKGIFEKVIEATAAVTSKDPHFQKVAQ", "text": "FUNCTION: Confers resistance to lithium. FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur- activation pathway by converting PAPS to APS. SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
{"protein": "MPIGVPRVRFQYRRDRSRVWIDIYNRLYRERCLFLAHVVESQIANQLVGLFIYLGVQDETKDIFLFINSPGGGIISGFAIYDTMQFVRPDIQTICVGLAASMGSFLLVGGAITKRLAFPHARVMIHQPMSAFFETQTVEAILEAEELLKLRESLAKVYVQRTGKPDWVIAEDMERDVFLSATEAQSYGIVDVVGVALASKG", "text": "FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the peptidase S14 family."}
{"protein": "MKKLLISFIAILFFICGFNLKAFAAEEIIDYQSLYNQAIQEGVLDQNSVSYNEWLKQNKEEFMPIYQDGLKQGVFLEPLSYNEWLKLNNYGQAPTGDIELFDDVTPRGSWGGFTLKAGDIFITNATSSAGIVGHAAIANGDNYILHMPGAGQGNQQLSTSNWMQKYTASGKWIKVYRLKDQTLARDVARYADRNFYSTTGSATKNVYLDYGIDTHLYQKNPTYCSKLVFQALYFGSGSRNVMQAVSGIVTPYGLIDTFTSAYRPSLVKTY", "text": "FUNCTION: Possibly involved in pGI2 replication mechanism."}
{"protein": "MPCLFIFIALLLSSCIGTLKALDQTCGNKVVNTIVVDQAGSGEGQRVTTITYNGHAATDVSSTFTSYPSHIVVRNLSIMNTYNRLTSLTKANGMSWDIKPAVAISVYGDKSAFYNCDFLGLQDTVWDNLGRHHFKNCYIEGAIDFIFGSGQSVYEDCHINATAGALASKVSFGYITAQGRSSDSDPSGFVFLRGSVSGSTSVYLGRAYGPFSRVIFIQTDLSSVVHPEGWYSWHYGGYEMSFTYAEVECKGAGSDMSRRVPWIDKLHSFYTKQQFSISNFIDQDQWISNIPRF", "text": "FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the pectinesterase family."}
{"protein": "MEKYEPVREIGAGNFGVAKLMRNKETRELVAMKFIERGNRIDENVFREIVNHRSLRHPNIIRFKEVVVTGRHLAIVMEYAAGGELFERICEAGRFHEDEARYFFQQLVCGVSYCHAMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSLLHSRPKSTVGTPAYIAPEVLSRREYDGKLADVWSCGVTLYVMLVGAYPFEDPKDPKNFRKTISRIMSVQYKIPEYVHVSQPCRHLLSRIFVANPYKRISMGEIKSHPWFLKNLPRELKEEAQAVYYNRRGADHAASSASSAAAAAAFSPQSVEDIMRIVQEAQTVPKPDKPVSGYGWGTDDDDDDQQPAEEEDEEDDYDRTVREVHASVDLDMSNLQIS", "text": "FUNCTION: May play a role in signal transduction of hyperosmotic response. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MSALGESNNKQNGKEILHNYVTKKLTSQPYSCQWIPTSCSVVTVGKKTSGGISKGDIKIHQLEFDDTSGDPKLNLVYENEFTNPFRCLSFFKQANQLQQQDNRKFITGDFNGQISEWDSDICDIPIWGVKGAHQGSISAIDAYADNLVVCGGKDGTIKVYDTRIKPNSANDNNGNNSSPISTFEQTNKSNCWSICTNDNNIIAGFENGDLNIYNLKTNSIQSTTKLNGGICSIDSNDRSNILNQFLITTNKSFISIASFNNNNNNNIEFKDYDINKEPNQTIWSGIYSPWNKKDNENIFTIAQGDGSVSMYRDDCKLIDKVLVSDLPILSLDYSKDRKGLLCCISLKKQLSILISPC", "text": "FUNCTION: Key assembly factor specifically required for the stability of axonemal dynein heavy chains in cytoplasm. SUBCELLULAR LOCATION: Dynein axonemal particle."}
{"protein": "MPKLILASTSPWRRALLEKLQISFECAAPEVDETPRSDESPRQLVLRLAQEKAQSLASCYPDHLIIGSDQVCVLDGEITGKPLTEENARLQLRKASGNIVTFYTGLALFNSANGHLQTEVEPFDVHFRHLSEAEIDNYVRKEHPLHCAGSFKSEGFGITLFERLEGRDPNTLVGLPLIALCQMLRREGKNPLMG", "text": "FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Maf family. YceF subfamily."}
{"protein": "MTEAVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGDIVGMIVAEIKNRTKIHKEDGDILASSFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAISFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALANLSPCSIPHRIYRQAQSLLCSFLPWSSISTKGGIEYSRTM", "text": "FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N- terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Note=Probably forms a intramembrane hairpin-like structure in the membrane. SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily."}
{"protein": "MDPIELRSVNIEPYEDSCSVDSIQSCYTGMGNSEKGAMDSQFANEDAESQKFLTNGFLGKKTLTDYADEHHPGTTSFGMSSFNLSNAIMGSGILGLSYAMANTGIVLFVIMLLTVAILSLYSVHLLLKTAKEGGSLIYEKLGEKAFGWPGKIGAFISITMQNIGAMSSYLFIIKYELPEVIRVFMGLEENTGEWYLNGNYLVLFVSVGIILPLSLLKNLGYLGYTSGFSLTCMVFFVSVVIYKKFQIPCPLPVLDHNNGNLTFNNTLPMHVIMLPNNSESTGMNFMVDYTHRDPEGLDEKPAAGPLHGSGVEYEAHSGDKCQPKYFVFNSRTAYAIPILAFAFVCHPEVLPIYSELKDRSRRKMQTVSNISITGMLVMYLLAALFGYLSFYGEVEDELLHAYSKVYTFDTALLMVRLAVLVAVTLTVPIVLFPIRTSVITLLFPRRPFSWVKHFGIAAIIIALNNVLVILVPTIKYIFGFIGASSATMLIFILPAAFYLKLVKKEPLRSPQKIGALVFLVTGIIFMMGSMALIIIDWIYNPPNPDHH", "text": "FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane (PubMed:11118514). The transport is electrogenic, pH dependent and partially tolerates substitution of Na(+) by Li(+) (PubMed:11118514). Preferentially transports smaller amino acids, such as glycine, L-alanine, L-serine, L-asparagine and L-threonine, followed by L-cysteine, L-histidine, L-proline and L-glutamine and L-methionine (PubMed:11118514). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, microvillus membrane; Multi- pass membrane protein Note=Microvillus membrane localization in placenta. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
{"protein": "METQRASLCLGRWSLWLLLLALVVPSASAQALSYREAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDPGTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVKQCVGTVTLDQIKDPLDITCNEVQGVRGGRLCYCRGWICFCVGRG", "text": "FUNCTION: Microbicidal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cathelicidin family."}
{"protein": "MTYSTVNINTPPPYLALASNEKLPTVLSIAGTDPSGGAGVEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVSQILDANLQDMKCDVIKTGMLTTAAIEVLHEKLLQLGENRPKLVVDPVLVATSGSSLAGKDIASLITEKIAPFADILTPNIPECFKLLGEDREISKLRDIFEVAKDLAKITKCSNILVKGGHIPWNDEEGKYITDVLYLGAEQRFITFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYGGIEYVQNAVAIGCDVTKETVKDNGPINHVYAIEIPLEKMLSDECFTASDAVHKKPVKSSLNKIPGGSFYKYLINHPKVKPHWDSYVNHDFVRKVADGSLEPKKFQFFIEQDYLYLVNYARISCIAGSKSPCLEDLEKELVIVECVRNGLCQHERRLREEFGIKDPDYLQKIQRGPALRAYCRYFNDVSRRGNWQELVIALNPCLMGYVHALTKIKDEVTAAEGSVYREWCETYSSSWCHEAMLEGEKLLNHILETYPPEKLDTLVTIYAEVCELEANFWTAALEYE", "text": "FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P. SIMILARITY: In the C-terminal section; belongs to the thiaminase-2 family. SIMILARITY: In the N-terminal section; belongs to the ThiD family."}
{"protein": "MSNTPFLSEVSKRRTFAIISHPDAGKTTITEKVLLFGNAIQKAGTVKGRGNAQHAKSDWMEMEKERGISVTTSVMQFPYNDCLVNLLDTPGHEDFSEDTYRTLTAVDSCLMVIDAAKGVEDRTRKLMEVTRLRDTPIVTFMNKLDRDVRDPMEVLDEVENELGMMCAPITWPIGCGKEFKGVYHIHRDETILYESGHGHEIQEVRIIKGLDNPELDEKVGESLAASVREELELVMGACPEFDKELFLTGELTPVYFGTALGNFGVDHMLDGLTEWAPAPKTRQAVERDVEATEDKFSGFVFKIQANMDPKHRDRIAFMRIVSGTYTQGMKMNHVRLGKQVSISDAVTFMAGDRSRAEHAYAGDIIGLHNHGTIQIGDTFTQGESLKFSGIPNFAPELFRRIRLKDPLKQKQLLKGLVQLSEEGAVQVFRPLQNNDLIVGAVGVLQFDVVVARLKSEYNVEAIYEGVNVATARWVECGDAKKLDEFQRKNQANLALDGGDNLTYIAPTMVNLNLAKERFPDVEFRATREH", "text": "FUNCTION: Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily."}
{"protein": "MSQLITSPKINEKETLKFECETGNYHTFCPISCVSWLYQKIEDSFFLVIGTKTCGYFLQNALGVMIFAEPRYAMAELEEADISAQLNDYKELKRLCLQIKRDRNPSVIVWIGTCTTEIIKMDLEGMAPRLETEIGIPIVVARANGLDYAFTQGEDTVLAAMACRCPDKISTTSDSKNLETPMMIDNTQKNGQNSKALAHPPLVLFGSLPSAVVNVLTLELNKQGITVDGWLPSSRYTDLPALGEDVYVCGVNPFLSRTAMTLMRRKKCKLINAPFPIGPDGTRAWIEKICNVLGVIPTGLEEREKKIWQSLENYLPLVRGKSVFFMGDNLLEISLARFLTRCGMIVYECGVPYLDKRYQASELLLLEQTCLEKNVPMPRIVEKPDNYYQIQRIRELQPDLVITGMALSNPLEARGINTKWSVEFTFAQIHGFANSKDVLELVTRPLRRNMMQQVSNKTLVKPAK", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the BchN/ChlN family."}
{"protein": "MMAKLMITVMTVFFLSLQQGADGLFERWRKNQMAASRIMGNLITARLDPPGYCTHKICYEDGECNQWCTAGCNPDTGKCDTT", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Pg turripeptide superfamily."}
{"protein": "MGPRSSNRRSNAKDGFKGSNKASKFPLPLAMWDFGHCNPNACSGKRLERLGCVRNLRIGQKFRGVVITPNGKVPVSPADKEYFDNGGASVVECSWARIEEIPFSRIGGRCERLLPYLVASNPVNYGRPWRLNCAEALAACMYIVGYPNEARLLMDNFKWGHSFFEVNEELLDIYAQCHDAQDIQEKEKKYLEEMEASYQEQRNQTTDDIWSAGNLNHKPTLNTSSTHSNSEESRSPLHEPSEASLAHDEHSIPTDDNEETLTNLQANDVDEDEVWRKIVRMKVHSTDT", "text": "FUNCTION: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Required for processing 35S pre-rRNA at site D. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TDD superfamily. TSR3 family."}
{"protein": "DRDSCIDKSRCSKYGYYQECQDCCKKAGHNRGTCMFFKCKCA", "text": "FUNCTION: Blocks human voltage-gated potassium channel Kv11.1/KCNH2/ERG1 (IC(50)=16.9 nM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily."}
{"protein": "MDLRRAERNLKILGDANSDEDMPVAHSVEETQGQALFSESDEADAEEDAAESPQSGVGGRTTTAESGGEEHREQVFLSTQVQGRIDEFEATEGARRQFRQLVTGFTYAQEDGEANAGGRTAKRVPKVRRTRRNNTKVRSLTEFNTENFERLRKEDRARSLLTMLSGKTQKVNNLLRGLQQERSRERAFHGCSVYNEGEWREIVRLLHERLPKATRSDVACIKSYVYGDGLDETPWCASHARPPDCPAQSQERQGTCGPGDDELRIFTLSQLLEDQSASEDVIPDSMDAGDAVSLGSPQPQAGLSQHSFCPDSTATSPLRPPATPLTRAPASPLPVRVYTAPASPLDYIPDSEDDPYVLQGPSQARSPPSLLEVRRTLKNIGVRPGRSAAAVRKAAAAVARIEAASDAASLGTASDADRRSALFLRMTALVRRSPRLLAHIYCLRPVALDDLRAVLEADDDFIALLDDSLIRQWADFTGICVKNDTSDSQRPPQPLESQ", "text": "FUNCTION: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX4 family."}
{"protein": "MEIGTEISRKIRSAIKGKLQELGAYVDEELPDYIMVMVANKKSQDQMTEDLSLFLGNNTIRFTVWLHGVLDKLRSVTTDPASLKSSDTNLFDGNVPSNKSSFSRGDERRHEAAVPPLAVSSTRPEKRESRVSTSSQEQKATNVRQTYDDGAATRLMSTVKPLRELAPSEDVIDIKPEPDDLIDEDLNFVQENPLSQKKTTVTLTYGSSRPSIEIYRPPATRNTDSGAHLNRLQFQQQQNSIHAAKQLDIQSSRVYETGRLCEPEVLNSLEETYSPFFRSNAEKMSIEEENFRKRKLPVVSSVVKVKKFSHDGEEEEEDDDCGSRTGSISSSVSVPAKPERRPSLPPSKQANKNLILKAISEAQESVTKTTNYSTVSQKQTLPVAPRTRTSQEDLLAEVAQGHGRVPRISSPVKEEEAQGGSVDERQGTQQRQLLSRLQIDPVMAETLQISQDYYDMESMVHADTRSFILKKPKLCEELVVAASQASGMETADALQARSGHLVQTRDLVQPDKPASPKFIVTLDGVPSPPGYMSDQEEDMCSEGMRPAQHPAASHGGLAGLLHPQRSRVLSRQLEDPDGSFANAEMSELSVAQKPEKLLERCKYWPACKNGDECAYHHPVSPCKAFPNCKFAEKCLFVHPNCKYDAKCTKPDCPFTHMSRRTPGLPPKPVTAPAPPSSSQLCRYFPACKKMECPFYHPKHCRFNTQCTRPDCAFYHPTITVPPRHALKWIRPQTSD", "text": "FUNCTION: Involved in poly(A) tail length control in neuronal cells. Binds the polyadenosine RNA oligonucleotides. SUBCELLULAR LOCATION: Nucleus speckle Note=Colocalizes with poly(A) RNA in nuclear speckles. SIMILARITY: Belongs to the ZC3H14 family."}
{"protein": "MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE", "text": "FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:6504138, PubMed:2207090, PubMed:7704569). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:6504138, PubMed:2207090, PubMed:7704569). FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the tubulin family."}
{"protein": "MSDVTVAETPAVKTPTKAPKAPKSKTTKEPKAKVAAAHPPFINMVTAAISSLKERKGSSKIAILKYITANYKVGDQLTKINSRLRAALNKGVASKALVQSVGNGASGRFRVAEKAAATKKPVAKKPVAKKAATGEKKAKKTTVAKKTGDKVKKAKSPKKIAKPAAKKVAKSPAKKAAPKKAPAKKAAAPKA", "text": "FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H1/H5 family."}
{"protein": "MNSLIPPPTSEQQMNMFRLRDKMSLLNAEFLKVINGYFTEKNHYDFSGTMKSYMDHVAQLKQIYKVDDDVAADMTVPRRTENSSESSGETVAPRKIAKAVRKNGTPKNPLNSTVFAASSPAATVASVPKFGDISVITKETPAPLAKTAEPLVAPAAPATARKRAIRGGGPLGGAESVVFKSGEDGQAATSSVKIPATTIKFPEPTKDFWTKKSDAPAAPSNSGSLFAFLGKDGDKPKETPKFSGFSFGKKPAEPSEEPKAADSTPKLTFGSPKEADLPKPASSLFGASPSKPLVFGGSSADSTTSAPKPFSALSTAASLFGSSSASTTTTATQPLSFGSSSTGGSSLFSGFAGLAQKAMENQNQAKPEGSGEDDEGEYVPPKVETVENQEPDAVLSSKVSVFKFTGKEYTKLGVGMLHIKDNDGKFSVLIRAATATGTVWLNSLCNKAMKATVVDAKGDRIRLTCPSSSTEMATMMIRFGTADGAKKFTDKILEVAV", "text": "FUNCTION: Component of the nuclear pore complex (PubMed:24011592). Plays a direct role in nuclear protein import (By similarity). Required for anoxia-induced prophase arrest; may function in concert with cdk-1 to arrest prophase blastomeres in response to anoxia (PubMed:20053678). SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side."}
{"protein": "MQKDASLSGFLPSFQHFATQAIHVGQEPEQWNSRAVVLPISLATTFKQDFPGQSSGFEYSRSGNPTRNCLEKAVAALDGAKHSLAFASGLAATITITHLLKAGDEIICMDEVYGGTNRYFRRVASEFGLKISFVDCSKTKLLEAAITPQTKLVWIETPTNPTLKLADIGACAQIVHKRGDIILVVDNTFMSAYFQRPLALGADICMCSATKYMNGHSDVVMGLVSVNSDDLNSRLRFLQNSLGAVPSPFDCYLCCRGLKTLQVRMEKHFKNGMAVARFLETNPRVEKVVYPGLPSHPQHELAKRQCSGCPGMVSFYIKGALQHAKAFLKNLKLFTLAESLGGYESLAELPAIMTHASVPEKDRATLGINDTLIRLSVGLEDEQDLLEDLDRALKAAHP", "text": "FUNCTION: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate. Part of the L-cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione. Besides its role in the conversion of L-cystathionine into L-cysteine, it utilizes L-cysteine and L- homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce hydrogen sulfide (H2S). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, and two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia. Lanthionine and homolanthionine are structural homologs of L,L-cystathionine that differ by the absence or presence of an extra methylene group, respectively (By similarity). Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function (PubMed:19903941, PubMed:22244329). By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (PubMed:18948540) (By similarity). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (PubMed:33826201). Can also accept homoserine as substrate (By similarity). Catalyzes the elimination of selenocystathionine (which can be derived from the diet) to yield selenocysteine, ammonia and 2-oxobutanoate (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
{"protein": "MSDLLPLATYSLNVEPYTPVPAIDVTMPITVRITMAALNPEAIDEENKPSTLRIIKRNPDFEDDDFLGGDFDEDEIDEESSEEEEEEKTQKKKKSKGKKAESESEDDEEDDDEDDEFQESVLLTLSPEAQYQQSLDLTITPEEEVQFIVTGSYAISLSGNYVKHPFDTPMGVEGEDEDEDADIYDSEDYDLTPDEDEIIGDDMDDLDDEEEEEVRIEEVQEEDEEDNDGEEEQEEEEEEEQKEEVKPEPKKSKKEKKRKHEEKEEEKKAKKVKKVEFKKDLEEGPTKPKSKKEQDKHKPKSKVLEGGIVIEDRTIGDGPQAKRGARVGMRYIGKLKNGKVFDKNTSGKPFAFKLGRGEVIKGWDIGVAGMSVGGERRIIIPAPYAYGKQALPGIPANSELTFDVKLVSMKN", "text": "FUNCTION: Proline isomerase that belongs to an abundant class of enzymes that catalyze the cis-trans isomerization of X-Pro peptide bonds and can accelerate the refolding of proline-containing polypeptides (PubMed:7925954, PubMed:8051210, PubMed:7525596). Specifically binds nuclear localization sequences (PubMed:7925954). May be involved in the assembly or folding of ribosomal proteins (PubMed:8051210). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily."}
{"protein": "MVKKKVATKKNSPSLAIAKKKSRSNKDVVSVEAPIISSYNDRIRPLLDTVDRLRNLNVMREGIHLPTIVVVGDQSSGKSSVLESLAGISLPRGQGICTRVPLVMRLQRSSSPEPEIWLEYNDKVVPTDEEHIAEAIRAATDVIAGSGKGVSDAPLTLHVKKAGVPDLTMVDLPGITRVPVNGQPENIYEQISGMIMEYIEPQESIILNVLSATVDFTTCESIRMSRKVDKTGQRTLAVVTKADMAPEGLLQKVTADDVSIVLGYVCVRNRIGEETYEEARMQEELLFRTHPVLSLIDEDIVGIPVLAQKLMLIQSSMIARCLPKIVSKINQKLDTAVLELNKLPMVMASTGEALMALMDIIGSAKESLLRILVQGDFSEYPDDQNMHCTARLADMLSQFSDSLQAKPKEVAEFLMDEIKILDECKCVGLPNFIPRSAFLAILSQHVDGIQDKPVEFINKIWDYIEDVLSSVTAKRSDNFPQIQSSIKRAGRNLISKIKEQSVNRVMEIVEMEKLTDYTCNPEYMTSWTQKTSAQESFIDAVVKNENIPDYFSVTGFGNVKISHLRKYHAHLLIPAFDMKMRITSYWKIVLRRIVDNLALYLQLSVKSLVNTRFQKEIVAEMVDPRDGGGVEKMLEESPLVASKREKLQNSIKLLKESKDAVAAIVDQNC", "text": "FUNCTION: Putative microtubule-associated force-producing protein, able to bind and hydrolyze GTP. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Note=Microtubule-associated. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MAKHPFEQFNLESSLIDAVKDLNFEKPTEIQNRIIPRILKRTNLIGQSQTGTGKSHAFLLPLMQLIDSEIKEPQAIVVAPTRELAQQLYDAANHLSQFKAGVSVKVFIGGTDIEKDRQRCNAQPQLIIGTPTRINDLAKTGHLHVHLASYLVIDEADLMIDLGLIEDVDYIAARLEDNANIAVFSATIPQQLQPFLNKYLSHPEYVAVDSKKQNKKNIEFYLIPTKGAAKVEKTLNLIDILNPYLCIIFCNSRDNANDLARSLNEAGIKVGMIHGGLTPRERKQQMKRIRNLEFQYVIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYSPDEEHNISLIEDRGFVFNTVDIKDGELKEVKAHNQRQARMRKDDHLTNQVKNKVRSKIKNKVKPGYKKKFKQEVEKMKRQERKQFSKQQNRQKRKQNKKG", "text": "FUNCTION: Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. CshB subfamily."}
{"protein": "MNFNKIFVFVALILAISLGNTEAGWLRKLGKKIERIGQHTRDASIQVLGIAQQAANVAATARG", "text": "FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cecropin family."}
{"protein": "MYSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLSEKPEVKQKWASRLLAKLRKDIRPEYREDFVLTVTGKKPPCCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKSPQCSNPGLCVQPHHIGVSVKELDLYLAYFVHAADSSQSESPSQPSDADIKDQPENGHLGFQDSFVTSGVFSVTELVRVSQTPIAAGTGPNFSLSDLESSSYYSMSPGAMRRSLPSTSSTSSTKRLKSVEDEMDSPGEEPFYTGQGRSPGSGSQSSGWHEVEPGMPSPTTLKKSEKSGFSSPSPSQTSSLGTAFTQHHRPVITGPRASPHATPSTLHFPTSPIIQQPGPYFSHPAIRYHPQETLKEFVQLVCPDAGQQAGQVGFLNPNGSSQGKVHNPFLPTPMLPPPPPPPMARPVPLPMPDTKPPTTSTEGGAASPTSPTYSTPSTSPANRFVSVGPRDPSFVNIPQQTQSWYLG", "text": "FUNCTION: Recognizes and binds the palindromic sequence 5'- TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CTF/NF-I family."}
{"protein": "MAKHAPIFPNVQGFLHGGDYNPDQWLAYPDVLEQDVQLMREAKWNVVSLGIFSWVSLEPEEGLFTFEWLDEAIERLTHAGVRILLATPSGARPAWLSAKYPEVLRVGPDGRRNRHGGRHNHCYTSPIYREKVRIINRKLAERYAHHPGVIGWHVSNEYGGECHCPLCQEAFREWLKRKYKTLDALNHAWWTPFWSHTYTDWSQIESPMPHGETSIHGLNLDWKRFVTDQTVDFCRHEIEPLKQVNPNLPVTTNFMGTYPGLNYWRFRDVLDVISWDSYPRWHAHETLVPEAVHTAMVHDLNRSILKKPFLLMESTPSVTNWQAVSKQKRPGVHVLVSLQAVAHGADSVQYFQWRKSRGSYEKFHGAVVDHVGHANTRVFRDVQAVGEMLERLAPMAGAEVKADAAVIFDWENRWALEDAKGPRNIGMHYEETVVNHYAALWRMGVPMDVIDEEQPLDGYKLVVAPMLYMVRPGVAERMKAFVERGGSLVLTYWSGIVDENDLVFLGGFPGPLRELAGVWAEEIDALYDGERVPVRVADGNPLGLAGHYEARELCEVVHLEGAEPIAVYGADYYEGMPAATVHRVGKGKVYYVAARLEDAFLRDFFARVAAEAGVARAIERELPDGVSAMVRSGDGVEYVMLMNFTPEAREVALDEAEYKPLYGEAPTDGAVRLPAYGVSVLERPARNG", "text": "FUNCTION: Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta- D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose, including lactose in milk. SIMILARITY: Belongs to the glycosyl hydrolase 42 family."}
{"protein": "MKPTLYTATGECVTPGRELGKGGEGAVYDINEFVDSVAKIYHTPPPALKQDKLAFMAATADAQLLNYVAWPQATLHGGRGGKVIGFMMPKVSGKEPIHMIYSPAHRRQSYPHCAWDFLLYVARNIASSFATVHEHGHVVGDVNQNSFMVGRDSKVVLIDSDSFQINANGTLHLCEVGVSHFTPPELQTLPSFVGFERTANHDNFGLALLIFHVLFGGRHPYSGVPLISDAGNALETDIAHFRYAYASDNQRRGLKPPPRSIPLSMLPGDVEAMFQQAFTESGVATARPTAKAWVAALDLLRQQLKKCTVSAMHVYPGHLTDCPWCALDNQGVIYFIDLGEEVITTSGDFVLAKVWAMVMASVAPPALQLPLPDHFQPTGRPLPLGLLRREYIILIEIALSALSLLLCGLQAEPRYIILVPVLAAIWIIGSLTSKVYKAEIQQRREAFNRAKMDYDHLVSQIQQLGGLEGFIAKRAMLEKMKDEILGLPEEEKRALAALHDTARERQKQKFLEGFFIDAASIPGVGPARKAALRSFGIETAADVTRRGVKQVKGFGDHLTQAVIDWKASCERRFVFRPNEAVTPAERQAVMAKMAAKRHRLESALTVGATELQRFRLHAPARTMPLMEPLRQAAEKLAQAQADLSRC", "text": "FUNCTION: Probable serine/threonine kinase."}
{"protein": "MIENILIIDNYDSFTYNLYQYVGEISPNIEVYRNDKITLEKIEEMNPTHIIISPGPGFPKDAGICIEAIRKFGRYIPILGVCLGHQAIGEA", "text": "FUNCTION: Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity)."}
{"protein": "MAKIKKKGTSGQAKNYITRTQAVRKLQISLPDFRRLCIFKGIYPREPRNKKKASKSATQSTTFYYTKDIQYLLHEPLLRKFREQKALAKKIARSLGRGEVSDAARLEKNHAPKLTLDHVIKERYPTFIDALRDLDDALSLLFLFANLPSTSHVPPKTIALCQRVTHEFQHYLITTNSLRKSFLSIKGIYYQATIQGQDIMWLVPYRFVQRVNGDVDYRIMATFVEFYTTLLGFVNYRLYSSIGLRYPPKFDTRLDENGAELAAFTLEGRTVGDAPKAIEPAKSSSDAANQEVSAEVQKKVDNVIKKAGLDQASSEQPTETAEEVTDAIDKFETTAPEADTLPQPDMSGDQAGSLFAPFTFYISREAPKTPLEFILRAFGCKRIGWDTVLGGGAFTHNEADPRITHQIVDRPSLPESSLPSIPAAATDGGAVQKVKPGTRVPGRTYVQPQWVWDCINEGKLLRPDLYAPGATLPPHLSPWVNPKKGGYDPRASLAEQEEDGEADIDAEEESDEEMEEAGEEKPAPTAANESEDSEDESVDGGMDVAETDDDDSESEEEEEEEDEFAGIDDEDAGSESEDEEETARTQHQKELEAEAAGLPFSSSGAGDDAAAKKKSQAKKRAAKKRQEEEELERQKMMMSRKKRKLLEKMMYSNKKTAEESAKLRSKRRKIEKGAAGK", "text": "FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the pescadillo family."}
{"protein": "MAFQQGVLSRCSGVFRHHVGHSRHINNILYRHAIAFASIAPRIPKSSFHTSAIRNNEAFKDPYDTLGLKKSATGAEIKKAYYKLAKKYHPDINKEPDAEKKFHDLQNAYEILSDETKRQQYDQFGPAAFGGGGAAGGAGGGSGSPFGSQFHDFSGFTSAGGSPFGGINFEDLFGAAFGGGGRGSGGASRSSSMFRQYRGDPIEIVHKVSFKDAVFGSKNVQLRFSALDPCSTCSGTGMKPNTHKVSCSTCHGTGTTVHIRGGFQMMSTCPTCNGEGTMKRPQDNCTKCHGEGVQVNRAKTITVDLPHGLQDGDVVRIPGQGSYPDIAVEADLKDSVKLSRGDILVRIRVDKDPNFSIKNKYDIWYDKEIPITTAALGGTVTIPTVEGQKIRIKVAPGTQYNQVISIPNMGVPKTSTIRGDMKVQYKIVVKKPQSLAEKCLWEALADVTNDDMAKKTMQPGTAAGTAINEEILKKQKQEEEKHAKKDDDNTLKRLENFITNTFRKIKGDKKN", "text": "FUNCTION: Plays a role in mitochondrial biogenesis and protein folding. SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MQAACWYVLFLLQPTVYLVTCANLTNGGKSELLKSGSSKSTLKHIWTESSKDLSISRLLSQTFRGKENDTDLDLRYDTPEPYSEQDLWDWLRNSTDLQEPRPRAKRRPIVKTGKFKKMFGWGDFHSNIKTVKLNLLITGKIVDHGNGTFSVYFRHNSTGQGNVSVSLVPPTKIVEFDLAQQTVIDAKDSKSFNCRIEYEKVDKATKNTLCNYDPSKTCYQEQTQSHVSWLCSKPFKVICIYISFYSTDYKLVQKVCPDYNYHSDTPYFPSG", "text": "FUNCTION: May be signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurexophilin family."}
{"protein": "MPEIEQDDAAAETVDSSTVKFGTPEALEYVRSLTDVGAMTRLLHECIAYQRSLDSDLDTLLSQRTELDRNLVQLQRSAEILDIVKADADHMLGNVRSTCDLADQVSGKVRELDLAQSRVNVTLSRIDAIVERGNCIEGVKTALESEDYESAAKFVQRFLQIDLQYKDSGSDQSEQLHASKEQLEGIAKKKLLAAIDQRDHPTILRFVRLYSPLGMETEGLQLYVGYLKKVIALRGRMEYENVVELMEQGLGQVNFVGCLTNLFKDIVMAIEENDEILRGLCGEDGVAYAICELQEECDLRGSLILKKYMDFRKLAILASDINNSPNLNILPGGASEGPDPREVELYVEEILSLMQLGEDYTEFMVSKIKSLTSVDPELLPTATKAFRNKSFSKAIQDVTRYYVILEGFFMVENVRKAIRIDEHVPDSLTTSMVDDVFYVLQSCLRRAISTSNISSVIAVLSYAGSLLGNDYHEALQQKIREPNLGARLFLGGIGVENTGTEIATALNNMDVSCEYILKLKHEIEEQCTEVFPAPADRERIKSCLSELGELSSTFKQLLNSGMEQLVATVTPRIRPVLDTVATISYELTETEYAENEVNDPWVQRLLHSVETNAAWLQPLMTSNNYDSFLHLIIDFIVKRLEVIMMQKRFSQLGGLQLDRDTRALVSHFSGMTQRTVRDKFARLTQMATILNLEKVSEILDFWGENSGPMTWRLTPAEVRRVLGLRVEFKPESIAALKL", "text": "FUNCTION: Required for normal Golgi function. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the COG4 family."}
{"protein": "KKGVTLREDDRTFPCSSGLCACLPLDSYSYICLSPSSSTANCENDECISEDDW", "text": "FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion channels. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTNQESQSVKVVFVTRDETLQPEAPLPPVMVPTSLKRLGLSEIVNQLLDTETPVPLDFLIVKATAGDGGASILDEESASSSSVLLRPGASLESFLADNGLSSEVSLSIEYIRSVLPPSFLASFSNPDWVAAVDINARWTGDLKPVIASGSYDGVVRLWDHSGHVTGQLVGHNSAAKAVRWISNDQLVSGGSDRLLYLWNPDGKKYRRKEPGQVGKKELNYDSEEDSDEEMLDELPAASTVTPMAALHGHTAPINDLAVHAKTGKIISASADGSVGLWSTDYNDMPAIEPHTAAAGGLTSTSAQKRRKLANSGSGATGLGAARQRGPLAVMGGHSAAVSAVAFHHSDPTVAYSVSLDHTIKTWDLATAEAVQSNAGSPDPSVDTRSTSFSLLSLCTLPQGLIACGSSARHITLHDPRVTAQVATQAKLVGHTNFVSSLSRGPESNPFLLASGSHDGTVRIWDVRTTKSLHVIHRETLTENNAVFGVDWKQNLGIVSGGQDNKIQINNNPQSA", "text": "FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family."}
{"protein": "MYRMQLLSCIALTLALVANGAPTSSSTENTKKQVQSLLQDLQLLLKEINNYENLKLFRMLTFKFYMPKKATELKHLQCLAEELKPLEDVLNVAQSKTQNSIDIKDLMDNINRIVLTLKGSETRFTCEYDEKTVTAVELLNKWITFCQSIIST", "text": "FUNCTION: Cytokine produced by activated CD4-positive helper T-cells and to a lesser extend activated CD8-positive T-cells and natural killer (NK) cells that plays pivotal roles in the immune response and tolerance. Binds to a receptor complex composed of either the high- affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122 and IL2RG/CD132) or the low-affinity dimeric IL-2R (IL2RB and IL2RG). Interaction with the receptor leads to oligomerization and conformation changes in the IL-2R subunits resulting in downstream signaling starting with phosphorylation of JAK1 and JAK3. In turn, JAK1 and JAK3 phosphorylate the receptor to form a docking site leading to the phosphorylation of several substrates including STAT5. This process leads to activation of several pathways including STAT, phosphoinositide-3-kinase/PI3K and mitogen-activated protein kinase/MAPK pathways. Functions as a T-cell growth factor and can increase NK-cell cytolytic activity as well. Promotes strong proliferation of activated B-cells and subsequently immunoglobulin production. Plays a pivotal role in regulating the adaptive immune system by controlling the survival and proliferation of regulatory T-cells, which are required for the maintenance of immune tolerance. Moreover, participates in the differentiation and homeostasis of effector T-cell subsets, including Th1, Th2, Th17 as well as memory CD8-positive T-cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-2 family."}
{"protein": "MPPMAKNAAVTDVVHLDSDSDSDNGVVGGRESASTIAGAATMAPRETLECRSFWKAGDYFVIPNVVTPTAPGMLEHARVHPRFLHSNATSHKWAFGAIAELLDNAVDEIQNGATFVKIDKINIVKDNSPALVFQDDGGGMDPAGLRKCMSLGYSSKKSNTTIGQYGNGFKTSTMRLGADAIVFSRSTRGGTSTQSVGILSYTFLRKTGQDDVTVPMIDIDISKERPQPIIYGSPEDWAANLEILLKWSPFSTEDELLQQFEDVGTHGTKVIIYNLWLNDEGIYELSFDDDEEDIRLRDESVNDGKRLHHKILELRSHISYHLRYSLRAYASMLYLKKFKNFKIIIRGIPVEQFNIADGFRFPEIIKYKPHTATTEQASTEIKIGFVKEAPKLAICGFNVYHKNRLIRPFWKVTMGGDSTGHGVVGVLEANFIEPAHDKQDFERSSLFQRLEARLKKIVYSYWYSHCHLLGYHKYQMPADKSKKIAIPDQPPTISTVNPSPLPSDKISQGGPIIREINLSNATSSRTVAFASPHLRNSTGLRSNFQPVQLNPQPTAADTGNNLDGKSAGEIRQENLQLFMRCEEYIKKENETEQTVKSLEKELEEFKSKCAHLALLVDAKKKEMQQA", "text": "FUNCTION: Mediator of defense signaling triggered by distinct classes of R proteins. Required during hypersensitive response (HR) that confers disease resistance to turnip crinkle virus (TCV) (PubMed:19704828). Contributes to resistance against Pseudomonas syringae and Hyaloperonospora arabidopsidis, at early stages prior to cytosolic calcium ions Ca(2+) accumulation (PubMed:20332379). Required for pathogen-associated molecular pattern (PAMP)-triggered immunity, basal resistance, non-host resistance and systemic acquired resistance (SAR) (PubMed:23250427). Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing (PubMed:24799676). Exhibits ATPase activity (By similarity). SUBCELLULAR LOCATION: Nucleus Endosome Note=Present in nuclear bodies near chromocenters. Localized in endosome-like vesicles displaying rapid cytosolic streaming. Accumulates in the nucleus following pathogen- associated molecular pattern (PAMP) treatment or infection with an avirulent pathogen. SIMILARITY: Belongs to the MORC ATPase protein family."}
{"protein": "MAANGGGGGAGGCSNGGGGGAVNGAAANGGGGGGGGSKGATTRRAKVSPMDRYWVPTDEKEMAAAVADGGEDGRRPLLFRTFTVRGILLHPYRLLTLVRLVAIVLFFIWRIRHPYADGMFFWWISVIGDFWFGVSWLLNQVAKLKPIRRVPDLNLLQQQFDLPDGNSNLPGLDVFINTVDPINEPMIYTMNAILSILAADYPVDKHACYLSDDGGSIIHYDGLLETAKFAALWVPFCRKHSIEPRAPESYFAVKSRPYAGSAPEDFLSDHRYMRREYDEFKVRLDALFTVIPKRSDAYNQAHAEEGVKATWMADGTEWPGTWIDPSENHKKGNHAGIVQVMLNHPSNQPQLGLPASTDSPVDFSNVDVRLPMLVYIAREKRPGYDHQKKAGAMNVQLRVSALLTNAPFIINFDGDHYVNNSKAFRAGICFMLDRREGDNTAFVQFPQRFDDVDPTDRYCNHNRVFFDATLLGLNGIQGPSYVGTGCMFRRVALYGVDPPRWRPDDGNIVDSSKKFGNLDSFISSIPIAANQERSIISPPALEESILQELSDAMACAYEDGTDWGKDVGWVYNIATEDVVTGFRLHRTGWRSMYCRMEPDAFRGTAPINLTERLYQILRWSGGSLEMFFSHNCPLLAGRRLNFMQRIAYINMTGYPVTSVFLLFYLLFPVIWIFRGIFYIQKPFPTYVLYLVIVIFMSEMIGMVEIKWAGLTLLDWIRNEQFYIIGATAVYPLAVLHIVLKCFGLKGVSFKLTAKQVASSTSEKFAELYDVQWAPLLFPTIVVIAVNICAIGAAIGKALFGGWSLMQMGDASLGLVFNVWILLLIYPFALGIMGRWSKRPYILFVLIVISFVIIALADIAIQAMRSGSVRLHFRRSGGANFPTSWGF", "text": "FUNCTION: May catalyze both beta-1,3 and beta-1,4 glycosidic linkage on beta-D-glucan. Essential for (1,3;1,4)-beta-D-glucans synthesis in grasses and cereals (Poaceae). The mixed-linked glucans (which are not present in walls of dicotyledons or most other monocotyledonous plants) are particularly important constituents of the walls of the starchy endosperm and aleurone cells of cereal grains such as oats, wheat, rice and barley. They can account for up to 70% by weight of the wall (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like F subfamily."}
{"protein": "MQYSRMTATRENPKYKNLRVEECDVLIIGSGPVGATYAREILDPGSGASPGRKAPKVIMVETGAQESKVPGEHKKNAVVYQKHIDSFVNVIQGSLFATSVPTRVDPNLKLPPVSWSPREKQNFNGQNKEQNIYHNLDANGVSRNVGGMSTHWTCATPRQHELERSKIFDDATWDRLYKRAEELIGTRTDVLDQSIRQRLVLDILRKKFKNRDAKALPLAAEKVEGKNLIKWSSSSTVLGNLLEDEKFTLLDQHHCEKLEFNDETNKVSFAIIKNLAKPQTSKEDEDRLRIKAKYVIVCGGPILTPQLLFKSGFRYDEEDAEDSEGNKSSLYIPALGRNLTEQTMCFCQIVLKDKWVEELQKNNWGPECEEHRRKYDEEDDPLRIPFDDLDPQVTLPFTENTPWHTQIHRDAFSYGAVPPAIDKRTIVDLRYFGRAETQWRNRVTFSKKLTDAYGMPQPTFDFKLSTKDRLESHRMMQDMEKVAGELGGYLPGSEPQFLAPGLALHVCGTTAALRKGCRSEDEMKRISVCDENSKVWGVENLHLGGLNVIPGPRSNASNPTLTAMCFAIKGAEEIRRKLGKKGSHSGNRDDGDVDTDTDDDA", "text": "FUNCTION: Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MLEDALVPDDKLIYVSPENLYYCYANDTIDQDDKWTSIQPQQGYIPILSANLRAYKIELLKKLRFSGQNNVSPSIKKEKKNLEPNKKITTKPTESTGSKKYLIPEQFIPDSLEKQLRTLTVILKDALYLGKNNRFIKENEVVSDDTRLLILDEFLKLIIPNYIDSLANWTLVDLNKGTDDESLLYLRFNESGTQSMISFYKKHSKMAKYMEIHYDTNTEKYINDNFKDDGDEDNVEAEQSHSVGEILKSMETAFEKARSQVGTFKGDINDDQDDKINYKIDYNTLLDIPSDSLEQLTKEILNFRTKVIDIEKQKQLRQQYEDNERRQKHMTQLFEKLRKGTKSNDSNRNMDIESTDTINDSDSEEDDDEEDEDDLAIEKRKEEKRKEEEARKYRALLKDYETTIEPHLHLLSQQYKQNLEYEKELAANREANVKDLLRQANDIYYDKDRSFKDREEQEDKLDREKYGDIIIEDIVIDDDRKGQKKLLEKDKKVKKAGEPAIKINLAFKKAMDNSIQDKRDKAEDIEPVSQPIEARSTNRYAALKEKRVVDELVKELLGVYEDDVVAYVFEILEKPEMSDEKKQSELVTEMEDLFDKEGAVQFAEQVFKALDEA", "text": "FUNCTION: Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SNU71 family."}
{"protein": "MGDMKYTELSDLYRRLEKTTLKTLKTKFVADFLKKTPDELLEVVPYLILGKVFPDWDERELGVGEKLLIKAVSMATGVQEREIENSVKDTGDLGESVALALKKKKQKSFFSQPLTIKRVYQTFIKIAEASGEGSQDRKLKYLANIFMDAQPEEGKYIARTVLGMMRTGVAEGILRDAIAEAFKVKAELVERAYMLTSDFGYVAKVAKLEGNDGLGKVHIQIGKPIRPMLAQNAASVKEALLEMGAEAAFEIKYDGARVQVHKDGDRVVIYSRRLENVTRSIPEVVDAIKASIKSEKAIVEGELVAVGEGGRPRPFQYVLRRFRRKYNIEEMIEKIPLELNLFDVLYVDGEPLIDTPFRERRAKLEEIVEEGEKLKLAQQLVTKKVEEAEEFYKKALELGHEGLMAKRLDSVYEPGNRGKKWLKIKPTMEDLDLVIIGAEWGEGRRAHLLGSFLVAAYDPHSGEFVPVGKVGSGFTDEDLVEFTKMLKPLIIGGEGKFVEIEPKVVIQVTYQEIQKSPKYRSGFALRFPRYVALREDKSPEEADTIERIAQLYEFQERFKAKK", "text": "FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use both ATP and NAD(+), but NAD(+) may be a preferred nucleotide cofactor. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
{"protein": "MSFRSAEGVSIMQALAMTVAEIPVFLYSTFGQSIFSQLKLSPSLKKVLFATALGSVALALTAHQLKRRGRKRKQTLGKEAQKPVGIPEQLLRSSRPASLKRGPVPARQMMSPSTRSNDTLSGVSSIAQSKHSSSSHSIASMRVPSSPNQSVNAGAAWEAEPVAEEPAVGEDANAENLYLMGMELFEEALRKWELALNIRHRSHSRASASNSQGSELVERHSPEVRNHQFAERLETLLHRAYHLQEDFGSTIPPDSLLADLESEGTLILPTLGSSHPIQDDDATTVTSDDSFFSAAELFETFSLEDSFHLLKPAALYEEALSLVKDGDVACRSLRTELLECYSDQDFLAKLHCVRQAFQVLLLDETHRMFFMETGKQMISGLLVKANKSPKAFLESYEDMLQYTQREETWPVSKMELEGRGVVCMNFFDIVLDFILMDAFEDLESPPSSVVAVLRNRWLSDSFKETALATACWSVLKAKRRLLMVPDGFIAHFYVISEHVSPVLAFGFLGPHQHLSEVCTIFKQQIVQYLKDMFDHDKVRFTSVPSLAEDILRLSHRRADILMGYLGIENLPETNGALPKSPCQAESGNLDASGQQD", "text": "FUNCTION: Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of pld6/MitoPLD dimers. May act by regulating phospholipid metabolism via pld6/MitoPLD. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitoguardin family."}
{"protein": "MASKRKSTTPCMVRTSQVVEQDVPEEVDRAKEKGIGTPQPDVAKDSWAAELENSSKENEVIEVKSMGESQSKKLQGGYECKYCPYSTQNLNEFTEHVDMQHPNVILNPLYVCAECNFTTKKYDSLSDHNSKFHPGEANFKLKLIKRNNQTVLEQSIETTNHVVSITTSGPGTGDSDSGISVSKTPIMKPGKPKADAKKVPKKPEEITPENHVEGTARLVTDTAEILSRLGGVELLQDTLGHVMPSVQLPPNINLVPKVPVPLNTTKYNSALDTNATMINSFNKFPYPTQAELSWLTAASKHPEEHIRIWFATQRLKHGISWSPEEVEEARKKMFNGTIQSVPPTITVLPAQLAPTKVTQPILQTALPCQILGQTSLVLTQVTSGSTTVSCSPITLAVAGVTNHGQKRPLVTPQAAPEPKRPHIAQVPEPPPKVANPPLTPASDRKKTKEQIAHLKASFLQSQFPDDAEVYRLIEVTGLARSEIKKWFSDHRYRCQRGIVHITSESLAKDQLAIAASRHGRTYHAYPDFAPQKFKEKTQGQVKILEDSFLKSSFPTQAELDRLRVETKLSRREIDSWFSERRKLRDSMEQAVLDSMGSGKKGQDVGAPNGALSRLDQLSGAQLTSSLPSPSPAIAKSQEQVHLLRSTFARTQWPTPQEYDQLAAKTGLVRTEIVRWFKENRCLLKTGTVKWMEQYQHQPMADDHGYDAVARKATKPMAESPKNGGDVVPQYYKDPKKLCEEDLEKLVTRVKVGSEPAKDCLPAKPSEATSDRSEGSSRDGQGSDENEESSVVDYVEVTVGEEDAISDRSDSWSQAAAEGVSELAESDSDCVPAEAGQA", "text": "FUNCTION: Acts as a transcriptional repressor (PubMed:12741956). Represses the promoter activity of the CDC25C gene stimulated by NFYA (PubMed:12741956). May play a role in retinal development where it regulates the composition of bipolar cell populations, by promoting differentiation of bipolar OFF-type cells (By similarity). In the brain, may promote maintenance and suppress differentiation of neural progenitor cells in the developing cortex (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with EFNB1 intracellular domain in the nucleus. SIMILARITY: Belongs to the ZHX family."}
{"protein": "MSEAYRQPVLGVIGGSGVYDIDGLEGARWQTVESPFGDVSDQILRGTLDGLEMAFLPRHGRGHVLAPSDVNYRANIDALKRAGVTEILSVSAVGSLAEDLPPGTFVIADQFIDRTFAREKSFFRQGSGRPCQHGPSGQRLAGRSRRRGSGRSGHSPSPGRHLSVHGGAAVLDPGRKQSLSAMGLPRHRHDQHARGQAGPRSRDRLLHRGHGHRFRLLAPRSRPRQRRGGGSRAAAKRR", "text": "SIMILARITY: Belongs to the PNP/MTAP phosphorylase family."}
{"protein": "MLTLPFDESVVMPESQMCRKFARQCEDQKQIKKPESFPKQVVLRGKSIKRAPGEETEKEEEEEDREEEDENGLSRRRGLRKKKTTKLRLERVKFRRQEANARERNRMHGLNDALDNLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILRIGKRPDLLTFVQNLCKGLSQPTTNLVAGCLQLNARSFLMGQGGEAAHHTRSPYSTFYPPYHSPELATPPGHGTLDNSKSMKPYNYCSAYESFYESTSPECASPQFEGPLSPPPINYNGIFSLKQEETLDYGKNYNYGMHYCAVPPRGPLGQGAMFRLPTDSHFPYDLHLRSQSLTMQDELNAVFHN", "text": "FUNCTION: Activates E box-dependent transcription in collaboration with TCF3/E47. May be a trans-acting factor involved in the development and maintenance of the mammalian nervous system. Transactivates the promoter of its own gene. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPCPCGSGCKCASQATKGSCNCGSDCKCGGDKKSACGCSE", "text": "FUNCTION: This protein binds cations of several transition elements. It is thought to be involved in detoxification processes. SIMILARITY: Belongs to the metallothionein superfamily. Type 5 family."}
{"protein": "MSQTNANDLRNNEVFFISPSNNTNKVLDKISQSEVKLWNKLSGANQKWRLIYDTNKQAYKIKVMDNTSLILTWNAPLSSVSVKTDTNGDNQYWYLLQNYISRNVIIRNYMNPNLVLQYNIDDTLMVSTQTSSSNQFFKFSNCIYEALNNRNCKLQTQLNSDRFLSKNLNSQIIVLWQWFDSSRQKWIIEYNETKSAYTLKCQENNRYLTWIQNSNNYVETYQSTDSLIQYWNINYLDNDASKYILYNLQDTNRVLDVYNSQIANGTHVIVDSYHGNTNQQWIINLI", "text": "FUNCTION: The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host. Involved in binding to the small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (By similarity). Erythrocyte agglutination only occurs when the entire complex is assembled (PubMed:17581814). Binds eukaryotic host mucins as well as N-acetyl-beta-neuraminic acid, N-acetyl-D-galactosamine and galactose (but not glucose) via 2 sites (By similarity). FUNCTION: Agglutinates human erythrocytes (PubMed:2205574). The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The hemagglutinin (HA) component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Binds galactose or oligosaccharides with galactose at their non-reducing end (PubMed:14663070). Binds eukaryotic host mucins; binding is inhibited by N-acetyl-beta-neuraminic acid, N-acetyl-D- galactosamine, galactose, and methyl N-acetyl-beta-neuraminic acid (PubMed:18178224). Binds N-acetyl-beta-neuraminic acid, N-acetyl-D- galactosamine and galactose (but not glucose) via 2 sites (PubMed:18178224, PubMed:21640703). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MNPANYLYLSVLLFTIGASGVLLRRNAIVMFMCVELMLNAVNLAFVTFARMHGHLDAQMIAFFTMVVAACEVVVGLAIIMTIFRTRKSASVDDANLLKG", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
{"protein": "MDLLSLITGKKFEKHYSKVGSRFSDESLNGLEKQLSNGADAAIDTTADDRGSVVSLGASLPLSQGRPAKSKNILNDTLLAEDQYLVTWDGPDDPLNPRNWSHSYKWWIVIQVSVITIVVTFASSVYSSGIIDIASELHSSIPVSTLGSCTFLVGFGVGSLPFAPLSDIYGRFIIYFVTLLIFTIFQVGGGCAHNVWTLAIVRFFQGVFGSTPLANAGGTISDLFTPVQRTYVLPGFCTFPYLGPIIGPIIGDFITQSYLEWRWTFWINMIWAAAVIVFVFIFFPETHEDTILDYKAKYLRKTTGNTAYYTIHERERDPKNAMIQAATQAVSLIFTEPIVVCFTLYLTVVYIINYINFEGYPIVFAKYGFNKGEQGLSFIGVGVGIVCAGLCTPFIYWHYLKVNKKRNGVICPEDRLYPLFIGCFLLPISMFWFAWTCYPHHIHWIVPIIASAFFGFSLLIVFFVSYNYIIDSYQHMAPSALAAATLVRYSASGGISMVARPMYLNLGDHWATSVLGFISVAMVPIPFIFYRFGKSIRAWSKNAYKL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family."}
{"protein": "MSNIHYIKGNILKGRTYKRIIIHSCNANGAWGGGIAYQLAVKHPKAEEVYVDLCERFGQKLLGKCVVIPSYSDDDVLIGCLFTSIFGGASHGSGTSIVDYTDKALSHFDELLAKEQSKSDNANLDKEIEKLLKLKSGVLKDYKLEMPKINSGIFGVPWPETEEVLKKYDRSMNFTVYEL", "text": "FUNCTION: Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing. SIMILARITY: Belongs to the POA1 family."}
{"protein": "MKLVESNDTVDFPDGVTFTVKNRVVHVTGPRGTLKRDFRHLHMEMERVGKNQLRVRKWFGVRKEIAAIRTVCSHIQNMIKGVTKGFRYKMRSVYAHFPINVTLQDGGRTVEIRNFLGEKIVRPVPLRMCHCHVVHFTRTLD", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL6 family."}
{"protein": "MFPLISSHHLWWGGLRRTVCLNLPVLTLQHFQHMHIKVGDRAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFLSQEISFPAPLYIGEVVLASAEVKKLKRFIAIIAVSCSVIESKKTVMEGWVKVMVPEASKS", "text": "FUNCTION: Mitochondrial 3-hydroxyacyl-thioester dehydratase, which may be involved in fatty acid biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the HTD2 family."}
{"protein": "MGFLVAVMNFSPTLVHHHMKSKPQCQNEKLRQGQTSSLFDRRGFLKCVVGASSFMATIEFSGLQAQASEEKLDEGEGVVGAFKTLFDPNERTKSGKELPKAYLKSAREVVKTMRESLKENPKDNAKFRRSADAAKESIRDYLSNWRGQKTVAGEESYVELENVIRALAKFYSKAGPSAPLPDEVKTEILDDLNKAEEFL", "text": "FUNCTION: Required, but not essential, for D1 (psbA) precursor processing and thus correct photosystem II assembly (PSII). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen Note=Associated with PSII on the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the Psb27 family."}
{"protein": "MAEMSFLSSEVLGGDFVSPFDQLGLGAEESLGLLDDNLEVAKHFKHHGFSCDKAKAGSSEWLAVDWLVSDNSKEDAFSGTDWMVEKMDLKEFDFDILFSKDDLETMPDELLATLDDTCDLFQPLVQETNKEPPQIVNPIGHLPEGLPTIDQGAPFTFFQPLPPSPGTLSSTPDHSFSLELCSEVVIPEGDSKPDSTTTGFPQCIKEEDAPSDNDSGICMSPDSSLGSPQDSPSTSRGSPNKSLLSPGALSGSSRPKPYDPPGEKMVAAKVKGEKLDKKLKKMEQNKTAATRYRQKKRAEQEALTGECKELEKKNEALKEKADSLAKEIQYLKDQIEEVRKAREKKRVL", "text": "FUNCTION: Transcription factor that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') and displays two biological functions, as regulator of metabolic and redox processes under normal cellular conditions, and as master transcription factor during integrated stress response (ISR) (By similarity). Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (By similarity). Core effector of the ISR, which is required for adaptation to various stress such as endoplasmic reticulum (ER) stress, amino acid starvation, mitochondrial stress or oxidative stress. During ISR, ATF4 translation is induced via an alternative ribosome translation re- initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced ATF4 acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (By similarity). Promotes the transcription of genes linked to amino acid sufficiency and resistance to oxidative stress to protect cells against metabolic consequences of ER oxidation (By similarity). Activates the transcription of NLRP1, possibly in concert with other factors in response to ER stress. Activates the transcription of asparagine synthetase (ASNS) in response to amino acid deprivation or ER stress. However, when associated with DDIT3/CHOP, the transcriptional activation of the ASNS gene is inhibited in response to amino acid deprivation (By similarity). Together with DDIT3/CHOP, mediates programmed cell death by promoting the expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the terminal unfolded protein response (terminal UPR), a cellular response that elicits programmed cell death when ER stress is prolonged and unresolved (By similarity). Together with DDIT3/CHOP, activates the transcription of the IRS-regulator TRIB3 and promotes ER stress-induced neuronal cell death by regulating the expression of BBC3/PUMA in response to ER stress. May cooperate with the UPR transcriptional regulator QRICH1 to regulate ER protein homeostasis which is critical for cell viability in response to ER stress (By similarity). In the absence of stress, ATF4 translation is at low levels and it is required for normal metabolic processes such as embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (By similarity). Acts as a regulator of osteoblast differentiation in response to phosphorylation by RPS6KA3/RSK2: phosphorylation in osteoblasts enhances transactivation activity and promotes expression of osteoblast-specific genes and post-transcriptionally regulates the synthesis of Type I collagen, the main constituent of the bone matrix (By similarity). Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes. Mainly acts as a transcriptional activator in cellular stress adaptation, but it can also act as a transcriptional repressor: acts as a regulator of synaptic plasticity by repressing transcription, thereby inhibiting induction and maintenance of long-term memory (By similarity). Regulates synaptic functions via interaction with DISC1 in neurons, which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with GABBR1 in hippocampal neuron dendritic membranes (By similarity). Colocalizes with NEK6 at the centrosome. Recruited to nuclear speckles following interaction with EP300/p300 (By similarity). SIMILARITY: Belongs to the bZIP family."}
{"protein": "MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNALQ", "text": "FUNCTION: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the class-C beta-lactamase family."}
{"protein": "MHITQLNRECLLHLFSFLDKDSRKNLARTCPQLQDVFEDPALWPLLHFRSLTELKKDNFLLSPALRSLSICWHSSRVQVCSIEDWLKSALQRNICSRHESLVNDFLLQVCDRCPNLASVTLSGCGHVTDDCLARLLRCCPRLRALHLENCARVTNRTLTAVAAHGRALQTLHVDFCRNVSAAGLRRLRAACPRLTLRAEHSAAMIPDQLPRGPHAPGAALRKLLLR", "text": "FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC) (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line."}
{"protein": "MSSNRTVHSDTSTLKMNSAVQISCLLLVLGCLLGSGHSQSEAEFAAKSREISQIFGNPSVDKYTKARNFPKLIAFYEKYSSRLHLTAQEKNNIDNSIKQYRAQQNHQVDGVSAQGGKLFDVLKKIIKVIVMVVDSTKANEERQKT", "text": "FUNCTION: A humoral factor that may play a role in stress tolerance. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Turandot family."}
{"protein": "MNGATSLYDEVIIINKIPPKKIDTKGVATEEVATKKVLLNKLLTTQLLNEPE", "text": "FUNCTION: Identified as a multicopy suppressor of the slow growth phenotype of an rsgA (yjeQ) deletion mutant."}
{"protein": "MAHRFPALTPEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAMANCQAAQGQYVHTGSSGAAATQSLFTASYTY", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family."}
{"protein": "MGLQFLAPGEKVFPSLHRIIISTFALIAAYIFIVRPLRNILFHPLKKYPGPKLFGASSIPYGFYYMTGKWHLKIRNLHATYGPIVRIGPDELSYACPEAWEDIYGRYVPTKRRENPKPVWYCSPDAHDMVGASLGDHGRMRRVMAPGFTYSAMCKQEPLIKGHVDMFLSKLCSLCGDGRAEVNILDWLTYCTFDLIGDLSFGEPFGCMENNMLHPWLQLVFANIYITHIILLCQRIPFFYLFLPIKTTYQLWRDFRRHVVLLREVVERRLSLSTPRDDFLDVMTTKQTSTLYMTKEEIFKNAILLTGGGAETTSSSLSGMMYMLTMRPDVKEKILEELRDTFPSEDDINMRSVAQLTYTGAFIEESMRYYPPGPNTMWRITPPAGNTILGDYIPGNTIVGIPHRVLYRSEAYWKDADGFRPERWLPDSQRPAEFDEDKREGFHPFSYGPRACIAMNLAYAEMRYILARFLWHFDIEATKESKKWMDDQKAYLVWDKPGLFVHLKPRAGVKVAA", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II (PubMed:31553484). The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations (PubMed:31553484). The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain (PubMed:31553484). Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE (PubMed:31553484). The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I (PubMed:31553484). The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I (PubMed:31553484). The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (PubMed:31553484). Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II (PubMed:31553484). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSAVVYFSSASRNTERFVEHCDFPSCGVNVFRIPLQPNAAPLNVREPYIIIVPTYGGGDARKAVPPQVKRFLNDPANREWIRGVIASGNTNFGEAYAAAGPIISRKCHVPLMYRFELMGTREDVHAVREGVRRFFSDTPTD", "text": "FUNCTION: Probably involved in ribonucleotide reductase function. SIMILARITY: Belongs to the NrdI family."}
{"protein": "MDLSSRLSSGSSRIPKRHRDYRDEEPRRERGSGGIGREDPRGHYGSERPRRRRRDESDFRRHRESRERSYREDERPRRERRYDDYEPRSLRYSSVGRSRSPPPSRERSVRSIEQELEQLRDVTPINQWKRKRSLWDIKPPGYELVTADQAKMSGVFPLPGAPRAAVTDPEKLLEFARSAEGSIIAPPPPLQPGASRQARRLVVTGIPNEFVEDAFVSFIEDLFISTTYHKPETKHFSSVNVCKEENFAILEVATPEDATFLWGLQSESYSNDVFLKFQRIQNYIVPQITPEVSQKRSDDYAKNDVLDSKDKIYISNLPLNLGEDQVVELLKPFGDLLSFQLIKNIADGSSKGFCFCEFKNPSDAEVAISGLDGKDTYGNKLHAQFACVGLNQAMIDKSNGMAILTELAKASSQSIPTRVLQLHNLITGDEIMDVQEYEDIYESVKTQFSNYGPLIDIKIPRSIGTRNSGLGTGKVFVRYSDIRSAEVAMEEMKGCKFNDRTIVIAFYGEDCYKANAW", "text": "FUNCTION: Necessary for the splicing of pre-mRNA. The SF1-U2AF59-U2AF23 complex has a role in the recognition of the branch site (5'-UACUAAC- 3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family."}
{"protein": "MTSCVAEEPIKKIAIFGGTHGNELTGVFLVTHWLKNGAEVHRAGLEVKPFITNPRAVEKCTRYIDCDLNRVFDLENLSKEMSEDLPYEVRRAQEINHLFGPKNSDDAYDVVFDLHNTTSNMGCTLILEDSRNDFLIQMFHYIKTCMAPLPCSVYLIEHPSLKYATTRSIAKYPVGIEVGPQPHGVLRADILDQMRRMLKHALDFIQRFNEGKEFPPCAIDVYKIMEKVDYPRNESGDVAAVIHPNLQDQDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIRSTLH", "text": "FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily."}
{"protein": "MTTLSPDHLKTLEQSRQRLIQLTHSLGSLITSLNQSDPLPTWSSLQTQASIISNNLQSISTHLSENHELLRSISALPAPEFPTKTHANTLEQLLRTKLDPRVEDWVSRGRKADNSAIQGSSGSTGMFSTLPSASAAGMNAGVVGAGAGGRLSEDDLAALWEWAPVEANSEARRRNWGGNFTLEEKERGIQQVVAELGLKRVLEDDDESEEEDEEMDVGFGGRIDGAPDNAGAAAGEHALPLVPINEILRYMTTGVMPAVR", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 8 family."}
{"protein": "MGDSDDEYDRKRRDKFRGERSAGESYARGADRADRSRGRDEWAERGRPRQDYRDYRPPPRDRGYSPTREGPPMKRMRGDGWGDDARPRFGGHEPYGMYGGYNHDHFGMHPAGPYGHPGGLHPREQQSAGDMQTQPCMMTLKQFLATQDDSISDSEAIQKYNDYKLEFKRQQLNEFFVAHKDEEWFKMKYHPEESLKRKEEQFGFLKRRCDVFVELLDHGDISKVSVDTSNTDPLLRLLDTVVIKLEGGTDEDLKVLDEKPVEIVKILPEKPKVEVKKEPTLEDTIKKEKISIKEEKVEEADKPKEEKDDDKEKPAAEGEEPEGEKNDAEKEVTAEREDMDAEPAAKEPEPEEEPSRKKDRRKRSRSDSGSSSSSSSSSSSSDSEDEKEKEKEDKEEEEEKKETEEEAAPKSPKPVEEGEKEPQEEVENNGHKSGDEEEATKKDQAEPEKMDTDEAVVENNKESEEAEKEKDTSKDEEEANKESNEDKQESEKTETIDLVKDTTVGNSPRALHRTSSIFLRNLAPSITKAEVEAMCKRYNGFLRVAIADPLLERRWFRRGWVTFRRDVNIKEICWNLNNIRLRDCELGAIVNKDLSRRVRPVNGLTCHKTIVRSDIKLCAKIAHNLDDKVGLWKEQEDNGEKNGESFGLQSKNPVLQNITDYLIEEASAEEDELLGLSTEAAKKSNDGELVERDTQLIEVLDKLILYLRVVHSIDFYNHCEYPYEDEMPNRCGIIHARGPPPQNKVTSNEIQEYIRTFEGKMGSFLARAVDLEEEEMKKLGAKDAEAEVEKFIQANTQELAKDKWLCPLSGKKFKGPDFVRKHIFNKHNEKVDEVRKEVEYFNNYLKDTKRPQLPEHPGNTKKAPSDAAPPTAGYRPPYGMAHAYAPMYAPYAQPMMAPAGRARPGFGRGGREPMGEIRRPIIAYSDLDMPNFSDSFL", "text": "FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and RNA-mediated gene silencing (RNAi). Involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. Also involved microRNA (miRNA)-mediated silencing by contributing to the stability and delivery of primary miRNA transcripts to the primary miRNA processing complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARS2 family."}
{"protein": "MDLIETVNACVGLQKRVLKLAPNTNLNTAGQSVLNDYNALASRVNGRTYALLDQTAVYTPYTVNAPIISLAVRISTDDYDDMRSGIDSILDILAAAIRTEGSRPTRVIERRVIEPNVKQLVEDLKLKSLTSEISIANMAAVDTALIQPEIIETENPLFADIIEQVIHRPNASMTGGNIRATLGRWSGNKGIVTCMSGMDSEHRFTVDFKTRTCGIINVVYAPTAGVIMIPMPTGRNREGHLIDVSAEMMAENFAIDFMDDDDIIQTETGVGVFSFPMCNRIRFRINPWDMQKHNDNLWTVNLANWPQGTSPRQPAISFLFETRRTFTEGDYQHLSRCAPKVQYMMDTIFPETAFTNRPVVDWNVQSLLTSSSQKTWCQKIAMLIAAYAAKI", "text": "FUNCTION: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP. SUBCELLULAR LOCATION: Virion Note=Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus VP6 family."}
{"protein": "MTILSLSRFMLAGVLLASFNASAIPGFWQQGYGQGNTEYSVTEASGKTFTINCTGNPDQNGFYQHSVFLTLADDKMVSSHDDDTTITVVMDHQQYIIPSSLGWRNGDNAWFDFISNISEAGQFDVYVNDHKAGTFTADRKNAEKVLSTLGDCSND", "text": "SIMILARITY: To E.coli YfjT."}
{"protein": "MRLDVVSKAARAAQRFSAQCHGQKFRTAHASATLRAALAVEASEANQKGRSAGLLAAMALMGVAGVASMDDNAAAKCEGAAKPVSREAVTQAMLKEVVTKLNRIESAVANPHRHTDGLNVGVDVVLGAQWGDEGKGKLVDSLSQSYDVIVRVAGGSNAGHTIVHEGKKYKFHLVPSGILNPNAICIIGNGVVVHLPSFLEELEELKRMGVDYEGRILISDRAHMVLDLHQEVDGINELRRGRNKIGTTKKGIGPAYSSKMLRNGVRVGDLRYFDDFTEKMVDLVKFYKDNYPELEADAEAEIKVYSDMKDKILDMTVDTVSYLNNAYVAGKKILVEGANATMLDIDFGTYPYVTSSNPSIGSVCTGGGISPNRLNGIIGIVKAYCTRVGEGPFPTELHDDVGEHLGTVGAEFGTTTGRARRCGWLDIPQMRYSNMVNGFTELNLTKLDVLTGLKKVKIGVAYWHEGKKLDGMPSNLQLLQDSVVEYEEMEGWSEDISKCKTFEELPVAAQKYVLRVEELLGTHIKWIGVGPDRFDVITRTHPLEKAYISGN", "text": "FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylosuccinate synthetase family."}
{"protein": "MEQPVIKEGTLALIDTFAYLFRSYYMSAKNKPLTNDKGFPTGLLTGLVGMVKKFYKDRKNMPFIVFALESQTKTKRAEKLGEYKQNRKDAPKEMLLQIPIALEWLQKMGFVCVEVNGFEADDVIASLATLSPYKTRIYSKDKDFNQLLSDKIALFDGKTEFLAKDCVEKYGILPSQFTDYQGIVGDSSDNYKGVKGIGSKNAKELLQRLGSLEKIYENLDLAKNLLSPKMYRALIHDKASAFLSKELATLERGCIKEFDFLSCAFPSENPLLKIKDELKEYGFISTLRDLENSPTPLILDNAPLLDNTPALDNTPKKSCMIVLESAAPLSAFLEKLEKTNARVFARLVLDKEKKVLALAFLYEDQGYFLPLEEALFSPFSLEFLQNAFFKMLQHAQIIGHDLKPLLSFLKAKYQVPLENIRIQDTQILAFLKNPEKVGFDEVLKEYLKEELIPHEKIKDFKTKAEKLELLSVELNALKRLCEYFEKGGLEENLLSLAREIETPFMKVLMGMEFQGFKIDAPYFKRLEQEFKNELHVLERQILELIGVDFNLNSPKQLSEVLYDKLGLPKNKSHSTDEKSLLKILDKHPSIALILEYRELNKLFNTYTTPLLRLKDKDDKIHTTFIQTGTATGRLSSHSPNLQNIPVRSPKGLLIRKGFIASSKEYCLLGVDYSQIELRLLAHFSQDKDLMEAFLKGRDIHLETSKALFGEYLAKEKRSIAKSINFGLVYGMGSKKLSETLNISLNEAKSYIEAYFKRFPSIKDYLNRMKEEILKTSKAFTLLGRYRVFDFTGANDYVKGNYLREGVNAIFQGSASDLLKLGMLKVSERFKNNPSVRLLLQVHDELIFEIEEKNAPELQQEIQRILNDEVYPLRVPLETSAFIAKRWNELKG", "text": "FUNCTION: In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. SIMILARITY: Belongs to the DNA polymerase type-A family."}
{"protein": "MAQFAPGVFRTLHGLFAVYKPPGVHWKSVRDTVETNLLKELNALKQRPPRQQIRFLPAGTEGSNGLEVTRVPSAVPVLADHVLVKGPAFTHIRVGTGHRLDIQSSGVFVLGIGHGNKLLKDMYNSHFTRDYTVRGMLGKATEDFTELGKTIEKTTYDHITREKLERILAVIQGTNQKALITHSHLDLQSQEAYDLAVQGKLRPMVKSPPIILGIRCLEFSPPEFTLEIQCMHETQQYLRKMIHEIGLELRSSAVCTQVRRSRDGPFTVDCSLLRTQWDLGSIQGAIRECRAQTEGVSRGNPDREAAEGPIPGPSRGAEGEGELRA", "text": "FUNCTION: Minor enzyme contributing to the isomerization of uridine to pseudouridine (pseudouridylation) of specific mitochondrial mRNAs (mt- mRNAs) such as COXI and COXIII mt-mRNAs, modulating the efficiency of mitochondrial protein synthesis without changes in transcript abundance or stability (By similarity). Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix Note=Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. SIMILARITY: Belongs to the pseudouridine synthase TruB family."}
{"protein": "MLWFQGAIPAAIASAKRSGAVFVVFVAGDDEQSTQMAASWEDEKVREASSDNFVAIKIDTKSEACLQFSQIYPVVCVPSSFFIGDSGIPLEVIAGSVSADELVTRIHKVQQMHSLKGETSVTNDKQSESSVSTPSASFEPDICESAESRNTELCETPTTSDPKSDTAAGGECAGHDSLSQEPPGCSNQRPAEDLTVRVERLTKKLEERREEKRKEEAQREIKKEIERRKTGKEMLDYKRKQEEELTKRMLEERSREKAEDRAARERIKQQIALDRAERAARFAKTKEAEAAKAAALLAKQAEAEVKRESSTRDRSTIARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRKLLDLELAPSASVVLLPAGRPATSIVPSSSGDIWTLLGTVLYPFLAIWRLISNFLFSNPPPAQTSARATSTEPSNSASSSKSEKREPVRKRVLEKRGEDFKKEGKIYRLRTQDDGEDENNTWNGNSTQQM", "text": "FUNCTION: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Nucleus envelope Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER."}
{"protein": "MRKIALILAMLLIPCVSFAGLLGSSSSTTPVSKEYKQQLMGSPVYIQIFKEERTLDLYVKMGEQYQLLDSYKICKYSGGLGPKQRQGDFKSPEGFYSVQRNQLKPDSRYYKAINIGFPNAYDRAHGYEGKYLMIHGDCVSIGCYAMTNQGIDEIFQFVTGALVFGQPSVQVSIYPFRMTDANMKRHKYSNFKDFWEQLKPGYDYFEQTRKPPTVSVVNGRYVVSKPLSHEVVQPQLASNYTLPEAK", "text": "SIMILARITY: Belongs to the YkuD family."}
{"protein": "MATLASSTKPQKWVSLIAGGVAGGVEAASTYPFEYAKTRVQLLRTSKSTPSNPLRLIFTVAQQEGVGALYTGCSTLIIGTTAKAAVRFVSYDTIKNSLSDERGSLSPARGIVAGVVAGATESVLAVTPTERIKTALIDDAKNARQFRSSLHATQVLVRTHGLRELYRGLVSTTLKQSATSAVRMGTYNILKESFKAHDIPPTLFTTFCMGALAGVVTVYATQPFDTIKTRAQGVQGAGLVEAIRNIQSDYGVRGFWKGSSMRLGRLLLSGGIVFSVYEKMTYLLHSRAGVE", "text": "FUNCTION: Mitochondrial transporter that mediates citrate export from mitochondria to cytoplasm (PubMed:36177470). Both ctpA, ctpB, and ctpD play important roles in citric acid transport across the mitochondrial membrane and function in a redundant manner (PubMed:36177470). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MKIYYIGVFRSPAEQSSDEKALELTEVKDLSQFGFFERNSVGQFMTFFAETVATRTTAGQRQSVEEGNYIGHVYARSEGICGVLITDKDYPVRPAYTLLNKVLDEYLVAHPADQWKSITATNDSLKMAELSTYISKYQDPAQADAIMKVQQELDETKIVLHKTIENVLQRGEKLDNLVDKSESLTASSKMFYKQAKKTNSCCIIM", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the synaptobrevin family."}
{"protein": "MASAEVVSKLEAAFAKLQNASDCHSLLKKYLTKEVFDQLKGKQTKMGATLMDVIQSGVENLDSGIGVYAPDAESYTLFAALFDPIIEDYHKGFKPSDKQPPKDFGDLNTFIDVDPDKKYVISTRVRCGRSLEGYPFNPCLKKQQYEEMESRVKGQLESMSGELRGKYYPLTGMTKETQKQLIDDHFLFKEGDRFLQAAHACKFWPTGRGIYHNDAKTFLVWVNEEDHLRIISMQKGGNLKEVFGRLVTAVGVIEEKVKFSRDDRLGFLTFCPTNLGTTIRASVHIKLPKLGADRKKLEEVAAKYNLQVRGTAGEHSDSPDGVYDISNKRRLGLSEYEAVKEMQDGILELIKAEESAR", "text": "SIMILARITY: Belongs to the ATP:guanido phosphotransferase family."}
{"protein": "MFDDPSKRLTYFEYAVGVLLCSWPVMKQAVEEEWADVDTADKRDWMAGVLVDYITVTSDVEAWDVEELILQVLQDEFNVGSIEDDSPYILAQDLVNVWKAACEDNYEPIREIHERLGKQLLEKEEGKEKTREESNPPVLVEDETIVDAEDGGAAQNQQEKQQGPIVDDDGFTVVQKRRR", "text": "FUNCTION: Required for 20S pre-rRNA processing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TSR2 family."}
{"protein": "MSMNPIKKTEETVAAPAVNKISITLTSRNPKSLEKVCADIITLAKNKKVKAKGPIRIPNKVLKITTRKSPCGEGTNTWDRFEMRIHKRVIHILSTQDFVKEMNTISIEAGVDVEVIMDKKEAKN", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS10 family."}
{"protein": "MHCAILKAEAVDGAHLMQIFWHDGAESLYPAVWLRDNCQCSDCYLHSAKARKLLLEALDVNIRIDDLTFDRKKVYITWPNDHYSEFEANWLKKRCFSQQARARLQGELFLPECQYWGSELQLPTLNFEDVLNDDDHAYKWLSSLKKVGIVRLTGAADKRGEIIKLGKRIGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKEKNPQAFHILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRVNFNNATRDTVFDVPIERVQPFYAALKEFVDLMNSKEYKYTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVTNGN", "text": "FUNCTION: Catalyzes the formation of L-carnitine from gamma- butyrobetaine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gamma-BBH/TMLD family."}
{"protein": "MSVNYMRLLCLMACCFSVCLAYRPSGNSYRSGGYGEYIKPVETAEAQAAALTNAAGAAASSAKLDGADWYALNRYGWEQGKPLLVKPYGPLDNLYAAALPPRAFVAEIDPVFKRNSYGGAYGERTVTLNTGSKLAVSAA", "text": "FUNCTION: Chorion membrane (egg shell) protein; plays a role in protecting the egg from the environment. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the chorion protein S16 family."}
{"protein": "MIFKRAVSTLIPPKVVSSKNIGSAPNAKRIANVVHFYKSLPQGPAPAIKANTRLARYKAKYFDGDNASGKPLWHFALGIIAFGYSMEYYFHLRHHKGAEEH", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase F chain family."}
{"protein": "MREIIERVKEKTTIPVYERTIENVLSAIQASGDVWRIVDLSEEPLPLVVAVVTALYELGYVAFENNQVILTRKGKELVEKYGIGPRADYTCSHCQGRTVEIDAFSELLEQFKEITRDRPEPAHQFDQAYVTPETTVARVALMHSRGDLENKEVFVLGDDDLTSVALMLSGLPKRIAVLDIDERLTKFIEKAADEIGYENIEIFTFDLRKPLPDYALHKFDTFITDPPETVEAIRAFVGRGIATLKGPGCAGYFGITRRESSLDKWREIQRVLLNEFGVVITDIIRNFNEYVNWGYVEETRAWRLLPIKVKPSYNWYKSYMFRIQTLEGSKGFEDEITVGQELYDDEESSTT", "text": "FUNCTION: Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine. Can also use spermine to produce N(4)-aminopropylspermine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the branched-chain polyamine synthase family."}
{"protein": "MAMSPAATVARRRLAAASQGSHEGGARTWKILSFVLALPGVGVCMANAYMKMQAHSHDPPEFVPYPHLRIRTKPWPWGDGNHSLFHNAHTNALPTGYEGPHH", "text": "FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family."}
{"protein": "MDEPACNGTSNEWQRPQLIVAGPRAARRRQMLASLDLNTLLALEALLEHRNVTQAARHLGLSQPSVSRALIRLRGVFNDDLLVRGSSGMVPTPHAQRLGQMLPPVLDSIRGMVDPGLDQGEWRLTARMAMPDHQAIVLLPPFLPLMRERAPNLDIVTDSLLALRRLEQGEIDLAVGQIGEAPPGYFRRRLYNDRFACLLRNGHPALEQESIIDTFSALRHAAIASDTKDGFGRVHDDLVKLDLQDPDPVLVSNVLTAGLAIVSTDLVLVVPRRVATRNAALLPLVIVDPPVELPPYEVALIWHERCHRDPDHRWLRQEIAAAATATEQGQSTDAASRQ", "text": "FUNCTION: Transcriptional activator that regulates the expression of genes involved in symbiosis. Among other targets it acts on the nolWBTUV operon. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MRAAGPWRAASPAPCTRYLARCKPGFRPSSSFVVDLLVDSGDPGLEDVALTECLSPPSLSCSNSTLSLLSPLGHQSFPFGADDSEGEDEEALDEDARESESKVESLEGIEFQQRSSCEVESQDKQEKLVLLQHGSLTPWEMWFVGKEKEERGRLQQKFLEELNQQIEKRKEMEEREKRKIIAEVKHKEWVQKKNKQERKEREQKINKEMEEKEAKKREKEHLQEKAKEKYQEWLKKKKAEEYEKKKKEKEKEKQRQAELQEKKEIAEKKFKEWLENAKNKPRPAAKSYGYSSGKLTGFYSGNSYPEPTFYNPIPWKPIHMPPPKEAKSGPGKKSKRHAASQPLPSSSLAVHNAKSSLCLGALCRGQR", "text": "FUNCTION: Involved in spermatogenesis. Has a probable role in anterograde intraflagellar transport which is essential for the formation of sperm flagella. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum Note=Mainly located in the mid-piece of sperm flagella."}
{"protein": "MDVIPTEAIWWRLFLLFTAVGVLAAGTVTAFFIYSLFKYRSSGQALGEDQGTAGRIYRIMVESPVSGKSKYLLFVTGIIVMGLIVATIDETLYLEKSPPVEDALVVMVIGFQFGWQFEYSVGGETVTTLNYLVVPSDTLIEFRVTSRDVFHAFGIPEFKNKIDAIPGILNSMWIKTPDEPGKVYNAYCYELCGIGHSLMVGKVIVVDKEEFYNAYNSGPDVFSEYVNNVISKYK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family."}
{"protein": "MDAQSKEVDALVQKITGLHAAIAKLPSLSPSPDVDALFTDLVTACVPPSPVDVTKLAPEAQAMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGVFPYYSNYINLSKLEYELLARYVPGGIAPARVAFIGSGPLPFSSYVLAARHLPDTVFDNYVPVRAANDRATRLFRADKDVGARMSFHTADVADLTDELATYDVVFLAALVGMAAEDKGQGDPHLGAHMADGAALVRSAHGARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAQKSKDMFANGPRNGCGGRYARGTVPVVSPPCRFGEMVADVTQKREEFAKAEVAF", "text": "FUNCTION: Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron. SIMILARITY: Belongs to the nicotianamine synthase (NAS)-like family."}
{"protein": "MDHQNYQYQNPFERRPILKSKAPAVKWIKEWVPQDIVATGGKCHLHKWVTEDTFSRLKEKEKEPDVPEPEPEPTTEILFLCSYDGCGKTFFDVSALRKHSHIHGERQYVCDQEGCGKKFLDSSKLKRHYLIHTGERNYICTYEGCGKAFSLDFNLRSHMKTHSQENYHICPYSGCVKRYAHEYKLKNHVAAYHEKNGGGETPKYTPPAEKVLRTVKTPATVCGPSSDRPYACPYEGCEKAYIHEYKLKLHLKREHPGHLQEENADTPTLNKHNGNDRNEIDDGSDQDVYRKHASNGKGQTHKQQSRAKPNMRTPPAKVGKKGSTSSPAKARIAKKPWQAKETFEEVEREEEEDSEETEEDRDNVEDGWRFGENNEDDDDDEETEYED", "text": "FUNCTION: Dual-function transcription factor with both repression and activation activities. Binds to 5'-CCATATT-3' motif in target gene promoters (e.g. ABR1) (PubMed:26961720). Binds also to G-rich DNA motif 5'-GGGGGCAGTGG-3' (PubMed:22508367). Regulates the expression of genes involved in diverse cellular pathways, including glucose metabolism, photosynthesis, phototropism and stress response (e.g. salt, drought and osmotic stress) (PubMed:22508367, PubMed:26961720). Regulates plant immunity, especially during necrotrophic fungal infection (e.g. B.cinerea) (PubMed:24451981). Binds to ABR1 promoter and promotes its expression, thus negatively regulating the abscisic acid (ABA) signaling pathway. Represses ABA- and salt-responsive genes expression (PubMed:26961720). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKVYACLCAAVVMLVMTSRVSEARSTGAPLSACRDMMPQHNATAQTSPPPYTITTDAQSVAPGDSVEVVIAGKLPEDTLRGYLLQARQGDDILGTFSLEDGDVFSQLINCGKPGNAVTHKKHDNKEDKRQVRVRWSPPQGLTGEVVFRATIVKTLKVFWVGVQSAPIKIVS", "text": "FUNCTION: May have antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insect defense protein family."}
{"protein": "MTVQTAQIVKNYIGGEWVESISTKMEAVYNPATGEVIAQVPLSTKVDVEQAVLAANEAFKSWSKTAVPRRARILFKYQQLLVDNWEELAKLITIENGKSYNEAYGEVLRGIECVEFAAGAPTLMMGKQLPDIATGIESGMYRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAARLAELAEEAGLPKGVLNIVNGAHDVVNGLLEHKLVKAISFVGSQPVAEYVYKKGTENLKRVQALAGAKNHSIVLNDANLELATKQIISAAFGSAGERCMAASVVTVEEEIADQLVERLVAEANKIVIGNGLDEDVFLGPVIRDNHKERTIGYIDSGVEQGATLVRDGREDTAVKGAGYFVGPTIFDHVTKEMKIWQDEIFAPVLSIVRVKSLDEAIEIANESRFANGACIYTDSGASVRQFRETIESGMLGVNVGVPAPMAFFPFSGWKDSFYGDLHANGTDGVEFYTRKKMLTSRWEK", "text": "FUNCTION: Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA subfamily."}
{"protein": "MNKHERLDEIAKLVNKKGTIRTNEIVEGLNVSDMTVRRDLIELENKGILTKIHGGARSNSTFQYKEISHKEKHTRQIAEKRFIARKAASLIEDGDTLFFGPGTTVELLAEEVNHHTLTIITNCLPVYKILLEKQTAHFRVYLIGGEMRHITEAFVGEMANAMLEKLRFSKMFFSSNAVNKGAVMTSTLDEAYTQQLALSNSIEKYLLIDHTKVGKEDFTSFCQLNELTAVVMDYEDEEKVETIKTYIEVVD", "text": "FUNCTION: Repressor of the lactose catabolism operon. Galactose-6- phosphate is the inducer (By similarity)."}
{"protein": "MEDTTFLEGANLAGITTLMNNLHINEQANLEELEKQVMGKQQNFPTDHFDEELNGLAKSLGINFNDPEFSLDSAHSVISKKPSRGGSDMISRDGLRHDGLRRDSVCTDSICSESVCSGSMRSGSMRHGSIRNGSVRDGSVRSGRTRRGPARSSSSRNDRIHSYSLSTHRKKYAESEASQKTVISKRDRKHHYAESEYSEKSIKPSTKQVDRLINHLRSNGDPNSFYKKEHDYDRKTKLVKLEKINMLLTYLGNEQISTDGIKIPTIDSSMQEIDDAIEMLTLRNVGIRYSSIAEEILIGLARGLEIVFDGTREIPFLNYRPDYTGLHNTFMIKLFKMRYETSQVVGNFVQNMSPLSKICLELGPSLLLYPALIRTKHKASEDLYNLLQKGPEDPFTAYNEIHETLKKNNK", "text": "SIMILARITY: Belongs to the asfivirus B407L family."}
{"protein": "MAEGDNRSSNLLAAETASLEEQLQGWGEVMLMADKVLRWERAWFPPAIMGVVSLVFLIIYYLDPSVLSGVSCFVMFLCLADYLVPILAPRIFGSNKWTTEQQQRFHEICSNLVKTRRRAVGWWKRLFTLKEEKPKMYFMTMIVSLAAVAWVGQQVHNLLLTYLIVTSLLLLPGLNQHGIISKYIGMAKREINKLLKQKEKKNE", "text": "FUNCTION: Positively regulates SLC1A1/EAAC1-mediated glutamate transport by increasing its affinity for glutamate in a PKC activity- dependent manner. Promotes the catalytic efficiency of SLC1A1/EAAC1 probably by reducing its interaction with ARL6IP5, a negative regulator of SLC1A1/EAAC1-mediated glutamate transport. Plays a role in the formation and stabilization of endoplasmic reticulum tubules. Negatively regulates apoptosis, possibly by modulating the activity of caspase-9 (CASP9). Inhibits cleavage of CASP9-dependent substrates and downstream markers of apoptosis but not CASP9 itself. May be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum Note=Predominantly localized to intracytoplasmic membranes. Preferentially localizes at the ER tubules and the edge of the ER sheets, both of which are characterized by a high membrane curvature. SIMILARITY: Belongs to the ARL6ip family."}
{"protein": "MGITHEFHIFLVDENVSLKSVSLLKGDSYGCNIHLKNSECKYITFILVLEPDWSEIAEAKPIRIRLNGKKMRTQLLTKTLMSIIYKAVIYVEENALVQFYSDTDRLYTDMYPTFLIDMDKQHYHILDNGYTYTYIDSFISECDKQRYLTSDIGENGYEDSTEEEDNEEDTDGVCLYCLEEEEEEDEDEDEDEDEDEEE", "text": "FUNCTION: Plays a role for multiplication of the virus in different cell types. SIMILARITY: Belongs to the poxviridae C7 protein family."}
{"protein": "MKFLVVGAGGVGGYIGGRLSEKGNDVTFLVRQKRAEQLKKTGLVIHSEKGNVSFQPELISAGETGQFDVVIIASKAYSLGQVIEDVKPFIHQESVIIPFLNGYRHYEQLFAAFSKEQVLGGLCFIESALDNKGEIHHTSASHRFVFGEWNGERTERIRALEEAFSGVKAEVIISGHIEKDIWKKYLFIAAQAGITTLFQRPLGPILATEAGRHTAQTLIGEICTVLRKEGVPADPALEEESFRTMTSMSYHMKSSMLRDMENGQTTEGDHLHGFLIEKAKRLSLAAPVLETVYANLQMYEAEK", "text": "SIMILARITY: Belongs to the ketopantoate reductase family."}
{"protein": "MKRDRLGRFLSPGSSRQCGASDGGGGVSRTRGRPSLSGGPRVDGATARRAWGPVGSCGDAGEDGADEAGAGRALAMGHCRLCHGKFSSRSLRSISERAPGASMERPSAEERVLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQRVNASPAGRRKPCAKVGAQPPTGAEEGACLVDLITSSPQCLHGLVGWVHGHAASCGALPHLQRTLSSEYCGVIQVVWGCDQGHDYTMDTSSSCKAFLLDSALAVKWPWDKETAPRLPQHRGWNPGDAPQTSQGRGTGTPVGAETKTLPSTDVAQPPSDSDAVGPRSGFPPQPSLPLCRAPGQLGEKQLPSSTSDDRVKDEFSDLSEGDVLSEDENDKKQNAQSSDESFEPYPERKVSGKKSESKEAKKSEEPRIRKKPGPKPGWKKKLRCEREELPTIYKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIDRYLQRHVKLIHTEVRNYICDECGQTFKQRKHLLVHQMRHSGAKPLQCEVCGFQCRQRASLKYHMTKHKAETELDFACDQCGRRFEKAHNLNVHMSMVHPLTQTQDKALPLEAEPPPGPPSPSVTTEGQAVKPEPT", "text": "FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore."}
{"protein": "MIGRISQPLLNTSQKFMAPAARTLMLHEHHGMKILQNYEIKVPPFGVAQDAETAFSEAKRIGGKDYVVKAQVLAGGRGKGRFSSGLQGGVQIVFTPDEVKQKAGMMIGANLITKQTDHRGKKCEEVMVCKRLFTRREYYFSITLDRNTNGPIVIASSQGGVNIEEVAATNPDAIVKMPIDVNVGITKELAHEIAVKMGFSKDCEQQASEIIEKLYQMFKGSDATLVEINPMAEDVNGDVYCMDCKLLLDSNAEFRQAKLFDLKDKKQEDELEIRAAAANLNYIRLDGTIGCMVNGAGLAMATMDIIKLHGGEPANFLDVGGGATVEQVTEAFKIITADKDKVSAILVNIFGGIMRCDVIAQGIIQAARELDLKIPIVVRLQGTKVEDAKALIATSQLRILPCDNLDEAAKMVVKLSNIVDLARATNVDVKFELSI", "text": "FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family. ATP-specific subunit beta subfamily."}
{"protein": "MDILKKSLFLVLFLGLVSLSICEEEKRENEDEEKQEDDEQSEMKRALWKTMLKKLGTVALHAGKAALGAAADTISQGAQ", "text": "FUNCTION: Potent antimicrobial peptide with activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MAAGKFASLPRNMPVNHQFPLASSMDLLSSKSPLVERRADAYQDVSIHGTLPRKKKGPPPIRSCDNFSHVGTLPHSRSPRHHSPLIQDVIQEQPLQDWKGEAFTFRDQHLLDPTLEYVKFSKERHVMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLMQRDGDFLVRDSLSSPGDFVLTCQWKNLPQHFKIRRTVVRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPVNRTVPLRCLEERYGASSPDRAHEGSLTEGRPDAAKRLSLTVGGTQAREQGLPRGNLLRNKEKSGSQPACLDHMQDRRALSLKAHQSESYLPIGGKLTPQSPSVGTSPCPNSPVFRTGSEPTLSPAVVRRVSSDARPGEALRGSDSQLCPKPPPKPCKAPLLKAPPSPSIWLNSEANYCELNPALAASYDGASRLPFCAQDSYVELLTAKQNGGLGTRNSDTSYLILDDDDRTRPWKPPPAPGDTVGEDQDTFVMPLLETTSSFKPNDFESKLLPPENKPLETSMLKRAKELFTNSDPKVIAQHLLSVDCKVARILEVSEEMRKNMGVNSGLELITLPYGHQLRLDIIERHNTMAIGIAVDILGCTGSLEDRAATLNKIIQVAVELKDSMGDLYSFSAIMKALEMPQITRLEKTWTALRHQYTQTAILYEKQLKPFSKVLHEGRESTCVPPNNVSVPLLMPLVTLMEREAVTFEGTDMWEKNDESCEIMLNHLATARLMAEAADSYRMNAERILAGFQPDEEMSEVFKTEFQMRLLWGSKGAQVNQTERYEKFNQILTALSRKLEPPPVKQMEF", "text": "FUNCTION: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (By similarity). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1. Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity. May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling. Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA. Positively regulates integrin-induced tyrosine phosphorylation of BCAR1. Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion Note=Localization to focal adhesions depends on interaction with PTPRA."}
{"protein": "MGLSDKINSKSDEAVGAAKEKIGGLTDDSDLKSAGADQKASGKVAQKVEDVKDKANDLKHNVQAAADKLKG", "text": "SIMILARITY: Belongs to the UPF0337 (CsbD) family."}
{"protein": "MEKLTILLLVAAVLLSIQALNQEKHQRAKINLLSKRKPPAERWWRWGGCMAWFGLCSKDSECCSNSCDVTRCELMPFPPDW", "text": "FUNCTION: Gamma-conotoxins may act on voltage-gated non-specific cation pacemaker channels (HCN). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O2 superfamily."}
{"protein": "MFSKVLVANRGEIAVRVMRACEELGVRTVAVYSEADKHGGHVRYADEAYNIGPARAADSYLDHESVIEAARKADADAIHPGYGFLAENAEFARKVEDSEFTWVGPSADAMERLGEKTKARSLMQDADVPVVPGTTEPADSAEDVKAVADDYGYPVAIKAEGGGGGRGLKVVHSEDEVDGQFETAKREGEAYFDNASVYVEKYLEAPRHIEVQILADEHGNVRHLGERDCSLQRRHQKVIEEAPSPALSEDLRERIGEAARRGVRAAEYTNAGTVEFLVEDGEFYFMEVNTRIQVEHTVTEEVTGLDVVKWQLRVAAGEELDFSQDDVEIEGHSMEFRINAEAPEKEFAPATGTLSTYDPPGGIGIRMDDAVRQGDEIGGDYDSMIAKLIVTGSDREEVLVRAERALNEFDIEGLRTVIPFHRLMLTDEAFREGSHTTKYLDEVLDPERIEAAVERWSPEAVAGDEEEGEVTERTFTVEVNGKRFEVSLEERGAPAIPLGGASAAASASKPSGPRKRREESDEGGQQVIEGDGESVAAEMQGTILAVEVDEGDDVEPGDTVCILEAMKMENDVVAERGGTVSQVLVGEGDSVDMGDVLLVLE", "text": "FUNCTION: This is one of the subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl- CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase is involved in propionate utilization and in the production of the poly(3-hydroxybutyrate-co-3- hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as intracellular energy reserve material when cells grow under conditions of nutrient limitation (PubMed:25398867). Propionyl-CoA carboxylase is also able to catalyze the carboxylation of acetyl-CoA (PubMed:25398867)."}
{"protein": "GLLDIVTGLLGNLIVDVLKPKTPAS", "text": "FUNCTION: Has no antimicrobial or anticancer activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Aurein subfamily."}
{"protein": "MSSFVTNGYLPVTLEPHELTLDIKTNIRNAVYKTYLHREISGKMAKKIEIREDVELPLGEIVNNSVVINVPCVITYAYYHVGDIVRGTLNIEDESNVTIQCGDLICKLSRDSGTVSFSDSKYCFFRNGNAYDNGSEVTAVLMEAQQGIESSFVFLANIVDS", "text": "FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:31835031). Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase. FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase. SUBCELLULAR LOCATION: Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle. SUBCELLULAR LOCATION: Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle. SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 18 kDa subunit family."}
{"protein": "MKTLHLLLLISGLLSVFVKGVGSHPGTVHVRFKCIPKIAAVFGDNCPFYGNVDGLCNDKKSVCCMVPVRLDNI", "text": "FUNCTION: Has bactericidal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MSPSNVFIDSSVMVGLFIGDEKAHKLLSKLINDGFMLCINPIVFSETMFKVTFHIALEDGIRGVYDLKKNLNRYSWVYEEVREKIDKMIKMNYLKILDTNWEVLKLAPEIGKKYNLLTNDAIIIATCKYYRINKLATFDSDFEKVDFIEIIKE", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. SIMILARITY: Belongs to the PINc/VapC protein family."}
{"protein": "MIAAVEKDAVPRKRRVISQVSQACIRCRQKKIKCSGEKPSCQACSNNKVECIWPDRPNMRGKKPSSAARTLSPLTGIVQPYLGSHPFSPTILSPSSPNMDFTYSINSFGDYQKQLRLPTSRKLLQLWDIFLKTSYTELFGIFNKAQITSQIASDTAPPVLVLCICAHAARFSQEEVNRFKSSTAASDYYANQAFSLLPCRFQDISLTNITCLLLLCLIELGSCRGAKAWLLLGMALRMVDSLDLGNEINDNPLTMGSNTVSWTEAEQKRRVYWACFFVERLLSTGYMAPSKLRSLSLSLQKTSIQLPCPEPNFLFNQPILTELFDGSLPENTQSDTTSMAPYQRSLQLEFMTGSLIRLSNLWSEISRWALCGGYTKDITPPWLNQSQFHRSFELLKAWHENLPPRAVWSYTNYSAYSSPGESAGACYTFMHLLYHTTLTYLLRNVLDLFPEKSRQKSKLFSSVSQRFGQQPPTVWMDMILDQVITSADFITKLSKDPLNYIMSPFVGFSILTAATIHMLLKFCVVNIDQNYISSSRLVHVDHQILQDRSKYWKINQAMLVTLQRLYNFYRFQYLEEQSLYNFKIPGFPLCILEYGIVEDQSMKSNPDLNSFSKELFSRGTNELLNNGDDTQSGNSTPAMGVSEIRTDTILDEEVPVDPLITSILDDGRWWEEMFGSERKAGFKETVFEDMNGRSIRL", "text": "SUBCELLULAR LOCATION: Nucleus membrane; Single-pass membrane protein."}
{"protein": "MGGEQEEDRFDGMLLAMAQQHEGGVQELVNTFFSFLRRKTDFFVGGEEGMAEKLITQTFNHHNQLAQKARREKRARQETERREKAERAARLAKEAKSETSGPQIKELTDEEAERLQLEIDQKKDAENQEAQLKNGSLGSPGKQEAEEEEEEDDEKDKGKLKPNLGNGADLPSYRWTQTLSELDLAVPFCVNFRLKGKDVVVDIQRRHLRVGLKGQPAIVDGELYNEVKVEESSWLIEDGKVVTVHLEKINKMEWWSRLVSSDPEINTKKINPENSKLSDLDSETRSMVEKMMYDQRQKSMGLPTSDEQKKQEILKKFMDQHPEMDFSKARFN", "text": "FUNCTION: Plays a role in neurogenesis and neuronal migration. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (By similarity). Necessary for cytokinesis and cell proliferation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus Cytoplasm, cytoskeleton, spindle Midbody Note=A small proportion is nuclear, in a punctate pattern (By similarity). In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells (By similarity). Localizes to the mitotic spindle in a EML4-dependent manner (By similarity). SIMILARITY: Belongs to the nudC family."}
{"protein": "DRVYIHPF", "text": "SIMILARITY: Belongs to the serpin family."}
{"protein": "MNKPKIFIDGEAGTTGLQIYSRLNERDDIELVSIAASKRKDADERAKLLNSVDVAILCLPDDAAREAVSLVHSSQVKILDASTAYRTAQGWVYGFPELNPGQREKIANAQFVSNPGCYPTGFLACVRPLIAQGILPSSFPITINAVSGYSGGGKSLIQKYDSFHEQQKGATSDYPFGIYGLQFGHKHVKEMHQHSGLASPPLFIPAVGDFEQGMLVQIPLPLWTLDNPPSGEEIHQAIAQYYQGEKFVQVASFKDPSLLRDGTFLDATAVNGTNIVQVFVFANDNTKEALLVARLDNLGKGASGAAVQNLNIMLGLPEELGL", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2 subfamily."}
{"protein": "MRPSTDTMEADTAATHRNFITKVDVPDHAHYTVAFFVSVIGTLGVTGNALVQFAFYSNKKLRNLPNYFIMNQAASDFLMAFTQSPFFFINCLNREWIFGELGCKLYAFLGALFGITSMINLLAISLDRYMVITRPLEAMKWNSKRRTTIAILLVWLYSLAWSLAPLVGWSSYIPEGLRTSCTWDYVTYTASNRSYTMMLCCFVFFIPLAIISYCYLFMFLAIRKTSRDVERLGIQVRKSTIIRQKSIRTEWKLAKIAFVVIVVYVLSWSPYACVTMISWSGHANILSPYSKTVPAVIAKASTIYNPFIYAIIHQKYRKTLADKVPCLRFLAPNKRKDCTSSSFSGSSYRDSVISRTSTAIRRQSTAASRHASASKTAAGASSYSSSDRVFGDVEMDPIDWRSGASFRRHSSRGSTRRDRLLKKQQMERTNKSAAHKQPSPSTKMSATHCKNKTVSSSVNMAAAPPQLVLIRKRSQSLTNGLSDAGKKTTVANGTPGNHKSKSADLHFRNLPALDQALNVPRIIVISPTSEDCLVKHESSFTDDGSVGTVVDEDSLEDNDVV", "text": "FUNCTION: Photoreceptor implicated in non-image-forming responses to light. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MASIQFIQGVDEDIIPTVRLTRSRDGQTGTAVFRFVQPKLLQQQGEITGMYMIDEEGEIVTREVQAKFVNGQPQIIEALYVMKNAQAWERFMRFMNRYAEAKGLSFQRS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the Psb28 family."}
{"protein": "MKTLSDISESVLIPTNSSLDKLLGGGIEKGCITQFYGPPGSGKTNIALKILYEATKNGSKAIYMDTEGGLSLERIQQIAGTDFGSISKNIYILEPKSFDEQILDIQNIEDILKKDKSIDMLIIDSIVALYRVEDGDPSEINKRLGRLMAKLLRLSREYNVAIVITNQIYSPFDSDDLIIEPIGGTVLKYWSKIIIEIEKSVDSLKRTATLQRHKTKAPGQSIKFEIIDRGII", "text": "FUNCTION: Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange. SIMILARITY: Belongs to the eukaryotic RecA-like protein family. RadB subfamily."}
{"protein": "MPTGCEFPMIKTFENALTAADFESTVELTNFPAVFRGCASVWDAYSKWNPFNSGLDYLEERAGSVEVEAMLSRTAPVFNGDIRSHERVSLPFSDFIRFCKQHMRGKGNGSGVDAKSADLNPMCEDYRPGQIYLAQFPILNDEKEEKVLLKILRQDIQTPTFLDAKSLSSINFWMNSAEARSSTHYDPHHNLLCVVSGRKKVVLWPPSASPSLYPMPIYGEASNHSSVGLENPNLSDYPRAEHSLKQSQEITLNAGDAVFIPEGWFHQVDSDELTVAVNFWWQSNYMSNMPEHMDSYYLRRITRSLLVSKPSSTDLRHLSEHIDQSRIEMAEGGNDNIGNESIKKGLSTLHEKASLHDLDPSASQALHDLISLVHDHVNAVDTSKGLQHTSPSCSEGGEKSKFLVNAMSCLEDDRVAHLLWNLEASRLRDVLLAMALELSYLKLLVKMEIFVLVLHKIFETLEALILHMLSPIAAEVLTQKFDEIDQQTGEEDRTQFFREFYSAFDDEAAAMDIILSRKEAFAFQVCSLASLCRLRTYHKLKGEKFSASY", "text": "FUNCTION: May function as histone H3 lysine demethylase and be involved in regulation of gene expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the JARID1 histone demethylase family."}
{"protein": "MTAPRDPDALIRRAGRPNPDFDQHFLIDDRVLDRIPTYADGFDRGHVLEIGAGTGALTDRLLSVADRVTAVERDESYASFLREEFADAIAAGDLDVVAGDALAVDLPAFTCAVSNLPYGVASEVTFRLLPAGKPMVLMYQLEFAERMAADPGTSEYGRLSVATQHYADVSIVETVPAAAFDPQPRVESAVVRVTPRDPDYVVADEAFFLSFVKALFTQRRKTTRNAIRNTAHISGLDDPDAVVAAVDDDVLGTRPGSLSPATFAALANVAWGVETAPGPDPQ", "text": "FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily."}
{"protein": "MLCVGRLGGLGARAAALPPRRAGRGILEAGIRARRVSTSWSPVGAAFNVKPQGSRLDLFGERRGLFGVPELSAPEGFHAAQEKALRKAELLVGRACSTPPGPQTVLIFDELSDSLCRVADLADFVKIAHPEPAFREAAEEACRSIGTMVEKLNTNVDLYQSLRKLLADKKLVDSLDPETRRVAELFMFDFEISGIHLDKEKRKRAVDLNVKILDLSSTFLMGANFPNKIEKHLLPEHIRRNFTSAGDHIIIDGLHAESPDDLVREAAYKIFLYPNAGQLKCLEELLSSRDLLAKLVGYSTFSHRALQGTIAKNPETVMQFLEKLSDKLSERTLKDFEMIRGMKMKLNPQNSEVMPWDPPYYSGVIRAERYNIEPSLYCPFFSLGACMEGLNILLNRLLGISLYAEQPAKGEVWSEDVRKLAVVHESEGLLGYIYCDFFQRADKPHQDCHFTIRGGRLKEDGDYQLPVVVLMLNLPRSSRSSPTLLTPGMMENLFHEMGHAMHSMLGRTRYQHVTGTRCPTDFAEVPSILMEYFANDYRVVNQFARHYQTGQPLPKNMVSRLCESKKVCAAADMQLQVFYATLDQIYHGKHPLRNSTTDILKETQEKFYGLPYVPDTAWQLRFSHLVGYGAKYYSYLMSRAVASMVWKECFLQDPFNRAAGERYRREMLAHGGGREPMLMVEGMLQKCPSVDDFVSALVSDLDLDFETFLMDSE", "text": "FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase M3 family."}
{"protein": "MRRKAVLLTVVLSLSGGSAQAMGLLDAWELALRNDAQLRAAGFERDAGQEEVAIGRAGLLPSLQYTYGANYSHSKVTQRDRTLNNTTKRDYDNYVSTLTLRQPLLDYAAWARYQQGVTRKLMADQRFRDRSQDLMVRLYQSWSEALLAQEKLMLLDAQRRAYQEQLALNRRLLAAGEGTQTDLRETEARYTVTEAQRIEQEDTLDAAMTDLENMMGSPLQIQDLSPLALDTLPDNVTENRSLSQWRELTVRHNAKLAVQRENVDYSRYEIERNRAGHLPTLDLVASTRNSLSESEYNYNQKYDTQTVGLQVRVPLYSGGAVSASMRQAAAEYQQSQAELDNQTRQTFAELRRQFNLCANGAAKIRAWQMSVAAAEEAIRATRQSVAGGERINLDVLMAEQEWYNARRELTEVKYRWLQAWLNLRYTAGTLNEQDMMQLAAWFQSAPVINKTGINAATGNKTN", "text": "FUNCTION: Involved in the secretion of proteases A, B, C and G. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family."}
{"protein": "MSREQRGPNEKLGTVLALAGISNAGLARRVNDLGAQRGLTLRYDKTSVARWVAKGMVPQGAAPHLIAAAIGAKLGRPVPLHEIGLADADPAPEVGLAFPRDVGEAVRSATELYRLDLAGRRGGGGIWQSLAGSFSVSAYATPASRWLITPADPSVARDPTAAQAAILGARGGGSGSPGGAGARGPGAAPDARGAHLLHPGGATPGAAGSVPLQPGPEAVADASPLRVGHSDVSKLREAAQDARRWDSKYGGGDWRSSMVPECLRVDAAPLLLGSYTDEVGRALFGASAELTRLAGWMAFDTGQQEAAQRYYIQALRLARAAADVPLGGYVLASMSLQATYRGFADEGVDLAQAAVERNRGLATARTMSFFRLVEARAHAKAGDAPAAGAALKGAESWLERSRAGDSDPPWLGFYGYDRFAADAAECYRDLKAPRQVRRFTEQALSRPTEEFVRSHGLRLVVSAVAELESGNLDAACAAGTRAVEVAGRISSARTTEYVRDLLHRLEPYGDEPRVAELRERARPLLVTPG", "text": "FUNCTION: Might be a catalyst/regulator pair of proteins involved in the temporal controlled sporulation process. The decrease in level of the smaller protein early in sporulation may relieve negative regulation of the activity of the larger protein."}
{"protein": "MLVFEILVVLAAIFLGVRLGGIAIGYAGGLGMIVLCLGLGLKPGSIPIDVILIIMSVIAAIAAMQVAGGLDYLVHLAEKLLRSQPKHITFLAPVVTYFMTLLAGTGHTAFSTLPVIAKVAKEQGVKPSVPLSIAVVASQIAITASPVSAAVVFMSGALEPLGVGYLQLLAICIPTTFIGCMITAFICNLFNTDLSKDPVYQERVAKGMVKLRGQTQYVAKPGAKLSVLIFLVGILAVVFYATAISKNVGLIQNPIVGRDSAIMMFMLTTATLIAMFAKIDTDAVLNASTFKSGMTACICVLGVAWLGDTFVSNHINDIKGFAGGILEGHPWMLAITLFFASMLLYSQAATAKALIPAAIALSVDPVTLIASFAAVSALFVLPTYPTLLAAVQMDDTGSTRIGKFVFNHPFIVPGVLAIGISVALGFIVAPILL", "text": "FUNCTION: Responsible for the transport of C4-dicarboxylates. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DcuA/DcuB transporter (TC 2.A.13.1) family."}
{"protein": "MSPRKTYILKLYVAGNTPNSMRALTTLREILQTDFKGVYALKVIDVLKNPQLAEEDKILATPTLAKILPPPVRRIIGDLSDRERVLIGLDLLFEELSESDFFSGSPDSEFSSDEGKS", "text": "FUNCTION: Component of the KaiBC clock protein complex, which constitutes the main circadian regulator in cyanobacteria; it may modify the ATPase activity of KaiC. FUNCTION: May be a metamorphic protein which reversibly switches between an inactive tetrameric fold and a rare, thioredoxin-like monomeric fold (KaiB(fs)). KaiB(fs) binds phospho-KaiC, and perhaps clock output effectors. SIMILARITY: Belongs to the KaiB family."}
{"protein": "MASATTSDHAKQAGGAHSRQRDSGLLDQLGKLFGQEGSRKVPEKGKEPATRSVLMAPTTHKAHQGARRQTDDSPVVHFFKNMMSPKKAPVQQKAKSGASRAITKFIWGTDGQRAHYGAAGSSKSKDGFRGRRDGSGTLSSFFKMGKKGEGSPARR", "text": "FUNCTION: This protein may function to maintain proper structure of myelin. SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin. SIMILARITY: Belongs to the myelin basic protein family."}
{"protein": "MSIEVNWGTATSGPDGEALAERIRSFIHDKFQQVPLPRFIRSVQVHSFDFGTVAPDLEIKDFCEPFADFYEDDEDGDSGSEISEELQHRTHDNPWDRTQSELNETSFRDDRPVTSHHALRDPFDEDFRQHTSSPLRSPIALGDHLNPHFLPRAGTPGIPGGTSTLGYHLMSLGGLSGTQTPLAAVAGGSPFTTNWTDPSPMGQGNKTGIRPSPLHRADADIDSSNPASRPSTASTHPSGSNRSSHPDGHPEHNDDPISSSENPLLQNQPPPRMRERRPEDFQILCHVKYAGDIRLSLTAEILLDYPMPSFVGLPLKLNVTGITFDGVAVIAYIRKRVHFCFLSPEDAEALVGSGSYSGQQETPGPSTGSSGGGNPSPHQKGLSLLQEIRVESEIGRKEDGKQVLKNVGKVERFVLAQVRRIFDEELVFPSFYTFLI", "text": "FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. Mdm12 is required for the interaction of the ER-resident membrane protein mmm1 and the outer mitochondrial membrane-resident beta-barrel protein mdm10. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MDM12 family."}
{"protein": "MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQMLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPHPAMLNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTMDFFEGCWIEQYNFGGFPGSDDYPQFLRRMNGLGHCVGASLWPKELFDERKNFLEITTAVAQMENWMVWVNDLMSFYKEFDDERDQISLVKNFVTCHEITLDEALEKLTQETLHSSKQMVAVFADKDPQVMDTIECFMHGYVTWHLCDARYRLHEIYEKVKDQDTEDAKKFCKFFEQAANVGAVAPSEWAYPQVAHLANVRAKGDVKEAQKPILSSIELVE", "text": "FUNCTION: TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway. SIMILARITY: Belongs to the trichodiene synthase family."}
{"protein": "MFFSLLLMLGLTEAEKIKICLQKQVNSSFSLHNGFGGNLYATEEKRMFELVKPKAGASVLNQSTWIGFGDSRTDKSNSAFPRSADVSAKTADKFRSLSGGSLMLSMFGPPGKVDYLYQGCGKHKVFYEGVNWSPHAAINCYRKNWTDIKLNFQKNIYELASQSHCMSLVNALDKTIPLQATAGVAKNCNNSFLKNPALYTQEVNPSVEKCGKENLAFFTLPTQFGTYECKLHLVASCYFIYDSKEVYNKRGCDNYFQVIYDSSGKVVGGLDNRVSPYTGNSGDTPTMQCDMLQLKPGRYSVRSSPRFLLMPERSYCFDMKEKGPVTAVQSIWGKGRESDHAVDQACLSTPGCMLIQKQKPYIGEADDHHGDQEMRELLSGLDYEARCISQSGWVNETSPFTEEYLLPPKFGRCPLAAKEESIPKIPDGLLIPTSGTDTTVTKPKSRIFGIDDLIIGLLFVAIVEAGIGGYLLGSRKVSGGGVTKESAEKGFEKIGNDIQILRSSTNIAIEKLNDRISHDEQAIRDLTLEIENARSEALLGELGIIRALLVGNISIGLQESLWELASEITNRAGDLAVEVSPGCWVIDNNICDQSCQNFIFKFNETAPVPTIPPLDTKIDLQSDPFYWGSSLGLAITAAISLAALVISGIAICRTK", "text": "FUNCTION: Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O- acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the influenza viruses hemagglutinin family."}
{"protein": "MLQRIYLDNNATTRIDPKVKEIMDPFLRDHYGNPSSLHQFGTETHPAIAEALDKLYKGINARDIDDVIITSCATESNNWVLKGVYFDECLKKGKNHIVTTVAEHPAVRSTCNFLESLGVEVTYLPINEHGSITAEQVKEAITEKTALVSVMWANNETGLIFPIEEIGAICKEKGVLFHTDAVQAIGKIPVDVLKANADFLSFSAHKFHGPKGIGGLYIRSGVGLTPLFHGGEHMNGRRSGTLNVPYIVGMGEAMKLAVEHLDYEKEVVGKLRDKLEEALLKIPDVMVVGDRIHRVPNTTLVSVRGIEGEAMLWDLNRSNIAASTGSACASEDLEANPVMVAIGASKELAHTAIRLSLSRFNTEAEIDKTIEVFSQAAVRLRNISSSY", "text": "FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily."}
{"protein": "MFIWQRKSILLGRSILGSGRVTVAGIIGSSRKRYTSSSSSSSSPSSKESAPVFTSKELEVARKERLDGLGPFVSRLPKKWIPYAELMRLEKPVGTWLLYLPCSWSILMGAMMQGATLSATAGMLGIFGVGALVMRGAGCTINDFLDRKLDQRVIRSVERPIASGRVSPRRALVFLGAQTLVGMGVLSLLPAQCWWLGLASLPIVFTYPLFKRFTYYPQAALSACFNWGALLGFPAMGVMSWPTMIPLYLSSYLWCMTYDTIYAHQDKKFDIKAGIKSTALAWGPRTKSIMKAMSASQIALLAVAGLNSGLLWGPGFIGGLGVFAYRLFSMIKKVDLDNPKNCWKYFNANINTGLYFTYALAVDYILRLFGFL", "text": "FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
{"protein": "MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNRDEAARTNGHPRGDRRRDLGLPPDSASTVLSSELESSSFIDSDEEDNTSRLSSSTEQSTSSRLVRKHKCRRRKQRLRQTDRASSFSSITDSTMSLNIITVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTIPRADPVRPIDPAAWLSHTAALTGALPRYGTSPCSSAITRTSSSSLTSSVPGAPQLEEAPLTVKSDMSAIVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSMLKHGFLRHTVNKITFSEQCYYVFGDLCSNLASLNLNSGSSGASDQDTLAPLPHPSVPWPLGQGYPYQYPGPPPCFPPAYQDPGFSCGSGSAGSQQSEGSKSSGSTRSSHRTPGREERRATGAGGSGSESDHTVPSGSGSTGWWERPVSQLSRGSSPRSQASAVAPGLPPLHPLTKAYAVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM", "text": "FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytosol Cytoplasmic vesicle Note=Localizes at the cell membrane upon interaction with frizzled family members. SIMILARITY: Belongs to the DSH family."}
{"protein": "MLRLNLRFLSFLLCIIQSVELQAAPSVPTFLTENGLTYCTHASGFSFNPQTADAGTSMNVVTEQIYNKLFDIKNHSATLTPMLAQSYSISADGKEILLNLRHGVKFHQTPWFTPTRDFNAEDVVFSINRVLGGHNTYLPTLAETNVTYSNPQYRVFHEQARKVRFPYFDSIKLNEKIKSVTALSPYQVKIELFAPDSSILSHLASQYAIIFSQEYAYQLSADDNLAQLDTHPVGTGPYQVKDYVYNQYVRLVRNENYWKKEAKIEHIIVDLSTDRSGRLVKFFNNECQIASYPEVSQIGLLKNDDKHYYMQSTDGMNLAYLAFNFDKPLMRDHEIRAAISQSLNRARIIHSIYHNTATVANNIIPEVSWASSVNTPEFEFDYNPKIAKNKLADKNLLLNLWVINEEQVYNPAPFKIAEMIKWDLAQAGVKVKVRAVTRPFLTAQLRNQSENYDLILSGWLAGNLDPDGFMRPILSCGTKNELTNLSNWCNEEFDQFMDRAITTSHLSSRAKAYNEAQELVLRELPIIPIANVKRILVANSRVKGVKMTPFGSLDFSTLYFIQEKY", "text": "FUNCTION: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
{"protein": "MRGLRWRYTRLPSQVEDTLSGEEGNEEEEEEEAAPDPAAAPEDPTVPQLTEASQVLSASEIRQLSFHFPPRVTGHPWSLVFCTSRDGFSLQSLYRRMEGCSGPVLLVLRDQDGQIFGAFSSSAIRLSKGFYGTGETFLFSFSPQLKVFKWTGSNSFFVKGDLDSLMMGSGSGRFGLWLDGDLFRGGSSPCPTFNNEVLARQEQFCIQELEAWLLS", "text": "SIMILARITY: Belongs to the OXR1 family."}
{"protein": "MDYQQLANQIKQWAIELGFEKVGICDVDLSEHEPALQAWLDAGYHGEMDWMARHGMMRARPAELLPGTLRVISARINYLPPQAQFASNLSDPNQAYISRYALGRDYHKLVRNQLKKLGEKIEQEVGKLGYRPFVDSAPILERPLAQKAGLGWTGKHSLILDKENGSWFFLGELLVDIPLPVDEPSENQCGKCTACITSCPTNAIVAEGVVDARRCVSYLTIEYSGVIPLEFRRAMGNRIYGCDDCQLVCPWNRFAPLTQQSDFHRRQSLNNADLVVLFEWDEATFLKNMEGSAIRRIGHQQWRRNLIIAMGNAPYSPRIIDTLQRHLGQSELLDEHIHWALEEQTQKTATPRQHARLIRIIEKGLPRDA", "text": "FUNCTION: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the QueG family."}
{"protein": "MASQHLQANPHAEGEWSTGFCDCFSDCQNCCITWLCPCITFGQVADIVDRGNTSCGTAGALYVLLAAITGCGCLYSCIYRGKIRAQYNIRGDGCTDCLKHFCCELCALTQEYRELKHRGFDMSLGWAGNVEKQQNQGGVAMGAPAFQGGMSR", "text": "FUNCTION: May be involved in heavy metals transport. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cornifelin family."}
{"protein": "MDISTDNPDHGFQFPGTFELSAMGAAERGLETELPRLLAATGVELLQESVSWKHSSSGKYVSVKIGFRAESREQFDAAHQALRDHPEVKWTL", "text": "SIMILARITY: Belongs to the UPF0250 family."}
{"protein": "MMVLDKEDGVPMLSVQPKGKQKGCAGCNRKIKDRYLLKALDKYWHEDCLKCACCDCRLGEVGSTLYTKANLILCRRDYLRLFGTTGNCAACSKLIPAFEMVMRARDNVYHLDCFACQLCNQRFCVGDKFFLKNNMILCQMDYEEGQLNGTFESQVQ", "text": "FUNCTION: May be involved in gene regulation within neural lineage cells potentially by direct DNA binding or by binding to other transcription factors. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNGRADEEGLQRKQRLIRLLHQTNPYPQGLGTARQRRNRRRRRKQHWRQLVALANSIYTFPDPPADSPLDRAIQRLQGLTIQELPDPPTNLPESSESTNNNQGLAETYNSLPAIWVRVDPRSAPGPCKDYERDSCERVERLVGGNGTDRQGNTCSSKKDQAGGRTCPPVRGSGINRETL", "text": "FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre- mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs (By similarity). SUBCELLULAR LOCATION: Host nucleus, host nucleolus. Host cytoplasm. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm."}
{"protein": "MTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL", "text": "FUNCTION: Enoyl-ACP reductase of the type II fatty acid syntase (FAS- II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls (PubMed:25227413). Catalyzes the NADH-dependent reduction of the double bond of 2-trans- enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway (PubMed:7599116). Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates (PubMed:7599116). The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids (PubMed:25227413). FUNCTION: Enoyl-ACP reductase of the type II fatty acid syntase (FAS- II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls. Catalyzes the NADH- dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway. Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates. The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids. FUNCTION: Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH) (PubMed:8284673, PubMed:12406221, PubMed:16906155, PubMed:17227913). Overexpressed inhA confers INH and ETH resistance to M.tuberculosis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA (PubMed:9417034, PubMed:16906155). Similarly, the ETH-NAD adduct binds InhA (PubMed:17227913). FUNCTION: Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH) (PubMed:12406221). Overexpressed inhA confers INH and ETH resistance to M.bovis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA (By similarity). Similarly, the ETH-NAD adduct binds InhA (By similarity). FUNCTION: Enoyl-ACP reductase of the type II fatty acid syntase (FAS- II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls. Catalyzes the NADH- dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway. Shows preference for long-chain fatty acyl thioester substrates, and can also use 2-trans-enoyl-CoAs as alternative substrates. The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids. FUNCTION: Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH). Overexpressed inhA confers INH and ETH resistance to M.tuberculosis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA. Similarly, the ETH-NAD adduct binds InhA (By similarity). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily."}
{"protein": "MKVLWAALLVTFLAGCQAKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGTSAAPVPSDNH", "text": "FUNCTION: (Microbial infection) Through its interaction with HCV envelope glycoprotein E2, participates in the attachment of HCV to HSPGs and other receptors (LDLr, VLDLr, and SR-B1) on the cell surface and to the assembly, maturation and infectivity of HCV viral particles (PubMed:25122793, PubMed:29695434). This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (PubMed:29695434). FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:6860692, PubMed:1911868, PubMed:14754908). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:6860692, PubMed:2762297, PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:14754908, PubMed:23620513). Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:6860692, PubMed:2762297, PubMed:9395455). As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL) (PubMed:6860692, PubMed:1911868). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (PubMed:2762297, PubMed:1917954, PubMed:7768901, PubMed:8939961, PubMed:12950167, PubMed:20030366, PubMed:2063194, PubMed:8756331, PubMed:20303980, PubMed:1530612, PubMed:7635945). Finally, APOE has also a heparin-binding activity and binds heparan- sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:9395455, PubMed:9488694, PubMed:23676495, PubMed:7635945). A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:23676495, PubMed:29516132). APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues (PubMed:2762297, PubMed:29516132). By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis (PubMed:2762297, PubMed:1917954, PubMed:29516132). APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis (PubMed:9395455, PubMed:14754908, PubMed:23620513). First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes (PubMed:9395455). APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting (PubMed:8939961, PubMed:25173806). APOE is also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells (By similarity). Binds to the immune cell receptor LILRB4 (PubMed:30333625). APOE may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP (PubMed:28111074). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Secreted, extracellular space, extracellular matrix Extracellular vesicle Endosome, multivesicular body Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins (PubMed:1911868, PubMed:8340399). Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner (PubMed:9488694). Lipidation induces the release from the extracellular matrix (PubMed:9488694). Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. SIMILARITY: Belongs to the apolipoprotein A1/A4/E family."}
{"protein": "MNIQQVIAITGAGSGIGLELVRSFKAAGYCVSALVRNEEQEAGLRSEFKDAIEIVAGDVCDHATNEKLVNKAVARFGHLDCFIGNAGIWDYMLGVDEPWEKLSGSFEEIFDINVKSYFSGISAALPELKKTNGSVVVTASVSSYAAGGGGSCYIASKHAVLGMVKALAYELAPHIRVNGVAPGGTVTSLAGPASAGFDKTKMKDMPGIDDMIKGLTPLGFAARPEDVVAPYLLLASREQGKFITGTVIGIDGGMALGRK", "text": "FUNCTION: Catalyzes the oxidation of naphthalene dihydrodiol into 1,2- dihydroxynaphthalene. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSLRPDEVDVRILEENLLKTNTLVESMVASCQKISNSSYKAEITIEPISGMQRRMQVYETNLNNCLKVVDGIRDYAKVTAREEKIIRQGPEAVGLPAYVAAIQSVIRVNDEIEQRKLHSIPKVKEKAVDLARMGTSGLKENLATILKEESNPIDPVPILASGKPFPLMSPKNADKLNELMGIVARFSARQDNTYVDSRSRYLAMSLSPVASKVKPTVRTGKAPYDKQSNGIHIYAEALLKMLQAEHDNLRCAFPKDEARVKQYFTQLAQTPLQTYQAAGEEISNHVQRNISTDALLIFELIEGTVALKRGLEPLTNSAAPLDRLIQSSYNVSQGVFTEILKICEARVQQVMTLPSDNGVCDATVEVMSRIRRFAEYKDSAVLAISGMKYQQWIPQPRPAWMSTFSSAPAGYTTTKPQELLSAVFSDSIDAFYVTLEMKAKQLNPKKPSQVGFFLLTNLTLIERFVTKSEVYKVLGGQGRERLEKLRKRGLNLFLEGWKATASLLMDTTVVNSKGSLSSKDRELVKDKFKTFNADFEELVKNHKTYTITDPALKQLLAKEVAFICPLYHRYYDKHIGGDFSKNVDKYIKYDKAQFDRVLQELGD", "text": "FUNCTION: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst (By similarity). SUBCELLULAR LOCATION: Bud Bud neck. SIMILARITY: Belongs to the EXO70 family."}
{"protein": "MKDLDFSKKPLIGVVHLKPLPGSPRYGGDFEEVIEWAIRDAKTYEEAGFDGIIVENFGDSPFSKTLPREVIPAFTVVAKAVKKEVSLPLGINALRNDCIVAYSIAHAVGGSFIRVNVLTGVAFTDQGIIEGCARELWNVKRIIGGDILTLADVHVKHAVHFTNFEDAVKDTVERGLADGIIVTGRRTGESISLEDLILAKRVSSIPVLVGSGVNPRNFRTLFKYADGFIVGTWVKENGKINNPVSLERAKILVRMKNSLMGV", "text": "SIMILARITY: Belongs to the BtpA family."}
{"protein": "MAQRKMIVFPTKNELSEAMAEYTANLSAKFIKEKGLFTVVLSGGDLIDWLCKLVQPPYIDSIEWPKWHVFWVDERVCAWEDPDSNYKLAMEGFLSKVPIPDKNIYAIDKHLAADGNAEHCATLYEECLKNLVKEKIIPISKKTGYPEFDLQLLGMGPDGHMASLFPNHPQINEKQKWVTYITDSPKPPPKRITFTLPVINSTLYNLMAICDKAPAKSVAEIMKHNNLSLPSAHLSAQVENVWYLDQAAASEL", "text": "FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily."}
{"protein": "MQMPRRFNTYCPHCNEHQEHEVEKVRSGRQTGMKWIDRQRERNSGIGNDGKFSKVPGGDKPTKKTDLKYRCGECGKAHLREGWRAGRLEFQE", "text": "FUNCTION: Binds to the 23S rRNA. Binds deacetylated tRNA in the E site; when the tRNA binds a stretch of 7 amino acids are displaced to allow binding. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family."}
{"protein": "KAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVS", "text": "FUNCTION: Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSLNQYIRPVRTKLSHISFIRNISITQSSINTTIKNDESISKTTTIPENIQQAKELAGYRALEIPEFKTLGSAEGTTATATGSSSILSINVPPSVPVYIRRGSLLSIYGIQEISSIDSVRSQLQFPNFWKRLIYGGYVSGYQKLISTTPFSLLISSKSRSSGSGSGSGFEKSFVNLVLDGTTDWAILDKSALQVYTGNSLSITMHKLPKFISKKLSRSLKKDKKSKTNTNKLETGLFSWKKLGYTLLSGRGKVGLVGNGSSSGYGSSIYNINLNQNEEILINKNNLLGITVNGPYDLQNCIVKYEFPIINNANPTNTNTNINIKEPVTIVKPKLIQPTTWNLIVLKLKNFNNGFKKIFQIINKYTLGLKTTSYNYLAGNQDFIKVIGPRNLLLQSNTNKSHRGFYNIIPRNKPQAKVWPTNQTTTKVDESSSFSTPKDYLNYVTIEPGKGAVFKSTLDFSETVESIENKNKNKNK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM24 family."}
{"protein": "MPIETEPNRTRKNFEPKRFGGSLFILFTLLLFLNLFVLRGPRFPITAYSDFITQVEAGQVERVEVRPDRIRYILKSDQYGFNEGTETAAVFDTVPVGIDLELPKFLREHDVQYFAPPPSSLSWLPTLLGWVVPPLIFFGIWSWLINRNQGAGPAALTVGQSKARIYSEGSTGVTFDDVAGVEEAKTELLEIVDFLAHADKYTRLGAKIPKGVLLVGPPGTGKTLLAKAIAGEAKVPFFSISGSEFIELFVGIGAARVRDLFEQAKQQAPCIVFIDELDALGKARGGPGGFTGGNDEREQTLNQLLSEMDGFDPNVGVILLAATNRPEVLDPALLRPGRFDRQIVVDRPDKMGREAILKVHVRGVKLAEDINLTKLAVRTPGFSGADLANLVNEAALLAARQSRDAVVMSDFNEAIERVVAGLEKKSRVLNDLEKKTVAYHEVGHAIVGSLMPGAGTVEKISVIPRGIGALGYTLQLPEEDRFLITASELRGRIATLLGGRSAEELIFGVVSTGASDDIQKATDLAERYVTLYGMSDELGPIAYEKAQQQFLEGVPNPRRTVGPQVVEAIDQAVKDVVDGAHHMALSILSINQDMLQLTASHLLEKEVLESQELHSLLSQPQFPPDMDEWLQTGKLPQGKELIQTTLNSHQLIGIN", "text": "FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein; Stromal side. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family. SIMILARITY: In the central section; belongs to the AAA ATPase family."}
{"protein": "MTELKAKGPRAPHVAGGPPSPEVGSPLLXRPAAGPFQGSQTSDTLPEVPAIPISLDGLLFPRPCQGQDPLDEKTQDQQSLTDVEGAYSRAEATRGTGGSSSRPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPASGSPHWSGVPVKPSPQPTAVEVEEEDGSESEDSAGPLLKGNPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTTMDFIHVPIRPLNHALLAARTRHLLEEESYDGGAGAASAFAPPRSSPSASSTPVAVGDFPDCAYPPDADPKDDAYPLYGDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSSSSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGAGGCLLPRDGLPSTSASAAXAGAAPALYPALGLNGLPQLGYQAAVLKEGLQQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVMRALDAVALPQPVGIPNESQALSQRFTFSPGQDIQFFPPLINLLVSIEPDVIYAGHDNSKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK", "text": "FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family."}
{"protein": "MIDQIIDEVTDSDPYQELLVTADGVAEGTLGVRLDKWLAEQLPELSRSRCQKLIESGQVQRNGLVCQDKNLILKTGDRLVVNIPELIPLDVVAQNIPLDILYEDEQLIIINKPAGLVVHPGPGHPDGTVVNALLAHCPDLAGIGGVQRPGIVHRLDKDTTGAMVVAKTELALHNLQVQLKEKTARRLYWGIVYGSPKEIQGTVNLPVGRHPGDRQKMGIVPVEKGGREAVTHWRLLERIGNHSWLEFQLETGRTHQIRVHSKQMGHPLVGDNLYTSPGSVNVNLPGQALHAHQLSLIHPVSGEIITAIAPMPAHFEKLLVYLRQRIP", "text": "SIMILARITY: Belongs to the pseudouridine synthase RluA family."}
{"protein": "MAKIGLFFGSNTGKTRKVAKSIKKRFDDETMSDALNVNRVSAEDFAQYQFLILGTPTLGEGELPGLSSDCENESWEEFLPKIEGLDFSGKTVALFGLGDQVGYPENYLDALGELYSFFKDRGAKIVGSWSTDGYEFESSEAVVDGKFVGLALDLDNQSGKTDERVAAWLAQIAPEFGLSL", "text": "FUNCTION: Flavodoxins are low-potential electron donors to a number of redox enzymes. NifF is the electron donor to nitrogenase, and is thus implicated in nitrogen fixation. Does not function as an electron donor to nitrite reductase. SIMILARITY: Belongs to the flavodoxin family."}
{"protein": "MAIIIGADTAGSKLKDVVKDFLVGENFEVVDVTQDGQDFVDVTLAVAAEVNKQEENLGIVIDAYGAGPFMVATKIKGMVAAEVSDERSAYMTRGHNNSRMITMGSEIVGEGLAKNIAKGFVNGKYDGGRHQIRVDMLNKMC", "text": "SIMILARITY: Belongs to the LacAB/RpiB family."}
{"protein": "MAPRSSTSKSATREKKDHKKAPIKKAIAKKDTKPTPTKGKAASASTTPVKKDVTPVKADTKKKIHKTKTMKETVSDAKKTVHAAAGDKKLSKKRPAKEAAKKAINPGKKAAAQPKSTKKEVKKDNKTAKKETKKDHKPAKKEAKKETKPAKKDAKKSSKPAKKN", "text": "FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Macronuclei."}
{"protein": "MFGGGGGLNPRKMKQMMNQMGIDLEEIDAEEVVIRTADEELVFDDAEVQLMDAQGQQTYQVVGEPESRERGDSGSEDDSETESGGEFSEDDVEIVAQRAGVSESTARETLEETGDLAAAVQKLE", "text": "FUNCTION: Contacts the emerging nascent chain on the ribosome. SIMILARITY: Belongs to the NAC-alpha family."}
{"protein": "MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELHKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMTQILPCIKELVSDANQHVKSALASVIMGLSPILGKDSTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPVLEKLTQDQDVDVKYFAQEALTVLSLA", "text": "FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (By similarity). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway. Dephosphorylation of AKT1 is essential for regulatory T-cells (Treg) homeostasis and stability (By similarity). SUBCELLULAR LOCATION: Chromosome, centromere Nucleus Cytoplasm Lateral cell membrane Cell projection, dendrite Note=Centromeric localization requires the presence of BUB1. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family."}
{"protein": "MEFAELIKTPRVDNVVLHRPFYPAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGSLGTIIIKCKDFRIIQLDIPGMEECLNIASSIEALSTLDSITLMYPFFYRPMFEVIEDGWHSFLPEQEFELYSSATSEWRLSYVNKEFAVCPSYPPIVTVPKSIDDEALRKVATFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYIIDTRSLNVAQQTRAKGGGFEQEAHYPQWRRIHKSIERYHILQESLIKLVEACNDQTHNMDRWLSKLEASNWLTHIKEILTTACLAAQCIDREGASILIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCNTKQKWEAPVFLLFLDCVWQILRQFPCSFEFNENFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNQPSELSKFTNPLFEANNLVIWPSVAPQSLPLWEGIFLRWNRSSKYLDEAYEEMVNIIEYNKELQAKVNILRRQLAELETEDGMQESP", "text": "FUNCTION: Acts as an adapter for myotubularin-related phosphatases (PubMed:19038970, PubMed:22647598). Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5- bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols (PubMed:19038970, PubMed:22647598). Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3- phosphate (PubMed:22647598). The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970). Stabilizes MTMR8 protein levels (PubMed:22647598). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580). Negatively regulates autophagy, in part via its association with MTMR8 (PubMed:22647598). Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 (PubMed:19038970, PubMed:22647598). Does not bind mono-, di- and tri- phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (PubMed:19038970). SUBCELLULAR LOCATION: Cytoplasm Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, perinuclear region Endoplasmic reticulum Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the perinuclear region (PubMed:19038970). Partially localizes to the endoplasmic reticulum (PubMed:19038970). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily."}
{"protein": "MTRVIHTGDTHLGYQQYHSPERRQDFLDAFERVVADALDGDVDAVVHAGDLYHDRRPELPDLLGTLAALRRLDDAGIPFLAIVGNHESTRGGQWLDLFERLGLATRLGRDPHVVGGVAFYGLDHVPRSRRDELDYQFDPVDADRAVLVAHGLFTPFAHADWETETVLAESNVDFDAVLLGDNHVPDTAELDGTWVTYCGSTERASASERDPRGYNLVEFTPDAVDIRRRTLETRPFAFVEVDLAGDEGIERVRQRVREFDLEDAVVIVELRGEGETVTPAAVESFAVEEGALVARVNDKRDIDDDGDLATDVTFADPDDAVRERVREMGLSSAALDVDETVRASKVADSNVRDEVRERVESLLSDDPDAFVAAERESDAEAEESESVEDAADGEDAAAVEDTAETAAEAATDTDTETTADTDSETAADPAASRDSSLGDFA", "text": "FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity (By similarity). In polyploid organisms, the Rad50/Mre11 complex appears to restrain the repair of double-strand breaks by homologous recombination, allowing another pathway to act as the primary mode of repair (PubMed:19593371). SIMILARITY: Belongs to the MRE11/RAD32 family."}
{"protein": "MTVNIAILGFGTVGTGLPTLISENKEKLSKILDEEIVISKVLMRDEKAIEKARAQGYQYDFVLTLEEILADSEISIVVELMGRIEPAKTYITKVIKAGKNVVTANKDLLAVHGTELRALAEKHHVALYYEAAVAGGIPILRTLANSFSSDKITHLLGILNGTSNFMMTKMSEEAWTYDQSLAKAQELGYAESDPTNDVDGIDASYKLAILSEFAFGMTLSPDQISKSGLRTIQKTDVEIAQQFGYVLKLTGEINEVESGIFAEVSPTFLPKSHPLASVNGVMNAVFIESDGIGDSMFYGAGAGQKPTATSVLADIVRIVKREKDGTIGKSFNEYARPTSLANPHDIVNKYYFSVETPDSTGQLLRLVELFTSEDVSFEQVLQQKGDGHRAVVVIISHQINRVQLLAIQDKLKEEVDFKLLNYFKVLGD", "text": "SIMILARITY: Belongs to the homoserine dehydrogenase family."}
{"protein": "MESSKSPSEVEKSSSASPAPQKPMIRVSKQWVVPPRPKPGRKPALDALGRRKAPIKPRPGPTSALSVEEAKFRVREKQYQDTIGKLQKENNELLEQLEMLQAQLKNSTLDSPKEVEVNSEVVKPDSATTENENRYVNQYNYPVEPPCAKNAVYTEIPIELDPHAFLGDSAKRIRVDSDSKDAKSVPSENGRIRVSMSPQNEINFTPENPAVMEKIRKRGVCNSVEGCLYSGSPKSVKRVRESEETKVYAQLLIDLHKSSKSAPMLKAGPSIAFKLPTMEPNFNDVRPVTSISSSS", "text": "FUNCTION: Component of the transcription regulatory CCAAT-binding complex. Required for the reprogramming of the cell for iron use. Down- regulates pcl1, sdh4, and isa1 underlow-iron conditions. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, spindle pole. Note=Iron starvation induces nuclear accumulation and iron induces relocalization to the cytoplasm, in association with exportin crm1."}
{"protein": "MTEDFISSVKRSNEELKERKSNFGFVEYKSKQLTSSSSHNSNSSHHDDDNQHGKRNIFQRCVDSFKSPLDGSFDTSNLKRTLKPRHLIMIAIGGSIGTGLFVGSGKAIAEGGPLGVVIGWAIAGSQIIGTIHGLGEITVRFPVVGAFANYGTRFLDPSISFVVSTIYVLQWFFVLPLEIIAAAMTVQYWNSSIDPVIWVAIFYAVIVSINLFGVRGFGEAEFAFSTIKAITVCGFIILCVVLICGGGPDHEFIGAKYWHDPGCLANGFPGVLSVLVVASYSLGGIEMTCLASGETDPKGLPSAIKQVFWRILFFFLISLTLVGFLVPYTNQNLLGGSSVDNSPFVIAIKLHHIKALPSIVNAVILISVLSVGNSCIFASSRTLCSMAHQGLIPWWFGYIDRAGRPLVGIMANSLFGLLAFLVKSGSMSEVFNWLMAIAGLATCIVWLSINLSHIRFRLAMKAQGKSLDELEFVSAVGIWGSAYSALINCLILIAQFYCSLWPIGGWTSGKERAKIFFQNYLCALIMLFIFIVHKIYYKCQTGKWWGVKALKDIDLETDRKDIDIEIVKQEIAEKKMYLDSRPWYVRQFHFWC", "text": "FUNCTION: Required for high-affinity tryptophan transport. Also transports cysteine, phenyalanine and tyrosine. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family."}
{"protein": "MERFIENLMYTSRWLLAPVYLGLSLGLLALAIKFFQEVFHVLPNIFDIAEADLVLVLLSLIDMTLVGGLLVMVMLSGYENFVSALDITDGREKLNWLGKMDSGSLKNKVAASIVAISSIHLLRVFMDARNIPDNKLMWYVIIHLTFVLSALVMGYLDRMSRYEKSKAA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0114 family."}
{"protein": "MVSMQISDSLKQKAEKCGIALSHYDIDGHLIFADEKTVSTFVELLQPPPKAKGQFDDVLAAFENEPIDYRLNRLDLPPSAEYRYQLTDESNAILLEKILSNLSVLSLPPLPFGYYQLSIFSDTEQYRIRLLISPKTAFQPPVLENKKVWGVNVQLYSLRSEQNWGIGDFGDLAYLIEQSAKQGADYVGINPLHLPYPAVPNWASPYSSSSRRWLNFLYLDIPDLPEFKRCRSVQNWFKREDIQAKIAALRESDCVDYSSILALKLTALEPLFDFFQRSQSVEIVTRRKIFAEYLKNKGEPLLLQGLFNVLDLQEHADHQAEENTIGWLGWRKEWQHLSAAKRKALLKTHHEKIQFFAWLQWLTEEQLSALQNLCKQSGMKLGIYGDLAVNSSRGSADVWSDPDLYCVNASIGAPPDPLGPVGQNWNLPPYNPTVLKARGFAPFIDMLCANMQYFGVLRIDHVMGLFRLWWIPKGKTAADGAYVHYPFDELMAILAIESVRNECLIIGEDLGTVPDEVRWKLNEFQIFSYFVLYFAQRNGEFPRISDYPRNAYATIGTHDVPSLQSFWHCRDLELFNQLGILNGEVLKQKYDQRVMDKQALLNSLHRDNYLPPHYEGDALSMAMHDYLNRMIHYYLAESNSRLIGVQLENLLSQEISFNLPSTSNEYPNWCKKLAQPLAFIFSNEALKTFFVQINQGRNV", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the disproportionating enzyme family."}
{"protein": "MAMRSGRHPSLLLLLVLLLWLLQVSIIDSVQQETDDLTKQTKEKIYQPLRRSKRRWVITTLELEEEDPGPFPKLIGELFNNMSYNMSLMYLISGPGVDEYPEIGLFSLEDHENGRIYVHRPVDREMTPSFTVYFDVVERSTGKIVDTSLIFNIRISDVNDHAPQFPEKEFNITVQENQSAGQPIFQMLAVDLDEENTPNSQVLYFLISQTPLLKESGFRVDRLSGEIRLSGCLDYETAPQFTLLIRARDCGEPSLSSTTTVHVDVQEGNNHRPAFTQENYKVQIPEGRASQGVLRLLVQDRDSPFTSAWRAKFNILHGNEEGHFDISTDPETNEGILNVIKPLDYETRPAQSLIIVVENEERLVFCERGKLQPPRKAAASATVSVQVTDANDPPAFHPQSFIVNKEEGARPGTLLGTFNAMDPDSQIRYELVHDPANWVSVDKNSGVVITVEPIDRESPHVNNSFYVIIIHAVDDGFPPQTATGTLMLFLSDINDNVPTLRPRSRYMEVCESAVHEPLHIEAEDPDLEPFSDPFTFELDNTWGNAEDTWKLGRNWGQSVELLTLRSLPRGNYLVPLFIGDKQGLSQKQTVHVRICPCASGLTCVELADAEVGLHVGALFPVCAAFVALAVALLFLLRCYFVLEPKRHGCSVSNDEGHQTLVMYNAESKGTSAQTWSDVEGQRPALLICTAAAGPTQGVKDLEEVPPSAASQSAQARCALGSWGYGKPFEPRSVKNIHSTPAYPDATMHRQLLAPVEGRMAETLNQKLHVANVLEDDPGYLPHVYSEEGECGGAPSLSSLASLEQELQPDLLDSLGSKATPFEEIYSESGVPS", "text": "FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Ligand for integrins alpha-E/beta-7, ITGAE:ITGAB7, alpha-4/beta-7, ITGA4:ITGAB7 and alpha-4/beta-1, ITGA4:ITGAB1 through which modulates CD4(+) T cells activation (PubMed:28051089). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MAFFLIFLSSFFGLCIFCTALLRWNQVKYNQKNLPPGTMGWPLFGETTEFLKLGPSFMKNQRARYGSFFKSHILGCPTIVSMDSELNRYILVNEAKGLVPGYPQSMIDILGKCNIAAVNGSAHKYMRGALLSLISPTMIRDQLLPKIDEFMRSHLTNWDNKVIDIQEKTNKMAFLSSLKQIAGIESTSLAQEFMSEFFNLVLGTLSLPINLPNTNYHRGFQARKIIVNLLRTLIEERRASKEIQHDMLGYLMNEEATRFKLTDDEMIDLIITILYSGYETVSTTSMMAVKYLHDHPKVLEELRKEHMAIREKKKPEDPIDYNDYRSMRFTRAVILETSRLATIVNGVLRKTTQDMEINGYIIPKGWRIYVYTRELNYDPRLYPDPYSFNPWRWMDKSLEHQNSFLVFGGGTRQCPGKELGVAEISTFLHYFVTKYRWEEIGGDKLMKFPRVEAPNGLRIRVSAH", "text": "FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids biosynthesis (PubMed:15710611). Converts 6-deoxocastasterone (6- deoxoCS) to castasterone (CS) (PubMed:15710611, PubMed:9990098). May also convert 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3- dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) to 3- dehydroteasterone (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY), but not castasterone (CS) to brassinolide (BL) (PubMed:15710611). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MGRGPPAVLAPWMLFLSLAQANFAPHFFDNGAGSTNGNMALFSLPEDTPVGSHVYTLNGTDPEGDPVSYHISFNPSARSVFSVDPNLGNITLIEELDREREDEIEAIISISDGLNLVAEKVTILVTDANDEAPRFIQEPYVVQVPEDTPSGSSIARVRAVDRDTGSAGSVTYFLKNPHPTEFSVDRHSGVLRLRAGAILDFEKARAHFVTVVAKDGGGKLRGADVVLSATTVVTVNVEDVQDMGPVFVGTPYYGYVYEDTLPGSEVLMVVAMDGDRGKPNRVLYSLVNGSDGAFEINETSGAISVMQSPSQLRREVYELHVQVTEVSSAGTPAAQAMVPVTIRIVDLNNHPPTFYGESGPQNRFELSMYEHPPQGEILRGLKITVNDSDQGANAKFNLRLVGPGGIFRVVPQTVLNEAQVTIIVENSAAIDFEKSKVLTFKLLAIEVNTPEKFSSTADVVIQLLDTNDNVPKFTSHYYVARIPENAPGGSNVLAVTAVDPDSGPWGEVKYSIYGSGADLFLIHPSSGIIYTQPWASLDAEATARYNFYVKAEDMEGRYSLAEVFITLLDVNDHYPQFGKSVQEKTMVLGTPVKIEATDQDAEEPNNLVDYSITHAEPANVFDINAHTGEIWLKNSIRSLDALHNITPSGDRTWSLEVQAKDRGSPSFSTTALLKIDIVDTEMLSRSPMAAFLMQTKDNPMKAVGVLAGIMAIIVAITVLISTATFWRNKKSNKVQPVRRVLRKRPSPAPRSVRIEWLKFRRTKAADKFVLREAPPNENCNNNSRGSTPAPQAPAPPPPPSPAPSVGQAPWTVPTVSGSLAPQQPQQPSPKPRAVAKRKAVGSPVQSALVSELRQKFEKKNLHSKAYF", "text": "FUNCTION: Potential calcium-dependent cell-adhesion protein. May be required for the structural integrity of the outer segment (OS) of photoreceptor cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Localized at the junction between the inner and outer segments of rod and cone photoreceptors cells. Confined to the base of the OS. Localized on the edges of nascent evaginating disks on the side of the OS opposite the connecting cilium. Expressed at postnatal day 2 at the apical tip of the rod photoreceptor cells, the site of the developing OS. Colocalized with rhodopsin between postnatal days 2 and 9 at the base of the growing OS region (By similarity)."}
{"protein": "MNVNSVIYYILFLFASTILAADKTSSSVSPTLVWVTGTDANGKLATTQSTYYQSFMSTYTTAETPSSGSIGLGSISGTVGEIRTYSMTTISQGNGGLSKFNQNGLEMKNLSFVKLIGVSFIAFISFILLI", "text": "FUNCTION: Involved in cell wall 1,6-beta-glucan assembly possibly by the addition of linear side chains of 1,6-linked Glc units to a highly branched 1,6- and 1,3-linked glucan backbone. FUNCTION: Involved in cell wall 1,6-beta-glucan assembly possibly by the addition of linear side chains of 1,6-linked Glc units to a highly branched 1,6- and 1,3-linked glucan backbone. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted, cell wall. SIMILARITY: Belongs to the KRE1 family."}
{"protein": "MSAEASGSSGGHAVTVSGSSPSSSSHVGEEKPGRSLVSSKYVKLNVGGTLHYTTVQTLSKEDSLLRSICDGSTEVSIDSEGWVVLDRCGRHFSLVLNFLRDGTVPLPDSTRELEEVLKEAQYYRLQGLVQHCLSTLQKRRDVCRGCHIPMITSAKEEQRMIATCRKPVVKLQNNRGNNKYSYTSNSDDNLLKNIELFDKLGLRFNGRVLFIKDVLGDEICCWSFYGEGRKIAEVCCTSIVYATEKKQTKVEFPEARIFEETLNILIYENGRGSGGMALLESGGVSSSGAGQSEEEGAGAGGGDRRVRRIHVRRHIMHDERGHGQQTVYKD", "text": "FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for synaptic transmission (By similarity). The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and promoting synaptic transmission (PubMed:29088697). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BACURD family."}
{"protein": "MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR", "text": "FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:7744004, PubMed:19273597, PubMed:19923322, PubMed:9171063, PubMed:12853446, PubMed:16617111, PubMed:33693784). Acts as downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (PubMed:7744004). Full- length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (PubMed:9171063, PubMed:12853446, PubMed:16617111). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964). SUBCELLULAR LOCATION: [PAK-2p34]: Nucleus Cytoplasm, perinuclear region Membrane; Lipid-anchor Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region (PubMed:15471851). Myristoylation changes PAK-2p34 location to the membrane (PubMed:16617111). SUBCELLULAR LOCATION: [Serine/threonine-protein kinase PAK 2]: Cytoplasm Nucleus Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MISLTDTQKIGMGLTGFGVFFLFFGMILFFDKALLAIGNVLFVAGLAFVIGLERTFRFFFQKHKMKATGFFLGGVFVVLIGWPLIGMIFEIYGFFLLFRGFFPVVVGFIRRVPVLGSLLNLPGIRSFVDKVGESNNMV", "text": "FUNCTION: May be involved in fusion of ER-derived transport vesicles with the Golgi complex. FUNCTION: May be involved in fusion of ER-derived transport vesicles with the Golgi complex. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the GOT1 family. SIMILARITY: Belongs to the GOT1 family."}
{"protein": "MKAAVLDLGSLLAKLFETSTAPPAGPSSRPSGGAAAAGSGGSRAGTPLGTAPTLLRALAPDSPSASRRSPAPLLSSPYSRGSAASRAAGAVGTLLSWPSSPRAGKAPPQPPTPSGGGCSPARLVVPARPPSGPGGVWAALPRNPLQPGPGERELGACVAPGAGPRTLFLTLPDIGEEGASDGDSGDGEARGLSEGRRRHGFTVRSKDSLPTHFTRNVQKAIDKYTCKSLSSFSSSGSHTPTGAHTSWSGSATQSSTTGSSTERGSVYSWRDDEFDEASSQSVQRLLWEVEEMLFEGKVNPQTQSLLAECGEWTRRSLHLRVLGRQLILPTDKGVQHFQGSTPASAVHRPPLSACGHSSNIRELCISGSQIVPAALSASALPGPDDTGVADLTARSSLEEEVYHVDGKIEEYFAFDRKEDDDECLEQKPAQPGRKWRKLGLPPVSPRDCVKDAVAAEVFDHVWTNMVELLEELIRKHWETTLTEGKKQRETLKVAGNRFPHVLVPHAHADGASGPPSGHAEAHGISLASRLNPPQIHHFSSSFYSDMNGVMTIQAKPLQRRPAYFADRTQNEKEDKASGGGAGALSSAPHRLGRASDTHGLSPSAKKTPVPWRLPSLASDSQRLKTPNIYSDEVLRGTKLPTGVDHMASPLVQTSRSRFPPLVTETRGQNTAVPGCRLVSYRGRHLQNRVLSAMPDGTERSRLRERTATLERLSRPSTTHTFRQSDTPRKSSLTQMEFAAHTWTGQSILTGSQYVPKSFQRTTLTFKRRFQVTS", "text": "SIMILARITY: Belongs to the FAM149 family."}
{"protein": "MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYGAKQEPLILTAVTKVEEARVPEEKHWTKEFQPTGKAFTGNLLHHPLVHMERLELLRNVCRDTALRNLSHTAVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAYSSIDEIPESIVHDHEKNGLPRLSSFSDSEIKKRLNLYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPSIIRKYRRNRMETKGLQFEDFVRYLGDPNHRWLDVQFGDHIIHWVTYVELCAPCEITYSVIGHHETLEDDAPYILKAAGIDRLVSYPTIPPGITVYNKTKVERYFSGISKRDIRRLYARFEGDFKLFGYRVPDFLLN", "text": "FUNCTION: Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 2 family."}
{"protein": "MIYPIPNSETSTVHFKDVYDNYIGGQWMKPHSGEYFSNTSPVNGLVFCRVARSSSQDVELALDAAHNALESWSTTSAVERSNILLRIADRIESNLETLAIVESWDNGKPIRETLAADLPLTIDHFRYFAACIRSQEGAASELDSRTLTYHLPEPIGVVGQIIPWNFPLLMAAWKLAPALAAGCTVVLKPAEQTPVSILFLMEIIGDLIPAGVINVVNGFGSEAGNALATSQRIDKLAFTGSTEIGNHILKCAADNLIPSTIELGGKSPNIYFPDIFSHEDQYLDKCIEGALLAFFNQGEVCTCPSRILVHESIYEKFIAKIIERVALIKQGNPLDTETQIGAQVSKEQYDKILGYIQIGKDEGAELIFGGHPNNQENYLSGGYYIKPTLFFGHNQMHIFQEEIFGPVIAITKFKDEIEALHLANDTVYGLGAGVWTRDINIAHRMAKNIKAGRVWVNCYHAYPAHAAFGGYKKSGIGRETHKLTLSHYQNIKNVLISHEIHPLGLF", "text": "FUNCTION: May be involved in V.cholerae virulence, as its expression is under the control of ToxR, a transcriptional activator of several genes associated with virulence. FUNCTION: May be involved in V.cholerae virulence, as its expression is under the control of ToxR, a transcriptional activator of several genes associated with virulence. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MSGESDQPQPGPSHAGLYLEHRERDQAGVPGGVIRRAGSQRHRSWIQTVIEQITGSPRQCVTLSEVVPVSVLAVQRYLLEDEPRDTVPKPPLYCYDVTISDGVYQEKCYLDPSLNFLVYQNILKVGIEMRISRVSCLYNEKRLGQGILCIDKVHCGEPLDVISVETPFRNRAHEEKPERPLRGSKSHYLALWNNEDPYGDIWKTNKQPEEFNFNNTKIISLSHLEMTWHNRKNFPALLVRILHKSKLRYYGKPNKKMIEPYQTYLEVADSSGMVSVIMWNALCPEWYKSLRVGLILLLQDYSVKKSYPLRIQPDPVDPQMKLISTMEICLNLRDPPTNIVIIPEKQLKSEWKLPKLINRFITRSELDDMPENSICDVIGMLSFVGRVQRSKKKENSEDFWSYRWIHITDGTSEQPFIVQLFSTSQPEVFENIYPMTYFVCTQLKVVRNNSQVPKLLYLTTTNESRVLITGHRGQPYTYDTKAKKIIQWIKTKTNLEAKNTVIGGYYPYPPVPETFSKYSRFIKAESLLTTISEVRKVIEDLQYREQKRIAIQGIITAIKYIPYNHSAKSAPASETLQNASPPSTSQAAAKEGHYHERGSKRSQDDRPMDSLPMVLSLCAKRKILQGPTANPVPVPQPHSSAQMKGNKPNIPSRENSTANATGKSKRIINDRWESQLWRDKKFSLRDHLHYGHVDPESIPRKFILGHEKFLTQQFNSQPAKYVPPEGKPPKLDEFQSARSLGHFEVTILGLNHEIAIDVAFLPMYSPEDVETSQIDTFLTCMNYSCVYPPAAPVSGRVPDPKAVAGDIVKAAADLDRVHIIGILDICNLGNNKVEVCLQKIYTPE", "text": "FUNCTION: Single-stranded DNA-binding protein recruited to replication forks to maintain genome stability. Prevents fork collapse by antagonizing the accumulation of RAD51 at forks to ensure the proper balance of fork remodeling and protection without interfering with the capacity of cells to complete homologous recombination of double-strand breaks. SUBCELLULAR LOCATION: Chromosome Note=Recruited to replication forks."}
{"protein": "MNVSKYVAIFFFVFIQLISVGKVFANADEWMTTFRENIAQTWQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGQSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPATFQMTYIPGTYNNGNVYFAWMRFQF", "text": "FUNCTION: Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the lipid A palmitoyltransferase family."}
{"protein": "MNIRGAPDLGQPSDDPNSGGERERIRQRMKMVIGQLEGILRELKEVAKELREVVSQIDKLTSDFDFELEPDDWTTATVSSTSSSDKAGVGGPFDLGHLDFMTADILSDSWEFCSFLDVSTPSDSVDGPEAPRPGTGPDYQLMNGGLPIPNGPRVETPDSSSEEAFSAGPAKGQVPQRTPGTRERVRFSDKVLYHALCCDDEEGDGEEGEEEEEGDLAPELPRVEPHTGPLKPSPAPYKTKRSPLTTRRLGPTLAPEQTRRVTRNSSTQTVSDKSTQTVLPYTATKQKAKGKN", "text": "FUNCTION: Component of the protein machinery at the inhibitory synapses, probably acting as a scaffold. Inhibitory synapses dampen neuronal activity through postsynaptic hyperpolarization. This synaptic inhibition is fundamental for the functioning of the central nervous system, shaping and orchestrating the flow of information through neuronal networks to generate a precise neural code. SUBCELLULAR LOCATION: Postsynaptic density. SIMILARITY: Belongs to the INSYN1 family."}
{"protein": "MVDTTQTTTEKKLTQSDIRGVFLRSNLFQGSWNFERMQALGFCFSMVPAIRRLYPENNEARKQAIRRHLEFFNTQPFVAAPILGVTLALEEQRANGAEIDDGAINGIKVGLMGPLAGVGDPIFWGTVRPVFAALGAGIAMSGSLLGPLLFFILFNLVRLATRYYGVAYGYSKGIDIVKDMGGGFLQKLTEGASILGLFVMGALVNKWTHVNIPLVVSRITDQTGKEHVTTVQTILDQLMPGLVPLLLTFACMWLLRKKVNPLWIIVGFFVIGIAGYACGLLGL", "text": "FUNCTION: Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA. FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ManXYZ PTS system is involved in mannose transport. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MTLLQREENIIRKGNIDKEFSEKIKAAGGDSLEYCFQCGTCTGSCPSGRRTPYRVRQIIRKANVGLKDEIISDPALWMCTTCYSCQERCPRKVKIVDVVKLARNEAAKAGFMAPAHKAVGSFVIKTGHGVPINDATMELRKAVGLGELPPTTHQFPEALEEVQKIIKATGFDQLIGYNWETGELE", "text": "FUNCTION: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B). SIMILARITY: Belongs to the HdrC family."}
{"protein": "MAPSFDHLPDPEEDEYDEEELDISDLRERFEVQLEQGLDTFVVIDGLPEVNEDTKPKLIKFLLRKLDSVGQTKKDSIHMPIGPDGKSFKFAFVEYSSPAEAIAACKALDGVPLDKKHTLRVNKLTDIDRYGREGRIDENYTPPKIEEFTEKEHLRSWLADPAGRGRDQFVMYKDDRVQVFWNNEKDAPESIVDRQHWTESFVQWSPQGTFLTSMHQQGVQLWGGPSWTRQKRFAHPFVNLVDFSPGEKYLTTWSNRPISIGEEGHPALSVDDDGKNYVIWDIETGLPLRSFANLDLPSNSVDAEGNPVKRKIQWPAFKWSSDDKYVARLTQGSSISVYELPRMNLLDKTSIKIDGVMDFDWAPATPHREGVKNYEQLFCYWTPEIGSNPAKVGLMSIPSKEVVRTLNLFSVTDAKLHWQSDASYLCVKVDRHSKSKKSLATSLEIFRVKEKGVPVEVVDSIKDTVINFAWEPKGDRFVIITTAEVVAATAVPPKTSVSFFCPEKVKGNGVGNFKHIRTYDKKNSNAIYWSPKGRFVIVATVHSQQSFDMEFYDMDFEGEKPESDKDLTANLQLMNTADHYGVTDIDWDPTGRFVATSASIWKHTMENGYHLYDFKGEQLREEPVEKFKQWLWRPRPPTLLSKEEQKQIRKNLREYSKVFDQEDADRGASADLAVVEHRRRLLDEWLAWRANIEEDVQAEREDAGLPRDPLEPLKSKMASGDEGQAIEIEEIVEEIVEETEEIIS", "text": "FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit B family."}
{"protein": "MIRVAIPTGRMLEQALDFLRNFDDRLLDEEKGRKLRIHGERFEVFLAKPWDLPLYVEERVVDLGIIGRDVIWEQEKNVVNLISLPFGYCKMVIAGYPYVSLKGNGKEIRIATKYENITKKLLENRWGKIKIIKLNGSVELGPILNISDLIVDIVETGKTLRDNGLEVKEVLFESSACLISNVVSFAYLRKEILSFVKEVRKLNDKCN", "text": "FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short subfamily."}
{"protein": "MTILFLTMVISYFGCMKAAPMKEANARGQGSLAYPAVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEDLLDEGQKVRPDEENSKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR", "text": "FUNCTION: Important signaling molecule that activates signaling cascades downstream of NTRK2 (By similarity). During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability (By similarity). FUNCTION: [BDNF precursor form]: Important signaling molecule that activates signaling cascades downstream of NTRK2. Activates signaling cascades via the heterodimeric receptor formed by NGFR and SORCS2. Signaling via NGFR and SORCS2 plays a role in synaptic plasticity and long-term depression (LTD). Binding to NGFR and SORCS2 promotes neuronal apoptosis. Promotes neuronal growth cone collapse. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: [BDNF precursor form]: Secreted Note=A proportion of BDNF is secreted as immature precursor (proBDNF). SIMILARITY: Belongs to the NGF-beta family."}
{"protein": "MGIVGVGIDLVSIPDFAEQVDQPGTVFAETFTPGERRDASDKSSSAARHLAARWAAKEAVIKAWSGSRFAQRPVLPEDIHRDIEVVTDMWGRPRVRLTGAIAEYLADVTIHVSLTHEGDTAAAVAILEAP", "text": "FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein (PubMed:16709676, PubMed:21697604). Involved in the post-translational modification of Fas-I and the AcpM subunit of Fas-II (PubMed:21697604). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family."}
{"protein": "MSTHFLGKVKFDEARLAEDLSTLEVAEFSSAYSDFACGKWEACVLRNRTGMQEEDIVVSHNAPALATPLSKSLPYLNELVETHFDCSAVRYTRIVRVSENACIIPHSDYLELDETFTRLHLVLDTNSGCANTEEDKIFHMGLGEIWFLDAMLPHSAACFSKTPRLHLMIDFEATAFPESFLRNVEQPVTTRDMVDPRKELTDEVIEGILGFSIIISEANYREIVSILAKLHFFYKADCRSMYDWLKEICKRRGDPALIEKTASLERFFLGHRERGEVMTY", "text": "FUNCTION: Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-4-hydroxy-L-proline (cis-4-Hyp). SIMILARITY: Belongs to the L-proline cis-4-/cis-3-hydroxylase family."}
{"protein": "MKVSVLITLAVWGVMFLLTSAQERGSDQMDSPAWLKSMERIFQSEERECRWMFGGCTTDSDCCEHLGCRWEKPSWCAWDGTFRK", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 06 (F4b) subfamily."}
{"protein": "MNTESLALDFKSATLYAIRVVLHDADTTRLRAALDKRMADAGSFFENEPVVIDATRVDAPVDWPALLQALADHNLPPIGVVAEGANLQGARDAGLVPVELSTPVARAPQVIDTAPPNDVATPVPSVPEATAEAAAKAGPQDDEAYGEQADEAPAHNPESVPTRAARETTEANRPTATPPQSSSALVITKPLRSGQRVYARHTDLIVIGMVSQGAEVIADGNVHVYGPLRGKAMAGARGDTSARIFTTQLDAELLAVAGVYRVVEDKLDRALHNQPALVRLDGDTLRIEALKG", "text": "FUNCTION: Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. SIMILARITY: Belongs to the MinC family."}
{"protein": "MHSSLIKLGFLLLLIQVSLSHAQLSPSFYDKTCPQVFDIATTTIVNALRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFDVIDKMKAAVEKACPKTVSCADLLAIAAQESVVLAGGPSWRVPNGRRDSLRGFMDLANDNLPAPFFTLNQLKDRFKNVGLDRASDLVALSGGHTFGKNQCQFIMDRLYNFSNTGLPDPTLDKSYLSTLRKQCPRNGNQSVLVDFDLRTPTLFDNKYYVNLKENKGLIQSDQELFSSPDASDTLPLVREYADGQGKFFDAFAKAMIRMSSLSPLTGKQGEIRLNCRVVNSKSKIMDVVEDALEFASSM", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. SUBCELLULAR LOCATION: Secreted Vacuole Note=Carboxy-terminal extension appears to target the protein to vacuoles. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "LWLPVIFFVVSNPKLILLKRVVFFQSWSNRPHGSSYFNKNIQFRRNSFVIVKASGSRTSKKQVEITYNPEEKFNKLADEVDREAGLSRLTLFSPCKINVFLRITSKRDDGYHDLASLFHVISLGDKIKFSLSPSKSKDRLSTNVAGVPLDERNLIIKALNLYRKKTGTDNYFWIHLDKKVPTGAGLGGGSSNAATTLWAANQFSGCVATEKELQEWSGEIGSDIPFFFSHGAAYCTGRGEVVQDIPSPIPFDIPMVLIKPQQACSTAEVYKRFQLDLSSKVDPLSLLEKISTSGISQDVCVNDLEPPAFEVLPSLKRLKQRVIAAGRGQYDAVFMSGSGSTIVGVGSPDPPQFVYDDEEYKDVFLSEASFITRPANEWYVEPVSGSTIGDQPEFSTSFDMS", "text": "FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. SUBCELLULAR LOCATION: Plastid, chloroplast Plastid, chromoplast. SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily."}
{"protein": "MPKSVSSHISLATSTGRSGPRDIRRCLSSRLRSVPPGARSASVSSKHRNGLRKFISDKVFFSILSHRHELGVDFLREMETPICTSKTVMLPLDLSTVAPGRCVSLSPFGHSSNMGFQCALCPSTENPTVAQGSRPQTMVGDALKKNNELCSVALAFYHHADKVIQHKTFYLSLLSHSMDVVRQSFLQPGLLYANLVLKTFGHDPLPIFTTNNGMLTMCILFKTRALHLGETALRLLMDNLPNYKISADCCRQSYVVKFVPTHPDTASIAVQVHTICEAVAALDCTDEMRDDIQKGTALVNAL", "text": "FUNCTION: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. SUBCELLULAR LOCATION: Host nucleus inner membrane Note=Remains attached to the nucleus inner membrane through interaction with NEC2. SIMILARITY: Belongs to the herpesviridae NEC1 protein family."}
{"protein": "MIQPQSYLTAADNSGARKLMCIRVLGGGNRRYARIGDVIVAVVKDGIPNIPIKKSDTVKAVIVRTRKELKRDNGMNICFDDNAAVIINADGNPRGTRVFGPVARELRDKNFTKIISLAPEVL", "text": "FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
{"protein": "MEFVERYVNKYASADYHSCADESVTHQFKSLLTQCQRYNNKVKCNHLAKMVKKIKMANEILALLKMKVIAENKAEQWRNEKVQFREDLEKFGESLIVAASTSEEHISELEELREKVELLAKQNDLLEEKLKDCEERCRLREQEVISLESKAGYELNVPVSVCPVTEQEIKDGEQGIRPQTLPSPTLFSPQSECARQRINNTYVPTDNNIHSNSALKIQEVISLTQILGKFDTNLSPISLYNKLEAVVKQYNLGNKDACALLRAWLPYQLAAELRPPVGKHIGTLSNINENWGSTSERLRELQRILGGRDIRGTNALENARYRKGDDPMLFCTDYLSLYKVVFNCPDMLPDEPNFLYSMANKCNVDYNTRTALRYATSYNNFINTLRDWSQESFEFQRHISVAYKKKQSRRFPRKCYSCGKYGHIARFCRTSANQHDTYPIHSIQRQEGDAQENLNDYLLDHSPPSETETVVSSDNIDTGSNSAGDQKESQNEPKREFHTPPCKTGKEGTTAPPFIPWVNIPLWLYSSWSHIAMLMLMDNIAQFAQGVPNTNMPVF", "text": "FUNCTION: This protein is expressed exclusively in posterior mesoderm and ectoderm of early embryos suggesting a possible role in organization of anteroposterior axis."}
{"protein": "MKVYLVGGAIRNKFLNLPVQDRDWVVVGATPEILLSLKFKQVGKGFPVFLHPYSKEEYSLARVDRKIGVGHTGFSFDYSNKVTLKEDLMRRDLTINAIAQDNNGNYIDPFKGIRDIKNRILRHVSPAFSEDPLRVLRIARFCALFHHLGFRIATETMKIMSIVVKNNELLNLTRDRVWKETEKAFNTDNPHVYFQVLKNCNALSVIFPEINLVYQRQYYCIDNMYHNFYDTFDIFMGLAELSKISRDIDIRFSYLFFCINRMLFIDTSSYILVINQKELVRYFKALCQRFCIPAYIKNVSICFSRFYKFLSVIHYQSSKDIIMFFYIIDAWRKPYMIRKLSVLNNFCVSRNAYFKNITCQQYPRNFLKYAFNVANKISIKPILKMGFSGLQIKYELIRLRINAIENWRQNITVYKKCCF", "text": "FUNCTION: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 2 subfamily."}
{"protein": "MAEAWFETVAIAQQRAKRRLPKSVYSSLIAASEKGITVADNVAAFSELGFAPHVIGATDKRDLSTTVMGQEVSLPVIISPTGVQAVDPGGEVAVARAAAARGTVMGLSSFASKPIEEVIAANPKTFFQVYWQGGRDALAERVERARQAGAVGLVVTTDWTFSHGRDWGSPKIPEEMNLKTILRLSPEAITRPRWLWKFAKTLRPPDLRVPNQGRRGEPGPPFFAAYGEWMATPPPTWEDIGWLRELWGGPFMLKGVMRVDDAKRAVDAGVSAISVSNHGGNNLDGTPASIRALPAVSAAVGDQVEVLLDGGIRRGSDVVKAVALGARAVMIGRAYLWGLAANGQAGVENVLDILRGGIDSALMGLGHASVHDLSPADILVPTGFIRDLGVPSRRDV", "text": "FUNCTION: Involved in the biosynthesis of the enzyme cofactor mycofactocin (MFT). Catalyzes the oxidative deamination of AHDP (3- amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one), forming an alpha-keto amide moiety on the resulting molecule, which is called pre-mycofactocin (PMFT). This reaction occurs via a 5-[(4- hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one intermediate, which converts to PMFT. The alpha-keto amide moiety is the redox-active center for the redox activity of mycofactocin. SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
{"protein": "IVGGRPARPHAWPFMASLQRRGGHFCGATLIMGWGQLGTNRPLPSVLQELNVTVVTAGICFGDSGGPLVCNGL", "text": "FUNCTION: May be involved in the degradation of connective tissue in chronic lung disease. SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily."}
{"protein": "MMAAAVVRAEVRRQRREERKKMAAARTTEDPPENHVVADVACGTGAVTRSSSSSLVVSSSSASGSDEPSSASPLSFPVCSPSTAVRSPGSAGVSTSLCSVERMVELSAQSPAADFSVSEAWRFEEAVNMALVACEAVSPYDRFRLIETPDENFLLVTNVIPRESAEVPVLDSSSSGGDSGPEDKKKNVGNKTAGEKNGGGSRAKRRRRRRAPKNDAATPSFLRRHDVLERFAAAAEPLPSLCVRDYALRNADRVTYDGELIYGSYLLYRKAHVELSLSSNKVQHVEAVLRQVYTPGLLDHHNVCDVEALLWLLYCGPRSFCARDTCFGREKNGCPFPALLPKLFYEPVRDYMTYMNLAELYVFVWYRGYEFPAPTPQATTAGSGGGGGAGACAVETSASAGRVDDAGDEVHLPLKPVSLDRLREVLQAVRGRFSGREVPAWPASSRTCLLCALYSQNRLCLDLARDEARTVSYSPIVIQDCAAAVTDVTLSHILPGQSTVSLFPVYHVGKLLDALSLNDAGLITLNL", "text": "FUNCTION: Participates in the expression of late viral mRNAs. Expressed before viral DNA replication, UL95 assembles at the viral pre- replication complexes (pre-RCs) containing the early viral protein UL44. SUBCELLULAR LOCATION: Host nucleus Note=Recruited to nuclear replication compartments. SIMILARITY: Belongs to the herpesviridae UL95 family."}
{"protein": "MISATNWVPRGFSSEFPEKYVLDDEEVERINQLAQLNLDDAKATLEEAEGESGVEDDAATGSSNKLKDQLDIDDDLKEYNLEEYDDEEIADNEGGKDVSMFPGLSNDSDVKFHEGEKGEDPYISLPNQEDSQEEKQELQVYPSDNLVLAARTEDDVSYLDIYVYDDGAGFHSSDIPVEEGDEADPDVARGLVRDPALYVHHDLMLPAFPLCVEWLDYKVGSNSEEAANYAAIGTFDPQIEIWNLDCVDKAFPDMILGEPLDNSMVSLKSKKKKKKSKTGHITTHHTDAVLSMAHNKYFRSVLASTSADHTVKLWDLNSGNAARSLASIHSNKNVSSSEWHMLNGSILLTGGYDSRVALTDVRISDESQMSKYWSAMAGEEIETVTFASENIILCGTDSGNVYSFDIRNNENRKPVWTLKAHDAGISTLCSNKFIPGMMSTGAMGEKTVKLWKFPLDDATNTKGPSMVLSRDFDVGNVLTSSFAPDIEVAGTMVIGGVNKVLKLWDVFTNRSVRKSFKSELENVQARAKEEAQKIGKSSRIARKYTSNDNPDTVITIDDQGEDEEEREGGDEHDDMA", "text": "SIMILARITY: Belongs to the WD repeat PWP1 family."}
{"protein": "MARTGRRAAVGRPARTSSLTERRRVLLAGVRSHTRFYKAFAREVREFNATRICGTLLTLMSGSLQGRSLFEATRVTLICEVDLGPRRPDCICVFEFANDKTLGGVCVILELKTCKSISSGDTASKREQRTTGMKQLRHSLKLLQSLAPPGDKVVYLCPILVFVAQRTLRVSRVTRLVPQKISGNITAAVRMLQSLSTYAVPPEPQTRRSRRRVAATARPQRPPSPTRDPEGTAGHPAPPESDPPSPGVVGVAAEGGGVLQKIAALFCVPVAAKSRPRTKTE", "text": "FUNCTION: May participate in nuclear egress of viral particles. Plays a role in the dispersal of several host nucleolar proteins including NCL/nucleolin and NPM1. Since deletion of host NCL/nucleolin negatively impact on nuclear egress, UL24 supposedly acts on this process through its effect on host nucleoli (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm Host nucleus, host nucleolus Host Golgi apparatus. SIMILARITY: Belongs to the herpesviridae UL24 family."}
{"protein": "MRHMQSATRATLVCGSGVKQIIAKGHPNTRVFGARKARIPEREVLAAKPKITRITHLNLQPQERQAFYRLLENELIQEFLSMDSCLKISDKYLIAMVLAYFKRAGLYTGEYTTMNFFVALYLANDMEEDEEDYKYEIFPWALGDSWREFFPQFLRLRDNFWAKMNYRAVVSRRCCDEVMAKDPTHWAWLRDRPIHHSGALRGYLRNEDDFFPRGPGLTPASCALCHKASVCDSGGVAHDNSSPEQEIFHYTNREWSQELLILPPELLLDPESTYDIHIFQEPLVGLEPDGAALEWHHL", "text": "FUNCTION: Stimulates oocyte maturation by promoting meiotic G2/M progression in resting oocytes, via activation of the MAPK cascade and cdc2-cyclin B. Also activates the kinase activity of cdk2; this activation does not appear necessary for oocyte maturation. Necessary for polyadenylation in oocytes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Speedy/Ringo family."}
{"protein": "MKLLILTICALHVNQMMALKDCVVVNGKNYGKEVLKDNIHQAYQLSFDPQQNTLFFSYSDEVDSKTVLKMGYLNLATKSFGEISGVKDGMATAVDTTNHIVYLGGKDGIYTYDYATKSAKNIGVTSLSIWQMFYCPIHGLFFTTSDEKPYVFKDGQVNQIVEASSSKTRVMAVGEHHDVFFANSSGIFLFNHHTNKVIDLGDYNVNAFTKDSKGKLYFSSPVGFYAVNEADRKMNKLISETGEDSIWGAAFDKDDNIVYSNEDNIVKLVPKDKC", "text": "FUNCTION: Binds to an ommochrome, ommatin D which is a yellow chromophore. May be involved in guiding the chromophore through the hemolymph from the epidermis to the gut."}
{"protein": "MQDKAMLMIPGPTPVPESVLLSLGKHPIGHRSGEFSQIMAAMTAGIKWLHQTQNEVLILAASGTGAMEAGIINFLSAGDRVVVGCNGKFGDRWGEVCDAYGLTTERISAPWGQPLNPDDFKAVLDGHRQKPSKAVIVTHSETSTGVINDLEAINRHVKAHGQALIIVDAVTSLGAVSVPIDEWGLDVVGSGSQKGYMIPPGLAFVSVSPKAWEAYKTATLPKFYLDLGKYRKDAAKHTTPFTPPVNLFFALKTALEMMQAEGLEAIFQRHQRLMQATRAAMKALNLPLYAADSCASPAITAVAPQGVEAENIRSLMKKRFDIALAGGQDHLKGQIFRIGHLGFVGDRDILAAVSALEAVLAELGYTNFTPGAGVAAASRVLSTA", "text": "FUNCTION: Soluble hydrogenase catalyzes both production and consumption of hydrogen from suitable artificial electron donors or acceptors. This subunit catalyzes the tritium-exchange activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MSLSRLLIKDFRNIENADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQPGRVIRHEQEAFVLHGRLQGEERETSIGLTKDKQGDSKVRIDGTDGHKIAELAHLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEAGFFTAWSNLKRLLKQRNAALRQVSRYEQLRPWDKELIPLAEQISTWRAEYSSAIAQDMADTCQQFLPEFSLTFSFQRGWEKETDYADVLERSFERDRMLTYTAHGPHKADFRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDARRGLLASRLKATQSQVFVSAISAEHVIDMSDENSKMFTVEKGKITD", "text": "FUNCTION: The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecF family."}
{"protein": "MKCVDLFSGCGGLSLGFELAGFEICAAFENWEKAIEIYKNNFSHPIYNIDLRNEKEAVEKIKKYSPDLIMGGPPCQDFSSAGKRDISLGRADLTYSFANIVCNIRPKWFVMENVEQIKKSHILQDIINQFIDFGYGLTSAILDASYCGVPQSRTRFSLIGKLNSEHNFLIPTLSRKLSDKPMTVRDYLGNSLNLEFYYRHPRNYNRRGIFSIDEPSPTIRGVNRPIPKGYNINSCDPKGVELAKVRPLTTIERSYIQTFPKSFLFSGTKTDLEQMIGNAVPVNLAKFVASAIINFEKEPIRSMG", "text": "FUNCTION: A methylase, recognizes the double-stranded sequence 5'- GRCGYC-3', methylates C-? on both strands, and protects the DNA from cleavage by the HindV endonuclease. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
{"protein": "MANKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTVQWLPDVTRPEGKDYALHWLVLGTHTSDEQNHLVVARVQVPNDDAQFDASHYDSEKGEFGGFGSVSGKIETEIKINHEGEVNRARYMPQNPCIIATKTPSADVLVFDYTKHPSKPDPSGECSPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDISAGPKEGKVVDAKAVFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEEPDIPASELEAQGS", "text": "FUNCTION: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
{"protein": "MQAHELLQYFRLPELVDIRQYVRTLPTNTLMGFGAFAALTTFWYATRPKALKPPCDLSMQSVEVAGSDGARRSTLLDSDEPLVYFYDDVRTLYDVFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVEDLSECIGSALLQKGFQASPDQFIGIFAQNRPEWVIIEQACFAYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKARILLESVENKLTPGLKIIVVMDSYGSELVEQGKKCGVEVISLKAMEGLGRANRRKPKPPEPDDLAVICFTSGTTGNPKGAMITHKNVVSDCSAFVKATEKALVLNASDIHISFLPLAHMYEQLLQCVMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFAQANTTVKRWLLDFASKRKEAELRSGIIRNNSVWDKLIFHKIQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLSVPGDWTAGHVGAPMPCNFIKLVDVEEMNYMAAMGEGEVCVKGPNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYVRSEPVAQVFVHGESLQAFLIAIVVPDAESLASWARKRGFEGSFEELCRNKDVKKAILEDMVRIGKDSGLKSFEQVRGIALHPELFSVDNGLLTPTMKAKRPELRNYFRSQIDELYSTIKV", "text": "FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity). Preferentially uses palmitoleate, oleate and linoleate (By similarity). Preferentially activates arachidonate than epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs). SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein Peroxisome membrane; Peripheral membrane protein Endoplasmic reticulum membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MVEAGTRDPLESALLDSRYLVQAKIASGGTSTVYRGLDVRLDRPVALKVMDARYAGDEQFLTRFRLEARAVARLNNRALVAVYDQGKDGRHPFLVMELIEGGTLRELLIERGPMPPHAVVAVLRPVLGGLAAAHRAGLVHRDVKPENILISDDGDVKLADFGLVRAVAAASITSTGVILGTAAYLSPEQVRDGNADPRSDVYSVGVLVYELLTGHTPFTGDSALSIAYQRLDADVPRASAVIDGVPPQFDELVACATARNPADRYADAIAMGADLEAIAEELALPEFRVPAPRNSAQHRSAALYRSRITQQGQLGAKPVHHPTRQLTRQPGDCSEPASGSEPEHEPITGQFAGIAIEEFIWARQHARRMVLVWVSVVLAITGLVASAAWTIGSNLSGLL", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MARKEIIDEITMKRAITRITYEIIERNKELDKLVLIGIKTRGVYLAKRIQERLQQLEGLEIPFGELDTRPFRDDKQAQEDTTEIDIDITGKDVILVDDVLYTGRTIRAAIDGIVKLGRPARVQLAVLVDRGHRELPIRADYVGKNIPTGHDEEIIVQMSEHDGNDSILIKRED", "text": "FUNCTION: Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. FUNCTION: Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. FUNCTION: Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines, probably by binding to specific sites on pyr mRNA. This probably disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily."}
{"protein": "MSGEKTEQPTPKKIRDARKKGQVAKSKEVVSTALIVALSAMLMGLSDYYFEHFSKLMLIPAEQSYLPFSQALSYVVDNVLLEFFYLCFPLLTVAALMAIASHVVQYGFLISGEAIKPDIKKINPIEGAKRIFSIKSLVEFLKSILKVVLLSILIWIIIKGNLVTLLQLPTCGIECITPLLGQILRQLMVICTVGFVVISIADYAFEYYQYIKELKMSKDEIKREYKEMEGSPEIKSKRRQFHQEIQSRNMRENVKRSSVVVANPTHIAIGILYKRGETPLPLVTFKYTDAQVQTVRKIAEEEGVPILQRIPLARALYWDALVDHYIPAEQIEATAEVLRWLERQNIEKQHSEML", "text": "FUNCTION: Component of the yop secretion machinery. FUNCTION: Component of the yop secretion machinery. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the type III secretion exporter family."}
{"protein": "MSLQGLMMKRTLLCWPLSCLFVLLPWPLATPTPITPWLCPPGKEPDPDPGQGTLCRTCPPGTFSASWNSYPCQPHYRCSLQKRLEAQAGTATHDTMCGDCQHGWFGPQGVPHVPCQPCSKAPPSTGGCDESGRRGRRGVEVAAGTSSNGEPRQPGNGTRAGGPEETAAQYAVIAIVPVFCLMGLLGILVCNLLKRKGYHCTAQKEVGPSPGGGGSGINPAYRTEDANEDTIGVLVRLITEKKENAAALEELLKEYHSKQLVQTSHRPVPRLLPASPSIPHICPHHHHLHTVQGLASLSGPCCSRCSQKWPEVLLSPEAAAATTPAPTLLPTASRAPKASAKPGRQGEITILSVGRFRVARIPEQRTSSLLSEVKTITEAGPSEGDLPDSPQPGLPPEQRALLGSGGSHTKWLKPPAENKAEENRYVVRLSESNLVI", "text": "FUNCTION: May play a role in apoptosis. Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. Involved in dental enamel formation (PubMed:30506946). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cytoplasm Cytoplasm, perinuclear region. SIMILARITY: Belongs to the RELT family."}
{"protein": "MAYTNNLQIIYGDATLGITGKNFHYLFSYERGGLESLNINNKEWLYRVPTPTFWRATTDNDRGNGFNLKASQWLGADMFTKCTKIELKVDDRQFDELPIAPINNQFSNHEYADHVQIAFWYQTLTNPATDVKIIYNIDNTGCINIVMHYFGKKGLPPLPVIGMRFIMPTAATGFDYEGLSGETYPDRMAGAKEGKFHVDGLPVTKYLVPQENGMHMQTKALKITRSSTLNNADQESEFSLKLKQDKQPFNFSCLPYTAEELENATHLEELPLARRTVLVIAGAVRGVGGIDSWGADVEKQYHINPEKDYEFSFNLN", "text": "FUNCTION: Component of a beta-galactosidase. SIMILARITY: Belongs to the bacterial beta-galactosidase small subunit family."}
{"protein": "MLAKQTPLTKQMLSELLRASSSKPKQLKKIHAIVLRTGFSEKNSLLTQLLENLVVIGDMCYARQVFDEMHKPRIFLWNTLFKGYVRNQLPFESLLLYKKMRDLGVRPDEFTYPFVVKAISQLGDFSCGFALHAHVVKYGFGCLGIVATELVMMYMKFGELSSAEFLFESMQVKDLVAWNAFLAVCVQTGNSAIALEYFNKMCADAVQFDSFTVVSMLSACGQLGSLEIGEEIYDRARKEEIDCNIIVENARLDMHLKCGNTEAARVLFEEMKQRNVVSWSTMIVGYAMNGDSREALTLFTTMQNEGLRPNYVTFLGVLSACSHAGLVNEGKRYFSLMVQSNDKNLEPRKEHYACMVDLLGRSGLLEEAYEFIKKMPVEPDTGIWGALLGACAVHRDMILGQKVADVLVETAPDIGSYHVLLSNIYAAAGKWDCVDKVRSKMRKLGTKKVAAYSSVEFEGKIHFFNRGDKSHPQSKAIYEKLDEILKKIRKMGYVPDTCSVFHDVEMEEKECSLSHHSEKLAIAFGLIKGRPGHPIRVMKNLRTCDDCHAFSKFVSSLTSTEIIMRDKNRFHHFRNGVCSCKEFW", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PPR family. PCMP-H subfamily."}
{"protein": "MESIPLSPFDLQGSFSNIPYAFFYENTQSENDFMPFDFLKGSLWASLQRFPILTGRLRARSTGHIVVEVDAGNPNQPDIRETLCDSVHWSQLKESSFAWDAWPAGVATVGPVATAAADGEIKLLNIHVMRLAQNSGVILFINIPHYVVDGVGYFAFINHWAETMRMQQQQQEQENEARSRFSFDRGIIQRYLPTERAPLDPLTASIYGQRNLLVDWLAWLSPTTLGGLLSKTAAMARGEAHLFRIPRASLDQVHKDVQPYIPASARLSDNDLLVALISKTYIQSQPQPKPPTGFLSWLRPGQGQPESHCTVRIPCDVRRHLKVRERYTGNLLLGMMVRTPLAELARPTSSETLAAAALNVRQSIERVQPGLVAAYHDLIQANPTSHMRPLAFTATRTTTSLVTTSQVRFPMYEADFGSGKPCFVCLTPVFAGSYTMAAILPTPEGREGGVYVLLTSNVEAMQGIKKNQYWNGLVEIIW", "text": "FUNCTION: Acyltransferase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24- dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519). SIMILARITY: Belongs to the plant acyltransferase family."}
{"protein": "MFQLLRCVPRVLGTAVAGLRAAAPSLPRLQPASRPCARPFGLLSVRARSVQLPGLLKPRGPCACGCGCSGLHTEGDKAFVDFLSDEIKEEKKIQKYKSLPKMSGGWELEVNGTEAKLVRKVAGEKITVTFNINNSIPPAFGGEEEEPSQGQKAEEQEPELTSTPNFVVEVTKDGSSKALVLDCHYPEDEIGQEDDQSDIFSIKEVSFQATGESDWKDTNYTLNTDSLDWGLYDHLMDFLADRGVDNTFADELVELSTALEHQEYISFLEDLKGFVKSK", "text": "FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA- binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense. SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Cell membrane; Peripheral membrane protein; Extracellular side Secreted Cytoplasm Nucleus, nucleolus Note=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes. SIMILARITY: Belongs to the MAM33 family."}
{"protein": "MSLLLSFYLLGLLVRSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAIMMPQKSFNATAERGEEMTLTCKASGSPDPTISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFVQPHILQLKNETTSENGHVTLVCEAEGEPVPEITWKRAIDGVMFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDIEYAPKFVSNQTMYYSWEGNPINISCDVTANPPASIHWRREKLLLPAKNTTHLKTHSVGRKMILEIAPTSDNDFGRYNCTATNRIGTRFQEYILELADVPSSPHGVKIIELSQTTAKISFNKPESHGGVPIHHYQVDVKEVASETWKIVRSHGVQTMVVLSSLEPNTTYEIRVAAVNGKGQGDYSKIEIFQTLPVREPSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLGYSEPTVYEFSMPPKPNIIKDTLFNGLGLGAIIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERITNHEDGSPVNEPNETTPLTEPEKLPLKEENGKEVLNAETIEIKVSNDIIQSKEDDIKA", "text": "FUNCTION: May play important roles in selective fasciculation and zone- to-zone projection of the primary olfactory axons. SUBCELLULAR LOCATION: [Isoform Short]: Cell membrane; Lipid-anchor, GPI-anchor. SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane; Single-pass type I membrane protein."}
{"protein": "VIIYELNLQGTTKAQYSTILKQLRDDIKDPNLXYGXXDYS", "text": "FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
{"protein": "MSSEVLPASIEPPNVEGKPGASDSEEERQKQRVDAEAQPISKRQLKKLMKQRLWEEQREQRKEKRKEKRKRKKLERRCQLESNSDGNDRKRIRRHVAPSNLRLIIDCSFDDLMVLKDIKKLHKQIQRCYAENRRASHPVQFYLTSHGGQLKKNMDENDQGWVNWKDIHIKSEHYSELIKKEDLVYLTSDSPNVLKDLDESKAYVIGGLVDHNHHKGLTFKQASSYGIKHAQLPLAEFVKMNSRKVLAVNHVFEIILEFLETGDWQEAFFTILPPRKGAVPAHKACESSPQDHQALPGGWDSAIEGEHGRDDPGSPHKEQQGQQSSSVSAVSPDPQ", "text": "FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)- methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. TRM10 family."}
{"protein": "MKFSKIACAAAFVLSSQAAIIHHAPEFNMKRDIATADPVVAEPDVSVAANVDTSIAKRSIIGILTAILNNVPQIINVITTIIKSITGNKREDIDSVVSGVIADMPFVVRAVDTALTSVASTKRDGTNDDVTNAIVRLPEIVAPVATGVQQTVENAKRDGVEDIGLNIVANSPRLVSDVIGGVSETVKQAKRDNAEDILTKVLQELPDIISKVSNSTLKNSPPFKRDANTVTLSKLIKKSIETIGVENAAKMVSKRDISSLIAEYFEEA", "text": "FUNCTION: Secreted protein cleaved by KEX2 in 8 similar peptides (ECE1- I to ECE1-VIII). Stimulates biofilm formation. FUNCTION: [Candidalysin ECE1-III]: Acts as a cytolytic peptide toxin that directly damages host epithelial membranes, triggers a danger response signaling pathway and activates epithelial immunity (PubMed:35073742). Probably acts similarly to cationic antimicrobial peptide toxins, inducing lesions after binding to target cell membranes and causing an inward current associated with calcium influx (PubMed:35073742). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: [Candidalysin ECE1-III]: Host cell membrane."}
{"protein": "MTKRTLQGSKRKKIRVSGFRARMKTPCGRSILNSRRRKGRKKIMVS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
{"protein": "MATIKSIKARQIFDSRGNPTVEVDVHISNGVFARAAVPSGASTGIYEALELRDGGSDYLGKGVSKAVNNVNSIIGPALVGKDPTDQTGLDNFMVHQLDGTQNEWGWCKEKLGANAILAVSLAVCKAGAAVRNVPLYKHIADLAGNKKLVLPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFKEAMKMGCEVYHHLKAVIKKKYGQDATNVGDEGGFAPNIQENKEGLELLKTAIEKAGYTGKVVIGMDVAASEFYGKDKSYDLNFKEESNDGSQKISGDQLKDLYKSFVSEYPIVSIEDPFDQDDWETYAKLTAEIGEQVQIVGDDLLVTNPKRVAKAIAEKTCNALLLKVNQIGSVTESIEAVKMSKKAGWGVMTSHRSGETEDTFIADLAVGLSTGQIKTGAPCRSERLAKYNQLLRIEEELGSEAVYAGASFRKPVEPY", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the enolase family."}
{"protein": "MLLANAPHNGCSRLQQVTLLRASGAKLHRKRALTVVARTGTPQPRLPLSTQTSASLRAAREQAVLQSLLFAGPDQLLLGVLAGSRLGNGKGAAAVLEAELGGGDCDSVREWLNEQSGSTAAKLQGSGWLRPSDVEFSPAARRVLSLAEAGAEAMGSSSVGTYHLLLVLMGAGGEQQAVQAGAEVASTEQVDGSGMAANSRGSTSGSEQPPRDSDLGLLRSLLDVAGVDRTALEVKLLALAEAGAEMPPAQDSQATAAGVVATLTSVYRQQVARAWHERDDNAFRQAHQNTAMATGPDPDDEYE", "text": "FUNCTION: Accessory protein regulating the assembly of the plastid Clp protease system. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ClpA/ClpB family."}
{"protein": "MGEDTDTRKINHSFLRDHSYVTEADVISTVEFNHTGELLATGDKGGRVVIFQREPESKNAPHSQGEYDVYSTFQSHEPEFDYLKSLEIEEKINKIKWLPQQNAAHSLLSTNDKTIKLWKITERDKRPEGYNLKDEEGKLKDLSTVTSLQVPVLKPMDLMVEVSPRRIFANGHTYHINSISVNSDCETYMSADDLRINLWHLAITDRSFNIVDIKPANMEDLTEVITASEFHPHHCNLFVYSSSKGSLRLCDMRAAALCDKHSKLFEEPEDPSNRSFFSEIISSVSDVKFSHSGRYMLTRDYLTVKVWDLNMEARPIETYQVHDYLRSKLCSLYESDCIFDKFECAWNGSDSVIMTGAYNNFFRMFDRNTKRDVTLEASRESSKPRAVLKPRRVCVGGKRRRDDISVDSLDFTKKILHTAWHPAENIIAIAATNNLYIFQDKVNSDMH", "text": "FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family."}
{"protein": "MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFLETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES", "text": "FUNCTION: Stores iron in a soluble, non-toxic, readily available form (By similarity). Important for iron homeostasis (By similarity). Has ferroxidase activity (By similarity). Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity). Also plays a role in delivery of iron to cells (By similarity). Mediates iron uptake in capsule cells of the developing kidney (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferritin family."}
{"protein": "QDLPGNDNSTATLCLGHHAVPNGTLVKTITDDQIEVTNATELVQSSSTGKICNNPHRILDGRDCTLIDALLGDPHCDVFQDETWDLFVERSNAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSNACKRGPNSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGVHHPSTNQEQTNLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGQSGRISIYWTVVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGLFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNADVLVALENQHTIDLTDSEMNKLFERTRRQLRENAEDMGNGCFKIYHKCDNVCIESIRNGTYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWACQRGNIRCNICI", "text": "FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin- independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host apical cell membrane; Single-pass type I membrane protein Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. SIMILARITY: Belongs to the influenza viruses hemagglutinin family."}
{"protein": "MVSSQKLEKPIEMGSSEPLPIADGDRRRKKKRRGRATDSLPGKFEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKDKVSLCHLGWSAMAPSGLTAAPTSLGSSDPPTSASQVAGTTGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGQAPEKGLPTPQVLQRNSSTMDLTLFAAEAIALNRQLSQHEENELAEEPEALADGLCSMKLSPPCKSRLARRRALAQAGRGEDRSPPTAL", "text": "FUNCTION: May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine- containing mRNA cap. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
{"protein": "MNQKKDEKVINQAVKMLTISEDEAGQRIDNYLLAKLKGVPKSLIYRILRKGEVRVNKGRIKPEYKLQANDIVRVPPVRVSEKEHAPISTKLNKVSQLEKQILFEDECLLVLNKPSGIAVHGGSGLSFGVIEALRTLRPDARFLELVHRLDRDTSGILLVAKKRSALRSLHEQLREKTVQKDYLALVRGQWQSHCKVVKAPLLKNELSSGERIVRVSEQGKPSETRFSIEERYEYATLVKASPVTGRTHQIRVHTQYAGHPIALDDKYGDKHFDEQMTQLGLTRLFLHAFSIRFEHPKTGETLRINAPLDPEMKKILGALREQKSSN", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil at positions 955, 2504 and 2580 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RluA family."}
{"protein": "MRGAYYVAFALLVAASTRTAAEPDQAEPHIAPNNDYMTSGGAFNKMLPRRILRESPDPKDRLPVYASDEERMVNRLSNGNSIAKGLERTIMKAANVLRTNGEDVIANAAKPIKNYNRLRPKLEIKKSKRQRIEPTLSKSSEHKLHTTSNSKKSLVSSASAKGQGRDEPRATVNTAKKMQHNHRSAPSRSSPTSADVSDGRLEKQLNAQKAINLDKNKRPDEAKIRNKKQHVIDPTPKNENGQALRAPPTPESLGIGGKQCTVRIGREK", "text": "FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MSTAKLVKTKASNLLYTRNDVSDSDKKATIELLNRQVIQFIDLSLITKQAHWNMRGANFIAVHEMLDGFRTALVTHLDTMAERAVQLGGVALGTTQVINSKTALKSYPLDIHSVQDHLKELADRYAIVANDVRKAIGEAKDEDTADILTAASRDLDQFLWFIESNIE", "text": "FUNCTION: During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Dps family."}
{"protein": "MTLLVGLVLILVGLIAWNICIWGYIIKWGYRRYKRHRLETEIERLNLILRERAEDSGNESNGEEEERLEQLIHNYNHNNHFANPMFDL", "text": "FUNCTION: Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo (By similarity). SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein."}
{"protein": "VAVKKIMKPFSTPVLAKRTYRELKLLKHLKHENVISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQIMRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINTIASENTLRFVKS", "text": "FUNCTION: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily."}
{"protein": "SPTLDDEHNDNFVRL", "text": "FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRF amide related peptide) family."}
{"protein": "MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSVLSRGHEERKTKRPSLRLFGDHDYCQSVNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSSQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPSQAVFDDKVDKTSELRDGNFSNEQFSKLPVFINSGLAMDGLFDDSEDENDKLSYPWDGTQSYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEANEHERLKRDEYRREYEKRESERAKQRERQKQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDSNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR", "text": "FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program (By similarity). Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, PML body."}
{"protein": "KYYGNGVTCGKHSXSVDWSKATTNI", "text": "FUNCTION: Bactericidal activity against a wide range of pathogenic bacteria, including Bacillus spp., Enterococcus spp., Listeria spp., Staphylococcus spp. and Streptococcus spp (PubMed:21477375). Has no activity against Lactobacillus salivarius, Staphylococcus aureus, Streptococcus pyogenes and Streptococcus suis (PubMed:21477375). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family."}
{"protein": "MVDYHAANQAYQYGPSSGGNGTGGGGGMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTSVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHLRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAAPGALDYKSFSTALYGESDL", "text": "FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell junction Cytoplasm, cytoskeleton, stress fiber Cytoplasm, perinuclear region Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). SIMILARITY: Belongs to the alpha-actinin family."}
{"protein": "MVLPVADLPDDVDALKAMILAMAKERAANEARLAAAAAEVARLKAVEKSANERIANLTSILKVLQRTQHGTRSERLRLAVNDEQVSFAFEEVETGLSEIQSELNRAAGDKPKRAPRPRKGFAAHLERIEEVIEPEVPADCAGLEKVLIGEDRSERLDVVPPKFRVIVTRRPKYAFRGRDGVVQALAPAHLIESGLPTERLLAYIAVSKYADGLPLYRQEAIYLRDGVEVSRSLMAQWMGHLGFELQMLADYILERVKEGERVFADETTLPTLAPGSGKTTKAWLWAYARDDRPYGGTSPPMVAYRFEDGRGADCVARHLAGFSGILQVDGYSAYTNLAKARAKTGSNETIQLAGCWAHLRRKFYDLHISGVSQAATDSIIAMTELWRLEDEVRGKDAASRAELRQEKSSAIVASLFELWEKELGKVSGKSKTAEAIRYALTRREALERFLTDGRIEIDSNIVERAIRPQTITRKNSLFAGSEGGGRTWATVATLLQTCKMNGVDPLDWLSQTLTRIAQGWPASEIEALMPWNFKPDAIG", "text": "SIMILARITY: Belongs to the transposase 25 family."}
{"protein": "MVSNLPSILVPMVGIVLPAIVMALLFVYIETDEIA", "text": "FUNCTION: May help in the organization of the PsaL subunit. SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaI family."}
{"protein": "MSEFWLCFNCCIAEQPQPKRRRRIDRSMIGEPTNFVHTAHVGSGDLFSGMNSVSSIQNQMQSKGGYGGGMPANVQMQLVDTKAG", "text": "FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T- cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages. FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T- cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell membrane; Lipid-anchor Cell projection, phagocytic cup Note=Recruited to the activated TCR prior actin polymerization. Localizes at the phagocytic cup of macrophages. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Lipid- anchor. Cell projection, phagocytic cup. Note=Recruited to the activated TCR prior actin polymerization. Localizes at the phagocytic cup of macrophages. SIMILARITY: Belongs to the CDC42SE/SPEC family."}
{"protein": "MDIDDILRQVDPSSHGVPSEARDLQALTRLWVAERSAPELLEWPTDGLFERVNARIKTQIEKVEDMTGDMDPKTNFALIVIQTELERYKFLMRSFLRARLAKIDKHTLHYLSSQELRDRLSPTELSYATKHQALLHNHYLSSFLASFPQQLQNLNDTAGNISMIDSPDLDTAVFIRMLRDKDVYGKGTDADITLPATNGDVLIIRWSSAKHMVDVGDAELV", "text": "FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GINS4/SLD5 family."}
{"protein": "MKCILLNQAEELPIEFLPKDGVYGKGKLFDSRNMEIENFTESDILQDARRAAEAHRRARYRVQSIVRPGITLLEIVRSIEDSTRTLLKGERNNGIGFPAGMSMNSCAAHYTVNPGEQDIVLKEDDVLKIDFGTHSDGRIMDSAFTVAFKENLEPLLVAAREGTETGIKSLGVDVRVCDIGRDINEVISSYEVEIGGRMWPIRPISDLHGHSISQFRIHGGISIPAVNNRDTTRIKGDSFYAVETFATTGKGSIDDRPPCSHFVLNTYKSRKLFNKDLIKVYEFVKDSLGTLPFSPRHLDYYGLVKGGSLKSVNLLTMMGLLTPYPPLNDIDGCKVAQFEHTVYLSEHGKEVLTRGDDY", "text": "FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily."}
{"protein": "MAKKQSIRSRNFRRSDPAYDLDSSTAIENETKLSVKEKVAKEIANIALRSGGSESNGISKKKKNKKQTSKKAKDKLAAALKAQAREERLDTKISKSLQKQEKLKARKQGDE", "text": "FUNCTION: Pre-ribosomal factor involved in 60S ribosomal protein subunit export from the nucleus. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the ECM1 family."}
{"protein": "MAAGGNGAGGDTRAAFARIYKTLKEELLTDPAFEFTEESRQWIDRMVDYNVLGGKCNRGLSVVDSYKLLKGADALGEEETFLACTLGWCIEWLQAFFLVLDDIMDDSHTRRGQPCWFRVPQVGLIAANDGIILRNHISRILRRHFKGKPYYADLLDLFNEVEFKTASGQLLDLITTHEGEKDLTKYNITVHGRIVQYKTAYYSFYLPVACALLLSGENLDNYGDVENILVEMGTYFQVQDDYLDCYGDPEFIGKIGTDIEDYKCSWLVVQALERADESQKRILFENYGKKDPACVAKVKNLYKELDLEAVFQEYENESYKKLIADIEAQPSIAVQKVLKSFLHKIYKRQK", "text": "FUNCTION: Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FPP/GGPP synthase family."}
{"protein": "MSKMESTQQMASSIINTSFEAAVVAATSTLELMGIQYDYNEVYTRVKSKFDYVMDDSGVKNNLLGKAATYDQALNGKFGSAARNRNWMADTRTTARLDEDVNKLRMMLSSKGIDQKMRVLNACFNVKRVPGKSSSIIKCTRLMRDKIERGEVEVDDSFVEEKMEVDTIDWKSRYEQLEKRFESLKQRVNEKYTSWVQKAKKVNENMYSLQNVISQQQSQIADLQNYCNKLEVDLQNKISSLVSSVEWYLKSMELPDEIKTDIEQQLNSIDVINPINAIDDFESLIRNIILDYDRIFLMFKGLMRQCNYEYTYE", "text": "FUNCTION: Plays an important role in stimulating the translation of viral mRNAs. These mRNAs are capped but not polyadenylated, instead terminating in a conserved sequence 'GACC' at the 3' that is recognized by NSP3, which competes with host PABPC1 for EIF4G1 binding. The interaction between NSP3 and host EIF4G1 stabilizes the EIF4E-EIF4G1 interaction, thereby facilitating the initiation of capped mRNA translation. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the rotavirus NSP3 family."}
{"protein": "MKSIRISSDYRAKRDNASCFDETFLKSFAEELYNAIIEIIKENKTIIKNEVRDELRNELATKEDILLVEERLGKKIELLNQKIEREIKLVRRDMIIINLVIILAMYAPEIIGKLLIFR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the M.jannaschii MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family."}
{"protein": "MILFQSNTTTSYAYTNIQPKYAMQLEITILIVIGILILSVILYFIFCRQIPNVHRNSKRRPIYSPMISRPHMALNEI", "text": "SUBCELLULAR LOCATION: Host nucleus membrane; Single-pass membrane protein. SIMILARITY: Belongs to the adenoviridae E3A-1 family."}
{"protein": "MSCSSLCAPACVATPTPLADSCNEPCVRQCPDSTVVIQPPATVVTFPGPILSSFPQYAAVGSAGVPAVGSGMGGTFGRGAGFGGYGGLGGYGGYGGLGGYGGYGGFGSCGYGGFGRGYRSLLGSCGPC", "text": "SIMILARITY: Belongs to the avian keratin family."}
{"protein": "MELPPNPGLVDVQRDALYAYDSEAHKAVVNSRPWTNDHKYFKTVRISSVAMIKMVMHARSGGNLEVMGMMQGYIEGSTMVITDAYRLPVEGTETRVNAQDEANEYMVEYLRLCREENRLENVIGWYHSHPGYGCWLSGIDVGTQSLQQQFNEPFVAVVIDPDRTVSQNKVEIGAFRTIPEGIKPFAATNTTTGDGQSVPLNKVEDFGAHSHRYYALDVEHFKSTLDSKLLETLWNKYWVQTLAQNPLLTNRDYTSSQMVDLGSRISKASKSLEMLSTTGQRGPKSDAVDQNIEKLLSEVKQIAAKERSGLMAAEVKGKVFGCGCRGQAEGVQPEKS", "text": "FUNCTION: Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the circadian clock through its control of the stability of the SCF(FWD-1) complex. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily."}
{"protein": "PTADAIAAKKMENGKAAIDFPDQSVIRRVSSADRISLQDIARERVDVICDRMHRLPDEFLDELKNGLRAILEGGNGSQHRDEFFILQKLVQSRSDLTAKTLIRAHRVQLEILVSINTGIQGFLHPSISLSQTSLIEIFLYKRCRNIACQNQLPADECSXDTCTNNNGFCNLCMCVICSKFDFEVNTCRWIGCDLXSHWTHTDCAIREQLICMGPSVKSGSGPSEMVFRCQACSXTSXLLGWVKDVFQHCAPSWDGDALIRELDFVSRIFHGSKDQRGMNLFWKCDDLKEKLKSRKMDSKAACRAILMVFQELDLDNSKSLENAESGRLIAPQEACNRIAEVVQEAIRKMEFVADEKMRMFKKARIAVEACDRELADKAREAGDLKVERQKKKSQIEELERIVRLKNAEADMFQLKANEAKREAERLQRIALAKSDKSEEEYTSNYLKQKLSEAEAEKQYLYEKIKLQESSRLSQSSGDPSSMLMYSKIHDLLYNGPPKADSQSNDCHPFRTNP", "text": "FUNCTION: Required for the maintenance and/or establishment of both the shoot and root meristems, probably by controlling the expression of the meristem genes and of genes required for auxin responses. Involved in the development of the basal pole and in auxin-mediated root and vascular development in the embryo (By similarity). Confers sensitivity to turnip mosaic virus (TuMV) probably by promoting viral movement and multiplication via interaction with TuMV VPg (Probable). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTAKSDEPGRWTVAVYCAAAPTHPELLELAGAVGAAIAARGWTLVWGGGHVSAMGAVSSAARAHGGWTVGVIPKMLVHRELADHDADELVVTETMWERKQVMEDRANAFITLPGGVGTLDELLDVWTEGYLGMHDKSIVVLDPWGHFDGLRAWLSELADTGYVSRTAMERLIVVDNLDDALQACAPG", "text": "FUNCTION: Catalyzes the hydrolytic removal of ribose 5'-monophosphate from nitrogen N6-modified adenosines, the final step of bioactive cytokinin synthesis. SIMILARITY: Belongs to the LOG family."}
{"protein": "MKLEFTEKNYNSFVLQNLNKQRKRKEYWDMALTVDHHVFFAHRNVLAAVSPLVKSLVSSNDMKTTDELYITIDPNYLSPATVDQLLDYFYSGKVVISEQNVEELLRGAQYFNTPRLRIHCNDFLIKSIRRVNCLRYLFLAELFELKEVSDLAYSGIRDNFHFWASPEGSMHFMRCPPVIFGRLLRDENLHVLNEDQALSALINWVYFRKEEREKYFKKFFNYINLNAVSNKTLMFASNKLTGLENNSAHATLIESVLMDRKQERPCSLLSYQRKGALLDSVVILGGQKAHGKFNDGVFAYIIQENLWLKLSEMPYRAAALSATAAGRYIYISGGTTEQISGLKTAWRYDMDDNSWTKLPDLPIGLVFHTMVTCGGTVYSVGGSIAPRRYVSNIYRYDERKEAWCLAGKMSIPMDGTAVITKGDRNLYIVTGRCLVKGYISRVGVVDCFDTCTGEVVQCITFPIEFNHRPLLSFHQDNILRVHSHRQSVEINLQKIKANKSTTSVPLLPNSCPLDVSHAICSIGDSKVFVCGGVTTASDVQTKDYTINPNAYLLDQKIGEWKTLACPPEALDCPACCLAKLPCKILQRI", "text": "FUNCTION: Possible morphogenetic cytoskeletal element in spermiogenic differentiation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca, calyx Note=Sperm head cytoskeletal structure tightly associated to the nucleus."}
{"protein": "MSELKERLLPPRPASAMNLRDASVTRPSASGRPPLLGVDVLGLKKRGQGLRSWIRVDTSGNTQVMEVDKFTMMRRCDLPARDLRLLDPLFVYPSTILGREKAIVVNLEQIRCIITADEVLLLNSLDNYVLRYVVELQQRLKTSSVGEMWQQENSQLSRRRSRSFDNAFENSSPDYLPFEFRALEIALEAACTFLDSQASELEIEAYPLLDELTSKISTLNLERVRRLKSRLVALTRRVQKVRDEIEQLMDDDGDMAEMYLTEKKRRMEGSMYGDQSLLGYRSNDGLSVSAPVSPVSSPPDSRRLDKSLSIARSRHDSARSSEGAENIEELEMLLEAYFVVIDSTLNKLTSLKEYIDDTEDFINIQLDNVRNQLIQFELLLTTATFVVAIFGVVAGIFGMNFEIDFFNQPGAFRWVLIITGVCGFVIFSAFVWFFKYRRLMPL", "text": "FUNCTION: Magnesium transporter that may mediate the influx of magnesium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35.5) family."}
{"protein": "MAKCGSCGPGYKSPLDAMKGPREEIVYLPCIYRSTGINKPDYLATVDVDPKSPSYSQVIHRLPMPNVNDELHHSGWNTCSSCYGDSSKVRNKLILPCLISSRIYVVDVGSDPRAPRIHKTVEPYEVFWKCGLANPHTSHCLGCGEIMISSLGDPCGNGKGGFVLLDGETFEVKGNWEVEGESAQFGYDFWYQPRHNVMISTEWGAPKAFALGFKMEDVQAGHYGHSLNVWDWTEHRLVQTIDLGKDGLIPLEIRFLHNPDADQGLVGCALSSSIFRFYKEKDGKWAAEKVIQVPSKKVEGWPMPEMPGLITDILISLDDRFLYFSNWLHGDIRQYDITDTRNPKLVGQIFLGGSIQRGGPVTVLEDKELECQPDPVTVKGKIIPGGPQMIQLSLDGKRIYVTSSLYSIWDKQFYPDLLKEGAVMLQIDVDTKKGGLKLNPNFLVDFGKEPDGPVLAHEIRYPGGDCTSDIWI", "text": "FUNCTION: Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria (By similarity). Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the selenium-binding protein family."}
{"protein": "MSSNKTEKPTKKRLEDSAKKGQSFKSKDLIIACLTLGGIAYLVSYGSFNEFMGIIKIIIADNFDQSMADYSLAVFGIGLKYLIPFMLLCLVCSALPALLQAGFVLATEALKPNLSALNPVEGAKKLFSMRTVKDTVKTLLYLSSFVVAAIICWKKYKVEIFSQLNGNIVGIAVIWRELLLALVLTCLACALIVLLLDAIAEYFLTMKDMKMDKEEVKREMKEQEGNPEVKSKRREVHMEILSEQVKSDIENSRLIVANPTHITIGIYFKPELMPIPMISVYETNQRALAVRAYAEKVGVPVIVDIKLARSLFKTHRRYDLVSLEEIDEVLRLLVWLEEVENAGKDVIQPQENEVRH", "text": "FUNCTION: Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the type III secretion exporter family."}
{"protein": "MKNAFKDALKAGRPQIGLWLGLANSYSAELLAGAGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGAQTLLIPMVQNADEARNAVAATRYPPAGIRGVGSALARASRWNRIPDYLHQANDAMCVLVQIETREAMSNLASILDVDGIDGVFIGPADLSADMGFAGNPQHPEVQAAIENAIVQIRAAGKAPGILMANEALAKRYLELGALFVAVGVDTTLLARGAEALAARFGAEKKLSGASGVY", "text": "FUNCTION: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2- ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde. SIMILARITY: Belongs to the HpcH/HpaI aldolase family."}
{"protein": "MDNIFVPSNIYMVRTPIFSIELYNQFLKSDNIDYDLILQNDIFKESIMTTTYNLYQSIGKIDWEKDNKKTRNVKESLLKYLIRMSTRSTPYGMLSGVALGEFSENNNIKIKDSSFHKKDVKIDGQWLYKLVHYLESDYTYYKDSFVIWNQQNYIYNNRLYLDNNSSITENKRNDVLSVKYNSILVFIHENSKKNITYEELVQLISSKYSIENKEEVKVFVQELINKEIIFSDLRPTLENKNPLDYIINSLNPKNSLVGTLINISNEITKYSKMPLGKGEYKYLDIVNLMSQLFVSKNYLQIDTYIDYSRNELKQSLADNISEAAYILWLLSPNHFGTKTIRNYHEFFMDKYGFEQLVNLKQLLSDINGFGYPKKDSYSFSNNIAFLKEKYLLAIQNNSHIEITENDVKNLEKNNTVSKINAPVSTEIYSEIYFGNSIKGYEDFAVISPILGSFNAGATFGRFTGNFNIKKKNQLQKEIVHHYNNYMNENGLEISQLNEGPLNSRNVNILNNNRIYNTCLNLNLPKSDIDINDIFIGATFNKLYLYSEKHDSRIVFVSNSMFNYEFGSELYKFLREISFEKTKFIQPITEEGIDSLPFCPRIIYKNIILKPATWKINSEMFSETENWLNRFATIREKWHIPKDVIIAFGDNRLLLNLLNDKHLIILKKELKKHGRIRILESFINESNNERMLEIVTPLYKKTSLKEQSFIIPKNRNKHFNNLKDWFSIHLSIPKTYQDNFIQDYLLPFITELKVNNFINKFFYIKFKEDEDFIKLRLLREDEDYSQIYSFIKNWKDYCLLNSELYDYSIVDYVPEVYRYGGPHVIEDIENFFMYDSLLSINIIQSEFKIPKEFIVAISIDFLLDYLEINKSEKEEILINNAEDLYRSNDIREYKNLLAKLTNPKNDYEILKKEFPNLHEFLFNKISILENLKKTLQKSLYTSRSRIIGSFIHMRCNRIFGINPEKEKFVLSIFNEITKTKKYWDGCD", "text": "FUNCTION: Involved in the post-translational modification of the lantibiotic epidermin. SUBCELLULAR LOCATION: Cell membrane. Note=Possibly associated with, and anchored to, the cytoplasmic side of the membrane. SIMILARITY: To B.subtilis SpaB and L.lactis NisB."}
{"protein": "MDFFSRVPLYDELSGLSQPETKCKLEEFTFSNFLKARRVREFLRAHAVAKLPAMRYVYVYYLFSRIGDYIGDDTVLAIFGEFMGVSDAGKARGEGDGESDVHGEGEEEGDGGGEAEPGVGPDIPEVYRVCECLPVRTKCRISLAIEAITRGQYENNLWEIFRDGIISSSKFYHAVRQQNSSKKLFQPWPIVNNYYPLSPLAFGLRCEDAVKTLLAEFVCGRKEVMCDVGFLQSPKDGIFGVSLDMCANVSVGRDNLLEFRADAEIYEIKCRFKYNYSKIECDPLYQKYVSLYNSPSKTTLIRFLSGINRPAVEYVPPGKLPTKNDFLLTSDRDWDLSPKRKRNLTPAHKSLYDCLRANEHASSQVLILSDPSETEGKIDIKARFDVDVFINPEHSYFYQILLQYKVVKNYIQYHSSPGLGSLKTFIVSGFFRKRNHSDPLECSIGGRGTLDSACEIPVLLILTPVYIPHCVVTESLKKASQYWNQSAEEEFSHPPWVSSSLFADGDMTP", "text": "FUNCTION: Plays a role in processing non linear or branched viral DNA intermediates in order to promote the production of mature packaged unit-length linear progeny viral DNA molecules. Exhibits endonuclease and exonuclease activities and accepts both double-stranded and single- stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'-> 3' direction and the products are 5'-monophosphate nucleosides. Additionally, forms a recombinase with the major DNA-binding protein, which displays strand exchange activity. Also acts as a cytoplasmic RNA endonuclease that induces degradation of the majority of the cellular messenger RNAs during early lytic infection. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and evasion from host immune response. Internally cleaves host mRNAs which are then degraded by the cellular exonuclease XRN1. Bypasses therefore the regulatory steps of deadenylation and decapping normally required for XRN1 activation. SUBCELLULAR LOCATION: Host nucleus Host cytoplasm. SIMILARITY: Belongs to the herpesviridae alkaline nuclease family."}
{"protein": "MRIENKQNKRQHHLLIVDDENNIRKILQTRLTLLGYSVSTACNGEEALKIFTTHSIDLIILDVMMPKLDGYGVCQEIRKESDIPIIMLTALEDVLDKVTGLELGADDYVIKPFSPRELEARIQSILRRIQTRNAKLKPYDNINLFKTGSLNIDLEKKQIYKNNELIRLTEMEFSLLELLVSQSGKAFSRSKILKEVWGYKLSKHEPIADTRIVDVHISRLRAKLEDDPTNPTLILTARGTGYLCRKLIT", "text": "FUNCTION: Probable promoter-specific protein mediating the interaction between DNA and RNA polymerase. SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MKKLAIVFTMLLIAGCSSSQDSANNQIDELGKENNSLFTFRNIQSGLMIHNGLHQHGRETIGWEIVPVKTPEEALVTDQSGWIMIRTPNTDQCLGTPDGRNLLKMTCNSTAKKTLFSLIPSTTGAVQIKSVLSGLCFLDSKNSGLSFETGKCIADFKKPFEVVPQSHLWMLNPLNTESPII", "text": "FUNCTION: Part of the tripartite complex that is required for the CDT activity. CdtC, along with CdtA, probably forms a heterodimeric subunit required for the delivery of CdtB. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
{"protein": "MSTKPELKRFEQFGEIMVQLYERYLPTAFDESLTLLEKMNKIIHYLNEIGKVTNELIEEWNKVMEWILNDGLEDLVKETLERWYEEGKFADLVIQVIDELKQFGVSVKTYGAKGDGVTDDIKAFEKAIESGFPVYVPYGTFMVSRGIKLPSNTVLTGAGKRNAVIKFMDSVGRGESLMYNENVTTGNENIFLSSFTLDGNNKRLGQGISGIGGSRESNLSIRACHNVYIRDIEAVDCTLHGIDITCGGLDYPYLGDGTTAPNPSENIWIENCEATGFGDDGITTHHSQYINILNCYSHDPRLTANCNGFEIDDGSRHVVLSNNRSKGCYGGIEIKAHGDAPAAYNISVNGHMSVEDVRSYNFRHIGHHAATDPQSVSAKNIVASNLVSIRPNNKRGFQDNATPRVLAVSAYYGVVINGLTGYTDDPNLLTETVVSVQFRARNCSLNGVALTGFSNSENGIYVIGGSRGGDAVNISNVTLNNSGRYGVSIGSGIENVSITNISGIGDGINSPVALVSTINSNPEISGLSSIGYPTVARVAGTDYNDGLTLFNGAFRASTTSSGKIHSEGFIMGSTSGCEASVSKSGILTSSSSKTSSERSLIAGSSTSEATGTYNTILGSLGAVADEQFAGLISASQSRASGNHNLILSSYGINTVGSYKVNGGFEKINWELDSLNGRIKARDTVTGGNTWSDFAEYFESLDGQVIETGYLVTLDKGKIRKAEKGEKIIGVISETAGFVLGESSFEWQGAVLKNEFGGIVYEEVTTEDGVKFKRPLPNPDFDPNKNYIPRSQRREWHVVGLLGQIAVRIDDTVKQGQGIDAVGGVATDGNNFIVKEITTPYNKEKGYGVAIVLIK", "text": "FUNCTION: Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation. SUBCELLULAR LOCATION: Virion Note=Present in 36 copies in the virion."}
{"protein": "MSEAEARPSNFIRQIIDKDLADGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYQGQCNLRFDDTNPEKENLEYVESIKKDVTWLGFDWSGEVCYSSDYFDKLYEYAIELIQKGLAYVDELTPEQIREYRGTLTEPGKHSPYRDRSVEENLALFEKMRAGEFAEGQACLRAKIDMASSFIVMRDPVLYRVRFAEHHQTGDKWCIYPMYDFTHCISDALEGITHSICTLEFQDNRRLYDWVLDNITIPCHPRQYEFSRLNLEYTVMSKRKLNQLVTEKLVTGWDDPRMPTISGLRRRGFTPSAIREFCKRIGVTKQENMIEYSALESCIRDDLNENAPRAMAVLDPVKLVIENFAAGTVETLTLANHPNKPEMGDREVPFTRELWIEREDFREEANKKYKRLVLGKEVRLRGAYVIKAERIEKDEQGNITTIFCSYDPETLGKNPADGRKVKGVIHWVSAEKGVPAEFRLYERLFTVPNPGAADNFAETINPESLVKVQGYVEPSLVEAKPEFGYQFERMGYFCADNKDSSPQALVFNRTVGLRDSFAKIDEE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MVLLDSLVGTIVGINGPVIKAEGMSKFKMREMVMVGKKKLIGEIIILENDLATIQVYEETSGLKIGENISSTGMPLSLKLGPGIIGNMFDGIQRPLKKINEISYGFIDEGIGLISIDEEKEWDVNIVVKVGDKLKPGDVYAEVQETNIIKHRIMVPQDVNGEVTKVKESGKYNIEEKIVTVKDGGNIYELNLYQRWPVRTPRPIKNRLSLGKPLITGQRILDMFFPIAKGGTVAIPGGFGTGKTMTQHQLAKWSDADIIVYIGCGERGNEMTEVLEDFPKLIDPKTNTSLMNRTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVAIMADSTSRWAEALREISGRLEEMPAEEGYPAYLPSRIAEFYERAGYVENLNDTEGSVTVIGAVSPAGADFSEPVTQNTKRFVGAFLGLDRKLAYARHYPAINWLTSYSQYNVMLTDWYLENISEDIIELRNKMLKILFEENKLQEIVKLVGEDVLPDDQRLILEVARILKVGFLQQNAYHDEDTYVPKEKQYKMLKAIELFYDNAYKCVKMGIPISKIRNEEIFGDLIKMKYNIPNEDISGIKVIEEKISSYYEELIEQYRK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MFTVKLLAFMVVAVSLQHLAEATPKVCAGCPVEVDPNREDIKKSLAHVMAAKNSPDELVRIIKASTQVVNGIKYKVVFEVKNPSTNQVKICKTAYVSRPWEYEGYNVLEFGCKA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cystatin family."}
{"protein": "MNEEEHNKSVHWSIVYRQLGNLLEQYEVEIARLKSQLVLEKKLRIQVEKELESVKTKQISSSASSKVSSNTIQELDSTTDEDEIPGSDTVDEEDPSLNAPFSEKNQSVKIPPHSPTLPVQNASAFVKPISVPLGNVKEEKFLDTNPIGAESFESSDGEMHLRARSPEDMILLRETQPLAPLDINTLGVSDNRQKKGTEKKRPFEPEFLNDDVIRGNKRKALPAYECPDCQKFYELHGPVKESSVAPTWNDENRLGGGSLPNCKHQPLVQKVGRHRKLNIPKPIPNGFWESDFVD", "text": "FUNCTION: Endonuclease that cooperates with the MRN complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of rec12 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for the formation of RPA-coated single strand DNA adjacent to the DSBs where it functions together with the MRN complex in 5'- 3' resection. Required for the repair of programmed meiotic DSBs. Involved also in an rhp51 recombinase-dependent recombinational repair pathway. SUBCELLULAR LOCATION: Nucleus Note=Accumulates at DSBs. SIMILARITY: Belongs to the COM1/SAE2/CtIP family."}
{"protein": "MGKHDKKTGKGRLDKFYRLAKEQGYRARSAFKLVHLNRKYDLLSKARCCIDLCAAPGGWLQVAEKYMPKGSLIIGVDLNAIKPLPHVTTFVADITTPHCRQTLRQHMHDWKADLVLHDGAPNVGSAWVQDAFTQNELVLQSLKLATEFLAKGGSFVTKVFRSQDYNSLLWVFGQLFKSVEATKPPSSRNVSAEIFVVCRDFIAPKHIDPKFLDPKHVFKDIASLPTSITEPTDTSIAPTSSSTASAAAAAARLAANSHAHSNVYAPEKKRRHREGYAEGDYTLHHTASAEEFVRGQDPVLLLGNMNKIEFRNETEKGWLKSRHTTPDIIANFEDLKVLGKGDFKALMKWRLAIRLEIGLDVKADKTQDATEEVVVEPMDEEEQITEELQKLQQAKLAKTKRERKRANEKKARELLKLQLNMTVPDDLDQNDLALQGEEEIFDLEEGENEARRRGKNGGLATLVDDGEGMDLASESEEEEDEDEEDDEVLDSDEERERKTAALEGELDGLYDSYVERKKERDAKWKVKQDRLKDKNFDAWHGIQEKSDEEGSDDDDGQDDDEEGGWDVIAQKKAKYGEGDSSDSDSDAEPETEVPKKIKKVSFEKPARSEKSSGLMTSLREPELRAQRSKQAQLWFDQPVFKEVGDLAALDGDDEEEEEEDESEEEESDDEDVDMEDASESSSTLEGDDDFEIVPQAPEDDGPEWDVDDEDQDEVKKKVIQDKGLLTAEAVSLATALVNRKTTADKLIDQGFNRLSAHNKDGLPTWFLDDESQFYKPNIPITKEAVDALRARQRALDARPIKKVAEAKGRKKMKAVARMEKAKKKADGVMESEEMGDGEKARQVRRMLARAAKGKEKAKEKKIVVAKGVNKGVKGRPTGVKGKYKIVDARMRKEVRALKRIKKAGSKRR", "text": "FUNCTION: Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily."}
{"protein": "MAQKKYLQAKLTQFLREDRIQLWKPPYTDENKKVGLALKDLAKQYSDRLECCENEVEKVIEEIRCKAIERGTGNDNYRTTGIATIEVFLPPRLKKDRKNLLETRLHITGRELRSKIAETFGLQENYIKIVINKKQLQLGKTLEEQGVAHNVKAMVLELKQSEEDARKNFQLEEEEQNEAKLKEKQIQRTKRGLEILAKRAAETVVDPEMTPYLDIANQTGRSIRIPPSERKALMLAMGYHEKGRAFLKRKEYGIALPCLLDADKYFCECCRELLDTVDNYAVLQLDIVWCYFRLEQLECLDDAEKKLNLAQKCFKNCYGENHQRLVHIKGNCGKEKVLFLRLYLLQGIRNYHSGNDVEAYEYLNKARQLFKELYIDPSKVDNLLQLGFTAQEARLGLRACDGNVDHAATHITNRREELAQIRKEEKEKKRRRLENIRFLKGMGYSTHAAQQVLHAASGNLDEALKILLSNPQMWWLNDSNPETDNRQESPSQENIDRLVYMGFDALVAEAALRVFRGNVQLAAQTLAHNGGSLPPELPLSPEDSLSPPATSPSDSAGTSSASTDEDMETEAVNEILEDIPEHEEDYLDSTLEDEEIIIAEYLSYVENRKSATKKN", "text": "FUNCTION: Specific down-regulator of the NEDD8 conjugation system. Recruits NEDD8, UBD, and their conjugates to the proteasome for degradation. Isoform 1 promotes the degradation of NEDD8 more efficiently than isoform 2. SUBCELLULAR LOCATION: Nucleus Note=Predominantly nuclear."}
{"protein": "MSGTAGTSRILRVYLDGPHGVGKSTTAEALVARCEPRRPIRSMLQEPMAYWRSTFASDAITEIYDTQHRLDSNEITAAEAGAFMTSLQLHMGTPYALLEEAMRPHVGRELAEPDDNGPLPQRRDFVLVVDRHAVASMVCYPLARFMMGCVSLRSVASLISHLPPPLPGTNLVVASLDFREHAARLRARARPGERLDLTMMAAIRNAYAMLANTSRYLLSGGDWRRDWGSLPVFKPSAFVARAAKTAYTLPLRDEPGLADTLFAALKVPEFLDARGYPRAAHAWTLDILANRIRALRVYTLDLTGPPEACAAAFRRLCAGLVLTEGSHPGALCELKRAAAAYAREMSVVGSREPTTAEVESA", "text": "FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors. SIMILARITY: Belongs to the herpesviridae thymidine kinase family."}
{"protein": "MAGSPLLWGPRAGGVGLLVLLLLGLFRPPPALCARPVKEPRGLSAASPPLAETGAPRRFRRSVPRGEAAGAVQELARALAHLLEAERQERARAEAQEAEDQQARVLAQLLRVWGAPRNSDPALGLDDDPDAPAAQLARALLRARLDPAALAAQLVPAPVPAAALRPRPPVYDDGPAGPDAEEAGDETPDVDPELLRYLLGRILAGSADSEGVAAPRRLRRAADHDVGSELPPEGVLGALLRVKRLETPAPQVPARRLLPP", "text": "FUNCTION: [PEN]: Endogenous ligand for GPR171. Neuropeptide involved in the regulation of feeding. FUNCTION: [Big LEN]: Endogenous ligand for GPR171. Neuropeptide involved in the regulation of feeding. FUNCTION: May function in the control of the neuroendocrine secretory pathway. Proposed be a specific endogenous inhibitor of PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal inhibitory domain, but not the further processed peptides reduce PCSK1 activity in the endoplasmic reticulum and Golgi. It reduces the activity of the 84 kDa form but not the autocatalytically derived 66 kDa form of PCSK1. Subsequent processing of proSAAS may eliminate the inhibition. Slows down convertase-mediated processing of proopiomelanocortin and proenkephalin. May control the intracellular timing of PCSK1 rather than its total level of activity (By similarity). SUBCELLULAR LOCATION: Secreted Golgi apparatus, trans-Golgi network Note=A N-terminal processed peptide, probably Big SAAS or Little SAAS, is accumulated in cytoplasmic protein tau deposits in frontotemporal dementia and parkinsonism linked to chromosome 17 (Pick disease), Alzheimer disease and amyotrophic lateral sclerosis- parkinsonism/dementia complex 1 (Guam disease)."}
{"protein": "MSDDRFAEDEIIQQRRKRRLEILKKYQQTGNGHSDLSIPEKKLKEDVDQVSTTKPIEAVPKMKTNASKIEINKEGSNSNTKLDVTNSTTSDSPSIKSSVQIEDTEDDMFADSPSPSVKRQNTGKGISTLTRSFADMQDNWDDIEGYYKVVLMEELDSRYIVQSNLGKGMFSTVVSALDRNRNQTFAIKIIRNNEVMYKEGLKEVSILERLQAADREGKQHIIHYERHFMHKNHLCMVFEMLSLNLRDILKKFGRNVGLSIKAVRLYAYQMFMALDLLKQCNVIHSDIKPDNMLVNEKRNILKICDLGSASDASENEITPYLVSRFYRAPEIILGFPYSCPIDTWSVGCSLYELYTGQILFPGRTNNQMLRYMMECKGKFSHKMLKRSQFLNDHFDADFNFIQIDHDPITNQETRKPVKFSKPTKDIRSRLKEVPTSTDEEFIIRQELMDLLEKCLELNPEKRVPPEVALKHPFFIKK", "text": "FUNCTION: Has a role in pre-mRNA splicing and is essential for growth. Phosphorylates srp1. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family."}
{"protein": "MNPNSHPITKSHLFHIVDPSPWPVLTSFALLLLVIGGVSFMHGYKFNIYILSAGVISVGYCLYSWWRDVVKEGIVEHQHTSPVRKGLQIGMALFILTEIVFFGVFFASFFKSSLSPVGLLDGVWVVKQGIWPPPTIKTFDPFDIPFINTLILLLSGTTVTWAHYALEEKNQKDCVTALALTILLGIFFTTMQAYEYYHAAFKFTDGIYASNFYLATGFHGAHVIIGTIFLIVCYFRAKRGDFTTEGNGHLGFEFAAWYWHFVDVVWLFLFTFVYIFGS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family."}
{"protein": "MGSLTSVDKSRIRQAFQKALNDYDRHALIQQKMTINLMAHLQDYLPNGSLDSVLELGCGSGMLSSLLQKQISADYWLFNDLCDVQTQLAEKLPQSFDFYCGDAEHFLFLQQFDLIASASAVQWFHQPDAFIAHCKTGLKTNGLLAVATFGEDNLKEVRQITNIGLNYPTLSQWQTWLAKDFELLWCEDFKVILDFDTPLDVLKHLKYTGVTATNQKNWTRKNLNGFIGDYLSAFGMPSGKVRLTYHPLFFIARYSHIENQ", "text": "FUNCTION: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L- methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. SIMILARITY: Belongs to the methyltransferase superfamily."}
{"protein": "MELLSRVLLWKLLLLQSSAVLSSGPSGTAAASSSLVSESVVSLAAGTQAVLRCQSPRMVWTQDRLHDRQRVVHWDLSGGPGSQRRRLVDMYSAGEQRVYEPRDRDRLLLSPSAFHDGNFSLLIRAVDRGDEGVYTCNLHHHYCHLDESLAVRLEVTEDPLLSRAYWDGEKEVLVVAHGAPALMTCINRAHVWTDRHLEEAQQVVHWDRQLPGVSHDRADRLLDLYASGERRAYGPPFLRDRVSVNTNAFARGDFSLRIDELERADEGIYSCHLHHHYCGLHERRVFHLQVTEPAFEPPARASPGNGSGHSSAPSPDPTLTRGHSIINVIVPEDHTHFFQQLGYVLATLLLFILLLITVVLATRYRHSGGCKTSDKKAGKSKGKDVNMVEFAVATRDQAPYRTEDIQLDYKNNILKERAELAHSPLPAKDVDLDKEFRKEYCK", "text": "FUNCTION: Transmembrane protein which can modulate activity of various signaling pathways, probably via binding to integrin ITGAV:ITGB3 (PubMed:18366072, PubMed:22492581, PubMed:29702220). Mediates heterophilic cell-cell interactions in vitro (PubMed:18366072). Inhibits osteoclastogenesis downstream of TNFSF11/RANKL and CSF1, where it may function by attenuating signaling via integrin ITGB3 and MAP kinase p38 (PubMed:22492581). Plays a role in cartilage formation where it promotes proliferation and maturation of growth plate chondrocytes (PubMed:29702220). Stimulates formation of primary cilia in chondrocytes (PubMed:29702220). Enhances expression of genes involved in the hedgehog signaling pathway in chondrocytes, including the hedgehog signaling molecule IHH; may also promote signaling via the PTHLH/PTHrP pathway (PubMed:29702220). Plays a role in angiogenesis where it suppresses migration of endothelial cells and also promotes their apoptosis (By similarity). Inhibits VEGF-induced activation of AKT and p38 MAP kinase in endothelial cells (By similarity). Also inhibits VTN (vitronectin)-mediated integrin ITGAV:ITGB3 signaling and activation of PTK2/FAK (By similarity). May play a role in the maturation and maintenance of the blood-brain barrier (PubMed:14603461). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell junction, tight junction Cytoplasm Cell projection, cilium membrane Nucleus Note=Primarily localizes to the cell membrane (PubMed:18366072). Detected in the cilium of primary chondrocytes (PubMed:29702220). Highly expressed at areas of cell-cell contact and may localize to tight junctions (PubMed:18366072). Also found in the nucleus where it is detected in the soluble (as opposed to chromatin-bound) fraction (PubMed:18366072)."}
{"protein": "MVLGGCPVSYLLLCGQAALLLGNLLLLHCVSRSHSFNATAELDLTPSGAAHLEGPAASSWEYSDPNSPVILCSYLPDEFVDCDAPVDHVGNATAYQELGYGCLKFGGQAYSDVEHTAVQCRALEGIECASPRTFLRKNKPCIKYTGHYFITTLLYSFFLGCFGVDRFCLGHTGTAVGKLLTLGGLGIWWFVDLILLITGGLMPSDGSNWCTVY", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TM2 family."}
{"protein": "MALLSQAGGAYTVPSGHVSSRTGTKTVSGCVNVLRMKETYVSSYSRTLSTKSMLKRSKRGHQLIVAASPPTEEAVVATEPLTREDLIAYLASGCKSKEKWRIGTEHEKFGFEVNTLRPMKYDQIAELLNSIAERFEWEKVMEGDKIIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVAEEMGIGFLGMGFQPKWRREDIPTMPKGRYDIMRNYMPKVGSLGLDMMLRTCTVQVNLDFSSEADMIRKFRAGLALQPIATALFANSPFTEGKPNGFLSMRSHIWTDTDKDRTGMLPFVFDDSFGFEQYVDYALDVPMYFAYRNGKYVDCTGMTFRQFLAGKLPCLPGELPTYNDWENHLTTIFPEVRLKRYMEMRGADGGPWRRLCALPAFWVGLLYDEDVLQSVLDLTADWTPAEREMLRNKVPVTGLKTPFRDGLLKHVAEDVLKLAKDGLERRGYKEVGFLNAVTEVVRTGVTPAENLLEMYNGEWGQSVDPVFQELLY", "text": "FUNCTION: Participates in the detoxification process. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the carboxylate-amine ligase family. Glutamate-- cysteine ligase type 2 subfamily."}
{"protein": "MRKHLGGCWLAIVCVLLFSQLSSVKARGIKHRIKWNRKVLPSTSQVTEAHTAEIRPGAFIKQGRKLDINFGVEGNRYYEANYWQFPDGIHYNGCSEANVTKEKFVTSCINATQVANQEELSREKQDNKLYQRVLWQLIRELCSIKHCDFWLERGAGLQVTLDQPMMLCLLVFIWFIVK", "text": "FUNCTION: Required for normal acrosome reaction and for normal male fertility (By similarity). Can bind Cu(2+) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the prion family."}
{"protein": "MNSLLMITACLVVIGTVWAKEGYLVDVKGCKKNCWKLGDNDYCNRECKWKHIGGSYGYCYGFGCYCEGLPDSTQTWPLPNKTCGKK", "text": "FUNCTION: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MPMVLLECDKDIPERQKHIYLKAPNEDTREFLPIANAATIPGTLSERGCLLRRKLVIGGVLKDTIQMIHGPLGCAYDTWHTKRYPTDNGHFNMKYVWSTDMKESHVVFGGEKRLEQRMHEAFDEMPDIKRMIVYTTCPTALIGDDIKAVAKKVMKERPDVDVFTVECPGFSGVSQSKGHHVLNIGWINEKVETMEKEITSEYTMNFIGDFNIQGDTQLLQTYWDRLGIQVVAHFTGNGTYDDLRCMHQAQLNVVNCARSSGYIANELKKRYGIPRLDIDSWGFSYMAEGIRKICAFFGIEEKGERLIAEEYAKWKPKLDWYKERLQGKKMAIWTGGPRLWHWTKSVEDDLGIQVVAMSSKFGHEEDFEKVIARGKEGTYYIDDGNELEFFEIIDLVKPDVIFTGPRVGELVKKLHIPYVNGHGYHNGPYMGFEGFVNLARDTYNAVHNPLRHLAAVDIRDSSQTTPVIVRGAA", "text": "FUNCTION: This vanadium-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family."}
{"protein": "MEPILQESDSRFVIFPIKYHDIWKMYKQSVASFWTVEEVDLSKDLDDWDKLTKDEKYFIKHILAFFASSDGIVNENLAERFYVDVQCSEARCFYGFQIAMENIHSEMYSLLIDTYVRDNIEKMHLFNAIETMECVKKKADWARKWISSNKVYGERVVAFAAVEGIFFSGSFAAIFWIKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLLHPPSKEVITSIIIDAVNIEKEFLTVAIPVDLIGMNCCLMSQYIEFVADRLLTELGCEKSQCI", "text": "FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small chain family."}
{"protein": "MSGRARVKARGIARSPSATEVGRIQASPLPRSVDLSNNEASSSNGFLGTSRISTNDKYGISSGDAGSTFMERGVKNKQDFMDLSICTREKLAHVRNCKTGSSGIPVKLVTNLFNLDFPQDWQLYQYHVTYIPDLASRRLRIALLYSHSELSNKAKAFDGAILFLSQKLEEKVTELSSETQRGETIKMTITLKRELPSSSPVCIQVFNIIFRKILKKLSMYQIGRNFYNPSEPMEIPQHKLSLWPGFAISVSYFERKLLFSADVSYKVLRNETVLEFMTALCQRTGLSCFTQTCEKQLIGLIVLTRYNNRTYSIDDIDWSVKPTHTFQKRDGTEITYVDYYKQQYDITVSDLNQPMLVSLLKKKRNDNSEAQLAHLIPELCFLTGLTDQATSDFQLMKAVAEKTRLSPSGRQQRLARLVDNIQRNTNARFELETWGLHFGSQISLTGRIVPSEKILMQDHICQPVSAADWSKDIRTCKILNAQSLNTWLILCSDRTEYVAESFLNCLRRVAGSMGFNVDYPKIIKVQENPAAFVRAIQQYVDPDVQLVMCILPSNQKTYYDSIKKYLSSDCPVPSQCVLARTLNKQGMMMSIATKIAMQMTCKLGGELWAVEIPLKSLMVVGIDVCKDALSKDVMVVGCVASVNPRITRWFSRCILQRTMTDVADCLKVFMTGALNKWYKYNHDLPARIIVYRAGVGDGQLKTLIEYEVPQLLSSVAESSSNTSSRLSVIVVRKKCMPRFFTEMNRTVQNPPLGTVVDSEATRNEWYDFYLISQVACRGTVSPTYYNVIYDDNGLKPDHMQRLTFKLCHLYYNWPGIVSVPAPCQYAHKLTFLVAQSIHKEPSLELANHLFYL", "text": "FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (By similarity). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (By similarity). Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements (By similarity). Associates with secondary piRNAs antisense and PIWIL2/MILI is required for such association (By similarity). The piRNA process acts upstream of known mediators of DNA methylation (By similarity). Does not show endonuclease activity (By similarity). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-incompetent' component that loads cleaved piRNAs from the 'slicer-competent' component PIWIL2 and target them on genomic transposon loci in the nucleus (By similarity). May be involved in the chromatin-modifying pathway by inducing 'Lys-9' methylation of histone H3 at some loci (PubMed:17544373). In addition to its role in germline, PIWIL4 also plays a role in the regulation of somatic cells activities. Plays a role in pancreatic beta cell function and insulin secretion (By similarity). Involved in maintaining cell morphology and functional integrity of retinal epithelial through Akt/GSK3alpha/beta signaling pathway (PubMed:28025795). When overexpressed, acts as an oncogene by inhibition of apoptosis and promotion of cells proliferation in tumors (PubMed:22483988). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. PIWIL2/MILI is required for nuclear localization (By similarity). SIMILARITY: Belongs to the argonaute family. Piwi subfamily."}
{"protein": "MASVSTHENQEKGPHLPPPSKQSLLFCPKSKLHIHRSEISKIIRECQEESFWKRALPFSLVSMLVTQGLVHHGYLAANPRFGSLPKVALAGILGFGLGKASYIGVCQSKFHSFEGQLRGAGFGPGHNRHCLLTCEECKTKHGLSQERSSQPSAS", "text": "SUBCELLULAR LOCATION: Endosome."}
{"protein": "MRESALERGPVPEAPAGGPVHAVTVVTLLEKLASMLETLRERQGGLARRQGGLAGSVRRIQSGLGALSRSHDTTSNTLAQLLAKAERVSSHANAAQERAVRRAAQVQRLEANHGLLVARGKLHVLLFKEEGEVPASAFQKAPEPLGPADQSELGPEQLEAEVGESSDEEPVESRAQRLRRTGLQKVQSLRRALSGRKGPAAPPPTPVKPPRLGPGRSAEAQPEAQPALEPTLEPEPPQDTEEDPGRPGAAEEALLQMESVA", "text": "FUNCTION: Regulates the traffic and/or budding of caveolae (PubMed:19262564). Plays a role in caveola formation in a tissue- specific manner. Required for the formation of caveolae in smooth muscle but not in the lung and heart endothelial cells. Regulates the equilibrium between cell surface-associated and cell surface- dissociated caveolae by promoting the rapid release of caveolae from the cell surface. Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane, caveola Cytoplasm, cytosol Note=Localizes in the caveolae in a caveolin-dependent manner. SIMILARITY: Belongs to the CAVIN family."}
{"protein": "MNPVPAQREYFLDSIRAWLMLLGIPFHISLIYSSHTWHVNSAEPSLWLTLFNDFIHSFRMQVFFVISGYFSYMLFLRYPLKKWWKVRVERVGIPMLTAIPLLTLPQFIMLQYVKGKAESWPGLSLYDKYNTLAWELISHLWFLLVLVVMTTLCVWIFKRIRNNLENSDKTNKKFSMVKLSVIFLCLGIGYAVIRRTIFIVYPPILSNGMFNFIVMQTLFYLPFFILGALAFIFPHLKALFTTPSRGCTFAAALAFVAYLLNQRYGSGDAWMYETESVITMVLGLWMVNVVFSFGHRLLNFQSARVTYFVNASLFIYLVHHPLTLFFGAYITPHITSNWLGFLCGLIFVVGIAIILYEIHLRIPLLKFLFSGKPVVKRENDKAPAR", "text": "FUNCTION: Necessary for the succinyl substitution of periplasmic glucans. Could catalyze the transfer of succinyl residues from the cytoplasmic side of the membrane to the nascent glucan backbones on the periplasmic side of the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acyltransferase 3 family. OpgC subfamily."}
{"protein": "MADPDVLTEVPAALKRLAKYVIRGFYGIEHVLALDILIRNPCVKEEDMLELLKFDRKQLRSVLNNLKGDKFIKCRMRVETAADGKTTRHNYYFINYRTLVNVVKYKLDHMRRRIETDERNSTNRASFKCPVCCSTFTDLEANQLFDPMTGTFRCTFCHTEVEEDESAMPKKDARTLLARFNEQIEPIYALLRETEDVNLAYEILEPEPTEIPALKQSKDRAATAAGAAGLAGGHHREAWTNKGPSYEDLYTQNVVINMDDQDDVHRPSLEGKAAKERPIWLRESTVQGAYSSEEMKEGGIDVDTFQEREEARAGPDDNEEVMRALLIHEKKTSSVTAGSVGAAAPVTAANGSDSESETSESDDDSPPRPAAAAPPHHHRDEDEEDEEFEEVADDPIVMVAGCPFSYSEVSQRPELVAQMTPEEKEAYIAMGQRMFEDLFE", "text": "FUNCTION: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIE alpha subunit family."}
{"protein": "MKTIYFLISLILIQSIKTLPVLEIASNSQPQDVDSVCSGTLQKTEDVHLMGFTLSGQKVADSPLEASKRWAFRTGVPPKNVEYTEGEEAKTCYNISVTDPSGKSLLLDPPSNIRDYPKCKTVHHIQGQNPHAQGIALHLWGAFFLYDRVASTTMYRGKVFTEGNIAAMIVNKTVHRMIFSRQGQGYRHMNLTSTNKYWTSSNETQRNDTGCFGILQEYNSTNNQTCPPSLKPPSLPTVTPSIHSTNTQINTAKSGTMNPSSDDEDLMISGSGSGEQGPHTTLNVVTEQKQSSTILSTPSLHPSTSQHEQNSTNPSRHAVTEHNGTDPTTQPATLLNNTNTTPTYNTLKYNLSTPSPPTRNITNNDTQRELAESEQTNAQLNTTLDPTENPTTGQDTNSTTNIIMTTSDITSKHPTNSSPDSSPTTRPPIYFRKKRSIFWKEGDIFPFLDGLINTEIDFDPIPNTETIFDESPSFNTSTNEEQHTPPNISLTFSYFPDKNGDTAYSGENENDCDAELRIWSVQEDDLAAGLSWIPFFGPGIEGLYTAGLIKNQNNLVCRLRRLANQTAKSLELLLRVTTEERTFSLINRHAIDFLLTRWGGTCKVLGPDCCIGIEDLSKNISEQIDKIRKDEQKEETGWGLGGKWWTSDWGVLTNLGILLLLSIAVLIALSCICRIFTKYIG", "text": "FUNCTION: GP2 acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide (By similarity). FUNCTION: GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection) (By similarity). SUBCELLULAR LOCATION: [GP2]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Note=In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site. SUBCELLULAR LOCATION: [GP1]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Note=GP1 is not anchored to the viral envelope, but forms a disulfid-linked complex with the extravirion surface GP2. In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site. GP1 can also be shed after proteolytic processing. SIMILARITY: Belongs to the filoviruses glycoprotein family."}
{"protein": "MIEIKDKQLTGLRFIDLFAGLGGFRLALESCGAECVYSNEWDKYAQEVYEMNFGEKPEGDITQVNEKTIPDHDILCAGFPCQAFSISGKQKGFEDSRGTLFFDIARIVREKKPKVVFMENVKNFASHDNGNTLEVVKNTMNELDYSFHAKVLNALDYGIPQKRERIYMICFRNDLNIQNFQFPKPFELNTFVKDLLLPDSEVEHLVIDRKDLVMTNQEIEQTTPKTVRLGIVGKGGQGERIYSTRGIAITLSAYGGGIFAKTGGYLVNGKTRKLHPRECARVMGYPDSYKVHPSTSQAYKQFGNSVVINVLQYIAYNIGSSLNFKPY", "text": "FUNCTION: A methylase, recognizes the double-stranded sequence 5'-GCGC- 3', methylates C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family."}
{"protein": "MALLELRNVIRRFGDFTAVDNVSLSIQAGEFFTLLGPSGCGKTTLLRMIAGFDVPDSGQILLDGQDIANTPPEKRPIHTVFQSYALFPHMTVADNVAFPLKMSKVAPAEIKKRMEKALEEVQLSRFTHRFPHELSGGQKQRVAFARGLINRPRLLLMDEPLGALDAKLREDMQRELINLQKEVGITFIFVTHSQDEALALSQRIAVMNLGNIEQIGTPSAIYGTPANRFIADFIGKINLMEARVTQISNTAMTLEINGLGTTVLPPKKEIQAGDQGVIAIRPEQVAVHALAKQAEIPHAHTGKVLDFLYVGDVTTYVIELDSGIQIEALLANSSPGRARFFEVDDPVIVSWPQEAAQFLVDRP", "text": "FUNCTION: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Spermidine/putrescine importer (TC 3.A.1.11.1) family."}
{"protein": "MAEPLKEEDGEDGSGEPPGRVKAEPVHTAASVVAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFRSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPVCPDVEMPSPWAPSGDCAMESPPPALPPCSGPAPDTVDLTLQPAPPASELAPPKREGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGTLGGPSTDPLAGLVLSDNDRSLLERWTRMARPPVPAPAPAPAPTPKPSSAQPTSPPNGPVSQSTAPLQPAGSIPGPASQPVCPPPGPVPQPAGPVPAPLQTAPSTSLLASQSLVPPSGLPGSGAPEVLPYFPSGPPPPDPGLTPQPSTSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLSDLPDLQEP", "text": "FUNCTION: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression (By similarity). Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body Note=Translocates to the nucleus upon activation. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
{"protein": "MSSRLRFLFSLAAAIAAASLLAAALRRRAPPSGLAARLVPAPMAAAAARNRSFVLWLHGLGDSGPANEPIRNFFSAPEFRLTKWAFPSAPNSPVSCNHGAVMPSWFDIHELPMSSGSPQDDSGVLKAVENVHAMIDKEVADGIPPENIFVCGFSQGGALTLASVLLYPKTLGGGAVFSGWLPFGSSVTERISPEARKTPILWSHGIADNVVLFEAGQAGPPFLQNAGFSCEFKAYPGLGHSISKEELYSLESWIKNHLKASQEKEN", "text": "FUNCTION: Possesses carboxylesterase activity in vitro. SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2 family."}
{"protein": "MRTAYFIFVGALLGVSYAKHHHAARAPIINLQGAEELVAVVREDENIISTVPDFAILSETGPVCNYLLTSQNNEPVPFDIQVVDKYTGAAVLRVKDAATLDCKKPEYNLQVQAVKCDNDNVKSEGVSLKIRVKDTNNHAPEIENPWYTFHVEEGKVVEEVGVLKASDKDCGHPNGEICEYEITNGLKELPFAINNHGVLRTTQPLNFTQSKSYILTVVAIDCAMRKSKSSLVTVHVDEKCVQGITAMNERVNYAPGVGSKLLLPDVSLEFCEKETICEPKSVQSVIELRAGHVTQGCARDTVYDNQTIQSCGLSTATVKLLNEEALTSSAENQILADQGIEFDGARGVTVSDENHQGLIPDHFTLSFSMKHAAGTKDEQSNKQNILCESDDFNMNRHHFSVYIRHCKLEVVLRREAGATSDFRAAEWRWSMPEVCDNEWHSYSLLFNGIDDVNVIVDGKSFKADERNPEILDDWPLHKTKATKTKLVVGACWHGRQQKLAQFFRGQLSSLYLLSGAVESERAIKCAHTCPEQLQFTGVDELLESQSATFSPDQTSLTLKAETSKQIGQMLKRVAYVNTQEKPAPGHRVFLVETEVTCKQDDKKMKLPSSKGYVFVQQAAEPTLSISASSQLKSNQHMVKVGQAMVPDLTITISQNNADGELEDVTQSHKIDYCKMHLQPARDMDVEYFSSPASLIAALNIEFEHDKDGILLRGEESAQGYKEVLSKVHYFNTRPESYAKRVYTVQCAMLKGRVLSNQLFVTMTIDGVTTTTSTTTEAPAPAQPDPIQFNFNSGETALDSLELIERHFEPAFDQLGSSRLQNILEMDLPRPKALLSHHGYDVGQGAIAGGAVAVVVVVCVGFLLVLLVIGVLKMRDTPMPRRRRQKRQSDGGMHWDDSGMNITVNPLDDVEKNGGAIDEFSDEEEEEETDGESECSYRDEEDDVSEDEEDQTEVLPHLDANQRVVGGLEWDDEDAISTNARSYRV", "text": "FUNCTION: Cell adhesion molecule involved in associative learning and memory (PubMed:18381821, PubMed:25035490, PubMed:19287492, PubMed:29529030). Acts as a regulator of GABAergic synaptic transmission at neuromuscular junctions by regulating GABA synaptic vesicle precursor transport: possibly functions as a cargo adapter for unc-104-mediated transport of synaptic vesicle precursors (PubMed:29529030). Promotes localization of isoform c of daf-2 (daf-2c) to synaptic regions by acting as a signaling adapter between klc-2 and daf-2c (PubMed:25035490). FUNCTION: [Isoform a]: Acts as aregulator of glutamate signaling in the sensory neurons by inhibiting the activity of command interneurons, thereby negatively regulating motor circuit activity and locomotion. SUBCELLULAR LOCATION: [Secreted calsyntenin-1]: Secreted Synaptic cleft Note=Released in the extracellular space following proteolytic cleavage. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I membrane protein Perikaryon Cell projection, axon. SIMILARITY: Belongs to the calsyntenin family."}
{"protein": "MSVLQELTKKKYSSLKTMFDDKYCPTFVYSILDQTIPGAVYADDQTFPKSFFIGTESGIYFIAGDQGNRDFHDFIAGYYEEQVKSSKRFTLFSSSDTWDSVLKPILKDDLNQMRRAAFSYQPKSFKKTLQLPKGLVLKRIDEDIISHSTAFNSAYYEEYWNSVSQFASKGFGFAVLHGNHVVSECTSIFLGHNRAEMDIYTLEEYRGLGLAYCVANRFIAFCMENGIVPSWDCDICNNSSIALAAKLGFKTVTEYTIYYSG", "text": "SIMILARITY: Belongs to the acetyltransferase family."}
{"protein": "MRGSSNRKIDPRIHYLVPKHEVLSIDEAYKILKELGIRPEQLPWIRASDPVARSINAKPGDIIRIIRKSQLYGEVVSYRYVISG", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family."}
{"protein": "MRKFSRYAFTSMATVTLLSSLTPAALASDTNHKPATSDINFEITQKSDAVKALKELPKSENVKNHYQDYSVTDVKTDKKGFTHYTLQPSVDGVHAPDKEVKVHADKSGKVVLINGDTDAKKVKPTNKVTLSKDEAADKAFNAVKIDKNKAKNLQDDVIKENKVEIDGDSNKYIYNIELITVTPEISHWKVKIDADTGAVVEKTNLVKEAAATGTGKGVLGDTKDININSIDGGFSLEDLTHQGKLSAYNFNDQTGQATLITNEDENFVKDDQRAGVDANYYAKQTYDYYKNTFGRESYDNHGSPIVSLTHVNHYGGQDNRNNAAWIGDKMIYGDGDGRTFTNLSGANDVVAHELTHGVTQETANLEYKDQSGALNESFSDVFGYFVDDEDFLMGEDVYTPGKEGDALRSMSNPEQFGQPSHMKDYVYTEKDNGGVHTNSGIPNKAAYNVIQAIGKSKSEQIYYRALTEYLTSNSNFKDCKDALYQAAKDLYDEQTAEQVYEAWNEVGVE", "text": "FUNCTION: Plays an essential role in immune evasion by helping bacteria to resist complement-mediated killing by neutrophils. Inhibits the deposition of host C3b on bacterial surfaces and the release of the chemoattractant C5a by cleaving the central complement protein C3. The cleavage site renders the C3b molecule vulnerable to proteolytic degradation by host regulators (PubMed:21502375). Cleaves and inactivates host SERPINA1, which is an endogenous protease inhibitor essential for controlling neutrophil serine protease elastase (PubMed:3533918). Also plays an essential role in the cleavage and subsequent activation of the serine protease SspA (glutamyl endopeptidase) which is involved in colonization and infection of human tissues (PubMed:17878159). SIMILARITY: Belongs to the peptidase M4 family."}
{"protein": "MKKAKILSGVLLLCFSSPLISQAATLDVRGGYRSGSHAYETRLKVSEGWQNGWWASMESNTWNTIHDNKKENAALNDVQVEVNYAIKLDDQWTVRPGMLTHFSSNGTRYGPYVKLSWDATKDLNFGIRYRYDWKAYRQQDLSGDMSRDNVHRWDGYVTYHINSDFTFAWQTTLYSKQNDYRYANHKKWATENAFVLQYHMTPDITPYIEYDYLDRQGVYNGRDNLSENSYRIGVSFKL", "text": "FUNCTION: Outer membrane channel protein allowing the entry of N- acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host cell surfaces) into the bacteria (Probable). NanC proteins form high- conductance channels which are open at low membrane potentials and which have a weak anion selectivity. FUNCTION: Outer membrane channel protein allowing the entry of N- acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host cell surfaces) into the bacteria. NanC proteins form high-conductance channels which are open at low membrane potentials and which have a weak anion selectivity (By similarity). SUBCELLULAR LOCATION: Cell outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the oligogalacturonate-specific porin KdgM (TC 1.B.35) family. NanC subfamily."}
{"protein": "MLTPRVLRALGWTGLFFLLLSPSNVLGASLSRDLETPPFLSFDPSNISINGAPLTEVPHAPSTESVSTNSESTNEHTITETTGKNAYIHNNASTDKQNANDTHKTPNILCDTEEVFVFLNETGRFVCTLKVDPPSDSEWSNFVLDLIFNPIEYHANEKNVEAARIAGLYGVPGSDYAYPRQSELISSIRRDPQGTFWTSPSPHGNKYFIWINKTTNTMGVEIRNVDYADNGYMQVIMRDHFNRPLIDKHIYIRVCQRPASVDVLAPPVLSGENYKASCIVRHFYPPGSVYVSWRQNGNIATPRKDRDGSFWWFESGRGATLVSTITLGNSGIDFPPKISCLVAWKQGDMISTTNATAIPTVYHHPRLSLAFKDGYAICTIECVPSEITVRWLVHDEAQPNTTYNTVVTGLCRTIDRHRNLLSRIPVWDNWTKTKYTCRLIGYPFDEDKFQDSEYYDATPAARGTPMVITVTAVLGLAVILGMGIIMTALCLYNSTRKNIRL", "text": "FUNCTION: May play an immunoevasive role in the pathogenesis of Marek's disease. It is a candidate for causing the early-stage immunosuppression that occurs after MDHV infection. SUBCELLULAR LOCATION: Secreted. Host cell membrane; Single-pass membrane protein. Note=Predominantly secreted. Secreted, but a small amount of mature GP57-65 is anchored in the plasma membrane or held by other interactions. SIMILARITY: Belongs to the herpesviridae glycoprotein C family."}
{"protein": "MARLPAGIRFIISFSRDQWYRAFIFILTFLLYASFHLSRKPISIVKGELHKYCTAWDEADVRFSSQNRKSGSAAPHQLPDNETDCGWAPFDKNNYQQLLGALDYSFLCAYAVGMYLSGIIGERLPIRYYLTFGMLASGAFTALFGLGYFYNIHSFGFYVVTQVINGLVQTTGWPSVVTCLGNWFGKGRRGLIMGVWNSHTSVGNILGSLIAGYWVSTCWGLSFVVPGAIVAAMGIVCFLFLIEHPNDVRCSSTLVTHSKGYENGTNRLRLQKQILKSEKNKPLDPEMQCLLLSDGKGSIHPNHVVILPGDGGSGTAAISFTGALKIPGVIEFSLCLLFAKLVSYTFLFWLPLYITNVDHLDAKKAGELSTLFDVGGIFGGILAGVISDRLEKRASTCGLMLLLAAPTLYIFSTVSKMGLEATIAMLLLSGALVSGPYTLITTAVSADLGTHKSLKGNAHALSTVTAIIDGTGSVGAALGPLLAGLLSPSGWSNVFYMLMFADACALLFLIRLIHKELSCPGSATGDQVPFKEQ", "text": "FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter. May transport cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocate inorganic phosphate into the opposite direction. Independent of a lumenal glucose-6-phosphatase. May not play a role in homeostatic regulation of blood glucose levels. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family."}
{"protein": "MKTLLLTLVVVTIVCLDLGYTMKCKICHFDTCRAGELKVCASGEKYCFKESWREAREVKIIRGCSSSCPEKKNVFCCSTNDCNW", "text": "FUNCTION: Binds and inhibits muscular and neuronal nicotinic acetylcholine receptors (nAChR). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Orphan group IV sub-subfamily."}
{"protein": "MSEADAGARDESPSRTAEEPAAAMRIKEERRSSSVDVVDVGNGELLVLHSIFYQGKTLRLPGNRAHMYPVVFQMIKGVCSLVKQLVVAFPKGWDQNTPSISEIAALTKSFNRVAKPFASNWSGSYNTDTLKEWGEPNCSAEVAKAITTYAYECAVPRPADLNQHYKSFTSETYGETNPEQLISIIDELNIGPQDVFVDLGSGIGQLVCLTAAYAKCKKSVGIELSQVPSNFAQDLAGYFKKFMSHFGKNHGKFEHIQGDFLNPKFKQLICEEATVIFINNFAFDAALMLRINTELLQDLKHGTRIVTTKELGTNKKEITFRSTSDINAISHTTELKTTESAVSWTSSHVKFWLTTIDHTKLIKYYEDQRRRQEVKSSREGSEISDGRDMGLKKRKSQRESSVHPDKLQKTEQAAASSHQSPKWNEPDTDYTPPAKKPKKEKLLREQQDATPASSHHHGASSSSGKDREKEKEKKKNKIYEEKKVKTPKPPKSSSSRYSSETPTSHHHHHRSNSISHSSDVIRPSQPKATAPPPPLVPAPARATASTPPPAPPAARAQSPKREEPLEPPTDLIHHGGGQLDAKTMNALHTIREAATTSAQAAAIQDAINSVLSQPTEASPSAFGPPLAHLPAPVAIYPTPPPPPAPAPAAPQQASAAPAAPNVMPVCTEIAAEQRHTFMIPPTDPFYNMIVSYYFAMKQFCNQSKTADPEFVGRLRLDIEAEEARRAELKESITLTSTQIDELLATGVNTLKSRLDELGMPSVTDVTELLAGSKQIVTQHKGLTNTVAQMENSVAVEEQKLRLIGGPDAVRYFDEAMSHPNVDIAKLTDLVITTRPPNFVAQILLPDDSPTASIDSKVSPSSSSSRRPRQPKPRANNTAAGAGGGGKRGTSGGRKSDGGGGGGATEDVELEIRQFVQHALKVDNAVKEKERKARGNFMAAAADRIPR", "text": "FUNCTION: Histone methyltransferase, which in complex with zfp-1, methylates 'Lys-79' of histone H3 to activate transcription (Probable). During stress, the zfp-1-dot-1.1 complex also plays a role in the deubiquitination of histone H2B sites, which negatively modulates the RNA polymerase II-induced transcription of highly expressed genes (PubMed:23806335). Involved in controlling tissue-specific gene expression, particularly in the epidermis (PubMed:31088904). SUBCELLULAR LOCATION: Nucleus Chromosome Note=zfp-1 and dot-1.1 colocalize to promoters of highly expressed genes (PubMed:23806335). zfp-1 recruits dot-1.1 (PubMed:23806335). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family."}
{"protein": "MKVVNVPSNGREKFKKNWKFCVGTGRLGLALQKEYLDHLKLVQEKIGFRYIRGHGLLSDDVGIYREVEIDGEMKPFYNFTYIDRIVDSYLALNIRPFIEFGFMPKALASGDQTVFYWKGNVTPPKDYNKWRDLIVAVVSHFIERYGIEEVRTWLFEVWNEPNLVNFWKDANKQEYFKLYEVTARAVKSVDPHLQVGGPAICGGSDEWITDFLHFCAERRVPVDFVSRHAYTSKAPHKKTFEYYYQELELEPPEDMLEQFKTVRALIRQSPFPHLPLHITEYNTSYSPINPVHDTALNAAYIARILSEGGDYVDSFSYWTFSDVFEEMDVPKALFHGGFGLVALHSIPKPTFHAFTFFNALGDELLYRDGEMIVTRRKDGSIAAVLWNLVMEKGEGLTKEVQLVIPVSFSAVFIKRQIVNEQYGNAWRVWKQMGRPRFPSRQAVETLPSAQPHVMTEQRRATDGVIHLSIVLSKNEVTLIEIEQVRDETSTYVGLDDGEITSYSS", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 39 family."}
{"protein": "MSENEVKDPRIDGIKTKIRVVPDFPKKGIMFQDITTLLLDPKAFKDTIDLFVERYRDMNISVVAGIEARGFIFGSPIALAIGAKFVPLRKPKKLPGQIIFEEYELEYGSDRLEMHVEAVDSGDRALVVDDLIATGGTLCAAMNLLKRVGAEVIECACVIELPELKGRERLEGKPLYVLVEYR", "text": "FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. May contribute to the recycling of adenine into adenylate nucleotides and the inactivation of cytokinins by phosphoribosylation. Possesses low activity toward adenine, but can efficiently convert cytokinins from free bases (active form) to the corresponding nucleotides (inactive form). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MTICGRGLRRAVGASPRPTWRRALSDTRGRLKPEYDAVVVGAGHNGLVAAAYLQRFGVNTAVFERRHVIGGAAVTEEIVPGFKFSRASYLLSLLRPQIYSELELKKHGLRLHLRNPYSFTPMLEEGTGGKVPRSLLLGTDMVENQKQIAQFSKKDAQAFPKYEAFMDRLALAIDPLLDSAPVDLEAFQRGSLLQRLKSLSTLKPLWQAGCILGAQLPQYYQVLTAPAAKVLDQWFESEPLKATLATDAVIGAMTNPYIPGSGYVLLHHVMGSLEGVRGAWGYVQGGMGALSDAIASSATAHGVSIFTEKTVAKVQVSSGGRVQGVVLQDGSEVRSKVVLSNASPQITFLKLTPQEWLPEEFVARIAQLDTKSPVTKINVAVNRLPDFLAAPNTPGDQPLPHHQCSIHLNCEDTLLVHQAFEDTLDGLPSKRPLIELCIPSSLDPTLAPPGCHVVSLFTQYTPYTLAGGKAWDEQQRNTYADRVFDCIEAYAPGFKGSVVGRDILTPPDLERVFGLPGGNIFHCAMSLDQLYFARPVPLHSSYCSPLRGLYLCGSGAHPGGGVMGAAGRNAAHVVFRDLRSM", "text": "FUNCTION: Probable oxidoreductase that may play a role as regulator of mitochondrial function. SUBCELLULAR LOCATION: Mitochondrion matrix Note=The import into mitochondria is dependent on TOMM40 and TIMM23. SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family."}
{"protein": "MSRRRAHDTEDESYDHRRNKRRRVSENQEIEDRLESLILRVGERSTSSVESNLEGLVSVLEADLGTFRLKILRILSDCAVRMPEKCTVYTTLVGLLNAKNYKFGGEFVDYMVKTFKESLKLCRWDAARYSLRFLADLVNCHVISATSLLQLLDTIIDVSNEDTVPQVRRDWFVFAVLSTLPWVGRDLYEKKESALESLLLRIEVYLNKRSKKHHNALRVWSSDAPHPQEEYLDCLWAQIRKLRQDNWAEKHIPRPYLVFDAILCEALQHNLPQITPPPHHDAIEYPMPWVVYRMFDYTDCPDGPNLPGAHSIERFLIEEHLHHIIETHHHERKDCAAQLLNFPFKHKIPLEYCIVEVIFAELFHMPTPRYLDICYGSILIELCKLQPGTLPQVLAQATEILFMRIDSMNTSCFDRFVNWFSYHLSNFKFTWSWDEWDSCLLLDAEHPRPKFIQEVLQKCLRLSYHQRITEMMPTTYAKLIPVMPVPNYKYTSEEAANLPGTTVALQLVGAIRQKCTPEEVVNILKEIPSSGYSGEEMSDGSFNALKIDFCGQSKFHVVFRALAETEEAQICILHNIFELWSSHQQMMVVLIDKLLKLQIVDCSAVATWIFSKEMTGEFTKMYLWEILHLTIKKMNKHVIKLDTELDNAKEKLSKADSSSSDTDEDTPHKRKKPITHADKPSEEVVERMEEKLEAANVNQKRLFLIVFQRFIMILSEHLLRSDTDGRDPDTDWYRWTIGRLQQVFLMHHEQVQKYSSTLETLLFTSDLDSHILEVFQQFVALRA", "text": "FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference via its interaction with Ars2 and is required for primary microRNAs (miRNAs) processing. Also involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. In the CBC complex, Cbp80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of Cbp20 and lock the CBC into a high affinity cap-binding state with the cap structure (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NCBP1 family."}
{"protein": "MTMKRLLLVSTLAGASALATLPANAFWGWNPFGWGGGPWDGPWGGGPWGSPWYGGYPYHGGYYPYGLYGVPYGWGAPVYGYPGYVYPGYAYPAPTQPSTKSQ", "text": "FUNCTION: Structural protein of the sulfur globules, which are intracellular globules that serve for sulfur storage in purple sulfur bacteria. SIMILARITY: To T.roseopersicina TR2."}
{"protein": "MSQDFVTLVSKDDKEYEISRSAAMISPTLKAMIEGPFRESKGRIELKQFDSHILEKAVEYLNYNLKYSGVSEDDDEIPEFEIPTEMSLELLLAADYLSI", "text": "FUNCTION: As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II subunit RPO21 to trigger its proteolysis; plays a role in global genomic repair (PubMed:19920177). Prevents degradation of interacting proteins like PCL6 by the proteasome (PubMed:11864988). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SKP1 family."}
{"protein": "MSGGLDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVCVISSRNTGQRAVLKFASASGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPITEASYVNIPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKATTKEEFQGEWTAPVAEFPQAEVADWSEGVQVPSVPIQQFTAERTDVPPAPKPTEDWSTQPASTDDWSAAPTAQASEWTGTTTEWS", "text": "FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. SUBCELLULAR LOCATION: Cell membrane Cytoplasm Nucleus Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MSHTAEIPLVPGSESPLELKPLKAADPHVVYHRRAHRLLSLAKDSPLADYFELCRRLVSIQAKLAEEADFGQLLAWGKDEATPLSLLGSEADSYWQGLLQQLLSDLLPQVDESIARVVRLLMQQSPEQLSSWGRSLRQGHVSEVPAHFSLFIWAAMGVYWSHWAPMVIKRMDQRKVAQQSMCPVCGCHPVASVIVDQPRAGLRYLHCSLCESEWHYIRAHCTSCGQDKEMTIWSLDDAQAQVRIESCDECHGYTKMMFVEMSPSMDVVADDLATLMLDSELNAKGFGATTLNPLLMAHEIT", "text": "FUNCTION: Necessary for formate dehydrogenase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FdhE family."}
{"protein": "MKLAYWMYAGPAHIGTLRVASSFKNVHSIMHAPLGDDYFNVMRSMLERERDFTPVTTSVVDRQVLARGSDEKVIRNIVRKDGEEQPDLIVVTPTCTSSILQEDLHHFVRQAQLSSRCDVLLADVNHYRVNELQAAERTLHQIVEFYINKARKSGELSGPPRRTERPSCNILGISSLGFHHAHDLRELKKLLQDLGIELNLVIPQGASVHNLKHLGRAWFNVVPYRELGPMTARYLQEQFGTPYVEITPMGVVETARFIRQIQQVLNEQGIPVDYEPYIQEQTLYVSQAAWFSRSIDCQNLTGKKAVVFGDCTHAAAITKILAREMGVHVVWAGSYCTYDGEWFQAEVGGYCDQVLLTEDHTRVADAIAQVEPAAIFGTQMERHVGKRLRIPCGVISAPMHVQDFPIGYRPFLGYEGANQIVDLIYNSFTLGMEDHLLEVFGGHDTKEVIHKSLSADSDLIWTREAQAELNKVPGFVRGKVKRNTEKFARERGLTEITLEVMYAAKEALGA", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SIMILARITY: Belongs to the ChlB/BchB/BchZ family."}
{"protein": "MLWALFFLVTTIHAELCHPDAENAFKVRLSIRAALGDKAYVWDTDQEYLFRAMVAFSMRKVPNREATEISHVLLCNITQRVSFWFVVTDPSNNYTLPAAEVQSAIRKNRNRINSAFFLDDHTLEFLKIPSTLAPPMEPSVPVWIIVFGVIFCIVTVAIALLVLSGIRQRRRNNKGPPGVEDAEDKCENIITIENGIPCDPLDMKGGHINDGFLTEDERLTPL", "text": "FUNCTION: Plays an important role in amino acid transport by acting as binding partner of amino acid transporters SLC6A18 and SLC6A19, regulating their trafficking on the cell surface and their activity (PubMed:17167413, PubMed:16985211). May also play a role in trafficking of amino acid transporters SLC3A1 and SLC7A9 to the renal cortical cell membrane (PubMed:16985211). Regulator of SNARE complex function (PubMed:16330323). Stimulator of beta cell replication (PubMed:16330324). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Localizes to the brush border membranes of cells in the proximal tubules of kidney (PubMed:17167413). Colocalizes with SLC6A19 in the early proximal S1 tubule (PubMed:17167413). SIMILARITY: Belongs to the CLTRN family."}
{"protein": "MTFSMRDLDQALQGAGQKSGIEIWRIENFKPVTVPQESHGKFFTGDSYIVLKTTASRSGSLHHDIHYWLGKDSSQDEAGAVAVMTVELDSALGGRAVQYREVQGHETEKFLSYFKPCIIPQEGGVASGFNHVKPEEHQTRLYICKGKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGRMMADAEAGEFWGLFGGFAPLPKKPAVNDDETAASDGIKLFSVEKGQTDAVEAECLTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEFFRSSEPPKSNLVSVMEGYETVMFRSKFDSWPASSTIAEPQQGRGKVAALLQRQGVNVQGLVKTSSSSSKDEPKPYIDGTGNLQVWRINCEEKILLEAAEQSKFYSGDCYILQYSYPGEDREEHLVGTWFGKQSVEEDRASAISLANKMVESMKFVPAQARINEGKEPIQFFVIMQSFITFKGGVSDAFKKYIAENDIPDTTYEAEGVALFRVQGSGPENMQAIQIEAASAGLNSSHCYILHGDSTVFTWCGNLTSSEDQELMERMLDLIKPNEPTKAQKEGSESEQFWELLGGKSEYPSQKIKRDGESDPHLFSCTYTNESLKATEIFNFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHDFLLENLASETPIYIVTEGNEPPFFTRFFTWDSSKSGMHGDSFQRKLAILTNKGKPLLDKPKRRVPAYSSRSTVPDKSQPRSRSMTFSPDRARVRGRSPAFNALAANFEKLNIRNQSTPPPMVSPMVRKLYPKSHAPDLSKIAPKSAIAARTALFEKPTPTSQEPPTSPSSSEATNQAEAPKSTSETNEEEAMSSINEDSKEEEAEEESSLPTFPYERLKTDSEDPVSDVDLTRREAYLTSVEFKEKFEMTKNEFYKLPKWKQNKLKMSVNLF", "text": "FUNCTION: Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Present in the apical and subapical regions of pollen tubes. SIMILARITY: Belongs to the villin/gelsolin family."}
{"protein": "MLRICGLGVVLSLAVAAVAVMAVWLMDWWGPRPGIRLFLPEELARYRGGPGDPGLYLALLGRVYDVSSGRRHYEPGAHYSGFAGRDASRAFVTGDYSEAGLVDDINGLSSSEILTLHNWLSFYEKNYVFVGRLVGRFYRKDGLPTSELTQVEAMVTKGMEANEQEQREKQKFPPCNSEWSSAKGSRLWCSQKSGGVHRDWIGVPRKLYKPGAKEPHCVCVRTTGPPSDQQDNPRHSNHGDLDNPNLEEYTGCPPLATTCSFPL", "text": "FUNCTION: Heme-binding protein which promotes neuronal but not astrocyte differentiation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily."}
{"protein": "MSDWQTVRTWLAGTYSNRAQAMAEPVWFIPVTLWYVEVAGLFGEGAGFFTEQVSEHTPNQPYRSRVLQLLDNPLRLENYRLKDQKVWAGAAKDPERLGRLRADDCEQLPGCTLYLERRGETFTGKMQPGGGCRLFPGDASYVEIEFELGERLFFTLDRGFEATTGEQTWGSRAGAYRYLKQLH", "text": "FUNCTION: Covalently attaches a chromophore to Cys residue(s) of phycobiliproteins. SIMILARITY: Belongs to the CpcT/CpeT biliprotein lyase family."}
{"protein": "MILIIYAHPYPHHSHANKRMLEQAGTLENVEIRSLYHLYPDFNIDVAAEQEVLSRASLIVWQHPMQWYSVPPLLKLWMDKVLTHGWAYGHGGTALHGKHLLWAVTTGGGENHFAIGSHPGFDVLSQPLQATALYCGLKWLPPFAMHCTFICDDDTLQAQARQYKQRLLTWQEVNHG", "text": "FUNCTION: Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF subfamily."}
{"protein": "MSDKPNAVSSHTTPDVPEVAATPELSTGICAGDYRAALRRHPAGVTVVTLDSGTGPVGFTATSFSSVSLEPPLVSFNIAETSSSINALKAAESLVIHLLGEHQQHLAQRFARSADQRFADESLWAVLDTGEPVLHGTPSWMRVKVDQLIPVGDHTLVIGLVTRVHAEEDDESAAAPLLYHEGKYYRPTPLGQ", "text": "FUNCTION: An NADH:FMN oxidoreductase which supplies reduced FMN for the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds (PubMed:9634856, PubMed:20349330). Provides DszA and DszC (DBTO2- monooxygenase and DBT-monooxygenase respectively) with reduced flavin (FMN); has no activity on NADPH or FAD (PubMed:9634856). The pathway substrate specificity has been augmented using mutagenesis, however no mutations allowed use of alkylated thiophenes (PubMed:11823208). FUNCTION: An NADH:FMN oxidoreductase which supplies reduced FMN for the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Provides DszA and DszC (DBTO2-monooxygenase and DBT-monooxygenase respectively) with reduced flavin (FMN). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family."}
{"protein": "MIIVIMGVSGSGKTVVGSQLAKKLGWNFYDADDYHPLENKEKMSQGTPLNDQDRHPWLCELHEIMMREKALGQHVVLACSALKRAYRSTLLTGSTPHWPENYQENDDLSSDTLFVHLHGSLEILSRRLLERKGHFMPRTLLDSQIDTLEPPSAPERFIAIDVDKDISVIVSEIEGEVDRKMMLVKSAQKD", "text": "SIMILARITY: Belongs to the gluconokinase GntK/GntV family."}
{"protein": "MENITRELFDQYISRQAQLNRVSPAAVAAKFAVDPTVQQKLEAAAQESDSFLSKINVFGVTQQIGQKVLIGSKGPLAGVNNSTTTRRNPADNSKMEPYDYMCRKVNYDYGISYEQLDAWAHQPNFQPLISSAMARQMSLDRIMIGFNGTSYADPSNRAANPLLQDCGIGFLEKIRKEAPHRVISNITVTSRDEDNKIITKGTYGNVSAAVYDAKNSLMDEWHKRNPDNVVILAGDLLTTSNFPAINAMSQTNPNTEMLAGQLIVAQERVGNMPTFIAPFFPVNGILITPFKNLSIYYQRGGLRRTIKEEPEYNRVATYQSSNDDFVVEDYGNVAFIDGITFAQPENGG", "text": "SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the P2-like viruses major capsid protein family."}
{"protein": "MNRIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTRVIKEDIVRRERIGFRVQPDQGKIFYSSIKEMKPPLRGHGKGAWGKENVRKTEESVLKVEVDLDQTQRERKMQNALGRGKVVPLWHPAHLQTLPVTPNKQKTDGRGTKPEASSHQGTPKQTTAQGAPKTSFIAAKGTQVVKISVHMGRVSLKQEPRKSHSPSSDTSKLAAERDLNVTISLSTDRPKQRSQAVANERAHPASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGSLSKDDGARGAHGKKLNFSESHLVIITKEEEQKADPKEVSNSKTKTIFPKVLGKSQSKHISRNRSEMSSSSLAPHRVPLSQTNHALTGGLEPAKINITAKAPSTEYNQSHIKALLPEDSGTHQVLRIDVTLSPRDPKAPGQFGRPVVVPHGKEKEAERRWKEGNFNVYLSDLIPVDRAIEDTRPAGCAEQLVHNNLPTTSVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDVIAKNRIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQRELRKKLKCKSFKWYLENVFPDLRAPIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHKSTSVFHPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYYEA", "text": "FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily."}
{"protein": "MPLGLGRRKKAPPLVENEEAEPSRSGLGVGEPGPLGGSGAGESQMGLPPPPASLRPRLVFHTQLAHGSPTGRIEGFTNVKELYGKIAEAFRLPAAEVMFCTLNTHKVDMDKLLGGQIGLEDFIFAHVKGQRKEVEVFKSEDALGLTITDNGAGYAFIKRIKEGSVIDHIQLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGRTFTLKLTEPRKAFDMISQRSSGGHPGSGPQLGTGRGTLRLRSRGPATVEDLPSAFEEKAIEKVDDLLESYMGIRDTELAATMVELGKDKRNPDELAEALDERLGDFAFPDEFVFDVWGAIGDAKVGRY", "text": "FUNCTION: May be involved in G protein-linked signaling. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the GIPC family."}
{"protein": "MVKGKSKKVVTSTIQEENVSKEPLAPIVPIVPDILRNEEELVFIEIEKRDKNEIVNVPITQTNPVVQTNNKTNNKNNINNNNNNNNNNNNNNINNNNKNNKVKKTTTTTKKNNEKSNEKQKSVKFANKINESRSARADLTFPVSRIEKMIREGRFTKRCSSDAPVFLAAVLEYLTLEILELSITYANQKNKTRITPQHIHLSICCDAELNDLLKNVTIANGGVPKFIHPILLDTPKKKGHQQNMNENDISKEKDIKSSKN", "text": "SIMILARITY: Belongs to the histone H2A family."}
{"protein": "MLSPFLAYLLSVVLLCRIARSQYSSDQCSWRGSGLTHEGHTRGVEQVYLRCAQGFLEWLYPTGAIIVNLRPNTLSPAASLLSVCIKPSKESSGTHIYLDRLGKLRLLLSEGDQAEGKVHCFNIQDGALFIEAVPQRDISRKITAFQYELVNHRPGADPQSLSAPCQPCTDAEVLLAVCTSDFVARGRILGVSEEDEQTSVTVSLSHLYRQKTQVFVSGGGRAKRWTGFVKMSRQCGVKPGDGEFLFTGTVRFGEAWLSCAPRYKDFLRVYQDARQQGTNPCHLETD", "text": "FUNCTION: Hormone induced following exercise or cold exposure that promotes energy expenditure. Induced either in the skeletal muscle after exercise or in adipose tissue following cold exposure and is present in the circulation. Able to stimulate energy expenditure associated with the browning of the white fat depots and improves glucose tolerance (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the meteorin family."}
{"protein": "MSDDTFSRIQSIVEEQLGVESSKIKLETDFQKDLGADSLDVVELIMAFEEEFDINVNDDAAGDIKTVQQVLEYIEAESAK", "text": "FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the acyl carrier protein (ACP) family."}
{"protein": "MEPTVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIVTIRAKVTRAFSTSMEISIKVRVQDKFTGIQKLLCVAFSTFVVKPLGKEKVHLKPVLLQTEQEQVEHRLASERRKVRLQHENTFSNIMKESNWLRDPVCNEEEGTATTMATSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFNAIVNNTFQNSVEVGVRVEAFDCREWAEGQGRHINSAFLIYNAVDDQEELITFPRIQPISKDDFRRYQGAIARRRIRLGRKYVISHKKEVPLGTQWDISKKGSISNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKQVGSPARVAYHLLSDFTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSQRKPLKDDNTYIVALMSVVLPSVPPSPQYIRSQVICAGFLIQPVDSSSCTVAYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENATHDGLKSVL", "text": "FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes acetyl-CoA. SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
{"protein": "MFPGSTWTVIVEQIAEYEEVIDPKAFFDKIISLWKEYPNAISNRITTSVSVDTDSDLWNEVLRTFETHYKFCPRDCSEIAITKIIHKDLANNKFSDNAFEVSYYEEELLVRFYPITLDGMQHPHFESPYSIAIKIPTDTSIQLQFLKQANSSQEHFEFMKKQAFKQLYTWLKGIDLSKSSRKTNSLLDKESYIKTYRHIREDYGRGMIKGWTENSNPQKSIFEDCGIASYINELVNSDLLPKPNKFVDIGCGNGLLVHLLNKIGMSGYGIDVRHRNIWKTTLKDVDLREMPVDPQIVVQNEPHFDLDVDLLIGNHSDELTPWIPVMAAKLNCNFFLIPCCPFNFFGKYANNGSHLGPKRIVSQYESFFEWTVSVAERLGFDVKIDRLAIPSTKRLCIIGRVPEGGLCPNVDETINSMTEGQKFIARPKEIKTTNCMNIPVTDRERIAKKLFDFVLNYSDAVRDGWRCGGEVPLAQLAALLTEEDKKLMKDQDGGLQTFLRNQHQIFHVYQATARLRDFRQPVVQKRQSWKPKKAETIRKAPCWMSLHHPDGCPVGQEACRYEH", "text": "FUNCTION: Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRM44 family."}
{"protein": "MQRITITIDDDLMAALDRMIEIKGYQNRSEALRDLARTGLQQASLEEGQMEACVGVLSYTYDHSARDLSKKLTNTHHDHHNISVASMHVHLDHDRCLEVSILKGKTDDVRHFADHVKAERHVTHGTLAVLPL", "text": "FUNCTION: Transcriptional repressor of the nikABCDE operon. Is active in the presence of excessive concentrations of intracellular nickel (By similarity). FUNCTION: Transcriptional regulator. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family."}
{"protein": "AVATALIQVAYMGLVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKDNKEFKDLPPERAFADFVLCNLVLHLVIMNFLG", "text": "FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DAD/OST2 family."}
{"protein": "MDWLAKYWWILVIVFLVGVLLNVIKDLKRVDHKKFLANKPELPPHRDFNDKWDDDDDWPKKDQPKK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0370 family."}
{"protein": "STLEVRSQATQDLSEYYNRPYFDLRNLSGYREGNTVTFINHYQQTDVKLEGKDKDKIKDGNNENLDVFVVREGSGRQADNNSIGGITKTNRTQHIDTVQNVNLLVSKSTGQHTTSVTSTNYSIYKEEISLKELDFKLRKHLIDKHDLYKTEPKDSKIRVTMKNGDFYTFELNKKLQTHRMGDVIDGRNIEKIEVNL", "text": "FUNCTION: Secreted protein that plays a role in the inhibition of host immune system. Targets myeloid cells such as monocytes or granulocytes through binding with sialyllactosamine-containing glycoproteins (PubMed:18045383). Prevents initial rolling of neutrophils toward the site of infection by interacting with host SELPLG (PubMed:18045383). Disrupts neutrophil motility by induction of cell adhesion via interacting with glycans but independently of SELPLG (PubMed:30862940). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family."}
{"protein": "MDAQKMKMVIGLVLVATTAFALMIPAASAVDDFITRRAYDNLVKSGAIKDIPVMAKTIISNPVLEEGMLTYYTNKKLGDSAISCGETCFKFKCYTPRCSCSYPVCK", "text": "FUNCTION: Probably participates in a plant defense mechanism. Has low hemolytic activity. SIMILARITY: Belongs to the cyclotide family. Moebius subfamily."}
{"protein": "MVQQKVEVRLKTGLQARPAALFVQEANRFTSDVFLEKDGKKVNAKSIMGLMSLAVSTGTEVTLIAQGEDEQEALEKLAAYVQEEV", "text": "FUNCTION: Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA. SIMILARITY: Belongs to the HPr family."}
{"protein": "MELNFEKPLSLLTLDEIDQQEGGVIQSFRTGHTSPYPDPADWLNGEEPPPGVFITSVEKVLNWSRHYSLWPVMFGLACCAIEMMCMAASRWDLARFGMDIFRASPRQADLMIVAGTLTWKMAPWLKRIYDQMPEPKWVLAMGACGTSGGLFRDSYSVVPGFNLVVPVDVYVPGCPPRPEALMRAIMDIHEKIDKTRILKR", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERSGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDQYVMEELDIATEALPEDERENRWRDLVTQNTEGEVDIALVGKYDLEDAYMSVHEALKHAGLEKNVDVNVQWVNSEKMNDHHADRMREADAIVVPGGFGARGTEGKIEAIRYARENDIPFLGLCLGFQMAVVEYARNVLDLDDAHSAELDEDTPHPVIDILPEQYEIEDMGGTMRLGAHETEIDANTLAATLYGGESCTERHRHRYEVNPEYIDDLEAAGLKFSGYAENRMEILELAPEDHPYFIGTQFHPEFRSRPTRASPPFVGLLEAVLGDDPHTVTTEEVSH", "text": "FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to the cytoophidium, a short subcellular filamentary structure where CTP synthase is compartmentalized. Only a few cells form cytoophidia under standard growth conditions, they are observed in late log phase. Stress conditions such as treatment with 50 uM 6-diazo- 5-oxo-l-norleucine (DON, an inhibitor) or growth at low salt (1.5 M instead of the usual 3.4 M) also induces their appearance. In all these conditions cells are barely growing. SIMILARITY: Belongs to the CTP synthase family."}
{"protein": "MPRRPSSGRRVLKHQPLTFSPFMRLLSFASMARRDLSHPEDCQCSDEDISFDEKQKIPNLPRKGKEEQVSDSSDEEDSQEDVQADFEFFDPKPTDFHGVKILLQNYLDDKEWDLSSFVDCILEQTTVGTVVKVADDEDESVFALVTALNMARDKDNKCFRELKEFLRKVCSEKNIANNLEMLLEKKAQDVGLLVSQRVMNLPPQLLPPLYDGLFDEVSWAIEDEPTEKLRRSFRFKSYLLVTKIYKLKNPKQRKPRHGEEDIEDTVFLKPEDELFLELSSWSFTFPMRSQLVTSQEMKNYQLMGLVMAVEANKIPKFRQMLNSLID", "text": "SIMILARITY: Belongs to the BCP1 family."}
{"protein": "MEKVPGDMEIERRERSEELSEAERKAVQATWARLYANCEDVGVAILVRFFVNFPSAKQYFSQFRHMEDPLEMERSPQLRKHACRVMGALNTVVENLHDPDKVSSVLALVGKAHALKHKVEPMYFKILSGVILEVIAEEFANDFPVETQKAWAKLRGLIYSHVTAAYKEVGWVQQVPNTTTPPATLPSSGP", "text": "FUNCTION: May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the globin family."}
{"protein": "MTYKKAVKIKTPGGKEAELAPEKAWTLAPKGRKGVKIGLFKDPESGKYFRHKLPDDYPV", "text": "FUNCTION: A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cren7 family."}
{"protein": "LTYDEIQSKGGSTGYDNAVALPAGGR", "text": "FUNCTION: Stabilizes the manganese cluster which is the primary site of water splitting. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbO family."}
{"protein": "AKKRSRSRKRSASRKRSRSRKRSASKKSSKKHVRKALAAGMKNHLLAHPKGSNNFILAKKKAPRRRRRVAKKVKKAPPKARRRVRVAKSRRSRTARSRRRR", "text": "SUBCELLULAR LOCATION: Nucleus. Chromosome."}
{"protein": "MNPSEMQRKGPPRRWCLQVYPTAPKRQRPSRTGHDDDGGFVEKKRGKCGEKQERSNCYCVCVERSRHRRLHFVMC", "text": "FUNCTION: May possess a function in tumorigenesis. SUBCELLULAR LOCATION: Nucleus Note=When overexpressed."}
{"protein": "MDNLNLNKHISGQFNAELESIRTQVMTMGGMVEQQLSDAITAMHNQDSELAKRVIEGDKNVNMMEVAIDEACVRIIAKRQPTASDLRLVMAIIKTIAELERIGDVADKICRTALEKFSQQHQPLLVSLESLGRHTVQMLHDVLDAFARMDLDEAVRIYREDKKVDQEYEGIVRQLMTYMMEDSRTIPSVLTALFCARSIERIGDRCQNICEYIFYFVKGQDFRHVGGDELDKLLAGKDPKE", "text": "FUNCTION: Part of the phosphate (Pho) regulon, which plays a key role in phosphate homeostasis. Encoded together with proteins of the phosphate-specific transport (Pst) system in the polycistronic pstSCAB- phoU operon. PhoU is essential for the repression of the Pho regulon at high phosphate conditions. In this role, it may bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR- PhoB transitory complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PhoU family."}
{"protein": "MTNPENTPMTTTNEGGKGLTEYEAKIYDRSIRLWGVDAQAKLRQSKVLFIGINGLMSEIIKNVVLAGVDSITLVDDHIITTSDLSAHLFINEDSVGKVISTESVFAISELNPLVTIDVYDKEIETMDDQFIKNYTMVVISDKNLNNVSKVNSLCRKNNVSFIFSHSFGLKGLFFSDLNEFKYFTKTTTEPPKTETHISIFKSFKESMGYDWSKTNSRTPLPFFALSTLYQFEEKHNRVPDNISDSDLSELKSIINSSIEKFNLKNTDSNKYFEETKDLLNKMNIEISPVCAIVGGIVGAEIIKIITQNMQVLNNFFFYDGVKGTGLVEQF", "text": "FUNCTION: The dimeric enzyme acts as an E1 ligase for sumo. It mediates ATP-dependent activation of sumo and formation of a thioester with a conserved cysteine residue on sae2 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ubiquitin-activating E1 family."}
{"protein": "MATPATESVQCFGRKKTAVAVTHCKRGRGLIKVNGSPIELVKPEILRYKAFEPILLLGRHRFVGVDMRIRVRGGGKTSQIYAIRQSIAKALVAYYQKYVDEQAKKEVKDILMRYDRTLLVADPRRCEPKKFGGRGARSRFQKSYR", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS9 family."}
{"protein": "MQKTSILIVALVALFAITEALPSLPTTGPIRVRRQVLGGSLTSNPAGGADARLDLTKGIGNPNHNVVGQVFAAGNTQSGPVTTGGTLAYNNAGHGASLTKTHTPGVKDVFQQEAHANLFNNGRHNLDAKVFASQNKLANGFEFQRNGAGLDYSHINGHGASLTHSNFPGIGQQLGLDGRANLWSSPNRATTLDLTGSASKWTSGPFANQKPNFGAGLGLSHHFG", "text": "FUNCTION: Hemolymph antibacterial protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the attacin/sarcotoxin-2 family."}
{"protein": "MGDGLTPEGKAQLITRNLQEVLGEDKMKEILKERPLRIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWDLLELRTRYYEQVIQAMLQSIGVPLERLRFIRGTEFQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYAKRIHLMNPMVPGLTGAKMSSSEEESKIDLLDSPADVKKKLKKAFCEPGNIENNGVLSFVRHVLFPLKSEFVVLRDEKFGGNKTYTDFETLEKDFTEQLVHPGDLKASVEKALNKLLDPIREKFNSPEMKKLSNDAYPGASKQKTVPKGSTKNSGPEEIDPSLLDLRVGKILSVRQHPDADSLYVESVDVGEENPRCVVSGLVQYVPSDQLLGRSVVLLCNLKPQKMRGIESQGMLLCASTEGEQKQVEPLDPPTGSAPGERIYIEGYENGEPEGELKPKKKVFEKLQVDFRISDDLCAQWKGKNFLTKLGSVTCKTLRGGSIS", "text": "FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MSKFLLQSHSANACLLTLLLTLASNLDISLANFEHSCNGYMRPHPRGLCGEDLHVIISNLCSSLGGNRRFLAKYMVKRDTENVNDKLRGILLNKKEAFSYLTKREASGSITCECCFNQCRIFELAQYCRLPDHFFSRISRTGRSNSGHAQLEDNFS", "text": "FUNCTION: Involved in glucose metabolism. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
{"protein": "MGLETEKADVQLFLDDDSYSHHGDVDYADPEKFADSGHDRDPHRLNSHLKVGFEDVIAEPMTTHSCDKVWICSHALFEISKYVMYKFLTVFLAIPLAFAAGILFATLSCLHIWIIMPFVKTCLMVLPSVQTIWKSVTDVIIAPLCTSVGRSLSSISLQLSHD", "text": "FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. Ser-36- phosphorylated form resides in intracellular compartments (By similarity). SIMILARITY: Belongs to the caveolin family."}
{"protein": "MMEGLGEHSTAGEMGPLLGAVAATASPQSLMEYSSDADFIESLPLVVKYRVYTLKKLQAKCAVLEAKYLREFHSVERKFATIYGPLLEKRRQITNALYEPTKEECER", "text": "SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
{"protein": "MAADGQCSLPASWRPVTLTHVEYPAGDLSGHLLAYLSLSPVFVIVGFVTLIIFKRELHTISFLGGLALNEGVNWLIKNVIQEPRPCGGPHTAVGTKYGMPSSHSQFMWFFSIYSFLFLYLRMHQTNNARFLDLLWRHVLSLGLLAAAFLVSYSRVYLLYHTWSQVLYGGIAGGLMAIAWFIFTQEVLTPLFPRIAAWPVSEFFLIRDTSLIPNVLWFEYTVTRAEARNRQRKLGTKLQ", "text": "FUNCTION: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dolichyldiphosphatase family."}
{"protein": "MVKTITISDDVYNELLRIKGNKSFSEVLRELLKERKGNKEVLKRIFGILSEEEYQEVKKRLKELEGEFEKWEQSLTQM", "text": "FUNCTION: Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. SIMILARITY: Belongs to the UPF0330 family."}
{"protein": "MKLTTMIKTAVAVVAMAAIATFAAPVALAAYPITGKLGSELTMTDTVGQVVLGWKVSDLKSSTAVIPGYPVAGQVWEATATVNAIRGSVTPAVSQFNARTADGINYRVLWQAAGPDTISGATIPQGEQSTGKIYFDVTGPSPTIVAMNNGMEDLLIWEP", "text": "SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MCVFQILIIVTTIKVAGTANINHIDVPAGHSATTTIPRYPPVVDGTLYTETWTWIPNHCNETATGYVCLESAHCFTDLILGVSCMRYADEIVLRTDKFIVDAGSIKQIESLSLNGVPNIFLSTKASNKLEILNASLQNAGIYIRYSRNGTRTAKLDVVVVGVLGQARDRLPQMSSPMISSHADIKLSLKNFKALVYHVGDTINVSTAVILGPSPEIFTLEFRVLFLRYNPTCKFVTIYEPCIFHPKEPECITTAEQSVCHFASNIDILQIAAARSENCSTGYRRCIYDTAIDESVQARLTFIEPGIPSFKMKDVQVDDAGLYVVVALYNGRPSAWTYIYLSTVETYLNVYENYHKPGFGYKSFLQNSSIVDENEASDWSSSSIKRRNNGTIIYDILLTSLSIGAIIIVIVGGVCIAILIRRRRRRRTRGLFDEYPKYMTLPGNDLGGMNVPYDNTCSGNQVEYYQEKSAKMKRMGSGYTAWLKNDMPKIRKRLDLYH", "text": "FUNCTION: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells. In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host cell junction Host Golgi apparatus membrane; Single-pass membrane protein Host endosome membrane; Single-pass membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN), maybe through an interaction with PACS-1 sorting protein. The heterodimer gE/gI then redistributes to cell junctions to promote cell-cell spread later in the infection (By similarity). SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family."}
{"protein": "MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRVSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAGNNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKALRPNGLPESLIRYDARQKDMATNSVTELVEAVKRPRALSESTNLHPFMTKSESDELPKKPARRMSENVVPSGRRNSGGGRRNSMQRINEIPEKKSRKSSLSFMGIKKKSESLDESIDDGFIEYGEEDDEISDRDERPESVDDKVRQKEMRKGIDLATTLERIEKNFVITDPRLPDNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDLTTVKKIRNAIDNQTEVTVQLINYTKSGKKFWNIFHLQPMRDQKGEVQYFIGVQLDGSKHVEPVRNVIEETAVKEGEDLVKKTAVNIDEAVRELPDANMTPEDLWANHSKVVHCKPHRKDSPPWIAIQKVLESGEPIGLKHFKPVKPLGSGDTGSVHLVELVGTDQLFAMKAMDKAVMLNRNKVHRARAEREILDLLDHPFLPALYASFQTKTHICLITDYYPGGELFMLLDRQPRKVLKEDAVRFYAAQVVVALEYLHCQGIIYRDLKPENVLIQGNGDISLSDFDLSCLTSCKPQLLIPSIDEKKKKKQQKSQQTPIFMAEPMRASNSFVGTEEYIAPEIISGAGHTSAVDWWALGILMYEMLYGYTPFRGKTRQKTFTNVLQKDLKFPASIPASLQVKQLIFRLLQRDPKKRLGCFEGANEVKQHSFFKGINWALIRCTNPPELETPIFSGEAENGEKVVDPELEDLQTNVF", "text": "FUNCTION: Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Phosphorylates BLUS1, a kinase involved in stomatal opening. Required for blue light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to a low rate of blue light. Also mediates rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under a low rate but not under a high rate of blue light. Contributes to the chloroplast accumulation but seems not to be required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Confers sensitivity to drought. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family."}
{"protein": "MSRSYNDELQFLEKINKNCWRIRKGFVPNMQVEGVFYVNDALEKLMFEELRNACRGGGVGGFLPAMKQIGNVAALPGIVHRSIGLPDVHSGYGFAIGNMAAFDMNDPEAVVSPGGVGFDINCGVRLLRTNLDESDVQPVKEQLAQAMFDHIPVGVGSKGVIPMNAKDLEEALEMGVDWSLREGYAWAEDKEHCEEYGRMLQADPNKVSARAKKRGLPQLGTLGAGNHYAEIQVVDEIFNEYAAKKMGIDHKGQVCVMIHSGSRGLGHQVATDALVAMEKAMKRDKIIVNDRQLACARIASPEGQDYLKGMAAAGNYAWVNRSSMTFLTRQAFAKVFNTTPDDLDLHVIYDVSHNIAKVEQHVVDGKERTLLVHRKGSTRAFPPHHPLIAVDYQLTGQPVLIGGTMGTCSYVLTGTEQGMTETFGTTCHGAGRALSRAKSRRNLDFQDVLDKLADMGIAIRVASPKLVMEEAPESYKNVTDVVNTCHDAGISKKAIKLRPIAVIKG", "text": "FUNCTION: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low. SIMILARITY: Belongs to the RtcB family."}
{"protein": "MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEALIGYDVRDQQAIDKAMIALDGTPNKGKLGANAILGVSIAVARAAADFLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMIVPAGAPTFKEALRWGAEIFHALKKILKERGLETAVGDEGGFAPKFDGTEDAVETIIKAIETAGYKPGEEVFLGFDCASSEFYDNGVYDYTKFEGEKGAKRSAAEQIDYIEELVNKYPIITIEDAMDENDWDGWKALTARLGDRVQLVGDDFFVTNTDYLARGIKEGAANSILIKVNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDSTIADISVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAEYRGLKSFYNLKK", "text": "FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds plasminogen and human salivary mucin MG2 when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity that may help the dissemination through oral tissues and entrance into the blood stream. SUBCELLULAR LOCATION: Cytoplasm Secreted Cell surface Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface. SIMILARITY: Belongs to the enolase family."}
{"protein": "MAHGKSAFFTTDAFVAISVLVVVFSIVVPLPTQILDALMAFNLIFNLLILLMVLFVEKPTDFSVFPSLLLTSTVFGLGLNVSSTRLILTLGDRFSGYMIRAFSSFVVGGSGTQGLVIGFTVFIILIAVQAFVITKGATRIAEVAARFTLDFNATKSMSIDAEYNAGVITEEEARERKRQIQREADFFGAMDGASKFVSGNVKIGIFITIVNVIAGLIVGVIFRREGFQAALQTYTNLTIGDGLLAQLPSLLLSVATGFIVTRSSDQGSFGQNVQEQFSKSALVYFIGSGALIVMAVLPGFPHSILFFMAVCFAFVGLQLRKRERVHVQEHEMQKSSDKKGMQQTQDSTSEMGPIVPLDPLSLELGYGLIPLVDKEKGAELLSRITVIRKDAALDLGLVAPKIRIIDNMRLDPSSYCFKIQGLEVARGKLRLGWFLAIKSGQVTEEVPGERTIDPTFGLPAVWISEENRDRAERVGYTVVAPSAIIATHLTQVIRTNAADILGRQNVQMIIDALRKEYPAVVDDVTQKCPLGKIQKVLQGLLREQVSIRNTVAIFETLADFASTSDTVPVPILIEKVRQRLGRQICLQYADEQNVLHVMRLDSSLETFLSEKIALTVDSLSILTLSLDEQRQVLQAVRTVFVPTRQEGYIPVLLTTDTIRSAMWNLFFSDRIEIAVMSYKEVSTDMRIETVGVVRIEESDVDAFVRKQ", "text": "FUNCTION: Involved in the export of flagellum proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family."}
{"protein": "MISVNLASLPIVEDMINRKEDLNIEVIKLENGATVLDCGVNVMGSFEAGKLFTKICLGGLAHVGISISGSLDNKLVLPCVKIKTSHPAIATLGAQKAGWSVSVGKYFAMGSGPARALAMMPKATYEEIDYKDEADVAILCLESSQLPDENVADHVAEKCGVDVSKVYLLVAPTASMVGAVQISGRVVENGTYKMLEALHFDVRKVKFAAGIAPVAPVIGDDLKMMGATNDMVLYGGRTYYYVKSDEGDDIENLCKSLPSCSAETYGKPFLDVFKEANYDFYKIDKGIFAPAVVTINDLRTGKLMSYGETNVDVIKKSLKFSQL", "text": "FUNCTION: Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MCH family."}
{"protein": "MAENSNIDDIKAPLLAALGAADLALATVNELITNLRERAEETRTDTRSRVEESRARLTKLQEDLPEQLTELREKFTAEELRKAAEGYLEAATSRYNELVERGEAALERLRSQQSFEEVSARAEGYVDQAVELTQEALGTVASQTRAVGERAAKLVGIELPKKAAPAKKAAPAKKAAPAKKAAAKKAPAKKAAAKKVTQK", "text": "FUNCTION: Required for extrapulmonary dissemination. Mediates adherence to epithelial cells by binding to sulfated glycoconjugates present at the surface of these cells; binds heparin, dextran sulfate, fucoidan and chondroitin sulfate. Promotes hemagglutination of erythrocytes of certain host species. Induces mycobacterial aggregation. FUNCTION: Required for extrapulmonary dissemination. Mediates adherence to epithelial cells by binding to sulfated glycoconjugates present at the surface of these cells; binds heparin, dextran sulfate, fucoidan and chondroitin sulfate. Promotes hemagglutination of erythrocytes of certain host species. Induces mycobacterial aggregation. FUNCTION: Required for extrapulmonary dissemination. Mediates adherence to epithelial cells by binding to sulfated glycoconjugates present at the surface of these cells (By similarity). SUBCELLULAR LOCATION: Cell surface. SUBCELLULAR LOCATION: Cell surface. SUBCELLULAR LOCATION: Cell surface. SIMILARITY: To M.leprae HbhA."}
{"protein": "MDLAANEISIYDKLSETVDLVRQTGHQCGMSEKAIEKFIRQLLEKNEPQRPPPQYPLLIVVYKVLATLGLILLTAYFVIQPFSPLAPEPVLSGAHTWRSLIHHIRLMSLPIAKKYMSENKGVPLHVGDEDRPFPDFDPWWTNDCEQNESEPIPANCTGCAQKHLKVMLLEDAPRKFERLHPLVIKTGKPLLSEEIQHFLCQYPEATEGFSEGFFAKWWRCFPERWFPFPYPWRRPLNRSQILRELFPVFTHLPFPKDASLNKCFFLHPEPVVGSKMHKMPDLFIIGSGEAMLQLIPPFQCRRHCQSVAMPIEPGDIGYVDTTHWKVYIIARGVQPLVICDGTAFSEL", "text": "FUNCTION: Exhibits histone deacetylase (HDAC) enhancer properties. May play a role in cell cycle progression and wound repair of bronchial epithelial cells. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Cytoplasm."}
{"protein": "MNKSVIGTKQMVVSPHYLASQAGNRILDKGGNAFDAAVAVSACLAVVYPHMTGLGGDSFWLTFHQETKAVKVYNGSGRSGKNVTRDVYKGKSAIPLRGIDSAITVPGMVDSWDAVLKEYGRLSLADVLEPARDYAQNGFPVSADQCRHTEKNIELLASTPYTADIFTRRGKAPVPGERFVQKELADSLNLIAEKGRSAFYEGDLAQRIVSHLQNNGSYMTIDDFKAHRGEWAAPVSSDYRGYSVYQAPPNSQGFTGLLTLNILENYDFTQIEHGSFEYYHVLVEALKKSFLDRDAVLTDPAFADIPLERLLDKRYAKQLAEEIGYLAIPAESRPVGSDTAYAAVIDADGNAVSFIQSLYFEFGSAVTAGDTGILLQNRGSFFSLDENHVNTLEPRKRTFHTLMPAMVCKGGKPKILYGTQGGEGQPQTQTAIITRMLDYGMHPQQAISEPRWVWGRTWGEEYEGLRVEGRFTDKTIQKLKDSGHLVEVVGDYDPLMGQAAAIKVDEEGFLQGGADPRGDGAAVGI", "text": "FUNCTION: Overexpressed protein with an N-terminal His tag has been reported not to hydrolyze glutathione; it is not clear if the construct is processed to 2 subunits (PubMed:14762019). SIMILARITY: Belongs to the gamma-glutamyltransferase family."}
{"protein": "MQLPAMSCSPSQSSAAAAAAYGCCQRILLASTSLPATGRPARLGLKLRSTHSLQIRNRRFVCQAMTETEPDGDGNGDEEKEELGDDASSPSVYSVTQENGSAESETNADNTKDETVNTEPLSSSDTVQNIDGDATPASDAQENVEVVDVAVGSPLPGMKQQLDESVRIPKATIDILKDQVFGFDTFFVTSQEPYEGGILFKGNLRGQPAKSYEKITNRLQNKFGDQYKLFLLINPEDDKPVAVVVPRQTLQPETTAVPEWFAAASFGVVTIFTLLLRNVPLLQDNLLSTFDNLELLKDGVYGALVTAAIIGVHEIAHILAARDTGIKLAVPYFVPSWQIGSFGAITRIVNIVRNREDLLKVAAAGPLAGFSLGFVLLLLGFILPPSDGLGLVIDPAVFHESFLVGGLAKLILGDALKEGTKLSINPLVLWAWAGLLINAINSIPAGELDGGRIAFAMWGRKISSRISSLAIGLLGISALFNDVAFYWVVLIFFLQRGPISPLSEEITEPENNYISIGVAILLFGLLVCLPYPFPFDPSQLTDFDL", "text": "FUNCTION: Probable membrane-associated metalloprotease that may be involved in chloroplast development. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
{"protein": "MHANWKTWAHVTKLDPDKRLPRGAVEEIATSGTDALMLSGTLNVTRENLQELLDLVSAYGLPLVVEPASPDCAIFDGGIDHLFVPSVLNTNDVRWIVGKHYAWLRQASGIDWEMVVPEAYIVLNPNSAVGRVTGADCSLSTGDVAAFAQVADRYFRFPIVYIEYSGTYGDPAIVQAASEAVENATLYYGGGIRSAEQAAEMGRYADTIVVGNAVYEEGIDVLRATVRAVQ", "text": "FUNCTION: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I subfamily."}
{"protein": "MATGDLKRSLRNLEQVLRLLNYPEEVDCVGLIKGDPAASLPIISYSFTSYSPYVTELIMESNVELIAKNDLRFIDAVYKLLRDQFNYKPILTKKQFIQCGFAEWKIQIVCDILNCVMKKHKELSSLQKIPSQQRKKISSGKSEPPLGNEKISAEAVGVDISGRFMTSGKKKAVVIRHLYNEDNVDISEDTLSPITDVNEAVDVSDLNATEIKMPEVKVPEIKAEQQDVNVNPEITALQTMLAECQENLKKLTSIEKRLDCLEQKMKGKVMVDENTWTNLLSRVTLLETEMLLSKKNDEFIEFNEVSEDYASCSDMDLLNPHRKSEVERPASIPLSSGYSTASSDSTPRASTVNYCGLNEISEETTIQKMERMKKMFEETAELLKCPNHYL", "text": "FUNCTION: Centriole-enriched microtubule-binding protein involved in centriole biogenesis. In collaboration with CEP295 and POC1B, is required for the centriole-to-centrosome conversion by ensuring the formation of bona fide centriole wall (PubMed:32060285). Functions as a linker component that maintains centrosome cohesion. Associates with CROCC and regulates its stability and localization to the centrosome (PubMed:31974111). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, spindle pole Midbody Note=Localizes to the proximal end of mother and daughter centrioles."}
{"protein": "MEGERAPLLGSRRAAAAAGVFAGRRAACGAVLLAELLERAAFYGVTANLVLFLNGAPFNWEGAQASQALLLFMGLTYLGSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPRSRSFLCGDPHPELVRNCSAPFPNGTAVCPDAAARRCAPATFAGLVLVGLGVATVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFLTGYLIPTVCVAIAFLVFLCGQSVFITKPPDGSAFTDMFRILTYSCCSQRGGQRRSGEGLGVFQQSSKHSLFDSCKMSRGGPFTEDKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYVLQSLHLKIPEISSITTTHHTLPAAWLTMFDAVLILLLIPLKDKLVDPVLRRHGLLPSSLKRIAVGMFFVTCSAFAAGILESKRLDLVKEKTINQTIGGVVYHAADLPIWWQIPQYVLIGISEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGIGSFVGSGLLALVSLKAIGWMSSHTDFGNINSCHLHYYFFLLAAIQGATLLLFLIVSVKYDRQRARTDGGTASTRT", "text": "FUNCTION: Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response (PubMed:9092568). Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans (By similarity). Transporter activity is pH-dependent and maximized in the acidic lysosomal environment (PubMed:9092568). Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD- like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso- 2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand. Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I) productions in plasmacytoid dendritic cells (pDCs). Independently of its transporter activity, also promotes the recruitment of innate immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9: TASL recruitment leads to the specific recruitment and activation of IRF5 (By similarity). Required for isotype class switch recombination to IgG2c isotype in response to TLR9 stimulation. Required for mast cell secretory-granule homeostasis by limiting mast cell functions and inflammatory responses (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
{"protein": "MPSPYDGKRTVTQLVNELEKAEKLSGRGRAYRRVCDLSHSNKKVISWKFNEWDYGKNTITLPCNARGLFISDDTTNPVIVARGYDKFFNVGEVNFTKWNWIEENCTGPYDVTIKANGCIIFISGLEDGTLVVCSKHSTGPRADVDRNHAEAGEKQLLRQLAAMNINRSDFARMLYTHNVTAVAEYCDDSFEEHILEYPLEKAGLYLHGVNVNKAEFETWDMKDVSQMASKYGFRCVQCITSNTLEDLKKFLDNCSATGSFEGQEIEGFVIRCHLKSTEKPFFFKYKFEEPYLMYRQWREVTKDYISNKSRVFKFRKHKFITNKYLDFAIPILESSPKICENYLKGFGVIELRNKFLQSYGMSGLEILNHEKVAELELKNAIDYDKVDERTKFLIFPISVIGCGKTTTSQTLVNLFPDSWGHIQNDDITGKDKSQLMKKSLELLSKKEIKCVIVDRNNHQFRERKQLFEWLNELKEDYLVYDTNIKVIGVSFAPYDKLSEIRDITLQRVIKRGNNHQSIKWDELGEKKVVGIMNGFLKRYQPVNLDKSPDNMFDLMIELDFGQADSSLTNAKQILNEIHKAYPILVPEIPKDDEIETAFRRSLDYKPTVRKIVGKGNNNQQKTPKLIKPTYISAKIENYDEIIELVKRCIASDAELTEKFKHLLASGKVQKELHITLGHVMSSREKEAKKLWKSYCNRYTDQITEYNNNRIENAQGSGNNQNTQVKTTDKLNFRLEKLCWDEKIIAIVVELSKDKDGCIIDENNEKIKGLCCQNKIPHITLCKLESGVKAVYSNVLCEKVESAEVDENIKVVKLDNSKEFVGSVYLNF", "text": "FUNCTION: One of the two proteins required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction. SIMILARITY: Belongs to the TRL1 family."}
{"protein": "MEVSRPYVNTVDVIDFGIDKRFFRLPVSGILAQEGITPNGPQIAIINALEDPRHRFVTACVSRRVGKSFIAYTLGFLKLLEPNVKVLVVAPNYSLANIGWSQIRGLIKKYGLQTERENAKDKEIELANGSLFKLASAAQADSAVGRSYDFIIFDEAAISDVGGDAFRVQLRPTLDKPNSKALFISTPRGGNWFKEFYAYGFDDTLPNWVSIHGTYRDNPRADLNDIEEARRTVSKNYFRQEYEADFSVFEGQIFDTFNAIDHVKDLKGMRHFFKDDEAFETLLGIDVGYRDPTAVLTIKYHYDTDTYYVLEEYQQAEKTTAQHAAYIQHCIDRYKVDRIFVDSAAAQFRQDLAYEHEIASAPAKKSVLDGLACLQALFQQGKIIVDASCSSLIHALQNYKWDFQEGEEKLSREKPRHDANSHLCDALRYGIYSISRGK", "text": "FUNCTION: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer. Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. SIMILARITY: Belongs to the Tequatrovirus large terminase family."}
{"protein": "MEVKIFRVKGTFEKGGKKFRFTKEYRALKPEDVRELVFSDIGSKHRVKRAKIFIESIEEIEPVEAENLVVKRLSLELA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL20 family."}
{"protein": "MDSVNSFKGYGKVDEAQDLALKKKTRKRLLLLSISVVVLIAVIIAAVVATVVHKNKNESTPSPPPELTPSTSLKAICSVTRFPESCISSISKLPSSNTTDPETLFKLSLKVIIDELDSISDLPEKLSKETEDERIKSALRVCGDLIEDALDRLNDTVSAIDDEEKKKTLSSSKIEDLKTWLSATVTDHETCFDSLDELKQNKTEYANSTITQNLKSAMSRSTEFTSNSLAIVSKILSALSDLGIPIHRRRRLMSHHHQQSVDFEKWARRRLLQTAGLKPDVTVAGDGTGDVLTVNEAVAKVPKKSLKMFVIYVKSGTYVENVVMDKSKWNVMIYGDGKGKTIISGSKNFVDGTPTYETATFAIQGKGFIMKDIGIINTAGAAKHQAVAFRSGSDFSVYYQCSFDGFQDTLYPHSNRQFYRDCDVTGTIDFIFGSAAVVFQGCKIMPRQPLSNQFNTITAQGKKDPNQSSGMSIQRCTISANGNVIAPTYLGRPWKEFSTTVIMETVIGAVVRPSGWMSWVSGVDPPASIVYGEYKNTGPGSDVTQRVKWAGYKPVMSDAEAAKFTVATLLHGADWIPATGVINQLS", "text": "FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin (By similarity). Demethylates protein phosphatase 2A (PP2A) that have been reversibly carboxymethylated by LCMT1. Acts as negative regulators of genes involved in salt stress response (PubMed:28741704). SUBCELLULAR LOCATION: Secreted, cell wall Golgi apparatus membrane Note=Cleaved in the Golgi apparatus by SBT6.1 (S1P) after the Arg-Arg-Leu-Met (RRLM) and Arg-Arg-Leu-Leu (RRLL) motifs. This processing is required for extracellular targeting. SIMILARITY: In the C-terminal section; belongs to the pectinesterase family. SIMILARITY: In the N-terminal section; belongs to the PMEI family."}
{"protein": "MVYRKPPDGGWGWVIVIVSFFTQFLCYGSPLAVGVLYLEWLDAFGEGKGKTAWVGSLANGIGLLASPVCSICVSSFGARPVAIFSGFMVAGGLMMSSFAPNIYFLYLSYGIVVGLGCGLLYNATVTITCQYFDKRRGLALGLISTGSSVGLFIYAALQRELIELYGLDGCLLIVGALSLNILACGSLMRPLESSDSPSPEKACTDKVPDQYFVYHEKEKTVEENISILEKGYIDEKCANNVPDYKQDNILNKNVLSSINVDEKDTYKKKVVEQTNFCKQLAKRKWQLYLNYWEETVVLFKNRVFSALFFAILLFDIGGFPPSLLMEDIARSANINEEDYHMPLVSIIGIMTAIGKLILGILADFKWVNTLYLYVLTLLMMGAALLAIPFARSYFTLAVLSGILGFLTGNWSIFPYVTTKTVGIEKLTHAYGILMFFAGLGNSLGPPIVGWFYDWTQEYDTAFYFSGFCVLLGGFLLLLAALPCWNACTDRSSKLPPNTYSYKVASSA", "text": "FUNCTION: Extracellular pH-and Na(+)-sensitive low-affinity creatine transporter. Functions also as a pH-independent carnitine efflux transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
{"protein": "MDEESLAAALQTYRAQLEQVDLTLRAVTDPTQLEDLTQLHTDLQQLIELTESSLLSIQKCNLLTSLEGNPSLPFHEDPISLPALEVPTSLSSQDKEYEAFRMAISEESQPLGSNDETSTCSKGSEEEEEEEEEEEDNTSGMKVKAPYYSTWGTLEYHNAMVVGSEQMEDGEAGVRVLYLYPTHKAMKPCPFFLDGKCLFNDNCRFSHGQVVSVTELQPFKEADLGSLAVDSPCLAQHNDGIWYPARITDIESGFYTVKFDSLLLKESVLEADSIIPPLRGSDSSSSSSSDEEEDGAAEDSVYAKVLGQEIAGTTCSSEFGGWEAHTRGIGSKLLVRMGYEFGKGLGRNAEGRVEPIQAVVLPKGKSLDQCMEIQQRKKAGGKHKHKTSKRRPKASGQGGGAKARDIFDFLNEKLEGKFTSACTAETQKTGEKKGKELYNASKDSKRALSVQVAITAEKIKQKQREICHLKESLARNAGRESVISNQLEVRLSGARKELAGLQQEERSLQREQKKADTHKKMTEF", "text": "FUNCTION: Transcription repressor that specifically binds the 5'- GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. Negatively regulates expression of EGFR, a gene involved in cell proliferation, survival and migration (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "GAVYLYNIGNLQCPNAVLQHMSIPQFLGEGTPVVFVRKSESDYGDVVRVMTVVYIKFFVKTTKLCVDQTVWKVNDEQLVVTGGKVGNENDIFKIMKTDLVTPGGSKYVYKLLHCPSHLGCKNIAGNFKNGYPRLVTVDDDKDFIPFVFIKA", "text": "FUNCTION: Inhibitor of cysteine proteases. May protect the plant by inhibiting proteases of invading organisms. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family."}
{"protein": "MAYLKVSGTKIVDKDGNEVILRGAGLGGWMNMENFITGYPGCEFQIRAALADVVGQEKSEFFFDKFLEYFFTDADAAFFKSLGLNCIRLPFNYRHFEDDMNPRVLKPEGFKHLDRVIDICAKHGIYTVLDLHTAPGGQNTDWHSDAGTHIAKFWEHKDFQDRVIWLWEELAQHYRDNTWIAGYNPLNEPTDPYQTRLIAWYDRVYAAIRKHDPHHALFLDGNTFASDFSHFGDAEKRWENTAYAIHDYSVFGFPAAPEPYVSSEAQRRRLRRSYEKKREWMDARGLCVWNGEFGPVYARREYEGDLTDSINEERYRVLKDQLEIYNKDRLSWSIWLYKDIGFQGMVHVSRDTPYMTLFRDFLAKKHRLAIDAWGADDSAVRHVYQPLIDLIKQEVKPEHQELYPAPVWKLSDRVGRLARNILVSEFLVREWAEHFRGKSTEELDAIAKSFAFENCLHRDGLNKVLTDNASLVAQGA", "text": "FUNCTION: Catalyzes the hydrolysis of xylo-oligomers to xylose units and plays an important role in xylan degradation. Can also perform the transglycosylation of xylose and alcohol. Has no endoglucanase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MGGTALNEIVKKVKIAEDVFDFWIHSPSVSKEARPGQFVVIRLHEKGERIPLTVADTKPEEGLFRMVVKVVGKTTHELSLKKEGDTILDVVGPLGNPSEIENYGNVLLVGGGVGIATLYPIAKALKEAGNNITTVLGARTKDYLIMVDEFKEISDVLLVTDDGSAGMKGVVTDAMDKLFRERKFDICWAVGPTIMMKFCTLKAREFGVPIWVSLNPIMVDGTGMCGACRVTVSGQIKFACVDGPEFRGEEVDWDELLKRLAQYREQEKISYERFLKTAGESE", "text": "SIMILARITY: Belongs to the PyrK family."}
{"protein": "MTMAANLLEDWCRGMEADIHRSLLVTGIPEDCGQAEIEETLNGVLSPLGPYSVLNKIFLRQENAKAALVEVGEGVNLRAIPREFPGRGGIWRVVCRDPTQDAEFLKNLNEFLDAEERTLEDVVHLLELSRASPPKTQNRSTENWAEALGVLLGAVVQIIYYMDAEMLSQEEARAQDLAKAQAVASLASAAGRKVKKEPGRAAERGSALKMENPDGWNDVADGGDGPKPLVRKAGALTHSRRKRQKKTPKQEPVPWKKSQGSHSHSSASLKHPEADDGKNRERLEHVRNNKKPCVKQEGSALKKAPVKCAWKFPSNLPHVAASRGVASESDQDGGLEGPPKKKAMGWVSAKSPAYMRKKKVSLGPVSYVLVNSEDPRKKPGVSKKGPGSGQDAPDQKAPGVPQAHESPTSASQGPEAKPQSPLHASSGENDGRSHLGCVNKWMEGEEQQGKAGAQEPKWAESQMVGEDPSAV", "text": "SIMILARITY: Belongs to the PNMA family."}
{"protein": "MYILEISLKFTPMPVSVQRKEAEAAQAAYQQVVEALRSGQPSVLELHCEFQAEKKLAVLTSGIASVQLYEKSGGSATVKRPGFAVIGE", "text": "SIMILARITY: Belongs to the UPF0367 family."}
{"protein": "MESQWRGAAATAFHQHWLARLLLWVSTLSCSFSLPASLPPSLVPRVRSSYTMGKTFLGLDKCNACIGTSICKKFFKEEIRFDNSLASHLGLPPQDLHSYAANYSDDSKTWRPVEISQLVSRYQIEISDRRICASVSAPKTCSIERILQKTGRFQKWLQAKRLTPDLVQGLPSPFLRCPSQRLLDRVVRRYAEVVDAGSIFMDHFTAGDKLRLLYTLAVNAHPIILQIFPGAEGWPMPRYLGSCGRFLVSTSTRPLQEFYDASPEQAADLAYQLLRVLESLRSNDLNYFFYFTHVDAGMFGIFDNGHLFIRDASALGIIDKQEGSQAAARTGENEDIFSCLVSDCQIQLSSCDTVPEKQSLVLVCQQLLPQLLQGKFPSPVQKEIDSALSLCSKDNSTDLEVLGATSWLKDILRSLRTCDPRFAYRYPDCKYNDRF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DIPK family."}
{"protein": "MGRKFFVGGNWKCNGTTDQVEKIVKTLNEGQVPPSDVVEVVVSPPYVFLPVVKSQLRQEFHVAAQNCWVKKGGAFTGEVSAEMLVNLGVPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQREAGSTMDVVAAQTKAIAEKIKDWSNVVVAYEPVWAIGTGKVATPAQAQEVHASLRDWLKTNASPEVAESTRIIYGGSVTAANCKELAAQPDVDGFLVGGASLKPEFIDIINAATVKSA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family."}
{"protein": "MCSTCANVLKYYDWDPHFKLVINPNNFLSVGFCSNPLMCCYPELLPEFGTVWDCDRSPLEIYLESILGDDEWASTFDAVDPVVPPMHWGAAGKIFQPHPGVLMHHLIGKVAAGWDPDLPLIRLEADDGSITAPEQGTMVGGVIAEPSAQMSTAADMATGKSVDSEWEAFFSFHTSVNWSTSETQGKILFKQSLGPLLNPYLEHLAKLYVAWSGSIEVRFSISGSGVFGGKLAAIVVPPGVDPVQSTSMLQYPHVLFDARQVEPVIFCLPDLRSTLYHLMSDTDTTSLVIMVYNDLINPYANDANSSGCIVTVETKPGPDFKFHLLKPPGSMLTHGSIPSDLIPKTSSLWIGNRYWSDITDFVIRPFVFQANRHFDFNQETAGWSTPRFRPISVTITEQNGAKLGIGVATDYIVPGIPDGWPDTTIPGELIPAGDYAITNGTGNDITTATGYDTADIIKNNTNFRGMYICGSLQRAWGDKKISNTAFITTATLDGDNNNKINPCNTIDQSKIVVFQDNHVGKKAQTSDDTLALLGYTGIGEQAIGSDRDRVVRISTLPETGARGGNHPIFYKNSIKLGYVIRSIDVFNSQILHTSRQLSLNHYLLPPDSFAVYRIIDSNGSWFDIGIDSDGFSFVGVSGFGKLEFPLSASYMGIQLAKIRLASNIRSPMTKL", "text": "FUNCTION: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm. SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the caliciviridae capsid protein family."}
{"protein": "NPDCLLPIKTGPCKGSFPRYAYDSSEDKCVEFIYGGCQANANNFETIEECEAACL", "text": "FUNCTION: This cocoon shell-associated protein inhibits trypsin Activity by forming a low-dissociation complex with trypsin. May play an important part in regulating proteolytic activity in the silk gland or protecting silk proteins from degradation during histolysis."}
{"protein": "MSMELTVLGPLAGRSFAIAGKPKLLLLRPTNLPLLRLSLPLSLPNFSSSSRFNSPIVFAAQESNLSVSNENETSEWLMQDFYTLRKDVEIASARVEEIRASANLQQLEQEITNLESKATDTSFWDDRTKAQETLSSLNDLKDRMRLLSEFKTMVEDAETIVKLTEEMDSTDVSLLEEAMGIIKELNKSLDKFELTQLLSGPYDKEGAVVYITAGAGGTDAQDWADMLLRMYMRWGEKQRYKTKVVEMSNGEEAGIKSATLEIEGRYAYGYISGEKGTHRIVRQSPFNSKGLRQTSFSGVEVMPLLPEEAVGIEIPEEDLDISFTRAGGKGGQNVNKVETAVRITHIPTGVAVRCTEERSQLANKTRALIRLKAKLMVIAEEQRATEIKEIRGDAVKAEWGQQIRNYVFHPYKLVKDVRTGHETSDITSVMDGDLDPFIKAYLKHKYTLAMASAVTN", "text": "FUNCTION: Directs the termination of translation in response to the peptide chain termination codon UGA. Required for the proper translation, stability and normal processing of UGA-containing polycistronic transcripts in chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
{"protein": "YGPNELPAEEGKNAESAIEALKEYEPEMGKEIVPGDLVEISVGDKIPADLRIDQSILTGESVSVIKNILFSGTNVAAGKTQMAETEEIKTPLQQKVGEATETALIVLGEKEFTLEFSRVIVITGDNKKAEIGIAMGSGTAVAK", "text": "FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Sarcoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily."}
{"protein": "MYLIYLRLVFCCALLLGCGDNSKFDSATDLPVEQEQEQETEQEGEPEESSEQDLVEEVDWKDIPVPADAGPNMKWEFQEISDNFEYEAPADNKGSEFLEKWDDFYHNAWAGPGLTEWKRDRSYVADGELKMWATRKPGSDKINMGCITSKTRVVYPVYIEARAKVMNSTLASDVWLLSADDTQEIDILEAYGADYSESAGKDHSYFSKKVHISHHVFIRDPFQDYQPKDAGSWFEDGTVWNKEFHRFGVYWRDPWHLEYYIDGVLVRTVSGKDIIDPKHFTNTTDPGNTEIDTRTGLNKEMDIIINTEDQTWRSSPASGLQSNTYTPTDNELSNIENNTFGVDWIRIYKPVEK", "text": "FUNCTION: Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. Also tolerant to hybrid substrates containing C6-sulfate groups at the -4, +1, and +3 positions. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 16 family."}
{"protein": "MDPDKEDKTLELMCSLPRSVWLGCSSVAESLCALRCLQSLPSSRAHNQNMTGMESQINTDEVSPKKTTVFKLGNGSLAGSRKRPSQGSFDKEKDLCIQLFDQWSESDQVEFVEHLIARMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSFLDARSLCSAELVCREWQRVISDGMLWKKLIERMVRTDPLWKGLSERHQWEKYLFKNRTNEVPPNSYYHSLYPKIIQDIETIEANWRCGRHNLQRIQCRSENSKGVYCLQYDDDKIISGLRDNSIKIWDKQSLECLKVLTGHTGSVLCLQYDERVIVTGSSDSTVRVWDVSSGEVLNTLIHHNEAVLHLRFCNGLMVTCSKDRSIAVWDMASATDISLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWSTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLQAALDPRAPASTLCLRTLVEHSGRVFRLQFDEFQIISSSHDDTILIWDFLNVSSNGQSDGRSPSRTYTYVSR", "text": "FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Probably recognizes and binds to phosphorylated target proteins: the interaction with substrates requires the phosphorylation of the two serine residues in the substrates' destruction motif D-S-G-X(2,3,4)-S (By similarity). SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling regulation (By similarity). Participates in Wnt signaling regulation, and plays a role in eye and jaw development (PubMed:31402090). SCF(FBXW11) plays a key role in NF- kappa-B activation by mediating ubiquitination of phosphorylated NFKBIA, leading to its degradation by the proteasome, thereby allowing the associated NF-kappa-B complex to translocate into the nucleus and to activate transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MQFAPLLLGVFLLCGSARGSDSSASNAITCFTRGLDLRKETEDVLCPANCPLWQFYVFGDGIYASLSSVCGAAIHRGVITNAGGAVRVQTLPGQENYPAVHANGIQSQVLSRWASSFSVTPGTNNLALEAVGRSVATARPATGKRPKKTLEKKAGNKDCKADIAFLIDGSYNIGQRRFNLQKNFVGKVAVMLGIGTEGPHVGVVQASEHPKIEFYLKNFTAAKEVLFAIKELGFRGGNSNTGKALKHAAQKFFSMENGARKGIPKIIVVFLDGWPSDDLEEAGIVAREFGVNVFIVSVAKPTTEELGMVQDIGFIDKAVCRNNGFFSYQMPSWFGTTKYVKPLVQKLCSHEQMLCSKTCYNSVNIGFLIDGSSSVGESNFRLMLEFISNVAKAFEISDIGSKIATVQFTYDQRTEFSFTDYTTKEKVLSAIRNIRYMSGGTATGDAISFTTRNVFGPVKDGANKNFLVILTDGQSYDDVRGPAVAAQKAGITVFSVGVAWAPLDDLKDMASEPRESHTFFTREFTGLEQMVPDVIRGICKDFLDSKQ", "text": "FUNCTION: Plays a role in the control of cell shape and motility in the trabecular meshwork. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MYSYEDRLRAVRLYLKLGRRMSATLRQLGYPTKNSLKAWLAEFERNQDLRRGYQRIKRQYTDEQKQRAVDHYIEQGYCLSHTIRSLGYPSREALRAWIRDLRPEFARTVVGSSAPTVARSRLEKQQAVIALNLRVGSAKDVADTVGVSRPTLYNWQHRLLGKVPLKPMTKKKGDTSLEQRHEALLRELAELESQNQRLRMENAILEKASELIKKDMGINPLELTSREKTKVVDALRVTFPLANLLCGLKLARSTYFYQRLRQTRPDKYTQVREVIRTIFEDNYRCYGYRRIDSALRLGGMRVSEKVVRRLMAQERLVVRTPRRRRFSAYAGDPTPAVPNLLNRDFHASAPNTKWLTDLTEIHIPAGKVYVSPIVDCFDGLVVAWNIGTSPDANLVNTMLDHAVRTLRPGEHPVIHSDRGSHYRWPAWIRRTENAQLTRSMSKKGCSPDNAACEGFFGRLKTELIYPRNWQHVTLKDLMTRIDAYIHWYNERRIKVSLGGRSPIEYRHAVGLMSV", "text": "FUNCTION: Probably involved in the transposition of insertion sequence IS1353. SIMILARITY: Belongs to the transposase 8 family."}
{"protein": "MAKFHAPVIQDNPSGWGPCAVPEKFKDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDEASFQLVDTAKTQKTAYQRNRMRFAQRNLRRDKDRRTLTQFNMQTLPKSAKQKERDRMRLQKKFQKQFGVRQKWDQKSQAQLKPRDSSVEVRSDWEVKEEMDFPRLMKMRYMDVADPLDIECCGALEHYDKAFDRITTRNEKPLKSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMCCTRSVNSWDIIVQRVGNKLFFDKRDNSDFDLLTVSETANEPPQDEGSSLNSPRNLAMEATYINHNFSQQCLRMGGERYKFPNPNPFVEEDTEKSEVASVAYRYRRWKLGEDIDLIVRCEHDGVMTGANGEVSFINVKTLNEWDSRYCNGVDWRQKLDSQRGAVLATELKNNSYKLARWTCCAILAGSEYLKLGYVSRYHVKDSSRHVVLGTQQFKPNEFASQINLSMENAWGILRCVIDICRKLEEGKYLILKDPNKQVIRVYSLPDGTFSSDEDEEEDDEDEEDEEEDEDN", "text": "FUNCTION: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7- methylguanosine cap of a subset of mRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit D family."}
{"protein": "LLKELWTKIKGAGKAVLGKIKGLL", "text": "FUNCTION: Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria. Is inactive against yeast, erythrocytes, and insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ponericin-L family."}
{"protein": "MAHTHLGRAVKNIEAPRPLKTQSRSSLKNSYLVIEELIQLIDNVTVGLQSCNTTPESITLLLHNLRVHGPQLEAVSKDTLDRAFVVFRNASQDERLNITTRLKLLELIELRAKSWDNDDTIAYYKSKQQISNVELPSEYQYDAGVQPGAFSTSPTFGVSGGVGGVNDGAAAAAAAVFNAASAAAAAQAAAIAAVGTSNQQHMLLPPGEVIRNSGKFPKPTKIPGKTYCKDEVVIRNADSGKVMGIKGRRVHMIEELSETIISFQRVNPGAKERLVQITGPAEDKINYAKQLMEDTIRRNASPVRLEPAPAVGGSCSSLNSSNSDDAIVQPRTPTGSSLANRLSFNSAQNFMTATAAAQQISQQMHHQTHHLQHQQQQQVAAVAAAAAAAAHAQATAAAGKVLRPNQQLLMHSYSTNDASVGEYKFTVNVGQHLIKITGDCCELVRVAKLVLDDYFSSSEFLASIEAGAAFDGTSLVTTPSTPLPGAGPPQFWLPGTDSGIGLNCVVSSSANNNGEGDDEVFAEPSNGGSSTSNQNGLARSRRSHFSRKESTPETKGAREKGDLDDLAGTNSLKSNASRVSYDIEHLLYYSMSPHSWTLPTDWQKMQETAPSILRNKDLQDESQRFDGDKYLASIKTAAKRDIVAADEVETLDE", "text": "FUNCTION: Plays a role in promoting translation. SUBCELLULAR LOCATION: Cytoplasm Note=In germ line cells, predominantly cytoplasmic and accumulates in the perinuclear nuage during oogenesis but disappears from there around stage 8."}
{"protein": "MALNDCFLLNLEVDHFMHCNISSHSADLPVNDDWSHPGILYVIPAVYGVIILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLITCAPVDASRYLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASHALMKICLKAAFIWIISMLLAIPEAVFSDLHPFHEESTNQTFISCAPYPHSNELHPKIHSMASFLVFYVIPLSIISVYYYFIAKNLIQSAYNLPVEGNIHVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLHFVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLIIRSHSTGRSTTCMTSLKSTNPSVATFSLINGNICHERYV", "text": "FUNCTION: Receptor for gastrin-releasing peptide (GRP) (PubMed:1655761). Signals via association with G proteins that activate a phosphatidylinositol-calcium second messenger system, resulting in Akt phosphorylation. Contributes to the regulation of food intake. Contributes to the perception of prurient stimuli and transmission of itch signals in the spinal cord that promote scratching behavior, but does not play a role in the perception of pain. Contributes primarily to nonhistaminergic itch sensation. In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to contribute to disinhibition of glutamatergic cells in the auditory cortex via signaling on vasoactive intestinal peptide- expressing cells which leads to enhanced auditory fear memories (By similarity). Contributes to the induction of sighing through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MLPSQTPAQGSGRFLLLSPPSLSSHPEKLNAILGLHARESTDLQMLDRLALGLVSLPQSTYDVVLLLTGADNTLAETYRLVSRGVLQGVVNSLKPGGKLRNRDNQIWGSGSDSAAGLGSSDGGGGGGGGEKKSSSEQAFRNEAILAGLVFDDRGELAKPDFGAQQAVPLKLGRKKNLGDSAFGNGTVELPASNGVRVTAGATTTTPTTTTTTTINSSTPSGVRFIDFSDDFGVPMVEETQELDEELIDEEELLGEFDMGRPIVQPPECRPKAGKRRRACKDCTCGLSQKLEAEDRAKRANADKALETLKLGTNDLAEVDFTVQGKVGSCGNCALGDAFRCDGCPYIGLPAFKPGEEVRLLNNDVQL", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space. SIMILARITY: Belongs to the anamorsin family."}
{"protein": "MKLTLKNLSMAIMMSTIVMGSSAMAADSNEKIVIAHRGASGYLPEHTLPAKAMAYAQGADYLEQDLVMTKDDNLVVLHDHYLDRVTDVADRFPDRARKDGRYYAIDFTLDEIKSLKFTEGFDIENGKKVQTYPGRFPMGKSDFRVHTFEEEIEFVQGLNHSTGKNIGIYPEIKAPWFHHQEGKDIAAKTLEVLKKYGYTGKDDKVYLQCFDADELKRIKNELEPKMGMELNLVQLIAYTDWNETQQKQPDGSWVNYNYDWMFKPGAMKQVAEYADGIGPDYHMLIEETSQPGNIKLTGMVQDAQQNKLVVHPYTVRSDKLPEYTPDVNQLYDALYNKAGVNGLFTDFPDKAVKFLNKE", "text": "FUNCTION: Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
{"protein": "RGLPSRSVFLRGCQASLSTAQERLGHPGVPTREGVRVATRSPRPYHEIPSPGDNGWLNLYHLAEEKGTHRVHYRHVQNFQKYGPIYRENLGNVESVYIMDPEDVALLFNSEGPQPERFLIPPWVAYHEYYRRPVGVLLKKAQGWKRDRVALNQEVMAPDAIKNFVPLLEAVSQAFVRMLHGRVQQGVFSGDISDDLFRFAFESMTNIMFGERLGMLEETVDPEAHEFIDAVYQMFHTSVPMLSLPPSLFRLFRTRTWRDHVAAWDVIFTNADKYTQSFYWDLRQKQDLGGSYRGILYSLLGTSKLSFEDIKANVTEMLAGSVDTTSMTLQWHLYEMGAALGMQEMLRAEVLAARRQAQGDMTAMLQSVPLLKASIKETLRLHPISVTLQRYLVNDLVLQDYMIPAKTLVQVANYGMGREPSFFANPEKFDPPRWLDKDKNATHFR", "text": "FUNCTION: A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R- hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron- sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein Note=Localizes to the matrix side of the mitochondrion inner membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MGSLSTLNLIKTCVTLASSEKLNQPSQCYTISTCMKSSNNPPFNYYQINGRKKMSTAIDSSVNAPPEQKYNSTALEHDTEIIEIEDHIECIRRLLRTAGDGRISVSPYDTAWIALIKDLDGHDSPQFPSSMEWVADNQLPDGSWGDEHFVCVYDRLVNTIACVVALRSWNVHAHKCEKGIKYIKENVHKLEDANEEHMTCGFEVVFPALLQRAQSMGIKGIPYNAPVIEEIYNSREKKLKRIPMEVVHKVATSLLFSLEGLENLEWEKLLKLQSPDGSFLTSPSSTAFAFIHTKDRKCFNFINNIVHTFKGGAPHTYPVDIFGRLWAVDRLQRLGISRFFESEIAEFLSHVHRFWSDEAGVFSGRESVFCDIDDTSMGLRLLRMHGYHVDPNVLKNFKQSDKFSCYGGQMMECSSPIYNLYRASQLQFPGEEILEEANKFAYKFLQEKLESNQILDKWLISNHLSDEIKVGLEMPWYATLPRVETSYYIHHYGGGDDVWIGKTLYRMPEISNDTYRELARLDFRRCQAQHQLEWIYMQRWYESCRMQEFGISRKEVLRAYFLASGTIFEVERAKERVAWARSQIISHMIKSFFNKETTSSDQKQALLTELLFGNISASETEKRELDGVVVATLRQFLEGFDIGTRHQVKAAWDVWLRKVEQGEAHGGADAELCTTTLNTCANQHLSSHPDYNTLSKLTNKICHKLSQIQHQKEMKGGIKAKCSINNKEVDIEMQWLVKLVLEKSGLNRKAKQAFLSIAKTYYYRAYYADQTMDAHIFKVLFEPVV", "text": "FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase that produces (+)-copalyl diphosphate ((+)-CPP) from geranylgeranyl diphosphate (GGPP) (PubMed:24990389). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MPLLLLSALLPFSLMAGPTPSTGKELSAASFLQDILQRYGENESLSMPQLQSLLENLEVGKGGGNQRNMSQCLSSSTLFAAHNLTSGSVVDAEGFQSFCPTILQQLETRACQESPAFQNETTPGAEGRPSPGEVWGYGFLCVTVISLCSLFGAGVVPFMKKACYKRLLLFCIALAIGTLFSNALFQLIPEAFGFNPLEDSYVFTSSVIFGGFYLFFFTEKVLKMMLKQKHEHGHSHYSADTSKRDAEEGVTEKLQNGDLDHMIPPPHGSESDLRGDEKAVQQQDLPGQQSSCYWLKGIRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGVSTSIAILCEEFPHELGDFVILLNAGMSIPQALFFNFLSACCCYLGLAFGILAGSHFSSNWIFALAGGMFLYIALSDMFPEMNEVSKEDEEGGRAFSAFMIQNAGLLTGFAIMLLLTTFSGQIQLG", "text": "FUNCTION: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (By similarity). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions. Beside these endogenous cellular substrates, can also import cadmium a non- essential metal which is cytotoxic and carcinogenic (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MQRRHFIARAGIAAATAALGLAAMPAQAQADKFPQRPIRLVIGYTAGGSTDIPFRVLADNASKILGQPVIVENKPGAGGVLPAQMMQSTAPDGYTLAQVAMPVYRLPYTTKINWDPVKDLNYIINLAGYSFGLVVPADSPIKTMQEYIAYAKANPGKLTYGSPGSMTTLHLTMEELAMKQGVQFSHIPYKGNSESMQALLGGHVMSVADTPAWAPYVEQGKLRLLSTWGEKRSARFPSVPTLKELGIGIVQTSPFGLVAPKGTDPKIVQKLHDAFKKAMDMPNYRESLAKFDMEPYYMNSQQYAQFAAETVKKEKAIIEKLGLAKAQ", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0065 (bug) family."}
{"protein": "APQAGFYGVR", "text": "FUNCTION: Myoactive peptide. Stimulates the contraction of the oviduct and foregut. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MATPSQHDLRNDFRALLASSECYFTASVFDPMSARIAADLGFEVGILGGSVASLQVLAAPDFALITLSEFVEQATRIGRVTRLPVIADADHGYGNALNVMRTITELERAGVAALTIEDTLLPAQYGHKSTDLIPLDEGVGKMRAALEARIDPAMAIIARTNAGQLDDEAAVERVCAYQAAGVDAICLVGVRDFDHLERLAAPLDIPLMLVTYGNPELRDRARLAALGVRVVVNGHAAYFAAIKATYDCLREQRDIAASELNASQLATRYSTLDEYREWARDYMDVKE", "text": "FUNCTION: Catalyzes the decarboxylation of oxaloacetate into pyruvate. Seems to play a role in maintaining cellular concentrations of bicarbonate and pyruvate. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Oxaloacetate decarboxylase family."}
{"protein": "MSVFPESFLWGGALAANQSEGAFREGDKGLTTVDMIPHGEHRMAVKLGLEKRFQLRDDEFYPSHEATDFYHRYKEDIALMAEMGFKVFRTSIAWSRLFPQGDEITPNQQGIAFYRSVFEECKKYGIEPLVTLCHFDVPMHLVTEYGSWRNRKLVEFFSRYARTCFEAFDGLVKYWLTFNEINIMLHSPFSGAGLVFEEGENQDQVKYQAAHHQLVASALATKIAHEVNPQNQVGCMLAGGNFYPYSCKPEDVWAALEKDRENLFFIDVQARGTYPAYSARVFREKGVTINKAPGDDEILKNTVDFVSFSYYASRCASAEMNANNSSAANVVKSLRNPYLQVSDWGWGIDPLGLRITMNMMYDRYQKPLFLVENGLGAKDEFAANGEINDDYRISYLREHIRAMGEAIADGIPLMGYTTWGCIDLVSASTGEMSKRYGFVFVDRDDAGNGTLTRTRKKSFWWYKKVIASNGEDLE", "text": "FUNCTION: Can hydrolyze salicin, cellobiose, and probably arbutin. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MDHVKLVNDPIDIAHIHQLLADEGCGASSVFVGTTRDNFQGKKVLSLAYEAYDSMALKEMNKICSDLRSKWLDLKHIVIYHRLGTVPVCEASVVIAASSPHRSEALESVSFAIDQLKTRVPIWKKEIYEGDNDGEWKENKESIRPKKSKSGFNYAACPCKVEESHDVPRTLVQIRVNDAELTKRLECFVNRKRDEINSQNVIDFKSSFVSSDKDLSDSCARTQSTIIKQEQSNCHLKVRRVNNRCGPQQMEMRPNYELELNKLMGSRDGQTDPIKEMRKSLPNSRLQAIESYMGLTTDNEENIFSRIKRVENRLLQLESISPEYRHFTKREPSSMEAAPPKKIRKKSYSAQELSAFIQKIKDGSEFS", "text": "FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated Mocs2A into precursor Z to generate a dithiolene group. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily."}
{"protein": "MFRQEQPLAEGSFAPMGSLQPDAGNSSWNGTEAPGGGTRATPYSLQVTLTLVCLAGLLMLFTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKVWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIVTVWVISAVISFPPLISIEKKGAGGGQQPAEPSCKINDQKWYVISSSIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDACSAPPGGADRRPNGLGPERGAGPTGAEAEPLPTQLNGAPGEPAPAGPRDGDALDLEESSSSEHAERPPGPRRPDRGPRAKGKTRASQVKPGDSLPRRGPGAAGPGASGSGHGEERGGGAKASRWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLIAVGCPVPSQLFNFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDRKRIV", "text": "FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2A sub-subfamily."}
{"protein": "MLRTIVVFAPIIAALAWVIFNIQKPAREQFNRDFLGKD", "text": "FUNCTION: Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbY family."}
{"protein": "MLDVDNLDLENLLKKYYEKTNEKIVFVNKDGKVIAMNDAAEEIISKDNNYSAMTNAICNRCEGYSNEFALQSCINCYLDTTKPNDMNFQVFMKTVDNKIQPFTASYQCIDDEAQIYAFTLQDISPQIERQEKMYQRQMLRKTIAAQENERKRISRELHDSVVQEMLNVDVELRLLKYQQDMAQLIEKSEHIELLMSNLINDIRDLSVELRPSSLDDLGLEAAFKSYFKQLEYNYGLNVVYQSNIQTIRFDSEIETVVYRVVQEAIFNALKYAGVYEVEVTIQQTEEGLIAEIIDRGKGFDPNLKPQGTGLGLYGMNERAELVKGTVNIETHIGKGTIITLEVPV", "text": "FUNCTION: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAGSVAIVGIFVALLAVAGEAAVFTVVNQCPFTVWAASVPVGGGRQLNRGESWRITAPAGTTAARIWARTGCKFDASGRGSCRTGDCGGVLQCTGYGRAPNTLAEYALKQFNNLDFFDISLIDGFNVPMSFLPDGGSGCSRGPRCAVDVNARCPAELRQDGVCNNACPVFKKDEYCCVGSAANDCHPTNYSRYFKGQCPDAYSYPKDDATSTFTCPAGTNYKVVFCP", "text": "FUNCTION: Has antifungal activity. Inhibits Candida albicans and Trichoderma reesei; marginal inhibition observed against Alternaria solani and Neurospora crassa. SIMILARITY: Belongs to the thaumatin family."}
{"protein": "MNLIINDKTASSSVGQTIGKAARLNHAHVGYVCGGHGLCQACYITVQEGADCLAPLTDVEKAFLSPRQIAAGGRIACQATIAKEGTVKVLSRPEEVRRMVFSNPFQLIGYAADMGKDTAQQIVPGVQNLIGRIQRGEMGGKDALGDMIESIQGAAGLVVEAIQQGPMALPIPFKEQIADLISKLPLPQIQLPSISLPQLPSISFPQLPFSLPKLPFSLPFLPQQPQATASLEKVTITVQPPAKD", "text": "FUNCTION: Could play a direct role in the oxidation or reduction of the quenching species formed in the chlorosome. SUBCELLULAR LOCATION: Chlorosome."}
{"protein": "MNLSDVPLRPGSAELLPVRGVRALQAFDNRDWVAVEVPVALEFNGIAHAVMLATPTDLADFALGFALSEGILLGRNELYGVEEAYAPEGITLKLDVASAAFARLKARRRSMAGRTGCGLCGTESLAHVTRALPPLPEGPALSTRAVARGMRELASMQVLQKVTGAVHAAAWCSAEGEALLVREDVGRHNALDKLVGALARSSVPASTGFIAVTSRASFEMVQKTVAARVPLLAAVSASTSLATAIAEDAGLTLAGFVRGDDLVIYTHPWRLNGLPANA", "text": "FUNCTION: Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FdhD family."}
{"protein": "MEANFSIPQNGSEVVFYDSTTSRVICIFLVVVLSITFLLGVIGNGLVIYVAGFRMTHTVTTICYLNLALSDFSYMTSLPFQITSIVMNGEWLFGWFLCKFVHMIINVNLFLSIFLITFIAMDRCICVLHPVWAQNHRTVNLARKVILGSWILVLMLIFPHFFFLTTVKDESGKVHCICNFESWAATPEEQVNMSMTVSLISVTLSFIVGFSIPMIFIVICYGLMAAKIGRRGLVNSSRPLRVLTAVAFSFFVCWFPFQLIFLLGNIGNKETQNNIDAWVNPASTLASFNSCLNPILYVFLGQQFRERLIYSLSASLERALREDSALNSDKIRNLSSQT", "text": "FUNCTION: May have an olfactory function associated with the identification of pathogens or of pathogenic states. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MGPWGEPELLVWRPEAVASEPPVPVGLEVKLGALVLLLVLTLLCSLVPICVLRRPGANHEGSASRQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALAALHVTLQFPLQEFILAMGFFLVLVMEQITLAYKEQSGPSPLEETRALLGTVNGGPQHWHDGPGVPQASGAPATPSALRACVLVFSLALHSVFEGLAVGLQRDRARAMELCLALLLHKGILAVSLSLRLLQSHLRAQVVAGCGILFSCMTPLGIGLGAALAESAGPLHQLAQSVLEGMAAGTFLYITFLEILPQELASSEQRILKVILLLAGFALLTGLLFIQI", "text": "FUNCTION: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space (PubMed:11301334, PubMed:12888280, PubMed:16844077). Functions as the major importer of zinc from circulating blood plasma into prostate cells (PubMed:12888280). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Shows a vesicular localization corresponding partially to the endoplasmic reticulum in several epithelial cell lines. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MARYDARLRGIGKAHACSAFAGHDFEGRNIMKTPWKFLAQLASRRRSASVQENFIAPDTDPEVIESETENKSPLPFDKPTQASGTPDHDSAVDRGSMLSDQLESDPNPLQEMNLTADIQEPGTPARSETKQSDAAGKRLGPQSQTSANSQKKPEIRCRERSKNARAEGVAQSAVATNEAETVQTSSSGDPFFNEVAILDEEIKELRRLLAQKLYLQNAQLKKMLERFDAS", "text": "SIMILARITY: To R.meliloti RA0936 and y4aO."}
{"protein": "MQGKALQDFVIDKIDDLKGQDIIALDVQGKSSITDCMIICTGTSSRHVMSIADHVVQESRAAGLLPLGVEGENSADWIVVDLGDVIVHVMQEESRRLYELEKLWS", "text": "FUNCTION: Functions as a ribosomal silencing factor. Addition to isolated ribosomal subunits partially inhibits their association, preventing translation. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8, preventing association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. FUNCTION: Functions as a ribosomal silencing factor. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Note=Comigrates with the 50S ribosomal subunit in sucrose gradients, specifically with ribosomal protein uL14 (rplN). SIMILARITY: Belongs to the Iojap/RsfS family. SIMILARITY: Belongs to the Iojap/RsfS family."}
{"protein": "MKSFTFLILFLFAAQSISVYAGSFHKDVKIHWGDGRGKIHDNQGKLLSLSLDKSSGSGFQSNQEFLYGKAEVQMKLVPGNSAGTVTTFYLKSPGTTWDEIDFEFLGNISGHPYTLHTNVYTKGSGDKEQQFHLWFDPTANFHTYCITWNPQRIIFTVDGIPIREFMNAESRGVPFPTKQPMRLYASLWEAEHWATRGGLEKTDWSKAPFTAYYRNYNVEGCVWVNGKSVCPANSQWFTQKLDSNGQTRMKGVQSKYMVYNYCSDKKRFPRGVPPECS", "text": "FUNCTION: Possesses xyloglucan endotransglucosylase (XET) activity in vitro. Does not possess xyloglucan endohydrolysis (XEH) activity (PubMed:20732879). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues (PubMed:23585673). Involved in cell proliferation in the tissue reunion process of wounded inflorescence stems. Maybe a downstream target of NAC071 as a consequence of auxin action in wounded stems (PubMed:25182467). SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2 subfamily."}
{"protein": "MSTNLLRLILLFITLSITSSLSTPSPADSPPYLWPLPAEFSFGNETLSVDPTVTLIVAGNGGGSLIIRAAFDRYMGIIFKHASGRGSLLSRIRFLKMVEYDITSLKIVVHSDSEELQLGVDESYTLMVSKKNEQSIVGAATIEANTVYGALRGLETFSQLCAFDYITKSVQIYKAPWYIQDKPRFGYRGLLIDTSRHYLPIDVIKQIIESMSFAKLNVLHWHIVDEQSFPLETPTYPNLWKGAYSRWERYTVEDASEIVRFAKMRGINVMAEVDVPGHAESWGTGYPDLWPSLSCREPLDVTKNFTFDVISGILADMRKIFPFELFHLGGDEVNTDCWKNTTHVKEWLQGRNFTTKDAYKYFVLRAQQIAISKNWTPVNWEETFSSFGKDLDPRTVIQNWLVSDICQKAVAKGFRCIFSNQGYWYLDHLDVPWEEVYNTEPLNGIEDPSLQKLVIGGEVCMWGETADTSVVLQTIWPRAAAAAERMWSTREAVSKGNITLTALPRLHYFRCLLNNRGVPAAPVDNFYARRPPLGPGSCYAQ", "text": "FUNCTION: Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2- acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2- acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4- methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU- GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D- glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and, to a lower extent, of leaves. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the glycosyl hydrolase 20 family."}
{"protein": "MRVMRVMRPRTLLLLLSGVLVLTETLAGSHSLRYFYTGVSRPGLGEPRFIAVGYVDDTQFVRFDSDAPNPREEPRVPWMEQEGPEYWDRNTRIYKDTAQIFRVDLNTLRGYYNQSETGSHNIQAMYGCDVGPDGRLLRGFWQFGYDGRDYIALNEELRSWTAADTAAQITKRKWEAAGAAETWRNYLEGECVEWLRRYLENGKDTLLRADPPKAHVTHHSISDREVTLRCWALGFYPEEISLTWQREGEDQTQDMELVETRPSGDGTFQKWAALVVPSGEEQRYTCRVQHEGLQEPLTLRWEPPQTSFLIMGIIVGLVLLVVALVAGAVIWRKKRSGEKGRIYTQAASSDSAQGSDVSLTVPKV", "text": "FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class I family."}
{"protein": "MNPVNATALYISASRLVLNYDPGDPKAFTEINRLLPYFRQSLSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYITQTTLARDIIEAVDCSSDILALLNDGSLFCEETEKPSDSSFTLCLTHSPLPSTSEPTADPQASLSPMSESTLSIAIGSSVINGLPTYNGLSIDRFGINIPSPEHPNTIDVCNTVDIKTEDLSDNLPPVCDTVATDLCSTGIDICSFSEDIKPGDSLLLSVEEVLRSLETVSNTEVCCPNLQPNLEATVSNGPFLQLSSQSLSHNVFMSTSPALHGLSCTAATPKVAKLNRKRSRSESDSEKVQPLPISTIIRGPTLGASAPVTVKRESKISLQPIATVPNGGTTPKISKTVLLSTKSMKKSHEHGSKKSHSKSKPGILKKDKAVKEKMPSHHFMPGSPTKTVYKKPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKKLEAFAVPEKALEQTRLTLGINVTSIAVRNASTSTSVINVTGSPVTTFLAASTHDDKSLDEAIDMRFDC", "text": "FUNCTION: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure (By similarity). Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histone H3 methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1 (By similarity). SIMILARITY: Belongs to the MSL2 family."}
{"protein": "MKSFFLVVTILALTLPFLGAEVQNQEQPTCFEKVERLLNEKTVKYFPIQFVQSRYPSYGINYYQHRLAVPINNQFIPYPNYAKPVAIRLHAQIPQCQALPNIDPPTVERRPRPRPSFIAIPPKKTQDKTVNPAINTVATVEPPVIPTAEPAVNTVVIAEASSEFITTSTPETTTVQITSTEI", "text": "FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kappa-casein family."}
{"protein": "MSVSVALKAKPIAYGAVACANYVNLSGAGSISVKYEDVALLDKQNKESNVSIQLNGSDSPVFGSKLALQTFSQVYPKLFIGENDRSLVESWVETASALAGNHNFLELSSLLAQLDDHLIMRSLFVGYSLTSADFSIWGALKSNNMAAGAVRTGQYFNLARWYKFMDSQNAVSVTMEEFTKAVNISKKQKSSGPNYEIGLPDAIDGKVVTRFPPEPSGYLHIGHAKAALLNQYFANKYHGKLIVRFDDTNPSKENSEFQDAILEDVALLGIKPDVVTYTSDYLDTIHQYCVDMIKSGQAYADDTDVETMRHERTEGIPSKHRDRPIEESLEILSEMDKGSDVGLKNCIRAKISYENPNKAMRDPVIYRCNLLPHHRTGTKYRAYPTYDFACPIVDSLEGVTHALRTTEYRDRNPLYQWMIKAMNLRKIHVWEFSRMNFVRTLLSKRKLTEIVDHGLVWGWDDPRFPTVRGVRRRGMTIEALQQYIVSQGPSKNILTLDWTSFWATNKKIIDPVAPRHTAVESGDVVKATIVNGPAAPYAEDRPRHKKNPELGNKKSIFANEILIEQADAQSFKQDEEVTLMDWGNAYVREINRDASGKVTSLKLELHLDGDFKKTEKKVTWLADTEDKTPVDLVDFDYLITKDKLEEGENYKDFLTPQTEFHSPVFADVGIKNLKKGDIIQVERKGYYIVDVPFDGTQAVLFNIPDGKTVNRYGVKN", "text": "FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily."}
{"protein": "MSSSENTLLDGKSENTIRFLTFNVNGIRTFFHYQPFSQMNQSLRSVFDFFRADIITFQELKTEKLSISKWGRVDGFYSFISIPQTRKGYSGVGCWIRIPEKNHPLYHALQVVKAEEGITGYLTIKNGKHSAISYRNDVNQGIGGYDSLDPDLDEKSALELDSEGRCVMVELACGIVIISVYCPANSNSSEEGEMFRLRFLKVLLRRVRNLDKIGKKIVLMGDVNVCRDLIDSADTLEQFSIPITDPMGGTKLEAQYRDKAIQFIINPDTPHRRIFNQILADSLLPDASKRGILIDTTRLIQTRNRLKMYTVWNMLKNLRPSNYGSRIDFILVSLKLERCIKAADILPDILGSDHCPVYSDLDILDDRIEPGTTQVPIPKFEARYKYNLRNHNVLEMFAKKDTNKESNKQKYCVSKVMNTKKNSNIKNKSLDSFFQKVNGEKDDRIKESSEIPQQAKKRISTPKLNFKDVFGKPPLCRHGEESMLKTSKTSANPGRKFWICKRSRGDSNNTESSCGFFQWV", "text": "FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family."}
{"protein": "MNNPIPSNLKSEAKKAAKILREFTEITSRNGPDKIIPAHVIAKAKGLAVLSVIKAGFLVTARGGSGIVLARLPDGKWSAPSAIGIAGLGGGFEIGIEVSDLVIILNYDRAVEAFAKGGNLTLGGNFTVAVGPLGRNLEGNVSLRSSAAVFTYCKSRGLFAGISLEGSCLIERKETNRKFYCQDIRAYDILFGDVPQPAQAEDLYEILNSFTEKYETEGQRINLKKVAREQRKAKELPPKPSSRPQPAHPPVQLNAGSQGNRNEYKLYPELSSYHEKTGNLNQPIEVTALYSFEGQQPGDLNFQAGDRIIVISKTDSNFDWWEGKLRGQTGIFPANYVTMN", "text": "SIMILARITY: Belongs to the SH3YL1 family."}
{"protein": "MAMFLKSRGVRSCRDRRLLSDEEEETSQSSSYTLGSQASQSIQEEDVSDTDESDYSDEDEEIDLEEEYPSDEDPSEGSDSDPSWHPSDSDESDYSESDEDEATPGSQASRSSRVSPSTQQSSGLTPTPSFSRPRTRAPPRPPAPAPVRGRASAPPRPPAPVPQSTKDKVPNRPTRPVLRGPAPRRPPPPSSPNTYNKHMMETTPPIKGNNNYNWPWL", "text": "FUNCTION: Histone-binding protein that binds to histones H2A/H2B, H3/H4 and cellular chromatin to overcome the host DNA damage response triggered by the viral genome ends. Interferes with histone ubiquitination and recruitment of repair proteins. SUBCELLULAR LOCATION: Virion tegument Host nucleus Host cytoplasm, host perinuclear region. SIMILARITY: Belongs to the lymphocryptovirus BKRF4 family."}
{"protein": "MSMVVYNNQEGEEGNPFAGALTEFSQWLWSRPLGNPGAEDAEEEAIAAQEELEFPEDEAQARHSCLQRTTSWATPKEVSPSGRVYQTVRHSRMEYSRPTMSIRSQASYFSSSARPLPPPPVPSLMSWTPIAKYHPSSPTSTSSKLRRAAPKLIKRG", "text": "FUNCTION: Together with movement protein P3a, facilitates long-distance movement of virions in host (Probable). Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (Probable). The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier (Probable). Binds ssRNA (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma Host chloroplast envelope Host Golgi apparatus Host mitochondrion outer membrane Note=Localizes to secondary branched plasmodesmata in source organs. Targeted to plasmodesmata in an actin- and endoplasmic reticulum-Golgi-dependent manner (By similarity). P3a directs P17 to the mitochondrial outer membrane while P17 regulates the localization of the P3a-P17 heterodimer to plastids (By similarity). SIMILARITY: Belongs to the polerovirus movement protein family."}
{"protein": "MRTSYLLLFILCLVLCDMDSGDTFLTGLGHRSDHYNCVKGGGQCLYSACPIYTKVQGTCYGGKAKCCK", "text": "FUNCTION: Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility. SUBCELLULAR LOCATION: Secreted Membrane Note=Associates with tumor cell membrane-derived microvesicles. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MPRIAIVGGSGVYDFPAENKREETVKTPYGEVKITVGVVGDEEVAFLARHGKGHSIPPHKINYRANIWALYELGVERIIATSAVGSMNPEMKPGDFVILDQIIDFTVSRPRTFYDGEESPHERKFVAHVDFTEPYCPEIRKALITAARNLGLPYHPRGTYVCTEGPRFETAAEIRAYRILGGDVVGMTQCPEAILARELEMCYATVAIVTNYAAGMSGKKLTHSEVVELMQKKSEDIVKLILAAIPLIPKERRCGCKDALKGATG", "text": "FUNCTION: Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily."}
{"protein": "MNKKAWTVLLIEDDPMVQEVNRQFIEQVEGFTVIAAASNGLEGVQLIKQHQPDLTIIDMYMPSQDGLTTLQQIRANGYKTDVIAVTAASDIETVRKVLQYGAVDYIMKPFKFERMKQALEQYRSFQVKISQKEHITQSELDSMLFQQFEEKADLLPKGLNAVTLRRIQQYLSEQNHPISAEEVADGVGIARVTARRYLEFLEQENELKLSVEYGRVGRPINRYMLKIN", "text": "FUNCTION: Member of the two-component regulatory system DctS/DctR. Essential for expression of DctP (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSPARRCRGMRAAVAASVGLSEGPAGSRSGRLFRPPSPAPAAPGARLLRLPGSGAVQAASPERAGWTEALRAAVAELRAGAVVAVPTDTLYGLACAASCSAALRAVYRLKGRSEAKPLAVCLGRVADVYRYCRVRVPEGLLKDLLPGPVTLVMERSEELNKDLNPFTPLVGIRIPDHAFMQDLAQMFEGPLALTSANLSSQASSLNVEEFQDLWPQLSLVIDGGQIGDGQSPECRLGSTVVDLSVPGKFGIIRPGCALESTTAILQQKYGLLPSHASYL", "text": "FUNCTION: Cytoplasmic and mitochondrial threonylcarbamoyl-AMP synthase required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (PubMed:29760464, PubMed:31481669, PubMed:34545459). Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate (PubMed:29760464). Participates in t(6)A37 formation in cytoplasmic and mitochondrial tRNAs (PubMed:29760464). May regulate the activity of some transporters (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Cell membrane; Peripheral membrane protein Note=A large fraction localizes in the cytoplasm, whereas a smaller fraction is imported to mitochondria. SIMILARITY: Belongs to the SUA5 family."}
{"protein": "MNNNDLVAKLWKLCDNLRDGGVSYQNYVNELASLLFLKMCKETGQEADYLPEGYRWDDLKSRIGQEQLQFYRNLLVHLGADEKKLVQAVFQNVNTTITQPKQLTELVSSMDSLDWYNGDHGKSRDDFGDMYEGLLQKNANETKSGAGQYFTPRPLIKTIIHLLKPQPREVVQDPAAGTAGFLIEADRYVKSQTNDLDDLDGDAQDFQIKKAFVGLELVPGTRRLALMNCLLHDIEGNLDHGGAIRLGNTLGSDGENLPQADIVATNPPFGSAAGTNITRTFVHPTSNKQLCFMQHIIETLPPGGRAAAVVPDNVLFEGGKGTDIRRDLMDKCHLHTILRLPTGIFYAQGVKTNVLFFTKGTVANPNQDKNCTDDVWVYDLRTNMPSFGKRTPFTEQHLQPFETVYGEDPHGLSPRTEGEWSFNAEESEVADSEENKNADQHQATSRWRKFSREWIRTAKSDSLDISWLKDKDSIDADSLPEPDVLAAEAMGELVQALGELDALMRELGAGDEADAQRQLLEEAFGGVKA", "text": "FUNCTION: The subtype gamma methyltransferase (M) subunit of a type I restriction enzyme. The M and S subunits together form a methyltransferase (MTase) that methylates A-2 on the top strand and A-3 on the bottom strand of the sequence 5'-AACN(6)GTRC-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated (PubMed:3025838, PubMed:12654995). After locating a non- methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage (By similarity). SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MAPGSVTSDISPSSTSTAGSSRSPESEKPGPSHGGVPPGGPSHSSLPVGRRHPPVLRMVLEALQAGEQRRGTSVAAIKLYILHKYPTVDVLRFKYLLKQALATGMRRGLLARPLNSKARGATGSFKLVPKHKKKIQPRKMAPATAPRRAGEAKGKGPKKPSEAKEDPPNVGKVKKAAKRPAKVQKPPPKPGAATEKARKQGGAAKDTRAQSGEARKVPPKPDKAMRAPSSAGGLSRKAKAKGSRSSQGDAEAYRKTKAESKSSKPTASKVKNGAASPTKKKVVAKAKAPKAGQGPNTKAAAPAKGSGSKVVPAHLSRKTEAPKGPRKAGLPIKASSSKVSSQRAEA", "text": "FUNCTION: May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome. SIMILARITY: Belongs to the histone H1/H5 family."}
{"protein": "MKYTATFALLILAIGIQTQRRSTICRCRQEDACWPTTAEWSSLNQSIDGKLRHLRPVGLPCQQSAYHKEKCDEVLAMTHNSSWRVDHPESLQLVSWESWPEKNQSCQIVREAVDGCAQGRIPLYSAAVESTKQVQQAVSFAKHRNLRLVVRNTGHDMAGRSSAPGSLQILTSGLKGINYTENFVPFITQGSAEPMGPAVTIGAGILTGELYATGSEKGFVVLGGACSTVGIAGGFIQSGGMGILSPSKGLGSDHVLQVEIVTADGSHIIANQYQNEDLFWAVRGGGGGTFGVITSVTLRAFADLPATVTGIQINTPSADAIFWAGVKTVLSILPELTDAGNSARMIVLPASSTGGASASFEGYTFNKKGAVSLLALQRALDDFGIPFKLSHDFQGNLSRFLAAPKGVDLAGISVIPGSVFLSYDLVASKDGPAKVTSALSDLRLGPGSSFSVDAFGGGQVVNNKNRINSAVHPDWRSALLSLTVGRGVPPGYTLETLKSIESELENDQLPRLRSLEGGRKGAYLAVAYPNEVYFQDSFWGKNYDRLLKVKRAWDPEDLFITRVGVGSERWDDEGMCTRADSGLWHALARF", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:23213353, PubMed:31548667, PubMed:28777910). The first step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading (PubMed:23213353, PubMed:31548667). This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE (PubMed:31548667). The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway (PubMed:31548667). Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid (PubMed:31548667). Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide (PubMed:31548667, PubMed:28777910). MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C (PubMed:28777910). Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C- 8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D (PubMed:28777910). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGPPPPGMRPPRP", "text": "FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28502770, PubMed:28781166, PubMed:28076346). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (PubMed:12975319). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=SMN- mediated assembly into core snRNPs occurs in the cytosol before SMN- mediated transport to the nucleus to be included in spliceosomes. SIMILARITY: Belongs to the snRNP SmB/SmN family."}
{"protein": "MSNSILNLGSFACLLSLGSIVLWYTISAVLAWYPLRKIPAPSFLATFSYLWLAKTTYSGKQYWIQRDLHKKYGPLVRIGPTDIITDDPEIIKKISSARSSHRRGDWYLTGRFNPYYDNMFTMLEPGPHAKAKARTAAAYSGRDMPDLEVGVNAQLQTLIGLMRSKYASNTVKPHQPLLDLGQVSCFFTMDVITRLAFGEEFGYLKEETDQYGFLGEVRELWPRMSTSADTPWIRKFLFSPPFLKVLGPKPTDKTGFGALMAVAEHHVGKRFAPDAKKKEDMLGSFIRHGLNQQECEVEGLFMIVAGTESTASAIRSTLVHVMTCPRVYQKLKTEINLAVEEGKVSSPIKLEEAKLLPFLQAVIYEGIRMRPPLLGLFPKIVPDGGEEFHGMFIPAGTAICMNTSSLLRSTALFGDDAEVYRPERFMELEKSKRGEMERNVELAFGYGQYMCVGKTVAFMELNKSIFEILRAFDLQLLSPAKPCDVLSYGIFLESNMLVKVTESEGTEYK", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses (PubMed:15240257, PubMed:16820452). The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha- ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (PubMed:30226766). The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha- ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha- ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom (PubMed:16820452). SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSFEIIAKDLAGRVGKLYTKSGVIETPALFPVVDPRKQELPSAVIERYFGQIITNAYFVYRLTGGRAVDIKKVLSWNAVLMTDSGAYQILRYGSVEVDPDEILQFQARIGSDIGVILDLPFDYEEPYESALLKVEETIRRAKRASAMLDKLEDMLVVGPIQGGLYLDLLATSAREISKLGFHIFAVGSPTTLLEEYRFDLLLEVILHVKANILREAPLHLFGAGHPLVLPFAVALGVDLFDSASYILYARDDRIMLRDRTLRLEDVKTDYLPCSTKLCHKPVKELREMPHEERIQLIAEHNLAILREELLEIKQRIHEGTLWEYLEIKARAHPTLYRFLRSLGRYKRLIEEYDPETHPETHGLFFYQDTAESRPEPHRHWSRTANLYTPSKVAIVIRAGEKPYNKSWEYRYLKSLVGDRAHVLFYDPVFGLVPEEVAEIYPLSQNEAEGESEAARAFAYEWLNNYDVILLYRVDLPMLSKKVIPLRSLDDVLHYI", "text": "FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family."}
{"protein": "MANKVKAEIGVIGGSGFYSFLDDVTEVRVDTPYGPPSDSLFLGEVAGRRVAFLPRHGRGHHLPPHRINYRANLWALRSVGARQVLGPCAVGGLRPEYGPGTLLVPDQFVDRTRSRPSTYFDGLPMPDGTVPNVVHVSLADPYCPTGRAAALKAARGREWEPVDGGTLVVVEGPRFGTRAESLWHRAQGWSVVGMTGHPEAALARELELCYTSLTLVTDLDAGAESGEGVSHEEVLRVFAANVDRLRGVLFDAVAALPASGERDCPCGAALGGMDPGIALP", "text": "FUNCTION: Purine nucleoside phosphorylase involved in purine salvage. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily."}
{"protein": "MARLNESTASSEPIEILKRRFVRQNREIARVNSIQSLRIRSLESEVSNLLSENVSLREQIITLTQELERFEAARTLHDGVYDVKARLDSKLVELGNLITELGSLPRRYSRAVRENGEPAPARQSRESGPKEVDDTDPEPNLGFLDGRLPVIMEDKLYPRRTLTAQEVQELRDSDTDGPNCSGFEDSSISPKQRVEYDEAATGGPAYFIDTNTIVEEIENEHSLPPNLETRRKKKIGPATVNKDQADTRPISLLDSKFTRKCGAKRKFSAEDDESLFESSPSEDDEFQFSRPAQSPKLFSQNEHASADDGSGELRRPIQSPTLSSQNDHSPVKMKPQSERSIAHVHGERRVLEPKSTNTNILSPAKPSIMKDYNQNHDFGYNEKSEKPLPRQGKGAVDGSKNASPKKSSTRTPVFGNDGNKSGNKQKKSGAIKSNTPSLDGIEDSEIATTADMPSTRPSRRRGTVSQPESHKTEGISMPP", "text": "FUNCTION: Plays a central role in chromosome cohesion during cell division by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere. SIMILARITY: Belongs to the shugoshin family."}
{"protein": "MILGYVNNTYFNQAPNFSSNFNFQFQKRLTKEDIYFIVPDYLIPDDCLQIHKLYDNCMSGNFVVMQNKPIQYNSDIEIIEHYTDELAEVALSRFSLIMQAKFSKIFKSEINDESINQLVSEIYNGAPFVKMSPMFNADDDIIDLTSNSVIPALTEMKREYQNKISELSNYLGINSLAVDKESGVSDEEAKSNRGFTTSNSNIYLKGREPITFLSKRYGLDIKPYYDDETTSKISMVDTLFKDESSDING", "text": "FUNCTION: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the 6 packaging RNA molecules (pRNA) forming a double-ring structure which in turn binds to the ATPase gp16 hexamer, forming the active DNA-translocating motor. This complex is essential for the specificity of packaging from the left DNA end. SUBCELLULAR LOCATION: Virion Note=Present in 12 copies in the virion. SIMILARITY: Belongs to the phi29likevirus portal protein family."}
{"protein": "MAQISVTPEELKSQAQVYIQSKEEIDQAIQKVNSMNSTIAEEWKGQAFQAYLEQYNQLHQTVVQFENLLESVNQQLNKYADTVAERDAQDAQSFGF", "text": "SIMILARITY: Belongs to the WXG100 family. sagEsxA-like subfamily."}
{"protein": "MTSIHTGSNNNIVELDMSELIRPIPPVLDMNKVNSMMETMTGKTPPASCGLTSEDLEAGELPPVDVLTFKKSGKPYYFAFGGCHRLRAHDEAGRKKVRCKLVNCSPNTLRLYLGASANKFLDSD", "text": "FUNCTION: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in a peroxiredoxin. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the sulfiredoxin family."}
{"protein": "MLSILFDDPARTSSGALLIVGILLLRWALWPAPSSHWPLVNGKRWFEITTTKSKDRFVANGKDILLSSFKRLSKGFRLGTDNGPMIILSPEYVDEFRSEDRLCPVKFQAELAHTHLPGFEILSDKHVPKSVFTDFILRKLTPAIDSTAPASVTRLREALESTWTNSSEWHQIDLHSSVQVLSHTTTSPIFVGPELSSSKAWEELTYRYVGNFPVVACSLRLWPKFSQRFVNMILPSCTSLRKDVNQARQMVNEVLQKRAASQAARISQGLEPEKFSDGLQWWQELSGPPCDPACLQLALIFSAVHSTVDLLSQTILNLAERPELVDELRQEIIAVRESQPWGKAAFYKLGLMDSVLKETQRLKPVSIATEDVTFSDGLVIPKGSLVMMSCHNMREDSVTYPNPLEFDGHRFRKMRESPTNGAMAHLVSSSQHHMGFGIGTHSCPGRFFIAAGLKLTLSQILLNYDLRLSDPSENVTQNQGLFLMPNFKAKVEVRRREPEIEL", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture (PubMed:27602587). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B (PubMed:27602587). The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK (PubMed:27602587). Finally, prhA leads to berkeleydione via the berkeleyone B intermediate (PubMed:27602587, PubMed:29317628). PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione (PubMed:27602587, PubMed:29317628). Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MRHPREENSIVVELEPSLATFIKQGFNNLVKWPLLNIGIVLSNTSTAINEEWLTVVEHIPTMKIFYKHIHKILTREMGFLVYLKRSQSERDNYITLYDFDYYIIDKDTNSVTMVDKPTELKETLLHVFQEYRLKSSQTIELIAFSSGTVINEDIVSKLTFLDVEVFNREYNNVKTIMNPDFVSRSPFIVISPMGKLTFFVEVYSWFDFKSCFKDIIDFLEGALIANIHNHMIKVGDCDETVSSYNPESGILFVNDLMTMNIVNFFGCNSRLESYHRFDITKVDVELFIKALSDACKKILLASNRL", "text": "FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of D6 and A7, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase. SUBCELLULAR LOCATION: Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle. SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 35 kDa subunit family."}
{"protein": "MSKVLILFGSSTGNTESIAQKLEELVAAGGHEVTLLNAAEASADNLADGYDAVLMGCSAWGMEDLELQDDFAPLFDEMENMGLKGKKLAAFASGDMEYEHYCGAVPAIEEKARGLGAEVICEGLKIEGDASSDPDAVSAFAEDVLKKL", "text": "FUNCTION: Low-potential electron donor to a number of redox enzymes. SIMILARITY: Belongs to the flavodoxin family."}
{"protein": "MQIKRSIEKIPGGMMLVPLFLGALCHTFSPGAGKYFGSFTNGMITGTVPILAVWFFCMGASIKLSATGTVLRKSGTLVVTKIAVAWVVAAIASRIIPEHGVEVGFFAGLSTLALVAAMDMTNGGLYASIMQQYGTKEEAGAFVLMSLESGPLMTMIILGTAGIASFEPHVFVGAVLPFLVGFALGNLDPELREFFSKAVQTLIPFFAFALGNTIDLTVIAQTGLLGILLGVAVIIVTGIPLIIADKLIGGGDGTAGIAASSSAGAAVATPVLIAEMVPAFKPMAPAATSLVATAVIVTSILVPIITSIWSRKVKARAAKIEILGTVK", "text": "FUNCTION: Catalyzes the proton-dependent uptake of 2-keto-3- deoxygluconate (KDG) into the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KdgT transporter family."}
{"protein": "MRMKQTIPSSYVGLKINEWYTHIRQFHVAEAERVKLEVEREIEDMEEDQDLLLYYSLMEFRHRVMLDYIKPFGEDTSQLEFSELLEDIEGNQYKLTGLLEYYFNFFRGMYEFKQKMFVSAMMYYKRAEKNLALVSDDIEKAEFAFKMAEIFYNLKQTYVSMSYAVQALETYQMYETYTVRRIQCEFVIAGNYDDMQYPERALPHLELALDLAKKEGNPRLISSALYNLGNCYEKMGELQKAAEYFGKSVSICKSEKFDNLPHSIYSLTQVLYKQKNDAEAQKKYREGLEIARQYSDELFVELFQFLHALYGKNIDTESVSHTFQFLEEHMLYPYIEELAHDAAQFYIENGQPEKALSFYEKMVHAQKQIQRGDCLYEI", "text": "FUNCTION: Involved in the regulation of sporulation (PubMed:1624431, PubMed:8001132, PubMed:11923303, PubMed:22267516). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:8001132, PubMed:11923303, PubMed:22267516). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rap family."}
{"protein": "MTLALTAEKIERNRFTGLKVENSTFHHCDFSGADLTGTEFIGCQFYDRENQKGCNFSRAILKDAIFKNCDLSMADFRNASALGIEIRGCRAQGADFRGTSFMNMITTRTWFCSAYITNTNLSYANFSKAVLEKCELWENRWMGTQVLGATFSGSDLSGGEFSSFDWRAANVTHCDLTNSELGDLDVRGVDLQGVKLDSYQVSLIMERLGVAIIG", "text": "FUNCTION: Confers reduced sensitivity to the fluoroquinolone antibiotic ciprofloxacin (five-fold increase in minimum inhibitory concentration) when expressed in E.coli. SIMILARITY: Belongs to the pentapeptide repeat protein family."}
{"protein": "MEPAAGFLSPRPFPRAAVPSAPPAGPGPPANASPRSEPEVLAGPRAPDPPGRLITDPLSGRTYTKGRLLGKGGFARCYEATDTESGIAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITDNMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIEQILRHDFFTKGYTPDRLPVSSCVTVPDLTPPNPARSLFAKVTKSLFGRKKNKNKNHSEDQDNVSCLAPVVSGQAPASLIETAAEDSSPRGTLASSGDGFEEGLTVATVVESALCALRNCVAFMPPAEQNPAPLAQPEPLVWVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSMGSVPRALQPQLGILRYFASYMEQHLMKGGDLPSVEEAEVPAPPLLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDQSPA", "text": "FUNCTION: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nucleolus Golgi apparatus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
{"protein": "MVTPGNIGSFTVWDYVVFALMLLISAVIGIYYAFAGGGQKTSKDFLMGGRSMTAVPVALSLTASFMSAVTVLGTPAEVYRFGSMFSIFAFTYAIVVVISSEVFLPVFYRLGITSTYEYLELRFNKFVRLLGTILFIIQTVLYTGIVIYAPALALNQVTGFDLWGAVVATGVVCTFYCTMGGLKAVVWTDVFQVGIMVAGFSSVIIRAVVVQGGIGPILNDSYYGDRLNFWDFTPNPLQRHSFWTIVVGGTFTWTGIYGVNQSQVQRYIACKTRFQAKLSLYINLLGLWAILACAVLSGLAMYSIYKDCDPWTAQFVSAPDQLMPYLSLDILRDYPGLPGLFVSCAYSGTLSTVSSSINALAAVTVEDLIKPYFRSLSETKMSWISKGTSLIYGAICIAMAGLASLMGGLLQAALSIFGMVGGPLLGLFALGIIFPFVNSLGAVIGLLSGFAISLWVGIGSQIYPPTASSSLPKPLSLEGCNFTSFESNWTTTVMPMMTTLIPEVSSRPELADSWYSLSYLYFSTLGTIVAVVVGVIASLLSGGLKQNVNRDFLLTSQDFSYLNVLFSNCKKKGQEEKVEVLNWKMRSTDTDMDQGTDNPAFNHMEMSSTEKKEKMNGIIA", "text": "FUNCTION: Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)- dependent sodium-coupled solute transporter, including transport of monocarboxylates (short-chain fatty acids including L-lactate, D- lactate, pyruvate, acetate, propionate, valerate and butyrate), mocarboxylate drugs (nicotinate, benzoate, salicylate and 5- aminosalicylate) and ketone bodies (beta-D-hydroxybutyrate, acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate stoichiometry of between 4:1 and 2:1 (By similarity). Catalyzes passive carrier mediated diffusion of iodide. Mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane (By similarity). Mediates sodium-coupled electrogenic transport of pyroglutamate (5-oxo-L-proline) (By similarity). Can mediate the transport of chloride, bromide, iodide and nitrate ions when external concentration of sodium ions is reduced (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
{"protein": "EPRTPWDWV", "text": "FUNCTION: Putative defense peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Tryptophillin subfamily."}
{"protein": "MDRVAKAREIIEKAKAENRPLVEPEAKEILKLYGIPVPEFKVARNEEEAVKFSGEIGYPVVMKIVSPQIIHKSDAGGVKINIKNDEEAREAFRTIMQNARNYKPDADLWGVIIYRMLPLGREVIVGMIRDPQFGPAVMFGLGGIFVEILKDVSFRVAPITKEDALEMIREIKAYPILAGARGEKPVNIEALADIIVKVGELALELPEIKEIDINPIFAYEDSAIAVDARMIL", "text": "FUNCTION: Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl- CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetate CoA ligase beta subunit family."}
{"protein": "MANMLVASSSKTLPTTTTTTITPKPKFPLLKTPLLKLSPPQLPPLKHLNLSVLKSAAITATPLTLSFLLPYPSLAEEIEKASLFDFNLTLPIIMAEFLFLMFALDKIYYTPLGDFMDKRDASIKEQLSGVKDTSSEVKQLEEQANAVMRAARAEISAALNKMKKETQLEVEAKLAEGRKKIEVELQEALGSLEQQKEDTIKSLDSQISALSDDIVKKVLPVS", "text": "FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria (By similarity). FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single- pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MGFLTAVTQGLVRGADRMSKWTSKRGPRTFTKSRGAKKTGIYTSDRKFVQIKEMVPEFVVPDLTGFKLKPYVNYRAPAGIDTPLTAKALFQETVAPAIEKDFKEGTFDANNLEKYGFEPTQEGKLFQLYPKNFPR", "text": "FUNCTION: Component of the mitochondrial ribosome large subunit. Also involved in apoptosis and cell cycle. Enhances p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis in response to growth-inhibitory condition. Enhances p53/TP53 translocation to the mitochondria. Has the ability to arrest the cell cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B (p27Kip1) proteins. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL41 family."}
{"protein": "MAATAPKAGGSAPEAAGSAEAPLQYSLLLQYLVGDKRQPRLLEPGSLGGIPSPAKSEEQKMIERAMESCAFKAVLACVGGFVLGGAFGIFTAGIDTNVGFDPKDPYRTPTAKEVLKDMGQRGMSYAKNFAIVGAMFSCTECLVESYRGKSDWKNSVISGCITGGAIGFRAGVKAGAIGCGGFAAFSAAIDYYLR", "text": "FUNCTION: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family."}
{"protein": "MDEGYYSGNLESVLGYVSDMHTKLASITQLVIAKIETIDNDILNNDIVNFIMCRSNLNNPFISFLDTVYTIIDQEIYQNELINSLDDNKIIDCIVNKFMSFYKDNLENIVDAIITLKYIMNNPDFKTTYAEVLGSRIADIDIKQVIRENILQLSNDIRERYL", "text": "SIMILARITY: Belongs to the poxviridae A49 protein family."}
{"protein": "MTEFIPFIILIGVAFVILSIILSFVPVGLWITAQFSGVKVGIFTLVGMRFRRVQPIRIINPLIKATKAGIDINIDKLEAHYLAGGDVNTLVDALIAAQRAEINLPFERAAAIDLAGRQVLEAVQVSVNPKVIETPKIAAVAKDGIEVMARARVTVRANIERLVGGAGEETIIARVGEGIVTTVGSATTHKHVLENPDMISKTVLSKGLDAGTAYEILSIDIADIDIGRNIGAQLQTDQADADKRIAQAKAEERRAMAVAKEQEMKAAVQEMRAKVVEAEAEVPKALATALREGKMGVMDYYNMKNIMADTDMRDSISKVAPNEKKYEEE", "text": "FUNCTION: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Membrane raft; Multi-pass membrane protein. SIMILARITY: Belongs to the flotillin-like FloA family."}
{"protein": "MYSLLIALLCAGTAVDAQALQQRQAGTTLTVDLSTTYQRIDGFGTSEAFQRAVQMSRLPEEGQRRALDVLFSTTNGAGLSILRNGIGSSPDMSSDHMVSIAPKSPGSPNNPLIYSWDGSDNKQLWVSQEAVHTYGVKTIYADAWSAPGYMKTNGNDANGGTLCGLSGAQCASGDWRQAYADYLTKYVEFYQESNVTVTHLGFINEPELTTSYASMRFSASQAAEFIRILYPTIQKSNLTYKPTIACCDAEGWNSQAGMLGALSSVNSMFGLVTAHAYTSQPGFSMNTPHPVWMTEAADLQGAWTSAWYSYGGAGEGWTWANNVYNAIVNGNASAYLYWIGAQTGNTNSHMVHIDANAGTVEPSKRLWALGQWSRFVRPGARRVAVSGASGSLRTAAFRNEDGSVAVVVINSGGDAAVNVRLASSSSADQQPASAKAWATDNSRAIEEIQASFADGVATVNVPSRSMTTVVLYPAADA", "text": "FUNCTION: Xylanase exhibiting endo- and exo-xylanase activity (PubMed:31110561). Shows the highest activity toward beechwood glucuronoxylan, which consists of a beta-1,4-linked xylose backbone decorated with the methylated form of D-glucuronic acid (MeGlcA) attached directly to the main chain at xylose C2 (PubMed:31110561). Acts also against wheat arabinoxylan, a xylan without MeGlcA substituents along the main chain, but the xylanase activity is about two orders of magnitude lower than that achieved in the case of beechwood xylan (PubMed:31110561). Shows no activity against carob galactomannan, konjac glucomannan, or barley beta-glucan (PubMed:31110561). The recombinant xylanase also exhibits an exo- activity by releasing processively disaccharide units from the non- reducing end of linear and decorated xylooligosaccharides (XOS) (PubMed:31110561). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 30 family."}
{"protein": "MSGVWVFKNGVIRLVENPNQSGSDTQNRRKVMVYLPTGEVVSSYSTLEQILQSLGWERYFGGGDTDLLQFHKRSSIDLISLPRDFTKFNSVYMYDIVVKNPNYFHVRDSH", "text": "FUNCTION: Modulates the competence to flowering of apical meristems. Involved in a GA-dependent response in apical meristems during the transition to flowering. SIMILARITY: Belongs to the FPF1 family."}
{"protein": "MEGPTHPKPSKDKTFSWDLMILVGVLLRLDVGMANPSPHQIYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDHPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSITGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGNRLINLVQGTYLALNVTNPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSDPQHKLTISEVSGQGLCIGTVPKTHQALCKKTQKGHKGTHYLAAPSGTYWACNTGLIPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFDKTVRLRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQMAMHTDIQALEESISALEKSLTSLSEVVL", "text": "FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity)."}
{"protein": "MKFVLLFGVFLVTLFSYSSAEMLDDFDQADEDELLSLIEKEEARKDCIPKHHECTNNKHGCCRGHLFKYKCQCTTVVTQSGEETERCFCGTPPHHKAAELVVGFGKKIFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 03 subfamily."}
{"protein": "LLGMIPLAISAISALSKL", "text": "FUNCTION: Antimicrobial peptide active against S.aureus (MIC=8 uM) but inactive against E.coli (PubMed:17561225). Shows also fungicide activity (By similarity). Also inhibits growth of B.dendrobatidis zoospores at high concentrations (above 25 uM) (PubMed:17561225). Shows anticancer activities since it is cytolytic against HepG2 human hepatoma-derived cells (LC(50)=35 uM) (PubMed:17561225). Is strongly hemolytic on human erythrocytes (LC(50)=40 uM) (PubMed:17561225). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Medusin subfamily."}
{"protein": "MATGDLQGKYQKLAQEYSKLRAQNQVLKRAVVDEQANGTALKEQLKMKDQSLRKQQQEMDSLTFRNQQLAKRVELLQDELSLMDVKGKKTKKNMDTSQLSQEQKSVFDEDLQKKIEENERLHIQFFEASETHRQMESELTSRLQELETNTAQHQAVVDGLTQKYMDTIEKLQGDKAKLEVKCQALEREAKDCRLRTEDCQNQLKTLHTDLSSRLDDSLVIINEKLPFNDTRTSQLNALNVPVHNKRYQLKARELANQGLSFVRDLVTALLNFHTYTEQRVQIFPIDSAIDVVSPLNKKFSEYLHENASYVRPLEDGMLQLFESITEDTVTVLETAVKLKIFSENFSSYVCFLQKILPYQLKSLEEESEFSSGTSALRSRNQELHKDMQKITAVFDKLKTYITLLALPSTKPEGLLRTNYGTILTQISEALHRLHDISQELSKHYNNKAALEQELPAATDKLKTTNDCVLSSLAALTNVTSKIATFFGNNLDYFISSLSYGPKGGRGFTNPLSAETMLVYKKKAAQYMNNLRKPCPASVPYEEALVNRRVLLSSTESREGLAQQVQQSLEKIGKLEQEKEHWMLEAQLSKIKLEKETLRIAALIKGTEKGQLPEVPHDNALLLDAGEHGKGNSTETKSTSLIGMLTVTIEDLQAPDHDSREELIKNHYMTRIAELTTHLQQADSKAVHLYAECRALAKRLTLSDKSNRSLTEETKYSVQSISKLQDELITTKRSYEDQLSMMSDHLCVMNETLSKQREEIDTLKMANKGNSKKNKMR", "text": "FUNCTION: Putative regulator of protein phosphatase 1 (PP1) activity. May play a role in the endosomal sorting process or in endosome maturation pathway. SUBCELLULAR LOCATION: Early endosome."}
{"protein": "MNEWSEMLVCRDYCALMMRDRKECDARCCRDGEGERVRARERLDATVAGLTELEYLRQRQELLVRSVLSCPEAAGQDKPCLTVDDSYLNTEEKLLEENILLLRKQLNCLRRRDAGLINQLQELDRQISDLRLDTETSHEHVETDSRPSSGFYDLSDGASGSLSNSSNSVFSECLSSCRSTTCLCTPLDTSLCASEGRLKPADDPGSCAECDCHCEDSSSGTVRRSLSASYSPSPDSSCDGISKFHCDLIAKNGNDVYRYPSPLHAVAVQSPIFIQSMTSHLKDDCNFSKPGEALNDEQKPEQVVGSQTSSWHASQMLPNKKLDSYIYGLLQRRAQPLRTNKPRTSINTDPSKSILRQASLCSRAPASVQAQQWTSDLKPNWQTCLQDASATSTEPSTASPQRQWSAESKGGTPQNGAYLSSSQPQNSYSTTNENTNCLLKKKVSGTSKGQLLSATPKDCPDLGSPKAVSSPKLNKHCFYNVEDNKTGQAMKASPLKRSPKTQTSLSCGKDSEQLAQELVSLGSSSQSQDEGGPLVSAQYIPAQKQNVNLQKGGTKNIKIVKVKNSASSKSRPQVFEHVSETVRDKHRTGSRRTRQVDEVHHLHKSSKKASAKTKRIPASIPEGRILERHTSSSGARSSAQRHHGHHRHHEAVLAKPKYKRNDFHRRPRGLHEIPYEEAYRRAHRRQKREMLSHMYLPSNAHYTSPYAYVGSDSEYSAECASLFHSTILDTSEDERSNYTTNCFGDSESSASEADYVAESSTSSDSEGSAGVNWRQISQAGSGSHGMTSAQAKAFVKIKASHNLKKKILRFRSGSLKLMTTV", "text": "FUNCTION: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. Binds to dvl2 and may regulate the degradation of ctnnb1/beta-catenin, thereby modulating the transcriptional activation of target genes of the Wnt signaling pathway. Seems to activate the canonical Wnt signaling pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dapper family."}
{"protein": "MLTLNEHLLNQVLLIAYQSGKHLQQFYQKQVHVELKEDNTPVTEADLFVSQFLTEKLTALFPNVPVLSEENCHISFEERKNWKEYWLIDPLDGTQQFINRTDQFSVLITLVRKNKPVLSVIHAPILSTTYYAMCDFGTFKKQLDQVKKLTKNTTNFDRPLRIAVGATTSQEKVRSILPKDFPCEFVVVGSSSLKSGLVAEGAVDCYVRLGQTGEWDTAGAEVLLGETHGAIFDSHFEPLTYNQRETLINPHFVMVGDQSFDWRSIFQFN", "text": "FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the inositol monophosphatase superfamily. CysQ family."}
{"protein": "MPAEMQAPQWLLLLLVILPATGSDPVLCFTQYEESSGRCKGLLGRDIRVEDCCLNAAYAFQEHDGGLCQACRSPQWSAWSLWGPCSVTCSEGSQLRHRRCVGRGGQCSENVAPGTLEWQLQACEDQPCCPEMGGWSEWGPWGPCSVTCSKGTQIRQRVCDNPAPKCGGHCPGEAQQSQACDTQKTCPTHGAWASWGPWSPCSGSCLGGAQEPKETRSRSCSAPAPSHQPPGKPCSGPAYEHKACSGLPPCPVAGGWGPWSPLSPCSVTCGLGQTLEQRTCDHPAPRHGGPFCAGDATRNQMCNKAVPCPVNGEWEAWGKWSDCSRLRMSINCEGTPGQQSRSRSCGGRKFNGKPCAGKLQDIRHCYNIHNCIMKGSWSQWSTWSLCTPPCSPNATRVRQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGTPRPLCEALQGQKLVVEEKRSCLHVPVCKDPEEKKP", "text": "FUNCTION: A positive regulator of the alternate pathway of complement (PubMed:28264884). It binds to and stabilizes the C3- and C5-convertase enzyme complexes (By similarity). Inhibits CFI-CFH mediated degradation of Inhibits CFI-CFH mediated degradation of Complement C3 beta chain (C3b) (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKNINEWHHIFKLDPAKEISDEHLDQICESGTDAIIVGGTDNVTLDGVLDLLSRIRRSHMVPVVLEVSEEETLTPGFDYYFVPMVLNSKEKKYMMDIQHKAIKEFIDMMEFAEVYFEGYCILNEDAKAFQYTNCVMPDLDDVKAYAYMAEKVFHLPFFYIEYSGAYGDPTLVKEVKEELQNTQLLYGGGIETTAQAKEMKEYADTIIVGNSIYTNINEALKTVEAVKGN", "text": "FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I subfamily."}
{"protein": "METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS", "text": "FUNCTION: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Secreted. SIMILARITY: Belongs to the tissue factor family."}
{"protein": "MEESVNQMQPLNEKQIANSQDGYVWQVTDMNRLHRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTTKQEPMLFALAICSQCSDISTKQAAFKAVSEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDAAFYKTFKTVEPTGKRFLLAVDVSASMNQRVLGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMVPCPVTTDMTLQQVLMAMSQIPAGGTDCSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTGALDVIRNFTLDMI", "text": "FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (PubMed:18056422, PubMed:26382853). Binds to endogenous Alu retroelements which are induced by type I interferon and stimulate porinflammatory cytokine secretion (PubMed:26382853). Regulates the expression of Alu retroelements as well as inflammatory genes (PubMed:26382853). May play roles in cilia formation and/or maintenance (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SIMILARITY: Belongs to the Ro 60 kDa family."}
{"protein": "MLLDLNVESPERSGTSSSSVLNSGDAGGGGGGGGGGGLFRFDLLASSPDDDECSGEQHQLPAASGIVTRQLLPPPPPAAPSPAPAWQPPRRAAEDAALAQRPVVAKKTRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGLEADINFNLSDYEDDLKQMRNWTKEEFVHILRRQSTGFARGSSKFRGVTLHKCGRWEARMGQLLGKKYIYLGLFDTEVEAARAYDRAAIRFNGREAVTNFEPASYNVDALPDAGNEAIVDGDLDLDLRISQPNARDSKSDVATTGLQLTCDSPESSNITVHQPMGSSPQWTVHHQSTPLPPQHQRLYPSHCLGFLPNLQERPMDRRPELGPMPFPTQAWQMQAPSHLPLLHAAASSGFSAGAGAGVAAATRRQPPFPADHPFYFPPTA", "text": "FUNCTION: Probable transcription factor (By similarity). Involved in spikelet transition (Probable). Together with SNB, controls synergistically inflorescence architecture and floral meristem establishment via the regulation of spatio-temporal expression of B- and E-function floral organ identity genes in the lodicules and of spikelet meristem genes (PubMed:22003982). Prevents lemma and palea elongation as well as grain growth (PubMed:28066457). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. AP2 subfamily."}
{"protein": "MDQLASLAESVAMEEDSEKQSIKGESSLEPDSTPSSPKITARWNPSEACRPLVDDAPIFYPTNEDFDDPLGYIEKLRSKAESYGICRIVPPVAWRPPCPLKEKKIWENSKFPTRIQFIDLLQNREPIKKSTKTKKRKRRRISKIGYTRRKRDSGCDTASSGSSDSEGKFGFQTGPDFTLEEFQKYDEYFKECYFQSEDHPGSKASENKKFKPKVKDLEGEYWRIVEQATDEVEVYYGADLETKKFGSGFPKYKPGYPISEADQYSQCGWNLNNLSRLPGSVLAFESCDISGVIVPWLYVGMCFSTFCWHVEDHHLYSMNYLHTGDPKVWYGIPGNHAESFENVMKKRLPDLFEEQPDLLHQLVTQLSPRILKEEGVPVYRAVQRSGEFILTFPKAYHSGFNCGFNCAEAVNVAPVDWLVHGQNAVEGYSKQRRKSSLSHDKLLLGAAMEATYCLWELSLSKKKTPVIARWKRVCSEDGLLTKAVKKRVQMEEERLNHLQDGFSLRKMEGDFDNKRERECFLCFYDLHMSASSCKCSPNRFACLIHAKDLCSCESKDRYILIRHTLDELWALVRALEGDLDAIDLWASKCRDQYPSQHPRAREYAYLKSAPCIKSRGSSKVQQREQNNLQLVSERLQSDLTSNKEVQLKQDGDSDVNRHGHESERNHVHGITDKSAVTDVKLGVGGKFDEKKISVESQNPHSVSDVGCSELAKKVDGCLGGKDQNAATNRLSLSVELLSSGSLVVKKLWCSKQAIYPKGFKSRVKFLSVLDPTNLTNYISEVLDAGLLGPLFRVSVEDYPTENFSNVSAEKCWQMVTQRLKLEIIKKCDQPVSSLTSLQPLESINGLEMFGFLSPHVIKVVEALDPKHQLEEYWNQKAVKLFGAEPIKEGEKDDTEKGGASDPSLDRDTRLLRGLLKKATPEELVMMHGLLCGETRNTELKEELSTLVDKMEISP", "text": "FUNCTION: Transcriptional repressor (PubMed:25578968). Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a higher activity for H3K4me3 and H3K4me2 than H3K4me1 (PubMed:29233856). No activity on H3K9me3/2, H3K36me3/2 and H3K27me3/2 (PubMed:29233856). Function as a nocturne 'eraser' to counteract the diurnal 'writer' methylase activity of ATXR3/SDG2 thus orchestrating the circadian rythm of histone modifications (e.g. H3K4me3) and modulating the rythmic expression of diurnal target genes; this mechanism relies also on the circadian clock oscillators CCA1 and LHY (PubMed:31429787). Involved in a negative regulation of root meristem growth upon suboptimal root growth conditions (PubMed:31826870). Represses FT and TSF expression to inhibit the floral transition. Binds around the transcription start site of the FT locus. Involved in the DRM2-mediated maintenance of DNA methylation, but not required for the de novo DNA methylation. Required for demethylating histone H3K4me3 at the target of RNA silencing. Counteracts the DNA methylation of expressed transgenes; specific attenuation of transgene DNA methylation enhances the production of aberrant RNAs (e.g. uncapped and antisense) that readily induce systemic RDR6-dependent post-transcriptional transgene silencing (PTGS) spreading (PubMed:33986281). Together with NAC051/NAC052 and NAC050, regulates gene expression and flowering time, probably by the promotion of RNA-mediated gene silencing (PubMed:25578968). Together with JMJ16 and JMJ17, required for plant growth and development (PubMed:31038749). Promotes local and systemic immunity (especially toward the bacterial pathogen Pseudomonas syringae Pst DC3000 avrRpt2) by regulating positively pathogen-induced H3K4me3 enrichment and expression of defense genes involved in salicylic acid (SA)- and pipecolic acid (Pip)-mediated defense pathways (e.g. PR1, FMO1, ALD1 and SARD4) (PubMed:31622519). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus Note=Not detected in the nucleolus and the chromocenters. SIMILARITY: Belongs to the JARID1 histone demethylase family."}
{"protein": "MSQEDKGFPAEVVEIIGRTGVAGEVIQVRAKILAGRDKGRVLTRNVKGPVRVGDILILRETEIEARKLKPR", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 family."}
{"protein": "MPPHLALPFRRLFWSLASSQLIPRRHRGHSLLPTTPEAHTDGSVPVFIRALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTQPHVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISENPQKGSPYIIHAEGNERGTKVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYPSGQRSQPGQG", "text": "FUNCTION: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MPSTGTICSLLLLSVLLMADLAMAGSSFLSPEHQKVQQRKESKKPAAKLKPRALEGWLGPEDSGEVEGTEDKLEIRFNAPCDVGIKLSGAQSDQHGQPLGKFLQDILWEEVTEAPADK", "text": "FUNCTION: [Obestatin]: Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility (By similarity). FUNCTION: [Ghrelin]: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the motilin family."}
{"protein": "MVFHYRSILKYQVFRAYFHRQYEQVRIHTGGSQLLTCDCQNYSSRLNQSLPNEFKLDVDSPLPSKVPSYKKHALVLSLQNKSADELEWMTNWQSKLELNPMWPYSIIGDLKTHLKHTKFGSDVLVNAISIHSGNLSAPSRDPHERAHIFVIPDMKLYKISPQDVVSFAHFLGGGHTRQVADHQLSFADFLKGADNVVNKTELVSEPSNADHAFPHEDCKRDWILVCGHNQRDRRCGILGKELINEISAKGLDKDKNVALISHVGGHKFAGNLILYNYVGTNEKTGENQLDSLWFSRVLPPNLGTLLEHVDAKKIPQEYYRGGTSMN", "text": "SIMILARITY: Belongs to the AIM32 family."}
{"protein": "MAKIIGIDLGTTNSCVAVMEGDKPKVIENSEGHRTTPSIVAFTDDNEILVGQSAKRQSVTNPEKTLFAIKRLIGRRFDDPIVQKDIKMVPYKIMKADNGDAWVRVKDQDKAPPQISAEVLRKMKKTAEDYLGEEVKEAVITVPAYFNDSQRQATKDAGRIAGLEVKRIINEPTAAALAYGMDKKRGDSVIAVYDLGGGTFDISIIEIAEVDGEHQFEVLATNGDTFLGGEDFDLALIEYLASEFKKDTGIDLHNDPLALQRLKEAAEKAKIELSSAQQTDVNLPYITADASGPKHLNIKLTRAKLESLVEKLVERTIEPCKTALKDAGLTVSQINEVILVGGQTRMPLVQKTVEEFFGKEPRKDVNPDEAVAVGAAIQAAVLSGEVKDILLLDVTPLSLGIETMGGVMTKLIEKNTTIPTKATQVFSTADDNQTAVTVHVLQGEREQASANKSLGRFDLRDIPPAPRGVPQIEVTFDIDANGILNVSAKDKATGKAQSIVIKASSGLSEEEVAAMVKDAQSHAEEDKKFKEMAELRNQADSLIHSCEKSMKDLADELSEDEKRGIETAISELKEAVQGTDKARIEDKLKVLTDASAKMAERIYAKKSSEGQAAQGQTQSQESTKPAEEGVVDAEFEEVKEEDKK", "text": "FUNCTION: Acts as a chaperone. FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MAPKKPEPKKDDAKTAAPKAAPAPAAAPAAAPEPERPKEAEFDASKIKIEFTPEQIEEFKEAFQLFDRTPKGEMKITYGQCGDVLRALGQNPTQAEVLRVLGKPKQEELNSKMMDFETFLPMLQHISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGERLTEDEVEKLMAGQEDSNGCINYEAFVKHIMAS", "text": "FUNCTION: Regulatory light chain of myosin. Does not bind calcium."}
{"protein": "MAAPVDGSSGGWAARALRRALALTSLTTLALLASLTGLLLSGPAGALPTLGPGWQRQNPDPPVSRTRSLLLDAASGQLRLEDGFHPDAVAWANLTNAIRETGWAYLDLSTNGRYNDSLQAYAAGVVEASVSEELIYMHWMNTVVNYCGPFEYEVGYCEKLKNFLEANLEWMQREMELNPDSPYWHQVRLTLLQLKGLEDSYEGRLTFPTGRFTIKPLGFLLLQISGDLEDLEPALNKTNTKPSLGSGSCSALIKLLPGGHDLLVAHNTWNSYQNMLRIIKKYRLQFREGPQEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGCVLEWIRNVVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPGSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIPYFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLMRYNDFLHDPLSLCEACNPKPNAENAISARSDLNPANGSYPFQALHQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPPFQWSKSPFHSMLHMGQPDLWMFSPIRVPWD", "text": "FUNCTION: Putative phospholipase. SUBCELLULAR LOCATION: Lysosome lumen. SIMILARITY: Belongs to the phospholipase B-like family."}
{"protein": "MQPIPDVNQRIARISAHLHPPKYQMEESSVLRRANCRAKGGAPGFKVAILGAAGGIGQPLAMLMKMNPLVSVLHLYDVVNAPGVTADISHMDTGAVVRGFLGQQQLERALTGMDLVVIPAGVPRKPGMTRDDLFKINAGIVKTLCEGIAKCCPTAIVNLISNPVNSTVPIAAEVFKKAGTYDPKRLLGVTMLDVVRANTFVAEVLGLDPRDVNVPVVGGHAGVTILPLLSQVKPPSSFTQEEINYLTDRIQNGGTEVVEAKAGAGSATLSMAYAAVKFADACLRGLRGDAGVVECAFVSSQVTELPFFATKVRLGRNGIDEVYSLGPLNEYERIGLEKAKKELAGSIEKGVSFIRG", "text": "SUBCELLULAR LOCATION: Glyoxysome. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family."}
{"protein": "MVSSTTPSSGEYLLEMSGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGTILFQGKEIDFHSAKEALENGISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRETKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEVTVLRDGQWIATEPLAGLTMDKIIAMMVGRSLNQRFPDKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKQINNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSGIVDTKTTTQNEILRLASLHL", "text": "FUNCTION: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system (Probable). FUNCTION: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Galactose/methyl galactoside importer (TC 3.A.1.2.3) family."}
{"protein": "QARPRHPKIPP", "text": "FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-potentiating peptide family."}
{"protein": "MREKRKYFIAERVLLIKRSKIRELFERASKMEDVISLGIGEPDFDTPKNIKEAAKRALDEGWTHYTPNAGIPELREAVVEYYKKFYGIDIEVENVIITAGAYEGTYLAFESLLERGDEVIIPDPAFVSYAEDAKVAEAKPVRIPLREENNFLPDPNELLEKISKNTRMIVINYPNNPTGATLDKELAKTIADIAEDYNIYILSDEPYEHFIYEDAKHYPMIKFAPENTILANSFSKTFAMTGWRLGFVVAPSQVIKEMTKLHAYVIGNVASFVQIAGIEALRSEESWKAVEEMKKEYNERRKIVVKRLKNMPGIKVKEPKGAFYVFPNISGTGMSSEKFSEWLLEKARVVVIPGTAFGRMGEGYVRISYATSKEKLIEAMNRIEKALEGEK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MRGAGQQPIIVLSQGTKRESGHQVQIGNINACKTIADVIRTSLGPRAMLKMLMDPMGGIVMTNDGNAILREITVKHPAAKSMIEIARTQDEETGDGTTSVIILAGEVMAHAQTYLEQKTHPTLIIKAYRQALEDMIQWSENKFSKTVDITDDAEIAKVVKSCLGTKMISKWMDLAVNISIQAVKTIRVEKAGVREIDIKRYCRIEKIPGGRIEDSQVVKGIVVNKDILHAKMRRRIENPRIVLLDCNLEYKKGESQTSLEIMREEDISAILEQEEQAIRKQCDEIIKLKPDLVFTEKGISDLAQHFLLKAGITCLRRLKKTDNNRLARVCGARVVHDTSDLRDEDVGTKAQLFEVVKIADEYYTYVTAETTTACTVVLRGPSKDVINEVERNLQDSLHVVRNIMINPKLVPGGGALEMALSREIEQQGAKMDGVKKWPYKAIGLALEVIPRTLIQNCGGSTIRKMTELRAIHAQNAENWTFGVDGTSGDLVDMNKLEIWDPLAVRIQVLKTAIETSVMLLRIDDIVSGTKKAVGGEKQEMMPQ", "text": "FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity). Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Plays a role in microtubule polymerization (PubMed:16054029). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family."}
{"protein": "MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQILEGPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVPSTETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQNTSMRDVYRKFDLGQDVIDFTGHALALYRTDDYLDQPCLETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVQKAGQVIRIICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETAEPEKEVEPALELLEPIDQKFVAISDLYEPIDDGSESQVFCSCSYDATTHFETTCNDIKDIYKRMAGSAFDFENMKRKQNDVFGEADQ", "text": "FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus, trans- Golgi network. SIMILARITY: Belongs to the Rab GDI family."}
{"protein": "MNTKLTKIISGLFVATAAFQTASAGNITDIKVSSLPNKQKIVKVSFDKEIVNPTGFVTSSPARIALDFEQTGISMDQQVLEYADPLLSKISAAQNSSRARLVLNLNKPGQYNTEVRGNKVWIFINESDDTVSAPARPAVKAAPAAPAKQQAAAPFTESVVSVSAPFSPAKQQAAASAKQQAATPAKQTNIDFRKDGKNAGIIELAALGFAGQPDISQQHDHIIVTLKNHTLPTALQRSLDVADFKTPVQKVTLKRLNNDTQLIITTTGNWELVNKSAAPGYFTFQVLPKKQNLESGGVNNAPKTFTGRKISLDFQDVEIRTILQILAKESGMNIVASDSVSGKMTLSLKDVPWDQALDLVMQARNLDMRQQGNIVNMAPRRAACQRQSLLTSGKRHCRSGRAVFPKLPIEIQKCGRIPQHPALDNADTTGNRNTLVSGRGSVLIDPATNTLIVTDTRSVIEKFRKLIDELDVPAQQVMIEARIVEAADGFSRDLGVKFGATGRKKLKNETSAFGWGVNSGFGGGDKWEAKPKSTCRLPCRKQHFAGARDFSGALNLELSASESLSKTKTLANPRVLTQNRKEAKIESGYEIPFTVTTRSGGGNSTNTELKKAVLGLTVTANITPDGQIIMTVKINKDSPRQCASGNNTILCISTKSLNTQAMVENGGTLIVGGIYEENNGNTLTKVPLLATSPLSATSLKHSGKNRPPRTADFQLPPREL", "text": "FUNCTION: Required for type IV pilus biogenesis and competence. Could function as a pore for exit of the pilus but also as a channel for entry of heme and antimicrobial agents and uptake of transforming DNA. SUBCELLULAR LOCATION: Cell outer membrane. Note=Associated with the membrane through its C-terminus. SIMILARITY: Belongs to the bacterial secretin family. PilQ subfamily."}
{"protein": "MGSQVRLVIAVCGIYATFLTWSLAQEPLTTSVWPNSAARFSHSSFIVLCQALTAAVVGLCYLKAQRSGYGAREFIRKHWADVAGISLTQALSAPAANHSLQYVDYVGYMLAKSCKLLPIMLVHVLVYRTPIGRDKALVGVLVSGGVALFTLGGAERKQGEASLYGLGMLLVSLFLDGLTNASQDRLLRRPASKKITGAHLMVALNTAIVLWNLAYLVLFDRTQWQGSLQQLHADPAILTYLFTYCACGALGQCFVFFTLEHYSSLVLATVTVTRKMVSMLLSIVVYGHSVRPVQWLGILVVFGGIIWETVKKGQRGSGQKSKQH", "text": "FUNCTION: May be involved in specific transport of UDP-Gal from the cytosol to the Golgi lumen. Involved in the maintenance of optimal conditions for the folding of secretory pathway proteins in the endoplasmic reticulum (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily."}
{"protein": "MFRLNTLSALAELAVGSRWYHGASQPTQTKRRLMLVAFLGASAVTASTGLLWKKAHAESPPCVNSKKPDTEDKERNKDSGEVSSREGRAADAAAEPYPEDKKKKRSGFRDRKVMEYENRIRAYSTPDKIFRYFATLKVINEPGETEVFMTPQDFVRSITPNEKQPEHLGLDQYIIKRFDGKKIAQEREKFADEGSIFYSLGECGLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQRKLQHDVLKLEFERHDPVDGRISERQFGGMLLAYSGVQSKKLTAMQRQLKKHFKDGKGLTFQEVENFFTFLKNINDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRLMRGLEKPKDMGFTRLMQAMWKCAQETAWDFALPK", "text": "FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains (PubMed:24560927). MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium (PubMed:24560927). MICU1 acts both as an activator or inhibitor of mitochondrial calcium uptake (By similarity). Acts as a gatekeeper of MCU at low concentration of calcium, preventing channel opening (By similarity). Enhances MCU opening at high calcium concentration, allowing a rapid response of mitochondria to calcium signals generated in the cytoplasm (PubMed:24560927). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (By similarity). Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein Mitochondrion intermembrane space Note=The topology is subject to debate. SIMILARITY: Belongs to the MICU1 family. MICU1 subfamily."}
{"protein": "MADRVNASQGAAAAPTANGPGGVRNVVLVGPSGGGKTTLIEALLVAAKVLSRPGSVTEGTTVCDFDEAEIRQQRSVGLAVASLAYDGIKVNLVDTPGYADFVGELRAGLRAADCALFVIAANEGVDEPTKSLWQECSQVGMPRAVVITKLDHARANYREALTAAQDAFGDKVLPLYLPSGDGLIGLLSQALYEYADGKRTTRTPAESDTERIEEARGALIEGIIEESEDESLMERYLGGETIDESVLIQDLEKAVARGSFFPVIPVCSSTGVGTLELLEVATRGFPSPMEHPLPEVFTPQGVPHAELACDNDAPLLAEVVKTTSDPYVGRVSLVRVFSGTIRPDTTVHVSGHFSSFFGGGTSNTHPDHDEDERIGVLSFPLGKQQRPAAAVVAGDICAIGKLSRAETGDTLSDKAEPLVLKPWTMPEPLLPIAIAAHAKTDEDKLSVGLGRLAAEDPTLRIEQNQETHQVVLWCMGEAHAGVVLDTLANRYGVSVDTIELRVPLRETFAGNAKGHGRHIKQSGGHGQYGVCDIEVEPLPEGSGFEFLDKVVGGAVPRQFIPNVEKGVRAQMDKGVHAGYPVVDIRVTLLDGKAHSVDSSDFAFQMAGALALREAAAATKVILLEPIDEISVLVPDDFVGAVLGDLSSRRGRVLGTETAGHDRTVIKAEVPQVELTRYAIDLRSLAHGAASFTRSFARYEPMPESAAARVKAGAG", "text": "SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MAPSLLGGFTKSLAMTVLSEIGDKTFFAAAILAMRYPRKLVLAGCLTSLTVMTALSVSLGWVAPNLISRKWTHHVTTLLFFVFGILSLWEGFKEDGDSEELAEVEAELDANFKSNKAESKSKSKANDDKKKQQRPFVLQFFSPIFIKAFSITFFGEWGDKSQIATIGLAADENPFGVVLGGVLAQALCTTAAVMGGKSLASQISEKMVGLSSGVLFLLFGIMSYLSGPEGEL", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GDT1 family."}
{"protein": "MDAQLEWASSLVPKRQLQQQQQQEQQQQQQQDFHKDQLMTVGMRIRQRVDQGYASRTPSTSDASLQPGVIRDYSSVIVPQFTRSPLPTANSLPPMLINQRTMSTEASSLEKWDVAEPAAEHEAMVNGSKRRL", "text": "FUNCTION: Mediates the nuclear localization of RNR2 and RNR4, 2 subunits of the ribonucleotide reductase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DIF1/spd1 family."}
{"protein": "MTTHLVWFRQDLRLHDNLALAAACRNSSARVLALYIATPRQWATHNMSPRQAELINAQLNGLQIALAEKGIPLLFREVDDFVASVEIVKQVCAENSVTHLFYNYQYEVNERARDVEVERALRNVVCEGFDDSVILPPGAVMTGNHEMYKVFTPFKNAWLKRLREGMPECVAAPKVRSSGSIEPSPSITLNYPRQSFDTAHFPVEEKAAIAQLRQFCQNGAGEYEQQRDFPAVEGTSRLSASLATGGLSPRQCLHRLLAEQPQALDGGAGSVWLNELIWREFYRHLITYHPSLCKHRPFIAWTDRVQWQSNPAHLQAWQEGKTGYPIVDAAMRQLNSTGWMHNRLRMITASFLVKDLLIDWREGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIFNPTTQGEKFDHEGEFIRQWLPELRDVPGKVVHEPWKWAQKAGVTLDYPQPIVEHKEARVQTLAAYEAARKGK", "text": "FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. SIMILARITY: Belongs to the DNA photolyase class-1 family."}
{"protein": "MEMAESIPCNSVVGGNFKEVSPEKVIRFKPPLYKQRYQFVRDLVDRHEPKKVADLGCGDAKLLKLLKIYPCIQLLVGVDINEEKLHSNGHRLSPYLGEFVKPRDLDLTVTLYHGSVVERDSRLLGFDLITCIELIEHLDSDDLARFPDVVFGYLSPAMVVISTPNAEFNPLFPTVTLRDADHKFEWSRMEFQTWALHVANCYNYRVEFTGVGTPPAGSEHVGYCTQIGVFTKNGGKLSKPSVSQQCDQHVYKPVYTTSYPSLQQEKVLKFVLVGELLIQVDRLRLRYQRMLRDREKDRGPKPGDMDSCPAPHLLLGAVFTEAEKARIESSPKPFCEGEKFYIPLQRLLTYPKLHRLCADEDRVRSLIADSVCLSSDGSAVVVDLHNSWDYRPEEN", "text": "FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis. SUBCELLULAR LOCATION: Cytoplasm Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family."}
{"protein": "MNGEYDYEDGAQHQDGARESAVAGASNTNQISTSFFPPPPQVYKKFTKRNLRYLEILNSHKLADDEPSWDLLSVTQRLERQNAILRQPGSSSKIDAEQLQDEEADMAAIQDQDCDKPMTDLPDFDLKAELEPPNVDWIEEDGGYTVFGQLWPIPDVTPTLQQLGIPVLYPLEGTDRKELLLTLLRTLLQTYREITGDLLKPAQPYDVWVPAVPDPNLTPEQQQQQMATNPGFWTQTTEAKDRLKHMQNVVVNMQFLINELRPVQAKETLKLIMQMQLERRKQEMQLIQERCATMRARVEELKKMLGKQSDCYGSS", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 7 family."}
{"protein": "MTDLSTPDLPRMSAAIAEPTSHDPDSGGHFGGPSGWGGRYVPEALMAVIEEVTAAYQKERVSQDFLDDLDRLQANYAGRPSPLYEATRLSQHAGSARIFLKREDLNHTGSHKINNVLGQALLARRMGKTRVIAETGAGQHGVATATACALLGLDCVIYMGGIDTARQALNVARMRLLGAEVVAVQTGSKTLKDAINEAFRDWVANADNTYYCFGTAAGPHPFPTMVRDFQRIIGMEARVQIQGQAGRLPDAVVACVGGGSNAIGIFHAFLDDPGVRLVGFEAAGDGVETGRHAATFTAGSPGAFHGSFSYLLQDEDGQTIESHSISAGLDYPGVGPEHAWLKEAGRVDYRPITDSEAMDAFGLLCRMEGIIPAIESAHAVAGALKLGVELGRGAVIVVNLSGRGDKDVETAAKWFGLLGND", "text": "FUNCTION: The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. FUNCTION: The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. SIMILARITY: Belongs to the TrpB family. SIMILARITY: Belongs to the TrpB family."}
{"protein": "MAGKEEIIAKAKDSITEFDEEMAQEAANEALVAGLDPVEIIEHGYTAGMQYVGDQFEQGTLFLPHVLAAAEAMKAGIEVLQPEMEKRKAKTTTLGTVIIGTIEGDIHSIGKDIVASMLNIAGFEVVDLGRDVAIKTFVEKAKELKPDIVATSALMTTTMVNQIQLEEQLKEAGIRGQVKTMVGGAPVTQGWADKIGADIYGESATDAVNKIKAAIKS", "text": "FUNCTION: Acts probably as a methyl group carrier between MttB and either MtbA or MtaA. SIMILARITY: Belongs to the methylamine corrinoid protein family."}
{"protein": "MLTSSMPQNLSLFGFSPLKSSSFALILRPFSLYPPIFASSSPAPSRRPPRTAGYRRSGPSPPRRKWSSFEEQKRKGRSPMEKDKAISFNHSSDSFEFNKRRAEGLDKVDKPKKNLKRNTRTLNPTNTIAYVQILGTGMDTQDTSPSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLSRVCSETAGGLPGLLLTLAGIGEQGLSVNVWGPSDLKYLVDAMRSFIPRAAMVHTRSFGPSLNISDSAPQIGLSKPKDDAYVLVDDEVVKISAILLEPSRLEESGSKPGETAVIYVCELPEIKGKFDPKKAMALGLRAGPKYSYLQSGQSVKSDFKDITVHPSDVMGPSVPGPVVLLVDCPTESHAEELLSIPSMKTYYSCLDNSTDGAKLVNCIIHLSPASVTNSSTYRSWMKRFHSAQHILAGHEAKNMEFPILRASSRITARLNYLCPQFFPAPGFWSHQHDNNSINPTSLSKCFDSNLGESISAENLLKFTLRPHGNLGVDRSSIPSRLTALRVMDELLSEIPEISSKTEEIKQLWNGQHNKMMIEEPWLGESTVPSCLENIRRDDMEIVLLGTGSSQPSKYRNVTAIYIDLFSRGSILLDCGEGTLGQLKRRYGLEGADEAVRNLRCIWISHIHADHHTGLARILARRRELLKGLAHEPAIVVGPRSLKNFLDAYQRLEDLDMEFLDCRNTTTTSWASVETSRPEKNTSSGNAEGSLFSKGSLMQSIYKRPSSPLTDNSSALPFLKKLKKVLGEMGLEHLISFPVVHCPQAFGVSLKAAERKNIAGDEIPGWKMVYSGDTRPCPEMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKIPVIDESHMHNTCIAFDMMSINMADLHVLPKILPYFKTLFRNQVVEEEEEEEETDDDSLIRDKVPSFFIN", "text": "FUNCTION: Zinc phosphodiesterase, which displays tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'- trailer from precursor tRNA. Can process the mitochondrial tRNA-like structures (t-elements). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RNase Z family."}
{"protein": "MSNTAPGPTVANKRDEKHRHVVNVVLELPTEISEATHPVLATMLSKYTRMSSLFNDKCAFKLDLLRMIAVSRTRR", "text": "FUNCTION: Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the capsid protein VP5 and UL48A assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly. FUNCTION: Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the major capsid protein and small capsomere-interacting protein/SCP assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae small capsomere-interacting protein family."}
{"protein": "MVNLSIIISSSEVNGPGGLFDINATLPLVAIQFLLLMVLLNVILYSPLLTIIEERKEYILNKLAKASEILSQANELTAQYEQELNTVRKEAQLEITNSQKIHKEILEIELNISQKYIDNLLENITDDLLEKKNTALNSLDTIVQSLCVQIENRLSI", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "LTTLIPPKVASASNLGSNPAAKRMQHIVSFYSKLPRGEASFPKAKSPLGLYREKYFDTGSGAPLLHASLFFLAVGYGLEYYFHLSHHKEH", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27791192). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Part of the complex F(0) domain (PubMed:27791192). Minor subunit located with subunit a/ATP6 in the membrane (PubMed:27791192). SUBCELLULAR LOCATION: Mitochondrion inner membrane Note=The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix. SIMILARITY: Belongs to the ATPase F chain family."}
{"protein": "MKKRMLDVLMLVIGAFFFALAVNLFAIPNDLGEGGVTGITLILYYLFQWSPGVTNFILNAFLLLIGYKFLDGKTTVYTIIAVAANSLFLHLTHGWSIPSDELIINTIFAGVFAGVGIGMIIRVGGTTAGSAILARIANKYLDWNISYALLFFDLIVVFSSYFIIGAEKMMFTIVMLYIGTKVMDFIIEGLNTKKAITVISENKSEIAEQVNTLMDRGVTILSGKGNYTGQSKEILYIVINKQELSMLKKIIRSCDKKAFVIVHDVRDVFGEGFVDISK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0750 family."}
{"protein": "MGSRNSSSAGSGSLEPSEGLSRRGAGLRRSEEEEEEDEDVDLAQVLAYLLRRGQVRLVQGGGAANLQLIQALSDSEEEHDSAWDGRLGDRYNPPVDATPDTRELEYNEIKTRVELATGRLGLGRTAQEHSFPRMLHQRERGLCHRGSFSLGEQSRVMSHFLPNDLSFTDTYSQKAFCGIYSKDGQIFMSACQDQTIRLYDCRYGRFHKFKSIKARDVGWSVLDVAFTPDGNHFLYSSWSDYIHICSIYGEGDTHTALDLRPDERRFAVFSIAVSSDGREVLGGANDGCLYVFDREQNRRTLQIESHEDDVNAVAFADISSQILFSGGDDAICKVWDRRTMREDDPKPVGALAGHQDGITFIDSKGDARYLISNSKDQTIKLWDIRRFSSREGMEASRLAATQQNWDYRWQQVPKKAWKKLKLPGDSSLMTYRGHGVLHTLIRCRFSPAHSTGQQFIYSGCSTGKVVVYDLLSGHIVKKLTNHKACVRDVSWHPFEEKIVSSSWDGSLRLWQYRQAEYFQDDMTESDRNRVCSSGPAPVPCPSVAFSSPQ", "text": "FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex."}
{"protein": "MDWHSFRIAALLLTSLVVLEVNSEFQIQVRDHNAKNGTIKWHSIRRQKREWIKFAAACREGEDNSKRNPIAKIHSDCAANQPVTYRISGVGIDQPPYGIFIINQKTGEINITSIVDREVTPFFIIYCRALNAQGQDLENPLELRVRVMDINDNPPVFSMTTFLGQIEENSNANTLVMKLNATDADEPNNLNSMIAFKIIRQEPSDSPMFTINRKTGEIRTMNNFLDREQYSQYSLVVRGSDRDGGADGMSAESECSITILDVNDNIPYLEQSSYDITIEENTLHSQLLQIRVIDLDEEFSDNWKAIIFFISGNEGNWFEIEMNERTNVGTLKVVKPLDYEAVKNLQLCIGVRNVAEFHQSIISQYRLTVTLITVTVLNVVKGCVFQPGSKTFIVDSRMEANHTVGEFLATDCETGQATNKFKNVRYRYVMGNNPENLLVVDSGIITLRNRVTMEQYERLNKRYEGTVLSIHDSLQRTCTGTIIMVLCGFWTTTEHPTTSTEKPVTLSITPNVDNVHFGPAGIGLLIMGFLVLGLVPFLLISCDCGGAPGGGAGFEPVPECSDGAIHTWAVEGPQPGGITTICVPQMPPGNANVIEYIDNSGVYTNEYCGREMQDLGGGERTTGFELMDGVKTSAAPEICQEYSGTLRRNSMRECRDGGLNMNFMESYFCQKAYAYADEDEGRPSNDCLLIYDIEGVGSPAGSVGCCSFIEDLDESFLDTLGPKFKKLADISLGKEIDSYPDPDPSWPPQSTEPICPQHMEQLASGHPSISPHFGKTTVISENAYPSGPGVQHPMLIPDPLGYGNITVRESYTTSGTLKPSVHFHDNQQASNVVVTERVVGPISGADLHGMLEIPALRDGTNVIVTERVIAPGSSLPNSLTIPNPRETSNVVVTERVIQPTSGMIGNLSIPP", "text": "FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell junction, desmosome Cytoplasm Nucleus."}
{"protein": "MAESSGSWRDSYKGMSSDNIKGLVLALSSSLFIGASFIVKKKGLKKAASTGTRAGVGGYSYLYEPLWWIGMTTMLLGEIANFAAYAFAPAILVTPLGAVSIIISAVLAHIILREKLHIFGILGCALCVVGSTTIVLHAPQEREIDSVIEVWNLATEPAFMFYASLVIGAAVFLIIRFVPQYGQTNVMVYIGICSLVGSLSVMSVKALGIALKLTFSGTNQLFYPQTWIFTLVVLTCVVTQLNYLNKALDTFNTAIVSPIYYVMFTSLTILASVIMFKDWDRQNGTQIVTEICGFVTILSGTFLLHRTKDMVEGSSVILPLRISKHINEEEGIPLRRQESLRSP", "text": "FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome Note=Recruited to the cell membrane in response to low extracellular magnesium. SIMILARITY: Belongs to the NIPA (TC 2.A.7) family."}
{"protein": "MEGQPRGSRGPLEKPLPAATHPTLSSLGAVFILLKSALGAGLLNFPWAFYKAGGMLPTFLVALVSLVFLISGLVILGYAASVSGQTTYQGVVRELCGPAMGKLCEICFLTNLLMISVAFLRVIGDQLEKLCDSLLPDAPQPWYAAQNFTLPLISMLVIFPLSALREIALQKYTSILGTLAACYLALVITVQYYLWPQGLIRQPGPLLSPSPWTSVFSVFPTICFGFQCHEAAVSIYCSMWNQSLSHWTLVSVLSLLACCLVYTLTGVYGFLTFGPEVSADILMSYPGNDTAIIVARVLFAVSIVTVYPIVLFLGRSVMQDFWKKSYWATRGPPVLADPSGPWVRLPLTFLWVVVTLTMALFLPDLSEIISIIGGVSSFFIFIFPGLCLICAVDTEPMGPRVKCCLEAWGILSVLVGTFIFGQSTAVAMVELL", "text": "FUNCTION: Putative sodium-dependent amino acid/proton antiporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
{"protein": "MGPPPAARRREGEPDNQDPAGLLTDKYELTMLAAALRDGSANRPTTFEVFARRLPTGRRYGVVAGTGRLLEALPQFRFDADACELLAQFLDPATVRYLREFRFRGDIDGYAEGELYFPGSPVLSVRGSFAECVLLETLVLSIFNHDTAIASAAARMVSAAGGRPLIEMGSRRTHERAAVAAARAAYIAGFAASSNLAAQRRYGVPAHGTAAHAFTMLHAQHGGPTELAERAAFRAQVEALGPGTTLLVDTYDVTTGVANAVAAAGAELGAIRIDSGELGVLARQAREQLDRLGATRTRIVVSGDLDEFSIAALRGEPVDSYGVGTSLVTGSGAPTANMVYKLVEVDGVPVQKRSSYKESPGGRKEALRRSRATGTITEELVHPAGRPPVIVEPHRVLTLPLVRAGQPVADTSLAAARQLVASGLRSLPADGLKLAPGEPAIPTRTIPA", "text": "FUNCTION: Involved in the Preiss-Handler pathway, which is a recycling route that permits the salvage of free nicotinamide (NM) and nicotinic acid (Na) involved in the NAD biosynthesis. Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. It is not able to use nicotinamide. PncB1 contributes to basal NAD level (By similarity). SIMILARITY: Belongs to the NAPRTase family."}
{"protein": "MTVEDIFTGIAAYLRGFLAGAPPWVVTLAIGVLYLIGVLAFIFLNALYLIYLERKISAYMQQRIGPNRLGPHGLLQSVADAVKLLGKEDIIPRGADRWVFIIAPVLIFIPATMLYAVIPFGKGMVPADLNIGVFYFLAVASTTTIAILMGGWGANNKYALLGSMRCVAQMVSYEIPLTFSILGVIMLAGSLQTSQIVAAQGKIWYILLQPLAFIIYFIAATAEVNRAPFDLVEGEQEIIAGPYTEYTGMRYALFYLSEYANLVSVSALAVTLFLGGWQGPWLPSWLWFLIKVYIMIFIFMWVRWTFPRIRIDHLLSFNWKVLLPLSLANILVTGVGIKIYQLLTLGRW", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "MGESHAPSKPKLDGELCLRPSSSVFLGDQQLYFTQEYLRTNSLNLKYVVYFTACQFSGPIAVAYSPRPASWYIWIRTISGRILKRDMAFNEPVFMEWTRAHCLLVLNKAGRAHIFSSLGEKISEVIFDSQMSDVHECRTFATSRGDSGIAVMDVDGQVSVVNSVSEPVIWSMKPPYSEMPTAWTAFQPHSQLTHILLIFEAVFLMGCQGESLREQSHAASWVDSNTKYVKCVVDDARSRIAMMTESGKIQIVSIDLSTCFCTVEITDHDIAKCINFGWVGNSAVFVQMSPSLIVFVNVSARRKPGDEVQIYEKMTANAKISIEPDGIRLFESTQVEFVEAASREKIAVLNRNPNEDGAHLYKAAQEMSQGTGHNSFAASTVIQDLYKAIDDCISTACDTWQPEEQKLLLKAARFGMAYTNTTPDTTKLMRAIKEIRVLNELRMVRTGIPLTHRQFRAIGETCVINRLIDMGSYSVAIKVAQWLGGETSENVDRVLLEWVRRSISKVSKSNMKMDQPALEALDEKISAKLLQFPHVSIADAARRAIEAKLPELARLFIRRETDDANHVAVLLQLNDVSAALQKASASQRPQLIHQVVRHLMNSESRSSYELAISRIPLAQCLYQDLVRQEGETRGASSRQMLALLEQASDFERQTLFHFDVAETERNPDERLNALRRAKDAAKSMGDKAIEEILNDVSAFAPLQIQRGQADMSVRDTVIEMAHDTAKVAQLKQQARLTDKQVLLWTIEGLAKKGKMEQLFDLAQKRSPIGYAPFVKACVRYKRLDEIKKYFAKVNGYPDLVAAHLAMKNYVEAAKLAYDRRDRDVLHAVHMKSHEDPTQCPRVGQFLRSLDQN", "text": "FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways (PubMed:26783301). Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the rab-5-to-rab-7 endosome conversion probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion (By similarity). The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (By similarity). Within the HOPS complex, contributes to the normal development of gut granules in the adult intestine (PubMed:15843430, PubMed:24501423, PubMed:25273556). The CORVET complex is proposed to function as a rab-5 effector to mediate early endosome fusion probably in specific endosome subpopulations (By similarity). Required for recruitment of vps-33.1 to the HOPS complex (By similarity). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with vps-33.1 but not vps-33.2 (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Note=Cytoplasmic, peripheral membrane protein associated with late endosomes/lysosomes. SIMILARITY: Belongs to the VPS16 family."}
{"protein": "MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVKEMEQFVKKYKSEALGVGDVKLPCEMDAQGPKQMNIPGGDRSTPAAVGAMEDKSAEHKRTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSTCHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDSILAGEIYVMVNDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKRMS", "text": "FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth. FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Note=Detected along actin stress fibers. SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion Note=Detected along actin stress fibers. SIMILARITY: Belongs to the prickle / espinas / testin family."}
{"protein": "MSGNIAFGRFDDSFSAASLKAYVAEFISTLVFVFAGVGSAIAYTKLTGGAPLDPAGLVAVAVCHGFGLFVAVAIGANISGGHVNPAVTFGLALGGQITILTGVFYWIAQLLGAIVGAVLVQFCTGVATPTHGLSGVGAFEGVVMEIIVTFGLVYTVYATAADPKKGSLGTIAPIAIGFIVGANILVAGPFSGGSMNPARSFGPAVASGDYTNIWIYWVGPLVGGGLAGLVYRYVYMCGDHAPVASSEF", "text": "FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. May be involved in transport from the vacuolar compartment to the cytoplasm (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP (TC 1.A.8.10) subfamily."}
{"protein": "MTVQRILIVAGTHGNEINPIWAVKQFNRNENSLKHGIEYEYIIGNPIAYEKGCRYIDADLNRSFKKSKNYDQNENSFYEISRANFLVDQFGINGSKPCQIAIDLHTTTANMGTSIVMYGRRFKDFCLAALLQNKFGLPIYLHEKDKSQTGFLVEAWPCGLVIEIGAVAQNFYDPKIINRFLIIISSLRDEIDKLKKNLIELPKDLVVHVHQGSVDYPRDEKGDIDGLIHPKRINRDWKMIKKGDPLFLNSQGIIYKYDGDQFIWPVFIGEVAYKEKQIAMSYTNKEVICSKNEWVQEFHRL", "text": "SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily."}
{"protein": "MMPNSRSATITPTTESTTTTTTTTTTLTTSYWCYSCTRFISVWEDQDANAGVLCPYCNGGFIEEIEDSSNSTVAAIPASTPEVRSVEETHRSIIRRRRSNRRTSFNPVIVLHGGGGGGAGERVENEEGDGATRERRAYEFYYDDGSGSGLRPLPDSVSEILMGSGFERLLEQLSQIEASGNGIGRSGNPPASKSAIESLPRVEISDCHTKAEANCAVCTEVFEAGIEGREMPCKHIFHGDCIVPWLSIRNSCPVCRFELPSDPIQRSNEEEHAVGMTIWRLPGGGFAVGRFNAGVREGERILPVVLTEMDGGGLGSNEGPRRISWVRAHETPEMSRNGGRSGNGGRLRRAVRGMVSFMRRVRPSRGSSNSNVIDLDSDGETRVMNRSTSLIRRFF", "text": "FUNCTION: E3 ubiquitin-protein ligase involved in the positive regulation of abscisic acid-dependent drought stress responses (PubMed:22405823). Involved in the positive regulation of responses to salt and osmotic stresses during seed germination and early seedling development (PubMed:23951086). Possesses E3 ubiquitin ligase activity in vitro (PubMed:22405823, PubMed:23951086). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus."}
{"protein": "MQYLQFLSLVVLLLMCHARKSVYRRNSPSLRRLTRNYDWEVDEHGGLKPIINPAKVERATKNCANDSFILGTIMSNYNRHKIPGGQVDVEVEVWVQEITTISDITSDFQLDIYIYETWYDPALNYAFMNPCKYNLSLNSVLLEKLWTPNSCFINSKTADIHKSPFPNIFLMIYANGTVWTNYRLKLQGPCIMDLTKFPFDNVTCSLTFESFNYNTDEVKMDWSVNGVQKMRDKMELADYELVDIHKIRTTEEYPAGYWHELTMSFEFKRRAGWYILQAYLPTYLTICISWISFALGSKAIPARTMLGVNSLLAMTFQFGNIIRNLPRVSYVKAIDVWMLSCMTFVFCSLLELAWVGYLSREEEPTSAKCLQPSAQVAPKPCHPPPVQQNANNSSVHRRQKQPKNEEESALLSLRDNDYGYIPPGFGLNGNVANAMKSFSSSCSCEPTNVVNLMLDEAETIPTSTSSSLSRKQRREILAHKIDSVSVFMFPFLFVLFNIAYWQHYLRGY", "text": "FUNCTION: Probable component of a ligand-gated anion channel. Negatively regulates synaptic transmission and synaptic vesicle release in response to acetylcholine in cholinergic motor neurons. Role in synaptic vesicle release kinetics may be in association with the ligand-gated ion channel protein acc-4. SUBCELLULAR LOCATION: Presynaptic cell membrane; Multi-pass membrane protein Cell projection, axon Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family."}
{"protein": "MSFQQRFARALDVGYKNFLSKDAVRNIFAYDNHLRGLVQKECKIHQTPYRVPSDLMVQSASDPARANLFNYSSQLVNHDFFFSGLISPERPSADADLGAINLKPGIDASFGSFGELKSQMVDVGNSVFGDGWLWLVYSPEKSLFSLLCTYNASNAFLWGTGFPKFRTNAIVPLLCVNLWQYAYLDDYGLNGKKMYITKWWDMINWTVVNNRFQATRIESL", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS42 family."}
{"protein": "MDRVFSVEDISDQFWSPPAREDSSKLVMNRSDSEWAFQSFLQQASALESSQPLPSDPVPVAGDVKNPVEIPANVPVDSEDYQAYLKSRLDLACAAVALTRASSLKPQDSAALLDNGSQASNTSQLVSQVPPKGSGHDLSKEEDKEALAATATPLLPALQKKSAIQVKSTTSGSSRDHSDDDDELEGETETTRNGDPSDAKRVRRMLSNRESARRSRRRKQAHMTELETQVSQLRVENSSLLKRLTDISQRYNDAAVDNRVLKADIETMRAKVKMAEETVKRVTGLNPMFQSMSSEISTIGMQSFSGSPSDTSADTTQDGSKQHFYQPAPTSHMPAQDQKIQNGLLQVPPVDNLQQHSASGPVEGNKMERTSSMQRVASLEHLQKRIRGGVSSCEAQVSGKQ", "text": "FUNCTION: Binds to the G-box-like motif (5'-ACGTGGC-3') of the chalcone synthase (CHS) gene promoter. G-box and G-box-like motifs are defined in promoters of certain plant genes which are regulated by such diverse stimuli as light-induction or hormone control. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MTENMIVIYHNPDCGTSRNVLQLIEAAGYLPQVIEYVKEGWTKPQLLGLFAAADLTPRSALRTTKSPAAELNLLEETVTDAQILDAMVEYPILVNRPIVCTPKGVRLCRPSEVVLDLLDHWPSGPFAKEDGELIIDERGNRVYT", "text": "FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. Does not constitute the major arsenate reductase in cells: essential only in the absence of ArsC (AC P74313). SIMILARITY: Belongs to the ArsC family."}
{"protein": "MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGGGGAGGRDQLRGQTGFFPSPGGASRDGSGPGEEGKQRTLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSEKRRREQEEAAAPRGPPQVTPKASNPFEDEDDDEPTVPEIEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRARVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVRVAKEHCQQLGDIGLDLTFIVHALLVKDIQGALHSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPESTTSVV", "text": "FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Cell projection, growth cone Cell projection Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). Localizes at the leading edge of migrating cells (By similarity). SIMILARITY: Belongs to the EXO84 family."}
{"protein": "MGHFTFTGLCLLAMFLSLRGAECYTCPIDWLPKNGLCYKVFSKHKTWFDAEKYCRKFKPGCHLASLHSNADAVEFSEYISDYLTGRGHVWIGLRDTKKKYIWEWTDRSRTDFLPWRKNQPDHFNNNEFCVEIVNFTGYLQWNDDNCAALRPFLCQCKY", "text": "FUNCTION: Recombinant C-type lectin BML-1 is able to agglutinate erythrocytes. May be a calcium-dependent lectin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the true venom lectin family."}
{"protein": "MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETRNNNSLVPKYHPNFWMDGKWRCCSQLEKLATGCAQYDPTKNASKKPLPPTPEDNRRPLWEPEETVVIALYDYQTNDPQELALRRNEEYCLLDSSEIHWWRVQDRNGHEGYVPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTAGTYTVSVFTKAVVSENNPCIKHYHIKETNDNPKRYYVAEKYVFDSIPLLINYHQHNGGGLVTRLRYPVCFGRQKAPVTAGLRYGKWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKERPEDRPAFSRLLRQLAEIAESGL", "text": "FUNCTION: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation (PubMed:12186560, PubMed:12682224, PubMed:21725281). Required for TCR-mediated calcium response in gamma-delta T-cells, may also be involved in the modulation of the transcriptomic signature in the Vgamma2-positive subset of immature gamma-delta T-cells (By similarity). Phosphorylates TBX21 at 'Tyr-530' and mediates its interaction with GATA3 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily."}
{"protein": "MLALWSISFVLLCSWRLSYAQYEHLGFAIAYQEPEQDLYTPPELPADTPRIQLRLAGEKRKHNEGRVEVFYEGEWGTVCDDDFTIHAAQVICRELGYFEAISWSPSSKYGKGEGRIWFDNVHCKGKEKSLAQCESNGIGVSDCKHSEDVGVVCSDKRIPGFKFVNTLTNNINSLNIQVEDVRIRPILASYRKRIPVTEGYVEVKDGGKWKQICDDEWTQMNSRVICGMFGFPGQKRYNTRVYKMFARRRKPSYWDYTINCTGKEAHLSSCTLGHTLSNSTCEEGTPVVVSCIPGRAFAPTPMTGYKKAFRQEQPLVRLRGGAVVGEGRVEVLKNGEWGTICDDNWNLLAATVVCRELGFGSAKEALSGGQLGQGMGPVHMNEVQCSGFEKSVTECSFNMEKDSEGCSHEEDAGVKCNVPAMGFQQRLRLSGGRNPFEGRVEVLVERNGSLVWGTVCGEGWTTMEAMVVCRQLGLGFASNAFQETWYWPGAVNADAVVMSGVRCAGTEMSLSHCLHHGEYLSCPKGGGRFAAGVSCSETAPDLVLNPQVVEQTTYLEDRPMFMLQCAYEENCLASTSSATPANSPRRLLRFSSQIHNNGQSDFRPKISRENWVWHDCHRHYHSMEVFTHYDLLSTNGTKVAEGHKASFCLEDSECDEGIEKRYECANFGEQGITVGCWDTYRHDIDCQWVDITDVKPGDYIFQIVINPNYEVAESDYTNNIVKCRCRYDGHRIWMYNCHIGGSFSAETEDTFPGLINNQVTHR", "text": "FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2a for correct expression of Sox2 and for neural differentiation (PubMed:25959397). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane Nucleus Chromosome Endoplasmic reticulum Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. SIMILARITY: Belongs to the lysyl oxidase family."}
{"protein": "MNLMLITFNEFKTGISLNDTRAEHLVKILKLKDNDKFKFGILGEKNIYHCIYKKDKKLFFKKIFKVGESNKLKKLYVLIGMIRPIVAKRIIKELASIGTYKIIFFNTELTEKSYLNSKIFKNNDCEKHLIAGAMQGKITYLPKIKIIKNLKESLKYIQQENFEIKILLEKNSEKNLIDIEQINNAVIIVGPERGFTEKEKQLIAQYNFSPYSISTNTLRTETATIAASIITASKLINM", "text": "FUNCTION: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase RsmE family."}
{"protein": "MRLTQGTFSFLPDLTDEQINKQLTYIVSKGLSANVEYTDDPHPRNSYWELWGLPLFDVKDASAVMYEISSCRKAKPNYYVKVNAFDNTRGIESCVMSFIVNRPANEPGFLLQRQDFEGRTMKYSLHSYATEKPEGARY", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO small chain family."}
{"protein": "MRRNCCHVSFASTLKILNFVQAFIGVSIIIYSIWMLHEYSRHLPVDPPPSASSSSGTEIATSVSEPLKNPIDFVASIILGSNGGDHGFNLRSLDLPAPWFIYSFMAVGILVCIVTFIGFIAAEAINGCCLCFYSILKTLLILLEAALVAYIAIDRHWEKDLPYDPTGELSSLRAFIEENIDICKWVGIAVVAVQLLSLLLAMVLRAMVSTPKPELDEEEDDENPRSRTWDPLLGPQGNQAPAGSSKIENWSSRIREKYGLNQSPPVNPKG", "text": "FUNCTION: May be involved in the regulation of cell differentiation. FUNCTION: Promotes intracellular multiplication of tobamoviruses, probably being a component of the replication complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
{"protein": "MSREIEPLIVGRVIGDVLEMFNPSVTMRVTFNSNTIVSNGHELAPSLLLSKPRVEIGGQDLRSFFTLIMMDPDAPSPSNPYMREYLHWMVTDIPGTTDASFGREIVRYETPKPVAGIHRYVFALFKQRGRQAVKAAPETRECFNTNAFSSYFGLSQPVAAVYFNAQRETAPRRRPSY", "text": "FUNCTION: May form complexes with phosphorylated ligands by interfering with kinases and their effectors. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family."}
{"protein": "MSRRRHSDENDGGQPHKRRKTSDANETEDHLESLICKVGEKSACSLESNLEGLAGVLEADLPNYKSKILRLLCTVARLLPEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANNYNEAVYLVRFLSDLVNCHVIAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWVGKELYEKKDAEMDRIFANTESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLKKDRWQERHILRPYLAFDSILCEALQHNLPPFTPPPHTEDSVYPMPRVIFRMFDYTDDPEGPVMPGSHSVERFVIEENLHCIIKSHWKERKTCAAQLVSYPGKNKIPLNYHIVEVIFAELFQLPAPPHIDVMYTTLLIELCKLQPGSLPQVLAQATEMLYMRLDTMNTTCVDRFINWFSHHLSNFQFRWSWEDWSDCLSQDPESPKPKFVREVLEKCMRLSYHQRILDIVPPTFSALCPANPTCIYKYGDESSNSLPGHSVALCLAVAFKSKATNDEIFSILKDVPNPNQDDDDDEGFSFNPLKIEVFVQTLLHLAAKSFSHSFSALAKFHEVFKTLAESDEGKLHVLRVMFEVWRNHPQMIAVLVDKMIRTQIVDCAAVANWIFSSELSRDFTRLFVWEILHSTIRKMNKHVLKIQKELEEAKEKLARQHKRRSDDDDRSSDRKDGVLEEQIERLQEKVESAQSEQKNLFLVIFQRFIMILTEHLVRCETDGTSVLTPWYKNCIERLQQIFLQHHQIIQQYMVTLENLLFTAELDPHILAVFQQFCALQA", "text": "FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (PubMed:26382858). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SIMILARITY: Belongs to the NCBP1 family."}
{"protein": "MQREFVSGAGLGLRRALLEPLGAGDEVRVDFLEVAPENWIGIGGRLGRQFRELTERLPFLCHGLSLNLGGYAPLDMSLLRAIKGFIEQHGIRAYSEHLSACADDGQLYDLMPLPFSDESVRRVAERVRVVQDVLERPLIVENVSAYARLPGELEEVDFVRAVLEEADCQLLLDVNNVYVNACNFGFDAHAYIAAMPSRRIAYLHMAGHDEQGASLKIDTHGAPVCDPVWELLAHAYACHGERPTLLERDFNLPPLSELYAETDRIRELQRRSGEAQLRSLGYGT", "text": "SIMILARITY: Belongs to the UPF0276 family."}
{"protein": "MPAAPECRLSNHGRIMKCVTFLLLLPETLKKLKRASKHPGRLSVCYNILTLSLKKRMAAELYPVSDHATLQKSGAVMLSLPEKKRNVEPVSQTTASIATTPTTEQNINNNNVEIPSWHSAHPTLRERNALMFNNEQMADVHFIVGPPGESQRVPAHKYVLAVGSSVFCAMFYGDLAEGDSDIHIPDVEPAAFLILLKYMYSDEIELAPDTVLATLYAAKKYLVSALARACVGFLETSLEARNACVLLSQSRLFEEPELTQRCWEVIDAQAELALRSEGFSEIDLPTLESILHRETLNVKESVVFQAVLGWADAECRRQGLSPTSQNQRSVLGKALHLVRLPSMTLQEFADGAAQVDILTLEETHSIFLWYTAATKPSLGFPVNAREGLTAQRCHRFQSSAYRSNQWRYRGRCDSIQFAVDKRVFIAGLGLYGSSGGKAEYSVRIELKRQGVLLAQNLTKFVSDGSSSTFPVWFEHPVQVEQDAFYTVSAVLDGSELSYFGQEGMTEVQCGKVTFQFQCSSDSTNGTGVQGGQIPELIFYA", "text": "FUNCTION: Adapter protein for the cul3 E3 ubiquitin-protein ligase complex. Promotes the export of zbtb16/plzf from the nucleus to the cytoplasm and targets zbtb16/plzf for ubiquitination and degradation. Up-regulates neurog1 expression and antagonizes zbtb16/plzf, to promote neurogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Present mainly, but not excusively in the cytoplasm."}
{"protein": "MARYLELNPQNYSDEEYDYDSYNPFPNFEKNLASHYGTDFVPRINLDDFFLDDEDFEFCDDPLNCCFPDYLASLGEEEFIYEGDEPYIVLKHQLVSSTMWDDGTFTYPILPPFKTSSISYFLPKPGEVLHRCLMAVAKGMDPDLQVAVGTEFQFRAESDSSHPPDITTEDQGTVVATGPQPSAPAMATLATAATGTMPEEWKNFFSYYTTINWATTDETGKVLFVQNLAPRMNPFLDHIAKMYTGWSGSMEVRFTISGSGVFGGKVAAVLVPPGISTEGGTNLLQFPHVLVDARQTEPVIFTIPDIRTQLWHDMHDTSTSHLVILVYNDLVNPFQGGENGTSCTITVETRGGTDFEFHLLKPPTRKMIFGADPSRLIPRRSQFWEGNRLPGVITSFVCLPRMFQANRHFDCKRQTFGWSRPVHKGIEVRVDATNKDAANTTDIGIHVVTARNAIKSDIPDGWPDYYRTGEQVYNNTTQTFQEVKESVMGSAVPDSTATAMTWHHLPTVVFGHGTAVGSKTTNSKVLSGNFYAIGNFDQSGNIKLYPSYWIAKEQSAGGAPIGAYEDMVKRIDVLPTAQTTGGNFPVAFVSKFASSHNGNGVSVYNSQILTTSALLAQDVYDIGPNALAVFKIKGSGGYWFDLGISADGFSYVGGGNLNFSSLQFPLEATYVGMASLHNKLQYNLGGSATTL", "text": "FUNCTION: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to specific cellular receptor. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the caliciviridae capsid protein family."}
{"protein": "MPGAIDDHCPAQPGEEGTAFNVTMGYKYPPLCLGHATRCIHLETQVWAAYLLERLATGKWGHLVSGLSLCPLRQMKRGVIGDTPYFQYKPVGKLCPKNFEGPSKTLIWGDCVNSHAVVLKNDSYALVIDWAPKGYLKNTCSSGGGEFLEATYFISYWEDEDHHPTLHRWFGSFFTLKWEDKDITLHPQGLV", "text": "FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the beta type-B retroviral envelope protein family. HERV class-II K(HML-8) env subfamily."}
{"protein": "MAANKGINGGIKNHFIAFLGEFVGTFLFLFFAYGGTQTANQTSQKNPSIVASPDINQLLYIALIFGFSLTVNVWIFFRVSGGLFNPAVTIALCLVGVVGPVRSIFIFIAQVVASIAAAAAVRGLLPGDTVLFSCALAPGTSIAQGLFLEMFFTIELVFTILMLAAEKTKVTFVAPVGIGLSLFVAELMGVAWTGGALNPARAFGAEVIGGFRGYHWIYWLGPLMGAVLAAGFYKVIKFLNYEQVNGEQDLSAEEKQLKDEKKARKKEERRRKQNFAGLFQTGRMHHHHHANTRNATVNDAGDGRPNSAPPYTEPPAQQQTWPHSASTIRENEDFSRFAEMGSQDGIVITREQPAEQYRLSGERYVQDANAQNRAKTP", "text": "FUNCTION: Water channel required to facilitate the transport of water across membranes (Probable). Involved in conidiation (PubMed:26527167). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MDFDSPEEKEFPGLYASEAADAKSRKSKEESDFSEDHDHSKKDLLIGRRKDKKEKGKDRGYAALEGESSPEEELDTKSPSKSKKSKTFKFTSSKSKEKREKSRDKSEKDSKHAEEEPSVSHKVKEKERDKEKDRDEPKKKDKEEKRKEKDKKADKKDKKDKKSKQLSQQQDDVSAAEEVLALGYPVFGVSVSLATERSRCHDGVDIPLVVRDCIDFLQDHLKCEQIYKIEPIKTRLMHFKRLYNNREHDSAVDELNLPTACSLLKLFLRELPEPLLTTDLVARFEEVASHPKVTTQQAELQQLLEQLPKCNRTLLAWVLLHFDAVIQQERHNKLNAQSLAMLLSPTLQMSHRLMVALLCHCNNLFADVQLIKYVPPLTSTSPKLPDTPEDIQTELRKQDSLLSQIHSEMNAGFITKKREEQLWEVQRIITQLKRKLRTFEKKQEKTAEEVDNSSSAPPAVASEDTTDSKPAGTPAVSTNNSISQEEPKTDTLTPKDAPNDFTIDPSTGFILLPKSNPHRENLLRLQIEYDELMEWQNELKARIVAERNEVYRLKQLYEQQSINSQMASLASGSQAPPESDYERIIEHYTRENALLEHKKNMLGMELKEERRACIALQVELRLQQF", "text": "FUNCTION: Participates in receptor endocytosis during interphase, is also involved in mitotic processes when endocytosis is switched off."}
{"protein": "MIPVAEFKQFTEQQPAFKVLKPWWDVLAEYLTVAMLMIGVFGCTLQVTQDKIICLPNHELQENLSEAPCQQLLPRGIPEQIGALQEVKGLKNNLDLQQYSFINQLCYETALHWYAKYFPYLVVIHTLIFMVCTSFWFKFPGTSSKIEHFISILGKCFDSPWTTRALSEVSGENQKGPAATERAAATIVAMAGTGPGKAGEGEKEKVLAEPEKVVTEPPVVTLLDKKEGEQAKALFEKVKKFRMHVEEGDILYTMYIRQTVLKVCKFLAILVYNLVYVEKISFLVACRVETSEVTGYASFCCNHTKAHLFSKLAFCYISFVCIYGLTCIYTLYWLFHRPLKEYSFRSVREETGMGDIPDVKNDFAFMLHLIDQYDSLYSKRFAVFLSEVSESRLKQLNLNHEWTPEKLRQKLQRNAAGRLELALCMLPGLPDTVFELSEVESLRLEAICDITFPPGLSQLVHLQELSLLHSPARLPFSLQVFLRDHLKVMRVKCEELREVPLWVFGLRGLEELHLEGLFPQELARAATLESLRELKQLKVLSLRSNAGKVPASVTDVAGHLQRLSLHNDGARLVALNSLKKLAALRELELVACGLERIPHAVFSLGALQELDLKDNHLRSIEEILSFQHCRKLVTLRLWHNQIAYVPEHVRKLRSLEQLYLSYNKLETLPSQLGLCSGLRLLDVSHNGLHSLPPEVGLLQNLQHLALSYNALEALPEELFFCRKLRTLLLGDNQLSQLSPHVGALRALSRLELKGNRLEALPEELGNCGGLKKAGLLVEDTLYQGLPAEVRDKMEEE", "text": "FUNCTION: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:24790029, PubMed:26824658, PubMed:28193731). The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (PubMed:24790029, PubMed:26824658). Mediates efflux of amino acids, such as aspartate, in response to osmotic stress (PubMed:28193731). The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'- 3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (PubMed:33171122). Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (PubMed:24790029, PubMed:26824658, PubMed:28193731). Also plays a role in lysosome homeostasis by forming functional lysosomal VRAC channels in response to low cytoplasmic ionic strength condition: lysosomal VRAC channels are necessary for the formation of large lysosome-derived vacuoles, which store and then expel excess water to maintain cytosolic water homeostasis (PubMed:33139539). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane Lysosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=In the absence of LRRC8A, resides primarily in the endoplasmic reticulum (PubMed:24790029, PubMed:33139539). Requires LRRC8A for localization at the cell membrane or lysosome membrane (PubMed:24790029, PubMed:33139539). SIMILARITY: Belongs to the LRRC8 family."}
{"protein": "MIKNTIKKLIEHSIYTTFKLLSKLPNKNLIYFESFHGKQYSDNPKALYEYLTEHSDAQLIWGVKKGYEHIFQQHNVPYVTKFSMKWFLAMPRAKAWMINTRTPDWLYKSPRTTYLQTWHGTPLKKIGLDISNVKMLGTNTQNYQDGFKKESQRWDYLVSPNPYSTSIFQNAFHVSRDKILETGYPRNDKLSHKRNDTEYINGIKTRLNIPLDKKVIMYAPTWRDDEAIREGSYQFNVNFDIEALRQALDDDYVILLRMHYLVVTRIDEHDDFVKDVSDYEDISDLYLISDALVTDYSSVMFDFGVLKRPQIFYAYDLDKYGDELRGFYMDYKKELPGPIVENQTALIDALKQIDETANEYIEARTVFYQKFCSLEDGQASQRICQTIFK", "text": "FUNCTION: Catalyzes the addition of a second glycerol phosphate unit from CDP-glycerol to the prenolpyrophosphate-linked disaccharide, to complete the linkage unit. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase family."}
{"protein": "MTSFPTTPPPAEELMATTILQATEALSPEAEASTALIAVVITVVFLTLLSVVILIFFYLYKNKGSYVTYEPADGEPGAVVLMENDSAKGREKEEYFI", "text": "FUNCTION: May play a role in epithelial cell-cell contacts. May play a role in tumor invasiveness and metastasis formation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein Cytoplasmic vesicle membrane; Single-pass type III membrane protein Note=Predominantly on lateral parts of the membrane, at cell-cell epithelial junctions. Detected on cytoplasmic membranes in undifferentiated tumors. SIMILARITY: Belongs to the SMAGP family."}
{"protein": "MHLNKMKKVSLKTYLVLFFLIFFIFCSFWFIKPKEKKLKLEKLRYEEVIKKINAKNNQNLKSVENFITENKNIYGTLSSLFLAKKYILDKNLDKALIQLNNSLKYTKEENLQNILKIRIAKIKIQQNKNQDAIKILEEIKDNSWKNIVENMKGDIFMKNKEIKKAILAWKKSKYLEKSNASKEIINMKINEIKR", "text": "FUNCTION: May mediate protein transfer from the SecYEG translocon to the periplasmic chaperone network via its periplasmic C-terminal region. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the YfgM family."}
{"protein": "MQTSLANIVLFSSLQVLLSLTCFQEVVEAASGKGFGDNIHWRTLDDGKKEAEASGLPIMLIIHKSWCGACKALKPKFAESKEISELAHNFVMINLEDEEEPKDDAFSPDGGYIPRILFLDPSGKVHPEITNKNGNPNYKYFYSNAEQVISGMKEAQEKLTGDAFKQRHTGDEL", "text": "FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol- disulfide oxidase activity. May function as an important antioxidant, and may be involved in the responses to viral infection. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "RKRLFYRYYSHPGNYMYLGHYGRYYNMLHNCNAMLLAHQMQAMRRYQHRMRVKQMYRRIKMKQMYRHMKWMGMYRQAKAARLRCI", "text": "FUNCTION: Is lethal to drosophila larvae. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the turripeptide family."}
{"protein": "MIVNKKYFLLICIIILISINCLVLAKDEIENFLKEGDDLVSKGKYDLANENYSNAIDLIGSDTQHPQYVSLLFKRAGIYHQKGKNILALSDLNRAIEANPDNIHARLKRAKIQSSLGRFEEAMDEYKRVLKIRPDNSQAKQQIEKLKKVEQQLEKVRDMVKVEKNYKDSIAILLDIQSVVSDLKEVRLMLCECFFQQGDHRKVLDETMTILKSEPSSVAALYWRGKTFFSMGEKEIAMKFLKEGLKFDPDNTNCRAMIKTINKFEKSTANAQELFNQQKYQDALGQIEDALEIEPNSPTHSTPLYLLKCKCLLKVKKGKESIEACNRALELDELNADALYNRAEAYMYEEDYQKALNDYNKAREHKPNDPQIHDGIRRAQKAQQMAKRKDYYKILGIQKSATPEEIKKAFKKLAIKNHPDKSTETDKEKAQQIYMDINEAYEALKDEEKRKRYDMGEDINDPHGGQGGQGGGFGGFGGFHGFQGFQGFQQGGGGGGFQFHFR", "text": "FUNCTION: May be involved in the unfolded protein response (UPR) during ER stress. SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum lumen."}
{"protein": "MQAEFKLRSKILLQPLVLLHIIDAYERRPKDCTQVIGTLLGRNNPESGHLEISNCFTLLHKDYPNSDRIDVDLQYANDMYELNQLTYPQEKIIGWYATGKEVSRSAVNLHEYYARECADGNPMHLLIDTSLRGQRMMMRLYTAVVMGVPNGTKGLMFSLLPVEMSSGNPESVALNLMKKNALQPTKQVGRILPELVQVVDITRDLQTKLDLVLRYVNETLARKRTPNNTVGRALHDALTSVPLVDAESFRMMFNANVRDMLMSITLATMIKAQLKISESVIAMPDL", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit F family."}
{"protein": "MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIPINNIIVGS", "text": "FUNCTION: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (By similarity). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma family."}
{"protein": "MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA", "text": "FUNCTION: [Isoform 3]: Sequesters MAD2L1 in the cytoplasm preventing its function as an activator of the mitotic spindle assembly checkpoint (SAC) resulting in SAC impairment and chromosomal instability in hepatocellular carcinomas. FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (PubMed:10049595, PubMed:20133940, PubMed:29162720). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (PubMed:29162720). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Nucleus envelope Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=Co- localizes with TPR at the nucleus envelope during interphase and throughout the cell cycle (PubMed:22351768, PubMed:18981471). From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody (PubMed:9546394). Localizes to kinetochores during prometaphase (PubMed:22351768, PubMed:29162720). Does not localize to kinetochores during metaphase (PubMed:29162720). Colocalizes with NEK2 at the kinetochore (PubMed:14978040). Colocalizes with IK at spindle poles during metaphase and anaphase (PubMed:22351768). SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. SIMILARITY: Belongs to the MAD1 family."}
{"protein": "MMPPKPAAEDVADEQPEPPDEDPDVAEADPTGRYLRYREIIGSGSSKTVYKAFDAVDGIEVAWGKVEINERIMGSSKELQRLRTEIQLLKSLQHKHILKLYASWVDTNRRTVNIVTELFTSGNLREYRTKHKKVDMKAMRRWAKQILTGLEYLHSQKPPIIHRDLKCDNIFINGNHGKVKIGDFGLAMVMQQRKTRSIQGTIEFMAPELFGENYNELVDIYSFGMCMLEMVTCECPYSECKGFIQIYKKITEGVKPAALSKVKDAEVRGFIESCLASVSDRLPASELLKSPFLQSDDANHRSSNSVQEPVKFPENNFTKDEPIFVSLAPNNGTVNGKEQSFILVLQKSDFLLEGNMSTTNPVMLFLRFPGPDGKFKNVQFPFDMEKDTSLSVSTEMVEQLELPEWNNPVLAELIDAFLLHILPSWKPCVKVGKMLPSSS", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WNK subfamily."}
{"protein": "MVKEIDINKLLAQENNALNTILSQVNELCKQNKQLQGLIEIQNETKELEKEHNRSLPWFKRFVKTVSNVKYILIKSEEQLTNEAIKYNNKILKDIDNKIYNIAEKSAPLKQALQEEIEKNFKDLTKKDLSKDQRARLSEVFFSYKSKPERFSALHMTNPLQFINAEALEKQYNSLNATKQNIQNLISANSNIKELKEIQKQVAEIRAEVPHTFFEKLNNIWQNVKNVFVNNSEQVLAKNKESNTRTIRKIDEQLYKTKHKFEELIENKERNIKDIIAKLPDNEKLQKIVSNLTNHMASQKEPILANASLAKPLENNITPPSPLPENNIPSPPPPPPPSPLPENNIPSSPPPPPPPPLPENNIPSPPPPPPPPPPPPMAPAQAETLSKPIESTTVKKLANQPRPSIDTSDLMREIAGPKKLKKVEFDPNTGKPVAHSHSKPAQNVNALSGLESIFARRAVIKVSDSSSSESDSGNWSDVSVNRNKSKMLKTKGERDAKMTTHAQKINNRNSQNPSFVR", "text": "FUNCTION: Recruits and activates the Arp2/3 complex, which in turn leads to actin polymerization, promoting Rickettsia motility during infection. SUBCELLULAR LOCATION: Cell surface."}
{"protein": "MLDKNQLAKYKQDHLCEYEKIMSNNEKEALEEKVASLDLDFIAKLYNDLYINKKTIDDVSAVSEVKYDIKSQMSDDEIKRLEEQGLQAIKEGQFAVLLMAGGQGTRLGYKGPKGSFEIEGVSLFELQANQLKTLNHQSGHTIQWYIMTSDINHEETLAYFEAHSYFGYDQEAIHFFKQDNIVALSEEGKLILNQQGRIMETPNGNGGVFKSLDKAGYLEEMSNNGVKYIFLNNIDNVLVKVLDPLFAGFTVEHDYDITSKTIQPKPGESVGRLVNVDCKDTVLEYSELDPEVANQFNNANIGIHAFKLGFILNAVNRELPYHLAIKNLKQLDENFGVIEQPTLKFELFYFDIFTYGTSFVTLQVPREEEFSPLKNKEGKDSVATATEDLRRMGLI", "text": "SIMILARITY: Belongs to the UDPGP type 1 family."}
{"protein": "MPDSGTLGTPPPEQGPTPPTTLPDVPAPVIPSASVTSAASDFLAALHPPVTVPDPAPPPPPAPAAGNPPDTVTGDSVLQRILRGPTGPGTTSLAPAVRYGRQPGPEAPASAPPAAGRAVPGLYHHPVPEPDPVRVEEVSRRIKRWAEDEVQLYPEEWEGQFDGFSVGRYMVGCHPDAPTVDHLMLATRLMVAENAVDDCYCEDHGGSPVGLGGRLLLAHTAIDHFHSTAEYTPTWQASLAADAPRRAYDSAMGYFVRAATPSQSDRYRHDMARLHLGYLAEGAWAQTGHVPEVWEYLAMRQFNNFRPCPTITDTVGGYELPADLHARPDMQRVIALAGNATTIVNDLYSYTKELNSPGRHLNLPVVIAEREQLCERDAYLKAVEVHNELQHSFEAAAADLAEACPLPPVLRFLRGVAAWVDGNHDWHRTNTYRYSLPDFW", "text": "FUNCTION: Catalyzes the cyclization of 2-methylgeranyl diphosphate (2- MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the intermediacy of 2-methyllinalyl diphosphate. Is also able to catalyze the cyclization of geranyl diphosphate (GPP), albeit with much lower efficiency, leading to the formation of a complex mixture of cyclic monoterpenes, consisting of alpha-pinene (6%), beta-pinene (23%), limonene (32%), gamma-terpinene (29%), and delta-terpinene (10%). SIMILARITY: Belongs to the terpene synthase family. 2-methylisoborneol synthase subfamily."}
{"protein": "MDATLPSIHTALKILGPNNVSVSENTALPVIQPLDILVRVACISINHVDAKSADMSPSPGATSGTDFSGVVVAIGSDVPKESFRSTNGMKPVQIGDRVFGGVFGNNPLRRDNGAFAEYVAVPARLVWHIPGGMDFSTASTLGAAVATVGLSLFQYMQLPMPTTTSTASPDNGPFVLVYGGGTATGAMAIQVLKIAGFRPITTCSSASAGHATELGATATFDYRSPTCGAELREHTGDTLTLALDCITDTASMNICYEALGSSGGRYVALDSFPLRAHTRRSVVPDWVCTYSQFGHPIAWAAPYNLEARPEDLLTAEAWYVVAQKLIDQGLITPHPKEERLGGLAAIGEGMEAVRRGQIKGKKLVYPISNELCAAA", "text": "FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:30905148). IccB collaborates with the hybrid PKS-NRPS synthetase iccA to assemble the backbone of ilicicolin H (PubMed:30905148). The PKS portion of iccA and trans- acting enoyl reductase iccB work together to construct an octaketide, and two methyl groups are introduced by the MT domain of iccA during the chain assembly (PubMed:30905148). The nascent chain is then condensed with tyrosine, catalyzed by the iliA C domain, and the resulting PKS-NRPS hybrid is offloaded by the iliA RED domain to form an advanced tetramic acid intermediate (PubMed:30905148). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (PubMed:30905148) (Probable). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MKKKIKEVIVVEGKDDISAVKNAVDAEVFQVNGHAVRKNKSIEILKLAYENKGLIILTDPDYAGEEIRKYLCKHFPNAKNAYISRVSGTKDGDIGVENASPEDIITALEKARFSLDNSVNIFNLDLMMDYNLIGKDNSADLRSLLGAELGIGYSNGKQFMAKLNRYGISLEEFKKAYEKINMK", "text": "FUNCTION: Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease M5 family."}
{"protein": "MSTNNSVQPVSPASELLSNTTCQLEEDLSISFSIIFMTVGILSNSLAIAILMKAYQRFRQKYKSSFLLLASALVITDFFGHLINGTIAVFVYASDKDWIYFDKSNILCSIFGICMVFSGLCPLFLGSLMAIERCIGVTKPIFHSTKITTKHVKMMLSGVCFFAVFVALLPILGHRDYKIQASRTWCFYKTDQIKDWEDRFYLLLFAFLGLLALGISFVCNAITGISLLKVKFRSQQHRQGRSHHFEMVIQLLGIMCVSCICWSPFLVTMASIGMNIQDFKDSCERTLFTLRMATWNQILDPWVYILLRKAVLRNLYVCTRRCCGVHVISLHVWELSSIKNSLKVAAISDLPVTEKVTQQTST", "text": "FUNCTION: Receptor for prostaglandin F2-alpha (PGF2-alpha). The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "KRQQPGLWGRSADPQQAGLWGKRQQPGLWGRSADPQQAGLWGKRQNPGLWGRSADPQQAGLWGKRQHPGLWGRSADPQQAGLWGRSAGSGKRQERIGIWGRSAEPPQYKELEDLKQKSAIPKAKPQ", "text": "FUNCTION: Metamorphosin A may be part of an internal signaling system involved in control of metamorphosis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the LWamide neuropeptide family."}
{"protein": "MAGTSLGARFYRQIKRHPGLIPMIGFIGLGMGSAALYLLRLALRSPDVCWDRKNNPEPWNRLSPNDQYKFLAVSTDYKKLKKDRPDF", "text": "SIMILARITY: Belongs to the complex I NDUFA4 subunit family."}
{"protein": "MRNPKLKTLLAPTLLGLAIFAGTAQAAAPLRPPQGYFAPVDKFKTGDKSEGCDAMPTPYTGPLQFRSKYEGSDKARATLNVQSEKAFRDTTKDITTLERGTAKRVMQFMRDGRPEQLDCTLNWLTAWAKADALMSKDFNHTGKSMRKWALGSMASSYIRLKFSDSHPLAQHQQEAQVIEAWFSKMADQVVSDWDNLPLEKTNNHSYWAAWSVMATSVATNRRDLFDWAVKEYKVGVNQVDADGFLPNELKRQQRALAYHNYALPPLAMIASFAQVNGVDLRQENNGALKRLGDRVLAGVKDPDQFEKKNGKEQDMTDLKQDMKFAWLEPFCTLYTCSPDVIEKKHGMQPFKTFRLGGDLTKVYDPSHEKGNKGS", "text": "FUNCTION: Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the polysaccharide lyase 5 family."}
{"protein": "MPDQALQQMLDRSCWVCFATDEDDRTAEWVRPCRCRGSTKWVHQACLQRWVDEKQRGNSTARVACPQCNAEYLIVFPKLGPVVYVLDLADRLISKACPFAAAGIMVGSIYWTAVTYGAVTVMQVVGHKEGLDVMERADPLFLLIGLPTIPVMLILGKMIRWEDYVLRLWRKYSNKLQILNSIFPGIGCPVPRIPAEANPLADHVSATRILCGALVFPTIATIVGKLMFSSVNSNLQRTILGGIAFVAIKGAFKVYFKQQQYLRQAHRKILNYPEQEEA", "text": "FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1. FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Authors show that the protein can be detected in endoplasmic reticulum (PubMed:14722266). Authors (PubMed:16874301) show its presence only in mitochondria (PubMed:16874301). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein."}
{"protein": "MSYHEEERHGGNGLDWFEESMSSLLAADVDLAGGGGDAGGGGYAWWWAASPAAQQDDIGSVVAQTLSPPSTAAPAAASPSIASPAASSPSDVPSSSSKKRKSPAHRAPGHTGGKKGGGGKGGGGGSDRDMRWAEQLLNPCAVAVEAGNLSRVQHLFYVLGELESFSGDANHRLAAHGLRALARWLPAAVGPAAAAAVRVPPCSERPTTAFAAAEPRLFRASLIRFHEVSPWFALPNALANAAIAQASTCGAAGATPRPLHVVDLGVSHGVQWPTLLESLTRQPGGRAPPSVRLTVVGPGATATSPVAPFSASPPGYDFSPHLLRYAKSINLDLRISRAATLDDAVPGDDGEALVVCLQFRLGHAAAEERREVLRKARGLNPELVVLSELDSGVGVVGGDGGSAAGEFAARLELLWRFLESTSAAFKGKDVEERRLLEAEAGAILAAADVAAAGEGREGWRERMAAAGFEEAPFGAEAVESARSLLRKYDSGWEMSAPSPAAAAVALRWKGQPVSFCSLWRPAA", "text": "FUNCTION: Transcription factor involved in the control of strigolactone biosynthesis in roots through the activation of the beta-carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family."}
{"protein": "MNNQRKKTGRPSFNMLKRARNRVSTGSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWSSFKKNGAIKVLRGFKKEISSMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPTLIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITERQPDDVDCWCNATDTWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIGLFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKNKPTLDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDANFVCRRTFVDRGWGNGCGLFGKGSFLTCAKFKCVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTIATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNRVVLLTMKKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFAGHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVIDKEKPVNIEAEPPFGESYIVVGSGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIFGTAYGILFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGKELKCG", "text": "FUNCTION: [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side Note=Located in RE-derived vesicles hosting the replication complex. SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane; Multi-pass membrane protein Host endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane; Multi-pass membrane protein Host endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [Peptide pr]: Secreted. SUBCELLULAR LOCATION: [Capsid protein C]: Virion Host nucleus Host cytoplasm Host cytoplasm, host perinuclear region."}
{"protein": "MAVQKHTVALFLAVALVAGPAASYAADAGYAPATPATPAAPATAATPATPATPATPAAVPSGKATTEEQKLIEKINAGFKAAVAAAAVVPPADKYKTFVETFGTATNKAFVEGLASGYADQSKNQLTSKLDAALKLAYEAAQGATPEAKYDAYVATLTEALRVIAGTLEVHAVKPAAEEVKVGAIPAAEVQLIDKVDAAYRTAATAANAAPANDKFTVFENTFNNAIKVSLGAAYDSYKFIPTLVAAVKQAYAAKQATAPEVKYTVSETALKKAVTAMSEAEKEATPAAAATATPTPAAATATATPAAAYATATPAAATATATPAAATATPAAAGGYKV", "text": "SUBCELLULAR LOCATION: Note=Starch granule. SIMILARITY: Belongs to the Poa p IX/Phl p VI allergen family."}
{"protein": "MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSFDNEQLFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV", "text": "FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine- protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane Endosome Nucleus Note=Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily."}
{"protein": "MSGTTETQLRDLLSSMHLRHRFLGVFDKSFPGFLDPHVPASAIVNTGSRASGGMHWIGFAFDPAAGRCYMFDPFGWSDQKLWELYRVKYNAFMRRTGLRQPDRCFTLVRSTEAVQCPCSAACGLFSALFIVSFDRYRSKPMDGNPVIDTVVGVKHENMNSPPYRDILHRNQERTYYWWTKNSAYFRAHQEELRRETALNALPENHV", "text": "FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18. SUBCELLULAR LOCATION: Virion Host nucleus Note=Present in about 10 copies per virion. SIMILARITY: Belongs to the peptidase C5 family."}
{"protein": "MISFSSITDSPKLNLDDVSDWYITNTIIKDPPKGITTRRIIKVGEDNDLLNAEDDSTDRNDAILQFARNVNPMVSVQYNNTGLGFGRSSNEAFLPYRIIKDGAFRPPIVDLRDLMPLSRQPRNTTSINTSAEFIDFSKGIKPSENALKRNEVLNTLKTIPMCSNKGYNFKTGIDQPYDVVYHIEDKPQRIKQALYEYTEDNIGRNVIDGVTQNIYEGFVSPETNKTFSTFRDETSGMVEGFSGRIPISKNDSNWQQHPHMQFKNLQNVTIATNANGNVTKDNISRVEKDRERNLPLYSVKTHKIYKGLHVNYLNGQEDRTCTTGMINPKKQRQTYSYGNNGQGGGGGNKPITIKIREQNNLGYGFNAIRDNEGVKINY", "text": "SIMILARITY: Belongs to the IIV-6 329R family."}
{"protein": "MSKGIKMHNSVMRLTIPNKKIINYAPHIVTSIILFFICQQLAQLTWKIILPVNFTDNALSSADMTSPAAPSAETALPRFTLFGLAEKTSASAPGGNLDQAPVSALRLRVTGLLASTDPSRAIAIMMKGNQQVSLGIGDNTPGGEAKIIAISPDRLIVNYRGRNEAIPLFNDPPAVGKNSAAPPARHLAQELRAQPQNILHYLNISPVMVNDKLSGYRLNPGKDPALFRQSGLRENDLAIALNGLDLRDKEQARQVLAQLPELTEITLTVERDGQKNDIYLALRDE", "text": "FUNCTION: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of pullulanase. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP C family."}
{"protein": "MAPTFQTALFFTIISLSFAAPNAKQVRWCAISDLEQKKCNDLVGSCNVPDITLVCVLRSSTEDCMTAIKDGQADAMFLDSGEVYEASKDPYNLKPIIAEPYSSNRDLQKCLKERQQALAKKMIGHYIPQCDEKGNYQPQQCHGSTGHCWCVNAMGEKISGTNTPPGQTRATCERHELPKCLKERQVALGGDEKVLGRFVPQCDEKGNYEPQQFHGSTGYSWCVNAIGEEIAGTKTPPGKIPATCQKHDLVTTCHYAVAMVKKSSAFQFNQLKGKRSCHSGVSKTDGWKALVTVLVEKKLLSWDGPAKESIQRAMSKFFSVSCIPGATQTNLCKQCKGEEGKNCKNSHDEPYYGNYGAFRCLKEDMGDVAFLRSTALSDEHSEVYELLCPDNTRKPLNKYKECNLGTVPAGTVVTRKISDKTEDINNFLMEAQKRQCKLFSSAHGKDLMFDDSTLQLALLSSEVDAFLYLGVKLFHAMKALTGDAHLPSKNKVRWCTINKLEKMKCDDWSAVSGGAIACTEASCPKGCVKQILKGEADAVKLEVQYMYEALMCGLLPAVEEYHNKDDFGPCKTPGSPYTDFGTLRAVALVKKSNKDINWNNIKGKKSCHTGVGDIAGWVIPVSLIRRQNDNSDIDSFFGESCAPGSDTKSNLCKLCIGDPKNSAANTKCSLSDKEAYYGNQGAFRCLVEKGDVAFVPHTVVFENTDGKNPAVWAKNLKSEDFELLCLDGSRAPVSNYKSCKLSGIPPPAIVTREESISDVVRIVANQQSLYGRKGFEKDMFQLFSSNKGNNLLFNDNTQCLITFDRQPKDIMEDYFGKPYYTTVYGASRSAMSSELISACTIKHC", "text": "FUNCTION: Binds specifically to the neurotoxin saxitoxin. Its physiological role may be to transport or sequester an endogenous organic molecule other than Fe(3+). It may participate in a detoxification mechanism for neutralizing a microbial toxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the transferrin family."}
{"protein": "MQTPKRRRGAQGCPRSSPSPPLLLLVRAVWFCAALSVAAGSFELTILHTNDVHARVEQTSRDSGKCTGQDCYGGVARRATKIRELRAKHRHVLLLDAGDQYQGTVWFNFFKGREVVKFMNSLRYDAMALGNHEFDNGLAGLLDPLLKHANFPILSANIRPKGSIASNISGYILPYKIINVGSEKVGIIGYTTKETPVLSNPGPYLEFRDEVEELQNHANKLTTLGVNKIIALGHSGFSEDQRIARKVKGVDVVVGGHTNTFLYTGSPPSTEVAAGNYPFMVQSDDGRQVPVVQAYAFGKYLGYLNVIFDDKGNVIKSSGNPILLNKDISEDQDIKAEVNKMKIQLHNYSSQEIGKTIVYLNGTTQACRFHECNLGNLICDAVIYNNVRHPDDNEWNHVSMCIVNGGGIRSPIDERTNNGTITLEELTAVLPFGGTFDLLQIKGSALKQAFEHSVHRHGEGMGELLQVSGIKVVYDLSRKPGSRVLSLNVLCTECRVPTYVPLEKEKTYKLLLPSFLAAGGDGYHMLKGDSSNHSSGNLDISIVGDYIKRMGKVFPAVEGRMIFSAGTLFQAQLFLTWGLCVSLLYFIL", "text": "FUNCTION: Hydrolyzes nucleotides into nucleosides (By similarity). Snake venom 5'-nucleotidases are widely distributed among venomous snake taxa, but there is a lack of information about their biological activities. They have been shown to inhibit platelet aggregation. This effect may be due to the liberation of inhibitory AMP or adenosine by its action on ADP released upon initiation of aggregation. Venom 5'- nucleotidases are also known to synergistically act in vivo with other toxins like ADPases, phospholipases, and disintegrins to exert a more pronounced anti-coagulant effect. SUBCELLULAR LOCATION: Membrane; Lipid- anchor, GPI-anchor. SIMILARITY: Belongs to the 5'-nucleotidase family."}
{"protein": "MGSGAGNFLKVLLRNFDVLAGPVVSLVYPLYASVQAIETQSHADDKQWLTYWVLYSLLTLIELTFAKLIEWLPIWSYMKLILTCWLVIPYFSGAAYVYEHFVRPVFVNPRSINIWYVPKKMDIFRKPDDVLTAAEKYIAENGPDAFEKILSRADKSKRYNKHEYESYETMYGEGYQY", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DP1 family."}
{"protein": "MPKRVLKGAAKRAREAKHARDAAKARRLSSFLNVRLNQEHIPHEILPNSASDDKLLDRPVTGADLFAPSSGPSSNSVYPSLLQEEYFWNYFWQTYHVSLCPILDDAQFKQHYQSLLIADGKGRKPSALVDIVVAACMQYHISTLPLGSQSGLVEGKDASVAGRWHYWRGQTLLTYELESLSISTLQCHVLCSIYLCGGSFHNMMDTAMAQAVRTAYILGLHRDLPSTLPEAKREMRRRLWWTVYFMDTRATMKLGRSFMLSESHSMPALCIDSLRVAASSGSTFVPADEDMTWLSFNLRQITLCRTFRAAYTSFHNTDFHLQEGQPIWDRPDALQAGAEIIAKHIPSLDAWCDSVPDALKLKRQDSNSRPFSTDGARVVLELSAPEWLQRQRMLLENTYHHVCVNLFRSMICFPYQPASQVHISENSLPGELATRCAAHAIALTKLTHQVLEETSLLDGWHEAFYCQWDAVMTLIGFVLAYPGSGTVTLEAKSAIHLAIAVSENFGFKFAVGTSASKIVQGLCAKSETLTANEYASAYIGASTQNANIYRIYGGQICGVIDWQNS", "text": "FUNCTION: Transcription factor that regulates specifically the 4'- methoxyviridicatin/aspoquinolone biosynthesis cluster (PubMed:25251934). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MFYTNMETVHNCFNDATITGDEIIDILAFLQSDESDNPSGINEVVPVDDKKRRRTISNRESAKRSRMKKKKRFEELTEEVNRLNIRNQELKNRLANVVSCGNFISRENNRLKTESVCLEIRLLELYRFLVAMQSPISTSVNYITTLEI", "text": "FUNCTION: Probable transcription factor involved in somatic embryogenesis. Acts as positive regulator of BHLH109. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKKILERSMEGSGTWQGLVLVGIVTWICASSYLKFTHKFRSLLQPWVARQVVGGVPLILRIQKCQNGVLDAFFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDNAMEYGLPSSHTLNTVCLSGYLLHYVLSSLEYESVSIQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLWLTVNEKLDDFITSKQNVSSFWTALSFLLLFAYPTPEHPTPSYEYHTAFNGVTLGIVTGVQQTYSQFHHEAAPRIFSPELPISSYLGRVMVGIPTILLVKFCSKSLAKWTLPMVSNALGIPIRSSMYIPKLKGYASGKKTDEPKNSVGYLQKLCEFLSHDSFDIDTGIRFFQYAGLAWSVVDLVPSLFSYVNL", "text": "FUNCTION: Functions as sphingoid long-chain base phosphate (LCBP) phosphatase. May play a role in the regulation of LCBP levels and be involved in stomatal responses through LCBP-mediated ABA signaling. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family."}
{"protein": "MPAAGSEPSRPPSPPGVQEQSAEPRPPPPPHGELQYLGQIEHILRCGFRRDDRTGTGTLSVFGMQARYNLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDGLGFSDRAEGDLGPVYGFQWRHFGAEYKDMDSEYSGQGVDQLQKVIDTIKTNPNDRRIILCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITDLKPGDFVHTLGDAHIYLNHIEPLKTQALMELRGQSSRSLDGDGQAGTSRWAPVATDTERDRCCELQREPRPFPKLKILRKVETIDDFQAEDFQIEGYNPNPTIKMEMAV", "text": "FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine 5'- monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1- carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway. SUBCELLULAR LOCATION: Nucleus Cytoplasm Mitochondrion Mitochondrion matrix Mitochondrion inner membrane. SIMILARITY: Belongs to the thymidylate synthase family."}
{"protein": "MAGVCDAAAPGEGGGGGADGPERTGRGEAEQPGGGGHGPAPQHTETLGFYESDRRREKRRGRAELSLLRFLSAELTRGYFLEHNEAKYTERRERVYTCMRIPRELEKLMFFGIFLCLDAFLYVFTLLPLRVFLALFRLLTLPCYGLRDRRLLQPAQVCDILKGVILVICYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYVLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDIVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVARRMGFIPLPLAVLLIRVVTSSIKVQGILSYACVILFYFGLISLKILNSIVLLGKSCQYVKEAKMEEKLFNPPPASTPGKPSSKSQSKGKPSQGLSTEENLSASVTSQPGHQKENVIPLLVTSNSDQFLTTPDGDEKDITQENSELKHRSSKKDLLEIDRFTICGNRID", "text": "FUNCTION: Plays a role in primary cilia formation (By similarity). May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). May be involved in cartilage and bone development (By similarity). May play a role in the differentiation of cranial neural crest cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, cilium basal body Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TAPT1 family."}
{"protein": "MARHETSFPEILDVAALRARCDFIASAHAEQREPMRRALLAAFKEANIAGRAKARELLAADGAGIKCAERISWLQDQLITLLHDFVLNQVFDAAKAPETSRIAVTAVGGYGRGTLAPGSDIDLLFLLPAKKAVWAEPAIEFMLYILWDLGFKVGHATRTIEDCIRLSRADMTIRTAILECRYVCGSVALASELETRFDHEIVRNTGPEFIAAKLAERDERHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWISKYFYRVKDSADLVKLGVLSRQEYKLFQKAEDFLWAVRCHMHFLTGKAEERLSFDIQREIAEALGYHDHPGLSAVERFMKHYFLVAKDVGDLTRIFCSALEDQQAKDAPGISGVISRFRNRVRKIPGTLDFVDDGGRIALASPDVFKRDPVNLLRMFHIADINGLEFHPAALKQVTRSLSLITPHLRENEEANRLFLSILTSRRNPELILRRMNEAAVLGRFIPEFGKIVSMMQFNMYHHYTVDEHLLRAVDVLSRIERGLEEEAHPLTAMLMPAIEDREALYVAVLLHDIAKGRPEDHSVAGAKVARKLCPRFRLSPKQTETVVWLVEEHLTMSMVAQTRDLNDRKTIVDFAERVQSLERLKMLLILTVCDIRAVGPGVWNGWKGQLLRTLYYETELLLSGGFSELSRKERAKHAADMLEEALADWPKEERQTYVRLHYQPYLLTVALDEQVRHAAFIREADAAGRTLATMVRTHDFHAITEITVLSPDHPRLLTVIAGACAAAGANIVGAQIHTTSDGRALDTILVNREFSVAEDETRRAASIGKLIEDVLSGRKKLPDVIASRTRSKKRSRAFTVTPEVTISNALSNKFTVIEVEGLDRTGLLSEVTAVLSDLSLDIASAHITTFGEKVIDTFYVTDLVGSKITSENRQMNIAARLKAVLAGEVDEARERMPSGIIAPTPVPRASHGSKATKAET", "text": "FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism. SIMILARITY: Belongs to the GlnD family."}
{"protein": "MERLPHGRRDRSGGCRPHLAPGRAAAPASAARSVSSGIPVSATFLRPPGLFLRSTASSGRAGCAPGPGLDRALGAVGCGYPRTPKCARCRNHGVVSALKGHKRFCRWRDCACAKCTLIAERQRVMAAQVALRRQQAQEESEARGLHRLLYQGSSGSGAQASGGSGRTESPQVLNNPMAVAVLGAGASRHPGSRSVPTFEVFQQDYADRKQEPKQRNCESCQSRQEEPVSNTHHHSLGSSKGNVTVEKQGFMSSIPEHPDKSTIILSPCPTDQSGGEDSPRSFSSSDLESGNESEWARDYIATRASLSTVTSRPRDPLGILTRIFPGYKHSRLEGILQFCKGDVVQAIEQILNGREHKPDCRDLARADLENAAFQRASDFSLAGIGFGTLSNKSALSPLEAASAAYGGDSTLYSFNPRLAFSPLRLAYSSPGRALSGFVSPYLTPGLVPALPFRPTLDYAFPGMIREPSHLPSKHLVAGGRLYFRPNQEHL", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DMRT family."}
{"protein": "MAHSAEPSSSLSFTSSPHLSNGSISHNLSCSGSESVPSLEVISLSKLSSSLEQLLIDPGCDYSDADIVVEGIPVGVHRCILASRSGFFRELFKREKGSSGKEDRPKYCMSDFLPYGDVGYEAFLVFLSYVYTGKLKPSPVEVSTCVHNVCAHDACRPAINFVVELMYAASIFQMPDLVSIFERRLLNFVGKALSDNVVPILLVAFHCQLNQLIDQCVDRVARSDIDDISLEKGLPDEVVKKIKILRRNYQQDSDPNLPPADPLHEKRIRRIHKALDSDDVELVKLLLTESNITLDEANALHYAAAYCDPKVVTEVLALGLADVNLRNSRGYTALHIAVMRKEPSIIVLLLTKGARASELTSDGQSAVSICRRLTRPKDYHSKTEQGQEANKDRICIDVLEREMRRNPMAGDASISSQIMPDDLHMELLNLENRVALARLFFPAEAKLAMVIAHAETSEFAAPSSSKGSSGNLMEVDLNETPTVQNKRLHSRLEALMKTVRLGRCYFPHCSEVLDKFIDDDLPHLFYLEPGSSDEQKVKRRRFMELKEEVQKAFDKDKAECNLSGLSSSSSTTSPEKIGANQKVREP", "text": "FUNCTION: Probable component of the salicylic acid (SA) defense signaling pathway and pathogen-induced systemic acquired resistance (SAR) (Probable). May be involved in disease resistance against fungal pathogens (Probable). May be involved in tolerance to salt and osmotic stresses (PubMed:24407603)."}
{"protein": "MGKGTPSFGKRHNKSHTLCNRCGRRSFHVQKKTCSSCGYPAAKTRSYNWGAKAKRRHTTGTGRMRYLKHVSRRFKNGFQTGSASKASA", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family."}
{"protein": "MLSASRRALQLLSSANPVRRMGDSASKVISAEEALPGRTEPIPVTAKHHVSGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGHTRNPTYKEVCSEKTGHAEVVRVVYRPEHISFEELLKVFWENHDPTQGMRQGNDFGTQYRSAVYPTSAVQMEAALRSKEEYQKVLSKHNFGPITTDIREGQVFYYAEDYHQQYLSKNPDGYCGLGGTGVSCPMAIKK", "text": "FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Membrane; Lipid- anchor. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family."}
{"protein": "MGKRRNRGRSQMLSTMTKKQKKHLRDFGEEHPFYDRVSKKEAKPQICQLPESSDSSHSESESESEQEHVSGYHRLLATLKNVSEEEEEEEEEEEEEEEEEEEEEEEEEDDSAVGDAEMNEEAGSEDGSVGEAAVSEAAEEAAETQEHMSLADNSKEKDGEEPPGVSQKSSEEFTDVKHESLFSLETNFLEEDSGGSCSQRPSQDPFQQHVNKELKEKEIQAAASSPPATQQLKWPVLGHLVFSSKFQKTETFKPPKDIDLKLLHLQKPLESTWAKTNSQFLSGPQKSNSSFTPLQKELFLIMNSYRDLFYPERTALKNGEEVRHVYCLHAINHVLKANAQVLANNSRRRSQKLGVGEDDDFRDQGLTRPKVLIVVPFREAALRVVQLFISLLEGDSKKKIIVSNKKRFQGEYGSDPEERPPNLKRPEDYEAVFVGNIDDHFRIGVAILQRSIRLYAPFYSSDILIASPLGLRTIIGGEGEKKRDFDFLSSVELLIIDQADIYLMQNWEHVLHLMNHMNLLPLDSHGVDFSRVRMWSLNNWSKYYRQTLLFGALQDAQINSVFNKHCINAQGQVAVRNVPMTGSISHVLVQLPHVFQRMEAQDLSSVIDARFHFFINKILPQYRDAVMSHTLIYVPSYFDFVRLRNYFKKEELNFTHICEYTQKSGISRARHFFLQGEKQFLLLTERFHFYKRYTIKGIRNLIFYELPTYPHFYSEVCNMLRATSRGEEATWTCTVLYSKYDAQRLAAVVGVERAAQMLQSPKNVHLFVTGEK", "text": "FUNCTION: Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver (PubMed:29262616, PubMed:32303961). Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP25 family."}
{"protein": "MEPRAVADALETGEEDVVMEALRAYNRENSQSFTFDDAQQEDRKRLAKLLVSVLEQGLPPSRRVIWLQSIRILSRDRSCLDSFTSRRSLQALACYAGISASQGSVPEPLNMDVVLESLKCLCNLVLSSPVAQALAAEAGLVVRLAERVGLCRQSSFPHDVQFFDLRLLFLLTALRTDVRQQLFQELQGVRLLTRALELTLGMTEGERHPELLPPQETERAMEILKVLFNITFDSIKREVDEEDAALYRHLGTLLRHCVMLAAAGDRTEELHGHAVNLLGNLPVKCLDVLLTLEPHEGSLEFLGVNMDVIRVLLSFMEKRLHQTHRLKESVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGELLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTDEYKEAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSRHRVIQPMGMSPRGQLTSLQDAMCETMEGQLSSDPDSDPD", "text": "FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)- alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Colocalizes with RIC8A in CA2 hippocampal neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane (By similarity). SIMILARITY: Belongs to the synembryn family."}
{"protein": "MSVALLWVVSPCDVSNGTGFLVSVREGNRIFDSSGRRNLACNERIKRGGGKQRWSFGSYLGGAQTGSGRKFSVRSAIVATPAGEMTMSSERMVYDVVLRQAALVKRQLRSTDELDVKKDIPIPGTLGLLSEAYDRCSEVCAEYAKTFYLGTMLMTPERRKAIWAIYVWCRRTDELVDGPNASHITPAALDRWEDRLEDVFSGRPFDMLDAALSDTVSKFPVDIQPFRDMIEGMRMDLRKSRYRNFDELYLYCYYVAGTVGLMSVPIMGIAPESKATTESVYNAALALGIANQLTNILRDVGEDARRGRVYLPQDELAQAGLSDEDIFAGRVTDKWRIFMKKQIQRARKFFDEAEKGVTELSAASRWPVLASLLLYRRILDEIEANDYNNFTKRAYVSKPKKLIALPIAYAKSLVPSTRT", "text": "FUNCTION: Catalyzes the two steps reaction converting geranylgeranyl diphosphate to phytoene via prephytoene diphosphate. SUBCELLULAR LOCATION: Plastid, chromoplast stroma. SIMILARITY: Belongs to the phytoene/squalene synthase family."}
{"protein": "MGSNLPAQPNLRLTTDGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHVQSSTSSGLVPQVAPSSSHPAASGTAPVDPSASNPSLNPQRVPSTTRPSSTAAPASAAGAAVSNSHGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEHAQRSQREANMQLERRAHQSRMLPEDRTGANSPNLPESSQQAHTPPAGGSANAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGVLELTFSVDDEKFGERRTIDLKPGGRDIPVTNENKAEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDEVIQNFWKIVRSWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPAALPKSHTCFNRLDLPPYKSYETLEHKMSIAVEETLGFGQE", "text": "FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RSP5/NEDD4 family."}
{"protein": "MSLRPGRAHPLAASPLHTPLPARPRPQLRLSTSTSCAAMKSYRLSELSDAEVGGLKARPRIDFSSIFGTVNPIVEDVRMRGDAAVKDYTVKFDKVALDDVVVRVSDLPDVELDPAVKEAFDVAYDNIYAFHVSQKLPEKTVENMKGVRCKRITRCIGSVGLYVPGGTAVLPSTALMLAVPAQIAGCKTVVLATPPSRDGSICKEVLYCAKKAGVTHVLKAGGAQAISAMAWGTVSCPKVEKIFGPGNQYVTAAKMILQNSEAMVSIDMPAGPSEVLVIADKYANPVHVAADLLSQAEHGPDSQVVLVVAGDGVDLGAIEAEVSKQCSALPRGEFASKALGHSFTVFAKDMVEAISFSNMYAPEHLIINVKDAEQWEDLVENAGSVFLGQWTPESVGDYASGTNHVLPTYGYARMYSGVSLNSFLKYITVQSLSEEGLRSLGPHVAKMAEVEGLEAHRRAVTLRLQDIEATVTV", "text": "FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the histidinol dehydrogenase family."}
{"protein": "TTCTSTQQTAAYVTLVSILSDSSFNQCATDSGYSMLTATALPTTAQYKLMCASTACNTMINKIVTLNPPDCELTVPTSGLVLNVYSYANGFSATCASL", "text": "FUNCTION: Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the elicitin family."}
{"protein": "MKYDIIGDIHGCLQEFQNLTEKLGYNWSSGLPIHPDQRKLAFVGDITDRGPHSLRMIEIVWELVIHKKVAYYAPGNHCNKLYRFFLGRNVTIAHGLETTVAEYEALPSHKQNMIKEKFITLYEQSPLYHVLDEKRLLVCHAGIRQDYIGRQDKKVQTFVLYGDITGEKHADGSPVRRDWAKEYKGTTWIVYGHTPVKEPRFVNHTVNIDTGAVFGGKLTGLRYPEMETVSVPSSLPFVPEKFRPIS", "text": "FUNCTION: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP. SIMILARITY: Belongs to the PrpE family."}
{"protein": "MKKMLTLLLSAGLVASIFGVMPAAAAPTVVNSTIVVPKGTTYDGQGKTFVANPSTLGDGSQAENQKPVFRLEAGATLKNVIIGAPAADGVHCYGNCNISNVVWQDVGEDALTLKSSGTVNITGGAAYKAYDKVFQINAAGTINIKNFRADDIGKLVRQNGGTTFTVNMTLDNSNISNVKDAIMRTDSSSSQGRITNTRYSKVPTLFKGFASGKTSQSGNTQY", "text": "FUNCTION: Catalyzes the depolymerization of both polygalacturonate and pectins with low (20-34%) and high (90%) levels of methyl esterification, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Does not show xylanase and cellulase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 3 family."}
{"protein": "MALLCGLGQVTLRLWVSLPFQTENRIGFLAAGAFLRSGGMEALTTQLGPGREGSSSPNSKQELQPYSGSSALKPNQVGETSLYGVPIVSLVIDGQERLCLAQISNTLLKNYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITKREAERLCKSFLGEHKPPKLPENFAFDVVHECAWGSRGSFIPARYNSSRAKCIKCGYCSMYFSPNKFIFHSHRTPDAKYTQPDAANFNSWRRHLKLSDKSATDELSHAWEDVKAMFNGGTRKRTFSLQGGGGGGANSGSGGAGKGGAGGGGGPGCGSEMAPGPPPHKSLRCGEDEASGPPGPPPPHPQRALGLAAAANGPAGPGGPGGSAGVRSYPVIPVPSKGFGLLQKLPPPLFPHPYGFPTAFGLCPKKDDPVLVAGEPKGGPGTGSGGGAGTAAGAGGPGAGHLPPGAGPGPGGGTMFWGHQPSGAAKDAAAVAAAAAAATVYPTFPMFWPAAGSLPVPPYPAAQSQAKAVAAAVAAAAAAAAAAAGGGGPESLDGAEPAKEGSLGTEERCPSALSRGPLDEDGADEALPPSLAPLAPPPPPPARKSSYVSAFRPVVKDAESIAKLYGSAREAYGSGPARGPVPGTGTGGGYVSPDFLSEGSSSYHSASPDVDTADEPEVDVESNRFPDEEGAQEDTEPSVPSTGGGPDGDQPAGPPSVTSSGADGPTDSADGDSPRPRRRLGPPPAIRSAFGDLVADDVVRRTERSPPNGGYELREPCGPLGGPAAAKVYVPERDEHVKSAAAAAALGPAASYLCTPETHEPDKEDNHSTTADDLETRKSFSDQRSVSQPSPANTDRGEDGLTLDVTGTQLVEKDIENLAREELQKLLLEQMELRKKLEREFQSLKDNFQDQMKRELAYREEMVQQLQIVRDTLCNELDQERKARYAIQQKLKEAHDALHHFSCKMLTPRHCTGNCSFKPPLLP", "text": "FUNCTION: Inhibits BMP signaling. Acts as a transcriptional corepressor of LBX1 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SKI family."}
{"protein": "MARAKLKFRLHRAVIVLFCLTLLVALMQGASWFSQNHQRQRNPQLEELARTLARQVTLNIAPLMRSETPDENRINAVLRQLTQESRILDAGVYDEQGDLITRAGESVNVRDRLALDGKKAGSYFNQQIVEPIQGKNGPLGYLRLTLDTHTLATEAKQVDNTTNILRLMLLLSLAIGVVLTRTLLQGKRTRWQQSPFLLTASKPVPEEEEREEKE", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Smp family."}
{"protein": "MRHQCIQIPFKVNLLNKYFISGNHLSQLGELSGYYCVKDIHQRMLQHPIGQRILNDKPRVTPQTFKIEELLKLDENTFGHQYGKFMKDRDFSSGERPIVKYIPDLELAYVYQRYKEIHDFIHVLLMYDVSVYDEIVVKWFEMAQLGLPSATLSAFVGSFKLNCQEKQKLMETLPQILKRAHKSEFIMNVYFEEHINTDITQLRKSLRLL", "text": "FUNCTION: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ4 family."}
{"protein": "MPLSWLLPFSAMELLLTATIFYLVLWVVKAFRLQVPKGLKSPPGPWGWPLIGHVLTLGKNPHLALTRLSARYGDVLQIRIGSTPVVVLSGLDTIRQALVRQSDDFKGRPDLYSSTFISDGQSMIFNPDSGPVWAARRRLAQSALQSFSVASDPASVSSCYLEEHVSREAEHLVTKLLDLMAGPGCFEPSSQIVGSVANVIGAMCFGKNFPQTSEEMLQIVNTSKEFTEFASSGNPVDFFPILRYLPNPMLQQFKDFNKRFLQFLQKTVQEHYQDFDKNHVQDIASALFKHSEESPHVNGDLIPRKKIVNLVNDIFGAGFDTVTTAISWSLLYLVTKPEIQKKIHKELDAVIGRDRKPRLADRPQLPYMEAFILEVFRYSSFLPFTIPHCTTRDTILNGFYIPKDRCVFINQWQVNHDPKQWEDPFEFRPERFLLANNTAVDKTLSDKILLFGLGKRRCIGETLGRWEVFLFLAILLQQLEFSVPPGVKVDLTPVYGLTMKPPHCQHVQARPRFSK", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25- hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase- like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MGCAPGGPCCGPCGPCCGPCCGPCCGPCCGPCCGPCGPCCGPCGPRCGPCGPCGPCCGTMEKRNGLQRCCPF", "text": "SIMILARITY: Belongs to the MST(3)CGP family."}
{"protein": "MYPLAFAKEGEEVIVKKIDAGCGAMQRLVSMGINIGSKLKVIRNQNGPVIISTKGSNIAIGRGLAMKIMVEDAEYGGENEKL", "text": "FUNCTION: Might be involved in Fe(2+) ion uptake (By similarity). SIMILARITY: Belongs to the FeoA family."}
{"protein": "MASSDVKLIGAWASPFVMRPRIALNLKSVPYEFLQETFGSKSELLLKSNPVHKKIPVLLHADKPVSESNIIVEYIDDTWSSSGPSILPSDPYDRAMARFWAAYIDEKWFVALRGFLKAGGEEEKKAVIAQLEEGNAFLEKAFIDCSKGKPFFNGDNIGYLDIALGCFLAWLRVTELAVSYKILDEAKTPSLSKWAENFCNDPAVKPVMPETAKLAEFAKKIFPKPQA", "text": "FUNCTION: Involved in light signaling, mainly phyA-mediated photomorphogenesis and in the integration of various phytohormone signals to modulate various aspects of plant development by affecting glutathione pools. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Tau family."}
{"protein": "MGSSSPLTRRNRAPPSSVSSVYLIFLCFFLYFLNFSNAQSSPVFACDVAANPSLAAYGFCNTVLKIEYRVADLVARLTLQEKIGFLVSKANGVTRLGIPTYEWWSEALHGVSYIGPGTHFSSQVPGATSFPQVILTAASFNVSLFQAIGKVVSTEARAMYNVGLAGLTYWSPNVNIFRDPRWGRGQETPGEDPLLASKYASGYVKGLQETDGGDSNRLKVAACCKHYTAYDVDNWKGVERYSFNAVVTQQDMDDTYQPPFKSCVVDGNVASVMCSYNQVNGKPTCADPDLLSGVIRGEWKLNGYIVSDCDSVDVLYKNQHYTKTPAEAAAISILAGLDLNCGSFLGQHTEEAVKSGLVNEAAIDKAISNNFLTLMRLGFFDGNPKNQIYGGLGPTDVCTSANQELAADAARQGIVLLKNTGCLPLSPKSIKTLAVIGPNANVTKTMIGNYEGTPCKYTTPLQGLAGTVSTTYLPGCSNVACAVADVAGATKLAATADVSVLVIGADQSIEAESRDRVDLHLPGQQQELVIQVAKAAKGPVLLVIMSGGGFDITFAKNDPKIAGILWVGYPGEAGGIAIADIIFGRYNPSGKLPMTWYPQSYVEKVPMTIMNMRPDKASGYPGRTYRFYTGETVYAFGDGLSYTKFSHTLVKAPSLVSLGLEENHVCRSSECQSLDAIGPHCENAVSGGGSAFEVHIKVRNGGDREGIHTVFLFTTPPAIHGSPRKHLVGFEKIRLGKREEAVVRFKVEICKDLSVVDEIGKRKIGLGKHLLHVGDLKHSLSIRI", "text": "FUNCTION: Beta-D-xylosidase showing an optimal efficiency with the natural substrate xylobiose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 3 family."}
{"protein": "MAMAVDFKMYVDQACRAAEEFVNIYYETMDKRRHALVRLYLDKATLIWNGNVVTGLEALANFFEMLPSSEFQINMLDCQPVHEQATQYQTTVLVVTSGVVKFDGNKQHFFNQNFLLTAQSTPNSTVWKIASDCFRFQDWASI", "text": "FUNCTION: Regulator of protein export for NES-containing proteins. Also plays a role in mRNA nuclear export (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm."}
{"protein": "MQWTKVLGLGLGAAALLGLGIILGHFAIPKKANSLAPQDLDLEILETVMGQLDAHRIRENLRELSREPHLASSPRDEDLVQLLLQRWKDPESGLDSAEASTYEVLLSFPSQEQPNVVDIVGPTGGIIHSCHRTEENVTGEQGGPDVVQPYAAYAPSGTPQGLLVYANRGAEEDFKELQTQGIKLEGTIALTRYGGVGRGAKAVNAAKHGVAGVLVYTDPADINDGLSSPDETFPNSWYLPPSGVERGSYYEYFGDPLTPYLPAVPSSFRVDLANVSGFPPIPTQPIGFQDARDLLCNLNGTLAPATWQGALGCHYRLGPGFRPDGDFPADSQVNVSVYNRLELRNSSNVLGIIRGAVEPDRYVLYGNHRDSWVHGAVDPSSGTAVLLELSRVLGTLLKKGTWRPRRSIVFASWGAEEFGLIGSTEFTEEFFNKLQERTVAYINVDISVFANATLRVQGTPPVQSVVFSATKEIRSPGPGDLSIYDNWIRYFNRSSPVYGLVPSLGSLGAGSDYAPFVHFLGISSMDIAYTYDRSKTSARIYPTYHTAFDTFDYVDKFLDPGFSSHQAVARTAGSVILRLSDSFFLPLKVSDYSETLRSFLQAAQQDLGALLEQHSISLGPLVTAVEKFEAEAAALGQRISTLQKGSPDPLQVRMLNDQLMLLERTFLNPRAFPEERYYSHVLWAPRTGSVVTFPGLSNACSRARDTASGSEAWAEVQRQLSIVVTALEGAAATLRPVADL", "text": "FUNCTION: Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position (PubMed:25752612). Lacks carboxypeptidase activity. Lacks dipeptidyl- peptidase IV type activity (PubMed:25752612). SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein Note=Ileal brush border membrane. SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily."}
{"protein": "MAQIPSLENAPLNLKSIRDKSERELVNLLKDVRGTKCLVIDPKLSGSVSLIIPTSKLKELGLELRHLTAEPVQTECTKVVYLVRSQLSFMKFIASHIQNDIAKAIQRDYYVYFVPRRSVACEKILEQEKVHNLVTVKEFPLYMVPLDEDVISFELELSEKDCLVDGDVSSLWHIAKAIHELEFSFGVISKMRAKGKASVRVADILNRMQVEEPVNSNDVGRPEVDTLILLDREVDMVTPMCSQLTYEGLIDEILHISNGAVEVDSSVMGAQQEGKKMKVPLNSSDKLFKETRDLNFEVVVQVLRQKAMTMKEDYTEINSTQTVSELKDFVKKLNSLPEMTRHIHLAQHLTTFTSKQSFNSQLDMEQTLVEAENYDICYEYIEEMIHKQEPLTNVLRLLVLFSVTNSGLPKKQFDYIRMELLHSYGFEHVVTLNNLEKAGLLKKQEFKSNWLTVKRTLKLIVEDTDTSRPNDIAYVYSGYAPLSIRLIQQAIHSGWRPMEDILKLLPGPHLETKRSGFPSSPSVDSLHGASNGVADGRRSIVLVVFIGGVTFAEISALRYLASKEGMAYDLIVATTKIVNGATLIETFMEKLG", "text": "FUNCTION: Involved in regulating membrane fusion at the tonoplast and the prevacuolar compartment. SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein Prevacuolar compartment membrane; Peripheral membrane protein. SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family."}
{"protein": "MDTTNQSEDIKPCDSDLMESILMFDEPISDILAHNKLWISHARTRSNFFPQEGRHISNQHTEAATSLKMWMLSKNLVVIVKRKDDIFPCKILTRNPENLFVARFLESGKEKHIQVEYSDIIMTRSELEKALPLCQHLIPARNWDDFYIIRDFEKATPYFEQGLSALVKPGQQFELQLEDAPDFYVMATVVKNYRGFLLVEYQNFKRWIHMLSPYCHEIGWGKNEKQEYLKRGPYNRHMNVDLVAGLVKQSTNQKLGAVPEIVFRNNCPVPHRIPEYSACVYLDLDQKRFYFAHKVTTKTCRNNRHFFNISIGKNLVTSKQNNRPYEFHVYHPRILPYSVAKRMEVQIILPPDVKLLPDESNLDGYLRTYCNPCDKHKTSDRVQPSPKIAKKKNGPLLLDDTPDAMFRSRPLLGDNIGAHKEWTNFMNHIPDYKRKDLLKSMDTLKFCEIFRPTPTGALQLTAAEVTGQQECMLRLKVSGEDEPVYIHNADPHLYHLGACLDMELAINFHGEFFDEKPLKKNKNANNGFSSF", "text": "FUNCTION: Probably acts synergistically with sop-2 to maintain the transcriptionally repressive state of homeotic genes in order to regulate various neurogenic identities. Specification of some neuronal identities also involves expression of non-Hox genes. Specifies dopaminergic and serotonergic neuronal cell fate, and regulates neurotransmitter choice and axon pathfinding. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MWRNSQKWKNRASRRPQRKGEALIDKLWIFRGLDRGRMTKKTLLMHELIGLKVKVVKSSHPGLIGIEGYVIDETKNTLTILGTKVWAIPKIVAEFEFEVGDKKIRIKGEELVGRPEMRLKKR", "text": "FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 1 family."}
{"protein": "MANFKGHALPGSFFLIIGLCWSVKYPLKYFSHTRKNSPLHYYQRLEIVEAAIRTLFSVTGILAEQFVPDGPHLHLYHENHWIKLMNWQHSTMYLFFAVSGIVDMLTYLVSHVPLGVDRLVMAVAVFMEGFLFYYHVHNRPPLDQHIHSLLLYALFGGCVSISLEVIFRDHIVLELFRTSLIILQGTWFWQIGFVLFPPFGTPEWDQKDDANLMFITMCFCWHYLAALSIVAVNYSLVYCLLTRMKRHGRGEIIGIQKLNSDDTYQTALLSGSDEE", "text": "FUNCTION: Plays a role in innate immunity (PubMed:35938871). Mechanistically, promotes alphaviruses RNA degradation by interacting with the viral polymerase nsP4 and the mRNA-capping enzyme nsP1 and thereby interfering with the interaction between viral RNA and nsP1.(PubMed:35938871). SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM45 family."}
{"protein": "MPYTTIDDLVNSALDYVIIGGGTAGLVLAARLSEKDSVNVGVIEAGLSRLGDPKVDMPTGAALMLGNEDYDWNFKSVPQAASKDRVYHIPRGKMLGGSSAINFMAYGRPCAADIDDWSSKLGLPGWSWNELLPYLKKSQKLESDLPNIKQRDANLFPFLADSQGTDGAIHTSASPWHVPFEDDLLPALDKTSGYARPKDPYSGSHVGFYRSLWAIDRSKKPVRSYSASGFLAPIIDRPNLKVVTNTVACRVLTDSNEDGSMRATGVEVQHDGAIHVLSAQREVILSAGAFQSPQILEQSGIGDPAILHQLKIPCIIGNRNVGNNLQEKLLSAVVYELAPGTMSLDSVLRDPELRKEHQKLYTEAHSGALSGCINLTGFLPYSSLVTSDDIDDTIGDILSLKILSGSPQSPNQNGPFQRWQREAIAARMKSLNSADLQFVCTPANFDTANGYGNLARLSPGSPAGYNACYSLVVSQMYPLSRGSVHSTSSNPLDAPEIDPGFLSHPADVDVIAAGIQFADRVLSSEALRGKVGRRVVPPPSLDLQDRDQVRDFVREHIVTYHHSLGTCAMGQVVDERLRVKGVRSLRVVDASVMPMQVSTAILATVYAVAEKAADMILADHP", "text": "FUNCTION: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the selective antifungal agent ascochitine, an o- quinone methide that plays a possible protective role against other microbial competitors in nature and is considered to be important for pathogenicity of legume-associated Didymella species (PubMed:31554725). The pathway probably begins with the synthesis of a keto-aldehyde intermediate by the ascochitine non-reducing polyketide synthase pksAC from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (Probable). Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain (Probable). The HR-PKS (orf7) probably makes a diketide starter unit which is passed to the non-reducing polyketide synthase pksAC for further extension, producing ascochital and ascochitine (Probable). The aldehyde dehydrogenase (orf1), the 2- oxoglutarate-dependent dioxygenase (orf3) and the dehydrogenase (orf9) are probably involved in subsequent oxidations of methyl groups to the carboxylic acid of the heterocyclic ring (Probable). The ascochitine gene cluster also includes a gene encoding a short peptide with a cupin domain (orf2) that is often found in secondary metabolite gene clusters and which function has still to be determined (Probable). SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MSRFKVSKFRHMEARPSRREAWISDIRAVTTPTCGNHIKSSCSLIAFNSDRPGVLGVISLEGHEENKRHVTYLGCHSDLVTDLDFSPFDDFLLASGSADRTIKLWRLSGTGEALPSVPGVVLGPEELPVEVLQFHPTVDGVLVSTAGKTVKVWDVAKQQPLTELEAHKDLVQSAVWSRDGAIVGTACKDKQLRIFDPRARTQASQSTQAHENNRDIRLAWTGIQEHLVSTGFNQMREREAKLWDTRLFSSALASVTLDTSPGPLIPLLDPDSGLLVLAGKGENQLYCYEVTPQQPALSPVTQCILENVLRGAALVPRRALAVMSCEVLQVLQLSDTAIIPISHHVPRKAVEFHEDLFPDTAGSVPASDAHMWWAGDNQQVQKVSLNPARRPHPCFTSSLVPTMEPAPDMVQPAEMPRADTDLSEGFSSPSSLMSPSTPSSLGPSLSSTSGIGTSPSQRSLQSLLGPSSKFRHTQGSLLHRDSHITNLKGLNLTTPGESDGFCANRLRVAVPLLSSGGQVAVLELQKPGRLPDTALPTLQNGTAVMDLVWDPFDPHRLAVAGEDARIRLWRVPPGGLENVLTTPETVLTGHTEKIYSLRFHPLAADVLASSSYDLTVRIWDLQTGAERLKLQGHQDQIFSLAWSPDGKQLATVCKDGHVRVYEPRSSPLPLQEGPGPEGGRGARIVWVCDGGCLLVSGFDSRSERQLQLYIADALAQGPSALLGLDVAPSTLLPSYDPDTGLVLLTGKGDTRVFLYEVLPEAPFFLECNSFTSPDPHKGFVLLPKTECDIQDVEFARCLRLRQTSLEPVAFRLPRVRKEFFQDDVFPDTAVTWEPALSAKAWFEGANGQPRLLSLQPPGMTPVSQAPREVPARRAPSSAQYLEEKSDQQKKEELLNAMVAKLGNREDPLPQDSFEGVDEDEWD", "text": "FUNCTION: F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post-Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane Golgi apparatus, trans-Golgi network Cytoplasmic vesicle Cytoplasm, cytosol Note=Predominantly cytosolic. Detected on vesicle-like cytoplasmic structures and on the cis-Golgi. Not associated with actin filaments. SIMILARITY: Belongs to the WD repeat coronin family."}
{"protein": "MAMEGPILCRAVMQAKLPVTMISNSLTKSGQLGTAFLGCVCKYRNITRLISPIYQPAQKNFATVCGSFSSSSDGNGYMAGNFSESDEDYVNSTVLEAVEVRSGAEGYVIKMRDGKNLRCVHNNSQGRNIPESAPQPAIVLRIEDGSETLLPIIVLEMPSVLLMAAIRNVHIARPTIYQVVKEMIDKMGYEVKLVRINKRIQEAYCAELFLTKVGDHTESITFDLRPSDAINIAVRCKVPIQVHRSLAYSDGIRSVEPARMAIAAGMSDGLLFTELDRPDGQPCVEAQEFGLIRNMLIAAVEERYKDAATWRDKLMLLRSKRKNWA", "text": "FUNCTION: Bifunctional nuclease with both RNase and DNase activities. Involved in basal defense response. Participates in abscisic acid- derived callose deposition following infection by a necrotrophic pathogen (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bifunctional nuclease family."}
{"protein": "MASPRTPVSPPELPEKNFQYRQVQYWDQRYKDAADSGPYEWFGDFASFRALLEPELCPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSPVVVAAMQVRYAHVPSLRWETMDVRALDFPSGSFDVVLEKGTLDAMLAGEPDPWNVSSEGVHTVDQVLSEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPAVDWLEFLSFLLSPLELGDSEPVVVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMINEIRSAFEETLGDLVWMDEKTRLAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLTAFQNHTACMEEQYSQYQVNGERLNGLQTLGENIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW", "text": "FUNCTION: Converts big endothelin-1 to endothelin-1. May also have methyltransferase activity (By similarity). May play a role in amyloid- beta processing (PubMed:12464614). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Cytoplasmic vesicle, secretory vesicle membrane. SIMILARITY: In the C-terminal section; belongs to the peptidase M13 family. SIMILARITY: In the N-terminal section; belongs to the methyltransferase superfamily."}
{"protein": "MSQMKSRMETAAKMKDEDKLYRRDGILYSTVLSPPETLDKLKDLQAREDDLILVAYPKCGFNWMVAVLRKIINASTGKDEKPPERPPLVEFLPPTVQEEMAQMPPPRLLGTHLHPDNMPATFFTKKPKILVVFRNPKDTVVSYYHFMNKNPVLPNAESWDKFFSDFMTGDVSWGSYFDHALAWEKRIDDPNVMIVMYEDLKQNLPEGVKKISEFFSLPLTDEQVSSIAGQSTFSAMVENSQKSHGNFGSIFFRKGEVGDWKNHFSEAQSKQMDELYHSKLAGTKLAARMNYDLYCQ", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a variety of xenobiotic and endogenous compounds, including dopamine, T3 (triiodo-L-thyronine), T4 (thyroxine), flavonoids, isoflavonoids, and other phenolic compounds. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the sulfotransferase 1 family."}
{"protein": "MKRLGSVQRKMPCVFVTEVKEEPSSKREHQPFKVLATETISHKALDADIYSAIPTEKVDGTCCYVTTYKDQPYLWARLDRKPNKQAEKRFKNFLHSKENAKEFFWNVEEDFKPAPECWIPAKEIEQINGNPVPDENGHIPGWVPVEKNNKQYCWHSSVVNYEFEIALVLKHHPDDSGLLEISAVPLSDLLEQTLELVGTNINGNPYGLGSKKHPLHLLIPHGAFQIRNLPSLKHNDLLSWFEGCKEGKIEGIVWHCSDGCLIKVHRHHLGLCWPIPDTYMNSRPVIINMNLNKCDSAFDIKCLFNHFLKIDNQKFARLKDIIFDV", "text": "FUNCTION: Functions as an RNA ligase, in vitro. The ligation reaction entails three nucleotidyl transfer steps. In the first step, the RNA ligase reacts with ATP in the absence of nucleic acid to form a covalent ligase-AMP intermediate and release pyrophosphate. In step 2, the ligase-AMP binds to the nucleic acid and transfers the adenylate to the 5'-PO4 terminus to form an adenylylated intermediate. In step 3, the RNA ligase directs the attack of the 3'-OH on the 5'- phosphoanhydride linkage, resulting in a repaired 3'-5' phosphodiester and release of AMP. Exhibits selectivity for single-stranded RNA substrates and may not have nick-sealing activity on double-stranded DNA-RNA hybrids. May play a role in maintaining RNA integrity under stress conditions, for example in response to reactive oxygen species (ROS)."}
{"protein": "MEKLLWCSLVMIGFSQAFAQKDMSKTAFVFPKESANSYVSLEAQSKKTLKAFTVCLHIFTELSTTRSFSIFSYATKNSPNEILIFWSKDRGYAFGVGGPEVLFKASEIPEVPTHICASWESATGIAELWVDGKPKVRKILQKGYTVGTDASIILGQEQDSYGGGFDANQSLVGDIGDVNMWDIVLSPEQINTVCVGGTLDPSVLNWQALKYKVQGDVFIKPQLWP", "text": "FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pentraxin family."}
{"protein": "MLAIRSSNYLRCIPSLCTKTQISQFSSVLISFSRQISHLRLSSCHRAMSSSRPSAFDALMSNARAAAKKKTPQTTNLSRSPNKRKIGETQDANLGKTIVSEGTLPKTEDLLEPVSDSANPRSDTSSIAEDSKTGAKKAKTLSKTDEMKSKIGLLKKKPNDFDPEKMSCWEKGERVPFLFVALAFDLISNESGRIVITDILCNMLRTVIATTPEDLVATVYLSANEIAPAHEGVELGIGESTIIKAISEAFGRTEDHVKKQNTELGDLGLVAKGSRSTQTMMFKPEPLTVVKVFDTFRQIAKESGKDSNEKKKNRMKALLVATTDCEPLYLTRLLQAKLRLGFSGQTVLAALGQAAVYNEEHSKPPPNTKSPLEEAAKIVKQVFTVLPVYDIIVPALLSGGVWNLPKTCNFTLGVPIGPMLAKPTKGVAEILNKFQDIVFTCEYKYDGERAQIHFMEDGTFEIYSRNAERNTGKYPDVALALSRLKKPSVKSFILDCEVVAFDREKKKILPFQILSTRARKNVNVNDIKVGVCIFAFDMLYLNGQQLIQENLKIRREKLYESFEEDPGYFQFATAVTSNDIDEIQKFLDASVDVGCEGLIIKTLDSDATYEPAKRSNNWLKLKKDYMDSIGDSVDLVPIAAFHGRGKRTGVYGAFLLACYDVDKEEFQSICKIGTGFSDAMLDERSSSLRSQVIATPKQYYRVGDSLNPDVWFEPTEVWEVKAADLTISPVHRAATGIVDPDKGISLRFPRLLRVREDKKPEEATSSEQIADLYQAQKHNHPSNEVKGDDD", "text": "FUNCTION: Essential protein. DNA ligase that seals nicks in double- stranded DNA during DNA replication, DNA recombination and DNA repair. Involved in repair of both single strand breaks (SSBs) and double strand breaks (DSBs). Required in the endosperm for embryogenesis, probably to repair DNA-breaks generated by DME. SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. SIMILARITY: Belongs to the ATP-dependent DNA ligase family."}
{"protein": "MAQRAFPNPYADYNKSLAENYFDSTGRLTPEFSHRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSITFLCGDAGPLAVAAVLYHKMNSEKQAEECITRLIHLNKIDPHVPNEMLYGRIGYIFALLFVNKNFGEEKIPQSHIQQICENILTSGENLSRKRNLAAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQAYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEHGCRTADTPFSLFEGMAGTIYFLADLLVPTKAKFPAFEL", "text": "FUNCTION: Functions as glutathione transferase (PubMed:25158856). Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate (PubMed:25158856). Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (PubMed:25158856). May play a role in EPS8 signaling. Binds glutathione (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the LanC-like protein family."}
{"protein": "MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEDDGQRSSTEQSGEAQGEAAKSES", "text": "FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. SIMILARITY: Belongs to the PKI family."}
{"protein": "MAGVLKKTTGLVGLAVCNTPHERLRILYTKILDVLEEIPKNAAYRKYTEQITNEKLAMVKAEPDVKKLEDQLQGGQLEEVILQAEHELNLARKMKEWKLWEPLVEEPPADQWKWPI", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFA5 subunit family."}
{"protein": "MYENGISFIISLLICGCVKSEEMMKQHFVLVHGSCLGAWCWYKVKPLLEASGHRVTALDLAACGIDTRSITDISTCEQYSEPLIQLMTSLPNDEKVVLVGHSYGGLTLAIAMDKFPDKISVSVFVTSFMPDTKNSPSFVLEKFASTMTPEDWMGSELEPYVVFSAEFTKHRILQLSPIEDLELRLLLKRPGSLFLNDLSRMKNFSEKGYGSVPRAYIVSKDDHTISEEYQRWMIDNYPPNLVIEMEGTDHLPLFCKPQLLSDHLLAIADKFS", "text": "FUNCTION: Methylesterase shown to have carboxylesterase activity in vitro. SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase family."}
{"protein": "MVNIVEKQNRLSLISLSLVSIRYKSWDFLYRILHGSIFDYIIGPRKELLLYFKCVYDSTFFNGKNYFSNLFTDTATSFRLLTFLNEHDLKSIPPLPLDKCQGLDSYSTLYDGYIVQSSHESQGLYDGSGKDGNDYTMKMQIMKNVLEMQINEMDDEIKRIKLRRNVVAKKLDVIISRIVDHKENKSKTDGSTEDEVHIGNTSSVLKQTNHEHTIITSENNTDDKVSLLTLEPDNAQIGNKLQRYFEAMKLKKKSSGFDIEDFENIIGTKGQLGKTLKCHDDYINSLAINAQLGVLSSTANLDNEIKLWDISTTQCLGVLSGHRATVNTTRFIDDTRLLASAGKDASVKVWDVDNIVDKDGNANDNLCLATFDGHKDSVTALATTGNAIVSGSNDKTLRHWDLGSGKCIQSIDLTIALKMVPQSVSKLDITPSFNTPLIGGADCIDNALVTGTKDGIVYLWDLRIGRVVGSLEGHRGPITSLKYMGSELITGSMDKSTRIWDLRMGSVAELLSFEKEVVSVEESQTQLINALEGEPVKIYDRGERQYNSLPDSFNTTTLVVYESLLALGNDHGDITWWSL", "text": "FUNCTION: Involved in mitochondrial fission. Has a partially redundant function to MDV1 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family."}
{"protein": "MAPFSFILTVLLYALTCSARALGHAHALLPRAGSLEQVTDFGDNPTNVGMYIYVPNNLASSPGIVVAIHYSPEGTGTAEAYYTGSPYAQLAEQYGFIVIYPQSPYEGTCWDVSSQETLTHNGGGNSNSIANMVTWAISKYNADSSKVFVTGSSSGAMMTHQNVMAATYPELFAAATVYSGVPAGCFYSSSNQQDGWNSTCAQGQVITTPENWANVAKGMYPGYNGTRPKMQIYHGSVDTTLLPQNYYETCKQWAGVFGYNYDSPQQVQDNTPQSNYATTTWGDDLQGIFATGVGHTVPIRGDDDMAWFGFA", "text": "FUNCTION: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA subfamily."}
{"protein": "MTDYLLLFVGTVLVNNFVLVKFLGLCPFMGVSKKLETAMGMGLATTFVMTLASICAWLIDTWILIPLNLIYLRTLAFILVIAVVVQFTEMVVRKTSPVLYRLLGIFLPLITTNCAVLGVALLNINLGHNFLQSALYGFSAAVGFSLVMVLFAAIRERLAVADVPAPFRGNAIALITAGLMSLAFMGFSGLVKL", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR (PubMed:12773378). FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrDE/RnfAE family."}
{"protein": "MATLLRSLALFKRNKDKPPITSGSGGAIRGIKHIIIVPIPGDSSITTRSRLLDRLVRLIGNPDVSGPKLTGALIGILSLFVESPGQLIQRITDDPDVSIRLLEVVQSDQSQSGLTFASRGTNMEDEADQYFSHDDPISSDQSRFGWFENKEISDIEVQDPEGFNMILGTILAQIWVLLAKAVTAPDTAADSELRRWIKYTQQRRVVGEFRLERKWLDVVRNIIAEDLSLRRFMVALILDIKRTPGNKPRIAEMICDIDTYIVEAGLASFILTIKFGIETMYPALGLHEFAGELSTLESLMNLYQQMGKPAPYMVNLENSIQNKFSAGSYPLLWSYAMGVGVELENSMGGLNFGRSYFDPAYFRLGQEMVRRSAGKVSSTLASELGITAEDARLVSEIAMHTTEDKISRAVGPRQAQVSFLQGDQSENELPRLGGKEDRRVKQSRGEARESYRETGPSRASDARAAHLPTGTPLDIDTASESSQDPQDSRRSAEPLLSCKPWQESRKNKAQTRTPLQCTMTEIF", "text": "FUNCTION: Encapsidates the genome in a ratio of 1 N per 6 ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure with either 12.35 or 11.64 N per turn, approximately 20 nm in diameter, with a hollow central cavity approximately 5 nm in diameter. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases. N is released in the blood following lysis of measles infected cells, it interacts then with human FCGR2B on immune cells, inducing apoptosis and blocking inflammatory immune response. Ntail binds to a protein on human thymic epithelial cells, termed Nucleoprotein Receptor (NR), inducing growth arrest. SUBCELLULAR LOCATION: Virion Host cytoplasm. SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family."}
{"protein": "MNRGRGGFRGGRGGRTGPSQFQQGPPDTVLEMGAFMQSCEGDIVCRSINVKIPYFNAPIYLENKTQVGKVDEILGPVNEVFFTIKPSEGVQADSFKDGDKFYIGPDKLLPLERFLPKPKEFGTKPKKKSAGGAGRGGFGGRGGARGGRGGFGGRGGSRGGFGDRGGRGGSRGGFGGRGGSRGGFGDRGGFGGRGGSRGGFGDRGGRGGGFRGGRF", "text": "FUNCTION: Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the GAR1 family."}
{"protein": "MVLYIILAIIVIILIAVGVLFYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDKFSFNASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKFEPRLEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDSTLQSLKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVRENYYINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAEDNLLRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLVNAVYAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQVLESVEPGVTKHIEEEVIKQ", "text": "FUNCTION: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. Note=Colocalized with FtsZ to the nascent septal site. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Colocalized with FtsZ to the nascent septal site. SIMILARITY: Belongs to the EzrA family."}
{"protein": "MEGESSRFEIHTPVSDKKKKKCSIHKERPQKHSHEIFRDSSLVNEQSQITRRKKRKKDFQHLISSPLKKSRICDETANATSTLKKRKKRRYSALEVDEEAGVTVVLVDKENINNTPKHFRKDVDVVCVDMSIEQKLPRKPKTDKFQVLAKSHAHKSEALHSKVREKKNKKHQRKAASWESQRARDTLPQSESHQEESWLSVGPGGEITELPASAHKNKSKKKKKKSSNREYETLAMPEGSQAGREAGTDMQESQPTVGLDDETPQLLGPTHKKKSKKKKKKKSNHQEFEALAMPEGSQVGSEVGADMQESRPAVGLHGETAGIPAPAYKNKSKKKKKKSNHQEFEAVAMPESLESAYPEGSQVGSEVGTVEGSTALKGFKESNSTKKKSKKRKLTSVKRARVSGDDFSVPSKNSESTLFDSVEGDGAMMEEGVKSRPRQKKTQACLASKHVQEAPRLEPANEEHNVETAEDSEIRYLSADSGDADDSDADLGSAVKQLQEFIPNIKDRATSTIKRMYRDDLERFKEFKAQGVAIKFGKFSVKENKQLEKNVEDFLALTGIESADKLLYTDRYPEEKSVITNLKRRYSFRLHIGRNIARPWKLIYYRAKKMFDVNNYKGRYSEGDTEKLKMYHSLLGNDWKTIGEMVARSSLSVALKFSQISSQRNRGAWSKSETRKLIKAVEEVILKKMSPQELKEVDSKLQENPESCLSIVREKLYKGISWVEVEAKVQTRNWMQCKSKWTEILTKRMTNGRRIYYGMNALRAKVSLIERLYEINVEDTNEIDWEDLASAIGDVPPSYVQTKFSRLKAVYVPFWQKKTFPEIIDYLYETTLPLLKEKLEKMMEKKGTKIQTPAAPKQVFPFRDIFYYEDDSEGEDIEKESEGQAPCMAHACNSSTLGGQGRWII", "text": "FUNCTION: Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Nucleus, nucleoplasm Note=May be localized to the nucleolus in an NPM1/B23-dependent manner. May be displaced from the nucleolus into the nucleoplasm in an CDKN2A/ARF-dependent manner. May shuttle back and forth from nucleoplasm to nucleolus."}
{"protein": "MATDELATKLSRRLQMEGEGGGETPEQPGLNGAAAAAAGAPDEAAEALGSADCELSAKLLRRADLNQGIGEPQSPSRRVFNPYTEFKEFSRKQIKDMEKMFKQYDAGRDGFIDLMELKLMMEKLGAPQTHLGLKNMIKEVDEDFDSKLSFREFLLIFRKAAAGELQEDSGLCVLARLSEIDVSSEGVKGAKSFFEAKVQAINVSSRFEEEIKAEQEERKKQAEEMKQRKAAFKELQSTFK", "text": "FUNCTION: May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. SUBCELLULAR LOCATION: Membrane raft Note=In a mouse immature B-cell line WEHI-231."}
{"protein": "LMVVTSNADRICTGITSSNSPHVVKTATQGEVNVTGVIPLTTTPTKSHFANLKGTKTRGKLCPKCLNCTDLDVALGRPKCMGTIPSAKASILHEVKPVTSGCFPIMHDRTKIRQLPNLLRGYENIRLSTHNVINAETAPGGPYIVGTSGSCPNVTNGNGFFATMAWAVPKNNNNKTATNPLTVEVPFICTEGEDQITVWGFHSDSETQMVKLYGDSKPQKFTSSANGVTTHYVSQIGGFPKQAEDGGLPQSGRIVVDYMVQKSGKTGTITYQRGILLPQKVWCASGRSKVIKGSLPLIGEADCLHEKYGGLNKSKPYYTGEHAKAIGNCPIWVKTPLKLANGTKYRPPAKLLKERGFFGAIAGFLEGGWEGMIAGWHGYTSHGAHGVAVAADLKSTQEAINKITKNLNSLSELEVKNLQRLSGAMDELHNEILELDEKVDDLRADTISSQIELAVLLSNEGIINSEDEHLLALERKLKKMLGPSAVDIGNGCFETKHKCNQTCLDRIAAGTFNAGEFSLPTFDSLNITAASLNDDGLDNHTILLYYSTAASSLAVTLMIAIFIVYMVSRDNVSCSICL", "text": "FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host apical cell membrane; Single-pass type I membrane protein Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. SIMILARITY: Belongs to the influenza viruses hemagglutinin family."}
{"protein": "MTLLTVKHLTITDTWTDQPLVSDVNFTLTKGETLGVIGESGSGKSITCKSIIGLNPERLGVTGEIIFDGTSMLSLSESQLKKYRGKDIAMVMQQGSRAFDPSTTVGKQMFETMKVHTSMSTQEIEKTLIEYMDYLSLKDPKRILKSYPYMLSGGMLQRLMIALALALKPKLIIADEPTTALDTITQYDVLEAFIDIKKHFDCAMIFISHDLTVINKIADRVVVMKNGQLIEQGTRESVLHHPEHVYTKYLLSTKKKINDHFKHVMRGDVHD", "text": "FUNCTION: Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Probably responsible for energy coupling to the transport system (PubMed:23279021, PubMed:29581261). Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro (PubMed:23279021). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MLCLMLCVLCWSRSDVAALGSVVENEDALLRHLFQGYQKWVRPVENSNDTIKVLFGLKISQLVDVDEKNQLMTTNVWLKQEWMDHKLSWNPEEYGGITAIRVPSESLWLPDIVLFENADGRFEGSLMTKAIVKYNGVVQWMPPASYKSSCTMELTFFPFDRQNCSMKFGSWTYDGSMVDLILVDENVDTKDFFDNGEWEILNAKGMKGNRKDGLYSYPFVTYSFVLRRLPLFYTLFLIIPCLGLSFLTVLVFYLPSDEGEKLSLSTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLLFIMIFVTLSIIVTVFVINVHHRSSATYHPMAPWVKRLFLQKLPRLLCMKGHVDRYSFSDTEEKETTLKSKLPGKQKHKQAKDGEKVVIAFLEKAADSIRYISRHVKKDAFIRQVVQDWKFVAQVLDRIFLWLFLVVSVTGSVLIFTPALQMWLNSTL", "text": "FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-3/CHRNB3 sub- subfamily."}
{"protein": "MGFLAIVLSVALLFRSTSGTPLGPRGKHSDCNSVDHGYQCFPELSHKWGLYAPYFSLQDESPFPLDVPEDCHITFVQVLARHGARSPTHSKTKAYAATIAAIQKSATAFPGKYAFLQSYNYSLDSEELTPFGRNQLRDLGAQFYERYNALTRHINPFVRATDASRVHESAEKFVEGFQTARQDDHHANPHQPSPRVDVAIPEGSAYNNTLEHSLCTAFESSTVGDDAVANFTAVFAPAIAQRLEADLPGVQLSTDDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTATEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWANELMARLTRAPVHDHTCVNNTLDASPATFPLNATLYADFSHDSNLVSIFWALGLYNGTAPLSQTSVESVSQTDGYAAAWTVPFAARAYVEMMQCRAEKEPLVRVLVNDRVMPLHGCPTDKLGRCKRDAFVAGLSFAQAGGNWADCF", "text": "FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Releases 5 of the 6 phosphate groups to yield the end product myo-inositol 2-monophosphate. Specific for phytate. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the histidine acid phosphatase family."}
{"protein": "MPKLKKLLLKVSTSKPNTNPPSQNEEKGTIVKQEAPIHVSNVALVCPQTQTPTKVGIRIQSGKKVRYAKKSNQTLDEKN", "text": "FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
{"protein": "MAVGEPLVHIRVTLLLLWFGMFLSISGHSQARPSQYFTSPEVVIPLKVISRGRGAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGYVEGVPESLVALSTCSGGFLGMLQINDLVYEIKPISVSATFEHLVYKIDSDDTQFPPMRCGLTEEKIAHQMELQLSYNFTLKQSSFVGWWTHQRFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCIMHAYRKVTTKFSNCSYAQYWDSTISSGLCIQPPPYPGNIFRLKYCGNLVVEEGEECDCGTIRQCAKDPCCLLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVYVQDGISCNVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVGVIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAIPDIGEVKDGTVCGPEKICIRKKCASMVHLSQACQPKTCNMRGICNNKQHCHCNHEWAPPYCKDKGYGGSADSGPPPKNNMEGLNVMGKLRYLSLLCLLPLVAFLLFCLHVLFKKRTKSKEDEEG", "text": "FUNCTION: May be involved in sperm maturation and/or fertilization. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MAWRQLRKRALDAAIILGGGGLLFTSYLTATGDDHFYAEYLMPALQRLLDPESAHRLAVRVISLGLLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKQTQLTTDGLPLGINLGKNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIITNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIGVDHRR", "text": "FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily."}
{"protein": "MDKKKDLLENEQFLRIQKLNAADAGKRQSITVDDEGELYGLDTSGNSPANEHTATTITQNHSVVASNGDVAFIPGTATEGNTEIVTEEVIETDDNMFKTHVKTLSSKEKARYRQGSSNFISYFDDMSFEHRPSILDGSVNEPFKTKFVGPTLEKEIRRREKELMAMRKNLHHRKSSPDAVDSVGKNDGAAPTTVPTAATSETVVTVETTIISSNFSGLYVAFWMAIAFGAVKALIDYYYQHNGSFKDSEILKFMTTNLFTVASVDLLMYLSTYFVVGIQYLCKWGVLKWGTTGWIFTSIYEFLFVIFYMYLTENILKLHWLSKIFLFLHSLVLLMKMHSFAFYNGYLWGIKEELQFSKSALAKYKDSINDPKVIGALEKSCEFCSFELSSQSLSDQTQKFPNNISAKSFFWFTMFPTLIYQIEYPRTKEIRWSYVLEKICAIFGTIFLMMIDAQILMYPVAMRALAVRNSEWTGILDRLLKWVGLLVDIVPGFIVMYILDFYLIWDAILNCVAELTRFGDRYFYGDWWNCVSWADFSRIWNIPVHKFLLRHVYHSSMSSFKLNKSQATLMTFFLSSVVHELAMYVIFKKLRFYLFFFQMLQMPLVALTNTKFMRNRTIIGNVIFWLGICMGPSVMCTLYLTF", "text": "FUNCTION: Sterol O-acyltransferase that catalyzes the formation of stery esters. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily."}
{"protein": "MADFQDELLALAGIDDSDVASNRKRAHDDLDDVLSSSSDEDNNENVGQDYAEESGGEGNEKSEDEFEEKFKNPYRLEGKFKDEADRAKIMAMTEIERESILFEREEEISKLMERRELAIRLHQQNAQYMAQSTRRSTRDKPLTSAAAGKRDKLTELKKRRQERSARSVSERTRKRSPVSDYEEQNESEKSEEEEGYSPSYAEEKVEQVSKDNASANLYDLNAIRLGRKHVAEYMYHPIFESTVTGCFVRVKIGERDGQGVYRLCQVKGILESRKPYRVDGVLTKVSLECFHGRSKRVFDVNVLSNEPFSDHDFQRWHHQMMEDKLSMPSKNFVQRKLNDLRDMSKYVLSEKEVSDIINRKKELSRVPSNIAAEKTRLRQRRQAAYVAGNAELVKEIDDQLNTLEELSMGSNQNSNSAMDQLAKVNERNRRRNHTEIRLAEQRMNEERRRLSAAATATPMSAPTSVLTGTSPQPSPSLSTSIMSTPKLNPSESVVVASEKASSPDLSPKLLPSESQIFDEGIAVTQTPNTLEDKDFKLHEKAVHGIDDIIATVDFGIDINI", "text": "FUNCTION: The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. Also has a role in transcription- coupled histone modification. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of the TATA box-binding protein, and the relative activities of different TATA elements (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm."}
{"protein": "MKALILVGGYGTRLRPLTLSVPKPLVDFCNKPILLHQVEALVKAGVTHVILAVSYMSDMLEKEMKEQEKRLGIRISMSHEKEPLGTAGPLALARELLTENSEPFFVLNSDVICDFPFEDMVRFHKHHGKEGTIVVTKVEEPSKYGVVVYETESGQIQRFVEKPQVFVSNKINSGLYIFSPAVLDRIQLRPTSIEKEIFPAMAQEGQLYAMELQGFWMDIGQPKDFLTGMCMYLQSVRQKHPEWLHAGPGFIGNVLVDPTAKIGQNCSIGPNVTIGPGVTVEDGVRIKRCTVMKGSRLHSHSWLESSIVGWSSSVGQWVRMENVTVLGEDVIVNDELYLNGANVLPHKCISESVPEPRIIM", "text": "SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
{"protein": "MQPIRLGLVGYGKIAQDQHVPAINANPAFTLVSVATQGKPCPGVENFQSLGELLENGPPVDAIAFCTPPQGRFALVQQALAAGKHVLVEKPPCATLGKAALWIKREQASAPCSPCIAYAPAIAAARDWLATRTLQSVQIDWKEDVRKWHPGQAWIWQPGLGVFDPGINALSIVTHLLPLPLFVESAELRVPSNCQSPIAASIKMSDPRLLDVRAEFDFDHGHDELWSIQIRCAEGTLRLDNGGALLSIDGVRQTVAEEGEYAAVYRHFQQLIGDKTSDVDVQPLRLVADSFFVGSRVSVEAFYD", "text": "FUNCTION: Catalyzes the dehydrogenation of D-galactose by either NAD(+) or NADP(+). Oxidizes following sugars in decreasing order: D-fucose > D-galactose > L-arabinose > 2-deoxy-D-galactose >> 4-deoxy-D-galactose > 2-deoxy-2-amino-D-galactose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MQVHVGLTLLLCAVLLSSATASSDDESNQDESIDSKSSLPADESVKDHSTTGRVVAGQIFVDSEDPEVESPLQEEEESSKTEEEVSVGEEISFVESPSLSSKSYEEAKRARKPVLTAIEGTAHGEPCHFPFLFLDKEYDECTSDGRQDGRLWCATTYDYKTDEKWGFCETEEDAAKRRQMQEAEMIYQAGMKILNGSNRKSQKREAYRYLQKAAGMNHTKALERVSYALLFGDYLTQNIQAAKEMFEKLTEEGSPKGQTALGFLYVSGLGVNSSQAKALVYYTFGALGGNLIAHMVLGYRYWAGIGVLQSCESVLTHYRLVANHVASDISLTGGSVVQRIRLPDEVENPGMNSGMLEEDLIQYYQFLAEKGDVQAQVGLGQLHLHGGRGVEQNHQRAFDYFNLAANAGNSHAMAFLGKMYSEGSDIVPQSNETALHYFKKAADMGNPVGQSGLGMAYLYGRGIQVNYDLALKYFQKAAEQGWVDGQLQLGSMYYNGIGVKRDYKQALKYFNLASQGGHILAFYNLAQMHASGTGVMRSCHTAVELFKNVCERGRWSERLMTAYNSYKDGDYNAAVVQYLLLAEQGYEVAQSNAAFILDQREATIVGENETYPRALLHWNRAASQGYTVARIKLGDYHFYGFGTDVDYETAFIHYRLASEQQHSAQAMFNLGYMHEKGLGIKQDIHLAKRFYDMAAEASPDAQVPVFLALCKLGVVYFLQYIREANIRDIFTQLDMDQLLGPEWDLYLMTIIALLLGTVIAYRQRQHQDVPVPRPPGPWPAPPQQEGPPEQQPPQ", "text": "FUNCTION: Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Enhances SYVN1 stability. Plays a role in LPL maturation and secretion. Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells. May play a role in Notch signaling. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the sel-1 family."}
{"protein": "MKNKYISKLLVGAATITLATMISNGEAKASENTQQTSTKHQTTQNNYVTDQQKAFYQVLHLKGITEEQRNQYIKTLREHPERAQEVFSESLKDSKNPDRRVAQQNAFYNVLKNDNLTEQEKNNYIAQIKENPDRSQQVWVESVQSSKAKERQNIENADKAIKDFQDNKAPHDKSAAYEANSKLPKDLRDKNNRFVEKVSIEKAIVRHDERVKSANDAISKLNEKDSIENRRLAQREVNKAPMDVKEHLQKQLDALVAQKDAEKKVAPKVEAPQIQSPQIEKPKAESPKVEVPQIQSPKVEVPQSKLLGYYQSLKDSFNYGYKYLTDTYKSYKEKYDTAKYYYNTYYKYKGAIDQTVLTVLGSGSKSYIQPLKVDDKNGYLAKSYAQVRNYVTESINTGKVLYTFYQNPTLVKTAIKAQETASSIKNTLSNLLSFWK", "text": "FUNCTION: Plays a role in the inhibition of both the innate and adaptive immune responses. Possesses two N-terminal domains that bind the Fc region of IgG and two domains that form a tripartite complex with complement factors C3b and CFH. By recruiting CFH and C3b, the secreted form acts as a potent complement inhibitor of the alternative pathway-mediated lysis. SUBCELLULAR LOCATION: Secreted Cell membrane Note=Occurs both extracellularly and associated with the cytoplasmic membrane where only the domains I and II are exposed to the extracellular media. Membrane association occurs via binding to lipoteichoic acid. SIMILARITY: Belongs to the immunoglobulin-binding protein Sbi family."}
{"protein": "MNAVAEAPVTEDVPAPFVFTDSAADKVKQLIEEEGNAELKLRVFVQGGGCSGFQYGFTFDEEVNEDDTTMVKNGVTLLIDSMSYQYLVGAEIDYKEDINGAQFVIKNPNASTTCGCGSSFSV", "text": "FUNCTION: Required for insertion of 4Fe-4S clusters. SIMILARITY: Belongs to the HesB/IscA family."}
{"protein": "MANDIDELIGIPFPNHSSEVLCSLNEQRHDGLLCDVLLVVQEQEYRTHRSVLAACSKYFKKLFTAGTLASQPYVYEIDFVQPEALAAILEFAYTSTLTITAGNVKHILNAARMLEIQCIVNVCLEIMEPGGDGGEEDDKEDDDDDEDDDDEEDEEEEEEEEEDDDDDTEDFADQENLPDPQDISCHQSPSKTDHLTEKAYSDTPRDFPDSFQAGSPGHLGVIRDFSIESLLRENLYPKANIPDRRPSLSPFAPDFFPHLWPGDFGAFAQLPEQPMDSGPLDLVIKNRKIKEEEKEELPPPPPPPFPNDFFKDMFPDLPGGPLGPIKAENDYGAYLNFLSATHLGGLFPPWPLVEERKLKPKASQQCPICHKVIMGAGKLPRHMRTHTGEKPYMCTICEVRFTRQDKLKIHMRKHTGERPYLCIHCNAKFVHNYDLKNHMRIHTGVRPYQCEFCYKSFTRSDHLHRHIKRQSCRMARPRRGRKPAAWRAASLLFGPGGPAPDKAAFVMPPALGEVGGHLGGAAVCLPGPSPAKHFLAAPKGALSLQELERQFEETQMKLFGRAQLEAERNAGGLLAFALAENVAAARPYFPLPDPWAAGLAGLPGLAGLNHVASMSEANN", "text": "FUNCTION: May be a tumor suppressor gene."}
{"protein": "MAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGILVGKDRSSFFVNGLTLGGQKCSVIRDSLLQDGEFTMDLRTKSTGGAPTFNITVTMTAKTLVLLMGKEGVHGGMINKKCYEMASHLRRSQY", "text": "FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family."}
{"protein": "MIRLSPGFAINPRFRSDSFVNSQKPPFLSVQIGSQRRNLSRIGSENGDGVAFDAVAYEADRLSLDAAAMEDMAETAKKELESDPDSDPKAWKWVIRKKMWDLMEARNYAMSPRPVHHRIPNFVGASAAARKLAELDAFRMAMVVKVNPDSPQKQIRFLTLSGEKKLLTPQPRLRTGFFSVLESDLLKPETIMEACTSVGVAKYGRAIGLDEKIKVDLIVIGSVAVNPQTGARLGKGEGFAELEYGMLRYMGAIDDSTPVVTTVHDCQLVDDIPLEKLAIHDVPVDIICTPTRVIFTNTPIPKPQGIYWDKLSPEKLRQIRILRELKNRLEKKTGRKLPTGPSEKLPPTAERKRR", "text": "FUNCTION: May be involved in thiamine metabolism. Does not possess 5- formyltetrahydrofolate cyclo-ligase activity in vitro. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase family."}
{"protein": "MNHPGLFLFLGLTFAVQLLLLVFLLFFFLVWWDQFGCRCDGFIL", "text": "SIMILARITY: Belongs to the papillomaviridae E5 protein family."}
{"protein": "MAPQRMKNPPHPGLLIKSDLDGLGINITEAAKALDVTRAALSEIINGKRGISAKMAWKLSKAFTNSDPEFWLALQAKYDLSQVGEQCADKVRVLWQPSSLDNEGIEVNSSENKVK", "text": "SIMILARITY: Belongs to the VapA/VapI family."}
{"protein": "MGGQKEMADSVKTKLTGKLKAKKVTAPQAKAFSVHLLTASGSFLAFLSVVAASDGRYTAMWWWLGLALFVDGIDGPIARKLEVKYVLPNWSGELLDSIIDYVTYVLIPAFALYQSGFMGTNLSFISGAIIVVSSAIYYADTGMKTKENFFKGFPVVWNMVVFTLFIVRPGEWVAFGTVVASAILSFLPINFLHPVRVVRLRPLNLTIFLLWCAFGVIALYYMLDAPLWVRIGISVTGLYIYFIGAIMQLFPSLGREAALAKARKLVEKQQKSGEAP", "text": "FUNCTION: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family."}
{"protein": "MAHKGLQLLGFTLSLLGLIGLIIGTIMPQWKMSAYVGDNIITAIAMYQGLWMSCAYQSTGQQQCKVYDSVLQLDSALQATRALMVVAILLTVAGLGVASMGMKCTNCGGDDKVKKSRIAMTGGIILSVGALCSIVACGWFTSQIIRDFYNPFTPVNTKYEFGAAIFIAWAGAFLDIMGGGMLASSCSKGQSSPNYPKSSRPVKSSRPPSSSKEYV", "text": "FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the claudin family."}
{"protein": "MSKTAQKRLLKELQQLIKDSPPGIVAGPKSENNIFIWDCLIQGPPDTPYADGVFNAKLEFPKDYPLSPPKLTFTPSILHPNIYPNGEVCISILHSPGDDPNMYELAEERWSPVQSVEKILLSVMSMLSEPNIESGANIDACILWRDNRPEFERQVKLSILKSLGF", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Involved in resistance to cadmium poisoning. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=Anchored via the membrane protein CUE1 to the endoplasmic reticulum membrane. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MSLLTEVETYVLSIVPSGPLKAEIAQRLEDVFAGKNTDLEALMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQRRRFVQNALNGNGDPNNMDRAVKLYKKLKREITFHGAKEVALSYSTGALASCMGLIYNRMGTVTTEVAFGLVCATCEQIADSQHRSHRQMATTTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMEVASQARQMVQAMRTIGTHPSSSAGLKDNLLENLQAYQKRMGVQMQRFK", "text": "FUNCTION: Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place. FUNCTION: Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms. SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein; Cytoplasmic side Host nucleus. SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family."}
{"protein": "MNVLLGGLVIFATFVTLCNGSCYVIRHKIVPGETIKECTDLKGNKHPLDSRWRTEDCELCACRDIEISCCSLVSTPVGYDRHNCRKIFNKETCKISVVEKTDPNRPCGVSGWIS", "text": "SUBCELLULAR LOCATION: Secreted Note=Sperm surface. SIMILARITY: Belongs to the beta-microseminoprotein family."}
{"protein": "MPKIVVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRRYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVSVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEINAINGNEITFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNIVKFFDYTFASVGVKPNELKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRQILRAAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK", "text": "FUNCTION: Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MNLMTTITGVVLAGGKARRMGGVDKGLLELNGKPLWQHVADALMTQLSHVVVNANRHQEIYQASGLKVIEDSLADYPGPLAGMLSVMQQEAGEWFLFCPCDTPYIPPDLAARLNHQRKDAPVVWVHDGERDHPTIALVNRAIEPLLLEYLQAGERRVMVFMRLAGGHAVDFSDHKDAFVNVNTPEELARWQEKR", "text": "FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP cannot be utilized. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MobA family."}
{"protein": "MRAVALFPDEPELRVIEKPKPTPENGEALIRTVAVGIDGSDRRIAAGEIGGDVPDGEDHLVIGHEAVGVVEEPNGTDLARGDVVAPLVRRPVGDGSRFAANGELDMAPPGSFHECGITGAHGYMSEFFTARPGYLVPIPESRAAYGFFVEPASLVEKALDQTEAARSGFDWRPSSAFVLGNGNLGLLALTRLETGDEFERTYCLGRRDRPDPTIDVIENVGGTYVDSRELSLDEFPAVHEPVDFAFETTGHPAHAVEAVDALAPNGVVTLQGIPGSSSTVEIDGGAFHTDLVVTNKAILGVVNARRSHFRAAAEWLAETPESVLDALVTGVYGPDEIDEAFADSAETIKTVVSFDR", "text": "FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily."}
{"protein": "MTVLKPSHWRVLAELADGLPQHVSQLARMADMKPQQLNGFWQQMPAHIRGLLRQHDGYWRLVRPLAVFDAEGLRELGERSGFQTALKHECASSNDEILELARIAPDKAHKTICVTHLQSKGRGRQGRKWSHRLGECLMFSFGWVFDRPQYELGSLSPVAAVACRRALSRLGLKTQIKWPNDLVVGRDKLGGILIETVRTGGKTVAVVGIGINFVLPKEVENAASVQSLFQTASRRGNADAAVLLETLLAELDAVLLQYARDGFAPFVAEYQAANRDHGKAVLLLRDGETVFEGTVKGVDGQGVLHLETAEGKQTVVSGEISLRSDDRPVSVPKRRDSERFLLLDGGNSRLKWAWVENGTFATVGSAPYRDLSPLGAEWAEKVDGNVRIVGCAVCGEFKKAQVQEQLARKIEWLPSSAQALGIRNHYRHPEEHGSDRWFNALGSRRFSRNACVVVSCGTAVTVDALTDDGHYLGGTIMPGFHLMKESLAVRTANLNRHAGKRYPFPTTTGNAVASGMMDAVCGSVMMMHGRLKEKTGAGKPVDVIITGGGAAKVAEALPPAFLAENTVRVADNLVIHGLLNLIAAEGGESEHT", "text": "FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. FUNCTION: Activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the type III pantothenate kinase family. SIMILARITY: In the N-terminal section; belongs to the biotin--protein ligase family."}
{"protein": "MGNCTSHPHHEPQVHFDTVDGMATVKAFAGIRQVTMGVLRIDYEYQTNLGDILDPRSFDFRIISATAEGLTFAKAKAGDKLDATGKELLERAVRQLIDNGADFIVGDCGFLVYWQVMVRDYAQDYAQKKYGRKCPVMMSSLVLALPLLATIPSGGQIGILTASEKSLQAVQKKLPIVIEDQQKEDGGQRSRSVPAAEDPSGIMINFSDPRFKVVGLDEVKDFKHALDAQGADAVNDRRDIAVQIAAYCQKVQEKNPQIAAWLIECTEAGGFAWAIKVGTGLPVWDPITLGRFLSLGFTANVPNVALTLGQHGENPLDPSATTAGKGRCTGEEPGQIHALGAEFQAIREGTL", "text": "FUNCTION: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle. SIMILARITY: Belongs to the aspartate/glutamate racemases family. ALMA1 subfamily."}
{"protein": "MRRTAFIVLSLVALIAPCVTSVAVEDLAQANNIETNVNPNVKVGSRRHLRSEANGRLAVVDEEKVFRDFCGLGPCFDWLKPQNLGGFIYKFVEWASRDRVNFKLKMLKREHQIPIRKRNQ", "text": "FUNCTION: Effector that acts as a broad suppressor of cell death to interrupt plant immunity. Inhibits cell death induced by cell death- inducing proteins, including the PAMP elicitor INF1 from P.infestans. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MVHWTAEEKQIITGLWGKVNVADCGAEALARLLIVYPWTQRFFSSFGNLSSPTAILGNPMVRAHGKKVLTSFGDAVKNLDNIKNTFAQLSELHCDKLHVDPENFRLLGDILIVVLAAHFSKEFTPECQAAWQKLVRVVAHALARKYH", "text": "FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. The beta chain is a component of adult hemoglobin A and D. SIMILARITY: Belongs to the globin family."}
{"protein": "SCMKAAPMKEVSIRGQGSLAYPGLQTQGNLETLSGPNDATRGLTSLADTFEHVIEELLDEQQVIQSSKENKDADLYSSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCSSKGYAKEGCRGIDKRYWNSQCRTTQSYVRALTMDNKKRVGWRFIRIDTSC", "text": "FUNCTION: Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NGF-beta family."}
{"protein": "MKSAVLFLLGIIFLEQCGVRGTLVIRNARCSCISTSRGTIHYKSLKDLKQFAPSPNCNKTEIIATLKNGDQTCLDPDSANVKKLMKEWEKKISQKKKQKRGKKHQKNMKNRKPKTPQSRRRSRKTT", "text": "FUNCTION: May be a cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
{"protein": "MASLTVKAYLLGKEDAAREIRRFSFCCSPEPEAEAEAAAGPGPCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRRDHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAFPSPFGHLSEGFSHSRWLRKVKHGHFGWPGWEMGPPGNWSPRPPRAGEARPGPTAESASGPSEDPSVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPVSPESSSTEEKSSSQPSSCCSDPSKPGGNVEGATQSLAEQMRKIALESEGRPEEQMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL", "text": "FUNCTION: Autophagy receptor required for selective macroautophagy (aggrephagy) (PubMed:34471133, PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:28404643, PubMed:22622177, PubMed:33509017). Functions as a bridge between polyubiquitinated cargo and autophagosomes (PubMed:34471133). Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:28404643, PubMed:22622177). Along with WDFY3, involved in the formation and autophagic degradation of cytoplasmic ubiquitin- containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with WDFY3, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:24128730, PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). SUBCELLULAR LOCATION: Cytoplasm, cytosol Preautophagosomal structure Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Nucleus, PML body Cytoplasm, myofibril, sarcomere Note=In cardiac muscle, localizes to the sarcomeric band (By similarity). Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co- localizes with TRIM5 in cytoplasmic bodies. When nuclear export is blocked by treatment with leptomycin B, accumulates in PML bodies."}
{"protein": "MLQGHERSITQIKYNREGDLLFSCSKDQKPNVWYSLNGERLGTYDGHQGAVWCLDVDWESRKLITGAGDMTTKIWDVEYGTIIASIPSKSSVRTSNFSFSGNQAAYSTDKAMGQSCELFIIDVRNADSSLAEQTPTLRIPMTESKITSMLWGPLDETIITGHDNGNIAIWDIRKGQKVVDSGSDHTAGINDMQLSKDGTMFVTASKDTTAKLFDSESLMCLKTYKTERPVNSAAISPILDHVVLGGGQDAMEVTTTSTKAGKFDSRFFHLIYEEEFARLKGHFGPINSLAFHPDGKSYASGGEDGFVRVQTFDSTYFENIFE", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit I family."}
{"protein": "MYYLKNTNFWMFGFFFFFYFFIMGAYFPFFPIWLHEVNHISKGDTGIIFACISLFSLLFQPIFGLLSDKLGLRKHLLWVITGMLVMFAPFFIYVFGPLLQVNILLGSIVGGIYLGFIYNAGAPAIEAYIEKASRRSNFEFGRARMFGCVGWALCASIAGIMFTINNQFVFWLGSGCAVILALLLLFSKTDVPSSAKVADAVGANNSAFSLKLALELFKQPKLWLISLYVVGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIVNRIGGKNALLLAGTIMSVRIIGSHSHTALEVVILKTLHMFEIPFLIVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGKMYESIGFQGAYLVLGIIRVSFTLISVFTLSGPGPFSLLRRRESVAL", "text": "FUNCTION: Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Oligosaccharide:H(+) symporter (OHS) (TC 2.A.1.5) family."}
{"protein": "MSLNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSVTSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHSERYEASAEFTQVWRRLLLGETVDFNGKHIHVRGAKLLFPPIQQPYPPLYFGGSSDVAQELAAEQVDLYLTWGEPPELVKEKIEQVRAKAAAHGRKIRFGIRLHVIVRETNGEAWQAAERLISHLDDETIAKAQAAFARTDSVGQQRMAALHNGKRDNLEISPNLWAGVGLVRGGAGTALVGDGPTVAARINEYAALGIDSFVLSGYPHLEEAYRVGELLFPHLDVAIPEIPQPQPLNPQGEAVANDFIPRNVAQS", "text": "FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates. SIMILARITY: Belongs to the SsuD family."}
{"protein": "MAGRGGRVLLALCAALVAGGWLLAAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQRGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNLKKIVDQNSKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGTAHEYSSCPDDAIFQSLARAYSSFNPVMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKSYWEDNKNSLINYLEQIHRGVKGFVRDLQGNPIANATISVDGIDHDVTSAKDGDYWRLLVPGNYKLTASAPGYLAITKKVAVPFSPAVGVDFELESFSERKEEEKEELMEWWKMMSETLNF", "text": "FUNCTION: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein Secreted Note=Associated with the secretory granule membrane through direct binding to lipid rafts in intragranular conditions. SIMILARITY: Belongs to the peptidase M14 family."}
{"protein": "MDQQVKQERLQGRLEPEIKEFRQERKTLQLATVDAQGRPNVSYAPFVQNQEGYFVLISHIARHARNLEVNPQVSIMMIEDETEAKQLFARKRLTFDAVASMVERDSELWCQVIAQMGERFGEIIDGLSQLQDFMLFRLQPEQGLFVKGFGQAYQVSGDDLVDFVHLEEGHRKISNG", "text": "FUNCTION: Involved in heme degradation (PubMed:15205415, PubMed:22627893, PubMed:28481076, PubMed:28607990). Catalyzes the degradation of heme to biliverdin, with the release of iron (PubMed:22627893, PubMed:28607990). Forms biliverdin beta and delta (PubMed:28607990). Binds heme with high efficiency (PubMed:15205415, PubMed:22627893). SIMILARITY: Belongs to the heme oxygenase HugZ/HutZ family."}
{"protein": "MKSDLWYFLLFCFQVEALTGEINDSTKSEMFTFHDGGVQILCKFNAIVSQYKMELLKGTEVLCDLTTTKENGNTVSKNPKFCQSQSSSDGVSFFLYNLDSSHASYYACQLSIFDPPPFQRKNISREYLNVYESQTCCQLKFWLPIGCAAFVVVYIFGCIFLCWLTKKKYRSSVHDPNSEYMFMAAVNTAKKPGLTGVTHNLELCGTQA", "text": "FUNCTION: Enhances all basic T-cell responses to a foreign antigen, namely proliferation, secretion of lymphokines, up-regulation of molecules that mediate cell-cell interaction, and effective help for antibody secretion by B-cells. Essential both for efficient interaction between T and B-cells and for normal antibody responses to T-cell dependent antigens. Does not up-regulate the production of interleukin- 2, but superinduces the synthesis of interleukin-10. Prevents the apoptosis of pre-activated T-cells. Plays a critical role in CD40- mediated class switching of immunoglobin isotypes (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MLFKQWNDLPEPKHLLDLPEISKNLQSLEVCPVPKVEFPQDLDVPQYSTAVITTKIMNPLFPKNLLQLTSIGEIKTTLTVKSPSLPQSSGKHSWNYDENFPNEVDPDQKNDTADETVYGFSFPIYSFGKTLLFSMEENFISISPIFGNMISRSIISQLAQFSPDIIVIGTSDKIASMKVMTENECTLQPPEFITGFIGSVLTQLIVGPSKGLKFKCLVAPSEGPNGFEKLSLSDMGSLVDLCGQWLGFEPSRYSEECYRLWRCDSAAIGAQSGLYI", "text": "FUNCTION: Involved in 20S proteasome assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PSMG1 family."}
{"protein": "MPRLAFLLRPGWLALALVVVAFTYLCFTVLAPWQLGKNAKTSRENQQIRYSLDTPPVPLKTLLPQQDSSAPDAQWRRVTATGQYLPDVQVLARLRVVEGDQAFEVLAPFVVDGGPTVLVDRGYVRPQVGSHVPPIPRLPVQTVTITARLRDSEPSVAGKDPFVRDGFQQVYSINTGQVAALTGVQLAGSYLQLIEDQPGGLGVLGVPHLDPGPFLSYGIQWISFGILAPIGLGYFAYAEIRARRREKAGSPPPDKPMTVEQKLADRYGRRR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SURF1 family."}
{"protein": "MVKAICVVKGAVVNGTIIFSQENEGSPVYVNGTISGLSGGLHGFHIHEFGDTSNGCLSAGAHFNPFHVEHGGPNSAIRHVGDLGNITSCPSSKVANVLIQDNVISLFGDLSIIGRTLVVHENQDDLGLGGNLSKTTGNAGARVACGILAKI", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Protects spores from cellular damage caused by UV LIGHT. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MTDVERMVLRPNHEGEMCPVCGDRVSGYHYGLLTCESCKGFFKRTVQNKKQYQCSAEANCHVDRTCRKRCPSCRFQKCLTMGMKMEAVRADRMRGGRNKFGSFYKKDRAHRMQRNAMRVSTVQVPAVLGAQSQAQTFYQPPEHQVSSSTTDQNNQINYFDQTKIKTEYIKTEYDAHLQSPTLSSSTNQQLSVSDFIMRPGYLVDPQDSLAVLLGSTIDDPLLRHTFPAAYQLNEVKQEPFDYSEQFIHHSLHDYPTYTSNTTNYATMMPMTTVSSTQSLVTSTSSTTTGRMTEASSTSPILPLCPAPTEKTVDHFYNSSIAEMCKTLPDDAQIARIFTSVKGTSKPEKHAFSIQVAEENLKDIVIWAKNDQLFSKLSLDDQMILLQTSWTTVHIVDITNAMVHGNLLSQYKMSNGDEVPVGLVALLGNQTFVSSWNDVVIRLRNMGFTNFDYCAFRFLALFDQSMDSFPAVSTARSRVLQSWREVRCTTAFLEIFEQIRRLAYDSLRYLWNLHSNCPTNWEQFFPEASLVLEMIRTTVNRSASSSVTAITQVPAIQLPTPQATYTAVPYMAS", "text": "FUNCTION: Orphan nuclear receptor and probable transcription activator, required during development (PubMed:10772806, PubMed:15314147). Plays a role in male tail tip morphogenesis regulating the expression of the transcription factor dmd-3 in a negative feedback loop (PubMed:21408209). Regulates vulval precursor cell (VPC) differentiation, in concert with homeobox protein lin-39 (PubMed:15314147). Involved in promoting embryogenesis, in concert with homeobox protein nob-1 (PubMed:15314147). May play a role in modulation of lifespan and immunity (PubMed:29748542). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family."}
{"protein": "MYKKEKNRFLKSKQINYINWRFFLLYGFIFLSLFILTLRVIFLQIISSNRLITEGDRRTLRTQSLLSTRGAIKDRRGYPLAVTVLVNAICADPSVILKTKNIKNHKRWQALSEILSIPLKKMFLRINSHKKSKFIYLARQINPEISEYIKKLQLPGIFLLEESKRYYPFKEISAQLVGFTNIDGIGIEGIEKSFDLLLTGKPGKRKIRQDNKGHVIEKISLVHKRASNNLNLSIDTKLQTIVYNELQEGVKKSQSDSGTAILINIKSGEVLAMANSPSYNPNNIRHIIQKNVRNKAITDLFEPGSTVKPIVIIEALKLGIIQENSIIDTKPFLIQKHQIKDVSYHEKLTITGILQKSSNVGVSKIALSMPTLKLLDSYIKFGLGKPTQLGLIGEKHGFFPPKKRWSNLDKATLSFGYGLMVTPLQLARLYSTIASYGIYRPLSIIKTDRPTGGKQIFPPKYVKKVINMMESVSQPGGGGLQAAVRGYRVAVKTGTAKKVGIHGRYIKKYTAYTAGIAPASDPRFSLIIILDNPQGKKYYGGAVSAPVFSNIMKLILKKMNIKPDNLSNQKMILKSNKRN", "text": "FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily."}
{"protein": "MNYFILILPILPYLYGPAVCSEDETRLVKTLFTGYNKVVRPVSHFKDPVVVTVGLQLIQLISVDEVNQIVTSNVRLKQQWKDVHLQWNPDDYGGIRKIRIPSTDLWKPDLVLYNNADGDFAIVHETKVLLEHTGMITWTPPAIFKSYCEIVVLHFPFDLQNCSMKLGTWTYDGNLVIINPDSDRPDLSNFMESGEWVMKDYRSWKHWVYYACCPDTPYLDITYHFLLLRLPLYFIVNVIIPCMLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVIASIIITVIVINTHHRSPSTHIMPAWVRKIFIDTIPNMMFFSTMKRPSQERQEKRLFPADFDISDISGKPMPASVTYHSPITKNPDVRSAIEGVKYIADTMKSDEESNNAAEEWKFVAMVLDHILLCVFMAVCIIGTLGVFAGRLIELSML", "text": "FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-1/CHRNA1 sub- subfamily."}
{"protein": "MNDRELDLTEEQKALKAKYPPITKKYEYLDHTADVQIHSWGNSLEEAFEQCAMGMFGYMTDTETVEPIDTVEVESEGDDMESLLYHFLDDWLFKFSADIFFIPREVKVLHIDRMRYKIRSIGWGEEFSINKHPQGTEVKAITYSAMQIHETEQPEIFVIIDI", "text": "FUNCTION: Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB. Together with ddx1, acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (By similarity). SIMILARITY: Belongs to the archease family."}
{"protein": "MKHIGRIVSFPIGLVLIAVGIIIFVVVNRTIKDEFKKAAVVIPDNGAEEIVDPWVRFIGNEGDPNNVRTYTFMAYNLTNPIETMQGHLPKYQEVGPYSYNYIYERINANLYEDDEKLSFKLWKRYFPIVADGYRDPTKDTIYHFNLVYGAAVKQAGSEVALSVALTAAAMGKIITGLTDPSFKVKAGFAAAPTVTAGAFSNLLTAAGNDPATACGLWQTSTSSSTPLVPFSVPIIAGSPSDISQAQCQALFDPSNKFSLTDPTNVGVYLLNPAGSKAALLASPFGLTSVQADLIMKYQLALTSTFVPTTLVSRFAECSDPKTCTNNPLYFGLLQWAKNPSLLGQSVFAIPNSGVPAAPEFGIYTSSELSLTKAGSLFLNTSTINLITPTSIGTILVYGQKLKADPTSIPPALYAPFSSGEFDAIVKYTGYIMAAFVDGDIIKNQIFKDYQGGPIVKHTVHDFLFNSTDPLLKLMYPDTPSAWVSSPLDNIQDVKVANATLHTDEIYTGVGDIDLVSSPITFEGEEELNYNKKIKVSGSFAEQLPPSYLSKDPEAPVNVFTDEFARSLSFRKEVGGNFGGIPYYRYRINESNWEINPDYFQTIPYLLNLTSIKSGAPAYLSRPRLKGIDVGYYYKAGITDLINDDEDLDVFADYEPRSGKAIHGRYSLQVNTYIQGSDGTNSTLYNKYSAFRSDVVHPMFWGVNIIAATQEQIDILTKAYKVDSFRYAITVILIVVGGFLSLISGGLFVLDKIIDL", "text": "FUNCTION: May act as a lysosomal receptor (By similarity). May be involved in macropinocytosis and fluid phase exocytosis. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Note=Localizes to membranes of endolysosomal vesicles and macropinosomes. SIMILARITY: Belongs to the CD36 family."}
{"protein": "MFRKKKKKRPEISAPQNFQHRVHTSFDPKEGKFVGLPPQWQNILDTLRRPKPVVDPSRITRVQLQPMKTVVRGSAMPVDGYISGLLNDIQKLSVISSNTLRGRSPTSRRRAQSLGLLGDEHWATDPDMYLQSPQSERTDPHGLYLSCNGGTPAGHKQMPWPEPQSPRVLPNGLAAKAQSLGPAEFQGASQRCLQLGACLQSSPPGASPPTGTNRHGMKAAKHGSEEARPQSCLVGSATGRPGGEGSPSPKTRESSLKRRLFRSMFLSTAATAPPSSSKPGPPPQSKPNSSFRPPQKDNPPSLVAKAQSLPSDQPVGTFSPLTTSDTSSPQKSLRTAPATGQLPGRSSPAGSPRTWHAQISTSNLYLPQDPTVAKGALAGEDTGVVTHEQFKAALRMVVDQGDPRLLLDSYVKIGEGSTGIVCLAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHFNVVEMYKSYLVGEELWVLMEFLQGGALTDIVSQVRLNEEQIATVCEAVLQALAYLHAQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRSLYATEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKVSPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVPLIQLYRKQTSTC", "text": "FUNCTION: Serine/threonine protein kinase that plays a role in the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR- mediated transcription. Inhibits also ESR1-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cotranslocates into nucleus with AR in response to androgen induction. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MDVDVFNGWGRPRFEDESLMPPGFRFHPTDEELITYYLLKKVLDSNFSCAAISQVDLNKSEPWELPEKAKMGEKEWYFFTLRDRKYPTGLRTNRATEAGYWKATGKDREIKSSKTKSLLGMKKTLVFYKGRAPKGEKSCWVMHEYRLDGKFSYHYISSSAKDEWVLCKVCLKSGVVSRETNLISSSSSSAVTGEFSSAGSAIAPIINTFATEHVSCFSNNSAAHTDASFHTFLPAPPPSLPPRQPRHVGDGVAFGQFLDLGSSGQIDFDAAAAAFFPNLPSLPPTVLPPPPSFAMYGGGSPAVSVWPFTL", "text": "FUNCTION: Transcription activator of STM and KNAT6. Involved in molecular mechanisms regulating shoot apical meristem (SAM) formation during embryogenesis and organ separation. Required for the fusion of septa of gynoecia along the length of the ovaries. Activates the shoot formation in callus in a STM-dependent manner. Seems to act as an inhibitor of cell division. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRNTSKYYLVDASVLPKVFIKVVEAKRILASGAIKNVNEAVRKVGISRSAYYKYKDHIFPFYETSQGKVITLFFTVEDYAGILSSIINRIADSKANIITINQNIPINGLADVTITIETGQMTRDIKDLLDDISSIEGVKRQEILARE", "text": "SIMILARITY: Belongs to the UPF0735 family."}
{"protein": "MLFAKAFQSATVAGAVILAALVDVAHSTPLDDPGQCGLEAVAQCCTSLRESAVGDKVFAYGDIEYFRAKRSYYSVTTSLNSACIVLPESAEDVSTVLTTLTQPDLAETCPFAIRSGGHSMVVGFSDIAAGVTLDLSKLNHTIYHPETETVSLGPGGRWVNVYEELRPDNVMVSGGRFSSVGVGGFLTGGGITIYSAQRGLACDDVVSFDVVLANGTLIQATNATNPDLFHTLKGGSGNLGVVTNFEVRAFPQTQIWGGYTSYNVSKTPELARTLQNFTSNIEQDPKALLVTFWTYDTLTDVNRAANAMYYTDPVEYPEAFNDYYAIENISSTVHTRSIESLVTELEDTTNWFRVLFVTLAFKNDARVIEHGANLYQEYIDTIKANVSGGDWLVIAGFQPMPTLFGTSGQENGGNIIGLENNGDKIVLLFEAFWERTQDDELFEPLADELIHNLEEYARSLEQDSDFLYLNYADGWQDPISGYGGDNIEQLRAAAEKYDPNGVFQTQVPGGFKISKVPVAEQKK", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes (PubMed:34468074). The pathway begins with the synthesis of the backbone drimenol by the terpene cyclase drtB using farnesyl pyrophosphate (FPP) as substrate (PubMed:34468074). The cytochrome P450 monooxygenase drtD is then responsible for the hydroxylations at C-6, C-9 and C-12, as well as the oxidation of hydroxyl groups at C-6 and C-11 to a ketone and an aldehyde, respectively (PubMed:34468074). Then, the biosynthesis can go in two directions, either the hydroxylated drimenol is further hydroxylated at C-2 and C-3 by an enzyme(s) not associated with the drt cluster, or the FAD-binding oxidoreductase drtC further oxidizes C-11 or C-12 to form the butyrolactone ring (PubMed:34468074). DrtB, drtD and drtC are solely responsible for the formation of the different drimane structures observed during drimane sesquiterpenes biosynthesis (PubMed:34468074). The polyketide synthase drtA synthesizes different lengths (C6 and C8) of PKS chains, which are then oxidized to varying degrees by the short-chain dehydrogenase drtF (PubMed:34468074). Finally, these PKS chains are transferred onto drimane sesquiterpenes by the acyltransferase drtE, forming the sesquiterpene esters (PubMed:34468074). In addition to the different fatty acyl-CoA chains produced by drtA, drtE is also able to use cinnamoyl-CoA as a substrate (PubMed:34468074). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MEVIHAWSAPRSLSTTLMYSFAQRDDIEVLDEPLYAAFLKSTGVDRPYKDELLSKMECDGEKVVKDIIYGPGKKKYRFCKHISKQRLLGLPSELMSEGKHFILIRNPLNILPSFEKIHPSSFHELGLGELVSIYSDLCQMGTPPAIIDADELQRDPEATLRSLCDDLEIPFQASMLKWEAGPIPEDGLWAPWWYETLHKSTGFSSPQKYPQTFPLMHYDLLEQCLPLYNILRCHMKHKSSLLSSTLPPPSLPVPENAKLLAWVGDEIVPREMAKVSVFDSVVQGGDSVWEGLRIYKGKVFKLEEHLDRLSDSAKALAFNNVPTREEIKEAIFRTLITNGMFDNTHIRLSLTRGKKVTSGMSPAFNRYGCTLIVLAEWKPPVYDNDGGIVLVTATTRRNSPNNLDSKIHHNNLLNNILAKIESNNANVDDAIMLDKDGFVSETNATNIFMVKKDRVLTPHADYCLPGITRATVMELVVKENFILEERRISLSEFHTADEVWTTGTMGELSPVVKIDGRVIGEGKVGPVTRRLQNAYKKLTDGSGVPIPTYQEVKNLEPCV", "text": "SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MGEPRSQPPVERPPTAETFLPLSRVRTIMKSSMDTGLITNEVLFLMTKCTELFVRHLAGAAYTEEFGQRPGEALKYEHLSQVVNKNKNLEFLLQIVPQKIRVHQFQEMLRLNRSAGSDDDDDDDDDDDEEESESESESDE", "text": "FUNCTION: Histone-like protein which promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes (PubMed:10856248, PubMed:11447119). Part of the chromatin-accessibility complex (CHRAC) which uses energy/ATP to increase the general accessibility of DNA in chromatin (PubMed:10856248, PubMed:11447119). As an heterodimer with Chrac-14, binds DNA and facilitates nucleosome sliding by Acf (PubMed:16260604). As part of the CHRAC complex, required for oogenesis (PubMed:26851213). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGKAKGIRILITLECTECRSNTNKRSNGVSRYTTQKNRRNNPERIELKKYCPHCNKSTIHKEIK", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family."}
{"protein": "MRVVIAQCSVDYVGRLDAHLPMADRLILIKADGSVSIHADDRAYKPLNWMTPPCTFEESAIEDIDGEDTGEKLWLVENPKGEQLRITIAQIHQEIDMDLGEDPGLVKDGVEAHLQELLAEHIETLGEKYSLVRREYPTAIGPVDIMAKNSKNEFVAVEVKRRGGIDGVEQLTRYLELLNRDDLLAPVHGVFAAQEIKPQARTLAEDRGIRCVVLDYQELRGIESNELRLF", "text": "FUNCTION: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NucS endonuclease family."}
{"protein": "MGQALGCIQVDQSNVAIKETFGKFDEVLEPGCHCLPWCLGSQVAGHLSLRVQQLDVRCETKTKDNVFVTVVASIQYRALAESAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAASRMREAASEKAEAEKILQIKRAEGEAESKYLSGMGIARQRQAIVDGLRNSVLAFSESVPGTSSKDVMDMVLVTQYFDTLKEIGASSKSNSVFIPHGPGAVRDIASQIRDGLLQGNSAAE", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side."}
{"protein": "SDCTLRNHDCTDDRHSCCRSKMFKDVCTCFYPSQAKKELCTCQQPKHL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 12 subfamily."}
{"protein": "EDICSLPPEVGPCRAGFLKFAYYSELNKCKLFTYGGCQGNENNFETLQACXQA", "text": "FUNCTION: Inhibits trypsin."}
{"protein": "MTSKIEQPRWASKDSAAGAASTPDEKIVLEFMDALTSNDAAKLIEYFAEDTMYQNMPLPPAYGRDAVEQTLAGLFTVMSIDAVETFHIGSSNGLVYTERVDVLRALPTGKSYNLSILGVFQLTEGKITGWRDYFDLREFEEAVDLPLRG", "text": "FUNCTION: Catalyzes the conversion of limonene-1,2-epoxide to limonene- 1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide as substrates and also has some activity with 1-methylcyclohexene oxide, cyclohexene oxide and indene oxide as substrates. SIMILARITY: Belongs to the limonene-1,2-epoxide hydrolase family."}
{"protein": "MSRRNSYTWDELLQCARGEMFGPGNAQLPAPPMLMFDRITHIDSVGGAFDKGMIVAELDVKPELWFFDCHFISDPVMPGCLGLDAMWQMVGFYLGWIGGKGRGRALGVGEVKFRGQVLPHNRLVTYRINLKRVILRKLVMGIADAEMECDGKVIYEANDLRVGLFTSTDDF", "text": "FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioester dehydratase family. FabA subfamily."}
{"protein": "MAVSLNDIKTKIASTKNTSQITNAMQMVSAAKLGRSEEAARNFQVYAQKVRKLLTDILHGNGAGASTNPMLISRSVKKTGYIVITSDRGLVGGYNSSILKAVMELKEEYHPDGKGFEMICIGGMGADFFKARGIQPLYELRGLSDQPSFDQVRKIISKTVEMYQNELFDELYVCYNHHVNTLTSQMRVEQMLPIVDLDPNEADEEYSLTFELETSREEILEQLLPQFAESMIYGAIIDAKTAENAAGMTAMQTATDNAKKVINDLTIQYNRARQAAITQEITEIVAGASALE", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family."}
{"protein": "MTPNGKPAIRLSLRAGERIFINGAVLRADRKVSLELLNDATFLLENHVLQPEDTTTPLRQLYFAAQMMLIEPAMREQAHSTFAQMLKGMFSTFKDAEILNALKLVDELVHNGRIFEALKTIRAQYPREAELMGLESPVLPVAATRKSAEANP", "text": "FUNCTION: Has a post-transcriptional repressor function in flagellum biogenesis. Associates with the 5'-UTR of fljK mRNA and promotes its degradation. SIMILARITY: Belongs to the FlbT family."}
{"protein": "MPPSPDFEAFSLTPIDQANGQVFFFYNISYRVRNEASALQTIHNAIDVLLEKVPFLNGEIAFPAPVPDANNVLIVRPPRAKSEDQVPLVQVKRHSNCALPVKKLEQSPFNVPSSLPLNGLFNPLAAYPTPNRPTPVIRFQINLVNDGLILTLAFNHAVFDALGAAVIVKLLAESCRNQDKIGMDGRLGIPSTQARVRSPLLALSSRLKKNNRARVDAPSPSEFSENISHRPVAAPPPLKDECFVFCAEKLQQLRIACTSILEKLHENQKSVTGQGDVRFLSINDVLTALICESIAQARHAAKHPYRDEKLHAKPSVSECLMAVDLRKFVEPPLPHDYMGNAAIPLRFEVSSQRHASPDFHRAVREVPTGLNTSFFLAIAKTAYTIRAKLARFGESYIDSLSSFLNAHEEQKAVNILPACAIVSSLRHIKTYELQFGAELGEIQAFETGIPWVNGSCIILPLCANSSDVAGSAPWNVRITLDESTMYCFKNEPALRWALLEQGKSKVLGPCDCKADV", "text": "FUNCTION: O-acyltransferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD- binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O- acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family."}
{"protein": "MKLFLLLVFFASMLIDGLVNADGYIRGSNGCKISCLWGNEGCNKECKGFGAYYGYCWTWGLACWCEGLPDDKTWKSESNTCGGKK", "text": "FUNCTION: Causes a slow progressive depressant flaccid paralysis, when injected into S.falculata blowfly larvae. Inhibits dose-dependently the total sodium (Nav) currents both in dorsal root ganglia neurons and in ventricular myocytes. Is toxic to mice by intravenous injection, but not by subcutaneous or intracerebroventricular injection. Produces antiarrhythmia in rat. Is then active on both mammals and insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family."}
{"protein": "MEELLPDRQVWANMDPEERMLAAATAFTHICAGQGEGDVRREAQSIQYDPYSKASIAPGKRPTLPVQLQYPHVESNVTSETVSEASQRLRKPVMKRKVLRRKPDGEVLVTDESIISESESGTENDQGLWDLRQRLMNVQFQEDKESSFDISQKFNPPHEYQGISQDQLICSLQREGMGSPAYEQDLIVASRPKSFILPKLDQLSRNRGKTDRVARYFEYKRDWDSIRLPGEDHRKELRWGVREQMLCRAEPQSKPQHIYVPNNYLVPTEKKRSALRWGVRCDLANGVIPRKLPFPLSPS", "text": "FUNCTION: Plays a role in ciliogenesis. SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. SIMILARITY: Belongs to the HYLS1 family."}
{"protein": "MDEWLAEFIKRTILKLPFSETVTILKAWGFLTESELQTFTFRYPKDVTATEVVRLCEAKNATVDHAAALDLVFNHAYSNKKSWTVYQMSKPSESENDLFDASEFKLQFKKSIHAVSKNVTLNFKQFGEALWIRIAWGTHNTRPNQYKATFAVYHSQTPYVFITGLGKACRPLMCQALVIAAKYSQIQEMELKSRCLESLKDIVFKRFNQPFSSHHSIPHEKALIPKIVDPRVIYENMREKDRVSHLTRETFGEGPLPKLELASYKLETMFRAESIMDGNLTAVNEPFRCVVKFSSPHLLEAIRSLAPAGIAEAPISTLLSCIPHKARNSFKITEKRGMHPTSSQTTNF", "text": "FUNCTION: Probable component of a centromeric complex involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Localizes exclusively in the centromeres. SIMILARITY: Belongs to the CENP-N/CHL4 family."}
{"protein": "MAAVVGVSLKRGFSATALGRVGLQFQACREAQTAAAAAPRIKTFAIYRWDPDKAGDKPRMQTYKVDLNKCGPMVLDALIKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTDLGKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEDREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDEFTEERLAKLQDPFSLYRCHTIMNCTQTCPKGLNPGKAIAEIKKMMATYKEKRALA", "text": "FUNCTION: Iron-sulfur protein (IP) subunit of the succinate dehydrogenase complex (mitochondrial respiratory chain complex II), responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family."}
{"protein": "MLFFGFLLAFLSAVPGTEGEIIPRCELVKILREHGFEGFEGTTIADWICLVQHESDYNTEAYNNNGPSRDYGIFQINSKYWCNDGKTSGAVDGCHISCSELMTNDLEDDIKCAKKIARDAHGLTPWYGWKNHCEGRDLSSYVKGC", "text": "FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 22 family."}
{"protein": "MDTEGFGELLQQAEQLAAETEAVSELPHVERNLQEIQQAGERLRSRTLTRTSQDTADVKASILLGSRGLDIFHISQRLESLSAATTFEPLEPVKDTDIQGFLKNERDNALLSAIEESRRRTFLLAEEYHRDSMLVQWEQVKQRVLHTLLGAGEDALDFSQEVEPSFVSEVGVPGRSALDSVEVAYSRQIYVFNEKIVNGHLQPNLGDLCASVAESLDDKNVSEMWLMVKQMTDVLLVPAKDTLKSRVSVDMQMAFVRQALQFLENSYKNYTLVTVFGNLHQAQLGGVPGTYQLVCSFLNIKLPTPLPGRQDGEVEGHPVWALIYFCLRCGDLSAAMQVVNKAQHQLGDFKIWFQEYMNSPDRRLSPATENKLRLHYRRVLRNSADPYKRAVYCLIGKCDIGDNHGEVADKTEDYLWLKLNQVCFDEDGSSSPQDRMTLAQLQKQLLEDYGESHFSASHQPFLYFQVLFLTAQFEAAIAFLFRVERLRSHAVHVALVLYELKLLLKSSGQSAQLLSQEAGDPPMVRRLNFIRLLMLYTRKFESTDPREALQYFYFLRNEKDSQGENMFMRCVSELVIESREFDMLLGRLEKDGSRKPGVIDKFAGDTRAIITKVASEAENKGLFEEAVKLYELAKNADKVLELMNKLLSPVIAQVSEPQSNKERLKNMAVAIAERYRANGVAGEKSVDNTFYLLLDLMTFFDEYHAGHIDRAYDVIERLKLVPLSQDSVEERVAAFRNFSDEVRHNLSEVLLATMNILFTQYKRLKGAAAGTPGRPQRTLEDRDMLLRIQARALITFAGMIPYRMAGDTNARLVQMEVLMN", "text": "FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. SUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane protein Nucleus, nuclear pore complex Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. SIMILARITY: Belongs to the nucleoporin interacting component (NIC) family."}
{"protein": "MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDATDWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLKRNLDTYQKRLRFYWRPHCRGQTPGC", "text": "FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular lipids, exerting anti-inflammatory and immunosuppressive functions (PubMed:10455175, PubMed:10681567). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:10455175). In draining lymph nodes, selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are precursors of the anti-inflammatory lipid mediators, resolvins (By similarity). During the resolution phase of acute inflammation drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses dendritic cell activation and T-helper 1 immune response (By similarity). May act in an autocrine and paracrine manner (By similarity). Via a mechanism independent of its catalytic activity, promotes differentiation of regulatory T cells (Tregs) and participates in the maintenance of immune tolerance (By similarity). May contribute to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MAAGDGDVKLSTLGSGGERGGDGSPGGAGATAARSSWVAALLATGGEMLLNVALVALVLLGAYRLWVRWGRRGLCSGPGAGEESPAATLPRMKKRDFSLEQLRQYDGARTPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHSKQD", "text": "FUNCTION: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. May serve as a universal non- classical progesterone receptor in the uterus. Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus. Plays a role in adipocyte function and systemic glucose homeostasis. In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1. SUBCELLULAR LOCATION: Membrane; Single- pass membrane protein Nucleus envelope Endoplasmic reticulum. SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily."}
{"protein": "MEEFRRSYSRLCRESGAEPQEAVLQQLHQLPRGRLDLATQSLTVETCRALGKLLPRETLCTELVLSDCMLSEEGATLLLRGLCANTVLRFLDLKGNNLRAAGAEALGKLLQQNKSIQSLTLEWNSLGTWDDAFATFCGGLAANGALQRLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNVGLLGGRALMNCLPSNRTLWRLDLAGNNIPGDVLRAVEQAMGHSQDRLTTFQENQARTHVLSKEVQHLREEKSKQFLDLMETIDKQREEMAKSSRASAARVGQLQEALNERHSIINALKAKLQMTEAALALSEQKAQDLGELLATAEQEQLSLSQRQAKELKLEQQEAAERESKLLRDLSAANEKNLLLQNQVDELERKFRCQQEQLFQTRQEMTSMSAELKMRAIQAEERLDMEKRRCRQSLEDSESLRIKEVEHMTRHLEESEKAMQERVQRLEAARLSLEEELSRVKAAALSERGQAEEELIKAKSQARLEEQQRLAHLEDKLRLLAQARDEAQGACLQQKQVVAEAQTRVSQLGLQVEGLRRRLEELQQELSLKDQERVAEVSRVRVELQEQNGRLQAELAAQEALREKAAALERQLKVMASDHREALLDRESENASLREKLRLREAEIARIRDEEAQRASFLQNAVLAYVQASPVRTLSPPK", "text": "FUNCTION: Component of the proteinaceous fiber-like linker between two centrioles, required for centrosome cohesion. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to the proteinaceous linker between the proximal ends of the centrioles."}
{"protein": "GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL", "text": "FUNCTION: Algogenic for animals, human and insects (PubMed:7826413). At high concentrations (0.5-1 uM), it acts as a pore-forming protein that forms nonselective cation channels both in cell and artificial membranes (PubMed:7826413). It is weakly selective for cation over anions channel conductance is identical in both directions. At lower concentrations (1-10 nM), this heterodimer inhibits cardiac L-type calcium currents in isolated rat cardiac ventricular myocytes (PubMed:10336635). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the ectatomin family. Ectatomin-Et subfamily."}
{"protein": "MTDTNEKIRSLFLTALMVFSVFAGTIAFSGGAAAAANVSVQQAAEYDSGTVELALNGSTGSTVNTGDIDIYVDGNKNPSNYGVSSVDTTDDGTTGRLQFSLDQDVQPNRNLTVKVSGLTGGDNTVVAEDIDVTSQTIDADDDSGDTNAFRGEVLAIRADGDTDNDDATSSTKIVVEDSNGAVVTQDTYTANSKVYTYETENLDTGEEYEVSVAGDADENITISNLDLNVNIDDDVGDGANIDDKDTLAVNVSTTRGGEPANATLFNEDDDKVATQVESLKGNENVVFDFGNQSADDSPYYVKVTDNQTGVSAESDQINVSESDDGEASFESSTVQDNIGDVVNITVQVDNTEDAVINIGDENDDNYYIQGQLEDDNGDGEVTVQFNSYTAGNYSDSTVLSVPGDDDIDNIKEGGDYTRGSLSGDTLEAGSYSMNVTAGTSPDVTSPDTVGTLRLNENSVENIQTWAAPSDADIDDDDVDIYDRIGENLTQSDDVAAEDVVVHEIQASGIEGALEYEQEDGSASDVTEAFIAATDTTPYRINDSDATTSGLRLYVNRTDVGANADANPIDFSNSSDAVTVVDDPDNNTYFVAVDTSDVVFENGKTIVKEEDTRLNATFSVREGPLTDDRNSDSAIYTTSERDATLDLDDSGVVTVSAAAGQEVTGETNVAPGSELEVEMESESDANPFVIRPEVDVATDGTYTATADFQDYSAGTNFTVQTLDVDGDSDFSDEEDGRIVEADTATVSISEQESDGSEVVVDSAQLSEGGFIAIHAGNASGDVVGNSEYLGAGSHEDITVTLDEPMDEDFTAVAMPHQDTNGNEAYDFPGDDDPYTQNGSAVTDSANVTIVEEEQTEAPDTETETEAPDTETEEETDAPATDEPATDESETTAAEGPGFTAAIALIALVAAALLAVRRDN", "text": "FUNCTION: S-layer protein. The S-layer is a paracrystalline mono- layered assembly of proteins which coat the surface of the cell. In H.hispanica, the S-layer contains two different glycoproteins, Slg1 and Slg2, which share highly similar amino acid sequences. SUBCELLULAR LOCATION: Secreted, cell wall, S-layer Cell membrane. SIMILARITY: Belongs to the halobacterial S-layer protein family."}
{"protein": "MKNNKKVGTEDSTKWMLESVEIDPKGDSSVKQPESTINSNNPESSGAGGGILKNVSKNLAVGSIIRSMSVNKWRKSGNLGSPSTRKSGNLGPPLPVSQVKRPGPQRVERTTSSAARGLQSLRFLDRTVTGRERDSWRSIENRFNQFAVDGRLPKDKFGVCIGMGDTLEFAAKVYEALGRRRQIKTENGIDKEQLKLFWEDMIKKDLDCRLQIFFDMCDKDGDGKLTEEEVKEVIVLSASANRLVNLKKNAASYASLIMEELDPNEQGYIEMWQLEVLLTGIVSNADSHKVVRKSQQLTRAMIPKRYRTPTSKYVVVTAELMYEHWKKIWVVTLWLAVNVVLFMWKYEEFTTSPLYNITGRCLCAAKGTAEILKLNMALILVPVLRRTLTFLRSTFLNHLIPFDDNINFHKLIAVAIAVISLLHTALHMLCNYPRLSSCPYNFYSDYAGNLLGAKQPTYLGLMLTPVSVTGVLMIIFMGISFTLAMHYFRRNIVKLPIPFNRLAGFNSFWYAHHLLVIAYALLIIHGYILIIEKPWYQKTTWMYVAIPMVLYASERLFSRVQEHNHRVHIIKAIVYSGNVLALYMTKPQGFKYKSGMYMFVKCPDISKFEWHPFSITSAPGDEYLSVHIRALGDWTSELRNRFAETCEPHQKSKPSPNDLIRMETRARGANPHVEESQALFPRIFIKGPYGAPAQSYQKFDILLLIGLGIGATPFISILKDMLNNLKPGIPKTGQKYEGSVGGESLGGSSVYGGSSVNGGGSVNGGGSVSGGGRKFPQRAYFYWVTREQASFEWFKGVMDDIAVYDKTNVIEMHNYLTSMYEAGDARSALIAMVQKLQHAKNGVDIVSESRIRTHFARPNWRKVFSELSNKHETSRIGVFYCGSPTLVRPLKSLCQEFSLESSTRFTFHKENF", "text": "FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family."}
{"protein": "MMSEQDLADVVQIAVEDLSPDHPVVLENHVVTDDDEPALKRQRLEINCQDPSIKSFLYSINQTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNNDRQNAIVAKMEDPLSNRAPDSLENIISNAVPGRRQNTIVVKVPGQDDSHNEDGESGSEASDSVSNCGQPGSQNIGSNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPSSSSYSASETMMGTPPPTSELQQSQPQALHYALANAQQVQIHQIGEDGQVQVIPQGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQSWGLCQNPIPVSGDSVAQANPSQLWPLGGDTLDLPAGNEMIQVLQGAQLIAVASSDPAATGVDGSPLQGSDIQVQYVQLAPVSDHTAAAQTAEALQPTLQPDMQLEHGAIQIQ", "text": "FUNCTION: Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest and inhibits tumor growth (PubMed:12494467). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BANP/SMAR1 family."}
{"protein": "MVISRAEIYWADLGPPSGSQPAKRRPVLVIQSDPYNASRLATVIAAVITSNTALAAMPGNVFLPATTTRLPRDSVVNVTAIVTLNKTDLTDRVGEVPASLMHEVDRGLRRVLDL", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli and in M.smegmatis partially inhibits cell growth and colony formation; its toxic effect is neutralized by coexpression with cognate antitoxin MazE6. Acts as an mRNA interferase on ssRNA, cleaving between the second and third bases in the sequences CUCCU and UUCCU (PubMed:18485066). Further experiments demonstrate that it digests between the first and second bases of UCCUU, yielding a 5'- hydroxyl end; digests M.tuberculosis mRNA (in coding as well as the 5'- and 3'-UTR regions) and 23S rRNA, digests E.coli 16S rRNA both alone and in the 70S ribosome but no data for M.tuberculosis 16S rRNA cleavage was presented. 23S and 16S rRNA digestion occurs in predicted single-stranded regions, the 16S rRNA UCCUU site is in the anti-Shine- Dalgarno site and would cleave off the last 7 nucleotides (PubMed:24709835). Non-cognate antitoxins VapB27 and VapB40 partially neutralize toxicity in vivo (PubMed:20876537). FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease on single-strand RNA, cleaving between the second and third bases in the sequences CUCCU and UUCCU. Neutralized by coexpression with cognate antitoxin MazE2. FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease on single-strand RNA, cleaving between the second and third bases in the sequences CUCCU and UUCCU. Neutralized by coexpression with cognate antitoxin MazE6. SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient starvation. SIMILARITY: Belongs to the PemK/MazF family."}
{"protein": "MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL", "text": "FUNCTION: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:6765947, PubMed:15890657). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl- CoA/(S)-methylmalonyl-CoA (PubMed:6765947, PubMed:15890657). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate (PubMed:6765947). Other alternative minor substrates include (2E)- butenoyl-CoA/crotonoyl-CoA (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the AccD/PCCB family."}
{"protein": "MTMKLIWDKFYVSIIFVLTCIVLGIILMCTVVGGGNDYSEVNVSEGDSLWALADQYAGKSDMAKADFVSWVEKENNLADGHVEAGESVVIPVHKTKLIKSDSTIQLANQ", "text": "FUNCTION: Inhibits cell division during the SOS response. Affects a later stage of the cell division protein assembly, after the assembly of the Z ring, by probably suppressing recruitment of FtsL and/or DivIC to the division machinery. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YneA family."}
{"protein": "VVGGDECNINEHRFLVALYANSSLLCGGTLINQEWVLIAAHCDR", "text": "FUNCTION: Thrombin-like snake venom serine protease that coagulates fibrinogen by inducing a fast degradation of the alpha chain (FGA) from human citrated plasma, and a slow degradation of beta chain (FGB). Potently induces platelet aggregation in both platelet rich plasma and washed platelet preparations in a concentration-dependent fashion. Shows amidolytic activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MCGVRVAIVAESFLPQVNGVSNSVVKVLEHLRRTGHEALVIAPDTPPGEDRAERLHDGVRVHRVPSRMFPKVTTLPLGVPTFRMLRALRGFDPDVVHLASPALLGYGGLHAARRLGVPTVAVYQTDVPGFASSYGIPMTARAAWAWFRHLHRLADRTLAPSTATMESLIAQGIPRVHRWARGVDVQRFAPSARNEVLRRRWSPDGKPIVGFVGRLAPEKHVDRLTGLAASGAVRLVIVGDGIDRARLQSAMPTAVFTGARYGKELAEAYASMDVFVHSGEHETFCQVVQEALASGLPVIAPDAGGPRDLITPHRTGLLLPVGEFEHRLPDAVAHLVHERQRYALAARRSVLGRSWPVVCDELLGHYEAVRGRRTTQAA", "text": "FUNCTION: Catalyzes the addition of a mannose residue from GDP-D- mannose to GlcAGroAc2 to generate 1,2-di-O-C16/C18:1-(alpha-D- mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic acid)-(1-3)- glycerol(ManGlcAGroAc2). FUNCTION: Catalyzes the addition of a mannose residue from GDP-D- mannose to GlcAGroAc2 to generate 1,2-di-O-C16/C18:1-(alpha-D- mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic acid)-(1-3)- glycerol(ManGlcAGroAc2). SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MGWNGGLTSPSMEEHFYPFLIERRPSYMEEDEEEHEDEDLSLVLEKKDKDLLLAAELGKALLERNDQLMKAKDALEEELRETLETIEQEKHDMRLKMEVQESEWRAQVADLESDLAEARLQMQQLLSEQRECGRESASAAQELSEQNQRLVEQLAQASQVEQALNMELKSLREENRDLTISRGQFAPCLQSLRSENVLLLENKKEMESQTKQLQDENDNVQNQLISAKEGIFHLQRQKKDAELQVQQLQLEAQKLRDSQRTLQLQVKELQEELHMRDSQFSTHFSLHSEIQQSTAGQDHEMTTEAFPGLPCLPPSPYNLQKMGRNSVETQSITSDYMDTYLTEREGDLLRDSEEETIRLQDKVTMQHVELTTLQEEVQRLQDLLQQNNLDSIAKQAVLDRDEALMKKGELEQELARCQMEKESLNLQLLSTIQQKVMLSQELEAWQDDMQIVINQQLQSQKQQETQKVPETPQNSFMRRDSKQGRIFSFFKNI", "text": "SIMILARITY: Belongs to the BICDR family."}
{"protein": "MKNWGSSDSGGSEDPPQEDSCLDPLDGDPNSRPVPAKPHIFPTAKSRSRLFGKCDSEEASMDCSYEEGQLASCPAITVSPVVMIPKHEDGPTCARQPSQDSVTAGSEKSLKLYDRRKIFEAVAQNNCEELQSLLLFLQKSKKHLMDSEFKDPETGKTCLLKAMLNLHDGQNDTIPLLLEIARQTDSLKELVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLGIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILILGAKLHPTLKLEGLTNKKGLTPLALAARSGKIGVLAYILQREIQEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFIYCLYMIIFTTAAYYRPVDGLPPYKLKHTVGDYFRVTGEILSVLGGVYFFFRGIQYFLQRRPSLKTLFVDSYSEMLFFVQSLFMLGTVVLYFCHHKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSVPTESTLHRWRGPGCRPPDSSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGIKRTLSFSLRSGRVSGRNWKNFSLVPLLRDASTRERHPAQPEEVHLRHFAGSLKPEDAEIFKDPVGLGEK", "text": "FUNCTION: Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein Cell projection, dendritic spine membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV1 sub-subfamily."}
{"protein": "MRNFGIILAHTYKNRLMSKAFLISTVITLAFMLVLTNMDPYVNMLRGTSEAFSAAVAGADSIQVSPFDEPIQPSTSFSRRIARNTSLILMEESHLAATQDASGGAWYVEHLTDEIIVCKFKVILILNSVREYTDVIADSIFKLSRGH", "text": "SIMILARITY: To methylmalonyl-CoA mutase."}
{"protein": "MTFRKSFDCYDFYDRAKVGEKCTQDDWDLMKIPMKAMELKQKYGLDFKGEFIPTDKDMMEKLFKAGFEMLLECGIYCTDTHRIVKYTEDEIWDAINNVQKEFVLGTGRDAVNVKKRSVGDKAKPIVQGGPTGSPISEDVFMPVHMSYALEKEVDTIVNGVMTSVRGKAPVPKSPYEVLAAKTETRLIKNACAMAGRPGMGVOGPETSLSAQGNISADCAGGMTCTDSHEVSQLNELKIDLDAISVIAHYKGNSDIIMDEQMPIFGGYAGGIEETTIVDVATHINAVIMSSASWHLDGPVHIRWGSTNTRETLTIAGWACATISEFTDILSGNQYYPCAGPCTEMCLLEASAQSITDTASGREILSGVASAKGVVTDKTTGMEARMMGEVARATAGVEISEVNVILDKLVALYEKNYASAPAGKTFQECYDVKTVTPTEEYMQVYDGARKKLEDLGLVF", "text": "FUNCTION: Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC. SIMILARITY: Belongs to the monomethylamine methyltransferase family."}
{"protein": "MTERKREHKDRKQNKNSPKNQSKVTKFLKWFFIGILLLGITAVTVVGIYVLSIIRSSPELDVQAIQSLNQPSILYDDQGNFMDNVITREQRYVVKSEEIPDNLKKAFVAIEDERFYEHKGIDIKRIFGVIASNIKGKLSGSNTVQGASTITQQLIKNAVLTNEVSYERKIKEMYLALELEKHLSKDEILTTYLNTIPMGGYQYGVSAAAQRFFSKNVSDLNLVECAYLGGLTQAPTSYDGLSEANKENPSRYLNRTKSVLFKMHELGYISSEQYNDAINEIDTNGIKFTPNNKLSKTNFEWFTRPAITQVKQDLMDKYKYTQEEVDKLIANGGLKIYTSMDRNLQNNVQKVLDDPNNYKAITNNPNEKNEDGVYKLQASATIIDYKTGHVKALVGGRGEQPAMSHNRAYYDLKSIGSATKPLTVYGPAIDLGLGGAGSVVNDSPLSNKELSSTGYKDQPKNEYNSYRGPLTFREAIKISSNLAAIKVANEVGVSNSIAYGEKLGLVYGPHSRGISTTALGQFQNDPNNPDGGNTYTLASAFGVFGNNGVKTNAKLYTKVLDSHGNVILDTSTPEETKIFSPQASYIVYDMLKDQVESGSAKSAKFGNIPVAGKTGTTTGDKDYLFAGLTPYYSAAIWIGYDKPREMRTSSGTVTSPIFGKIMGLAHKDLQYKEVDNLVE", "text": "FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family."}
{"protein": "MGEALNVMESVRSIVFKESENLEGSATKIEGYDFNKGVNYAELFKSMASTGFQAANLGDAIQIVNQMLDWRLSHEQPMEDCSEEERDVAYRESVTCKIFLGFTSNLVSSGVRDTIRYLVQHRMVDVVVTTAGGIEEDLIKCLAPTYKGDFSLPGAVLRSKGLNRIGNLLVPNDNYCKFENWIIPIFDQMYEEQIKEKVLWTPSKVIARLAKEINDETSYLYWAYKNRIPVFCPGLTDGSLGDMLYFHSFKKGDPDNPDLNPGLIIDIVGDIRAMNSEAVHAGSRKTGMIILGGGLPKHHVCNANMMRNGADFAVYINTAQEFDGSDSGARPDEAVSWGKIRGGAKTVKVHCDATIAFPILVAETFAAKRKELSHIRCQV", "text": "FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. Also able to produce homospermidine from putrescine. SIMILARITY: Belongs to the deoxyhypusine synthase family."}
{"protein": "MISRLFASNQNVKLVRTFKSTSISMAAEKKKFERTKPHVNVGTIGHVDHGKTTLTAAITKTLSDRGLANFKSYAQIDKSPEEKARGITITASHIEYESATRHYAHIDCPGHQHYIKNMITGAAQMDGAILVVSAPDGPQEQTREHIILSREVGIPALVVFLNKMDNADPDLVEIVEMEVRELLSQYGFNGDETPFVKGAAAVALAETNETATQYGRKAIDELVEVLDTKIPLPHRAVDKPFLMPVEEVFSISGRGTVATGRIEQGTLKVGEEVAIVGIKPVPKVAVTGIEMFGKLLDFAQAGENVGCLLRGLKREEVLRGEVISKPGTIKASTKFKAKTYVLTEAEGGRKKGFATGYRPQFFIRTANVTGMIELPPTHAVILPGDSLEFTVELISPTPLSINGRFAIREGQLTVGAGVISEILN", "text": "FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily."}
{"protein": "MFSRTASKFRNTRRLLSTISSQIPGTRTSKLPNGLTIATEYIPNTSSATVGIFVDAGSRAENVKNNGTAHFLEHLAFKGTQNRSQQGIELEIENIGSHLNAYTSRENTVYYAKSLQEDIPKAVDILSDILTKSVLDNSAIERERDVIIRESEEVDKMYDEVVFDHLHEITYKDQPLGRTILGPIKNIKSITRTDLKDYITKNYKGDRMVLAGAGAVDHEKLVQYAQKYFGHVPKSESPVPLGSPRGPLPVFCRGERFIKENTLPTTHIAIALEGVSWSAPDYFVALATQAIVGNWDRAIGTGTNSPSPLAVAASQNGSLANSYMSFSTSYADSGLWGMYIVTDSNEHNVQLIVNEILKEWKRIKSGKISDAEVNRAKAQLKAALLLSLDGSTAIVEDIGRQVVTTGKRLSPEEVFEQVDKITKDDIIMWANYRLQNKPVSMVALGNTSTVPNVSYIEEKLNQ", "text": "FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2007593, PubMed:9299349, PubMed:9654444). Preferentially, cleaves after an arginine at position P2 (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase M16 family."}
{"protein": "MGELGEHRASLLSNPIPEVKTLGELKQGQNNGNLDLESEPFGSHWLQGSKATTGRTSEEPEEEIPPEEMAGEELPETSNLDGPLQQDLEVEVVEMSHLSITERTPSVSTAKGRKKRSRRLLELAKPKTNWQCLRDRTGRCCKGYAWISPRKTNLQFCLYWPSVYWTERFIEDTTLTITVPVVSQRMEELSRPKRFYQEYYNNNRTTPIWSIPRSTLEYQASNRLKQLATPKVRNNIWSINMSEVSQVSRAAQMAVPTPRTLRLAKPRPPATLLEEWDPMPKPKPYVSDYNRLLQLATPKALSEKCVPDRSPQWEVLDVTKNAVASSRIISLAQPKIRKDLNEGYNPYYISPASLVAQASPRIYELATPKYITKKV", "text": "FUNCTION: May be involved (but not essential) in spermatogenesis. SUBCELLULAR LOCATION: Nucleus Note=Localized predominantly in the nucleus of haploid round spermatid."}
{"protein": "MPTMGAEMNTRNMRYILLTGLLPMASAFGETALQCAALTDNVTRLACYDRIFAAQLPSSAGQEGQESKAVLNLTETVRSSLDKGEAVIVVEKGGDALPADSAGETADIYTPLSLMYDLDKNDLRGLLGVREHNPMYLMPLWYNNSPNYAPGSPTRGTTVQEKFGQQKRAETKLQVSFKSKIAEDLFKTRADLWFGYTQRSDWQIYNQGRKSAPFRNTDYKPEIFLTQPVKADLPFGGRLRMLGAGFVHQSNGQSRPESRSWNRIYAMAGMEWGKLTVIPRVWVRAFDQSGDKNDNPDIADYMGYGDVKLQYRLNDRQNVYSVLRYNPKTGYGAIEAAYTFPIKGKLKGVVRGFHGYGESLIDYNHKQNGIGIGLMFNDLDGI", "text": "FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein Note=One of the very few enzymes located there. SIMILARITY: Belongs to the phospholipase A1 family."}
{"protein": "MTAPSCAFPVQFRQPSVSGLSQITKSLYISNGVAANNKLMLSSNQITMVINVSVEVVNTLYEDIQYMQVPVADSPNSRLCDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHAMSLLDAHTWTKSCRPIIRPNSGFWEQLIHYEFQLFGKNTVHMVSSPVGMIPDIYEKEVRLMIPL", "text": "FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Note=Translocates to cytoplasm in response to apoptotic stimuli such as staurosporine treatment. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "MKLLEDRILNDGDVLGENILKLTFLTHQVDFELMREIGKVFAEKFKDTGITKVVAIEASGIAPALYATEALDVPMIFAKKAKNITMNEGILTAEVYSFTKQVTSTVSIASKFLTPEDKVLIVDDFLANGQAAKGLIQIIEEAGAHVEAVGIVIEKSFQDGRALLEEASYPVVSLARLERFENGQVVFKEADI", "text": "FUNCTION: Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. Xpt subfamily."}
{"protein": "MKRCCEGVGLPCLFKGVGMASSRPPKYLLVFDFDGTIINESSDDSIVRAAPGQALPEHIRQSFREGFYNEYMQRVLAYMGDQGVKMGDFKAVYENIPLSPGMPDLFQFLSKNHELFEIILISDANMFGIECKLRAAGFYSLFRKIFSNPSSFDKRGYFTLGPYHSHKCLDCPANTCKRKILTEYLAERAQEEVEFERVFYVGDGANDFCPSVTLTSADVAFPRKGYPMHQMTQEMEKKQPGTFQATVVPWESATEVARYLQELLKKKC", "text": "FUNCTION: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho) (By similarity). Involved in the generation of inorganic phosphate for bone mineralization (PubMed:15050893). SUBCELLULAR LOCATION: Extracellular vesicle Note=Localizes to special class of extracellular vesicles, named matrix vesicles (MVs), which are released by osteogenic cells. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO family."}
{"protein": "MSDSRTTTTKNNTTNHKTSRQGPGSACEECRRRKLRCDRQPQCQNCVDAGVYCVTNLARPARGPKKGHLKALKGRIATLERCLLEQRDGMLVDPISDDELLDKALSASSPASQSPDPSEEVSENILEDLDQVFFERVQPMVPILQRHRYFSWAREPQQSANRRGLQQAIRTLAAGVSSQLPEVRVALYRTTRHTLESLESDDTLLTAPDFEQVQAWILIAIYEFMQVSYSRGWMSAGRVFRLVQLLRLPEIDASPLSLLDLDLDPDSKWVVAEEKRRTVWMAYIMDCSLNLRHKGSLTLTEQALTRLPMPESEFQCGHPISMGFLAEALAGTDITSPLSSFAKCILLATISGRTLSHRHLSMAELLRGNPLQDVWTRHQWIDTTLTAHLQLSFSLPTAAESSDPMLLFAKMIGQAGVLSLYDILQSTPWEPETVSLLPDYEACALQAARETVVLARNLRHFSCFK", "text": "FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities (PubMed:22921072). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MMNMKPTESYEQLDNSALEQVVGGKYYGNGVHCTKSGCSVNWGEAFSAGVHRLANGGNGFW", "text": "FUNCTION: Inhibits a wide spectrum of lactic acid bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family."}
{"protein": "MDSYEKEESVASTSGIQDLQTLSELVGPENAGEGELTIAEEPEENPRRPRRYTKREVKCVSYHAYKEIEDKHPQHIKLQDWIPTPEEMIAQKVQNQDLGTILSFDVTCLKSITSLGRNDPGDDPSIMSHVLPVVTPWPMSQDHYAPTLFGILDRYYQGYLKSPATYQTWKFTCQVDPSGKRFMETQFWVPPLGQVNIQFYKNYQILTCCQAVDPFANIFHGTDEEMFDIDSGPDVWCSPSLCFKVIYEGAMGQKQEQKTWLCRLGHGHRMGACDYRKVDLYAMRQGKENPYGDRGDAALQYAYQVKRGCKAGCLASPVLNYKALQFHRTIMADFTNPRIGEGHLAHGYQAAMEAYGPQRGSNEERVWWNVTRNQGKQGGEYYREGGEEPHYPNTPAPHRRTWDERHKVLKLSSFATPSDIQRWTTKALPYGWKVVTESGNDYTSRRKIRTLTEMTQDEIRKRWESGYCDPFIDSGSDSDGPF", "text": "FUNCTION: Bet counteracts the innate antiretroviral activity of APOBEC3 family defense factors by inhibiting their incorporation into virions. May be implicated in the establishment and/or maintenance of viral persistance. Bet is required for viral replication (By similarity). SUBCELLULAR LOCATION: [Isoform Bel-2]: Host nucleus. SUBCELLULAR LOCATION: [Isoform Bet]: Host cytoplasm Host nucleus Secreted Note=Bet is highly expressed in infected cells, where it localizes to both cytoplasm and nucleus (PubMed:11884565). Also secreted and internalized by non-infected surrounding cells (PubMed:11884565)."}
{"protein": "MDKEECSSSESGWTTYLSSPIKVDEDEVVDEDYYYEGYNIYNYSSKVEHEEERNKDSDDSMASDASSGPNYQRFHQKNKALDLKNGKNEGNSKSKNDDDHHNHYHDGKKTSNSYRKKDKKKRENKSTYRMK", "text": "FUNCTION: Involved in cytokinin-mediated development. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SOFL plant protein family."}
{"protein": "MPGPPATAPPPEPIERPPTPPPPPPEDSAAPPPPPDMSAPPPPPQDELPPAPEPKKKKLGWGSKRPAAAPLSVEELVRKKREADAAAAKPKFLSKKEREKIALEKRAKEVEQSRRKTSTNGASDTASVRSESATPNGVDRTASIPTGPRAMRTSEAPPPPRPRHDSSSNGNGNSNSNSNSNGTVDEDEAAAQAALVKQRYMGAEMTSSFSAKKKRKRTTDRKFNFEWNAEEDTSRDYNPLYAQRHEANFFGRGRLAGFGDDVADGVARKYAAALEDRDREAGSVRAREILEMERRRREESTRNQLDKHWSEKKLEHMRERDWRIFKEDFNIATKGGSVPNPMRSWAESGLPSRLLDLVHRVGYKDPTPIQRAAIPIAMQSRDLIGVAVTGSGKTAAFLLPLLVYIAELPRIDEFEWRKNDGPYAIVLAPTRELAQQIEIEAKKFTIPLGFTVVSIVGGHSLEEQAYSLRNGAEIIIATPGRLVDCIERRLLVLSQCCYVIMDEADRMIDLGFEEPVNKILDALPVSNEKPDSDAAENAAAMSQLHHAGGGRDTRYRQTMMYTATMPTAVERIARKYLRRPAIVTIGSAGEAVDTVEQRVELIAGEDKRKKRLGDILSSGEFRPPIIVFVNIKRNCDAIAREIKQWGFSSVTLHGSKTQEQREAALASVRNGSTDVLVATDLAGRGIDVPDVSLVVNFNMATSIESYTHRIGRTGRAGKSGVAITFLGNEDADVMYDLKQMLIKSPISRVPDELRKHEAAQQKPTRGFSKKNDESSAFGGKGGW", "text": "FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28 subfamily."}
{"protein": "MDIISLGWVFLMVFFSFSLSLVVWARNGL", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetN family."}
{"protein": "ATTRCDPTLIPIAGGWFELLEGGEALRYRCPPGHIPTPLARRSCGPDGQXEPLXXXXXXXXXXXXXXXXKCRAVWCPPPQDMEHGSFWPRLPRYPPGSRLHFQCFQGFNLRGAPNRTCGEGGRWSGVTPVCDDGSGDCPAPPVXXXXXKEGSRYLLEDTVRFRCGPGLVLLGSAVRQCLEGGVWSGTEPQCRAPLSFDTPSDVAASFMASLSQSVERADSNSSHGPTEKLPRXIRVDGSAXLNVFLLXDA", "text": "FUNCTION: Required in both the classical and alternate pathways of the complement system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MTTQATPLTPVISRHWDDPESWTLATYQRHDRYRGYQALQKALTMPPDDVISIVKDSGLRGRGGAGFATGTKWSFIPQGDTGAAAKPHYLVVNADESEPGTCKDIPLMLATPHVLIEGVIIAAYAIRAHHAFVYVRGEVVPVLRRLHNAVAEAYAAGFLGRNIGGSGFDLELVVHAGAGAYICGEETALLDSLEGRRGQPRLRPPFPAVAGLYGCPTVINNVETIASVPSIILGGIDWFRSMGSEKSPGFTLYSLSGHVTRPGQYEAPLGITLRELLDYAGGVRAGHRLKFWTPGGSSTPLLTDEHLDVPLDYEGVGAAGSMLGTKALEIFDETTCVVRAVRRWTEFYKHESCGKCTPCREGTFWLDKIYERLETGRGSHEDIDKLLDISDSILGKSFCALGDGAASPVMSSIKHFRDEYLAHVEGGGCPFDPRDSMLVANGVDA", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 51 kDa subunit family."}
{"protein": "MKLLLLLTISASMLIEGLVNADGYIRGGDGCKVSCVINHVFCDNECKAAGGSYGYCWGWGLACWCEGLPADREWDYETNTCGGKK", "text": "FUNCTION: Depressant insect beta-toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage- independently at site-4 of sodium channels (Nav) and block action potentials, primarily by depolarizing the axonal membrane and suppressing the sodium current. This depressant toxin is active only on insects. It is found in a relatively small amount in the venom, and its activity on insects is 10-fold higher compared to other known depressant toxins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MPLWVFFVLLTLTSGSHCSLPPSPPFRVRRHADAIFTSSYRRILGQLYARKLLHEIMNRQQGERNQEQRSRFNRHLDRVWAEDKQMALESILQGFPRMKLSAEA", "text": "FUNCTION: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family."}
{"protein": "MLLLLLSIIVLHVAVLVLLFVSTIVSQWIVGNGHATDLWQNCSTSSSGNVHHCFSSSPNEWLQSVQATMILSIIFSILSLFLFFCQLFTLTKGGRFYITGIFQILAGLCVMSAAAIYTVRHPEWHLNSDYSYGFAYILAWVAFPLALLSGVIYVILRKRE", "text": "FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system. FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family."}
{"protein": "MQTYSTPLTLIIVTSLFLFTTQGSSSNAVEPTKKPLKLANYRATCEDRTRTLVTRLNTSHHSVVWQRYDIYSRYMRRMPPLCIITDAYKETTHQGGATFTCTRQNLTLYNLTVKDTGVYLLQDQYTGDVEAFYLIIHPRSFCRALETRRCFYPGPGRVVVTDSQEADRAIISDLKRQWSGLSLHCAWVSGLMIFVGALVICFLRSQRIGEQDAEQLRTDLDTEPLLLTVDGDLE", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein."}
{"protein": "MASRNSVAVIALFAFVFAVISPFAGAQSLAPAPSPTSDGTSIDQGIAYLLMVVALVLTYLIHPLDASSSSYTFF", "text": "FUNCTION: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the AG-peptide AGP family."}
{"protein": "MAPQHLPSTRMAPQGMLLGLLLASCLTFCLSCQNSNNFALTNPEKSTHEDSDTKETRREEELDAEVLEVLNPTQEWQALQPGQAVPAGSHVRMNLQTGVNEVKLQQEDKFQSNWKGFKRGRRLDINTNTYTSQDLKSALAKFKEGTEMENSKDELARQATVKQLFRPIEELKKEFDELNVVLETDMQIMVRLINKFNSSSSSLEEKVAALFDLEYYVHQMDNAQDLLSFGGLQVVINGLNSTEPLVKEYAAFVLGAAFSSNPKVQVEAIEGGALQKLLVILATEQPLPAKKKVLFALCSLLRHFPYAQQQFLKLGGLQVLRSLVQEKSAKVLAVRVVTLLYDLVTEKMFAEEEAELTQESSPEKLQQYRQVQLLPGLREQGWCEITAQLLALPEHDAREKVLQTLGALLATCRDRYRQDLELSRTLGSLQAEYQALASLELQEGEDDGYFRELLASIDSLVKELR", "text": "FUNCTION: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the SIL1 family."}
{"protein": "MMASQAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKQELAKLEALDCGKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLITPWNYPLLMATWKVAPALAAGCAAVLKPSELASVTCLELADICKEVGLPPGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMAAAAPMVKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLVHTKIAKEFNEKMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKKFILNAKSEGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIWREEVFGPVLCVKEFSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGIIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYRSPSKL", "text": "FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4- aminobutanoate and beta-alanine, respectively (PubMed:23408433). Catalyzes the oxidation of 4-(trimethylamino)butanal and 4- guanidinobutanal to 4-trimethylammoniobutanoate and 4- guanidinobutanoate, respectively (PubMed:23408433). Catalyzes the oxidation of betaine aldehyde to glycine betaine (PubMed:23408433). SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MDPPARKEKTKVKESVSRVEKAKQKSAQQELKQRQRAEIYALNRVMTELEQQQFDEFCKQMQPPGE", "text": "FUNCTION: Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin (PubMed:29146869, PubMed:31270470, PubMed:31235911, PubMed:31324789, PubMed:31171830, PubMed:31235910). This activity is critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning (PubMed:31171830). Also required to enhance the solubility and secretion of VASH1 and VASH2 (PubMed:20736312, PubMed:27879017, PubMed:30607023). Plays a role in axon and excitatory synapse formation (PubMed:31235911). SUBCELLULAR LOCATION: Cytoplasm Secreted Cytoplasm, cytoskeleton Note=Detected both intracellularly and extracellularly (By similarity). Within cells, localizes mainly to the apical part of the cell (By similarity). SIMILARITY: Belongs to the SVBP family."}
{"protein": "MTLNAESEALVGVSHPLDPLSRVEIARAVAILKEGPAAAESFRFISVELREPSKDDLRAGVAVAREADAVLVDRAQARSFEAVVDLEAGTVDSWKLLAENIQPPFMLDEFAECEDACRKDPEVIAALAKRGLTNLDLVCFEPWSVGYFGEDNEGRRLMRALVFVRDEADDSPYAHPIENFIVFYDLNAGKVVRLEDDQAIPVPSARGNYLPKYVGEARTDLKPLNITQPEGASFTVTGNHVTWADWSFRVGFTPREGLVLHQLKFKDQGVDRPVINRASLSEMVVPYGDTAPVQAKKNAFDSGEYNIGNMANSLTLGCDCLGEIKYFDGHSVDSHGNPWTIENAICMHEEDDSILWKHFDFREGTAETRRSRKLVISFIATVANYEYAFYWHLFLDGSIEFLVKATGILSTAGQLPGEKNPYGQSLNNDGLYAPIHQHMFNVRMDFELDGVKNAVYEVDMEYPEHNPTGTAFMAVDRLLETEQKAIRKTNEAKHRFWKIANHESKNLVNEPVAYRLIPTNGIQLAARDDAYVSKRAQFARNNLWVTAYDRTERFAAGEYPNQATGADDGLHIWTQKDRNIVDTDLVVWYTFGMHHVVRLEDWPVMPRQNIGFMLEPHGFFNQNPTLNLPTSTSTTQTGEADTCCHNGK", "text": "FUNCTION: The exact function of MaoXI is not known. SIMILARITY: Belongs to the copper/topaquinone oxidase family."}
{"protein": "MDAIKKKMQMLKLDKENALDRAEQAESDKKASEDRSKQLEDDLVALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALTKLEEAEKAADESERGMKVIENRAMKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELSESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI", "text": "FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Associates with F-actin stress fibers. SIMILARITY: Belongs to the tropomyosin family."}
{"protein": "MFVDKTLMITGGTGSFGNAVLSRFLKSDIINDIKEIRIFSRDEKKQEDMRIALSNPKLKFYIGDVRNYKSIDEAMRGVDYVFHAAALKQVPTCEFYPMEAINTNVLGAENVLSAAINNKVAKVIVLSTDKAVYPINAMGLSKALMEKLSIAKARMCSQGETVLCVTRYGNVMASRGSVIPLFINQIKQGKELTITEPSMTRFLMSLVDSVDLVLYAFEHGRQGDIFVQKSPASTIEILAKALQEIFGSKNKIRFIGTRHGEKHYESLVSSEDMAKADDLGGYYRIPMDGRDLNYAKYFVEGEKKVALLEDYTSHNTKRLNLEEVKKLLLTLDYIQEELKNA", "text": "FUNCTION: Epimerizes UDP-galactose to UDP-glucose. SIMILARITY: Belongs to the polysaccharide synthase family."}
{"protein": "MRTLALSLGLALLCLLHAKAAATVPDRSEIAGKWYVVALASNTEFFLREKDKMKMAMARISFLGEDELKVSYAVPKPNGCRKWETTFKKTSDDGEVYYSEEAKKKVEVLDTDYKSYAVIYATRVKDGRTLHMMRLYSRSPEVSPAATAIFRKLAGERNYTDEMVAMLPRQEECTVDEV", "text": "FUNCTION: Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "SSLLSIPSLSLQYNDKLKVGGNSLRFSKEQSNTFSNAKSSCRISMVAAVNVSRFEGIPMAPPDPILGVSEAFRADTSDAKLNLGVGAYRTEELQPYVLKVVNKAENLMLERGQNKEYLAIEGLAAFNKATAELLLGADNPAIKQQRVATVQGLSGTGSLRLGAALIERYFPGAKVLISAPTWGNHKNIFNDARVPWSEYRYYDPKTVGLDFEGMIEDIKAAPEGTFVLLHGCAHNPTGIDPTPEQWEKIADVIQEKNHIPFFDVAYQGFASGSLDEDAASVRLFVARGLEVLVAQSYSKNLGLYAERIGAINVISSSPESAARVKSQLKRIARPMYSNPPVHGARIVADIVGNPALFDEWKVEMEMMAGRIKNVRQQLYDSISSKDKSGKDWSFILKQIGMFSYTGLNKNQSDNMTNKWHVYMTKDGRISLAGLSLAKCEYLADAIIDSFHYVS", "text": "FUNCTION: Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MSFVTTRPDSIGETAANLHEIGVTMSAHDDGVTPLITNVESPAHDLVSIVTSMLFSMHGELYKAIARQAHVIHESFVQTLQTSKTSYWLTELANRAGTST", "text": "FUNCTION: Involved in cell wall lipids remodeling and in virulence (PubMed:26157429, PubMed:26902658, PubMed:28198348). Restricts the biofilm growth and is essential for the optimal intracellular survival of M.tuberculosis (PubMed:28198348). Shows esterase activity with a preference for short-chain esters, particularly pNP-acetate (C2) and pNP-butyrate (C4) (PubMed:26902658). Has weaker activity with pNP- octanoate (C8), pNP-laurate (C12) and pNP-myristate (C14) (PubMed:26902658). Shows weak long-chain triacylglycerol (TAG) hydrolase activity in vitro (PubMed:16354661). Not necessary for PPE17 stability or for its localization on the mycobacterial surface (PubMed:23469198). SUBCELLULAR LOCATION: Secreted, cell wall Note=Cell wall associated protein. SIMILARITY: Belongs to the mycobacterial PE family."}
{"protein": "MDVNASRALANVYDLPDDFFPQIDDLVRDAKDALEPYWKAETIKKHVLIATHFVDLIEDFWQTTQGMSQIADALRAVIPPTTVPVPEGFLITHSEAEEIPLNDLFSNQEERIVNFQPDYPITARIHTHLRVYTKLNEQALDKARRLLWWHYNCLLWGEATVTNYISRLRTWLSTPEKYRGKDAPTIEAITRPIQVAQGGRNQTKGTRKPRGLEPRRRKVKTTVVYGRRRSKSRGRRSSPSQRAGSPLPRNRGNQTRSPSPRE", "text": "FUNCTION: Self assembles to form an icosahedral capsid. Most capsid appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsid are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stucked in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genome for transcription, or bud through the endoplasmic reticulum to provide new virions (By similarity). SUBCELLULAR LOCATION: [Capsid protein]: Virion Host cytoplasm. SIMILARITY: Belongs to the avihepadnavirus core antigen family."}
{"protein": "MAPKKAKRRAAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASGPINFTVFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTQCDRFTPEEIKNMWAAFPPDVAGNVDYKNICYVITHGEDKEGE", "text": "FUNCTION: Myosin regulatory subunit that plays an essential to maintain muscle integrity during early development (By similarity). Plays a role in muscle contraction (PubMed:15256600)."}
{"protein": "MEKINSLSTQLVKCCFCDFLKVKMHTVSYIHFFYLGLCLLTLTSSAAAGPETLCGAELVDALQFVCGDRGFYFSKPTGYGSSSRRLHHKGIVDECCFQSCDLRRLEMYCAPIKPPKSARSVRAQRHTDMPKAQKEVHLKNTSRGNTGNRNYRM", "text": "FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
{"protein": "MLLRMALCLTVSTILCAGFASNLMDILRRPVNQVWDMFEESHLPAGIGLDAWSKAKEMATAMTSLGASQRALFLRQVSPSQADLTEAALVLRGAQPLPEDRKQVFIREGSPSTAVRDLAEALYSKGAVLADGTGRGALKMMSAFQPGEAFMLTIKLSLYAGVVISFPLLLYFLLQFIIPGLLEHERKLLYKCMAVGFGLFLAGTLFCYFIVLPRVLTFFYTYSLEFGISNEWRIGYYLSFATQMILMFGLAFELPVVVMPFVKLGVLTYDMMKSTRRYAIVAIAVLAAVITPTPDVATMMLMAVPMYALYEICIILAWMHERKEAARTREEIARFEEDFNNNNSPYNQ", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family."}
{"protein": "MAEKPLWYRWARVYFAGGCLVGLGVVLYKTIRPTDEELISRFSPEIRAEYERNKELRQKEQQRLMEIVKKTSASTDPIWKTGPIGSPLEKDQRNLSMQLVDQELFHKTKEEEKQKAEINKSVEEGKEVERLLRENKNQKSWWKFW", "text": "FUNCTION: Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CBP4 family."}
{"protein": "MTQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPSTVIATGGGIILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQVISEIRSALAQTINC", "text": "FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily. SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily."}
{"protein": "MAELRALVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTEDLVAKLKEIGRI", "text": "FUNCTION: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF- ubiquinone oxidoreductase. Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. ETFB binds an AMP molecule that probably has a purely structural role. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the ETF beta-subunit/FixA family."}
{"protein": "MQTVRMTTAQALVKFLNQQYIEFDGEQQKFIKGIFTIFGHGNVVGLGQALEEDAGELEVYQGRNEQGMANAAMAFAKQKHRKQIMACTSSVGPGSANMITSAATASANNIPVLLLPGDVFATRQPDPVLQQIEQTHDLSISTNDAFRAVSKYWDRINRPEQLMTAMIQAMRVLTNPADTGAVTICLPQDVQGEAWDFPSYFFQKCVHRIERRLPTRASLADAVEMIKRKKKPVMICGGGVRYAEAAEELKQFAEAFRIPFGETQAGKSAIESSHPYNLGGIGVTGNLAANTIAKEADLVIGIGTRFTDFTTASKQLFQNEEVEFVNINISEFHANKLDALKVIADAKEALLALINELQAIEYRSSYTVEIAAAKEFWETELARLHNIRFTGQDFKPEVEGHFDDNLNEYVDALGTQLTQTAVIGEMNTLLDEDAIIVGAAGSLPGDLQRMWTSRKPNTYHMEYGYSCMGYEVAGALGAKLAEPSKEVYAMVGDGSYQMLHSELVTSLQENKKINVLLFDNSGFGCINNLQMGNGMGSFGTEFRYRNEETRKLNGAIMKIDFAASAAGYGVKTYRVTSVEQLQEALKDAKKQTVSTLIDIKVLPKTMTNGYESWWHVGVAEVSNSQSVQAAYESKVSNLQKARSY", "text": "FUNCTION: Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG). SIMILARITY: Belongs to the TPP enzyme family."}
{"protein": "MILVLAESALELVPKEIWNHPAVLADARRRGKRPGEILLDRARHHPAMRLLADAKRRGRPDIVHQVLLAFQYSLLAKRGLGKAYIHTRDDYVIAVSPEARVPKNYNNFVALIEQLFALGKVPPKGEPLMELYRKDLATLLQELGGVWAVFHESGARKPLSQMGSELLKSVVVVGGFPHGDFQNKWVVEKAAVVYSLGEESLDAAQVICKAVTAAEVAAGLL", "text": "FUNCTION: Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family."}
{"protein": "MVSTRGVLYYLLRPKELRPILQWKALHGLGHQRDEKNESPDVKACYQYLALTSRSFAAVCQQLDRELLMPICIFYLILRGLDTIEDDMTLSKEVKEPLLRNFYTTIYDQTWTFNDSGTDEKDRELLVHFDCVAREFHKIKDEYKIIITDITKQMGNGMADFVVSGDLTGIQKIKDYELYCHYVAGVVGDGLTRLFVEANVADPSLLKNPRLIESMGQFLQQTNIIRDVREDHDEVRHFWPKEVWSKYAQDFDHLVSPKPQDRKKALQCSSEMVLMALNRADDCLNYMAGVREQTVFNFVAIPQSMAIATLELCFQNPAIFDKNIKITKGATCQLMIDSTQDLQHVCQAFRRYARRIKKKNHPEDPHFHDINAACNKIDRFIDDRYPNLQDEQAKADTMYLAVLVLGVFGVVAAIL", "text": "FUNCTION: Squalene synthase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) (PubMed:28605916). Catalyzes the condensation of 2 two farnesyl pyrophosphate moieties to form squalene (By similarity). The presence of a gene encoding a squalene synthase supports the identification of the cluster as being responsible for SQS1 production and suggests a likely mechanism for self-resistance (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the phytoene/squalene synthase family."}
{"protein": "MILQEQRRLRLWLYKSSLFISVLFLIGFSIVLPVDSIVQAIQSENNGFNTIIVIGSLAVFFVAAVTILIGRMLLHKSCLKDIPRRYIPVTNADLPHKSSRKMVIHNMERSKKLSGLFKTPKDPVIHPGLEPPARCDDPNTPKILPEYLNYKICIKSATDRLKYYGLFLNSASDDVKSSQTFTDLVKSQFIKGNHNKRQVQRAKDFIELYERIRFSGDEVSRSEFIQFAENCIYFSDLMITMDITKVGLGNISTRSQLSFNIAGSSVDRKLRKLNTARSNQISRLSSGQYPDITAFRYDTSNSDYHRQETDEDDFALDDMDYFPSVPPYMIRRNSTNTVSMRIPTSNSDDQYNLGFNEIGDEDIQNNDQIRRYMSNTSKTDSFKTVIHNG", "text": "FUNCTION: Required for growth under high-pressure and low-temperature conditions. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DLT1 family."}
{"protein": "MLRLLFGFLVTCFLLLPARAAEPQYAIFAGGCFWCVESDFDAVPGVLETISGYAGGKSANPTYEDYAKGGHREVVRVKFDPDRVSYAELVGVLFRTTDPTDGDGQFCDRGFAYTTAIHALNERQAMDAKAEKIKAEAELGRPIVTPVEGAAKFWPAEDYHQDFGKRNPIRYWYYRNGCGRNRTVEKLWGDRAYAGVSH", "text": "FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family."}
{"protein": "MPSMAEIYVKELRERDPATVDTLFLDNAEDGQIGGLTDQLINLEMLSMVKCGLTTLAGFPTLPALTYLDISDNQLGDNASFDVLVKNAPDLKKITLASNKLSLDNLRCLKVLPNLFELDLSNNPSLGLLEDYREKMFEMIPSLKILDGCDVDGEEVEEEFAGEGGEDSEEGSGDEDGPGLSYLEKSQFSDDETDDYAPEGGDAEPRGTKRGASDNGEEPDNKKAAGDDE", "text": "SIMILARITY: Belongs to the ANP32 family."}
{"protein": "MSNMPVLIITLLLFSMYISTAAQKPTEIKCRYPADCHIMCRKVTGRAEGKCMNGKCTCYY", "text": "FUNCTION: Inhibits voltage-gated potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 12 subfamily."}
{"protein": "MKNTEKLEQFKEVTEAELQEIRGGDKRLPYFFKHLFSNRTK", "text": "FUNCTION: Acts as a pheromone, induces cells to develop competence for genetic transformation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ComC family."}
{"protein": "HSEGTFTSDYSKYMDNRRAKDFVQWLMSTKRNGHAEGTYTSDVDSLSDYFKAKRFVDSLKSY", "text": "FUNCTION: Promotes hydrolysis of glycogen and lipids, and raises the blood sugar level. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family."}
{"protein": "MNTKITNFSFDKKNLSLAEDIIKKYPPEGKRSAILPLLDLAQRQNGGWLPVPAIEYVANMLEMPYMRAYEVATFYTMFNLKPVGKNHIQVCTTTPCWLRGSDDIMKTCKEKLGIKDEEVTKDQKFSLIEIECLGACVNAPVVQINDDYYEDLTPEKMEAIIDKLRND", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 24 kDa subunit family."}
{"protein": "MTEKSNIIKDYTYFLSKRGKLKEASPIRSLFQYSSLPGMISLGGGLPNASTFPFKSINIELKDGSKLEIEGSDLEEAFQYSPTPGLPRLQKALKDLQIRQHNLCPPDEAGKEWNLIISNGSQESLANAFEVLIDDNDSIITENPTYSGTLSILKPLSLNICGIETDRYGMIPEKLQRLLSEWDHSKFKFPRVIYLIPCGQNPSGTTMNHQRKLDIYSICSKYNLLIIEDDPYYYLQFESSENADDDDGASCSSLNLGKSLLSMDVDGRVLRFDSLSKILSSGLRIGFVTGNKQLLEKINFHQQSTTLHSSGLSQAVVLSLLNKWGVEKWNQHISFIQRFYLEKRNQMIDSIDKHLKGLVEFNIPSAGMFIWFKLPVEDSKTLIFKNAVEKKILLVPGISFSTDSTKPSQFVRASYSTASKEQIDEAIKRFADLLNEELKK", "text": "FUNCTION: Has aromatic amino acid transaminase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHSSSHSKKDKVVTCQRVSQEEVKKWAESLENLIHHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLQPTITCFDEAQKKIFNLMERDSYRRFLKSRFYLDLTNPSSCGAEKQKGAKSSADCTSLVSQCA", "text": "FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)- alpha-1 is inhibited by palmitoylation of the G-protein (By similarity)."}
{"protein": "MKLTCVMTVAVLFLTAWTFVTADDSRNGLKNLFPKARHEMKNPEASKLNKRDGCSNAGAFCGIHPGLCCSEICIVWCT", "text": "FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily."}
{"protein": "MLRRMNTFSGQKLAAVVKELENFAPTSWAEKWDNVGLLIEPHREKQIKKILLTNDLTEPVVKEALEKEAELIISYHPPIFKPLTRITQSHWKERVVAACLANDIALYSPHTAWDKKSGGVNDWLSKAVNIISIRPLEPELGAPPGTGSGRYIETKMELSQVVESLQKRIRNSVHVALAVGHTPKTLIQSVGICAGSGASLLKGIQADLIITGEMSHHEVLEFTHNNTTVLLCNHSNSERGFLHEFCPILAKSLNEECLVFVSEVDKDPLVTVASDINKELSAFVDVYKSTSK", "text": "SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family."}
{"protein": "SGKPVLHYFNVQGRMESIRWLLAAAGVEFEEKLIMCQEDLDKLKNDGLLMFQQVPMVEMDGMKMVQSRAILNYIATKYNLYGKDTKERLLIDMYTEGMTDLYELFFKVILAPPEEKDAAKSLIKDRAKNRFLPAFEKVLKSHGQGYLVGNKLSKADILLTELLYMVEEFDASLLANFTLLQALKTRVSNLPNVKKFLQPGSQRKPFPTQEMFEEMRKF", "text": "FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5- androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Alpha family."}
{"protein": "MADAMNELCNLTQHLQVDDDQLSNLKLKNGYSLFPHQEKVMLWMKYRENLTKKECRKEGEKTWGVRGGIISLCMGLGKTLTALAYSFQNKASFPTLVITSKTVMHEWKTEGVEKFFDSDNIRVLYLHRDYIKNIDKISRDDIMTYDIVITTYDVCLFACKKGNYFLQCFEMGEEQSLMKNKIVAIHTRKRKDANLPNLKGTAVIYGTPWERVICDESQKFANPKTMTYKCIMAVYGKYKWCLTGTPIRNYETDIWAQLRFCGYKGVERSHDWNRNGQGLIAFKDHNLISAIFTMSYDDAQMSLPEKTENNLTVKLEGQHKEIYEGILTETREMYKKMMNDLCSFTYVLAMFTRLRQCAIAPYLITPDAKRNSKEKKNCSEWCLDKFGGAGIKSSKILKIVEIIKSVTLNDNPNCNSNPKSLQLLAKEKAYSCFGSDYIKSSNFEISHPTKIIVFSMFTSCLDLLSEAIKEDYPNFKFVQVDGDTKNRSELFDQFKNDINTQGLFLTYKVGSEGLNLTEATHCICIEPWWTNAVHNQAKARLWRTGQTKQVYVHNVIIEGSIEEKIVEICKGKDDMAASYLEGKERIKSPVRAPKLDKFTLGKMLGI", "text": "SIMILARITY: Belongs to the SNF2/RAD54 helicase family."}
{"protein": "MAPKTTLIAEPELVSKSVNTIRFLAIDAVEKAKSGHPGMPMGCAPMGHVLYDEFMRFNPKNPYWFNRDRFVLSAGHGCMLQYALLHLSGYDSVKEEDLKSLRQWGSRTPAHPENFETPGVEVTTGPLGQGIASAVGLAVAEKHLAARYNKPGFEIVDHYTYVILGDGCQMEGVSNEACSLAAHWGLGKLIALYDDNHITIDGDTDVAFTEDVDKRFDALGWHVIWVKNGNDGCDEIRAAIEEAKSVKDRPTMIKVTTTIGYGAPSKANTYGVHGNALGPKEAEATRKNLGWPYEPFHVPDDVKKHWSRHIAEGAALESAWNAKFAEFQKKFPEEAADLKSIITGELPTNWESIFPTYTPENPGLPTRTLSHQILNGLGDVLPGLLGGSADLTLSNMAFLKNSGDFQKKSPGERNVKFGAREHAMGSICNGLALHSPGLLPYCATYFVFTDYMRAAMRISALSKARVLYIMTHDSIGLGEDGPTHQPVEHLASFRAMPNILTLRPADGNETAGAYRAAVQNGERPSILVLARQKLPQLPGTSIEGVSKGGYVISDNSRGGNSKPDVILIGTGSELEIAARAGDELRKEGKKVRVVSLVCWELFAEQSEKYRETVLPSGVTARVSVEAGSTFGWERFIGPKGKAVGIDRFGASAPAERLFKEFGITVEAVVAAAKEIC", "text": "FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. FUNCTION: Could be involved in the conversion of sugars, which are a major phenomenon in the rehydration process. SIMILARITY: Belongs to the transketolase family."}
{"protein": "MRTFAPWILSLLGASAVASAADATAEAPSDVVSLTGDTFETFVKEHDLVLAEFFAPWCGHCKALAPKYEQAATELKEKNIPLVKVDCTEEEALCRDQGVEGYPTLKIFRGLDAVKPYQGARQTEAIVSYMVKQSLPAVSPVTPENLEEIKTMDKIVVIGYIASDDQTANDIFTTFAESQRDNYLFAATSDASIAKAEGVKQPSIVLYKDFDEKKATYDGEIEQDALLSWVKTASTPLVGELGPETYSGYITAGIPLAYIFAETKEEREQFTEEFKFIAEKHKGSINIVTIDAKLYGAHAGNLNLDPSKFPAFAIQDPEKNAKYPYDQSKEVKAKDIGKFIQDVLDDKVEPSIKSEAIPETQEGPVTVVVAHSYKDLVLDNEKDVLLEFYAPWCGHCKALAPKYEELASLYKDIPEVTIAKIDATANDVPDSITGFPTIKLFAAGAKDSPVEYEGSRTVEDLANFVKENGKHKVDALEVDPKKEQESGDATETRAASDETETPAATSDDKSEHDEL", "text": "FUNCTION: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the protein disulfide isomerase family."}
{"protein": "MPRERQKRGRRAEAKRKRDDEVGDRTAPKRQKASEGDNDFNPLHSQAKIGDDYIPLEEEPASSMDTPFYGLLDPDEQEYFSHASGLLELNQFETEEEKSIFIERVYEEADGKELKIACSQSCSRLMEKLISASTVSQIKSLFNKFVGQFLNLVQHRFASHCCESLFLRAAPYVTLEMKKNSAEKNDNECEDSSANLRLEDLFLAVLSELEGNWGYLLTERFASHTIRVLLLILAGEQLDNPSKATVIASRKKENLDKPKVTQRDKSASDRRAVPPSFNAALEKMMNDLVTGLDNTYLRALATHPVGNPVLQVLLSVELTHLGKSKARDPDSVFRRLVPDENLEEGSESAAFIKGLFYDPVGSRLLETMVQLAPGKFFKTFYKALVLERIGSLSRNEIAGHVVARILERLSKEDLKSSMDLILPEVLSLVKRSRFTVIKTLIERGVIRGVDLRPLADSLLLAFGTDPIARINNVLKLHHLNEENDDTKRSSKNSTPEQLHGSLLAQTMLKAPGPLSELIQSSLLAVTLETLIAIAKDPVASHVLQDALTLPTSTIQFRRQITSRFSGKMAELALDSSGSHVVDAVWSATENLIFIKQRFAEELLANERPLRDSFVGRAVWKNWSMDLYKRRRGHWIAVAKGLESVNPSNSENRQPPKSNLDLARARFAEKSNTSTPKKISATF", "text": "FUNCTION: RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP9 family."}
{"protein": "MLREFSFYDVPPAHVPPVSEPLEIACYSLSRDRELLLDDSKLSYYYPPPLFSDLNTGFPNRFHPPKSDPDPISIVKDVLMTKGIQMNSSFLTWRGLITKIMCAPLDPRNHWETYLVMDPTSGIIMMEERTRSETSYANQDRMCYWGYKFEAISTLPEIWDACSRDQIEQRDNQDVVPDEQYCSIVKINIGKSKLILAGEVDCIWDKKPCSAKESDVHSDDGTIEEDASNAENPNLHYVELKTSKKYPLENYGMRKKLLKYWAQSFLLGIGRIIIGFRDDNGILIEMKELFTHQIPKMLRPYFKPNDWTPNRLLVVLEHALEWIKQTVKQHPPSTEFTLSYTGGSKLVLRQII", "text": "FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (PubMed:28283058). Specifically degrades pre-mRNAs with a defective m7G cap and is part of a pre-mRNA capping quality control (PubMed:28283058). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end- capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:28283058). Also possesses RNA 5'- pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DXO/Dom3Z family."}
{"protein": "KKDGYPVEYDRAY", "text": "FUNCTION: Potentiates the contractile activity of bradykinin on the isolated guinea-pig ileum. Inhibits the hydrolysis of bradykinin by angiotensin-converting enzyme (ACE) and also inhibits the conversion of angiotensin I to angiotensin II by kininase II from guinea-pig ileum tissue. Also increases the depressor effect of bradykinin on arterial blood pressure in the anaesthetized rat. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Scorpion BPP (group 1) family."}
{"protein": "MAGGAVIENLSNRKLFVIFAGLLVIQIMFFLIGAWYAPSPSSYMEFEMITCRDETKGLSGEWIHRDNCQQISELSEYTPSSFDLREIVFIAKMPHTRDGIELEYSPWFQFLLGVLHVDVEYSEHFKYVAHAPLELEVRMGYRDKESKKNEWKELVTSNVTRILECTIAEDEKKAGGTYDCDMLDLFELGSSSYPFYLINIRIPINQQACQFDNKSANCQIGKLTGLRLIEIHQNGGFTLVWLWTKTFMTPVVAICLWWYYNRINQLARNPLLLERAILLLGLSLVILDFPIEWISLTYRIPFLLLISDLRQGLFYTVLFSFWLIFAGEHLIDDNTRNNLKSYRFNLSFIITASLGLLIYDLIERGIQLYDPFYSVWSSPTGSQIAYFAIFISAISTVAYFIFLFFKIARVWSTIKSKRSAQIYQTSENRRLKVEGVIYRFKFLMLFTLLCSAFTIAAYFMKQYGEAQLHGDEARDGFLTGSTSAFFTGAFGMCNIYVLLLLAMYAPSHKHYRGASQLIDENDDDEIMEDPSNQHTESNAMTTFLKPSTD", "text": "FUNCTION: Probable sorting receptor which regulates endocytosis and secretion of the wnt ligand egl-20 (PubMed:18160346, PubMed:18160347, PubMed:21076391). Recycling of mig-14 from the plasma membrane to the Golgi apparatus by the retromer complex is essential for its function (PubMed:18160346, PubMed:18160347, PubMed:21076391). Its endosomal trafficking is regulated by its association with sorting nexin snx-3 on early endosomes and the mtm-6/mtm-9 myotubularin complex (PubMed:21076391). Required in embryonic development for endoderm specification and the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells (PubMed:9288749, PubMed:16678095). Functions during vulval development, playing a role in vulval precursor cell fate specification (PubMed:11063687, PubMed:18077322). During development, specifically regulates the migration of HSN neurons, the left Q neuroblast (QL) and its descendants and the distal tip cells of the gonads (PubMed:8898225, PubMed:10388818, PubMed:11063687, PubMed:18160346, PubMed:18160347). Positioning of Q neuroblasts may be both dependent and independent of hox gene mab-5 (PubMed:8898225). Involved in establishing ALM and PLM neuronal cell polarity (PubMed:18160346). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Basal cell membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Note=Traffics between endosomal cell membrane and the Golgi apparatus membrane and the cell membrane to mediate wnt/egl-20 secretion (PubMed:18160347, PubMed:21076391). Co-localizes with snx-3 on intracellular punctae and early endosomes to facilitate recycling and wnt/egl-20 secretion (PubMed:21076391). Localizes to the basolateral cell membrane of intestine cells, but not the apical cell membrane (PubMed:26115433). SIMILARITY: Belongs to the wntless family."}
{"protein": "MPNNDILRPLAIPAKYVGSFLVFLYNGLYFVFVVNLWSRLFGKATKTEVPPLPKIRKLGKDMASRAPPRRGQSSEDNEDGLPAEIFNVRRHHKQAYAYIARALEVDEGQGSLETKKRAVEFYNRGIEEMEAGLLIPCIDEGEEWDKARRLQEKMEANLENTRERMDELVIIFFIIVVALLVSAGMMDDQPLLSARKTSSEPSQAWDVSKPTGPSYKQSKSYKNSTTVTTKRSQASPSFSSSSSSVNSTAGSSRTKPAKPAPMAAPRRYNPQVRRTKSTKPAMMAKQSCVDEQKKKISHLKGIDPKLANIIMDEILESGPAVHFSDIAGVDNAKKALQEIVILPSLRPELWRGDPTLVLFQVLPYPPGSSHITLPRASTATSFTSCFFSISKRSSLVHPVVASFFVKSLEDLASILTTSLFTIDEVDSLLTERREGEHEHSRRLKTEFLVSFDGVVADPEERILVMGATNRPQELDDAALRRMVKRIHIPLPDKETRKVLLTKLLAKHHNPLSGAEIDRLARMTEHYSGSDLTALARDAALGPIRDLNSDQLKSMAANEVRNITFQDFVNSLQIIRPSVGPETLKAYDDWNRLYGSNA", "text": "FUNCTION: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton Note=Forms an intramembrane hairpin- like structure in the membrane. SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily."}
{"protein": "MRWEFLPCLLLLISNNKIFGFKVPSINFEMLKDEGFEVSIPDEPGIQRVFYMFQIDDTCPALMDYITEAVNGSWVSKQKMSLQNNDKLQISMLVQFNEEIFEKSETRVIINTRLLTTKDSSSRGITFLTGEGECQAYLAPAQQAKRCKAAQTIVSNGRHTCQGELIFEDNFSEAQLNKTTWKHDIRQRMYHVEEELVAFDDAARNCFVKEGELHIVPTIATEVTDGSFKLGDRCTAVESPEQECNIAHGIFYSIKPPVFSAQIHTRNSFSFKFGKIVVRAKLPKGDWLFPYLMLQPVSTYAETHYAKQLRIAYARGNANLRTKQGDDISGNHLYGGGVVWHHGNAVQFLKDKISNSHYGDDFHNYTMIWQRDKITLMVDDEVYGELYDGLPFFNEKCFIIFGVTVGGFLNFDDSLLAKDVKPYKNREPRAALSFWQHRDAWAPTWGRHSAMVIDYVRVYAE", "text": "FUNCTION: Involved in the recognition of invading microorganisms. Binds specifically to beta-1,3-glucan and activates the phenoloxidase cascade (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein family."}
{"protein": "MKKYNKSFLIDVNCETLKVRQAFPFTALIGQTNMKLALILNVIDPKIGGVMSMGDRGTGKSTIVRSLVDLLPNIQVVSEDPFNSDPIDYDLMSQEVKEAKKSGEKIYTTSIKTPMVDLPLGATEDRVCGTIDIEKALIDGTKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAAGGWNTVEREGISIVHPARFILIGSGNPEEGELRPQLLDRFGMHVRIKTIKDPLSRVKIVERRSNFDKSAESFLKNYEYLQDFLKNRIVNAQGSLKDIKIDYQYKVNIAELCSNLNIDGLRGDIVTNRAVKAFVALNSRKTVLDKDVFTIMSLCLTHRLKKNPLESIDSSQNIVTIFKDIFGYSDLTA", "text": "FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Mg-chelatase subunits D/I family."}
{"protein": "MADSGLDKKSTKCPDCSSASQKDVLCVCSSKTRVPPVLVVEMSQTSSIGSAESLISLERKKEKNINRDITSRKDLPSRTSNVERKASQQQWGRGNFTEGKVPHIRIENGAAIEEIYTFGRILGKGSFGIVIEATDKETETKWAIKKVNKEKAGSSAVKLLEREVNILKSVKHEHIIHLEQVFETPKKMYLVMELCEDGELKEILDRKGHFSENETRWIIQSLASAIAYLHNNDIVHRDLKLENIMVKSSLIDDNNEINLNIKVTDFGLAVKKQSRSEAMLQATCGTPIYMAPEVISAHDYSQQCDIWSIGVVMYMLLRGEPPFLASSEEKLFELIRKGELHFENAVWNSISDCAKSVLKQLMKVDPAHRITAKELLDNQWLTGNKLSSVRPTNVLEMMKEWKNNPESVEENTTEEKNKPSTEEKLKSYQPWGNVPDANYTSDEEEEKQSTAYEKQFPATSKDNFDMCSSSFTSSKLLPAEIKGEMEKTPVTPSQGTATKYPAKSGALSRTKKKL", "text": "FUNCTION: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME (By similarity). Not essential for the survival of KRAS-dependent AML cell lines. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily."}
{"protein": "MSDKIGRIIAKMDECGVKFVRLQFVDIHGKPKNMAIPLVRPDQIEDIIKDGLLFDGSSVEGFVDINESDLVLKPDPDTFSTLPWRPEEKGVCRFICDIYWPDGKPFEGDPRYVLKRALDKYAHLGYEYNVGPEPEFFILDQDEDGNIIPHDCGAYFDVEPVDQGTDFRRKLVMDLEALNFDVEVSHHEVAPGQHEIDFKFDKALKTADAVITFKQAIKAIVDKIGYMVTFMPKPFFGENGSGMHCHQSLFKDGENVFYDPDTETQLSEEALYFIGGLLKHAPALTAVCAPTVNSYKRLVPGYEAPVYIAYGLKNRSTLIRIPASRGKGTRVELRMPDPSCNPYLAFAAMLEAGMNGIQNKIDPGEPTEIDVYEKSMSELREMGIETLPSSLWEAYHALEEDDVIKGALGGHVYEKFMEIKHREWDDYRVRVFKYELERYLDI", "text": "FUNCTION: Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family."}
{"protein": "MRLFPVRFSAASSSMASLAKMLDFYSGFNPSPLSIKQFMDFGQNACEKKSYIFLRKELPVRLANIMKEIALLPDNLLHTRSVSEVSSWYVKSFEDVLVYEKAEPTHDNLQKFVADLDLIRNRHNDVVQTMAQGVIEMKENEGGQVDAPTESSIQYFLDRLYMSRISIRMLINQHTLLFGGNPHAGGRHIGCLDPACDLSDVVRDAYENARFLCDQYYLTSPALEIQQHSSEPGDNLPIRTVYVPSHLYYMLFELFKNSMRAVVEHHGHDNNDTLPPLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSKSDLHTVPLAGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYLKALSDEANELLPIFNKTSSKFYRATVPTGDWSNQVKYAKKKKTSAVNQ", "text": "FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the PDK/BCKDK protein kinase family."}
{"protein": "MSIFIFISLVLGLAHQHKRSSIIVRLYSKDGFQKCSLTIRAVSAYALACKLQLEHRPLRAQRLRQIRLAQKSRVFPFIFYQCPHKKKSARIHALTFTKEAELSKLSIETLRCIHLQLISCTRSPVVTNSSY", "text": "FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus Note=Accumulates at the margin of the nucleolus, but is absent within it. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MTGKELNKIVAAILFASLIAMIVGFIANILYKPNLHVLHRGYSIAIQKSSSNESATVIAQESVNIQELMKTANANHGREIAKKCLMCHSLDKDGPNKLGPHLWNIVGRPKASITDYKYSFAISKLGGVWDDENLFAFLHKPSSYAPGTKMSFAGISKPQDIADVILFLKNYVHDQ", "text": "FUNCTION: May be involved in electron transfer from bc1 complex to aa3. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MSDIKNFEFTPIGYIKSKSGENDAKETLMSPTGASVRSPGSVGHVRKARRRSINDTVNSSRVENDNDTFDETLPELEMRKLPQYRRVPESRTSARNSGAAPQEEQNRNDYSDILSKTSNPIKDQEQKIKDLEHENTVLKVKNVSYRSLLANYSGGSSQNNINLVEEVSIWKTKYLETNEKLLKVKQDFESYVQKMEQEKEVNTDQEKTKEPEVIPIDNPEYIKEREHILEELERVTEDFKNLRDRYNDLEIKFLSIQNELDEKKQEFESSTARLNEEIHTLKSTIDDKDATISEFKRKLGNAEDQLASIDDQNGNQNQKLLHDLKEREDAIDGLKEDIIEKENAIVHYKEEIQDKQNQLKESESKYAEVQKEFEDFKRELKKQTFEFEDGKKSTSRQLQELSVEKIQLEKQVCNLRGQIEKLEQQHRLTQSENDGLRTKLKHIESDLKNEKSRTEVKIKDLTSDLEDARKNLGEANNTIKELHHEIIKNATKSKDQLSEEVVEKDKEIDQLKHRVQRLDEELRTSQAELDKATKNREVDHELEIRRLQNKHEIEQESLKRELAHMTDEKERLVDLHRLDIETWERQIEALRKENENLISREHKESNNIEITLQDKNIQIRRLEADIVQLNEERNDILNKLRSLEQAKDRYKSEMKDALETISRLRVDLENNKSLKDSKDSLIERKYEKLKDEFKLMKKGYLDEMIKLQSRNRELNSDLQKRMDPSISTSANTTLADKLDYYKLKYNDEVRHNNDLRVINEYLNRVLRASAQDIRLNLLKVENDLNIDIHKENVPLSAPLSSSGGRPYSSSYTREFDKYDYRYRQKGKRFKTVALAVLAVIRMYRAAKKHNWNEQRIRYLQRKIIAKEDRITW", "text": "FUNCTION: Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Potential role in cross-linking filaments or anchoring other molecules. It is essential for growth (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body Note=Tightly associated with the nucleus. It is present in a granular pattern that excludes the nucleolus. SIMILARITY: Belongs to the SPC110 family."}
{"protein": "MFCCLGYEWLSGGCKTWHSAWVINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDGSTDVQQRARRSNCRRQEGIKIVLEDIFTLWRQVETKVRAKIRKMKVTTKVNRHDKINGKRKTAKEHLRKLSMKEREHGEKERQVSEAEENGKLDMKEIHTYMEMFQRAQALRRRAEDYYRCKITPSARKPLCNRVRMAAVEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHSIIDNSLSLKTPSERLLYPLPPSADDNLKTPPECLLTPLPPSALPSADDNLKTPAECLLTPLPPSAPPSADDNLKTPPECVCSLPFHPQRMIISRN", "text": "SIMILARITY: Belongs to the NPIP family."}
{"protein": "MPGALSGRRMLPSGLCLGRWQLLRTIRARGRGDPRELPSTPQVLCMKLYGNPKYHQALHYGTVEPQDEITVTYKHGLPLVTLTLPSRKERCQFVVKPMLSTVGSFLQDLQNEDKGIKTAAIITADGSEIPASTLMDTLLMTDFKLIINKLRYDIRCHKKEEPSGEHMTELENTKSLVHRLFTILHLEEIQKRRERHLMAKIDHLQEQLRPLEQVKAAIEARSEANTSGLLWAGLALLSVQGGALAWLTWWVYSWDIMEPVTFFLSFANSIVFFAYFIITRQNYTYSSLRSRQFLQFFHKKSQRRCFDVEQYNKLKEDLAEATESLESVRRSLRLRIQGEEASEKN", "text": "FUNCTION: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MCU (TC 1.A.77) family."}
{"protein": "MGAAVTLNRIKIAPGIADIRDKYMELGFNYPEYNRAVKFAEESYTYYYETSPGEIKPKFCLIDGMSIDHCSSFIVPEFAKQYVLIHGEPCSSFKFRPGSLIYYQNEVTPEYIKDLKHATDYIASGQRCHFIKKDYLLGDSDSVAKCCSKTNTKHCPKIFNNNYKTEHCDDFMTGFCRNDPGNPNCLEWLRAKRKPAMSTYSDICSKHMDARYCSEFIRIIRPDYFTFGDTALYVFCNDHKGNRNCWCANYPKSNSGDKYLGPRVCWLHECTDESRDRKWLYYNQDVQRTRCKYVGCTINVNSLALKNSQAELTSNCTRTTSAVGDVHPGEPVVKDKIKLPTWLGAAITLVVISVIFYFISIYSRPKIKTNDINVRRR", "text": "FUNCTION: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the mature virion (MV) membrane (Probable). The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. SIMILARITY: Belongs to the orthopoxvirus OPG143 family."}
{"protein": "MSGGKGKAGSSEKASTSRSAKAGLTFPVGRVHRLLRKGNYAQRIGSGAPVYLTSVLEYLAAEILELAGNAARDNKKSRIIPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNIHQSLLPAKKAKAGAASQEL", "text": "FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H2A family."}
{"protein": "MAKDPVRVLVTGAAGQIGYALVPMIARGVMLGPDQPVILHMLDIAPAAESLNGVKMELVDAAFPLLKGVVATTDVVEACTGVNIAVMVGGFPRKEGMERKDVMSKNVSIYKSQASALEKHAAANCKVLVVANPANTNALILKEFAPSIPERNISCLTRLDHNRALGQISERLNVQVSDVKNVIIWGNHSSTQYPDVNHATVNTPAGEKPVRQLVSDDAWLNGEFISTVQQRGAAIIKARKLSSALSAASAACDHIRDWVLGTPQGTFVSMGVYSDGSYNVPSGLIYSFPVTCANGEWKIVQGLSIDEFSRKKLDLTAEELTEEKNLAHSCLS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MEPHDQSGSTTRQLDEIRDRRGSQIRSVRLLPWRPFTRFPVCPSGTSPYSRGTHSQPSYVRCQNCERARQWFRAHDGPRCLHQRPDYSRLQAPPDPFQHLNSFEPILLAALSVLRPLPRDIQITIISCACDYFHSVRCASSRYLGSSRSAVKRRAARLNYCYKCGHPLYLNKPHTCRPGRLCSASISERLALLREGPIRSLTENPINARAAHFLAHELLDPR", "text": "FUNCTION: May act as a regulatory factor during viral transcription."}
{"protein": "MMTMTTMADGLEAQDSSKSAFMEFGQQSHSQQSSPSMAASHYPLHCLHSGSHHHHQHDSSPYSGSNSYNRSLPYSYVSHPHHSPYLPSYHSNASGTQTRLDATEQQKTTVIENGEIRFNGKGKKIRKPRTIYSSLQLQALNHRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKRSKFKKLLKQGGNPHETDTLPGSIALSPRSPAIPPIWDVSASSKGVNMSANSYMPGYSHWYSSPHQDAMQR", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the distal-less homeobox family."}
{"protein": "MARWRPDMAEREATPEALYLRRRDFLALGAAGAVGLLLPRGARAGDPTGAALQVARKVDQAGGETPTPWDSVTGYNNFYELGTSKEDPSRNAGSLRARPWTVTIAGEVKRPQTLDVDALVRMFPPEERVYRMRCVEAWSMVIPWVGFPLADLVRRLEPTSRAKYVAFQTLLDRDQLPGQRRPVLPWPYVEALRIDEANHPLALLAVGLYGRVLPGQNGAPLRLVVPWKYGFKGAKSIVRITFLADRPHTTWNDAAPDEYGFYANVNPEVDHPRWSQARERRIGEFFRRKTLPFNGYAAEVAPLYAGLDLRKNY", "text": "FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. SUBCELLULAR LOCATION: Periplasm Note=Is attached to the inner membrane when interacting with the MsrQ subunit. SIMILARITY: Belongs to the MsrP family."}
{"protein": "MSNQMTDSTSAGSGTEHSVDTNTALKAGSPNDLKVSHEEDLNDLEKTAEETLQQKPAKEYIFVSLCCVMVAFGGFVFGWDTGTISGFVNQTDFLRRFGQEKADGSHYLSNVRTGLIVSIFNIGCAVGGIVLSNIGDRWGRRIGLITVIIIYVIGIIIQIASVDKWYQYFIGRIISGLGVGGITVLSPMLISETAPKHLRGTLVSCYQLMITFGIFLGYCTNYGTKNYSNSVQWRVPLGLCFAWAIFMVLGMMFVPESARFLVETDQIEEARKSLAKTNKVSIDDPVVKYELLKIQSSIELEKAAGNASWGELITGKPSMFRRTLMGIMIQSLQQLTGDNYFFYYGTTIFQSVGMDDSFETSIVLGIVNFASTFFALYTVDHFGRRNCLLYGCVGMVACYVVYASVGVTRLWPDGPDHPDISSKGAGNCMIVFACFYIFCFATTWAPIAYVVISESYPLRVKGKAMAIASASNWIWGFLIGFFTPFITSAIHFYYGYVFMGCMVFAFFYVYFFVPETKGLTLEEVNEMYSEGVLPWKSSSWVPSSRRGAEYDVDALQHDDKPWYKAML", "text": "FUNCTION: Low-affinity glucose transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKDD", "text": "FUNCTION: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). GTPase that impacts interactions between enteropathogenic E.coli (EPEC) and epithelial cells and also has an effect on motility (PubMed:9622352). FUNCTION: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA. FUNCTION: A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity, required for 50S subunit assembly at low temperatures, may also play a role in translation (PubMed:30305394). Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable) (PubMed:25777676, PubMed:30305394). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides (PubMed:30305394). Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleotide binding (PubMed:26163516, PubMed:26283392). Interacts with ribosomes (Ref.12, PubMed:26283392). Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA. Ribosome binding alters its conformation (PubMed:26283392). Genetically its function does not overlap LepA, and it acts in a different pathway during ribosome assembly than does RNA helicase DeaD (PubMed:25777676). GTPase that affects interactions between enteropathogenic E.coli (EPEC) and epithelial cells (PubMed:9622352). Probably regulates expression of proteins required for (at least) K5 polysaccharide production (Probable). Deletion mutants of bipA are suppressed by an rluC deletion, which no longer modifies uracils 955, 2504 and 2580 to pseudouridine in 23S rRNA; there are 5 other pseudouridine synthases in E.coli, only rluC suppresses this phenotype. Mutating 23S rRNA so the 3 uracils are other nucleotides also suppresses the bipA deletion; pseudouridine-2504 is required for ribosome assembly and translational accuracy (PubMed:18820021, PubMed:25777676). SUBCELLULAR LOCATION: Cytoplasm Note=Binds to ribosomes. SUBCELLULAR LOCATION: Cytoplasm Note=Associates with 70S ribosomes and 30S and 50S subunits in the presence of GMPPNP (a nonhydrolyzable GTP analog) at both 20 and 37 degrees Celsius; no change in ribosome association is seen in the presence of ppGpp or when the stringent response is triggered. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily."}
{"protein": "MSFGVPHSGGSRRSKWDQAGPDADAGSAPTGALDAAAAVAAKINAMLVAKGKLKPSQISSAAPVDKAAGAGGNKLKDDLVVAEVEINDVPLTCRNLLTRGQTQDEISRVSGAAVSTRGRFMTVEEKSKALPSDRPLYLHVQGQTRDLVDKAVNRIKEIITNGVVKAATNSTYSGATVTVYQQSGPSVPTIPSAPHKPHYPGGMHYVQDKVFVGLDQALQGFNVKERVEGPSCSFLQHIQAETGAKVFLRGKGSGCLEPASGREAFEPMYIYISHPKPEGLASAKTLCENLLQTVHAEYSRYLNQMSSMMPTQGFIHPPVVNGLPPQPPYYSPAGFQPSYPAPVPPPPPPIAPQYPVAPVAPAPVPPPNAQYPITPVPAHVPTQTLLPAAFPPTAPVPPKLTAPPNPPQKRRFTEEVDEMDRGLLGYQHGPIHMTNLGAGMPVGSSETSGPPSAASSVPVRERDSSRQLMPPPCAPALLKPLRPLKADESPSAPSLLEPQVKRMRTGLVAYAGDSSDEEEDHGPSRAAVTAAGNPGAGWNPYRCPPSPPHRPKTQTAPQPTQQNMPFWMAP", "text": "FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. Involved in regulating splice site selection. Binds preferentially RNA with A/C rich sequences and poly-C stretches. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the KHDC4 family."}
{"protein": "MKARELDVPGAWEITPTIHVDSRGLFFEWLTDHGFRAFAGHSLDVRQVNCSVSSAGVLRGLHFAQLPPSQAKYVTCVSGSVFDVVVDIREGSPTFGRWDSVLLDDQDRRTIYVSEGLAHGFLALQDNSTVMYLCSAEYNPQREHTICATDPTLAVDWPLVDGAAPSLSDRDAAAPSFEDVRASGLLPRWEQTQRFIGEMRGT", "text": "FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family."}
{"protein": "MAALYGGVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPNLSENYLITTDAAGSIATATPDGGIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGHVKQAMFDYFQVPDRLGILTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPVLFQGELGLPILCVGSVWKSWELLKEGFLLALTLGREQQAQNSFSSFTLMKLRHSSALGGASLGARHIGYHLPMDYSINAIAFYSYTF", "text": "FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate (PubMed:10824116). Also has N-acetylmannosamine (ManNAc) kinase activity (PubMed:10824116). Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (PubMed:22692205). Also involved in innate immunity by promoting detection of bacterial peptidoglycan by NOD2: acts by catalyzing phosphorylation of muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, to generate 6-O-phospho-muramyl dipeptide, which acts as a direct ligand for NOD2 (PubMed:36002575). SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase family."}
{"protein": "MAKFRRGTCIILALFILFIFSLMMGLKMLRPNTATFGAPFGLDLLPELHQRTVHLGKSFDFQKSDRINSETNTKNLKSVEITMKPSKASELNLDELPPLNNYLHVFYYSWYGNPQFDGKYIHWNHPVLEHWDPRIAKNYPQGRHNPPDDIGSSFYPELGSYSSRDPSVIETHMRQMRSASIGVLALSWYPPDVNDENGEPTDNLVPTILDKAHKYNLKVTFHIEPYSNRDDQNMYKNVKYIIDKYGNHPAFYRYKTKTGNALPMFYVYDSYITKPEKWANLLTTSGSWSIRNSPYDGLFIALLVEEKHKYDILQSGFDGIYTYFATNGFTYGSSHQNWASLKLFCDKYNLIFIPSVGPGYIDTSIRPWNTQNTRNRINGKYYEIALSAALQTHPSLISITSFNEWHEGTQIEKAVPKRTSNTVYLDYRPHKPGLYLELTRKWSEKYSKERATYALDHQLPVS", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 99 family."}
{"protein": "MKGAAFVKKEGLKQKALEIGRVPTHLKLEIEDYGGDDKRAHFCWADPQDENTGIIVELGPDGELESLSRDIEPESGERLSEEKLEDIMRQFVETHHPGALSAFVREENDRAYGDKVRFSYVQMEAGLPLPMSGFMADVSLSGEIVYFRYYGEAGSIIKPKRVADVEEALAFIKKDVEFDLLFEVLHRSVYKNGDDQPHLVYEPEGRAITVPADLVQEEQAVDDDDDYREPESFPLPLFEGIREKADPDSMIGIENGFVKEREADLGDGRIGIVWRNPDDPVYQPADKSMDSWFKGRTHQVLKTIYNKETGKLEGVMSFMEKKGPLTVTLAECEKIALRFLFALFPNADQYFRIRYDEKDEEENAVAGFTFEAHCHGVPLRFGQIRICVSRQTGYITVYMGPDIDPNKLATIDPVPAISVEQAKSIFWQHFKVELGWEREYGDDEEHSYRLVYKPVYPHFIDAHTGEPVFSIW", "text": "SIMILARITY: To B.subtilis YcdC."}
{"protein": "GPMGWVPVFYRF", "text": "FUNCTION: This peptide activates mouse sensory neuron-specific G- protein coupled receptors MRGPRX1, but not human receptors (PubMed:30243794). In vivo, causes hyperactivity in mice when injected intracranially (PubMed:11738233). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
{"protein": "MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTAAQQRGELLHHTLGDGEFRHFYHMSEPITVAQAVLTEQNACYEIDRVLTTMLRERRPGYLMLPADVAKKAATPPVNALTHKQAHADSACLKAFRDAAENKLAMSKRTALLADFLVLRHGLKHALQKWVKEVPMAHATMLMGKGIFDERQAGFYGTYSGSASTGAVKEAIEGADTVLCVGTRFTDTLTAGFTHQLTPAQTIEVQPHAARVGDVWFTGIPMNQAIETLVELCKQHVHAGLMSSSSGAIPFPQPDGSLTQENFWRTLQTFIRPGDIILADQGTSAFGAIDLRLPADVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYTVERAIHGAEQRYNDIALWNWTHIPQALSLDPQSECWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGALTKALEACNNA", "text": "SIMILARITY: Belongs to the TPP enzyme family."}
{"protein": "MTEPDVEISSVLTGEDTLVLASMDTPAEIELVMDWLCQQRNRNPDIKFDVLKLPSRNLAPAALTALVEQLESDEDRSVVPVRVFWMPPAERSKLAKLAGLLPGRDPYHPNRRQQRHILKTDARRALVIAGDSAKVSELRQYWRDTTVGENECDFAQFVTRRAILAMERAESRILGPQYKSPRLVKPEILASTRFRAGLEKISGATVEEAGKMLDELATGWSRASVDLVSVLGRMLSRGFEPEIDYDEYQVAAMRAALEAHPAVLLFSHRSYIDGAVVPVAMQENRLPPVHVFAGINLSFGLMGPLLRRSGVIFIRRNIGDNPLYKYVLREYVGYIVEKRFNLSWSIEGTRSRTGKMLPPKLGLLTYVADAYLDGRSEDILLQPVSISFDQLHETAEYAAYARGGEKTPEGVAWLYSFIKAQGERNYGKIYVRFPEAVSMRQYLGAPHGALVQDQDAKRLALQKMSFEVAWRILCATPVTATALVSALLLTTRGVALTLDQLHHTLQESLDYLERKQTPVSKSALRLRSREGVRAAVDALSSGHPITRVDSGREPVWYITPGNEHAAAFYRNSVIHAFLETSIVELALAHARHVEGDRMKVFWAQAMRLRDLLKFDFYFADSAAFRANIAEEIAWHQNWEDRVSGDGDDIDAMLLTKRPLISDAMLRVFFEAYDIVADVLRDAPADVGQKELTELALGVGRQYVAQGRVRSGESVSTLLFATAYQVVVDQNLIAPAPDLAERRMVFRRELRDIRRDFDYVEQIARSRFIVREFKSR", "text": "SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family. SIMILARITY: Belongs to the GPAT/DAPAT family."}
{"protein": "MEDDGGERSSFVAGLIENRAKEVGMAAFDLRSASLHLSQYIETSSSYQNTKTLLRFYDPSVIIVPPNKLAADGMVGVSELVDRCYSTVRKVVFARGCFDDTKGAVLIQNLAAEEPLALGLDTYYKQHYLSLAAAAATIKWIEAEKGVIVTNHSLTVTFNGSFDHMNIDATSVENLELIDPFHNALLGTSNKKRSLFQMFKTTKTAGGTRLLRANLLQPLKDIETINTRLDCLDELMSNEQLFFGLSQVLRKFPKETDRVLCHFCFKPKKVTEAVIGFENTRKSQNMISSIILLKTALDALPILAKVLKDAKCFLLANVYKSVCENDRYASIRKKIGEVIDDDVLHARVPFVARTQQCFALKAGIDGFLDIARRTFCDTSEAIHNLASKYREEFNLPNLKLPFNNRQGFFFRIPQKEVQGKLPNKFTQVVKHGKNIHCSSLELASLNVRNKSAAGECFIRTETCLEALMDAIREDISALTLLAEVLCLLDMIVNSFAHTISTKPVDRYSRPELTDSGPLAIDAGRHPILESIHNDFVSNSIFMSEATNMLVVMGPNMSGKSTYLQQVCLVVILAQIGCYVPARFATIRVVDRIFTRMGTMDNLESNSSTFMTEMRETAFIMQNVTNRSLIVMDELGRATSSSDGLAMAWSCCEYLLSLKAYTVFATHMDSLAELATIYPNVKVLHFYVDIRDNRLDFKFQLRDGTLHVPHYGLLLAEVAGLPSTVIDTARIITKRITDKENKRIELNCGKHHEIHRIYRVAQRLICLKYSRQTEDSIRQALQNLNESFTEERL", "text": "FUNCTION: Involved in meiotic recombination in association with MSH5. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis. Promotes homologous recombination through facilitating chiasma formation during prophase I. Involved in the control of class I crossovers formation. SUBCELLULAR LOCATION: Nucleus Note=In pollen mother cells during meiosis, localizes to unsynapsed axes during leptotene and zygotene, but is not present on synapsed regions of zygotene nuclei. SIMILARITY: Belongs to the DNA mismatch repair MutS family."}
{"protein": "MKRDVRILLLGEPKVGKTSLIMSLVGEEFPEQVPLRAEEITIPADVTPEKVPTHIVDYSENEQTDEVLREEIVKANVVCVVYDVTQEETIDKIRTKWIPLVNGGAEKGSKIPIILVGNKSDLRSGSSMETILPIMNQFSEIETCVECSAKNLKNISELFYYAQKAVLHPTAPLYDPEDKQLKAQCVRALSRIFSISDQDNDHILSDAELNCFQKLCFGNPLAPQALEDVKTVVWKNTSDGVQDNGLTLNGFLFLNTLFIQRGRHETTWTILRKFGYDDTLELTDDYLYPVLRVSVGCTTELNHLGHQFLLKLFEKYDEDKDSALSPAELKNLFSVLPYMPWSSTVYSNIPLTDDCYISQHGYLCQWMLLAYLDVHRCLEHLGYLGYPILMEQECQTSAITVTREKALDLDNRQTQRTVFLCKVIGPRGTGKTDFLRAFLQRSTERSDRDPGAPSIYAINTVSIANQDKYLILEEVDVETEFLKAADAACDVACLMYDVSDPDSFNYCASIYKQHYMDSGIPCVVLGSKADLVEVKQHHGMSPSEFCYKHRLPSPLHFSALLTHTHTHIYSKLTWAAMYPHLNGSDMSSTSFWLRVTLGATIAAMLGFALYRAFSRHK", "text": "FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the mitochondrial Rho GTPase family."}
{"protein": "MEDPFEEADQPATEPGMVMDSVEAGDTTPPTKRKSKFSGVGKIFKPWKWRKKKSSDKFKETSEVLERKISMRKPREELVKRGVLLEDPEQGGEDPGKPSHAMLKNGHTTPIGNARSSSPVQVEEEPVRLASLRKAIPEEDLKKRLGSTGSQPNSEAESVPENVPKPPLLPPKRPLSSSHEASEGQAKDATSSGGTARFIISTSITTAPAATTAATSLAKTVNLSVTPSPAPRTLPAAPASTNTTATPSLTHMVPAKQPPIPPPKPAHRNSNPVIAELSQAINSGTLLSKPSPPLPPKRGIPSTSVPTLESAAAITTKTPSDEREKSTCSMGSELLPMISPRSPSPPLPTHIPPEPPRTPPFPAKTFQVVPEIQFPPSLDLHQEIPQQEDQKKEVPKRILDQNFGEPHIPSRLPPLPLHIRIQQALTSPLPVTPTLEGSHRAHSLLFENSDSFSEDSSTLGRTRSLPITIEMLKVPDDEEEEEQICPSTFSEETTPTSVIPKLPQCLREEEEKESDSDSEGPIQYRDEEDEDESYQSALANKVKRKDTLAMKLNHRPSEPELNLNSWPCKSKEEWNEIRHQIGNTLIRRLSQRPTPEELEQRNILQPKNEADRQAEKREIKRRLTRKLSQRPTVAELLARKILRFNEYVEVTDAQDYDRRADKPWTKLTPADKAAIRKELNEFKSSEMEVHEESKHFTRYHRP", "text": "FUNCTION: Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, lamellipodium. SIMILARITY: Belongs to the phosphatase and actin regulator family."}
{"protein": "MKSSKIVAILLASLFSGSVLAAGCSVDVEANDAMQYNTKNIDVEKSCKEFTVNLKHTGSLPKNVMGHNLVITKTADFKAVMNDGVAAGEAGNFVKAGDARVVAHTKLVGGGEKDSVKVDVSKLAAGEKYTFFCSFPGHATMMRGTVTVK", "text": "FUNCTION: This methylothroph organism uses azurin in the electron transport chain involved in methylamine/methanol oxidation. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MNGTTQNNAALFDGGVFSPYLTSRLPYWAGVRQNVVGSTVDGRPVAPANSSTLTYATIGPSPLDTAAAAAASAAASTARSMAADFSFYNHLASNAVTRTAVREDILTVMLAKLETLTAQLEELSQKVEELADATTHTPAQPVTQ", "text": "FUNCTION: Structural component of the virion that acts as a cement protein on the capsid exterior and forms triskelion structures consisting of three molecules that stabilize three hexon trimers at the center of each icosahedral facet and fixes the peripentonal hexons. Dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus. SUBCELLULAR LOCATION: Virion Host nucleus Note=Located in the canyons between the hexons on the outer surface of the capsid. Forms a sort of hairnet on the outer side of the virion. Present in 240 copies per virion. SIMILARITY: Belongs to the adenoviridae hexon-interlacing protein family."}
{"protein": "MSLCTSSHKDFSQLLPLQDIGCNKTEIKNSPAGVISPAPYSCNQSTLTAEHSPVYIPSSYMESRHEYSTMAFCSPAMVNYNIASNFGDPEAVAARQTSSPGALWSAPGHLSPLSLHCQSSLLYAEQPKSLWCEARPMEPVLPGSRETLKRKTNGNDCTSPIANNPGSKKDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMMKCGSRRERCGYRILRSHRGAEERVHCLGRARRYSEAATRVKEILLSTVSPEQFVLTLLEAEPPHVLVSRPSKPFTEASMMMSLTKLADKELVHMIGWAKKIPGFIDLSLYDQVRLLESCWMEVLMIGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLAMTSRFRELKLQHKEYLCVKAMILLNSSMFPLSAEEPESNRKLHHLLNVVTEALVWVIAKSGIPSQQQTTRLANLLMLLSHVRHASNKGMEHLLSMKCKNVVPVYDLLLEMLNAHTLRGQRKPLATHPEFGPLEQMEPGESLRKGEPQ", "text": "FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Locally synthesized estrogens may act via ER beta, in addition to ER alpha, to mediate seasonal or developmental effects on nearby song nuclei. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily."}
{"protein": "MIKWPWRTQPPAQQDSYPWPEACAIPLLAALGDDEQQRLIALARQVIRQKRLIPLQELRVTPLMEARIALLFALPVLELGIGWLDGFHEILLYPEPYVLHEEWEDDIGLVHCGPSVQAGQCSAQGPVVLNWLDVRDSFDCSGYNLIIHETAHKLDMRNAGIASGIPPIPLREIAAWEQALHAAMEAIQEEADLLGKEGASMDAYAASEPAECFAVLSEYFFSAPELLSERFPAVYAHFARFYRQDPLQRLYQSGLLTPESF", "text": "FUNCTION: Involved in the regulation of ptsG expression by binding and inactivating Mlc. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MtfA family."}
{"protein": "MREIKTPKAPVPVGPYSQAVEVNGFLFISGQIGINPETGKLVEGFKEQVIQIFKNVDAILEEAGLKRENIVKVTIYITDIKKFKELNEIYEDYFKDVSVKPARVTVGVKELPLNAEVEIEIVAVK", "text": "SIMILARITY: Belongs to the RutC family."}
{"protein": "MKLMRIQEMEEYILSHGTVSLDELCQVFNVSKNTVRRDINKLTEKGAIEKVYGGVTSIEKTALVPFENRTIQHQDEKTKIAHYASRFIEDHDLVFIDSGTTTKSILDTLDPAKNVTILTNSLDIINAASALKNINLIIIGNNYKRKTRSFVGMDDPAMLDKYNINKAFMSATGTTLTHGLTNSDLLEYEIKKRISEKAKEVYLLADHSKFGKSTLLTYAPFDRLHCIVTSQPLDDEYTQYCNEHQIGIHLA", "text": "FUNCTION: Iol operon repressor."}
{"protein": "MTSFEDADTEETVTCLQMTVYHPGQLQCGIFQSISFNREKLPSSEVVKFGRNSNICHYTFQDKQVSRVQFSLQLFKKFNSSVLSFEIKNMSKKTNLIVDSRELGYLNKMDLPYRCMVRFGEYQFLMEKEDGESLEFFETQFILSPRSLLQENNWPPHRPIPEYGTYSLCSSQSSSPTEMDENES", "text": "FUNCTION: Adapter molecule that plays a key role in the activation of pro-inflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs) (PubMed:12566447, PubMed:15492226, PubMed:26068852, PubMed:28877472, PubMed:28222186, PubMed:30111836). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism (PubMed:15492226, PubMed:26068852). TIFA-dependent innate immune response is triggered by ADP-D-glycero- beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram- negative and some Gram-positive bacteria: ADP-Heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of pro-inflammatory NF- kappa-B signaling (PubMed:30111836). SUBCELLULAR LOCATION: Cytoplasm Note=Colocalizes with lysosomal marker LAMP2 following homooligomerization and subsequent activation. SIMILARITY: Belongs to the TIFA family."}
{"protein": "MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM", "text": "FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors (PubMed:10688651, PubMed:12359225, PubMed:12873986, PubMed:15194700, PubMed:17344214, PubMed:18242580, PubMed:22306293, PubMed:23084476). Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (PubMed:17344214). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:12873986). Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes (PubMed:12359225). Activated by IL31 through IL31RA (PubMed:15194700). Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (PubMed:28065600). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (PubMed:17344214). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (PubMed:23084476). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. Identified in a complex with LYN and PAG1. SIMILARITY: Belongs to the transcription factor STAT family."}
{"protein": "MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSACSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLALDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNALTDHTSANHSLVKASVVTVRESPATPVSFQAATTSTVSDHAKLHAPGSECLGPKAVSCDPAKRKGWARFKDACGKGEDWNKVSKAESMETLPERTKAPGEATLKKTDSCDSGITKSDLRLDNVGETRSPQDRSPILAEVKHSFYPIPEQTLQATVLEVKYELKEDIKALNAKMTSIEKQLSEILRILMSRGSAQSPQETGEISRPQSPESDRDIFGAS", "text": "FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:19671703, PubMed:23975098). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Nucleus inner membrane; Multi-pass membrane protein Cell projection, dendrite Cell projection, axon Presynaptic cell membrane Perikaryon Postsynaptic density membrane Early endosome membrane Note=Perinuclear KCNH1 is located to NPC-free islands. SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Kv10.1/KCNH1 sub-subfamily."}
{"protein": "MPEGKFCNRKPVNTEEDLKALLGDKGGAQYYKEMEELEVDQEALWANIEKTCQSRTKTWLEICAHCGMCADSCFLYRVNDRDPKQVPAYKIQSTLGEIIRRKGKVDTQFMLHAMEVAWSQCTCCNRCGQYCPHGIDMGVMFSYLRGLLYSQGFVPWELKIGSGMHRVYGAQMDVTTEDWVETCEWMAEEQQEEWPGLEIPVDVENADIMYVLNAREPKHYPEDVAEAAILFHIAGENWTVPSEGWEQTSLAMFAGDWAACKMQVERVYAAIERLKPKCVVGTECGHAHRASAIEGPYWAGYEDGKTPAPWLHYVEWVAMALRTGKIKIDPEKRIKEPVTLQDSCNYIRNHGLAKCTREIMSYIADDFREMTPNREHNYCCGGGGGFNGIGKFRKQRNKALQTKRDQILATGAKLVVAPCHNCWDAIRDLEEEYRIGIRWSFLKPLIIKMAIIPEHLRPEEE", "text": "FUNCTION: HMWC (high-molecular-weight cytochrome c precursor), ORF2, ORF3, ORF4, ORF5, ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates. ORF6 is a redox protein. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MASAMTCSAAELFPHLGSSANATAAAEFICSRFSAVSEYLTNTTYAVDTTYLLFSAYLVFAMQLGFAMLCAGSVRAKNTMNIMLTNVLDAAAGGFSYYLFGFAFAFGAPSNGFIGKHFFGLKEFPSQAFDYSYFLYQWAFAIAAAGITSGSIAERTQFVAYLIYSSFLTGFVYPIVSHWFWSGDGWASASKTDGNLLLRFGVIDFAGSGVVHMVGGIAGLWGAFIEGPRIGRFDRSGRSVALRGHSASLVVLGTFLLWFGWYGFNPGSFLTILKSYDHTIRGTYYGQWSAIGRTAVTTTLAGCTAALTTLFCKRLLVAHWNVVDVCNGLLGGFAAITSGCAVVEPWAAIVCGFIAAWVLIGFNALAAKLKYDDPLEAAQLHGGCGSWGIIFTGLFAKKEYVNEVYPGFPNRPYGLFMGGGGKLLGAQVIQVVVIIGWVSVTMGPLFYLLHKFKLLRISRDDETAGMDLTRHGGFAYIYHDEDEGSSMPGFKMTRVEPTNTSTPDHQNRSVNVVV", "text": "FUNCTION: Ammonium transporter probably involved in ammonium uptake from the soil. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family."}
{"protein": "NQQSGXSETKVVVG", "text": "FUNCTION: N-acetyl-galactosamine and D-galactose specific lectin. Binds the Tn-antigen structure GalNAc-alpha-1-O-Ser, the T-antigen structure Gal-beta1-3-GalNAc and IgA. SIMILARITY: Belongs to the jacalin lectin family."}
{"protein": "MHKLTSKLSNLILLLLIIIIFISLILTNFNNYLLENLSEYEIKINNTEISREEFIQRYNLECFYNDKNFKNDIITNPKNPKYISEIYNITLSNIIYESLLQQYVHQLHFNIDYSHVKNYIYKQTIFRQNQKFNKEKYYEYLKKLQISSNEYIKKVMTYLEIKEFIKTLTNTDFILNNEKNNILKLFEQGRIVNKSYVNLNNLKLIEHISNKELKRYYINHKHQFLSPKKFKISYFLINKNNVFVPCIKKFYFKNKDNTFQHELFLQHKKSKKQNDNIIKKLLTTHTNTSQFKNIIQKNNICIHHTPWLTQTLYKHEKLPKKLLKYIINNNILFHNNKNTIKNYPTIIHMNNNNAYVLWIQKYEKATIENFSKKIRKKIINILKNEHSKKIRYQIVQKIVYQLNHGDTNLFSQLKLKFSNSEYYSRFNTNTLTNKIFSLPIPKKGQKIYFIFHDQKKLFLYQFSNIFYFKLTKKQKKMIASYISQSHSEIILNAILENLYKTAHISYKGYIN", "text": "FUNCTION: Chaperone that functions as a gatekeeper on the extracellular side of the Sec translocon. Facilitates the translocation of precursor proteins across Sec by interacting with the translocating substrate. Also plays a role in the release of newly synthesized secreted proteins at the extracellular exit site of the Sec translocon. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein; Extracellular side Note=Located at the lateral gate of SecY. SIMILARITY: Belongs to the PpiD chaperone family."}
{"protein": "MESSGLRAPCSLLVLLSALVLPPTLAIEVYTDREVYGTVGSRVTLSCSFWSSEWISDDVSVTWHYQPDHSREMYSIFHYAKGQPSIDAGVFKDRIEWVGSPKWKDASIVLHNLELIDNGTFTCDVKNPPDVVGKSSYVHLQVQEKGAARAGLVLGIIIAVALALVIVVTILILLIRYCWLRRQVRVQRELSALERGKLHKAKDSSKRSSRQTPILYAMLDQTRGKASEKKGKGGIGDSRKDRK", "text": "FUNCTION: Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the myelin P0 protein family."}
{"protein": "MVGHLSEGAIEVMIQQENTSIKPILQVINIRPISTGNRSPRYRLLMSDGLNTLSSFMLATQLNTLVEGGQLASNCVCQVHKFIVNTLKDGRKVVVLMDLEVMKSAEDVGLKIGNPVPYNEGYGQQQQQQQQQQQQAVPSPASAATPPASKPQPQNGSLGMGSTAAKAYGASKPFGKPAGTGLLQPSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGALKIANKQFSAVKNDYEMTFNNETSVLPCEDGHHLPTVQFDFTGIGDLESKAKDALVDIIGICKSYEDSIKITVKSNNREVAKRNIYLMDMSGKVVTTTLWGEDADKFDGSRQPVMAIKGARVSDFGGRSLSVLSSSTVIVNPDIPEAYKLRGWFDSEGQALDGVSISDHRSGGAGGGNTNWKTLHEAKSENLGQGDKADYFSTVAAVVFLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDREFPNFKYRMILSANIADFQENQWVTCFQESAEAILGQNTMYLGELKEKNEQAFEEVFQNANFRSFTFRIRVKLETYNDESRIKATVMDVKPVDFRDYGRRLIANIRKNM", "text": "FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. SUBCELLULAR LOCATION: Nucleus Nucleus, PML body. SIMILARITY: Belongs to the replication factor A protein 1 family."}
{"protein": "MAGEGDHQDAAHNMGNHLPLLPADSEDEDDEIEMEVEDQDSKEARKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPEVMMILIPGQTLPLQLSHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQEFGIEVVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPISWEDQYSCKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKEDSLPANPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKASNLNLIGRPSTVHSWFPGYAWTIAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPETEDEISPDKVILCL", "text": "FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large- conductance calcium-activated potassium (BK) channels in excitatory neurons. Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (By similarity). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity). Plays a negative role in TLR4 signaling by interacting with TRAF6 and ECSIT, leading to inhibition of ECSIT ubiquitination, an important step of the signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CRBN family."}
{"protein": "MTAVLFLCFLLICFSFTPSLQNVSESEPLVRFKRSVNITKGDLNSWRTGTDPCNGKWFGIYCQKGQTVSGIHVTRLGLSGTINIEDLKDLPNLRTIRLDNNLLSGPLPPFFKLPGLKSLLLSNNSFSGEIADDFFKETPQLKRVFLDNNRLSGKIPASLMQLAGLEELHMQGNQFTGEIPPLTDGNKVLKSLDLSNNDLEGEIPITISDRKNLEMKFEGNQRLCGSPLNIECDEKPSSTGSGNEKNNTAKAIFMVILFLLIFLFVVAIITRWKKKRQPEFRMLGKDHLSDQESVEVRVPDSIKKPIDSSKKRSNAEGSSKKGSSHNGKGAGGGPGSGMGDIIMVNSEKGSFGLPDLMKAAAEVLGNGSLGSAYKAVMANGLSVVVKRIRDMNKLAREAFDTEMQRFGKLRHPNVLTPLAYHYRREEKLVVSEYMPKSSLLYVLHGDRGVYHSELTWATRLKIIQGVARGMDFLHEEFASYDLPHGNLKSSNVLLSETYEPLISDYAFLPLLQPNNASQALFAFKSPEFVQNQQVSPKSDVYCLGIIVLEVMTGKFPSQYLNTGKGGTDIVEWVQSSIAQHKEEELIDPEIASNTDSIKQMVELLRIGAACIASNPNERQNMKEIVRRIERVTL", "text": "FUNCTION: Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth (PubMed:23024212). Can phosphorylate ROPGEF1 in vitro (PubMed:23024212). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MWELVGLLLLILAYFFWVKSKTPGAKLPRSLPSLPLVGSLPFLPRRGHMHVNFFKLQEKYGPIYSLRLGTTTTVIIGHYQLAREVLIKKGKEFSGRPQMVTQSLLSDQGKGVAFADAGSSWHLHRKLVFSTFSLFKDGQKLEKLICQEAKSLCDMMLAHDKESIDLSTPIFMSVTNIICAICFNISYEKNDPKLTAIKTFTEGIVDATGDRNLVDIFPWLTIFPNKGLEVIKGYAKVRNEVLTGIFEKCREKFDSQSISSLTDILIQAKMNSDNNNSCEGRDPDVFSDRHILATVGDIFGAGIETTTTVLKWILAFLVHNPEVKKKIQKEIDQYVGFSRTPTFNDRSHLLMLEATIREVLRIRPVAPMLIPHKANVDSSIGEFTVPKDTHVVVNLWALHHDENEWDQPDQFMPERFLDPTGSHLITPTQSYLPFGAGPRSCIGEALARQELFVFTALLLQRFDLDVSDDKQLPRLEGDPKVVFLIDPFKVKITVRQAWMDAQAEVST", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16- alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17- alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates androgens, relevant for estriol synthesis. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane Microsome membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MTLLGSEHSLLIRSKFRSVLQLRLQQRRTQEQLANQGIIPPLKRPAEFHEQRKHLDSDKAKNSLKRKARNRCNSADLVNMHILQASTAERSIPTAQMKLKRARLADDLNEKIALRPGPLELVEKNILPVDSAVKEAIKGNQVSFSKSTDAFAFEEDSSSDGLSPDQTRSEDPQNSAGSPPDAKASDTPSTGSLGTNQDLASGSENDRNDSASQPSHQSDAGKQGLGPPSTPIAVHAAVKSKSLGDSKNRHKKPKDPKPKVKKLKYHQYIPPDQKAEKSPPPMDSAYARLLQQQQLFLQLQILSQQQQQQQHRFSYLGMHQAQLKEPNEQMVRNPNSSSTPLSNTPLSPVKNSFSGQTGVSSFKPGPLPPNLDDLKVSELRQQLRIRGLPVSGTKTALMDRLRPFQDCSGNPVPNFGDITTVTFPVTPNTLPNYQSSSSTSALSNGFYHFGSTSSSPPISPASSDLSVAGSLPDTFNDASPSFGLHPSPVHVCTEESLMSSLNGGSVPSELDGLDSEKDKMLVEKQKVINELTWKLQQEQRQVEELRMQLQKQKRNNCSEKKPLPFLAASIKQEEAVSSCPFASQVPVKRQSSSSECHPPACEAAQLQPLGNAHCVESSDQTNVLSSTFLSPQCSPQHSPLGAVKSPQHISLPPSPNNPHFLPSSSGAQGEGHRVSSPISSQVCTAQMAGLHSSDKVGPKFSIPSPTFSKSSSAISEVTQPPSYEDAVKQQMTRSQQMDELLDVLIESGEMPADAREDHSCLQKVPKIPRSSRSPTAVLTKPSASFEQASSGSQIPFDPYATDSDEHLEVLLNSQSPLGKMSDVTLLKIGSEEPHFDGIMDGFSGKAAEDLFNAHEILPGPLSPMQTQFSPSSVDSNGLQLSFTESPWETMEWLDLTPPNSTPGFSALTTSSPSIFNIDFLDVTDLNLNSSMDLHLQQW", "text": "FUNCTION: Smooth muscle cells (SM) and cardiac muscle cells-specific transcriptional factor which uses the canonical single or multiple CArG boxes DNA sequence. Acts as a cofactor of serum response factor (SRF) with the potential to modulate SRF-target genes. Plays a crucial role in cardiogenesis, urinary bladder development, and differentiation of the smooth muscle cell lineage (myogenesis) (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAAEEGQVIGCHTNDVWTVQLDKAKESNKLIVIDFTASWCPPCRMIAPIFNDLAKKFMSSAIFFKVDVDELQSVAKEFGVEAMPTFVFIKAGEVVDKLVGANKEDLQAKIVKHTGVTTA", "text": "FUNCTION: Thiol-disulfide oxidoreductase probably involved in the redox regulation of a number of cytosolic enzymes. Possesses insulin disulfide bonds reducing activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily."}
{"protein": "MALRAMRGIVNGAAPELPVPTGGPAVGAREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH", "text": "FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)- ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32001091). In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity). SUBCELLULAR LOCATION: Apical cell membrane Melanosome Cytoplasm Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MSSVFGSVHILAMIAIQLLLTHSVSSLNLTNAYLHHKCSNTQGKYKQGSAFEKNLNLVLSTITSIGNFRDGFRYTEEGEDPNNVFVMFQCRGDSYWSKCPPCISTAVSGLRRRCPRNKGAIIWYDQCLLKISSVASFNKIDYENDFYLSNPNNMSDRGLFNKETSALLEKLAYKASDRNNLDGKQLVLYAAGEKRIGTKKVYAMVQCTKDLIFTKCFECLEGILRKFPQCCDGKRGGRVFGTSCNFRYELYPFLRN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cysteine-rich repeat secretory protein family."}
{"protein": "MKRFLKAWRKTSLIKKITIGVVIGLFLGILVPKASAIGLLGQLFVGGLKAIAPLLVFTLVISALSQHREGGKTNMSTIIGLYITATFAAALIAVVVNYIFPLTLILKTPAKTDLLPPKGISEVFQSLLLKIVDNPIHAITEANYMSILFWAVIFGLAMRSSNQRTKDLMQTFADATSQVVKWIINLAPIGIMGLVFTSISENGIAILGDYGLLILVLVGTMLFVALVVNPIIAFVMMRKNPYPLVLRCLKDSGITAFFTRSSAANIPVNMRLCEDLGLDKDTYSVSIPLGAAINMAGAAITINILTLAAVNTLGITVDFPTAFLLSVVAAVSACGASGVTGGSLLLIPVACSLFGISNDVAMQVVGVGFIVGVIQDSCETALNSSTDVLFTAVAEKSVFGKK", "text": "FUNCTION: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family."}
{"protein": "MKLSRRHFMKANAVAAAAAVAGITIPIAVRAATEQSDAIHWDKAPCRFCGVGCGVLVGTQNGRIVASQGDPEAPVNRGLNCIKGYFLPKIMYGQDRLTQPLLRMRNGQFDKEGEFTPISWDKAFDIMAEKFKTALKEKGPNAIGMFGSGQSTIWEGYASAKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQTDAFVLWGSNMAEMHPILWSRITDRRLSNSNVTVAVLSTYQHRSFELADNGMVFTPQTDLAILNYIANYIIQNNAVNEAFFTRHVNLRRGVTDIGYGLRPTHPLEKAAKNPGSDASEPMSFEEYKAFVADYTLEKTVAISGVPADQLEALAKLYADPKKKVISYWTMGFNQHTRGVWANNLVYNIHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNEKHRAIAEKLWQLPTGTIPEKIGLHAVAQDRALKDGTLNAYWVMCNNNMQAGPNINQERMPGWRDPRNFIVVSDPYPTISALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGESKSDLWQVVSFAKRFTVEDVWPEELLAQKPAYRGKTLYDVLFANDVTTRFPLSELAENQLNDESREFGFYLQKGLFEEYAAFGRGHGHDLAPFDAYHKVRGLRWPVVDGKETQWRYSEGHDPYVKAGEAYRFYGKPDGKAVIFALPYEPAAEAPDEEYDLWFSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPQDAKARDLRRGEKVRIISRRGEVISVVETRGRNKPPRGLVYMPFFDAAQMTNVLTLDATDPLSKETDFKKCAVKLAKV", "text": "FUNCTION: Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily."}
{"protein": "MSIQTQDSQETLKSLSLIAAHSHISGLGLDENLQPKPSSQGMVGQLQARRAAGVILKMVQNGSIAGRAVLVAGPPSTGKTALAMGLSQSLGKDVPFTAIAGSEIFSLELSKTEALTQAFRKSIGIKIKEETELIEGEVVEIQIDRSITGGHKQGKLTIKTTDMETIYELGNKMIEGLTKEKVLAGDVISIDKASGKITKLGRSFARSRDYDAMGADTKFVQCPEGELQKRKTVVHTVSLHEIDVINSRTQGFLALFTGDTGEIRSEVRDQINTKVAEWKEEGKAEIVPGVLFIDEVHMLDIECFSFINRALEDEFAPIVIMATNRGISKTRGTNYKSPHGLPLDLLDRSIIITTKNYDASEIKTILTIRSTEEEVELSPEALDLLTNIGSETSLRYSSNLISVSQQIAQKRKSNTVEVKDVERAYLLFLDSARSVKFVQEFESQYIDDKGQVNISIGKDEDAMDTTA", "text": "FUNCTION: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes and is involved in DNA repair. Also involved in pre-rRNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RuvB family."}
{"protein": "MMVKFVLVDSASLLSVSDVAFVSCPALNHADKKCGILAFLAPSSLSCCTGSMCCPRNSVDSRRSRWLRPFSLRTVVATSSSGWTSFSVAFSARCFAFCCRRNSSRKATFCVISRVAASESTGSGCGGSLGTRRPTPALGPILMGEPTVPKNVLVRDAGAFGSTRKELMGFLRRWNVNLRWLPRNFAFSLFMAKGCRR", "text": "FUNCTION: Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host chloroplast envelope. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "ADVPGNYPLNTYGNMYYCTILGENEFCRKVCKVHGVKYGYCFNSHCWCEYLEAKDVSVWNAAKNYCKNPVGK", "text": "FUNCTION: Binds to sodium channels (Nav) and affects the channel activation process. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MGDLSCWTKVPGFTLTGELQYLKQVDDILRYGVRKRDRTGIGTLSLFGMQARYNLRNEFPLLTTKRVFWRAVVEELLWFIRGSTDSKELAAKDIHIWDIYGSSKFLNRNGFHKRHTGDLGPIYGFQWRHFGAEYKDCQSNYLQQGIDQLQTVIDTIKTNPESRRMIISSWNPKDIPLMVLPPCHTLCQFYVANGELSCQVYQRSGDMGLGVPFNIAGYALLTYIVAHVTGLKTGDLIHTMGDAHIYLNHIDALKVQLARSPKPFPCLKIIRNVTDINDFKWDDFQLDGYNPHPPLKMEMAL", "text": "FUNCTION: Catalyzes the reductive methylation of deoxyuridylate to thymidylate. SIMILARITY: Belongs to the thymidylate synthase family."}
{"protein": "MENGLCSIQARELDEFICDYLFPDTTFLTELRADIDSISAFLKERCFQGAAHPVRVSRVVMGGSYDEHTALKGKSEAKMVLFFNNLTSFEEQLKRRGEFVEEIQKHLCQLQQEKPFKVKFEVQSSEEPNSRSLSFKLSSPELQQEVEFDVQPAYDVLYELRNNTYAEPQFYNKVYAQLIHECTTLEKEGDFSICFTDLHQNFMRYRAPKLWNLIRLVKHWYQLCKEKLREPLPPQYALELLTVYVWEHSNKNQEKVTTAKNFRTFLELVAYYKNLRIYWTWYYDFRHQEVCAYLCRQLKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQTWMQSSCFRNCDMSFVPTWDLSPERQECAFQ", "text": "FUNCTION: Does not have 2'-5'-OAS activity, but can bind double- stranded RNA. SIMILARITY: Belongs to the 2-5A synthase family."}
{"protein": "MPVEEPLATLSSIPDSSADQAPPLIADEFTLDLPRIPSLELPLNVSTKHSSIQKAIKMCGGIEKVKEAFKEHGPIESQHGLQLYLNDDTDSDGSKSYFNEHPVIGKRVPFRDESVILKVTMPKGTLSKNNNSVKDSIKSLKDSNKLRVTPVSIVDNTIKFREMSDFQIKLDNVPSAREFKSSFGSLEWNNFKSFVNSVPDNDSQPQENIGNLILDRSVKIPSTDFQLPPPPKLSMVGFPLLYKYKANPFAKKKKNGVTEVKGTYIKNYQLFVHDLSDKTVIPSQAHEQVLYDFEVAKKTKVYPGTKSDSKFYESLEECLKILRELFARRPIWVKRHLDGIVPKKIHHTMKIALALISYRFTMGPWRNTYIKFGIDPRSSVEYAQYQTEYFKIERKLLSSPIVKKNVPKPPPLVFESDTPGGIDSRFKFDGKRIPWYLMLQIDLLIGEPNIAEVFHNVEYLDKANELTGWFKELDLVKIRRIVKYELGCMVQGNYEYNKYKLKYFKTMLFVKESMVPENKNSEEGMGVNTNKDADGDINMDAGSQMSSNAIEEDKGIAAGDDFDDNGAITEEPDDAALENEEMDTDQNLKVPASIDDDVDDVDADEEEQESFDVKTASFQDIINKIAKLDPKTAETMKSELKGFVDEVDL", "text": "FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Participates in the interconnection of tauA with tauB via its contacts with TFC3 and TFC6. Serves as a scaffold critical for tauA-DNA spatial configuration and tauB-DNA stability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIIC subunit 5 family."}
{"protein": "MGSVSNQQFAGGCAKAAEEAPEEAPEDAARAADEPQLLHGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGPGGVFCIGSERRPKGKSMQKRRSKGDRCYNCGGLDHHAKECKLPPQPKKCHFCQSISHMVASCPLKAQQGPSAQGKPTYFREEEEEIHSPTLLPEAQN", "text": "FUNCTION: RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up- regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits TUT4 and TUT7 uridylyltransferases (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). This results in the terminal uridylation of target pre-miRNAs (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity). SUBCELLULAR LOCATION: Cytoplasm Rough endoplasmic reticulum Cytoplasm, P-body Cytoplasm, Stress granule Nucleus, nucleolus Note=Predominantly cytoplasmic (PubMed:22118463). In the cytoplasm, localizes to peri-endoplasmic reticulum regions and detected in the microsomal fraction derived from rough endoplasmic reticulum (RER) following subcellular fractionation. May be bound to the cytosolic surface of RER on which ER-associated mRNAs are translated (By similarity). Shuttle from the nucleus to the cytoplasm requires RNA-binding (PubMed:17617744). Nucleolar localization is observed in 10-15% of the nuclei in differentiated myotubes (By similarity). SIMILARITY: Belongs to the lin-28 family."}
{"protein": "MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI", "text": "FUNCTION: Repressor of the mexAB-oprM multidrug resistance operon. Also represses its own expression. Many variants lead to increased expression of the mexAB-oprM operon."}
{"protein": "KKWGWLAWVDPAYEFIKGFGKGAIKEGNKDKWKNI", "text": "FUNCTION: Kills Lactococci."}
{"protein": "MARSLLLPLQILLLSLALETAGEEAQGDKIIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVHLGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVKKVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKVYKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQPNDPGVYTQVCKFTKWINDTMKKHR", "text": "FUNCTION: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines. SUBCELLULAR LOCATION: Secreted Note=In ovarian carcinoma, secreted and also observed at the apical membrane and in cytoplasm at the invasive front. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily."}
{"protein": "MAAPEAWRARSCWFCEVAAATTMEATSREAAPAKSSASGPNAPPALFELCGRAVSAHMGVLESGVWALPGPILQSILPLLNIYYLERIEETALKKGLSTQAIWRRLWDELMKTRPSSLESVTCWRAKFMEAFFSHVLRGTIDVSSDRRLCDQRFSPLLHSSRHVRQLTICNMLQGATELVAEPNRRVLETLASSLHTLKFRHLLFSDVAAQQSLRQLLHQLIHHGAVSQVSLYSWPVPESALFILILTMSAGFWQPGPGGPPCRLCGEASRGRAPSRDEGSLLLGSRRPRRDAAERCAAALMASRRKSEAKQMPRAAPATRVTRRSTQESLTAGGTDLKRELHPPATSHEAPGTKRSPSAPAATSSASSSTSSYKRAPASSAPQPKPLKRFKRAAGKKGARTRQGPGAESEDLYDFVFIVAGEKEDGEEMEIGEVACGALDGSDPSCLGLPALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWVSLESLTLSYNGLGSNIFRLLDSLRALSGQAGCRLRALHLSDLFSPLPILELTRAIVRALPLLRVLSIRVDHPSQRDNPGVPGNAGPPSHIIGDEEIPENCLEQLEMGFPRGAQPAPLLCSVLKASGSLQQLSLDSATFASPQDFGLVLQTLKEYNLALKRLSFHDMNLADCQSEVLFLLQNLTLQEITFSFCRLFEKRPAQFLPEMVAAMKGNSTLKGLRLPGNRLGNAGLLALADVFSEDSSSSLCQLDISSNCIKPDGLLEFAKRLERWGRGAFGHLRLFQNWLDQDAVTAREAIRRLRATCHVVSDSWDSSQAFADYVSTM", "text": "FUNCTION: Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins."}
{"protein": "MAPPAPGAASGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKLSSPDREVERDVFLYRAYIAQRKYGVVLDEIKPSSAPELQAVRMFADYLATENRRDAIVVELDREMSRSVDVTNTTFLLMAASVYFHDQNPDAALRTLHQGDSLECMAMTIQILLKLDRLDLARKELKKMQDQDEDATLTQLATAWVNLAVGGEKLQEAYYIFQELADKCSPTLLLLNGQAACHSAQGRWETAEGVLQEALDKDSGHPETLINLIVLSQHLGKPPEVTNRYLSQLKDAHRTHPFIKEYQAKENDFDRLALQYAPSA", "text": "FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. SIMILARITY: Belongs to the COPE family."}
{"protein": "MSHQVKGLKEEARGGVKGRVKSGSPHTGDRLGRRSSSKRALKAEGTPGRRGAQRSQKERAGGSPSPGSPRRKQTGRRRHREELGEQERGEAERTCEGRRKRDERASFQERTAAPKREKEIPRREEKSKRQKKPRSSSLASSASGGESLSEEELAQILEQVEEKKKLIATMRSKPWPMAKKLTELREAQEFVEKYEGALGKGKGKQLYAYKMLMAKKWVKFKRDFDNFKTQCIPWEMKIKDIESHFGSSVASYFIFLRWMYGVNLVLFGLIFGLVIIPEVLMGMPYGSIPRKTVPRAEEEKAMDFSVLWDFEGYIKYSALFYGYYNNQRTIGWLRYRLPMAYFMVGVSVFGYSLIIVIRSMASNTQGSTGEGESDNFTFSFKMFTSWDYLIGNSETADNKYASITTSFKESIVDEQESNKEENIHLTRFLRVLANFLIICCLCGSGYLIYFVVKRSQQFSKMQNVSWYERNEVEIVMSLLGMFCPPLFETIAALENYHPRTGLKWQLGRIFALFLGNLYTFLLALMDDVHLKLANEETIKNITHWTLFNYYNSSGWNESVPRPPLHPADVPRGSCWETAVGIEFMRLTVSDMLVTYITILLGDFLRACFVRFMNYCWCWDLEAGFPSYAEFDISGNVLGLIFNQGMIWMGSFYAPGLVGINVLRLLTSMYFQCWAVMSSNVPHERVFKASRSNNFYMGLLLLVLFLSLLPVAYTIMSLPPSFDCGPFSGKNRMYDVLQETIENDFPTFLGKIFAFLANPGLIIPAILLMFLAIYYLNSVSKSLSRANAQLRKKIQVLREVEKSHKSVKGKATARDSEDTPKSSSKNATQLQLTKEETTPPSASQSQAMDKKAQGPGTSNSASRTTLPASGHLPISRPPGIGPDSGHAPSQTHPWRSASGKSAQRPPH", "text": "FUNCTION: Probable ion channel required for the normal function of cochlear hair cells (PubMed:11850618). Component of the hair cell's mechanotransduction (MET) machinery. Involved in mechanosensitive responses of the hair cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localized to the stereocilia of the cochlear hair cells. SIMILARITY: Belongs to the TMC family."}
{"protein": "MTETELFKEGLNLMFSGMGFVIIFLLILIWAIGIVSKLINTFFPEPIPVAQAKKTVTPTQSAVVDDIERLRPVIVAAIAHHRRTQGLN", "text": "FUNCTION: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the OadG family."}
{"protein": "MLGGGSVDGERDTDDDAAGAVAAPPAIDFPAEVSDPKYDESDVPAELQVFKEPLQQPTFPFLVANQLLLVSLLEHLSHVHEPNPLHSKQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSAKERVRQDPCQDNSYMQKIRSREIALEAQTSRYLNEFEELAILGKGGYGRVYKVRNKLDGQHYAIKKILIKSATKTDCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVLQPQDRVPIQLPSLEVLSEHEGDRNQGGVKDNESSSSIIFAELTPEKENPLAESDVKNENNNLVSYRANLVIRSSSESESSIELQEDGLNESPLRPVVKHQLPLGHSSDVEGNFTSTDESSEDNLNLLGQTEARYHLMLHIQMQLCELSLWDWIAERNNRSRECVDEAACPYVMASVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACADIIQKSADWTNRNGKGTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVILLELFQPFGTEMERATVLTGVRTGRIPESLSKRCPVQAKYIQLLTGRNAAQRPSALQLLQSELFQTTGNVNLTLQMKIMEQEKEIEELKKQLSLLSQDKGLKR", "text": "FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions. Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as heme deficiency, oxidative stress, osmotic shock, mitochondrial dysfunction and heat shock. EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming. Acts as a key sensor of heme-deficiency: in normal conditions, binds hemin via a cysteine thiolate and histidine nitrogenous coordination, leading to inhibit the protein kinase activity. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell: heme depletion relieves inhibition and stimulates kinase activity, activating the ISR. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. It thereby plays an essential protective role for RBC survival in anemias of iron deficiency. Also activates the ISR in response to mitochondrial dysfunction: HRI/EIF2AK1 protein kinase activity is activated upon binding to the processed form of DELE1 (S-DELE1), thereby promoting the ATF4-mediated reprogramming (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily."}
{"protein": "MAIKYGRPIELREVSRRDGAAASPALDLAIRPRRNRKAEWARRMVRENVLTTDDLIWPLFLIDGNNKREQIASMPGVERLSVDQAVREAERAMKLTIPCIALFPYTDPSLRDEEGSEACNPNNLVCQAVRAIKKEFPEIGVLCDVALDPFTSHGHDGLIADGAILNDETVAVLVRQALVQAEAGCDIIAPSDMMDGRVAAIREGLDQAGLIDVQIMAYAAKYASAFYGPFRDAIGSAKTLTGDKRTYQMDSANTDEALREVELDISEGADMVMVKPGMPYLDVVRRVKDTFAMPTFAYQVSGEYAMIAAAAGNGWLDGDRAMMESLLAFKRAGADGVLSYFAPKAAEKLRTQG", "text": "FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. Required for nodule development. SIMILARITY: Belongs to the ALAD family."}
{"protein": "TDAVADGEHAISGVVDS", "text": "FUNCTION: May act as an antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Frog skin active peptide (FSAP) family. Septenin subfamily."}
{"protein": "EHTYGEVNQLGGVFVNGRPLPNAIRLRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPNVVKHIRDYKQGDPGIFAWEIRDRLLADGVCDKYNVPSVSSISRILRNKIGSLSQPGGPYDGGKQPPPQPALPYNPLYQYPYPGPMDPRAAKMGADPPGPVPAAHVGLPRSWPSAHSVTNILG", "text": "FUNCTION: This protein is a transcriptional activator. It may play a role in the formation of segmented structures of the embryo. May play an important role in the normal development of the vertebral column (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MIGVCGFQWSLSFSTMYTVSLPHGPFLGSRAQEAFVGFSVLGLTLLFSKLFYNAYLHPLRKFPGPLLARLSRLYYSYYRSTGQLEWKTLELHKKYGSVVRIAPNELSFNAGTAWDDIYGHTTKRRSGRRLQKEAFFYLGAVAPNGEKNLGASSDEDHSRIRGVLSSAFSEKAVFAQEDLLMRHIGFMVERIRSLNGIPTDAVRWLHHCTFDITTDLSLGASAKTLACDEWSPLAHLMFEGIKEGITAVEILRFAPFKYQAFSLLIKAFGKARLEAFQAAINQAHIRMAQATTDKEDKKPDFMSYIIKANKTSKALTPSEITANVALLLDVGSETTASLLAGCLFYLTKTPHILEKLTSMIRKDFQTPQEINSKNLAQNSYLTAVLNEALRIYPPVAGATPRVTPPEGSQIDGRYVPGNISVAVNQVAMNRSPKNFTNPDQFVPGRWLGDGCFPDDQLQLCQPFSHGPRACQGRNLAWAEMRLIMGHLLWNFDVELSSESENWNSQKTWFIWDKPDLMIRFKSREGQ", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker (PubMed:22870285). The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H (PubMed:17360612). The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-2,10(14)-diene-8-beta-ol (PubMed:22870285). The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C- 16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol (PubMed:22870285). The dioxygenase fc-dox then catalyzes the 16- oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al) (PubMed:21299202, PubMed:22870285). The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol (PubMed:21299202, PubMed:22870285). The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O- glycosyltransferase PaGT (PubMed:22870285). Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O- methyltransferase PaMT to yield fusicoccin P (PubMed:22870285). Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT (PubMed:22287087). Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2 (PubMed:22870285). Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A (PubMed:22870285). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MPKSVIIPAGSSAPLAPFVPGTLADGVVYVSGTLAFDQHNNVLFADDPKAQTRHVLATIRKVIETAGGTMADVTFNSIFITDWKNYAAINEIYAEFFPGDKPARFCIQCGLVKPDALVEIATIAHIAK", "text": "FUNCTION: Involved in pyrimidine catabolism. Catalyzes the deamination of 3-aminoacrylate to malonic semialdehyde, a reaction that can also occur spontaneously. RutC may facilitate the reaction and modulate the metabolic fitness, rather than catalyzing essential functions. SIMILARITY: Belongs to the RutC family."}
{"protein": "MENTKTNASSSGMSSSSSFSVSYAEEMLLADEVSKINSMSILGPNQLKLCTQLVLSNGAAPVVLSLVSKEKKSILSRILPKIGQRLYVHHSAIYLLYMPNILKSSSGSITLKLFDEATEELVDVDTDHDATQACIFAGRYPRSILAKDAAKGHDLKLVVHAVASTKANSAVGVLYPIWEDELSRKQILERGADFLKFPIAETEPVRDLLNAGKLTDFVLDRTRLGVGSKNDPSPVLLEPRAKITGKAKTVFIPEGPSVPNTTISGMAPTVRIDAGSPKGLGVPKGFTYESFIKDEILPDH", "text": "FUNCTION: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma Note=Assembles into long tubular structures at the surface of the infected protoplast. SIMILARITY: Belongs to the alfamovirus movement protein family."}
{"protein": "MFARAAAIASVPVMREGTALDAIDSRIIHCKGALARLKELERVVRLLTDSMAGNSAERTIIPLMSYVLALCQGPLFGVSPTLRKRYELLSQMRLVKLTEVNAAASLGAVDLWSRWPADEDDASAVRSKFYDETLHGRILEHLLHTTRNCHALYQRRHKLLLAERDACRTAETQEWNDLYSLAVDDFLVPSEITLGLELAVLITDRDTDTTDMAYQKLNIQVLGMLLEYFNGVAMPTINQYYLELQRAVRNKGINQNNILTSLPFWAHTLHRIFAMLLRAKYLLDIIQSVLRLAYLPNKTHFSHPTVQLASPNLYLFRNVLEKLDEICCGTTVLSARVTEYISPFLQQGVTHRLTYDKVVHLYKEAVRPTVSSLTEAIDLMSNLLKSWEASCSAEHISRLQTLSEDDVSTLSAVEDKFLIDKSLYEEGQKRKQENKKSPAANSTSKKQAVTLQRRPSNRIVSTNASPLRQQVIANGEKRISTAPPMRRRSLSLQRVSPSPDPDANRRSNSLQFSSTNQILLQSSVREALSRYQSRHANIERPLSTPPGTFPYHAFASSMVDEESRRIASLSLAEGNGPAAIKVMANMASEYEDTSRESSLSGCCNYQTYANQVLAQPQLAGSFPTVPLVKKVRFTGVPPPTEDEDPKPKRKGWYKKPAVLHYPTPSQSMIQKNKQRHEGYVFRTSLREQQREKHKQPGRRFAAFLDHVKDTNTLSGHKAGKIKSKLTR", "text": "FUNCTION: GLC7 phosphatase-regulatory protein involved in GLC7 subcellular redistribution and chromosome segregation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GIP4 family."}
{"protein": "MSRSLALVYLSLLCLQTHLSISVTVPIPSVNGEIDAMLNRNGVIGEEEGEEMMPSEISRRVMMMRKQYISYETLRRDMVPCQKPGASYYACRSGQANAYNRGCSVITRCARDTNDIKT", "text": "FUNCTION: Cell signaling peptide that may regulate plant stress, growth, and development. Mediates a rapid alkalinization of extracellular space by mediating a transient increase in the cytoplasmic Ca(2+) concentration leading to a calcium-dependent signaling events through a cell surface receptor and a concomitant activation of some intracellular mitogen-activated protein kinases (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant rapid alkalinization factor (RALF) family."}
{"protein": "MDFSSSNGSEDTELSQAQIHLYKHVYNFVSSMALKSAMELGIADVIHSHGKPITLPELATALNLRPSKIGVLHRFLRLLTHNGFFAKTTVSRGEGAEEETAYGLTPPSKLLVKSNSTCLAPIVKGALHPSSLDMWRSSKKWFLEDNEELTLFESATGESFWEFLNKETESDTLSMFQEAMAADSHMFKLALKECKHVFEGLGSLVDVAGGRGGVTKLIREAFPHVKCTVFDQPQVVANLTGDENLNFVGGDMFKSVPPADAVLLKWVLHDWNDELSLKILKNCKEAISGRGKEGKVIIIDISIDETSDDRELTELKLDYDLVMLTMFNGKEREKKEWEKLIYDAGFSSYKITPICGFKSLIEVFP", "text": "FUNCTION: 2-hydroxyisoflavanone 4'-O-methyltransferase involved in the biosynthesis of formononetin. Can use 2,7,4'-trihydroxyisoflavanone as substrate, but not daidzein. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
{"protein": "MKVYFENYSYYPALRTRSAEMTGLNNLSYENKKKILPLISLGKWPRSEEIQVSLDKSLEVMSNLPFILDVTKDNSHHCASSFELLSPENGFKNWIEFCSRNDNIIPVVQMPDSAKLRDISIQARVLEELKGSIAFRIRNLNTDINKTLTSLVSMNSPENAIVFIDLGYIRGNVSAITAAAINSINQIRTEIPEAIISVLATSFPSSVTNFCRENGQSGYIDVIERELHQNIGGSDVAIYGDHGSIHSVVYDNIIGRYVPRIDIALNDSWYFERRPGMNKEGFIEAAKSILAEYPHYQREDSWGAAMIRNAAIGDIAGMGSPAKWIAVRVNLHLNKQIELSEALQYGFDHDEEDLI", "text": "FUNCTION: The presence of this protein prevents gop protein from killing E.coli."}
{"protein": "MNREVSERIHILFFPFMAQGHMIPILDMAKLFSRRGAKSTLLTTPINAKIFEKPIEAFKNQNPDLEIGIKIFNFPCVELGLPEGCENADFINSYQKSDSGDLFLKFLFSTKYMKQQLESFIETTKPSALVADMFFPWATESAEKLGVPRLVFHGTSFFSLCCSYNMRIHKPHKKVATSSTPFVIPGLPGDIVITEDQANVAKEETPMGKFMKEVRESETNSFGVLVNSFYELESAYADFYRSFVAKRAWHIGPLSLSNRELGEKARRGKKANIDEQECLKWLDSKTPGSVVYLSFGSGTNFTNDQLLEIAFGLEGSGQSFIWVVRKNENQGDNEEWLPEGFKERTTGKGLIIPGWAPQVLILDHKAIGGFVTHCGWNSAIEGIAAGLPMVTWPMGAEQFYNEKLLTKVLRIGVNVGATELVKKGKLISRAQVEKAVREVIGGEKAEERRLWAKKLGEMAKAAVEEGGSSYNDVNKFMEELNGRK", "text": "FUNCTION: Possesses quercetin 3-O-glucosyltransferase activity in vitro. Involved in stress or defense responses. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQPFANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
{"protein": "MAQRLTSAFLNWREHITPASKTSDFENTGMISPEEFVLAGDYLVSKFPTWSWECGDRIRGFLPKDKQYLVTRHVFCVQRNINIGVNEEWVDIETDDTRNKDDDQDDDAISSIHSDTSDIASAERLKGQSKELSDSGPLPLKDEEDDDQMVSPVIKEDEGRYYDLYIVYDKYYRTPRLFLRGWNAGGQLLTMKDIYEDVSGEHAGKTVTMEPFPHYHSHNTMASVHPCKHASVLLKLIKQHRERNDPIRVDQYMVLFLKFVSTMLPYFEIDYTIQA", "text": "FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C- terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Plays a role in meiosis and sporulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ATG3 family."}
{"protein": "MKLRNVEPRFLKAYNILMDKFGLFPFTYDMAEKVLKDNYENVNEVLSKLADAGLLEKTAKKEDKRKKIYKIKPLTTEKIEKVSKDKLIGLLKQGADLIRTQVDYKVLLLFLFFKAISDKYLLKVEELKKEFEDLDEEDIYVLANEEILELYDVEGKKLYVWHEVANNPEDFINALNKIVEMNKEKLSGLDELIKRTGLPTLFENENRHIVQHLINLFSRADFSEASYDILGDAYEWTLNYFAPTKAKEGEVYTPIEVSKLIAHLVEPKDDEVILDPACGSGSMLIEQYRFAGSNPNIVLVGQERNDVTAVLAKLNFILHGINLKDAKVFIGDSLLNPKFESFIXEVKGTGKADKVVANPPWNQDGYDENTLKVNEKYKDIYMYGFPNKNSADWAWVQLINYYTEKKAGIVLDSGALFRGGKEKTIRKRFVDDDLIEAVVLLPEKLFYNCPAPGIILILNKNKPEERKGKILFINASNEYIKHPEVKKLNKLSDENIEKIAKAYKEFKDVDGFCKVVDIEEIRKNDYNLNVSLYISPIEEDEDVDLGEVYEELNKLHNEYLEKFEVVKGYLEEINGLIK", "text": "FUNCTION: The subtype gamma methyltransferase (M) subunit of a type I restriction enzyme. The M and S subunits together form a methyltransferase (MTase) that methylates A-2 on the top and A-3 on the bottom strand of the sequence 5'-GAYN(5)GTAA-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage. SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MATTTPPETKSAAWWNYFFLYDGSKVKGEGDPTRAGICYFYPPQTLLDQQELLCGQLAGVVRCLWDLSGTPPMLIRMRNLKFAIRADGDYLWALGCGVEISDASCRQFLDQLIGFFHFYMGPVSLAYKSHPQEELSLQWDTSITQVLRSTSESHRIFNALWNLDRTKVEPLLLLKAALILQTCQRSPHVLAGCILYKGLIVNSQLLPSLTAKVLLHQTVPADQRLPGAGAAPQETGAALPPDVQITSVFLSEEEVASLHEFPVEHETRLQGSSVQYPPWDQSSPTQAEDAWASAAIPEPTPHDGACPSGSGADERLPRLEQECAGPTGLCTTACGQGSGLSSRLQKELCLSREELDSSEMHVSEAQEAFPPLPALGDLETLHSSHSAPTLPEDTAICSCLHPCPLERLPESGRLGQLADLPLTNGQTQVPGTDPLPSSMPVALPPQHPVGVEPSVEPYGNGAQESHSALPRSSRSPDSPGPSPSADRTGFKPSPSGRHAGLVPMNLYTHSVNGLVLSLLAEETLLSDTAAIEEVYHSSLASLNGLEVHLKETLPRDEASLTSSTYNFLHYDRIQSVLSANLPLVTAPQDRRFLQAVNLMHSDFALLPMLYEMTIRNASTAVYACSSPAQETYFQQLAPTARSSGFPNPQDCAFSLAGKAKQKLLKHGVNLL", "text": "FUNCTION: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38."}
{"protein": "MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPENAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL", "text": "FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11809832). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:25208553). Required for the centralization of the mitotic spindle and symmetric division of zygotes (PubMed:25208553). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (By similarity). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration (PubMed:15649475). SUBCELLULAR LOCATION: Nucleus matrix Cytoplasm, cytoskeleton Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium Cell projection, growth cone Cell projection, axon Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
{"protein": "MDVDSASLSPSSRLSVVCSASAEFSSSSSDSSNFSEGSPPESRRNSVNESVIKDEHYWERRRRNNDASRRSREKRRQNDLAMEEKIMLLSAENERLKSQLGTTPIPQPSVTEPPTSLIIPQVAKNLFPAGPIASLQASSMLTVPLLQAASHIPSMLQLCQLQPTTIQSPVYASTQQPASTSASSLFSSSSSSAFHPFRPSESAQQSFPSSSVIVKIERRSPDSSTDVNMPQPQLQPGSSVIQQIGQPAPSGTPQPVIQAVQQGPSLLSALLSQRRPSPTVPQSRTEHISGLNSPPRHTGNKSDCESVSSSASFSPSHSSEDHSNYSNKSPQYVDRRRRNNEAAKRCRANRRAVFEYRSRRVQLLEGENEDLRTQIETLKAEIAHFKSVLAQRASVVTALHP", "text": "FUNCTION: Acts as a transcription factor that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many promoters (PubMed:16310763, PubMed:21502138). Involved in the development of the excretory duct cell, by positively modulating embryonic transcription of putative transcription factor lin-48, acting in concert with cell death specification protein ces-2 (PubMed:16310763). Negatively modulates expression of key autophagy- related genes, bec-1/ATG6 and lgg-1/ATG8, and may link together autophagy and apoptosis during development (PubMed:21502138). Positively modulates expression of neuropeptide pigment dispersing factor homologs pdf-1 and pdf-2 (PubMed:19686386). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGLLEGNVRNSLWRPSPFKCPTCRKETSATGVNSLQVNYSLKGIVEKYNKIKISPKMPVCKEHLGQPLNIFCVTDMQLICGVCATRGSHTKHVFSSIEDAYTQERDAFEFLFQSFETWRRGDALSRLDTLETNKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQTYDPEINKLNSILQEQRMAFNIAEAFKDVSEPIIFLQQMQEFREKIKVIKETPLPPSNLPTSPLMKNFDTSQWEDIKLVDVDKLSLPQDTGVLTSRSPWHPCLLLMAVVLLGLLVFFGPTVFLEWSPLEELATWKDCLSSFNSYLTKSADFVEQSVFYWEQMTDGLFVFSERVKNVSLVALNNVAEFVCKYKLL", "text": "FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER- associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress- induced autophagy, and may act as a tumor suppressor. Also plays a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum."}
{"protein": "MQRQIKLKNWLQTVYPERDFDLTFAAADADFRRYFRATFSDGSSVVCMDAPPDKMSVAPYLKVQKLFDMVNVPQVLHADTDLGFVVLNDLGNTTFLTAMLQEQGETAHKALLLEAIGELVELQKASREGVLPEYDRETMLREINLFPEWFVAKELGRELTFKQRQLWQQTVDTLLPPLLAQPKVYVHRDFIVRNLMLTRGRPGVLDFQDALYGPISYDLVSLLRDAFIEWEEEFVLDLVIRYWEKARAAGLPVPEAFDEFYRWFEWMGVQRHLKVAGIFARLYYRDGKDKYRPEIPRFLNYLRRVSRRYAELAPLYALLVELVGDEELETGFTF", "text": "FUNCTION: Sugar kinase that catalyzes the ATP-dependent phosphorylation of N-acetylmuramate (MurNAc) and N-acetylglucosamine (GlcNAc) at its C1 hydroxyl group, leading to MurNAc alpha-1P and GlcNAc alpha-1P, respectively (By similarity). Is likely involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc (PubMed:23831760). Is able to complement the fosfomycin sensitivity phenotype of a P.putida mutant lacking amgK (PubMed:23831760). SIMILARITY: Belongs to the kinase AmgK family."}
{"protein": "MVAGKRTGAAKGSRHNKKYWRKGTNIDDIEDSIHIKSRQAATGGVISEMKDEDLFIVDRTATANKPVVPKLTKKQQAALEKITKNITQEHVTLPKPSTTSKILKKPAKLPRGNAILALKKGPKAAAPAAKKKNFDVWTTDLTPKIPKSKLENQEAAEHFLKVVKKKQPKTPGKSITSLLPAVQIAEGGASYNPESAEYQEYVAKIAGEEQKLIDHEAKIKAGIEPQWEKVTTEHERFLEMAEGLRIHPKYGKDDEEEEEAGNSEKSMKTGGEAEPKSQRVECDRMTKEQKKKKAKAQKLDKEEKRRLEEKAKEQDSHNVYRTKQLHKELDEEEKQRHEESEVRKKEKLINKLTKRQQLGKGKFVDAEDPFLLQEELTGNLRQLKPQGHVLDDRMKSLQRRNMLPIGGDKEKRRIKNRLKSKVVEKRSAKNIVKGSRVI", "text": "FUNCTION: May play a role in ribosome biogenesis, being required for integration of the 5S RNP into the ribosomal large subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the NOP53 family."}
{"protein": "MTTQYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKKHGDLAAVAPLPRAHFTKPNIVIKPNANSRPTGDTTGYLANPKEV", "text": "FUNCTION: Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds."}
{"protein": "MPEPSISALSFTSFVTNDDKLFEETFNFYTKLGFHATRSYVKDNRSDFELTGISTDSIKEIWLESFPLSEVVETSAGRELRKPLQESVGYQSEALLGYSPYQSDGVVIKLRLSNHDLQKNKDLPGEVTFFTASIDKLRAKLIEIGAEIIPSEIDLVEFSTKDPMGDVISFSSYPSLSSKKITSPDFFLHPKKEVRSQESIVEQVKSEEGKKKIAIITSGGDAPGMNAAVRAVTRAGIFYGCKVYACYEGYTGLVKGGDMLKELQWQDVRGLLSIGGTIIGTARSKEFRERWGRLQACYNMVSNGIDALVVCGGDGSLTGADLFRNEWPELIKELLGEGKITKEQYETHRNLTIVGLVGSIDNDMCGTDSTIGAYSSLERIIELVDYIDATAASHSRAFVVEVMGRHCGWLGLMSGIATGADYIFIPERPPSETNWKDDLKKVCLRHREKGRRKTTVIVAEGAIDDQLNPITSEEVKDVLVEIGLDTRITRLGHVQRGGAPCAFDRFLATVQGVDAVRAVLESTPAIPSPVISILENKIVRQPLVESVAQTKTVSDAIEAKDFDKALKLRDQEFATSYESFLSVSKYDDGSYLVPESSRLNIAIIHVGAPTSALNPATRVATLNSLAKGHRVFAIRNGFAGLIRHGAVRELNWIDVEDWHNTGGSEIGTNRSLPSDDMGTVAYYFQQYKFDGLIIIGGFEAFTALYQLDAARAQYPIFNIPMCCLPATVSNNVPGTEYSLGSDTCLNTLSGYCDAVKQSASASRRRTFVVEVQGGYSGYLASYAGLITGALAVYTPENPINLQTVQEDIELLTRTYEEDDGKNRSGKIFIHNEKASKVYTTDLIAAIIGEAGKGRFESRTAVPGHVQQGKSPSSIDRVNACRLAIKCCNFIEDANFQVKHNANLSADERHLRFFYDDGVKTSAVSGKSSVIDDNTSVVIGIQGSEVTFTPVKQLWEKETHHKWRKGKNVHWEQLNIVSDLLSGRLSIRTT", "text": "FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Involved in the modulation of glucose- induced microautophagy of peroxisomes independent of its ability to metabolize glucose intermediates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily."}
{"protein": "MAQQWSLQRLAGRHPQDSYEDSTQSSIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSVWMIFVVIASVFTNGLVLAATMKFKKLRHPLNWILVNLAVADLAETVIASTISVVNQVYGYFVLGHPMCVLEGYTVSLCGITGLWSLAIISWERWMVVCKPFGNVRFDAKLAIVGIAFSWIWAAVWTAPPIFGWSRYWPHGLKTSCGPDVFSGSSYPGVQSYMIVLMVTCCITPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVLAFCFCWGPYAFFACFAAANPGYPFHPLMAALPAFFAKSATIYNPVIYVFMNRQFRNCILQLFGKKVDDGSELSSASKTEVSSVSSVSPA", "text": "FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MPRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGLDKVFGTITRETDLKELLSGLFDNFSQDYQALLSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYVSEDVIPEYRKLALSPKQLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQTIPVIIVTSCDCKMFDDKDFIYCVASMEGKTPIVYRVPFIDSYFTGVGDLFSALLLDRVYKILSNPTTTLKFEDQVNNVLNVIQKVLKITRSYASGKMKAKMGSALEMKEMELRLIESRDIYETINIHQTDYIYARL", "text": "FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pyridoxine kinase family."}
{"protein": "MAREVKLTKAGYERLMQQLERERERLQEATKILQELMESSDDYDDSGLEAAKQEKARIEARIDSLEDILSRAVILEEGSGEVIGLGSVVELEDPLSGERLSVQVVSPAEANVLDTPMKISDASPMGKALLGHRVGDVLSLDTPKGRREFRVVAIHG", "text": "FUNCTION: Inhibits all catalytic activities of RNA polymerase (RNAP) by partially occluding its substrate-binding site and preventing NTP binding. SIMILARITY: Belongs to the GreA/GreB family."}
{"protein": "MTLLSSLGRASRSAPLASKLLLLGTLSGGSIVAYADANEEANKKEEHKKKKVVVLGTGWAGISFLKDLDITSYDVQVVSPQNYFAFTPLLPSVTCGTVEARSIVESVRNITKKKNGEIELWEADCFKIDHVNQKVHCRPVFKDDPEASQEFSLGYDYLIVAVGAQVNTFGTPGVLENCHFLKEVEDAQRIRRGVIDCFEKAILPGLTEEQRRRKLHFVIVGGGPTGVEFAAELHDFIIEDITKIYPSVKELVKITLIQSGDHILNTFDERISSFAEQKFTRDGIDVQTGMRVMSVTDKDITVKVKSSGELVSIPHGLILWSTGVGTRPVISDFMEQVGQGGRRAVATNEWLQVTGCENVYAVGDCASIAQRKILGDIANIFKAADADNSGTLTMEELEGVVDDIIVRYPQVELYLKSKHMRHINDLLADSEGNARKEVDIEAFKLALSEADSQMKTLPATAQVAAQQGAYLAKCFNRMEQCKELPEGPKRFRTGGHHQFRPFQYKHFGQFAPLGGDQAAAELPGDWVSAGKSAQWLWYSVYASKQVSWRTRALVVSDWTRRYIFGRDSSRI", "text": "FUNCTION: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane (By similarity). Calcium-dependent NAD(P)H dehydrogenase. Binds calcium ions. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Peroxisome. SIMILARITY: Belongs to the NADH dehydrogenase family."}
{"protein": "MGGLEPCSRLLLLPLLLAVGGLRPVQAQAQSDCSCSTVSPGVLAGIVLGDLVLTVLIALAVYFLGRLVPRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNTQRPYYK", "text": "FUNCTION: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). Also has an inhibitory role in some cells (By similarity). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte- derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allosimulatory ability (By similarity). Negatively regulates B cell proliferation (By similarity). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the TYROBP family."}
{"protein": "MWIYILVGIICLLAGLAGGFFIARRYMMSYLKNNPPINEQMLQMMMAQMGQKPSQKKINQMMSAMNKQQEKEKPKKAKK", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0154 family."}
{"protein": "MSPDKPFRIMGDVGELHILPPKYAYEVRNNEKLSFTMAAFKWFYAHLPGFEGFREGTNESHIMKLVARHQLTHQLTLVTGAVSEECALVLKDVYTDSPEWHDITAKDANMKLMARITSRVFLGKEMCRNPQWLRITSTYAVIAFRAVEELRLWPSWLRPVVQWFMPHCTQSRALVQEARDLINPLLERRREEKAEAERTGEKVTYNDAVEWLDDLAREKGVGYDPACAQLSLSVAALHSTTDFFTQVMFDIAQNPELIEPLREEIIAVLGKQGWSKNSLYNLKLMDSVLKESQRLKPIAIASMRRFTTHNVKLSDGVILPKNKLTLVSAHQHWDPEYYKDPLKFDGYRFFNMRREPGKESKAQLVSATPDHMGFGYGLHACPGRFFASEEIKIALSHILLKYDFKPVEGSSMEPRKYGLNMNANPTAKLSVRRRKEEIAI", "text": "FUNCTION: GA14 synthase; part of the gene cluster that mediates the biosynthesis of gibberellins (GAs), diterpenoids that may provide a selective advantage during infection of the preferred host plant, rice (PubMed:23825955, PubMed:9917370, PubMed:10347043, PubMed:12750377, PubMed:15925394). Gibberellins (GAs) are diterpenoids and are synthesized via the mevalonate pathway (PubMed:12750377). Biosynthesis of the major metabolite GA3 (gibberellic acid) from geranylgeranyl diphosphate (GGPP) requires 13 steps (PubMed:12750377). The GGPP produced by the geranylgeranyl diphosphate synthase GGS2 is converted to ent-kaurene via ent-copalyldiphosphate in a two-step cyclization reaction performed by the bifunctional ent-copalyl diphosphate synthase/ent-kaurene synthase enzyme (CPS/KS) (PubMed:9745028, PubMed:10803977, PubMed:12750377). Ent-Kaurene is metabolized to GAs by a series of oxidation reactions catalyzed by cytochrome P450 monooxygenases (PubMed:9917370, PubMed:12750377). Cytochrome P450 monooxygenase P450-4 is an ent-kaurene oxidase that catalyzes the three oxidation steps between ent-kaurene and ent-kaurenoic acid (PubMed:11472927). The highly multifunctional cytochrome P450 monooxygenase P450-1 then catalyzes four steps involving oxidation at two carbon atoms, in the main pathway from ent-kaurenoic acid to GA14 via GA12-aldehyde as well as producing kaurenolides and fujenoic acids as by-products (PubMed:11320210). The cytochrome P450 monooxygenase P450-2 then converts GA14 to GA4 by removal of C-20 (PubMed:11943776). GA4 is further converted to GA7 by the GA4 desaturase DES via 1,2- desaturation before cytochrome P450 monooxygenase P450-3, a 13- hydroxylase, hydroxylates GA7 to GA3, the final product of the GA- biosynthetic pathway (PubMed:12750377). SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEEPKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYDGGYVQDYEDFM", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit J family."}
{"protein": "AECMVDETVCYIHNHNNC", "text": "FUNCTION: Insecticidal toxin. Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.1 mg/kg body weight. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 16 (SFI) family."}
{"protein": "MPRSRALILGVLALTTMLSLCGGEDDIEADHVGSYGITVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFAQLRRFEPQGGLQNIATGKHNLEILTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class II family."}
{"protein": "MVSKIIKLGVPTATLAVGTLLLGDDEKRSAFFRTASAFTQNHGHKTFDEHFPRGEWDKNWDFRDPISLVDKGKWEKADEEGKKKLIEEKKATATRNIFLIRHGQYHLDHEVKMLTPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHLPDDLTRTSSPFIEEGPPYPPVPDHKTWRPLDPEFYTEAARIESAYRKIFHRASPSQKEDSFELIVCHANVIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVRSIGDIGHLPPNKISFT", "text": "FUNCTION: Displays phosphatase activity for serine/threonine residues. Has apparently no phosphoglycerate mutase activity. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
{"protein": "GIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILVITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAAL", "text": "FUNCTION: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MDVSNENANSSIMTMEANFFMCIIVVFTQVRPVNNPESSAYLFSGFCRHTHKNACFFSFDFFQLVFDASSFAIPATLFYKYTKVTNINMKNITKNQIRMILLSSYLLSLIVGVIYVITYEPDESLEVASETRKFHSTQYDFRYYADITGYQKHFWSWLATNLNMISIFVPPIMSIVFIRLIQIKLNSLKHLFTDKTAAQAKKFDLALTIQTLVPAVCVIPIYIAHLILENYDLPFLSNFEKVLYMMLSLPTAIDAFIVIVTITPYQKAFIAFFKDTFCGKKVSPAIVRRNNISAVSIF", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein srd family."}
{"protein": "MSTFEKINKVSVVIPVYNEEESLPQLLERTIKSCKQLEQEYELILVDDGSSDNSAKMLEEAANIEDNHVIAIILNRNYGQHSAIMAGFNQADGDLVITLDADLQNPPEEIPRLVATAEEGYDVVGTRRRNRQDSWFRKTASKMINAMITKATGRSMGDYGCMLRAYRRHIIDAMLQCHERSTFIPILANTFARRTIEIEVAHAEREYGDSKYSFLKLINLMYDLLTCLTTAPLRLLSVVGSVIAVAGFLLAVLLIVLRLIFGAIWAADGVFTLFAILFMFIGAQFVAMGLLGEYIGRIYNDVRARPRYFIQKVVGVKKPNKNQEED", "text": "FUNCTION: Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "VVNGKPTRTNVGRMVSLKYRNKHI", "text": "FUNCTION: HPTA is an acidic heparin-binding growth factor for hepatocytes."}
{"protein": "MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPIASLPGVARYGVNRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFQAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKETLMAHGLGSRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITHYTPQLLQWLKEE", "text": "FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). SIMILARITY: Belongs to the ALAD family."}
{"protein": "MQQETTDTQEYQLAMESFLKGGGTIAMLNEISSDTLEQLYSLAFNQYQSGKYEDAHKVFQALCVLDHYDSRFFLGLGACRQAMGQYDLAIHSYSYGAIMDIKEPRFPFHAAECLLQKGELAEAESGLFLAQELIADKPEFKELSTRVSSMLEAIKLKKEMEHECVDNP", "text": "FUNCTION: Mediates the negative regulation of the lcrGVH operon by ATP or calcium. Acts as a modulator of the yop operon expression. SIMILARITY: Belongs to the LcrH/SycD chaperone family."}
{"protein": "MATSRLPAVPEETTILMAKEELEALRTAFESGDIPQAASRLRELLANSETTRLEVGVTGESGAGKSSLINALRGLGAEDPGAALTGVVETTMQPSPYPHPQFPDVTLWDLPGAGSPGCSADKYLKQVDFGRYDFFLLVSPRRCGAVELPPSLLRSCARGRSFTLCAPRWTRIWRPPAARGPRVSARLQLLQEIRDHCTERLRVAGVNDPRIFLVSNLSPTRYDFPMLVTTWEHDLPAHRRHAGLLSLPDISLEALQKKKDMLQEQVLKTALVSGVIQALPVPGLAAAYDDALLIRSLRGYHRSFGLDDDSLAKLAEQVGKQAGDLRSVIRSPLANEVSPETVLRLYSQSSDGAMRVARAFERGIPVSARWWPGVSASARSTPCSRAVSMRWLRTPNASASKPWRKMSPRGVR", "text": "SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. IRG family."}
{"protein": "MSKRKTKEPKVENVTLGPAVREGEQVFGVVHVFASFNDTFIHVTDLSGRETLVRITGGMKVKADRDESSPYAAMLAAQDVAQRCKELGITAIHVKLRATGGNKTKTPGPGAQSALRALARSGMKIGRIEDVTPIPTDSTRRKGGRRGRRL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS11 family."}
{"protein": "MASSKFFTVLFLVLLTHANSSNDIYFNFQRFNETNLILQRDASVSSSGQLRLTNLNGNGEPRVGSLGRAFYSAPIQIWDNTTGTVASFATSFTFNIQVPNNAGPADGLAFALVPVGSQPKDKGGFLGLFDGSNSNFHTVAVEFDTLYNKDWDPTERHIGIDVNSIRSIKTTRWDFVNGENAEVLITYDSSTNLLVASLVYPSQKTSFIVSDTVDLKSVLPEWVSVGFSATTGINKGNVETNDVLSWSFASKLSDGTTSEGLNLANLVLNKIL", "text": "FUNCTION: This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil. SIMILARITY: Belongs to the leguminous lectin family."}
{"protein": "MGSAPSKILEDLLDDTNFDREEIERLRKRFMKLDRDSSGSIDKNEFMSIPGVSSNPLAGRIMEVFDADNSGDVDFQEFISGLSVFSGRSDKEEKLRFAFKIYDIDKDGYISNGELFIVLKIMVGNNLEDEQLQQVVDRTIMENDVDGDGKLSFEEFKSAVETTEVANSLTLQCDI", "text": "FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity (By similarity). SIMILARITY: Belongs to the calcineurin regulatory subunit family."}
{"protein": "MAKKTVGLLVMAYGTPYKEDDIERYYTHIRHGRKPPQEQIDDLKARYRAIGGLSPLAKITEAQAKQLEKRLNEMQDEVEFCMYLGLKHIEPFIEDAVERMHADGVKEAVAIVLAPHYSTFSICSYNERAKAAAEKLGGPVIYTIDQWYDEPKFLQYWSEKVKAIFDAMKEREREQAVLIVSAHSLPEKIIQAGDPYPAQLEDTAKRIAEQAGVTHYAVGWQSAGNTPEPWLGPDVQDLTRQLHDEQGYTSFVYAPVGFVADHLEVLYDNDIECKQVTEEIGARYYRPEMPNTDPLFIDALATVVLKRLAKEGDEHE", "text": "FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferrochelatase family."}
{"protein": "MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHMSKA", "text": "FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3- phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity). Binds DNA in vitro (PubMed:22589465). Together with DNA polymerase II subunit B3-1 (DPB3-1) and GAPC1, enhances heat tolerance and promotes the expression of heat-inducible genes (PubMed:32651385). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Accumulates in the nucleus under heat stress. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MSNAEHLANIMVERFISAVKNGVDLVPVVADSTSTAKIAPFIKEFPDRLVNVGIAEQSLVGCAAGLALGGKVAVTCNAAPFLISRANEQVKVDVCYNNTNVKLFGLNSGASYGPLASTHHSIDDIGVMRGFGNIQIFAPSSPNECRQIIDYAINYVGPVYIRLDGKELPEIHNDDYEFVPGQIDVLRKGGKIALVAMGSTVYEIVDAAVKLAEKGIEVTVVNVPSIRPCDTEALFNAIKDCKYVISVEEHNINGGVGSLVAEVIAEHGAPITLKRRGIADGGYALAGDRKSMRKHHGIDADSIVDLALSLN", "text": "FUNCTION: Involved in catabolism of D-apiose. Catalyzes the transfer of the glycolaldehyde group from apulose-4-phosphate to D-glyceraldehyde 3-phosphate, generating dihydroxyacetone phosphate and D-xylulose-5- phosphate. SIMILARITY: Belongs to the transketolase family."}
{"protein": "MTEYDYEELGLVAGLEIHQQLDTATKLFCDCPTTIREPEESDRSFTRYLHPTKSELGEIDEAALEESMVDREFEYLAYDTTCLVEEDDEPPHRVDREAMETTLEIAQLLDMSVADQVNIMRKIVVDGSNTTGFQRSMLVANDGAIETSAGPVGVEDMLLEEESCQRIEETEDGVRFSLDRLGIPLVEIGTKPDISSPEQAREAAERIGMLLRSTGKVKRGLGTIRQDVNVSIEEGARIELKGVQSLDDIDDLVRNEVRRQVELLDIAEELAERGATVGEPQDVTEVFEDTDSGVIEGALSSGGKVQGLLLSGFDGLVGREIQPDRRLGTELSDHAKRHGAGGIFHTDELPAYGVTEAEVEALRDAVGAGSEDAVAIVADDPETAELAIDAVAERAETALAGVPEETRDANEDATSRYLRPLPGAARMYPETDVPPVEPDVTEVETPELLTEKVDRYESEFDLGSGLAEQVAYGQRWPLFEALVAGEGVDPTLAAGTLESTLTELRRDDVPVENLTDKHLQGAILLVDGGDVPREGMEDLLTALAENPSLTAEEAVEQEGLGGVDESEVRDAVAEVVERHEDQVAEEGMGAFSALMGECMGALRGKADGDTVSDVLRSEIQKRA", "text": "FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily."}
{"protein": "MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVDFEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHIFKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDPHFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFLPGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMPYTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDTFNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLSLKFRMGITISPVSHRLCAVPQV", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system (PubMed:8631948, PubMed:19965576). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:8631948, PubMed:19965576). Catalyzes the epoxidation of double bonds of PUFA (PubMed:8631948, PubMed:19965576). Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE), likely playing a major role in the epoxidation of endogenous cardiac arachidonic acid pools (PubMed:8631948). In endothelial cells, participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15- lipoxygenase metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs), which are precursors of vasodilatory trihydroxyicosatrienoic acids (THETAs). This hydroperoxide isomerase activity is NADPH- and O2-independent (PubMed:19737933). Catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone (PubMed:19923256). Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole (PubMed:23959307). Catalyzes the sulfoxidation of fenbedazole (PubMed:19923256). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MQHPTLQPEVDPNPVVSSSSSSSSSNPLPAHLNPANYPQTRYFSDSNIHLELTYNPLDPTKSLAQIRSPHAGANVLFLGTTRSTFDNRPVARLTYTSYAPLALRTLEKIARGAVTKYQLCGISISHRLGEVRVAEESIAIAVAAGHRRPAWRAGEEVLEECKAAVEIWKREEFIGAGAGEGEGEWRANRDTDSQGNCRGDKVAEG", "text": "FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily."}
{"protein": "MTLKLCVLTPNRIFWDSEVEEIILSTNSGQIGILPTHTPIATSVDIGILRIRLNGRWLTMALMGGFARIGNNEITVLVNDAERSSDIDPQEAQQTVEIAEANFRKAKGKRQKIEANIALCRARTRVKAVSPISVGK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Plastid thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family."}
{"protein": "MADPSLYTYPSPLQGYENLAPLGTEVSPDGKSLLNPETGIKSKSYEKFTEPLDSGIRGAFDVHIYHFQKNKEQAKFARELWERIRREFPELRIYRFWEEPIGPHPVAMFEVNLFTPEQFGAFIPWLVINRGPLSALVHPNTVDEKGELLDEERDHTQRAIWMGEQLPLDLSLVKRLKQQKAAH", "text": "SIMILARITY: To A.muscaria DOPA 4,5-dioxygenase."}
{"protein": "MGYFRCARAGSFGRRRKMEPSTAARAWALFWLLLPLLGAVCASGPRTLVLLDNLNVRETHSLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENLLKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDGDDIQLEFVRIDPFVRTFLKKKGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFSMMLGLFIFSIVFLHMKEKEKSD", "text": "FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (PubMed:22467853). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the DDOST 48 kDa subunit family."}
{"protein": "MAAVAAEAAATAASPGEGGAGEAEPEMEPIPGSEAGTDPLPVTATEASVPDGETDGQQSAPQADEPPLPPPPPPPGELARSPEAVGPELEAEEKLSVRVAESAAAAPQGGPELPPSPASPPEQPPAPEEREEPPLPQPVAPALVPPAGGDSTVSQLIPGSEVRVTLDHIIEDALVVSFRFGEKLFSGVLMDLSKRFGPHGIPVTVFPKREYKDKPEAMPLQSNTFQEGTEVKCEANGAVPDDPSPVPHPELSLAESLWTSKPPPLFHEGAPYPPPLFIRDTYNQSIPQPPPRKIKRPKRKMYREEPTSIMNAIKLRPRQVLCDKCKNSVVAEKKEIRKGSSATDSSKYEDKKRRNESVTTVNKKLKTDHKVDGKNQNESQKRNAVVKVSNIAHSRGRVVKVSAQANTSKAQLSTKKVLQSKNMDHAKAREVLKIAKEKAQKKQNETSTSKNAHSKVHFTRRYQNPSSGSLPPRVRLKPQRYRNEENDSSLKTGLEKMRSGKMAPKPQSRCTSTRSAGEAPSENQSPSKGPEEASSEVQDTNEVHVPGDQDEPQTLGKKGSKNNISVYMTLNQKKSDSSSASVCSIDSTDDLKSSNSECSSSESFDFPPGSMHAPSTSSTSSSSKEEKKLSNSLKMKVFSKNVSKCVTPDGRTICVGDIVWAKIYGFPWWPARILTITVSRKDNGLLVRQEARISWFGSPTTSFLALSQLSPFLENFQSRFNKKRKGLYRKAITEAAKAAKQLTPEVRALLTQFET", "text": "FUNCTION: Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin- modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260, PubMed:30327463). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (PubMed:30228260, PubMed:30327463). Plays a role in facilitating transcriptional elongation and repression of spurious transcription initiation through regulation of histone acetylation (By similarity). Essential for proper mitosis progression (PubMed:28645917). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MINGVYYNEISRDLDISSSTQCLRFLKETVIPSLANNGNNSTSIQYHGISKNDNIKKSVNKLDKQINMADRSLGLQQVVCIFSYGPHIQKMLSILEIFKKGYIKNNKKIYQWNKLTSFDIKREGRNELQEERLKVPILVTLVSDSEIIDLNLHSFTKQ", "text": "FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MHIMEGFLPLQWCLFWFAVSAPFIAYGIYQLNRLVKENRSTLPLLAVCGAFIFVLSSLKMPSVTGSCSHPTGTGLGAIMFGPFITSVLSIIVLVYQALFLAHGGLTTLGANVFSMGICGPLLGYWVYQGGKAINLNSIVNVFLASALADIFTYVITSIQLSLAFPAAAGGYMTSFITFAGIFAVTQVPLAIIEGIFLTLTFKYINQIRPDILIHLGVISPAQSKQILEAYS", "text": "FUNCTION: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiM family."}
{"protein": "MKAFSPVRSVRKSSLTEHSLGIARSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQLALDSHPSIVSLHHARVGGSTSRTPLTALNTDISILSLQAAELSAEFTDESKSLCP", "text": "FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Inhibits the activity of both neurogenic (neurod1/neuroD) and myogenic (myod1/myoD) bHLH factors. May play a role in the regulation of the circadian clock (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MSGMWVHPGRTLIWALWVLAAVIKGPAADAPVRSTRLGWVRGKQTTVLGSTVPVNMFLGIPYAAPPLGPLRFKQPKPALPGNDFRNATSYPKLCFQDLEWLVSYQHVLKVRYPKLEASEDCLYLNIYAPAHADNGSNLPVMVWFPGGAFKMGSASSFDGSALAAYEDVLIVTTQYRLGIFGFFDTGDEHARGNWALLDQVAALTWVRDNIEFFGGDPRSVTIFGESAGAISVSSLILSPIANGLFHKAIMESGVAILPLLMRPPGDERKKDLQVLARICGCHASDSAALLQCLRAKPSEELMDISKKLTFSIPVIDDFFFPDEPVALLTQKAFNSVPSIIGVNNHECAFLLSTEFSEILGGSNRSLALYLVHTFLNIPTQYLHLVADHYFYNKHSPVEIRDSFLDLLGDVLFVVPGVVTARYHRDAGAPVYFYEFQHPPQCLNDTRPAFVKADHSDEIRFVFGGAFLKGDIVMFEGATEEEKLLSRKMMRYWANFARTGDPNGEGVPLWPAYTQSEQYLKLDLSVSVGQKLKEQEVEFWMNTIVP", "text": "FUNCTION: Carboxylesterase present at high level in urine that regulates production of felinine, a probable pheromone precursor. Probably acts by hydrolyzing the peptide bond of the felinine precursor 3-methylbutanol cyteinylglycine, producing felinine and glycine in cat urine. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "MKRKGFIMTVYPDKHDEYEKRHNEIWPEMVAELKKHGAHNYSIFLDKQTNQLFGYIEIEDEEKWSKMAETSINQKWWKFMKPVMKTNSDDSPVSTDLTEVFHMD", "text": "FUNCTION: Involved in the anomeric conversion of L-rhamnose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose mutarotase family."}
{"protein": "MSRFAILVTLALAIATVSVVIAQVPPEKQFRVVNEGEFGEYITEYDASYRFIESSNQSFFTSPFQLLFYNTTPSAYILALRVGLRRDESTMRWIWDANRNNPVGENATLSLGRNGNLVLAEADGRVKWQTNTANKGVTGFQILPNGNIVLHDKNGKFVWQSFDHPTDTLLTGQSLKVNGVNKLVSRTSDSNGSDGPYSMVLDKKGLTMYVNKTGTPLVYGGWPDHDFRGTVTFAVTREFDNLTEPSAYELLLEPAPQPATNPGNNRRLLQVRPIGSGGGTLNLNKINYNGTISYLRLGSDGSLKAYSYFPAATYLKWEESFSFFSTYFVRQCGLPSFCGDYGYCDRGMCNACPTPKGLLGWSDKCAPPKTTQFCSGVKGKTVNYYKIVGVEHFTGPYVNDGQGPTSVNDCKAKCDRDCKCLGYFYKEKDKKCLLAPLLGTLIKDANTSSVAYIKY", "text": "SUBCELLULAR LOCATION: Secreted Secreted, cell wall."}
{"protein": "MEVDTMETLIRLFVSILIICVLALMIKKSRCLDNEGVIGSSIMGFILLYFCGFKYLILLLSFFILGVLVSRVGLEKKKAKKMDETCRSLKNVLANGLIPILFAILAIFGFNWALIGYISSIAAATSDTFSSELGILSNEKPRLITTFEVVEKGTDGAITIFGTLAGVLGAFLIGLFGYLLFGDIKIVLCGTAGGIAGNLADSLVGALFERKGILNNEHVNLIATIVGGIIGVLIYCTL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM19 family."}
{"protein": "MKALRRFTVRAHLPERLAALDQLSTNLRWSWDKPTQDLFAAIDPALWEQCGHDPVALLGAVNPARLDELALDAEFLGALDELAADLNDYLSRPLWYQEQQDAGVAAQALPTGIAYFSLEFGVAEVLPNYSGGLGILAGDHLKSASDLGVPLIAVGLYYRSGYFRQSLTADGWQHETYPSLDPQGLPLRLLTDANGDPVLVEVALGDNAVLRARIWVAQVGRVPLLLLDSDIPENEHDLRNVTDRLYGGDQEHRIKQEILAGIGGVRAIRAYTAVEKLTPPEVFHMNEGHAGFLGIERIRELVTDAGLDFDTALTVVRSSTVFTTHTPVPAGIDRFPLEMVQRYVNDQRGDGRSRLLPGLPADRIVALGAEDDPAKFNMAHMGLRLAQRANGVSLLHGRVSRAMFNELWAGFDPDEVPIGSVTNGVHAPTWAAPQWLQLGRELAGSDSLREPVVWQRLHQVDPAHLWWIRSQLRSMLVEDVRARLRQSWLERGATDAELGWIATAFDPNVLTVGFARRVPTYKRLTLMLRDPGRLEQLLLDEQRPIQLIVAGKSHPADDGGKALIQQVVRFADRPQFRHRIAFLPNYDMSMARLLYWGCDVWLNNPLRPLEACGTSGMKSALNGGLNLSIRDGWWDEWYDGENGWEIPSADGVADENRRDDLEAGALYDLLAQAVAPKFYERDERGVPQRWVEMVRHTLQTLGPKVLASRMVRDYVEHYYAPAAQSFRRTAGAQFDAARELADYRRRAEEAWPKIEIADVDSTGLPDTPLLGSQLTLTATVRLAGLRPNDVTVQGVLGRVDSGDVLMDPVTVEMAHTGTGDGGYEIFSTTTPLPLAGPVGYTVRVLPRHPMLAASNELGLVTLA", "text": "FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). SIMILARITY: Belongs to the glycogen phosphorylase family."}
{"protein": "MRSGGTLFALIGSLMLLLLLRMLWCPADAPARSRLLMEGSREDTSGTSAALKTLWSPTTPVPRTRNSTYLDEKTTQITEKCKDLQYSLNSLSNKTRRYSEDDYLQTITNIQRCPWNRQAEEYDNFRAKLASCCDAIQDFVVSQNNTPVGTNMSYEVESKKHIPIRENIFHMFPVSQPFVDYPYNQCAVVGNGGILNKSLCGAEIDKSDFVFRCNLPPITGSASKDVGSKTNLVTVNPSIITLKYQNLKEKKAQFLEDISTYGDAFLLLPAFSYRANTGISFKVYQTLKESKMRQKVLFFHPRYLRHLALFWRTKGVTAYRLSTGLMIASVAVELCENVKLYGFWPFSKTIEDTPLSHHYYDNMLPKHGFHQMPKEYSQMLQLHMRGILKLQFSKCETA", "text": "FUNCTION: Alpha-2,8-sialyltransferase that prefers O-glycans to N- glycans or glycolipids as acceptor substrates. The minimal acceptor substrate is the NeuAc-alpha-2,3(6)-Gal sequence at the non-reducing end of their carbohydrate groups. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family."}
{"protein": "MLWQCWLQQAQRMRMMMKALLRFRATRLDSEMMGGWRRGAQRLAAGVVEGQRTLPQEGAAAGPRNLKEMPGPSTFRNLLEFFWRDGFSRIHEIQQNHIREYGRIFKSHFGPQFVVSIADRDMVAQILRAERDAPQRANMESWQEYRDLRGRSTGLISAEGKKWLAMRSVLRQKILRPRDVFIYAGGVNEVVSDLIKRIKTLRSREDDGETVTNVNDLYFKYSMEAVATILYECRLGCLQNEVPKQTLEYIEALELMFSMFKTTMYAGAIPKWLRPFIPKPWEEFCRSWDGLFRFSQIHVDGRLREIQACLDRGEEVKGGLLTSILISKELTLEELYANMTEMLLAGVDTTSFTLSWATYLLAKNPQAQQMVYDQIVQNLGKDTVPTAEDVPKLPLIRAVLKETLRLFPVLPGNGRVTQDDLVLGGYLIPKGTQLALCHYSTSYDQEYFTAAEDFQPGRWLRHGHLDRVENFGSIPFGYGIRSCIGKRVAELEIHLALIQLLQNFEIRTSPKTQTVLPKTHGLLCPAGAINVRFVNRE", "text": "FUNCTION: Efficiently catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4- didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4- didehydroretinal), also acts on all-trans retinal and all-trans retinoic acid. The replacement of 11-cis retinal chromophore in photopigments with 11-cis 3,4-didehydroretinal enhances sensitivity to long-wavelength light. This may improve vision in fresh water which is often turbid. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MASFTASASTVSAARPALLLKPTVAISAPVLGLPPMGKKKGGVRCSMETKQGNVSVMGAGVSAAATAALTAVMSNPAMALVDERMSTEGTGLPFGLSNNLLGWILFGVFGLIWTFFFVYTSSLEEDEESGLSL", "text": "FUNCTION: Stabilizes dimeric photosystem II (PSII). In its absence no dimeric PSII accumulates and there is a reduction of monomeric PSII. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single- pass membrane protein. Note=The N-terminus is found within the thylakoid lumen (By similarity). SIMILARITY: Belongs to the psbW family."}
{"protein": "MSSISELYDVTWEEMRDKLRKWREENYRNSEQIVDVGEELINEHASKLGDDIWIIYEQVMIAALDCSRDDLAWSCLQELKRQFPDSHRVKRLAGMRLEALERYDDANKLYDSILQDDPTNTAARKRKICILRAQGKSSEAIRELNEYLEQFVGDQEAWHELSELYINEHDYAKAAFCLEELMMTNPHNHLYCEQYAEVKYTQGGLENLELARKYFAQALKLNNRNMRALFGLYMSASHIAASPKVSAKVKKDNVKYAAWAAAQISRAYQMAGRGKKENKCSVKAVEEMLESLQITMS", "text": "FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N- exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the EMC2 family."}
{"protein": "MALVSMKEMLKKAKAGHYAVGQFNLNNLQWAQAILQAAEEEQAPVIVAASDRLVDFLGGFQTITSMVNSLLIEMKITVPVALHLDHGMTIDRCKQAIDAGFTSVMIDGSHSPIEDNIAMTKEVVAYAQPRNVSVEAEVGTVGGMEDGLIGGVKYADLDECVRVVEEANIDALAAALGSVHGPYQGEPKLGFEEMKVISERTGVPLVLHGGSGIPDYQIRKAILLGHAKINVNTECLQAWAHAVRTILTNDQDIYDYRAITTPGTEAIVETVKTKMREFQTSGKAKERV", "text": "FUNCTION: Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6- phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily."}
{"protein": "MADKEATVYIVDLGESMADCHNGRDESDLDFGMRYVWDKISTTVAASRKTWTLGVVGLNTEETNNAQDSEGLEGYEHISVLQDIGPMTMTQLRELRSSIQTSHTYGGDAISGIVVALAMIELFTKKLKYNRRIILVTNGESPIDDESSEDVANRLNYSNIELIVIGVDFDDADYGFKEEDKSKGKARNEKTLRKLVEQCNNGVFGTMQQAVEELAIPRIKPVRPFKAYDGALTLGDPEKYKSALSIHVERYFKTKRAPAPPASTVVVNSEPGGASQSETLNEDTEMGDAEFSGVKHMRTYRVNDPDAPGGKRDVEFEDLAKGYQYGRTVVPFSESDFSITKLETKKSFTILGFIPFSSYNPFLNLGETGIVVAQKHNEEAELGLSALIHALHELESYAVARYVQKDGAQPQLVLLKPNPAIEDDFECLYDVPLPFAEDLRSYQFPPLDKVLTVTGNIIKEHRLLPSEDLKQAMSDFVDAMDLSGFDVDEDGKPTEYAPIDETYNPTIHRMNQAIRARAVDPDAPIKPPAEILLRFSKPPEKLIEKAKPEIEALIDAAEIKKVPAKAQGRGSRKEPVKPLSGLDIDSLLGESKRTTISLDNAVPEFKQILATAADDATIESAAKQMGQIVRKLIQDSFADLFYARAAENLRVMREELISLEVPGLYNKFLTGLKKSILSGELDGDRREMWFKHIVGGHLSLITQDESEVSEVTAEEAKALCAWSRPNITYRYFRDTA", "text": "FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the ku80 family."}
{"protein": "MPRIPTSVLGKYLLSGQISRQGCVGARQITRHSALPSAAVSVANSARLLHVSSETVPPPPAQPVPLRKQLKDEAKKAKKQGKKKSKGDSQTVDGWELTVGIEIHAQLNTARKLFSPAVTSFNDEPNSHVALFDLSMPGSQPLFQKETLIPALRAALALNCDIQKLSRFDRKHYFWWDQPSGYQITQYYEPFARNGHITLLARDGISPQDGESVTIGIKQVQLEQDTAKTLAQADKVNWLDFNRVGVPLIEIITEPEMHHPRTAAVLVRKIQMLLNTVDACVSGMETGGLRADVNVSVRRTDGSNPSLGTRTEIKNLSTIKAVEDAIIAERDRQISELEAGRAIPSETRGWTLGSNETRRLRGKEGEVDYRYMPDPDIAPLVIGDDLVDHLRRSLAVSPDSELDTLIARYGLTAKDALSLINLENGSRVQYFYKVLKSVEEKLAAELTEEEMPEFKSYSTLVGNWIIHELGRLTTFKAGPLAARDLSFTPEGDCLQVPDADLAQLLYHLVRKQITGKVAKELLFAIYLNEIEGGITQAIEDNDLWFKEIPEEEYEKLADEVMEGEDKVLQEFVDYKQFPQGKLMYLVGKMMRLGPTERIVPANAERVMRAKVEKLRSE", "text": "FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily."}
{"protein": "MTKNISRDRHVAVLPFPFSSHAGRLLTLVRRLAAAAPNVTFSFYSTPKSIESLFSPAERVPGNVRPYAVPDGVPEGHVFSGEPVEHVNLYLTAVGEGESLRGVLKAAEAETGRRIGCVMSDAFMWFAGDLAEEMGVPWVPFMAGGANSITAHFYTDLIRETVGMHDIVGRENDIVKFIPGFSELRLGDLPTGVLFGNLESPFAIMLHKMGRALPKATAIAINSFEELDPDIIQDLKSKFKMILNVSPFSAISLPSSPPPPPTSYTDEYGCMPWLDNRKAASVAYIGFGTLATPPPVEIAALAEALEASGTPFLWSLKDNPKEFFPEGFIKRTSERQKIVPWAPQEQVLAHGSVGVFVTHCGWNSALESIAAGVPLIGRPFFGDHQLNAWLVENVWKIGVRVEGGVFTKSGTMSALELVLTHEKQKELRARVEMFKKLALKAVGPEQSSTRNLHTLLEIVAGYNL", "text": "FUNCTION: Flavonoid 3-O-glycosyltransferase involved in the biosynthesis of anthocyanins confering flower red/pink colors, mainly anthocyanidin 3-O-glycosides (PubMed:35651780). Catalyzes the addition of UDP-sugar to the 3-OH of anthocyanidin, with a preference for UDP- galactose (UDP-Gal) as sugar donor and cyanidin as substrate; able to use delphinidin, pelargonidin, peonidin, malvidin and petunidin as substrates in the presence of UDP-Gal (PubMed:35651780). Can also use UDP-glucose (UDP-Glu) as sugar donor with delphinidin, cyanidin and malvidin as substrates, but not active on pelargonidin, peonidin and petunidin (PubMed:35651780). SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MNFGMLKLLTVLIICYSNNFMRTRGGNGK", "text": "FUNCTION: Probable toxin. Does not show insecticidal, antimicrobial and antiparasitic activities. Does not induce increase in intracellular calcium in mouse DRG neurons, suggesting that it does not induce pain. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the limacoditoxin-12 family."}
{"protein": "MALLRGNSLAISQKMLSVFQASALPHISLRIFISPPSIANIWNSILLAVPKKKTSYTKKRSRLLSGKALKDKTVNRCPICGSFKLAHHLCSHCFRNIRREFNE", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
{"protein": "DRIRISISQKRTGPSKQHLAPPPIPTSPSSEQVGEASSPSKVQKSWSFNDRTRFRASLRLKPRCSAEEGPSEEVAEEKSYQCELTVDDVMPAVKTVIRSVRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQARVDQIVGRGPGDRKTREKGDKGPS", "text": "FUNCTION: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. SUBCELLULAR LOCATION: Basal cell membrane; Multi-pass membrane protein. Note=Situated at the basal membrane of cochlear outer hair cells. SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.4/KCNQ4 sub-subfamily."}
{"protein": "MKTIIDNFVDRVIEYGMYNEIDKIYVKNRVLALIGEEGTDRISDENDLKQIKDYLVEIALKNGKIKDLIEEKECLGAELMNFIVPLPSRLNDIFWSSYDISPQEAVEEFYKLSKDSDYIKTSAIAKNIEFRASTKYGELEITINLSKPEKDPKTIAAEKLVKATNYPKCLLCMENEGYQGRINYPARSNHRIIRLKLGDEVWGFQYSPYLYFNEHAIFLNSQHVPMAITSKTFEQLLEIVDILPGYFAGSNSDLPISGGSILSHNHYQGGKHIFPMEKAKFESEFRFKDFEDVNAGIVKWPMSVIRLQSENKNRLLDLATKILNKWREYSDLEVDIIAMTEDVPHHTVTPIARKVDGRYELDIVLRDNHTTEQYPDGVFHPHQDVQHIKKENIGLIEVMGLAILPPRLKPELEEVGKYLLGEDNAIADYHLEWADQLKEKYPRINKEEVNSVVQHEAGQVFARVLEDAGVYKNTPSGHEAFMRFVKSVGIN", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 2 family."}
{"protein": "MVSFKSLLLAASAFTAVLGRPFDSFDGPDVNITDADELLVRRQVTANSEGTHNGYFYSWWSDGGGQVTYTMGAGSRYSVTWKDTGNFVGGKGWNPGTGRTINYGGSFSPQGNGYLAVYGWTRNPLIEYYVVESYGTYNPGSGGQLKGTVTTDGGTYNVYVSTRTNQPSIDGTRTFQQYWSVRTSKRVGGAVTMQNHFNAWAQFGMNLGAHYYQIVATEGYQSSGPSDIYVQTQCKSLCDRGRVTWRDVVC", "text": "FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. The most favorable substrate is beechwood xylan. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MIDLKQYEFWFLVGSQYLYGLETLKKVEQQASKIVDSLNDDPIFPSKIVLKPVLKSSSEITEIFEKANADPKCAGVIVWMHTFSPSKMWIRGLSINKKPLLHLHTQYNREIPWDTIDMDYMNLNQSAHGDREHGFIHARMRLPRKVVVGHWEEKEVREKIAKWMRVACAIQDGRTGQIVRFGDNMREVASTEGDKVEAQIKLGWSINTWGVGELAERVKAVPDNEVEELLTEYREKYIMPEDEYSLKAIREQAKIEIALREFLKEKNAIAFTTTFEDLHDLPQLPGLAVQRLMEEGYGFGAEGDWKAAGLVRAIKVMGTGLPGGTSFMEDYTYHLTPGNELVLGAHMLEVCPTIAKEKPRIEVHPLSIGGKADPARLVFDGQEGPAVNASIVDMGNRFRLVVNKVLSVPIERKMPKLPTARVLWKPLPDFKRATTAWILAGGSHHTAFSTAIDVEYLIDWAEALEIEYVVIDENLDLEDFKKELRWNELYWGLLKR", "text": "FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. SIMILARITY: Belongs to the arabinose isomerase family."}
{"protein": "MLRSIQHVEALSSRQISTTSMLLKNRAGKTKSTSNRTQLLTYEMAQKPHHIGVRKSWLTWHSQNLEEFRQSQPLVVAQDEVVRRFIRGFFPQNLVVSGNEIVIKRRGNVLIVAGFLQYSRRLDIRRIYWMFGFAEEFLSILLKQPVKLEMAFVESEEDVAYNYI", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS3 family."}
{"protein": "MRHVQEARAVPAEHEARPAPVTMPANGSPYRLGAALLQSLAQEMNALAEQASALLSMPPESLSLDADAFAQIARRNVPRWHFAMLNDTERNTALMTALERGIPAGATVLDIGSGSGLLAMAAARAGAGRVFTCEMNPLLAEIARNVISAHGMSDVITVIGKPSTALDPVRDLGGPVDVLVSEIVDCGLIGEGLLPSVRHAREHLLKPDGIMLPSAARLHGRLVSSDEVLKLNQVTTAGGFDVSLMNTVATRGHFPVRLDTWPHRFLSEAAPLVEFDLARSALEPGERPLALTATADGEVQALAVWFELDMGSGITLSNPPDNPRSHWMQGWVPLDKPVPVKAGETLALRLGWSDFTLRVSI", "text": "FUNCTION: Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN) (PubMed:30728519, PubMed:30763082). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor (PubMed:30728519, PubMed:30763082). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family."}
{"protein": "MGKSIPQYLGQLDIRKSVVSLATGAGAIYLLYKAIKAGIKCKPPLCSNSPICIARLAVERERHGRDSGELRRLLNSLECKQDEYAKSMILHSITRCVYLLEAEASACTTDDIVLLGYMLDDKDNSVKTQALNTLKAFSGIRKFRLKIQEHSIKVLELISTIWDTELHIAGLRLLNNLPLPDYVHPQLRRVMPALMEILQSDYILAQVQAVRLLSYLAQKNDLLYDILNCQVHSNFLNLFQPTQSGSLLYEVLVFAERLSEGRNAPHYHVVKWHYNEQSLHESLFGEESRLADRLLALVIHPEEDVQIQACKVIVSLQYPQDLRARPSSCQPSRSYFKNTE", "text": "FUNCTION: Essential for male fertility and sperm mitochondrial sheath formation (By similarity). Required for proper mitochondrial elongation and coiling along the flagellum during the formation of the mitochondrial sheath (By similarity). Facilitates the growth and aggressiveness of neuroblastoma cells (PubMed:30026490). Increases the EZH2 activity and H3K27me3 levels in a RBBP4-dependent manner, and facilitates the enrichment of polycomb repressive complex 2 and H3K27me3 on gene promoters, resulting in transcriptional repression of tumor suppressors affecting the proliferation, invasion, and metastasis of tumor cells (PubMed:30026490). SUBCELLULAR LOCATION: Nucleus Mitochondrion outer membrane; Peripheral membrane protein."}
{"protein": "MLSQIYPQAQHPYSFELNKDMHISAAHFIPRESAGACSRVHGHTYTVNITVAGDELDDSGFLVNFSVLKKLVHGNYDHTLLNDHEDFSQDDRYSLPTTEVVAKTIYDNVQAYLDTLENKPTCVQVFVRETPTSYCVYRPKKGGLNG", "text": "FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. SIMILARITY: Belongs to the PTPS family. QueD subfamily."}
{"protein": "MRKECHPLLRGGRKDNKFRQGFSSSEMESLASICEVILPPLPMDALKIKKHDDVSIEDVEFFWNTSASHYPIPHEVAEILSKRSLIEAVILIRVVLWLLATRLGTFLLCGLLCFSEKWPFINNFSSMSLKKRERVMQWWLKNRFITPIRLAFAYLKVLCLFAYFTWVDENGDNPAWKAIGYEVSADEKLPNSSNGRLLEKGIVETMHETNSTLQQSLTEKGLNVTLDSRNNILKVKCDAIVVGSGCGGGVAASVLSGAGHKVVVLEKGNYFAPRDYSSLEGPSMDQLYETGGILASVDSRILLLAGSTVGGGSAVNWSACIKTPHEVLKEWSENHNLSLFSTSEYLSAMETVCERIGVTESCTHEGFQNQVLRKGCQNLGLKVDYVPRNSSGNHFCGSCGYGCPKGEKQGTQDTWLVDAVENGAVIITGCKAERFLLENNRNGSGRKKKCLGVLAKALSSRVTMKLQIEAKVTISAGGALLTPPLMISSGLKNKNIGKNLHLHPVLMTWGYFPESTSELKGKIFEGGIITSVHKVPSRDSNSYSDTRAIIETPSLGPGSFASLCPWESGLDFKERMLNYPRTAHLITIIRDKACGQVTTEGRVSYKLSAFDKENMKCGLQQALRILKAAGAVEVGTHRSDGQRVKCGEVSENEMAEFIDSVCPMEGALSPGENWNIYTSAHQMGSCRMGMNEKEGAVDENGESWEAQGLFVCDASLLPTAVGVNPMITIQSTAYCISNRVVDYLKRDQI", "text": "FUNCTION: Long-chain fatty alcohol oxidase involved in the omega- oxidation pathway of lipid degradation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MKVVIEADGGSRGNPGPAGYGAVVWTADHSTVLAESKQAIGRATNNVAEYRGLIAGLDDAVKLGATEAAVLMDSKLVVEQMSGRWKVKHPDLLKLYVQAQALASQFRRINYEWVPRARNTYADRLANDAMDAAAQSAAADADPAKIVATESPTSPGWTGARGTPTRLLLLRHGQTELSEQRRYSGRGNPGLNEVGWRQVGAAAGYLARRGGIAAVVSSPLQRAYDTAVTAARALALDVVVDDDLVETDFGAWEGLTFAEAAERDPELHRRWLQDTSITPPGGESFDDVLRRVRRGRDRIIVGYEGATVLVVSHVTPIKMLLRLALDAGSGVLYRLHLDLASLSIAEFYADGASSVRLVNQTGYL", "text": "FUNCTION: Catalyzes the hydrolysis of the phospho group from alpha- ribazole 5'-phosphate to form alpha-ribazole (PubMed:20363939). May also catalyze the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12) (By similarity). Has a possible role in B12 recycling, but the primary role of the C-terminal domain of this phosphatase enzyme could be phosphate generation to help bacterial survival within the macrophage, which is a phosphate-deprived environment (PubMed:20363939). FUNCTION: Endonuclease that displays both RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. As the only authenticated RNase HI in M.tuberculosis, probably plays an important role in the physiology of this organism, being likely involved in bacterial replication. SIMILARITY: In the C-terminal section; belongs to the histidine phosphatase superfamily. SIMILARITY: In the N-terminal section; belongs to the RNase H family."}
{"protein": "MRKTVLYLSAASLFLSSYTLKNDKEYSLAEEHIKNLPEAPEGYKWVVNEDYTDEFNGKRLNAAKWHAKSPYWTNGRPPATFKAENVSVKKGCLRIINTVLSPTEGLDGKPGDKYRLAGGAVASVKNQAHYGYYETRMKASLTTMSSTFWLSNRPVMKEIMKGGKKIKTWSSQELDIIETMGIIRSVNPDNPWNKTWNMQMNSNTHYWYQEQGGKRTDNTAKRSDVVSYMTDPSAEDFHTYGCWWVDANTVKFYYDGKYMYTIKPTTKYTDTPFDRPMFIHIVTETYDWEKQVPTAEDLKDKDKSTTYYDWVRAYKLVPIEE", "text": "FUNCTION: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6- sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6- sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone. SIMILARITY: Belongs to the glycosyl hydrolase 16 family."}
{"protein": "MSDVVKTVIGQRLDLYKLLELNYKDYKGNDDAATTHSLKKQYRKLSLRYHPDKNPGPEYIDRFHLLNLAITVLADPAKKAEYDQWVAQYLYPDNGLSEAEQTRREALVQKLNASERKVREDNQGGNVADIGKIQNYGEKLRRMAHFGLGFGDWRNLDEHISRATTNTIEDSTTDKEVCTLRAVFDFQSIENISDPNNLRRYMNEVFPEYMYDIDEIRYSSNNVYDGEEDIVVYIVLKDPIKTGRLYHQIKRNPPDAFVEIEPYISPKLFESFSKEIPLNDHVKNLLRGVPEVIDLD", "text": "FUNCTION: Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DnaJ family."}
{"protein": "MKFFFIFFIFLFSFLIQSCYSDNTILRSQSLKDGDVIYSEGKRFAFGFFSLGNSKLRYVGIWYAQVSEQTIVWVANRDHPINDTSGLIKFSTRGNLCVYASGNGTEPIWSTDVIDMIQEPALVAKLSDLGNLVLLDPVTGKSFWESFNHPTNTLLPFMKFGFTRQSGVDRIMTSWRSPGDPGSGNITYRIERRGFPQMMMYKGLTLWWRTGSWTGQRWSGVPEMTNKFIFNISFVNNPDEVSITYGVLDASVTTRMVLNETGTLQRFRWNGRDKKWIGFWSAPEDKCDIYNHCGFNGYCDSTSTEKFECSCLPGYEPKTPRDWFLRDASDGCTRIKADSICNGKEGFAKLKRVKIPNTSAVNVDMNITLKECEQRCLKNCSCVAYASAYHESQDGAKGCLTWHGNMLDTRTYLSSGQDFYLRVDKSELARWNGNGASGKKRLVLILISLIAVVMLLLISFHCYLRKRRQRTQSNRLRKAPSSFAPSSFDLEDSFILEELEDKSRSRELPLFELSTIATATNNFAFQNKLGAGGFGPVYKGVLQNGMEIAVKRLSKSSGQGMEEFKNEVKLISKLQHRNLVRILGCCVEFEEKMLVYEYLPNKSLDYFIFHEEQRAELDWPKRMGIIRGIGRGILYLHQDSRLRIIHRDLKASNVLLDNEMIPKIADFGLARIFGGNQIEGSTNRVVGTYGYMSPEYAMDGQFSIKSDVYSFGVLILEIITGKRNSAFYEESLNLVKHIWDRWENGEAIEIIDKLMGEETYDEGEVMKCLHIGLLCVQENSSDRPDMSSVVFMLGHNAIDLPSPKHPAFTAGRRRNTKTGGSSDNWPSGETSSTINDVTLTDVQGR", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MWHLVVLLEELCERGINFRALAQSIFAQQWGDECCKSKTICDLKVIV", "text": "SIMILARITY: Belongs to the site-specific recombinase resolvase family."}
{"protein": "MSSHARVYISNLSFEASENQLYEYLQDYNVISVLIPSQTVRGLKNKAVRPFGIAYAEFSNEEDANKVIQELNGKLFMERHLNLRMHIPIDSNKVQIVRKSSVAVVASSTAGADPSASSDTPAEAPEVASALEQQPLVKQLKSRKHRLTPFRRKKREEPAVEADIPEASTENVQETGNNETEVSEAVAGAADANAGANADANPIVTVDPVNSESSDVGNVTTVITEKPVSETIAFIGFIPRNTTDNQLREYFKGFDPQEIVVFKNRTYRRGFTFHRHFTAALVTFPDAFRLNDAKQFATQEKFRGKQINVKNAFIEKIEEVQRALEKKAGANTNGESAEGNNEIPADAGVTGDEPDTANAVAAIPIEGNPQPQADGNDGAVVEPEANAEPLIDQEDGVTASQDNPLLNSNAESQLESQQPVEQVAA", "text": "FUNCTION: May be involved in the modulation of rDNA transcription. SIMILARITY: Belongs to the RRT5 family."}
{"protein": "MWQLLLPTALLLLVSAGMRAEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTRWFHNESLISSQTSSYFIAAARVNNSGEYRCQTSLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDSIHLRCHSWKNTLLHKVTYLQNGKGRKYFHQNSDFYIPKATLKDSGSYFCRGLIGSKNVSSETVNITITQDLAVSSISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKKSIPSSTSDWKDHKFKWSKDPQDK", "text": "FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory- like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (By similarity). Costimulates NK cells and trigger lysis of target cells independently of IgG binding. Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (By similarity). FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory- like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation. Costimulates NK cells and trigger lysis of target cells independently of IgG binding (By similarity). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Secreted Note=Exists also as a soluble receptor."}
{"protein": "MDISALFLTLFAGSLFLYFLRCLISQRRFGSSKLPLPPGTMGWPYVGETFQLYSQDPNVFFQSKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFMPESIRNMVPDIESIAQDSLRSWEGTMINTYQEMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKGYNSMPVNLPGTLFHKSMKARKELSQILARILSERRQNGSSHNDLLGSFMGDKEELTDEQIADNIIGVIFAARDTTASVMSWILKYLAENPNVLEAVTEEQMAIRKDKEEGESLTWGDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSNPGKFDPSRFEVAPKPNTFMPFGNGTHSCPGNELAKLEMSIMIHHLTTKYSWSIVGASDGIQYGPFALPQNGLPIVLARKPEIEV", "text": "FUNCTION: Involved in the oxidative degradation of abscisic acid. Plays an important role in determining abscisic acid levels in dry seeds and in the control of postgermination growth. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MTDSVSKAVARTIRAPHGSELHCANWLIEAAYRMIQNNLDPDVAERPEDLVVYGGIGKAARNWACFEQILRSLQALQPEETLLVQSGKPVGVFRTHADAPRVLIANSNLVPHWATWDHFHELDKAGLMMYGQMTAGSWIYIGAQGIVQGTFETFVEAGRKHYNGDLTGKWILTAGLGGMGGAQPLAGVLAGACVLAVECQESRIDFRLRTRYLDHKAFSVDEALAIIDKACKEKRAISVGLLGNAAEILPELVQRAKAGGMKPDIVTDQTSAHDPINGYLPAGWDLARWESSRQSDPKAVEKAARASMAVHVQAMLDFCHMGIPTVDYGNNIRQVALDEGVKNAFDFPGFVPAYIRPLFCEGKGPFRWVALSGDPEDIYKTDAKLKALFPEHTNLHRWLDMAQERIAFQGLPARICWLGLGERHLAGLAFNEMVRNGELKAPVVIGRDHLDCGSVASPNRETEAMMDGSDAVSDWPLLNALLNTAGGATWVSLHHGGGVGMGFSQHAGVVIVADGTAEADARLSRVLWNDPATGVMRHADAGYEVARDCARRHELTLPMAKELP", "text": "SIMILARITY: Belongs to the urocanase family."}
{"protein": "MASLFRSYLPAIWLLLSQLLRESLAAELRGCGPRFGKHLLSYCPMPEKTFTTTPGGWLLESGRPKEMVSTSNNKDGQALGTTSEFIPNLSPELKKPLSEGQPSLKKIILSRKKRSGRHRFDPFCCEVICDDGTSVKLCT", "text": "FUNCTION: May play an important role in trophoblast development and in the regulation of bone formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
{"protein": "MWSPLILPLLAQIFACAFGDAVNEGCNVDPKGIHGLWYLDEPFGVYLSAIYNGSLAYIMMKERVPAIVTTVINSLEQDNDEIVQKYGVESQEELHRIVDSLKSLKTELSTNQPLTNLPLAHDEADRDAAVWNEHLDRQREIEGPNLSYFFTRFLLAESYTFRKMAHAFALAKNVRNFDFFGKQKEHLLTNSAKSLPILAHRALLEANRSKATKDEMREELAKFLKLSLWGNRFDLAASSGHEITQAGDPIELLSSFDEDLLIDHTRVAWDILNKPHGPNDPVIVDIVLDNAGYELFNDLCLATFLVSRGLATKVRFHAKQIPWYVSDVNIHDFHWVIGYMRSSSDPHLKEFGDLCARQLESGSWSVEADAFWTTFHGYGEMKKQAPVLYNTLSEATLLIFKGDLNYRKLLGDLNWEHTTSLDTALFHLDFKPTNVLSLRTIKARRVRRSYARDAASCGRRTRRRWATGRTGVIVASAKNAQCACAKSR", "text": "FUNCTION: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1- phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (By similarity). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily."}
{"protein": "KSAYMRF", "text": "FUNCTION: Myoactive; induces a rapid concentration-dependent muscle tension increase. FUNCTION: Active on neuromusculature. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family."}
{"protein": "MNAHQEDTPPGPSTVFRPPTSSRPLETPHCREIRIGIAGITVTLSLCGCANARVPTLRSATADNSENTGFKNVPDLRTDQPKPPSKKRSCDPSEYRVSELKESLITTTPSRPRTARRCIRL", "text": "FUNCTION: May act as transcriptional regulator. Induces apoptosis in infected cells. Element of infectious replication cycle (By similarity). SUBCELLULAR LOCATION: Host nucleus. Note=Host nucleus of infected cells. SIMILARITY: Belongs to the gyrovirus apoptin family."}
{"protein": "MIVNGTEKSALLLMAIGSDQAGEILKHLTPFEVQELITAMVNIKRVSAQKLNEILLQCYNLAIKNNAFNCNNSDKYLIKMLTKALGEKKGTSLLKEALEIRNARICIKALNYMKAKQVAFLLDKEHPQIITTILICLNKNQSAEVLSFLSDKKRAEIILRIVDFHGIEESSLVELTQVINNLLKNKKLILSEKGGIKTAAQILNSMKIKHEKEIIENISKSNEQLADKIIKEIFLFENLVDLDDKYIKILLENIEKEKLHIALQNTSQAIREKFFKNMSHTESNELTLNLEKKSYISDISIKNEQKLILIMLKSIVENGRISLKNLREYYV", "text": "FUNCTION: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Bacterial flagellum basal body. SIMILARITY: Belongs to the FliG family."}
{"protein": "MSEQNNEQRSQAAGTDTVDRGNSNAKLEQLEAYREDATGEALSTNTGTRIADNQNTLKAGERGPSLLEDFIMREKITHFDHERIPERVVHARGSAAHGYFEAYEDLSDLTKAGFLAEAGKRTPVFVRFSTVQGPRGSADTVRDVRGFAVKFYTDEGNFDLVGNNMPVFFIQDAIKFPDFVHAVKPEPHNEIPTGASAHDTFWDFVSLTPESAHMVMWLMSDRAIPIAYRNMQGFGVHTFRLVNAAGESVLVKFHWRPKSGTCSLVWDEAQKLAGKDPDFNRRTLWEDIEKGDYPEWELGLQVIPENQQDSFDFDLLDPTKLVPEELVPVRVVGRMVLNRNPDNFFAETEQVAFHVGHVVPGIDFTNDPLLQGRLFSYTDTQLLRLSGPNFNEIPINRPLCPFHNNQRDAPHRQTINRGRASYEPNSIDGGWPKETPPAARNGGFSTYHEPVSGSKLRKRADSFADHFSQAALFWHSMSEAEQAHIVAAYSFELSKVERQSIREREVNQILLNIDPQLAARVAANVGVQLAAPANPTPQPKPSPALSQMNLLSGDIRSRKVAILIADGVAESDVSDLRDALRQEGADAKLIAPSASPVQAENGAELSPEGTWDGLPSVAFDAVFVPGGAASSQAIGADGRGLHYLLEAYKHLKPVAFAGDAQALASQLSLPGDPGVVLGATATDVFPGLRQALMQHRIWQREAATKAIPA", "text": "FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the catalase family. HPII subfamily."}
{"protein": "MGAAAWAPPHLLLRVSLLLLLLLPLRGRLAGSWDLAGYLLYCPCMGRFGNQADHFLGSLAFAKLLNRTLAVPPWIEYQHHKPPFTNLHVSYQKYFKLEPLQAYHRVISLEEFMEKLAPIHWPPEKRVAYCFEVAAQRSPDKKTCPMKEGNPFGPFWDQFHVSFNKSELFTGISFSASYKEQWIQRFPPEEHPVLALPGAPAQFPVLEEHRALQKYMVWSDEMVKTGEAQISTHLIRPYVGIHLRIGSDWKNACAMLKDGTAGSHFMASPQCVGYSRSTATPLTMTMCLPDLNEIQRAVKLWVRALNARSIYIATDSESYVPEIQQLFKEKVKVVSLKPEVAQVDLYILGQADHFIGNCVSSFTAFVKRERDLHGRQSSFFGMDRPSQPRDEF", "text": "FUNCTION: Catalyzes the reaction that attaches fucose through an O- glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP- fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DELTA1 or JAGGED1 (By similarity). Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 65 family."}
{"protein": "MNEFLPFSRPAMGPEELAAVSEVLQSGWITTGPKNQALEQAFCALTGNQHSIAVSSATAGMHVALMALGIQAGDEVITPSLTWVSTLNMIVLLGAEPVMIDVDHDTLMVTPQAIEAAITPRTKAIIPVHYAGAPVDIDAIRAVADRHGIPVIEDAAHAAGTYYKGSHVGNRGTAIFSFHAIKNMTCAEGGLIVTDDEQLANRMRSLKFHGLGVDAFDRQTLGRAPQAEVISPGYKYNLADINAAIALVQLKKLEKNNARRTEIAERYLTELANTPFLPLSQPAWAHKHAWHLFIVRVDEATCGISRNGLMDDLKAKGIGTGLHFRAAHTQKYYRERYPALVLPNTEWNSDRICSIPLFPTMTDDDVTRVIAALRDVAGY", "text": "FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily."}
{"protein": "MAFSKSLVFVLLAALLISSAVAQSPAPAPSNVGGRRISPAPSPKKMTAPAPAPEVSPSPSPAAALTPESSASPPSPPLADSPTADSPALSPSAISDSPTEAPGPAQGGAVSNKFASFGSVAVMLTAAVLVI", "text": "FUNCTION: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the classical AGP family."}
{"protein": "MSLVESDFEECLEFFSRPLPELLDGLLASLGEAGNLDSQGQRVEKAALVLELTGTECVREVVFKQEERGRLRGTEGPSRPPSSGAGDPRGATTLG", "text": "SIMILARITY: Belongs to the herpesviridae UL91 family."}
{"protein": "MPHSYDYDAIVIGSGPGGEGAAMGLVKQGARVAVIERYQNVGGGCTHWGTIPSKALRHAVSRIIEFNQNPLYSDHSRLLRSSFADILNHADNVINQQTRMRQGFYERNHCEILQGNARFVDEHTLALDCPDGSVETLTAEKFVIACGSRPYHPTDVDFPHPRIYDSDSILSMHHEPRHVLIYGAGVIGCEYASIFRGMDVKVDLINTRDRLLAFLDQEMSDSLSYHFWNSGVVIRHNEEYEKIEGCDDGVIMHLKSGKKLKADCLLYANGRTGNTDSLALQNIGLETDSRGQLKVNSMYQTAQPHVYAVGDVIGYPSLASAAYDQGRIAAQALVKGEATAHLIEDIPTGIYTIPEISSVGKTEQQLTAMKVPYEVGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIHIGQAIMEQKGGGNTIEYFVNTTFNYPTMAEAYRVAALNGLNRLF", "text": "FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MGEKPEVLDAVLKETVDLENIPIEEVFENLRCTKEGLTATAAQERLSIFGYNKLEEKKESKFSKFLGFMWNPLSWVMEAAAIMAIALANGGGKPPDWQDFVGIITLLIINSTISFIEENNAGNAAAALMARLAPKAKVLRDGKWKEEDAAVLVPGDIISIKLGDIIPADARLLEGDPLKIDQSALTGESLPVTKGPGDGVYSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAVGMIIEIIVMYPIQHRKYRPGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLAQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLTVDKYLIEVFARGVDADTVVLMAARASRTENQDAIDAAIVGMLADPKEARAGIREIHFLPFNPTDKRTALTYLDGEGKMHRVSKGAPEQILHLAHNKSDIERRVHAVIDKFAERGLRSLAVAYQEVPEGRKESAGGPWQFIALLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGQTKDESISALPVDELIEKADGFAGVFPEHKYEIVKRLQARKHICGMTGDGVNDAPALKKADIGIAVDDATDAARSASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVLGFMLLALIWQFDFPPFMVLIIAILNDGTIMTISKDRVKPSPLPDSWKLAEIFTTGVVLGGYLAMMTVIFFWAAYKTNFFPRVFGVSTLEKTATDDFRKLASAIYLQVSTISQALIFVTRSRSWSFMERPGLLLVVAFFIAQLVATLIAVYANWSFAAIEGIGWGWAGVIWLYNIVFYIPLDLXXFLIRYALSGKAWDLVIEQRIAFTRKKDFGKEQRELQWAHAQRTLHGLQVPDPKIFSETTNFNELNQLAEEAKRRAEIARLRELHTLKGHVESVVKLKGLDIETIQQAYTV", "text": "FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily."}
{"protein": "MLFLGMLKQVVNGTAQSKASSCRKLVLPLKFLGTSQHRIPADANFHSTSISEAEPPRVLITGGLGQLGVGLANLLRKRFGKDNVILSDIRKPPAHVFHSGPFVYANILDYKSLREIVVNHRISWLFHYSALLSAVGEANVSLARDVNITGLHNVLDVAAEYNVRLFVPSTIGAFGPTSPRNPAPDLCIQRPRTIYGVSKVHTELMGEYYYYRYGLDFRCLRYPGIISADSQPGGGTTDYAVQIFHAAAKNGTFECNLEAGTRLPMMYISDCLRATLEVMEAPAERLSMRTYNISAMSFTPEELAQALRKHAPDFQITYCVDPLRQAIAESWPMILDDSNARKDWGWKHDFDLPELVATMLNFHGVSTRVAQVN", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate, mediating L-threonine catabolism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MGKLIIVGTPIGNLEDITIRALKTLREVDLILAEDTRRTMVLLNKYRIKKPLLSFNERNSKKRIKEILPLLKEGKKVAIVSDAGMPVISDPGYNLVEECWREGIEVDIVPGPSALTSAVAVSGFPGSKFIFEGFLPRGKNRRRLLKSLKKENRVIVFFESPERLLSTLRDILEIIGDREVFIAREMTKLHQEFFRGKVSEAISHFEKKKPLGEITVVLSGKE", "text": "FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family."}
{"protein": "MAIVNGAVGKPQHISDMVDSTKMNGNQSQDTAGRADTPVSNGGQDYLHVFDSRTCNIHHIPVSDGFVRGSDLSTIAAPLKGSSGRMQKLAVLDPGFQHTACKESSITFIDGEKGELRYRGVRIEDLFHDHDFDSTLHLLVWGRLPTKEEKIKFERRMFEVASPPQEVCDVIRKLPKNMDFISMFLTGLSTYMGTDEEMTRSRHQAVMTYHKNLQTTDDAIIRCFSYVSATLATVYCHVKGVELHHPQEGLTLVENFLHMIGMEDPDKKISRTIDRLSINMADHELSCSTAAFLHVASSLTDPMTCLLTAISAASGPLHGGALEVCYQGLELIGSVDNVPAYIAAVKAKKFRLFGYGHRVYKIQDPRAALTKELMEEHREAIDANPLLQIAVEIDRQANTDPYFVERKLKLNADFYGCFIYIALGIPRDMIPGLLTISRMGGLMAHWREAMNNPIKIWRPMQKFKL", "text": "FUNCTION: Citrate synthase-like protein; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) (PubMed:27056201). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms (PubMed:27056201). These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase pks2, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product (By similarity). The phenylalanine ammonia lyase (PAL) M7 and the acyl-CoA ligase M9 are involved in transforming phenylalanine into benzoyl-CoA (By similarity). The citrate synthase- like protein R3 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit (By similarity). The potential hydrolytic enzymes, M8 and M10, are in close proximity to pks2 and may participate in product release (By similarity). On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase pks1 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase M4 (PubMed:11251290, PubMed:15489970, PubMed:28106181). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (PubMed:11251290, PubMed:15489970, PubMed:28106181). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (PubMed:11251290, PubMed:15489970, PubMed:28106181). The enoyl reductase and C-MeT of pks1 are not active in the final round of extension (PubMed:11251290, PubMed:15489970, PubMed:28106181). The acetyltransferase M4 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (Probable). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases M1, R1 and R2 (Probable). Finally, in support of the identification of the cluster as being responsible for SQS1 production, the cluster contains a gene encoding a putative squalene synthase (SS) R6, suggesting a likely mechanism for self-resistance (Probable). SIMILARITY: Belongs to the citrate synthase family."}
{"protein": "MSLTVEIVATKPYEGQKPGTSGLRKKVKVFTQPNYTENFVQAILEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSKLLVGQNGILSTPAVSSLIRHNKALGGIVLTASHNPGGPENDFGIKFNCENGGPAPDAFTNHIYKITTEIKEYKLVRNLQIDISKVGVTSFDIAGKPFTVEVIDSVANYVRHMEEIFDFAKLKDFVSGKATGKPLKMRIDAMNGVTGSYVREIFLNRLGATESSVVHTTPLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYLEAIPYFQKNGVQGFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTGSNHIREKDGIWAVLAWISVMQHTGKGIEDILKQHWSVYGRNYFTRYDYEECASDPCNEMVATMEKTITAPEFVGKSYSSGGKTYKVKEADNFSYTDPVDKSVATKQGLRIVFEDGSRIVVRLSGTGSSGATVRLYIDSYEKENVLGQASVMLKPLIDIALEISQLPKFTGRNAPTVIT", "text": "FUNCTION: This enzyme participates in both the breakdown and synthesis of glucose. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MSEKVNNFPPLPKFIPLKPCFYQDFEADIPPQHLSMTKRLYYLWMLNSVTLAVNLVGCLAWLIGGGGATNFGLAFLWLILFTPCSYVCWFRPIYKAFKTDSSFSFMAFFFTFMAQLVISIIQAVGIPGWGVCGWIATISFFGTNIGSAVVMLIPTVLFTVMAVFSFIALSMVHKFYRGSGGSFSKAQEEWTTGAWKNPHVQQAAQNAAMGAAQGAMNQPQTQYSATPNYTYSNEM", "text": "FUNCTION: Required for the calcium-dependent exocytosis of signal sequence-containing cytokines such as CCL5. Probably acts in cooperation with the SNARE machinery (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi- pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Note=Mainly localizes in Golgi apparatus membrane. Upon calcium-triggered exocytosis, it translocates to the cell membrane. Highly enriched in synaptic vesicles (By similarity). SIMILARITY: Belongs to the SCAMP family. SCAMP5 subfamily."}
{"protein": "MNAQKGFTLIELMIVIAIIGILAAIALPAYQDYISKSQTTRVSGELAAGKTAVDAALFEGKTPVLSEESSTSKENIGLTSSETSTKPRSNLMASVELTGFADNGAGTISATLGNKANKDIAKTVITQERTTDGVWTCKIDGSQAAKYKEKFNPTGCVKK", "text": "SUBCELLULAR LOCATION: Fimbrium. Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the N-Me-Phe pilin family."}
{"protein": "MKKLFFLLLLLFLIYLGYDYVNEALFSQEKVEFQNYDQNPKEHLENSGTSENTQEKTITEEQVYQGNLLLINSKYPVRQESVKSDIVNLSKHDELINGYGLLDSNIYMSKEIAQKFSEMVNDAVKGGVSHFIINSGYRDFDEQSVLYQEMGAEYALPAGYSEHNSGLSLDVGSSLTKMERAPEGKWIEENAWKYGFILRYPEDKTELTGIQYEPWHIRYVGLPHSAIMKEKNFVLEEYMDYLKEEKTISVSVNGEKYEIFYYPVTKNTTIHVPTNLRYEISGNNIDGVIVTVFPGSTHTNSRR", "text": "FUNCTION: Cleaves the C-terminal D-alanine residue of UDP-muramyl- pentapeptide (UDP-MurNAc-L-Ala-D-Glu-mDAP-D-Ala-D-Ala) (PubMed:1510448). However the physiological substrate likely contains L-Lys instead of mDAP at the third position of the pentapeptide (Probable). Also releases the C-terminal D-lactate from UDP-MurNAc-L- Ala-D-Glu-mDAP-D-Ala-D-lactate, a depsipeptide produced by the vancomycin resistance protein VanA. Therefore, VanY should contribute in vivo to the hydrolysis of both the D-alanyl-D-alanine- and the depsipeptide-containing peptidoglycan precursors (PubMed:1510448). Is not necessary for vancomycin resistance of E.faecium BM4147 (PubMed:1398115). Does not display transpeptidase or beta-lactamase activities (PubMed:1510448). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase M15B family."}
{"protein": "MTQAAFDQASDNGPMTPSGSSFGLFAPAVVLLALISALATFLILMGLTPVVPTHQVVISVLLVNAAAVLILSAMVGREIWRIAKARARGRAAARLHIRIVGLFAVVSVVPAILVAVVASLTLDRGLDRWFSMRTQEIVASSVSVAQTYVREHALNIRGDILAMSADLTRLKSVYEGDRSRFNQILTAQAALRNLPGAMLIRRDLSVVERANVNIGREFIVPANLAIGDATPDQPVIYLPNDADYVAAVVPLKDYDDLYLYVARLIDPRVIGYLKTTQETLADYRSLEERRFGVQVAFALMYAVITLIVLLSAVWLGLNFSKWLVAPIRRLMSAADHVAEGNLDVRVPIYRAEGDLASLAETFNKMTHELRSQREAILTARDQIDSRRRFTEAVLSGVGAGVIGLDSQERITILNRSAERLLGLSEVEALHRHLAEVVPETAGLLEEAEHARQRSVQGNITLTRDGRERVFAVRVTTEQSPEAEHGWVVTLDDITELISAQRTSAWADVARRIAHEIKNPLTPIQLSAERLKRKFGRHVTQDREIFDQCTDTIIRQVGDIGRMVDEFSSFARMPKPVVDSQDMSEIIRQTVFLMRVGHPEVVFDSEVPPAMPARFDRRLVSQALTNILKNAAEAIEAVPPDVRGQGRIRVSANRVGEDLVIDIIDNGTGLPQESRNRLLEPYVTTREKGTGLGLAIVGKIMEEHGGGIELNDAPEGRGAWIRLTLKAEGPKAEPTDASTKATGAATPAAPAASAMARDAAADSAARGKNERT", "text": "FUNCTION: Member of the two-component regulatory system NtrY/NtrX involved in nitrogen level control. Probably activates NtrX by phosphorylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MTTARRRPKRRGTDARTALRNVPILADIDDEQLERLATTVERRHVPANQWLFHAGEPADSIYIVDSGRFVAVAPEGHVFAEMASGDSIGDLGVIAGAARSAGVRALRDGVVWRIAAETFTDMLEATPLLQSAMLRAMARMLRQSRPAKTARRPRVIGVVSNGDTAAAPMVDAIATSLDSHGRTAVIAPPVETTSAVQEYDELVEAFSETLDRAERSNDWVLVVADRGAGDLWRHYVSAQSDRLVVLVDQRYPPDAVDSLATQRPVHLITCLAEPDPSWWDRLAPVSHHPANSDGFGALARRIAGRSLGLVMAGGGARGLAHFGVYQELTEAGVVIDRFGGTSSGAIASAAFALGMDAGDAIAAAREFIAGSDPLGDYTIPISALTRGGRVDRLVQGFFGNTLIEHLPRGFFSVSADMITGDQIIHRRGSVSGAVRASISIPGLIPPVHNGEQLLVDGGLLNNLPANVMCADTDGEVICVDLRRTFVPSKGFGLLPPIVTPPGLLRRLLTGTDNALPPLQETLLRAFDLAASTANLRELPRVAAIIEPDVSKIGVLNFKQIDAALEAGRMAARAALQAQPDLVR", "text": "SIMILARITY: Belongs to the NTE family."}
{"protein": "MGSLPTNNLESISLCSQNPLDPDEFRRQGHMIIDFLADYYKNVEKYPVRSQVEPGYLKKRLPESAPYNPESIETILEDVTNDIIPGLTHWQSPNYFAYFPSSGSIAGFLGEMLSTGFNVVGFNWMSSPAATELESIVMNWLGQMLTLPKSFLFSSDGSSGGGGVLQGTTCEAILCTLTAARDKMLNKIGRENINKLVVYASDQTHCALQKAAQIAGINPKNVRAIKTSKATNFGLSPNSLQSAILADIESGLVPLFLCATVGTTSSTAVDPIGPLCAVAKLYGIWVHIDAAYAGSACICPEFRHFIDGVEDADSFSLNAHKWFFTTLDCCCLWVKDSDSLVKALSTSPEYLKNKATESKQVIDYKDWQIALSRRFRSMKLWLVLRSYGVANLRTFLRSHVKMAKHFQGLIGMDNRFEIVVPRTFAMVCFRLKPTAIFKQKIVDNDYIEDQTNEVNVKLLESVNASGKIYMTHAVVGGVYMIRFAVGATLTEERHVTGAWKVVQEHTDAILGA", "text": "FUNCTION: Tyrosine decarboxylase that converts tyrosine into tyramine, a precursor of isoquinoline alkaloids and various amides. SIMILARITY: Belongs to the group II decarboxylase family."}
{"protein": "MDDICSMAENINRTLFNILGTEIDEINLNTNNLYNFIMESNLTKVEQHTLHKNISNNRLEIYHHIKKEKSPKGKSSISPQARAFLEQVFRRKQSLNSKEKEEVAKKCGITPLQVRVWFINKRMRSK", "text": "FUNCTION: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of A1 at HMR. FUNCTION: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that, in a/alpha diploid cells, binds cooperatively with the ALPHA2 protein to a 21-bp DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MATA1 family."}
{"protein": "MTSTEAAGTGKAPAIRANPALQTYYESQESYLVYEVVLRGSHHFGFYEKDTYWPFPVGRSLERMEAKLLSALALPSGSQILDAGCGFGPVAISMAKKGMRVTAIDIIDHHVTKARRNVEKAGLPKGQVTVEKMDYQHLESIASESHDDAKAAATGFFRILKPGGRIAFFEAQRSRTSGDYDEGDELAGHLKLVNEYTAMPTNELSREDYFKDLLEDAGFVDVEFTLPPGTREPREHWSYSALKA", "text": "FUNCTION: S-adenosyl-l-methionine-dependent Diels-Alderase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4- hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:31216742). IliD catalyzes the Diels-Alder reaction that converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H (PubMed:31216742). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (PubMed:31216742) (Probable). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family."}
{"protein": "MDSKESLAPPGRDEVPGSLLGQGRGSVMDFYKSLRGGATVKVSASSPSVAAASQADSKQQRILLDFSKGSTSNVQQRQQQQQQQQQQQQQQQQQQQPDLSKAVSLSMGLYMGETETKVMGNDLGYPQQGQLGLSSGETDFRLLEESIANLNRSTSVPENPKSSTSATGCATPTEKEFPKTHSDASSEQQNRKSQTGTNGGSVKLYPTDQSTFDLLKDLEFSAGSPSKDTNESPWRSDLLIDENLLSPLAGEDDPFLLEGNTNEDCKPLILPDTKPKIKDTGDTILSSPSSVALPQVKTEKDDFIELCTPGVIKQEKLGPVYCQASFSGTNIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPVFNVIPPIPVGSENWNRCQGSGEDSLTSLGALNFPGRSVFSNGYSSPGMRPDVSSPPSSSSAATGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATAGVSQDTSENPNKTIVPAALPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSAWRIMTTLNMLGGRQVIAAVKWAKAILGLRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSGNLLCFAPDLIINEQRMSLPCMYDQCKHMLFVSSELQRLQVSYEEYLCMKTLLLLSSVPKEGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLTYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK", "text": "FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:12917342). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5- dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). In response to induction by transcription factor EGR1/NGFI-A in the hippocampus, may play a role in the behavioral and hypothalamic-pituitary-adrenal responses to stress in offspring (PubMed:15220929). FUNCTION: [Isoform A]: Has transcriptional activation and repression activity. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression. SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm Nucleus Mitochondrion Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=After ligand activation, translocates from the cytoplasm to the nucleus (By similarity). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (By similarity). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily."}
{"protein": "MYSVLKQSIRPRLLATHNQFRTMITAQAVLYTQHGEPKDVLFTQSFEIDDDNLAPNEVIVKTLGSPINPSDINQIQGVYPSKPAKTTGFGTAEPAAPCGNEGLFEVIKVGSNVSSLEAGDWVIPSHVNFGTWRTHALGNDDDFIKLPNPAQSKANGKPNGLTINQGATISVNPLTAYLMLTHYVKLTPGKDWFIQNGGTSAVGKYASQIGKLLNFNSISVIRDRPNLDEVVASLKELGATQVITEDQNNSKEFGPTIKEWIKQSGGEAKLALNCVGGKSSTGIARKLNNNGLMLTYGGMSFQPVTIPTSLYIFKNFTSAGFWVTELLKNNKELKTSTLNQIIAWYEEGKLTDAKSIETLYDGTKPLHELYQDGVANSKDGKQLITY", "text": "FUNCTION: Required for respiration and the maintenance of the mitochondrial compartment. Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
{"protein": "MKPENKLPVLDLISAEMKTVVNTLQPDLPSWPATGTIAEQRQYYTLERRFWNAGAPEMATRAYMVPTKYGQVETRLFCPQPDSPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGIDYTLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKIAGVLLWYGLYGLRDSVTRRLLGGVWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL", "text": "FUNCTION: Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family."}
{"protein": "MERARRRGGGGGRGRGGKNVGGSGLSKSRLYPQAQHSHYPHYAASATPNQAGGAAEIQELASKRVDIQKKRFYLDVKQSSRGRFLKIAEVWIGRGRQDNIRKSKLTLSLSVAAELKDCLGDFIEHYAHLGLKGHRQEHGHSKEQGSRRRQKHSAPSPPVSVGSEEHPHSVLKTDYIERDNRKYYLDLKENQRGRFLRIRQTMMRGTGMIGYFGHSLGQEQTIVLPAQGMIEFRDALVQLIEDYGEGDIEERRGGDDDPLELPEGTSFRVDNKRFYFDVGSNKYGIFLKVSEVRPPYRNTITVPFKAWTRFGENFIKYEEEMRKICNSHKEKRMDGRKASGEEQECLD", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PUR DNA-binding protein family."}
{"protein": "MSSRVLTPDVVGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALDDQLYQEPQAAPVAVPMGKFAMYPDWQPDADFIRLAALWGVALREPVTTEELTSFIAYWQAEGKVFHHVQWQQKLARSLQIGRASNGGLPKRDVNTVSEPDSQIPPGFRG", "text": "FUNCTION: This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'. SIMILARITY: Belongs to the DnaT family."}
{"protein": "MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H4 family."}
{"protein": "MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC", "text": "FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. This includes the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. As part of a multisubunit ubiquitin ligase complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (By similarity). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (By similarity). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (PubMed:33590678). FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (PubMed:27863225, PubMed:27863226). FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed:7821821). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity). FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:26138980, PubMed:29779948, PubMed:30166453, PubMed:29775578). This includes the von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). By binding to BC- box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). As part of a multisubunit ubiquitin ligase complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:26138980, PubMed:29779948, PubMed:29775578). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. This includes the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. As part of a multisubunit ubiquitin ligase complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (By similarity). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (By similarity). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SKP1 family."}
{"protein": "MAGIELERCQQQANEVTEIMRNNFGKVLERGVKLAELQQRSDQLLDMSSTFNKTTQNLAQKKCWENIRYRICVGLVVVGVLLIILIVLLVVFLPQSSDSSSAPRTQDAGIASGPGN", "text": "FUNCTION: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking. SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein Endomembrane system; Single-pass type IV membrane protein Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein Note=Associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Associated with the trans-Golgi, but not with the cis-Golgi apparatus (By similarity). SIMILARITY: Belongs to the synaptobrevin family."}
{"protein": "MKKVLALVVAAAMGLSSAAFAAETTTTPAPTATTTKAAPAKTTHHKKQHKAAPAQKAQAAKKHHKNTKAEQKAPEQKAQAAKKHAKKHSHQQPAKPAAQPAA", "text": "FUNCTION: Required for growth and/or survival at acidic conditions. FUNCTION: Required for growth and/or survival at acidic conditions (pH 4.5). Needed for the adaptation process at pH 4.5 that enables cells to survive at extremely low pH (pH 2.0). SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the Asr family. SIMILARITY: Belongs to the Asr family."}
{"protein": "MSFIMKPHRHFQRTLILLATFCMVSIIISAYYLYSGYKQESEVSGRASEVDCGDLQHIPSRLMEVRRTMISDASRTDPTVLVFVESQYSSLGQDIIMMLESIRFHYHTEIAPGKGDLPALTDNVKGKYVLIIYENILKYINMDSWNRSLLDKYCIEYGVGIIGFHKTSEKNLQSFQFRGFPFSISGNLAVKDCCINPHSPLLRVTKSSKLDRGSLPGTDWTVFQINHSTYQPVIFAKVKTPENLSPPISKHAFYATIIHDLGLHDGIQRVLFGNNLNFWLHKLIFIDAISFLSGKRLTLSLDRYILVDIDDIFVGKEGTRMNTNDVKALLDTQNLLRTQITNFTFNLGFSGKFYHTGTEEEDEGDDCLLGSVDEFWWFPHMWSHMQPHLFHNESSLIEQMILNKKFALEHGIPTDMGYAVSPHHSGVYPVHVQLYEAWKKVWNIKITSTEEYPHLKPARYRRGFIHKNIMVLPRQTCGLFTHTIFYKEYPGGPRELDKSIHGGELFFTVVLNPISIFMTHLSNYGNDRLGLYTFVNLANFVQTWTNLRLQTLPPAQLAHKYFELFPDQKDPLWQNPCDDKRHRDIWSKEKTCDRLPKFLVIGPQKTGTTALCLFLIMHPSILSNSPSPKSFEEVQFFNRNNYHRGIDWYMDFFPVPSNVTTDFLFEKSANYFHSEDAPKRAASLVPKAKIITILIDPSDRAYSWYQHQRSHEDPAALKFSFYEVISAGPNAPWELRTLQKRCLVPGWYANHIERWLVYFPPFQLLIIDGQHLRTTPATVMDEVQKFLGVSPHYNYSEALTFDSHKGFWCQLLEEGKTKCLGKSKGRKYPPMDSDSRAFLSSYYRDHNVELSKLLHRLGQPLPSWLRQELQKVR", "text": "FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily."}
{"protein": "MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSAGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAASLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAHSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHLWHRRESDESGESAPDEGGEGARAPQSIPRSASYPCAAPRPGAPETTALHGGFQRRYGGITDPGTVPRAPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV", "text": "FUNCTION: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (By similarity). In addition to autophagy, also plays a role in necrotic cell death (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Multi-pass membrane protein Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Mitochondrion membrane; Multi-pass membrane protein Note=Mainly localizes to the trans-Golgi network (TGN) and the endosomal system; cycles between them though vesicle trafficking. Export from the TGN to promote formation of autophagosomes is mediated by the AP-4 complex. Under amino acid starvation or rapamycin treatment, redistributes to preautophagosomal structure/phagophore assembly site (PAS). The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1. Upon autophagy induction, a small portion transiently localizes to the autophagic membranes. Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner. SIMILARITY: Belongs to the ATG9 family."}
{"protein": "MAGKRQATSNLNHENWDLEEEPEERGTFRTATEEELKTRVIKKARRKIAGGSSAAEEDGAEEKTAEPKSVFSGFSGFGKPAASPAAGSPFSFLANVTAPATTSSSEPKKSAFSFGFSSSSSSADRPVSTSICGTASTSSTAPSPLPAKESTSTVDGAKPTTSIFGNISAAKKESSEAKTSSSSTSLTSTMETSEYRESVADLNRSVIKFLQDQMGKSPYCILTPVFKNYDEHLKDLQDEESARTNSTKSKTAQARSQEPVAKVSRASSPPKAATTFTFGKPSAPIGASVSPLAKKPNCTITSGGTTTTTATPLVSFGSTASFTAPVPSSSSIFSLTAKPTGEAKSDDTPKSSIFSFGAKDTTTKKDEPNFSAPKTNGFSFGLKSNNDDKPSTSLFAGFGKAPGGAGDGAKGFSFTNSATPFSLGNIHPPAAAAAPAEEEKEEDTPPKVEFKQVVEDDAIYSKRCKVFIKKDKDFGDRGVGTLYLKPVKDSEKIQLLVRADTNLGNILVNLILSKGIPCQRMGKNNVLMVCVPTPEDSKATSLLLRVKTGDEADDLLEKIKEHIK", "text": "FUNCTION: Component of the nuclear pore complex that has a direct role in nuclear protein import (By similarity). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta- cargo complex and importin recycling (By similarity). Binds to transcriptionally active chromatin sites when located in the nucleoplasm and is involved in transcriptional activation (PubMed:20144760). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus envelope Chromosome Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side Note=Associates with chromatin (PubMed:20144760)."}
{"protein": "MRQLISSENTMQKTSFRNHYVKRFSSRQASKSRKENQPKRVVLFNKPYDVLPQFTDEAGRRTLKDFIPVQGVYAAGRLDRDSEGLLVLTNDGALQARLTQPGKRTGKIYYVQVEGIPDNAALQALRTGVTLNDGPTLPAGIEIVAEPDWLWPRTPPIRERKNIPTSWLKVTLYEGRNHQVRRMTAHVGHPTLRLIRYSMGDYTLNGLDNGQWCEIAQEKDR", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family."}
{"protein": "MGIKGLKPLLRSYGVHEYTVPLSQMSGKTIAVDGTFLLHKYKNCHSVPWHYLTLYTLSNLRLRNVKVLFIFDGMSPPEKSREKSNRRCRKQALMEKGTLVKAQLEVWKKDGGEQAPELAAVSERLVKTRGLDPSLTDPETVQVLTDYVDNMSRDTRVTSDDYELMRRSLDAFGFPYADAPDEAELCCVRVVQMGIADAPMTIDSDALACGALHGVDVVYTDLHGETLTAMSTSKSKEALGLNGEQFMDLCVMCGTDFNQRVHKLGPVTALKLIKAHGSIENIPSAAPSMSCLEAVRTREILSGGDMESRRKDYEAMVQKPVSAELIRSVFPPEFLDKLLHENWQLRDAMKRMAPEAFEKCKRK", "text": "FUNCTION: Probable endonuclease. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family."}
{"protein": "MAAKRGLAKQKSRVTKACDRCHRKKIKCNSKKPCFGCIGSQSKCTYRNQFREPIEAFFNYTGSLSNDLDNAKCSIAKLKAQLPPSAPASLQKGLANICTELEKIQPQLYLNLDSKEISSYGGLKSIETEIIGKQSKSLNRFSNAFESNTAQNVSMYFGVYSPLLYFASTGISWITKKLISCSNDRETRETIYLFLKFLDASSASHAGPKVTSISPLEYYSKLNGLSCGNDVLIQHIMSNISNEIKGNTNINQTIKFNKPTDWFMYGVQLMEQHHKALDRKSSKKLLPLKYFLEQDELIFCLCLEYFERSLFSTMYDLTILKGLVSLMKHRYWIDDPFVLGRIISTMSRRSLDAGLNRWEYYIGQDEDTAEEYRKLWWDCYWWDRWYSLVTGKQPLIPHEMTSCLFPKDVVGLGVDDSMDCFTLINLVELDPSKFDICISFGYILLTKIITAVFSGLLYNRHFTDYRLFATPNAKDLNGTARQLMVEFSKICKIFQCIQDKLIPFLKQYSENSNVFELYTHFGFAKVCCFQGMESLILRIQNLLQERERIELDSCVKDIRLQTFEASVDILTDVLKHEDTFYIFRCSWFIYAILMNITLNFIETPRRNSICYLSLMCRMIASYNDLFVSSGNVNFKGNNAFSKKLENGTAVSFILTRICCQMYTRSQKMAKESLFCELKKYGQACSDAGQAALDIECIWYRNIIGEHKESSFRKEILSILDREMGDLVNNRVIGVQGKNQEGACYEKLSPSSTSVSVGMDFCSLENFVTAESLPDLLNLFWEDTEFGITKENLGE", "text": "FUNCTION: Transcriptional activator required for growth on non- fermentable carbon sources and that regulates genes involved in fatty acid utilization (PubMed:11353088, PubMed:24998441). Acts as a direct activator that binds the promoters of oleate utilizing genes, encoded key enzymes in beta-oxidation and NADPH regeneration (POX1, FOX2,POT1 and IDP2), the glyoxylate shunt (MLS1 and ICL1), and gluconeogenesis (PCK1 and FBP1) (PubMed:24998441). Regulates also the abundance of peroxisomes that are vital for fatty acid oxidation (PubMed:24998441). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MATSSQLLPNGNLSRNGKTKTEDGEEVEAVVGARAAGADAGVALTGRLTGHPSTSGTFMKLKTYLLALRPWSLSASLVPTLLGSALAYRSQWAEEFSLATFFLTAFTVVTVHCAGNVVNTYFDFIKGIDKQKADDRTLVDHILTKDEVVSLGAILYMAGCGGFVLLAVLSPAKMEHLALIYFGGLSSSFLYTGGIGFKYIALGDLVILILFGPISVLFAFMSQTGHLDWTTMGYAIPLALNTEAILHSNNTRDADNDRRAGIVTLAILIGRTASHVLYAMLLFAPYSLFFIFGLKYSLWFLLPLVTLPQAFQIEKRFRNEQTMHLVPRQTAKLNFFFGILYVVACCCAHQLPTFGLRRN", "text": "FUNCTION: Prenyltransferase that mediates the formation of menaquinone- 4 (MK-4), a vitamin K2 isoform, thereby acting as a mitochondrial electron carrier. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. MK-4 acts as a membrane electron carrier downstream of a electron transport chain complex, improving mitochondrial oxygen consumption. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
{"protein": "MELEGRSAGGVAGGPAAGPGRSPGESALLDGWLQRGVGRGAGGGEAGAYQPPVRLDPESGPEYEALPAGATVTTHMVAGAVAGILEHCVMYPIDCVKTRMQSLQPDPAARYRNVLEALWRIMRTEGLWRPMRGLNVTATGAGPAHALYFACYEKLKKTLSDVIHPGGNSHIANGAAGCVATLLHDAAMNPAEVVKQRMQMYNSPYHRVTDCVRAVWQNEGAGAFYRSYTTQLTMNVPFQAIHFMTYEFLQEHFNPQRRYNPSSHVLCGACAGAVAAAATTPLDVCKTLLNTQESLALNSNITGHITGMASAFRTVYQVGGVTAYFRGVQARVIYQIPSTAIAWSVYEFFKYLITKRQEEWRAGK", "text": "FUNCTION: Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MLGLPERRLPSAEFLLLLPFLLLLLLLLPAAPAPHRAAYKPVIVVHGLFDSSYSFRHLLEYINETHPGTAVTVLDLFDGRESLRPLWEQVQGFREAVAPIMAKALQGVHLICYSQGGLVCRALLSVMDEHNVDSFISLSSPQMGQYGDTNYLKWLFPTSMRSNLYRICYSPWGQEFSICNYWHDPHHDDLYLNASSFLALINGERDHPNATAWRKNFLRLGRLVLIGGPDDGVITPWQSSFFGFYDANETVLEMEKQLVYLRDSFGLKTLLARGAIVRCPMAGISHTAWHSNRTLYETCIEPWLS", "text": "FUNCTION: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins (By similarity). SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the palmitoyl-protein thioesterase family."}
{"protein": "MAPNATTKKRAAAKDDDFVLTLSDDENDVLENGVEEDTLSSSKKRKRDAAEAPKGKNKKQKQLKKSKKGESAAGAVSDDQSGEEDEAEAMDAGEDDGALDSEFEFDVGGNANTGVIEGFDGWEARNGAGPADAPKNGDKKAVDIDDIISRRKAKKEAELKKKQQKEKKRREEEGEEESEDEDADSDGGMSVDFQDDELLAADGFGMGADGADESGDDVENDSNDSDDADEKGSEDEESDDDAAASDNDSVATPVHHPDDEAASDEESEAESEVDAEEAEKRKAFFAPEEKSTAASTSNRSFQDFNLSRPILRGLASVNFTTPTPIQQKTIPVALLGKDIVGSAVTGSGKTAAFVVPILERLLFRPRKVPTSRVAILMPTRELAVQCYNVATKLATHTDITFCQLVGGFSLREQENILKKRPDVIIATPGRFIDHMRNSPSFTVDTLEILVLDEADRMLEDGFADELNEILTTIPQSRQTMLFSATMTDSVDKLIRVGLNRPVRLMVDSKKNTSMNLTQEFVRLRPGREDKRLGYLLYLCNEIYTGRVIVFFRQKREAHRVRIVFGLLGLKAAELHGSMSQEQRIKSVENFREGKVAFLLATDLASRGLDIKGVETVINYEAPQSHEIYLHRVGRTARAGRSGRACTIAAEPDRKIVKSAVKAGKAQGAKIVSRVVDPAVADEWAAKAKGLEDEIEEVLQEEKLEKQMAQAEMQVTKGENMIKHEAEIMSRPKRTWFETERDKRAARKLGATELNGPSKKDKVKLSNKDKKRLDDARQRHEGNIGWKKGKADREAPKQGKNKGSKNKSDKKNNIKMKGKK", "text": "FUNCTION: ATP-binding RNA helicase involved in ribosome assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1 subfamily."}
{"protein": "MAPKVVDRRNTMPQLQAKSLEMRTPQATKTAVLVIGGAEDKVHGREILRTFFGRAGASKAYITIIPSASREPAIIGGRYIRIFEEMGAEKVEILDIREREQCESSQVKASLEACSGVFLTGGDQLRLCGVLSDTPVMEIIRQRVRGGQLTLAGTSAGAAVMGHHMIAGGGSGETPNRSLVDMATGLGLIPEVIVDQHFHNRNRMGRLISAVAAHPDRLGIGIDEDTCAVFERDGWLQVLGKGSVTIVDPTELTHTNEPHVGANEPLTVHNLRLHILSYGDRFHLYQRTVLPAVHRISS", "text": "FUNCTION: Exopeptidase that catalyzes the hydrolytic cleavage of multi- L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides. SIMILARITY: Belongs to the peptidase S51 family."}
{"protein": "MALAAARRVLLQAGSRLGRRGAVDGARRFSNKRVLVEKEGEAGIAVMKFKNPPVNSLSLEFLTEFVISLEKLENDKSIRGVILTSERPGIFSAGLDLMEMYGRNPAHYAEYWKAVQELWLRLYLSNLTLISAINGASPAGGCLMALTCDYRIMADNSKYTIGLNESLLGIVAPFWLKDNYVNTIGHRAAERALQLGTLFPPAEALKVGLVDEVVPEDQVHSKARSVMAKWFTIPDHSRQLTKSMMRKATADNLIKQREADIQNFTSFISRDSIQKSLHVYLEKLKQKKG", "text": "FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MGGGVSVELPKRDPPPGVPTDEMLLNVDKMHDVIAPAKLLEYVHIGPLAKDKEDKVKKRYPEFRLVNTGPGGLSALLRQSYNGTAPNCCRTFNRTHYWKKDGKISDKYEEGAVLESCWPDVHDTGKCDVDLFDWCQGDTFDRNICHQWIGSAFNRSNRTVEGQQSLINLYNKMQTLCSKDASVPICESFLHHLRAHNTEDSKEMIDYILRQQSADFKQKYMRCSYPTRDKLEESLKYAEPRECWDPECSNANVNFLLTRNYNNLGLCNIVRCNTSVNNLQMDKTSSLRLSCGLSNSDKFSTVPVNRAKVVQHNIKHSFDLKLHLISLLSLLVIWILIVAI", "text": "FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the mature virion (MV) membrane. The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. SIMILARITY: Belongs to the orthopoxvirus OPG086 family."}
{"protein": "MDLKTAVFNAARDGKLRLLTKLLASKSKEEVSSLISEKTNGATPLLMAARYGHLDMVEFLLEQCSASIEVGGSVNFDGETIEGAPPLWAASAAGHLKVVQSLLNHGASVNNTTLTNSTPLRAACFDGHLEIVKYLVEHKADLEVSNRHGHTCLMISCYKGHKEIAQYLLEKGADVNRKSVKGNTALHDCAESGSLDIMKMLLMYCAKMEKDGYGMTPLLSASVTGHTNIVDFLTHHAQTSKTERINALELLGATFVDKKRDLLGALKYWKKAMNMRYSDRTNIISKPVPQTLIMAYDYAKEVNSAEELEGLIADPDEMRMQALLIRERILGPSHPDTSYYIRYRGAVYADSGNFKRCINLWKYALDMQQNNLDPLSPMTASSLLSFAELFSFMLQDRAKGLLGTTVTFDDLMGILCKSVLEIERAIKQTQCPADPLQLNKALSIILHLICLLEKVPCTLEQDHFKKQTIYRFLKLHPRGKNNFSPLHLAVDKNTTCVGRYPVCKFPSLQVTAILIECGADVNVRDSDDNSPLHIAALNNHPDIMNLLIKSGAHFDATNLHKQTASDLLDEKEIAKNLIQPINHTTLQCLAARVIVNHRIYYKGHIPEKLETFVSLHR", "text": "FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1C) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg- Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation. The CRL2(FEM1C) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding. SIMILARITY: Belongs to the fem-1 family."}
{"protein": "MKCAGQIEARAVEESSINLDPIQAAGRLTPEAMKAVIAWGDGYSVCDNCHKPFRLDYVTKPPIADFHEEAAKWLGMDKIQLVPGARRAFQEVTGALVGKGEPVIMTGMGHYTAYLSVEVVNGVVREIRPTADHHITADAAAESIENAVREFGYAPKLVFVDAVDFMYGNMHEVEKIAKVAHQYDIPVLYNGVYTVGVLPVDGKKLGVDFVVGSGHKSMAAPAPSGILATTDEYAEIVLRTTKIQGDITGRKFGIKQVGILGCSLMGDPAVGLIASFPRVKERVNHFDEELKNHKIVTDALLSIEGTKVASEYPRKHTLTRMDTAGSFDVIARTHKKRGFFLSSALNKRGITGIMPGVTKQWKFNTYGLTKTQAEYLADSFIEIAEENSMVVG", "text": "FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). SIMILARITY: Belongs to the SepCysS family."}
{"protein": "MGEYIVTKTLNNNVVVCTNNDQEVILIGKGIGFNKKEGMTLNDQTITIEKIYKLESEQQKAHYKSLVEIADDNVLQVIIDSLNFISNTAMNVDSKQLVVSLTDHIIFAYKRLKQNQVISNPFVMETMQLYSDAYHIAKQVIDQLNAALDVHFPEDEIGFIALHIASNTEDLSMHEMTLINNVIKKGIDIIESDLVTTVDKESLQYQRFIRHVQFLIRRLRRKEYIHAQDDFVSMIKNHYPICYNTAYKILTMIQKQFDVNISESEIIYLTLHIHHFEERINQS", "text": "SIMILARITY: Belongs to the transcriptional antiterminator BglG family. GlcT subfamily."}
{"protein": "MDSFRKRGRRDSESLPFESENSSLGATPLSLPPSSPPPEFSDEAAEALVEEDIEDLDGEALDVEDEEGEDLFGEGMERDYQQNLELDRYDIEELDDDNDLEELDIGARRAVDARLRRRDIELDAAAGRTKPAAFLQDEDDDLDSNLGTGFTRHRHRIYDEYSPNVGALDESGELPLESIADVKADSIAEWVTLDPVRRTIAREFKNFLLEYTDENGTSVYGNRIRTLGEVNAESLMVNYAHLGESKPILAYFLANAPAPIFRIFDRVALEATLLHYPDYERIHSDIHVRITNLPTCFTLRDLRQSHLNCLVRVSGVVTRRTGLFPQLKYIRFTCTKCGATLGPFFQDSSVEVKISFCHNCSSRGPFVINSERTVYNNYQRITLQESPGTVPSGRLPRHREVILLADLVDVAKPGEEIDVTGIYRNNFDASLNTKNGFPVFATIIEANHISQLDGSGNTDDDFSLSRLTDDEEREIRALAKSPDIHNRIIASMAPSIYGHRSIKTAIAAALFGGVPKNINGKHKIRGDINVLLLGDPGTAKSQFLKYVEKTAHRAVFATGQGASAVGLTASVRKDPITNEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCTIIAAANPIGGRYNTTIPFNQNVELTEPILSRFDILQVVKDTVNPEIDEQLANFVVSSHIRSHPAFDPNMDVLKKVPTETGIDAKPIPQDLLRKYIHFAREKVFPRLQQMDEEKISRLYSDMRRESLATGSYPITVRHLESAIRLSEAFAKMQLSEFVRPSHIDKAIQVIIDSFVNAQKMSVKRSLSRTFAKYLI", "text": "FUNCTION: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Plays an important role in DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MCM family."}
{"protein": "MKYIKIYILRNKKFKNQNINFLKIKPFNCPNYNFFGNEIRRSLLLNIKKTMTITNIKFFISKSKSKHPKKLKIFHPVNEFFDIEEIKENLSNICINLKKLRFKFNPKNNKEKKTFIILNSFNKKSFSAKDIIIPSTSNLKIVNLKEHLFNKISQKINLKVLIKIENNENYFYNPIKRINFILEKNNNIGKYIILDLNSDININPFKAFIESLKYLNLNNT", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the RNA polymerase alpha chain family."}
{"protein": "MVAEAGSMPAASSVKKPFGLRSKMGKWCRHCFPWCRGSGKSNVGTSGDHDDSAMKTLRSKMGKWCRHCFPWCRGSGKSNVGTSGDHDDSAMKTLRSKMGKWCCHCFPCCRGSGKSKVGPWGDYDDSAFMEPRYHVRREDLDKLHRAAWWGKVPRKDLIVMLKDTDMNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNILDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTVLILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSRHNVICQLLSDYKEKQILKVSSENSNPEQDLKLTSEEESQRLKGSENSQPEEMSQEPEINKGGDRKVEEEMKKHGSTHMGFPENLPNGATADNGDDGLIPPRKSRTPESQQFPDTENEQYHSDEQNDTQKQLSEEQNTGILQDEILIHEEKQIEVAENEF", "text": "SIMILARITY: Belongs to the POTE family."}
{"protein": "MAAGPRNSVLLAFALLCLPWPQEVGTFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRGGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF", "text": "FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MEICRGLGSHLICLLLFLFHSETVGRPSGRKPSKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVPIEPHALFLGIHGGKMCLSCVKSGDETRLQLEAVNITDLSKNRKQDKRFAFVRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDKGVMVTKFYFQEDE", "text": "FUNCTION: Anti-inflammatory antagonist of interleukin-1 family of proinflammatory cytokines such as interleukin-1beta/IL1B and interleukin-1alpha/IL1A. Protects from immune dysregulation and uncontrolled systemic inflammation triggered by IL1 for a range of innate stimulatory agents such as pathogens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-1 family."}
{"protein": "MSTLGMMLLILLLLVPLATFADDGPTMRGHRSAKLLAHTTRDSCPSGTNCPSKICCNGNCCSKSSCRCETNQATKERVCVC", "text": "FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin N superfamily."}
{"protein": "MYHVPEMRLHYPLVNTQSNAAITPTRSYDNTLPSFNELSHQSTINLPFVQRETPNAYANVAQLATSPTQAKSGYYCRYYAVPFPTYPQQPQSPYQQAVLPYATIPNSNFQPSSFPVMAVMPPEVQFDGSFLNTLHPHTELPPIIQNTNDTSVARPNNLKSIAAASPTVTATTRTPGVSSTSVLKPRVITTMWEDENTICYQVEANGISVVRRADNNMINGTKLLNVTKMTRGRRDGILRSEKVREVVKIGSMHLKGVWIPFERAYILAQREQILDHLYPLFVKDIESIVDARKPSNKASLTPKSSPAPIKQEPSDNKHEIATEIKPKSIDALSNGASTQGAGELPHLKINHIDTEAQTSRAKNELS", "text": "FUNCTION: Putative transcription factor that functions in pseudohyphal growth. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EFG1/PHD1/stuA family."}
{"protein": "MSQATSMRKRHRFNSRMTRIVLLISFIFFFGRFIYSSVGAWQHHQSKKEAQQSTLSVESPVQR", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein."}
{"protein": "MFSDLRKKFVFLTMSILIVVVLFLFAVSNRYNQYWDEYDAYRIVKLVAKNDYLGIPGDEPIALVTIDNQKMVKIQSNNTDLTNDVIEKSSLKLLEQGKKSRKWKSFIYSIKEYKDKTYTIAIMDLASYEVPYARRFLILVFTIFGFCLLAAVSLYLSRFIVGPVETEMTREKQFVSDASHELKTPIAAIRANVQVLEQQIPGNRYLDHVVSETKRMEFLIEDLLNLSRLDEKRSKVNFKKLNLSVLCQEVLLTYESLAYEEEKCLNDTIEDDVWIVGEESQIKQILIILLDNAIRHSLSKSAIQFSLKQARRKAILTISNPSAIYSKEVMDNLFERFYQAKDDHADSLSFGLGLSIAKAIVERHKGRIRAYQEKDQLRLEVQLPIDGFWTNTMIN", "text": "FUNCTION: Member of the two-component regulatory system DltS/DltR. Regulates the expression of the dlt operon. Probably phosphorylates DltR (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MTIAPMANDLEDFESLLEPDFDAKQFGNDLLKATNNNDTTILDLNTPLKKLNYDLHEIDSRIDQLMNSNPLEIIELIYKNEHVNSTIVGELKPSLGYMNMSYDRLKNQVLDPYERARKVQLALSKVYQTSFLLRGALLYIHLSNKLNALSKTAQLSTSTAINLASLHYQLEITLEENKNLKSLRKIKQLDQDIVSPNKRELITFLSLQMCKECLNSIKIKSNKEIISQLAYSLYLLSSQEFESAINKIVLSNVTMSSQILSKILNSIRMFPDAFNEVVEKGYNIYILETLLQNIKTDNVTNSSRSIAANKSRLGNLLSEYTSMKSKAGSGTPRDLFWSKVSSAFKKDFDISVNRGGPVGKSLLKNKDFIINTMKQSMKKSSDNSDYQSYLDVMLNSVSISLNK", "text": "FUNCTION: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the COG5 family."}
{"protein": "MAASRSLVPDRLRLPLCFLGVFVCYFYYGILQEKITRGKYGEGPKQETFTFALTLVFIQCVINAMFAKILIQFFDTARVDRTRTWLYAACSVSYVGAMVSSNSALQFVNYPTQVLGKSCKPIPVMLLGVTLLKKKYPLAKYLCVLLIVAGVALFMYKPKKVVGIEEHTVGFGELLLLMSLTLDGLTGVSQDHMRAHYQTGSNHMMLNINLWSTFLLGAGILFTGELWEFLSFAERYPTIIYNILLFGLTSALGQSFIFMTVVYFGPLTCSIITTTRKFFTILASVILFANPISSMQWVGTVLVFLGLGLDAKFGKGTKKTSH", "text": "FUNCTION: ATP:ADP antiporter that catalyzes the exchange of ATP and ADP across the endoplasmic reticulum (ER) membrane. Imports ATP from the cytosol to the ER lumen and exports ADP in the opposite direction. Regulates ER energy metabolism and protein biogenesis. Appears to be part of a calcium-dependent ER to cytosol low energy response axis, where calcium efflux from ER to the cytosol triggers ATP import into the ER lumen to maintain sufficient ATP supply. Provides ATP to ER chaperone HSPA5 that drives protein folding and trafficking in the ER. Can transport dATP, UTP or UDP in exchange for ATP, but the physiological relevance of this process remains to be established. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily."}
{"protein": "MSGTDRSQAAGAVPDSDPGLAAVSSAYQRFEPRAYLRNNYAPPRGDLSCPDGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTIYQLLSACAHFEDITMTDFLEVNRQELRLWLREEPGAFDWSVYSQHVCLIEGKGESWQEKECQLRARVKRILPIDVHRPQPLGAGGLAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLAVVPVREEEVREALVRTATRCGICARTPMPAHLQTGVDDVKGIFFTRAQKKVGV", "text": "FUNCTION: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor (PubMed:5412063). Other substrates include phenylethanolamine and octopamine (By similarity). Also methylates normetanephrine (PubMed:13863458, PubMed:5412063). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family."}
{"protein": "MSFKKSLKMGENLASESDLLSMISEYLKFGEFEETARTFEKEVKRKGKPALKSAGASRRDSKIISIYEDFLSSFNDGDYKVFSELWAKNIPPEIRDFDPVAQKLEFYLQIHFTIYPLKSPLGSHDKAEFDSRITHFRHYLETRGAALSQTTEFLPFYALPFVPNPMVHPSFQELFQDSWMPDLRDRMEKFLTVTLKASNTPRLLALYNDAGKGNKEAIQQMQLQLTEAERKSAVHIRRFAKLQADHHNLIGVTAELVDSLEATVRGKMISPEYLQGVCVRLFSGNMRQSAAQSLDFTRPGTASSMLRASVAPQRPKDVPLLPSLDYEKLKKDLLTGSDRLKALLLQALRWRLTRSLHGEQRDTVLQAFISNDLLERYSNKQKTVLHLIKCKNEIVRQYTARLINAFASLCDGRLYLSQIPALLPFLLDCLKTEEKESVTRENVLAALQKLSLRRAQQSAMIRDGLIGWLVKELNDSDCLSDYTLEYAISLLMNLCLRTQGKKRCAEEAKYVLKVLTELLGHENHEIRYYVNGALYSILSVPEIREEAKQMSMEEILRCYNKEENPELNRQIEFIIKQLNSATIPEQEPESDDEEDEDDDDDEEDVMEADLDKEEVLQPQPKELSGESLLTTEYLGIMTNMMKTKRRSCPPSSRSIDEPLQRPVTPSSHKNTIAGGEGVYPVTRQRSEDSRFSSRPATRTGSRPSTAESIHQTLATDSDCWRSSVESGLMGSPERHVPAPGQTTNSVQSYSGHMVGFASRPKIPRTPDSDAGSAGRSRLPPLAPQFSNSEPQQSGSRPGSAGGSSGRPSQQSSQSNRK", "text": "FUNCTION: Involved in ciliogenesis (PubMed:28625504). It is required for appropriate acetylation and polyglutamylation of ciliary microtubules, and regulation of cilium length (By similarity). Acts as a positive regulator of hedgehog (Hh) signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Cell projection, cilium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localized to the proximal region in cilia. Stimulation of Hh signaling leads to redistribution of ARMC9 toward the ciliary tip within 6 hours, follow by a gradual return to its original proximal location (By similarity). Localizes to the daughter centriole of the primary cilium in RPE1 cells (By similarity)."}
{"protein": "MKFIFSKSIIIATAFFLFILSQLPAVFLNFLNSNGDTYGIAHKNTPPFIILTLVVVTICIFIGIKCGFYQNYRKSLEWKNILLIFSLLIITFFIQKFVVQFITSHNLYNVSHQITNQMKVENILSSLLFPGQFVAVSILAPILEESIYRACFYKLFGYYRWTFFLSCFFFSYVHSGFSWDILGYLPLSIALTYVYHRRQVLTDSILLHALFNTLLFVF", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0177 family."}
{"protein": "MTEFELPPKYITAANDLRSDTFTTPTAEMMEAALEASIGDAVYGEDVDTVRLEQTVARMAGKEAGLFCVSGTLSNQIAIRTHLMQPPYSILCDYRAHVYTHEAAGLAILSQAMVVPVVPSNGDYLTLEDIKSHYVPDDGDIHGAPTRLISLENTLHGIVYPLEELVRIKAWCMENGLKLHCDGARIWNAAAQSGVPLKQYGEIFDSISICLSKSMGAPIGSVLVGNLKFVKKATHFRKQQGGGIRQSGMMARMALVNINNDWKSQLLYSHSLAHELAEYCEAKGIPLESPADTNFVFINLKAARMDPDVLVKKGLKYNVKLMGGRVSFHYQVTRDTLEKVKLAISEAFDYAKEHPFDCNGPTQIYRSESTEVDVDGNAIREIKTYKY", "text": "FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. SIMILARITY: Belongs to the threonine aldolase family."}
{"protein": "METEYSKRVYQGVRVKHTVKDLLAEKRLRQTNTPRFSTSSSSSQPAFVPMPGSHVLPGYYSMRRSFLQDSELCHTVKQYSSDTYSSALGSKAFSYDHASTYPAFIDSYYTPDSYGDYRGPTSYTTSGGSLFPPSSLPTLLPTLSGESSSHLLLRDPWDQPSEDSVNQTEVLCPEAAAPVADSPSLAGPDSGSSSPYRLTSGRSGSSIPSSSQPYTLQPLEDVPYTAPSYTSASSYSCPPYMSTPGDLAVVKMTAVTSEEASGGVVSLSDTTSWAKDDGTGSWLSYETRRAF", "text": "FUNCTION: Transcriptional coactivator that may regulate cell type- specific differentiation pathways. SIMILARITY: Belongs to the POU2AF family."}
{"protein": "MTSSADLTNLKELLSLYKSLKFSDSAAIEKYNSLVEWGTSTYWKIGVQKVANVETSISDYYDEVKNKPFNIDPGYYIFLPVYFGSVFIYSKGKNMVELGSGNSFQIPDDMRSACNKVLDSDNGIDFLRFVLLNNRWIMEDAISKYQSPVNIFKLASEYGLNIPKYLEIEIEEDTLFDDELYSIIERSFDDKFPKISISYIKLGELRRQVVDFFKFSFMYIESIKVDRIGDNIFIPSVITKSGKKILVKDVDHLIRSKVREHTFVKVKKKNTFSILYDYDGNGTETRGEVIKRIIDTIGRDYYVNGKYFSKVGSAGLKQLTNKLDINECATVDELVDEINKSGTVKRKIKNQSAFDLSRECLGYPEADFITLVNNMRFKIENCKVVNFNIENTNCLNNPSIETIYGNFNQFVSIFNIVTDVKKRLFE", "text": "FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity). FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein OPG116 (PubMed:20861259). Serves as a bridge which links the DNA polymerase OPG071 and the uracil DNA glycosylase (PubMed:11711620). SIMILARITY: Belongs to the orthopoxvirus OPG148 family. SIMILARITY: Belongs to the poxviruses A20 family."}
{"protein": "MPSTGTLVIIFAIVLILCIMLLFFYKTVEAEKPGVLPPPIPPPTPPPSKKKYDHNEYMEKTDLEPEVKKNHRKWANEAEHLISSSVKGLENLDETAFLANHKGHGFRTFEHAKSLFKEFLKKY", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein Virion. SIMILARITY: Belongs to the asfivirus CP123L family."}
{"protein": "MKNSVGISIATIVAIIAAIYYVPWYEHFERKSPGAGEMRDRIESMFLESWRDYSKHGWGYDVYGPIEHTSHNMPRGNQPLGWIIVDSVDTLMLMYNSSTLYKSEFEAEIQRSEHWINDVLDFDIDAEVNVFETTIRMLGGLLSAYHLSDVLEVGNKTVYLNKAIDLGDRLALAFLSTQTGIPYSSINLHSGQAVKNHADGGASSTAEFTTLQMEFKYLAYLTGNRTYWELVERVYEPLYKNNDLLNTYDGLVPIYTFPDTGKFGASTIRFGSRGDSFYEYLLKQYLLTHETLYYDLYRKSMEGMKKHLLAQSKPSSLWYIGEREQGLHGQLSPKMDHLVCFMGGLLASGSTEGLSIHEARRRPFFSLSLERKSDWDLAKGITDTCYQMYKQSSSGLAPEIVVFNDGNIKQDGWWRSSVGDFFVKPLDRHNLQRPETVESIMFMYHLSHDHKYREWGAEIATSFFENTCVDCNDPKLRRFTSLSDCITLPTKKSNNMESFWLAETLKYLYILFLDEFDLTKVVFNTEAHPFPVLDEEILKSQSLTTGWSL", "text": "FUNCTION: Involved in glycoprotein quality control as it is important for the targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations it further trims the carbohydrates to Man(5)GlcNAc(2). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 47 family."}
{"protein": "MEETHDDRCMSRGDLYAYMRELINDKKWNFNLKNVWAHVHDSEFDTIRGYIRDHLDDAIIIHKDLRYKRLCHHRARIENLLKLNQSLKKEYENSISRYNGAAQESATRRNVPVRDKQRRAVAAAADRIDRKATRHCKSNRERTV", "text": "FUNCTION: Involved in late/very late gene activation. SIMILARITY: Belongs to the baculoviridae LEF-11 family."}
{"protein": "MGQTVTTPLSLTLGHWKDVERIAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDLITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLPPSAPSLPLEPPLSTPPRSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGNGGEATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRTGGNGQLQYWPFSSSDL", "text": "FUNCTION: Capsid protein p30 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). SUBCELLULAR LOCATION: [Matrix protein p15]: Virion. SUBCELLULAR LOCATION: [Capsid protein p30]: Virion."}
{"protein": "MFLMVEKKPVPEDWPHIVGDYVVGDEESPVAVVTLGSHMEDEPVKAGAAISGPLHTENLGIEKVVGNVIANPNLRFLVVCGAEVMGHITGQTMKALHSNGVDLETGRIIGATGAIPYIENMPEEAIERFRRQVELVDMVDVEDPDSIAARIQECVVHDSGAMEEEPLILKVPEIGKGDSEENT", "text": "FUNCTION: Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MtrA family."}
{"protein": "MLGTRNIPTTSGLPLPPPSSSLSAYIFPTILAIIFAVFALVAIHITTPEPFCTIHIDGASITITNCPDPAAILNKVAIGPWRGLSYHNNLK", "text": "FUNCTION: Plays a role in viral cell-to-cell propagation, by facilitating genome transport to neighboring plant cells through plasmosdesmata. May induce the formation of granular vesicles derived from the Endoplasmic reticulum, which align on actin filaments (By similarity). SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the Tymovirales TGBp3 protein family."}
{"protein": "MAGEQKPSSNLLEQFILLAKGTSGSALTALISQVLEAPGVYVFGELLELANVQELAEGANAAYLQLLNLFAYGTYPDYIANKESLPELSTAQQNKLKHLTIVSLASRMKCIPYSVLLKDLEMRNLRELEDLIIEAVYTDIIQGKLDQRNQLLEVDFCIGRDIRKKDINNIVKTLHEWCDGCEAVLLGIEQQVLRANQYKENHNRTQQQVEAEVTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKMSKVKGLVSSRH", "text": "FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF- type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily."}
{"protein": "MKLLLSGMLAGYILASSILSMTTGTPRMPAISRETLHLVGYSSKMKIPNVVCINSRYLSSEGGWVKRSVNYMFPIDKPWRGKSSTVEVKWEPYAVLLHMKTSYDVSRDLQTKSQYVVRNYDDNSLVLSDLNEVSSCSLWVTKEYLDKIPETTNRTFYHLCPDPVYTPFDENCYVN", "text": "FUNCTION: Salivary tick protein that modulates host immune response. This protein blocks dendritic cell (DC) differentiation from monocytes (PubMed:23825947). In addition, it inhibits up-regulation of costimulatory molecules and pro-inflammatory cytokines in response to stimuli and promotes up-regulation of co-inhibitory molecules and the anti-inflammatory cytokine interleukin-10. It has a pocket to accomodate cholesterol, which may have immune-modulatory roles, either directly or through interactions with the host gut microbiota (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MRRSRFVAQVFSDVTFADASTISAPIFTMSTRAPYRGARGRGRGRGGRSFSDRPYNDDAGRDQFVTGDSHFQSVHDANFRFRHGEPYRQHQPPLDQRQQPPFNQNYEFRPPPPSRGQWQQFRQPNQFPSNQNYAACPPPPFYQNQMSRPPPQQSFRQRPRSKPSDYREWEYAKTPPSPGSEKFVVLSYNILADYLANDHWRSLYFHIPRNMLSWGWRKSKLVFELSLWSADIMCLQEVDKFQDLEEEMKHRGYSAIWKMRTGNAVDGCAIFWRSNRFKLVHEESIQFNQLGLRDNVAQICVLETLLTSHTKENETPPPESSAGSHRVVICNIHVLFNPKRGDFKLGQVRTLLDKAHAVSKLWDDAPIVLCGDFNCTPKSPLYNFISDRKLDLSGLARDKVSGQVSAEFRPPRPENYTTRYQSANKSPQGQVQPPNLITNAHMENNSNIDVGTAPSEKTSELPCGDTILAGHEATSSSDQVLPCENMASDCQFGIENRKPDDSGNLSTAEDLSSLTISDTEPQHASSAREDLNTDRSVSSGLSETEQTPEEICSSDQDISSSLSTKVDTFVAEMKLDGLKLDEPVVFAQDEESLGEDGETFLAKLHDNNENLSQKGELVSEVPLKWSSEALNSDKITYSPSSWTPMEIATATGDPERTTVEHALELKSTYSEVEGQANTRDENGEPVVTSYHRCFMGTVDYIWRSEGLQTVRVLAPIPKQAMQWTPGFPTPKWGSDHIALVSELAFCSSKTLPKS", "text": "FUNCTION: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CCR4/nocturin family."}
{"protein": "MAVTFSDLHTADGLKALEAHLAGKTYISGDGITKDDVKVFAAVPLKPSAEFPNAARWYDTVAAAVSSRFPGQASGVSASSAPAAAAPAASKDEDDDDDMDLFGDETEEDKKAAAEREAAKPAKKKESGKSSVLMDIKPWDDETDMKKLEEAVRSVQMEGLTWGASKLMPVGYGIKKLQIMLTIIDDLASTPIEEVLCEAPINEYVQSCDIVAFNKI", "text": "FUNCTION: EF-1-beta and EF-1-beta' stimulate the exchange of GDP bound to EF-1-alpha to GTP. SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family."}
{"protein": "MDIEERISLVLKYPTEEVITVEELRELFQSGYKLNHYIGFEISGFIHIGTGVVSMSKVVDLQKAGVKTQVFLADIHSWLNNKLGGDLDIIRKVAVTYYVETFKKIIEVLGGDPDATRFILGSELYHHNDEYWLLLMDITRHLTLSQVRHSLTILGRKMGESIPLAYLVYPPLQVADVFALEAHIPHGGIDQRRAHILARQVADKIRFYPLKVDGKRIKPVALHHKLLPALNITSKPSSREELSEMKMSKSIPQSAIFVHDSPDEIRQKIAKAYCPPRDTEYNPVLELLRISAFREKRKTPLVIKRPAQYGGDLEVWSYEELEALYRDGRVHPADLKTATSEALITLLEPVYRYFQGPGAKLLEEMKNITITR", "text": "FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 4 subfamily."}
{"protein": "MEYMFLLMSKFFFVFPIIIYIGPAEIIKPQAAEENSRRRILNPNENKEEIVKRRRRIGSKPPSCEKKCYGCEPCEAIQFPTISSIPHLSPHYANYQPEGWRCHCPPP", "text": "FUNCTION: Controls stomatal patterning. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant cysteine rich small secretory peptide family. Epidermal patterning factor subfamily."}
{"protein": "MKCLEGLHLQQRPSKFSVSLAPEEGLVCAFQLEEEKENEDECVCSDQAPEVKEEGCGLGDPAIVSAFQNTQVPQQRGLHSSHRVKVSGALGMSSASLHFMWQSVFPRASSPAHHFGPQQPSPDPFLFYSPLTPWPPKLSLPSHLTQLHPQHQQILQQQQRWRRRRSPTARSVPAQKPWSREPAASDAYANLMTRKEKDWVIRVQMVQLQSENPRLDDYYYQKYYQKLEKRQADKELLGQKTRAESLKLVTPYIQKPEVYESVVRIEGSLGQVAVSTCFSPRRAIDAVSHGTQEQDTGAASSQRLRVLSQIEKMFLQLLKIEEGQNDGLPQLYHTREQSSQVEKLFQALKTQEQNNLEEAADNLLQVLSVRKGKVLVARLLPFLPPDQAVSLLLYITYHLPLLIQRDMADQGLHMLFKPLGKYISHLTFHQLLHAMQGLMLLSPGSSERPVSVVLQNQFGISLLYALLSHGEQLVSLDPSLRSSSDCATWTDLVILIAWEIAQLPAASLAEPLAFPRNLLPCSAITWTSN", "text": "FUNCTION: RNA-binding protein that acts as a translational repressor. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PAT1 family."}
{"protein": "MLVKPMACYFEIWTRKVTTIEDFSLAIANRFKQMGSHSDSEVDWDNEEEVWEDEVHEFCCLFCDSTFTCLKDLWSHCKEAHNFDFYQVKQQNNLDFYACIKLVNYIRSQVKEGKTPDLDKLSDILRSDEYMISVLPDDSVLFSLGDELDSDFEDDNTLEIEVENPADVSKDAEIKKLKLQNQLLISQLEEIRKDKMNELTSQTTDQLSVTPKKADNDSYYFESYAGNDIHFLMLNDSVRTEGYRDFVYHNKHIFAGKTVLDVGCGTGILSMFCAKAGAKKVYAVDNSDIIQMAISNAFENGLADQITFIRGKIEDISLPVGKVDIIISEWMGYALTFESMIDSVLVARDRFLAPSGIMAPSETRLVLTATTNTELLEEPIDFWSDVYGFKMNGMKDASYKGVSVQVVPQTYVNAKPVVFARFNMHTCKVQDVSFTSPFSLIIDNEGPLCAFTLWFDTYFTTKRTQPIPEAIDEACGFTTGPQGTPTHWKQCVLLLRNRPFLQKGTRVEGTISFSKNKKNNRDLDISVHWNVNGKADSQSYVLN", "text": "FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in ribosomal protein rps2. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family."}
{"protein": "MSGISFKSFVQSQYTPIPLPNHDFTGQTILITGASRGLGLEAASHFYRLNASKIILAVRDARKGPECIAFVRQYNPSSNTTVECWELDLTNVETIRQFVAKAKNLARLDAVILNAGMATMSFQAIDGMEKTLATNVTGTFLLAIGLLPALRLSGLRNNIRPRMVLVSSQGHEAAAFAERDADDIFAALNDADKTDMTDRYDTSKLIQLLAFYALKDTVDKSWPDSITFTAVDPGLCDTDLTRDIPLLIRIIHRIMKMLLARTAEVGGRCLVLGAADDEHSHGAYFKDGVIGSPPVAVTDPEGVELKNRVFSQLKSLLYSVDPQIMDACPVMESDEEAIRLN", "text": "FUNCTION: Short chain dehydrogenase; part of the Fg3_54/C64 gene cluster that mediates the biosynthesis of the octapeptide fusaoctaxin A, a virulence factor that is required for cell-to-cell invasiveness of plant host (PubMed:30804501). The 2 nonribosomal peptide synthetases NRPS9 and NRPS5 form an assembly line which likely utilizes GABA as a starter unit (loaded on the unique module M1 of NRPS9) and sequentially incorporates seven extender units composed of the residues L-Ala, L- allo-Ile, L-Ser, L-Val, L-Ser, L-Leu and L-Leu, respectively (PubMed:30804501, PubMed:31100892). During the process, each of the residues that are tethered on modules M3-M7 of NRPS5 containing an E domain can undergo an epimerization reaction to produce a D- configuration before the transpeptidation reaction occurs (PubMed:30804501, PubMed:31100892). The elongation of the peptidyl chain might be terminated by module M8-mediated L-Leu incorporation, followed by R domain-catalyzed 4 electron reduction to release the resulting octapeptide from the assembly line as an alcohol (PubMed:30804501, PubMed:31100892). Fusaoctaxin A is cleaved by the cluster specific ABC transporter FGM5 to the pentapeptide fusapentaxin A and the tripeptide fusatrixin A (PubMed:31100892). The other enzymes from the cluster, FGM1, FGM2, FGM3 and FGM9 seem not to be involved in the biosynthesis of fusaoctaxin A and their functions have still to be determined (Probable). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "QSTGGKAPECLLSNYCNNECTKVHYADKGYCCLLSCYCFGLSDDKKVLEISDSRKKYCDYTIIN", "text": "FUNCTION: Excitatory insect beta-toxins induce a spastic paralysis (PubMed:32442468). They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). In vivo, this recombinant protein is lethal to Locusta migratoria larvae after injection, but has no significant effect when orally administered. Is not toxic to mice after intracerebroventricular injection (PubMed:32442468). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily."}
{"protein": "MSYSGERDNFAPHMALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN", "text": "FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE (PubMed:24375411). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S14 family."}
{"protein": "FVANRMAHELGHNLGIDNDRDSCSCGANSCIMSATVSNEPSSRFSDCSLNQYSSDLINYYGCLLNEPLRTDIVSPPFCGNYYPEVGEDCDCGPPANCQNPCCDAATCKLTTGSQCAEGLCCDQCKFIKARQICRKGRGDNPDDRCTGQSGDCPRNS", "text": "FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced platelet aggregation (probably by binding integrin alpha-IIb/beta-3 (ITGA2B/ITGB3)) and degrades fibrinogen. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIb sub-subfamily."}
{"protein": "MAGNFSEIESQGNISLKFGFLGLGMGGCAIAAECANKETQIKNNKYPYRAILVNTNSQDFNKIEIKNAGNVRKIQLEGYEQGAARNPQVGEEAFVKHETKIFETVKQEFEDRDFIWITCGLGGGTGTGALLKAIEMLYEHDYNFGLLLTLPRDAEALKVLENATSRIRSIAMNQEAFGSIVLIDNAKLYRKFEEENPSALANEYTSYSNKYIADALHEINLVTSSFTPFSDTHFDASEFAQVINTPGVLSLAKLELKSNQLDTENPLGYLTQLGNALEKGVLYDTEREELESAKKSALSIVTSPLRASRLYNFSFLNQMENFLKDRTPYVDERPIAPYVNKHTAKKEEDIVKFYSVVAGLPLPKRVSDIIDEITRIKEEREQANSKKSNAVLNKLFAFDDSVQEEKPKKKKLNFGAEPEVEVADDSQPTKKKLSF", "text": "FUNCTION: A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBCXO1 plasmid. It is essential for plasmid replication (By similarity). Binds GTP and forms filaments. The filaments seed from a DNA centromere-like site (tubC)-TubR complex which extends to surround the TubZ filaments. Highly dynamic filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Forms long, dynamic filaments. SIMILARITY: Belongs to the FtsZ family. TubZ subfamily."}
{"protein": "MGFYEGDDNDANTKAFNDKYIKDQKFATAPFWNLFPKLRDIDEYDNPLLPLPFNFNFRDLGDSALAMASGIPTVKQFDKCEELKGQSAWTTQGIWKCLVPSKAIPPLPQLDFLLPLEEIKSDKSHSHGLFFNDFNLFLKWRSHMNRLQKQRIKTRTTAVEPLARTPEDLMLNWDDLHLGNDAEYASADGSKKIVGRAQSISTTKDSNDAKPSTVKTEKIYFDDGTVDITTTTTSKGSSPQVKHKVVSVDEDN", "text": "SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane protein."}
{"protein": "MEAVTGILNTTIAVVFTWVGYKTARIIWKYTPYSYPNARIKAMEAKLLTEQKFNELAESRTLQNFVVNLEDTDYKDYLADVSSYTVEEVEKALERALAGTYELMFKILPKRSKGFFELLLEGWDVRNIANVVKAKLANEPASDYVVELGTMLPKVKAMAEAKTLEEILVILEGTPYEEVYQKLLLGEIDVTRFETELYRMHYGKLLSYALSRKDDERIILEEFVRLSIDRVNILTALRAKKAGLSAEEIKPMLIPGGTVKLDPLLHVDSFDMALAELDSTKYGQVIRDVREEIEKDLSVLEKALNDHIIERISELERFYPLSIATPLSYVLRREREIRKLRAIAKLIENGVEPERIKELAGEVA", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family."}
{"protein": "MVQISEVKGNSRDNRTAAHTHIKGLGLNSQGIAEKQASGFVGQTTAREACGVVVDLIKAHKMAGRGVLLAGGPGTGKTALALAISQELGTKIPFCPITGSEIYSTEVKKTEVLMENFRRAIGLKVRETKEVYEGEVTELTPEEAENPLGGYGKTITTLLIGLKSAKGQKKLRLDPSIYEAIQKERVTVGDVIYIEANTGACKRVGRSDAYATEFDLEAEEYVPIPKGEVHKKKEIVQDVSLHDLDVANARPQGGQDIMSMMGQLMKPKMTEITDKLRSEINKVVSKYIDQGVAELVPGVLFIDEAHMLDVECFTYLNKALESPISPIVVLASNRGMTGIRGAEDLVAAHGIPPDFLSRLLIIPTTAYDPEEIKRIVKIRSTTEGVKITEAAIDKIAEHGVRISLRYCLQLLTPASILAKVNGRNEIDVQDVAECEDLFLDARRSAALLSSEQGQEFIC", "text": "FUNCTION: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant H2A.Z leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes and is involved in DNA repair. Also involved in pre-rRNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RuvB family."}
{"protein": "MNQEVKNKIFSILKITFATALFIFVVITLYRELSGINFKDTLVEFSKINRMSLVLLFIGGGASLVILSMYDVILSRALKMDISLGKVLRVSYIINALNAIVGFGGFIGAGVRAMVYKNYTHDKKKLVHFISLILISMLTGLSLLSLLIVFHVFDASLILNKITWVRWVLYAVSLFLPLFIIYSMVRPPDKNNRYVGLYCTLVSCVEWLAAAVVLYFCGVIVDVHVSFMSFIAIFIIAALSGLVSFIPGGFGAFDLVVLLGFKTLGVPEEKVLLMLLLYRFAYYFVPVIIALILSSFEFGTSAKKYIEGSKYFIPAKDVTSFLMSYQKDIIAKIPSLSLAILVFFTSMIFFVNNLTIVYDALYDGNHLTYYLLLAIHTSACLLLLLNVVGIYKQSRRAIIYAMISIILIIVATLFTYASYILITWLVIIFALLIVAFRRARRLKRPIRMRNLVAMLLFSIFILYINHIFIAGTFYALDVYTIEMHTSVLKYYFWITILIIAIIVGAIAWLFDYQFSKVRISSNIEECEEIIDQYGGNYLSHLIYSGDKQFFTNEDKNAFLMYRYKASSLVVLGDPIGDENAFDELLEAFYNYAEYLGYDVIFYQVTDQHMPLYHNFGNQFFKLGEEAIIDLTQFSTSGKKRRGFRATLNKFDELNISFEIIEPPFSTEFINELQHVSDLWLDNRQEMHFSVGQFNETYLSKAPIGVMRNENNEVIAFCSLMPTYFNDAISVDLIRWLPELDLPLMDGLYLHMLLWSKEQGYTKFNMGMATLSNVGQLHYSYLRERLAGRVFEHFNGLYRFQGLRRYKSKYNPNWEPRFLVYRKDNSLWESLSKVMRVIRHK", "text": "FUNCTION: Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LPG synthase family."}
{"protein": "MAKSPETEHPVKALGWAATDNSGTFSPFNFSRRATGERDVQFRVLYCGVCHSDLHMVKNEWGVTHYPIVPGHEIVGIVTEVGSKVEKVKIGDKVGVGVLVGSCRQCDQCSNDLENYCYKQILTYGAPYLDGTIARGGYSDIMVADEHFIIRWPENFPLDAGAPLLCAGITTYSPLKYFGLDKPGLRVGVNGLGGLGHVAVKFAKAFGTKVTVISTSLSKKEEAMQHLGVDEFVVSTDPQQMQAAVGTLDGIIDTVSAPHPIVPLLSLLKPHGKLIVVGLPDKPLQLPVFPLIQGRRTIAGSGIGGLKETQEMIDFAAKNNIVADVEVIPIDYINTAMDRLLKSDVKYRFVIDVEKSLKPQ", "text": "FUNCTION: Involved in the production of citral, a mixture of geranial and neral with a strong lemony scent. Reversibly oxidizes geraniol and nerol in equal efficiency. Also active, although at a lower efficiency, with cinnamyl alcohol. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MFQPAPKRCFTIESLVAKDSPLPASRSEDPIRPAALSYANSSPINPFLNGFHSAAAAAAAGRGVYSNPDLVFAEAVSHPPNPAVPVHPVPPPHALAAHPLPSSHSPHPLFASQQRDPSTFYPWLIHRYRYLGHRFQGNDASPESFLLHNALARKPKRIRTAFSPSQLLRLEHAFEKNHYVVGAERKQLAHSLSLTETQVKVWFQNRRTKFKRQKLEEEGSDSQQKKKGTHHINRWRIATKQASPEEIDVTSDD", "text": "FUNCTION: Transcription factor, which in cooperation with EMX2, acts to generate the boundary between the roof and archipallium in the developing brain. May function in combinations with OTX1/2 to specify cell fates in the developing central nervous system (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EMX homeobox family."}
{"protein": "MDYNLALDKAIQKLHDEGRYRTFIDIEREKGAFPKAQWNRPDGGKQDITVWCGNDYLGMGQHPVVLAAMHEALEAVGAGSGGTRNISGTTAYHRRLEAEIADLHGKEAALVFSSAYIANDATLSTLRVLFPGLIIYSDSLNHASMIEGIKRNAGPKRIFRHNDVAHLRELIAADDPAAPKLIAFESVYSMDGDFGPIKEICDIADEFGALTYIDEVHAVGMYGPRGAGVAERDGLMHRIDIFNGTLAKAYGVFGGYIAASAKMVDAVRSYAPGFIFSTSLPPAIAAGAQASIAFLKTAEGQKLRDAQQMHAKVLKMRLKALGMPIIDHGSHIVPVVIGDPVHTKAVSDMLLSDYGVYVQPINFPTVPRGTERLRFTPSPVHDLKQIDGLVHAMDLLWARCALNRAEASA", "text": "SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MSESNSVSVQQMLDRSCWVCFATDEDDRTAEWVRPCRCRGSTKWVHQACLQRWVDEKQRGNSTARVACPQCNAEYLIVFPNLGPVVYVLDLADRLISKACPFAAAGIMVGSIYWTAVTYGAVTVMQVVGHKEGLDVMERADPLFLLIGLPTIPVVLILGKMIRWEDYVLRLWRKYSNKLQILNSIFPGIGCPVPRVPAEANPLADHVSATRILCGALVFPTIATIVGKLMFSTVNSNLQRTILGGIAFVAIKGAFKVYFKQQQYLRQAHRKILDSQEPEPEEV", "text": "FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein."}
{"protein": "MHNYVIIDAFASVPLEGNPVAVFFDADDLPPAQMQRIAREMNLSESTFVLKPRNGGDALIRIFTPVNELPFAGHPLLGTAIALGAHTDNHRLYLETQMGTIAFELERQNGSVIAASMDQPIPTWTALGRDAELLKALGISDSTFPIEIYHNGPRHVFVGLPSIDALSALHPDHRALSNFHDMAINCFAGAGRRWRSRMFSPAYGVVEDAATGSAAGPLAIHLARHGQIEFGQPVEILQGVEIGRPSLMFAKAEGRAEQLTRVEVSGNGVTFGRGTIVL", "text": "FUNCTION: Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known. SIMILARITY: Belongs to the PhzF family."}
{"protein": "MDPEQEISNETLETILVSSTKGSNNNNKKMEEEMKKKVSRGELGGEAQNCPRCESPNTKFCYYNNYSLSQPRYFCKSCRRYWTKGGTLRNVPVGGGCRRNKRSSSSAFSKNNNNKSINFHTDPLQNPLITGMPPSSFGYDHSIDLNLAFATLQKHHLSSQATTPSFGFGGDLSIYGNSTNDVGIFGGQNGTYNNSLCYGFMSGNGNNNQNEIKMASTLGMSLEGNERKQENVNNNNNNSENPSKVFWGFPWQMTGDSAGVVPEIDPGRESWNGMVSSWNNGLLNTPLV", "text": "FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G- 3' consensus core sequence. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAEFTPITIAYGDGIGPEIMDAVLYILRQAEARISLETIEVGEKLYKKHYTSGISEESWNVIQRTGIILKAPITTPQSGGYKSLNVTIRKTLQLFANIRPAVSFHPFTRTLHPNLNLTIIRENEEDLYSGIEYRQTHNMYESLKLISHTGCKKIIRYAFEYAVKNNRKKVTCLSKDNIMKFSDGIFHRVFNEIAKEYPQIDNEHYIIDIGTAKLATTPEIFDIIVTSNLYGDIISDVAAEISGSVGLAGSANIGQHYAMFEAVHGSAPDIAGKGIANPSGLLNAAIMMLVHIGQGDIASLIENAWKKTIEDGVHTFDIYSEHSSSKKVCTKEFAEEVIKRLGQLPMTLPKASYPLIVKKQESKIEYKIDTTEVKKLVGTDIFINIHVFSAHDIADKINKLDIGNFELKTISSKGLKLWPHDLRFEIISDHWCCRFMNKDGTEIKHLDIIILLQALSKANIDFIKVENLFEFDGVACYSLAQGE", "text": "SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family."}
{"protein": "VGLAKGLRKVGTIYPLVVAVLPDVPPEHRRILVEQGCVVREIEPVYPPENHTEFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLENGYFYAVMDCFCEKTWSHTPQYQIGYCQQSPKRVHWPKQLGPKPPLYFNAGMFVYEPSLPTYHDLLHTLKITPPTPFAEQDFLNMFLRDVYRPIPNVYNLVLAMLWRHPENVNLEAVKVVHYCAAGSKPWRYTGEEENMDRNDIKMLVNKWRDIYDDEMLDYNAVADPAADGLQLTAVLTEAAGVVRFIPAPSAA", "text": "FUNCTION: May promote plant stress tolerance (By similarity). Galactinol synthase mainly involved in the biosynthesis of transport raffinose family oligosaccharides (RFOs) that function as osmoprotectants. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyltransferase 8 family. Galactosyltransferase subfamily."}
{"protein": "MSHLESMVLCREAQVSTLQSLFGERHHFSFPSIFIYGHTASGKTYVTQTLLKTLELPHAFVNCVECFTSRLLLEQILNKLSHLNSSDAGCSTEMTCETFNDFVQLFKQVTSAEHLKDQTVYIVLDKAEYLRDMEANLLPGLLRLQELTDRNVTVIFLSEIIWEKFRPNTGCFEPFVLYFPDYSIGNLQKILSHDHPPEYSADFYAAYINILLGVFYTVCRDLKELRHLAVLNFPKYCEPVVKGEAGERDTRKLWRNIEPHLKKAMQTVYLREISSSQWEKLQKDNTDPGQLKGLSAYTHMELPYYSKFILIAAYLASYNPARTDKRFFLKHHGKIKKTNFLKKHEKTSNHLLGPKPFPLDRLLAILYSIVDSRVAPTANIFSQITSLVTLQLLTIVGHEDQLNGPKYKCTVSLDFIRAIARMVNFDIIKYLYDFL", "text": "FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the ORC5 family."}
{"protein": "MGMRMMFTVFLLVVLATAVLPVTLDRASDGRNAAANAKTPRLIAPFIRDYCCHRGPCMVWCG", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. FUNCTION: Does not show activity on the acetylcholine receptors tested. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
{"protein": "MDHVPALVLAGCCFLALLPGWACGLGSMSSIAVSYGEDGPVFCGLNSDGSHLVACFGADASVLYGAPPNIPFLGLTAGDGFVCGLLLDTRQPYCWGSNSYVKSGVPQPMVEGARYSELSAGDNHLCALRAAQDGGRGSSAATSLIDCWGYNMTATHAVDEAVSTVSAGSVFNCGLFARNRTVFCWGDETVSGVVGLAPRDLHFQSIGAGGYHVCGVLENAQVFCWGRSLEMQQVVPSSAIGDGDVNIVPMDAMSTVVGGRFHACGIRSLDHQVACWGFTLHNSTSPPKGLKMYALVAGDYFTCGVPAETSLMPRCWGNSGPLALPMAVPPGICVPTACSHGYYEYVNHGEVGSIKVCKPANSRLCLPCSTGCPEGLYESSPCNATADRVCQFDCLKCVTDECLSFCLSQKRTKSRKLMAFQMRIFVAEIVFAVVLVLSVSVTTCLYVRHKLRHCQCSNRELRLAKSTAYSFRKDNMKIQPDMEDLKIRRAQEFSYEELEQATGGFSEDSQVGKGSFSCVFKGILRDGTVVAVKRAIKASDVKKSSKEFHNELDLLSRLNHAHLLNLLGYCEDGSERLLVYEFMAHGSLYQHLHGKDPNLKKRLNWARRVTIAVQAARGIEYLHGYACPPVIHRDIKSSNILIDEDHNARVADFGLSILGPADSGTPLSELPAGTLGYLDPEYYRLHYLTTKSDVYSFGVVLLEILSGRKAIDMQFEEGNIVEWAVPLIKAGDIFAILDPVLSPPSDLEALKKIASVACKCVRMRGKDRPSMDKVTTALEHALALLMGSPCIEQPILPTEVVLGSSRMHKVSQMSSNHSCSENELADGEDQGIGYRAPSWITFPSVTSSQRRKSSASEADIVGRRATDGRNVGSSIGDGLRSLEEEIAPASPQENLYLQHNF", "text": "FUNCTION: Putative receptor protein kinase. Could play a role in a differentiation signal. The CRINKLY4 (CR4) mutation affects leaf epidermis differentiation such that cell size and morphology are altered, and surface functions are compromised, allowing graft-like fusions between organs. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endosome, multivesicular body membrane; Single-pass type I membrane protein Note=Also localized into protein export bodies. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MKKVSTLDLLFVAIMGVSPAAFAADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAARRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAHAEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNGSTNDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFNLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVISSAQNRNYSAADVTRAFSTVGVTCPSAL", "text": "FUNCTION: Cleaves host elastase, collagen, IgI and several complement components as well as endogenous pro-aminopeptidase, pro-chitin-binding protein (cbpD). Cleaves its own pro-peptide. Involved in the pathogenesis of P.aeruginosa infections. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family."}
{"protein": "MAQAQIDEQRRLQDLYVQLKKEINDGEGVAWLFQQKTYTDKDNKPTKATPPLRTTSSDLRLAFDSIEENLTASNEHLTNNEINFCKLTLGKTLLLIDKHVKSHRWDSNKVNLIWQIEKGKTQQFHIHCCLGYFDKNEDPKDVQKSLGWFMKRLNKDLAVIYSNHHCDIQDIKDPEDRAKNLKVWIEDGPTKPYKYFNKQTKQDYNKPVHLRDYTFIYLFNKDKINTDSMDGYFAAGNGGIVDNLTNKERKTLRKMYLDEQSSDIMDANIDWEDGQDAPKVTDQTDSATTKTGTSLIWKSCATKVTSKKEVANPVQQPSKKLYSAQSTLDALFNVGCFTPEDMIIKQSDKYLELSLEPNGPQKINTLLHMNQVKTSTMITAFDCIIKFNEEEDDKPLLATIKDMGLNEQYLKKVLCTILTKQGGKRGCIWFYGPGGTGKTLLASLICKATVNYGMVTTSNPNFPWTDCGNRNIIWAEECGNFGNWVEDFKAITGGGDVKVDTKNKQPQSIKGCVIVTSNTNITKVTVGCVETNAHAEPLKQRMIKIRCMKTINPKTKITPGMLKRWLNTWDRQPIQLSHEMPELYLGKCRW", "text": "FUNCTION: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family."}
{"protein": "FLGKKVLKAVGKQAAKKQME", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 03 subfamily."}
{"protein": "MTTQVPPHSVQVHTTTTHRYEAGVVPPGARFETSYEAGVKAASIYHSERGPTTSQVLAVLAGLPVGGILLLLAGLTLAGTLTGLAVATPLFVLFSPVLVPATVAIGLAVAGFLTSGAFGLTALSSFSWILNYIRETQPASENLAAAAKHHLAEAAEYVGQKTKEVGQKTKEVGQDIQSKAQDTREAAARDAREAAARDAREAAARDAKVEARDVKRTTVTATTATA", "text": "FUNCTION: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth. SUBCELLULAR LOCATION: Lipid droplet. Membrane; Multi-pass membrane protein. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. SIMILARITY: Belongs to the oleosin family."}
{"protein": "MSSSTMDNNEPKVLEMVYDSPILPEGSSMDPNIINCINRHINMCLQHTYSSSIIAILDRFLMMNKDELNNTQCHIIKEFMTYEQMAIDHYGGYVNAILYQIRKRPNQHHTIDLFKKIKRTRYDTFKVDPVEFVKKVIGFVSILNKYKPVYSYVLYENVLYDELKCFIDYVETKYFQN", "text": "FUNCTION: Plays a role in the inhibition of host innate immune response. Within the host nucleus, inhibits activation of interferon- beta promoter by inhibiting IRF3 activation. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the poxviridae OPG036 family."}
{"protein": "MLTQKTKDIVKATAPVLAQHGYAIIQHFYKRMFQAHPELKNIFNMAHQERGEQQQALARAVYAYAANIENPESLSAVLKDIAHKHASLGVRPEQYPIVGEHLLASIKEVLGDAATDEIISAWAQAYGNLADILAGMESELYERSEERAGGWAGWRRFIVREKNPESDVITSFVLEPADGGPVADFEPGQYTSVAVQVPKLGYQQIRQYSLSDSPNGRSYRISVKREDGGLGTPGYVSSLLHDEINVGDELKLAAPYGNFYIDVSATTPIVLISGGVGLTPMVSMLKKALQTPPRKVVFVHGARNSAVHAMRDRLKEASRTYPDFKLFIFYDEPLPTDIEGRDYDFAGLVDVEKVKDSILLDDADYYICGPVPFMRMQHDKLLGLGITEARIHYEVFGPDLFAE", "text": "FUNCTION: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins subfamily. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
{"protein": "MHGLFVNKKKNDTGSTALVLKKIQSGDTKLKEEFIKDNVPYIIRTISNILGIVVDDRNSEEFSIGLAAFNEAIDRYDADKNGNFYTYSFVVIKSRLYDFIRRNRKHNNVLPFSYIEESTRVDERLLMSDASGQFEKIEVRQELVSFEKSLKEFGISLEDLVLSSPKHKDSRLLLIKIARIIADDDNMFRKLVEKKYIPMKEVLSRIKVNHKTIQRNRKFIIAVSLILRSNLYDLKEYVQGFEREGKYHG", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (By similarity). This sigma factor is involved in regulation of cellulosomal genes via an external polysaccharide-sensing mechanism (Probable). Recognizes the predicted promoters associated with sigI3 itself, pl11, ce12 and cipA (PubMed:26731480). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. SigI subfamily."}
{"protein": "MSQSVESRTRIKSERYESGVIPYAKMGYWDADYVIKETDILALFRITPQPGVDPIEASAAIAGESSTATWTVVWTDLLTACDLYRAKAYRVDPVPNVADQYFAYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRMPVAYLKTFQGPATGLIVERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRERFLYSMEGVNKASASAGEIKGHYLNVTAATMEDMYERAEFSKEVGSIICMIDLVIGYTAIQSMAIWARKHDMILHLHRAGNSTYSRQKNHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLESDTDINLPQGLFFAQNWASLRKVVPVASGGIHAGQMHQLLDYLGDDVVLQFGGGTIGHPDGIQAGATANRVALESMVMARNEGRNYVAEGPQILRDAAKTCGPLQTALDLWKDISFNYTSTDTADFVETPTANI", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity). FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily."}
{"protein": "MAGLATVSKLAGETVGQEFLIFTLGNEEYGIDILKVQEIRGYDQVTRIANTPDFIKGVTNLRGVIVPIIDLRVKFAQQGVSYDENTVVIVLNFGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLATEYLTGLGALGERMLILVDIEKLLSSEEMALVDNVAKSH", "text": "FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MTVGARLRSKAESSLLRRGPRGRGRTEGDEEAAAILEHLEYADEAEAAAESGTSAADERGPGTRGARRVHFALLPERYEPLEEPAPSEQPRKRYRRKLKKYGKNVGKVIIKGCRYVVIGLQGFAAAYSAPFAVATSVVSFVR", "text": "FUNCTION: Regulates drug efflux through modulation of ABCB1 localization and activity. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein."}
{"protein": "MHPSLLSPTSLGPSGSLHSPISTLSSPMNGLGSPFSVISSPMGPHSMASPGVGYGPSISPQLNSHMNSVSSSEDIKPPLGLNGVMKVPAQPSGTPLSLTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCVIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRAKERSENEVESTSSANEDMPVEKILEAELAVEPKTETYIETNVPMPSNSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPGEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT", "text": "FUNCTION: Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (rars) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription. The high affinity ligand for rxrs is 9-cis retinoic acid. In the absence of ligand, the rar/rxr heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily."}
{"protein": "MGLQACLLGLFALILSGKCSYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNLERLSELVQAVSDPNSPQYGKYLTLENVADLVRPSPLTLHMVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPRPYQLPQALAPHVDFVGGLHRFPPTSSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVTRVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDEEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRPSYQEEAVAKFLSSSPHLPPSGYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGLLSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTHGCHASCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP", "text": "FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity). SUBCELLULAR LOCATION: Lysosome Melanosome."}
{"protein": "MAVQAPCIQLNDGNTIPIVALGTGRGTAKESDSIDEVRQAVYWAIEAGYRHIDTAAVYQDEEQVGQGIAEAIANGLVTREELFVTTKLWNDKHARDQVVPALQESLKKLGLDYIDLYLIHFPIATKPDDSPDNIDYLETWQGMQDARQLGLARSIGVSNFNATQITRLVSNSYIRPVINQIEVNPTNTQEPLVAHCQSLGIAVMAYSPFGFVVSRGQTGAPPPRSDDPTLTALANKYRKSVGQILLRYLIDRGLIPIPKSTNKQRIAQNIDLFDFQLTFEEVAAINQFNKNHRVIDISDWKDYPNYPN", "text": "FUNCTION: NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. May play a role in the regulation of molting. Has lower activity with phenylglyoxal and isatin (in vitro). Has no activity with NADH as cosubstrate. Has no activity with nitrobenzaldehyde and 3-hydroxybenzaldehyde. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "AGEGNGRGPYVQADLAYAYEHITHDYPKPTDPSKGKLSTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNDSKYSVSIKNLQRRTSNGNRRDRKTENQENGSFHAVSSLGLSAVYDFKLNDKFKPYIGARVAYGHVRHSIDSTKKTTEFLTTAGARGTDPTVSSPYKNTQDAHQESNSIRRVGLGVIAGVGFDITPNLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF", "text": "FUNCTION: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the opacity porin family."}
{"protein": "MRLQCVVLFAALTLVAATHAPPNVKTVLSAEQHDIPVKRLLRPGNPAGKEDEERGINFSSVPGFEKLANLLKPKPGLKKLLKWADAKKPPETVFTRLRLDKTGTQLFDNTDFPVWAAYTRSVAQTDSEASAVMLKTLVSRYSDEVLSGMIAAAKKSSKTESIATKLETEQMRTWLAAKKTPDDMFLVFKLNKAGDDILSSPLLSAWTNYMKLSNKENPKAQTTLIATMTKHYGDSGVSQILAAARKSPATQSTAKRLEAEQVQLWLKKGRTPDDTFTLLSLDRAGDDLLASPQFNTWMKYINYYNKENPDEKTTVLAKLMTHFDDEELTPILVVARKVPSTESTAAKLQAEQFKNWLSADKSPEEAFTLLQLDKAGDDLLTNPQLTNWLKYTENFNLNKEINEQVTAIQVFRAQYVDDSRIANMVIAAEKVPNTQAIAKRVEDELFKGWTVVLNKPDDVFINLKLETVGENVFESPLWSFYTKFLEKYNTANPGKEQTMISGLARGYNDVTLTNMLLKAKEAPSTKTLATKLEDELVQYWLADKKLPDKLFGYLELKESVDGILTNPVFNVWLKYLNAFNDKAPVKKALMIDTLKSAFGDVAVSNMLFAAKKDPGTAKVAATLQTALLSKWVLEKKTPGQVSAILKEGAGADVSAKLLATYSAKFKVRWG", "text": "FUNCTION: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection (PubMed:23377181, PubMed:25387135, PubMed:30595554). Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4 (PubMed:30595554). Inhibits the host salicylic acid pathway during infection (PubMed:25387135). SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK", "text": "FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily."}
{"protein": "MAAFIAKQMVGNQLSAVKGAVGGDGGDDGDDKEKAEEEERERQEAIKEAEDRRKEKHRKMEEEREKMRQDIRDKYNIKKKEEIVEAAPQEEPNPLMRKKKTPEELAAEAEQEELDDFTKLKNQIETQVNELKTQIEGKCVMQ", "text": "FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SIMILARITY: Belongs to the complexin/synaphin family."}
{"protein": "IVGGQEASPGSWPXQVGLFF", "text": "FUNCTION: This enzyme is a serine protease capable of degrading the native triple helix of collagen. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MNKFILLLSLVTLSCVLAVPQLPAAQQYYMKGSFNIPYFNIVEPIELIYDSVNNRQYISVYNGMDITINFYNQDNTYNVGPVKYDMVCTTTPGNGSLVNVLPTEPSSWVYNGTSTVNGVQVFGYSQKITQYGRTGFYNFYVDANGVPVQFYMDGVDYVFGSHPDVYVLNFDIYTTDISSYESYFDIPVLCNNAKEAPAKENQFDGLFSSIGDNLLAKEEQASNLFKEYKAQYNKEYSSQDEHDERFINFKAARKIIATHNAKESSYKLGMNHYADLSNKEFNTLVKPKVARPSVTGADSVHDDESLRSIPSTVDWRNQNCVTPVKDQGICGSCWTFGSTGSLEGTNCVTNGELVSLSEQQLVDCAILTGSQGCGGGFASSAFQYVMEIGSLATESNYPYLMQNGLCRDRTVTPSGVSITGYVNVTSGSESALQNAIATTGPVAIAIDASVDDFRYYMSGVYNNPACKNGLDDLDHEVLAIGYGTYQGQDYFLVKNSWSTNWGMDGYVYMARNDNNLCGVSSQATYPIPTKN", "text": "FUNCTION: Inhibitor that slows proliferation of secreting cells (also known as chalone). Requires aprA for activity. SUBCELLULAR LOCATION: Secreted Note=Concentrated in subcellular structures, possibly vesicles. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MAPWGKRLAGVRGVLLDISGVLYDSGAGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKPVLISLGKGRYYKETSGLMLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQAVMIGDDIVGDVGGAQRCGMRALQVRTGKFRPSDEHHPEVKADGYVDNLAEAVDLLLQHADK", "text": "FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3- phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HAD-like hydrolase superfamily."}
{"protein": "MMIKWIISILTMSIMPVLVYSSSIFRFRSEDVELCYGNLYFDRIYNNVVNIKYIPEHIPYKYNFINRTFSVDELDNNVFFTHGYFLKHKYGSLNPSLIVSLSGNLKYNDIQCSVNVSCLIKNLATSISTILTSKHKTYSLHRSKCITIIGYDSIIWYKDINDKYNDIYDFTAICMLIASTLIVTIYVFKKIKMNS", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein Host cell surface. SIMILARITY: Belongs to the orthopoxvirus OPG172 protein family."}
{"protein": "MASFKIVIVCLALLVAVASARRRDMMSDDELDYHYSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ", "text": "FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process (PubMed:18538344). Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 (PubMed:18538344). This reveals high specificity for arthropod over mammalian channels (PubMed:18538344). In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours (PubMed:22048953). Also causes paralysis of cherry shrimps immediately after injection at very low doses (PubMed:29424690). Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes (PubMed:22048953). It has also been observed to cause death of zebrafish larvae within 1 hour (PubMed:31134275). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type II subfamily."}
{"protein": "MSAVRNRNNVEKQSNNGAQLTEVQKKELADLQKVHPANEFGGIIGTFLLTFILPVVVYWIWASIEFNNGYLLRPETLSVEGVKAFLAQLYHYVITYAYPTKEAAIIYFSWFGFQAFLQHVVPGRKVLGSPLPGGARLEYTLNGWASWWITLIVIPIAIYFGLFKATILIDNYAPMMTVVNIWSFVFTFLLKIHAKLKGEEERMSGHFFYDFWMGFARNPRIGSFDLKLFCEARPGLILWVLMNFSIAAKQLEVYGEISLSVILVCCFHFWYIADYYYHEEAILTTMDIITEKFGYMLVYGDLSWVPFTYCFQCYYLYKHLVNGAPLHISIGYAIFVVSLKCFGFYLFRWVNSQKHDFRRNPEAPVWGKPAEFILTKRGTKLLCSGFWGICRHLNYTGDIILSWAWCLPCQFDSLAPYFYGIYFTSLDLHRCWRDHNACLVKYGDDWRAYCKRVPYNFIPGLI", "text": "FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta- 8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERG4/ERG24 family."}
{"protein": "MLIPSKLSRPVRLDHTVVRERLLAKLSGANNFRLALITSPAGYGKTTLISQWAAGKNDIGWYSLDEGDNQQERFASYLIAAVQQATNGHCAICETMAQKRQYASLTSLFAQLFIELAEWHSPLYLVIDDYHLITNPVIHESMRFFIRHQPENLTLVVLSRNLPQLGIANLRVRDQLLEIGSQQLAFTHQEAKQFFDCRLSSPIEAAESSRICDDVSGWATALQLIALSARQNTHSAHKSARRLAGINASHLSDYLVDEVLDNVDLATRHFLLKSAILRSMNDALITRVTGEENGQMRLEEIERQGLFLQRMDDTGEWFCYHPLFGNFLRQRCQWELAAELPEIHRAAAESWMAQGFPSEAIHHALAAGDALMLRDILLNHAWSLFNHSELSLLEESLKALPWDSLLENPQLVLLQAWLMQSQHRYGEVNTLLARAEHEIKDIREGTMHAEFNALRAQVAINDGNPDEAERLAKLALEELPPGWFYSRIVATSVLGEVLHCKGELTRSLALMQQTEQMARQHDVWHYALWSLIQQSEILFAQGFLQTAWETQEKAFQLINEQHLEQLPMHEFLVRIRAQLLWAWARLDEAEASARSGIEVLSSYQPQQQLQCLAMLIQCSLARGDLDNARSQLNRLENLLGNGKYHSDWISNANKVRVIYWQMTGDKAAAANWLRHTAKPEFANNHFLQGQWRNIARAQILLGEFESAEIVLEELNENARSLRLMSDLNRNLLLLNQLYWQAGRKSDAQRVLLDALKLANRTGFISHFVIEGEAMAQQLRQLIQLNTLPELEQHRAQRILREINQHHRHKFAHFDENFVERLLNHPEVPELIRTSPLTQREWQVLGLIYSGYSNEQIAGELEVAATTIKTHIRNLYQKLGVAHRQAAVQHAQKLLKMMGYGV", "text": "FUNCTION: Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto- oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box. SIMILARITY: Belongs to the MalT family."}
{"protein": "SEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLK", "text": "FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). SUBCELLULAR LOCATION: [Amyloid-beta protein 42]: Cell surface Note=Associates with FPR2 at the cell surface and the complex is then rapidly internalized. SUBCELLULAR LOCATION: [Gamma-secretase C-terminal fragment 59]: Nucleus Cytoplasm Note=Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated form is localized to the nucleus (By similarity). SUBCELLULAR LOCATION: [Soluble APP-beta]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane; Single-pass type I membrane protein Perikaryon Cell projection, growth cone Membrane, clathrin-coated pit Early endosome Cytoplasmic vesicle Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N- glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. SIMILARITY: Belongs to the APP family."}
{"protein": "MSLMNDPRPVSKKAGAKPVYGKNTPQFTKTVGEIVNALINAYKEGKKVNLLKIKTELAAKNSLSDQPKSVDIISAIPESYKNTLLPLLKAKPVRTASGIAVVAVMCKPHRCPHLAMTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPFLQTRHRIDQLKRLGHNVEKVEFIIMGGTFMSLPSDYRDYFIRNLHDALSGHTSNNVAEAVKYSEQSNVKCVGITIETRPDHCLKLHLSNMLTYGCTRLEIGVQSVFEDIARDTNRGHTVRAVLESFQLAKDSGFKVVAHMMPDLPNMGMERDIYGFMEFFENPAFRADGLKIYPTLVIRGTGLYELWKTGTYKNYSPDSLVDLIAKVLALVPPWTRIYRIQRDIPMPLVTSGVEYGNLRELCLARMKDFGTKCRDVRTREVGIQEVHHKIKPDQVELIRRDYVANGGWETFLSFEDPKQDILIGLLRLRKCSETSFRPELKENCSIVRELHVYGSVVGIHNRDPTKFQHQGYGTLLMEEAERIAREEHGSIKLAVIAGVGTRHYYRKLGYELDGVYVSKYLG", "text": "FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). SIMILARITY: Belongs to the ELP3 family."}
{"protein": "MSIYSKFTINDVLLNKESLQKKNKYTCPICFELIYKKSIYQCSSGHYACQECWEKSLEIKQECMICRCKVKSFKNLSRCLVIEQNFSKKECNCIYSFHLDYFIDGANQENEDEENEDEENEDDEDENEDEENGEDDEDKDEDEENENENEENKDEENEKRKLIKDEENGCKEIINVDQLDRHIQNCKFKFVKCSHIGCDRVLRLNSLKEHENQCGFKLVKCEYCACDGIIQVQLENHYDECPKFVIGCPQGCLNFFERDQIKSHIENDCNNSTIQCKYYEYGCKVEMKRSELQRHLENVNHQLFMGKLIDKLSSTLDQSMKIQELLLKEIEKSKITCSELQRKNDELSSLITEIDDNYFNKNDFINSWKLTSQGYTNKWIISNYSNLVENTPHPEYIYSPSFDIVSREFVISIYPNGSLTGKDHLSLFLHNNNEDPNKLEFTLELVNLLDKSKSITRKGLEVFEEIERKGWSKFLASKLINKKNGWLSDDDKLTINIYVKILYDDIEPLES", "text": "FUNCTION: Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TNF receptor-associated factor family. A subfamily."}
{"protein": "MQLEKMITEGSNAASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHTQVSGGGRLIYLGAGTSGRLGILDASECPPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGGVNDLKNIGLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSSTAEFAITPVVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVNIVKNATGCNAEQAEAALIACERNCKTAIVMVLKNLDADEAKKCLDQHGGFIRKALEKE", "text": "FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily."}
{"protein": "MSEESNEETKIIELEDIPGVGPETARKLREAGYSTIEAVAVASPSELANVGGITEGNAVKIIQAARKLANIGGFESGDKVLERRRSVKKITTGSKDLDELLGGGVETQAITEFFGEFGSGKTQICHQLAVNVQLPEDEGGLEGSVIIIDTENTFRPERIIQMAEAKGLDGNEVLKNIYVAQAYNSNHQMLLVDNAKELAEKLKKEGRPVRLIIVDSLMSHFRAEYVGRGTLADRQQKLNRHLHDLMKFGELYNAAIVVTNQVMARPDVLFGDPTKPVGGHIVAHTATFRIYLKKGKDDLRIARLIDSPHLPEGEAIFRVTERGIEDAEEKDKKKRKK", "text": "FUNCTION: Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity). SIMILARITY: Belongs to the eukaryotic RecA-like protein family."}
{"protein": "MTPIEYIDRALALVVDRLARYPGYEVLLSAEKQLQYIRSVLLDRSLDRSALHRLTLGSIAVKEFDETDPELSRALKDAYYVGIRTGRGLKVDLP", "text": "FUNCTION: Immunity protein that plays a role in preventing early activation of toxin Tse6."}
{"protein": "MSESVSMSVPELLAIAVAALGGTRRRGQQEMAAAVAHAFETGEHLVVQAGTGTGKSLAYLVPAIIRALCDDAPVVVSTATIALQRQLVDRDLPQLVDSLTNALPRRPKFALLKGRRNYLCLNKIHNSVTASDHDDERPQEELFDPVAVTALGRDVQRLTAWASTTVSGDRDDLKPGVGDRSWSQVSVSARECLGVARCPFGSECFSERARGAAGLADVVVTNHALLAIDAVAESAVLPEHRLLVVDEAHELADRVTSVAAAELTSATLGMAARRITRLVDPKVTQRLQAASATFSSAIHDARPGRIDCLDDEMATYLSALRDAASAARSAIDTGSDTTTASVRAEAGAVLTEISDTASRILASFAPAIPDRSDVVWLEHEDNHESARAVLRVAPLSVAELLATQVFARATTVLTSATLTIGGSFDAMATAWGLTADTPWRGLDVGSPFQHAKSGILYVAAHLPPPGRDGSGSAEQLTEIAELITAAGGRTLGLFSSMRAARAATEAMRERLSTPVLCQGDDSTSTLVEKFTADAATSLFGTLSLWQGVDVPGPSLSLVLIDRIPFPRPDDPLLSARQRAVAARGGNGFMTVAASHAALLLAQGSGRLLRRVTDRGVVAVLDSRMATARYGEFLRASLPPFWQTTNATQVRAALRRLARADAKAH", "text": "FUNCTION: Probable helicase involved in DNA repair and perhaps also replication. SIMILARITY: Belongs to the helicase family. DinG subfamily."}
{"protein": "MVTMKLLYLTSFASLAVANGPGWDWKPRVHPKVLPQMIHLWDLLQGAQQLEDFAYAYPERNRVFGGRAHEDTVNYLYRELKKTGYYDVYKQPQVHQWTRADQALTVDGQSYDATTMTYSPSVNATAPLAVVNNLGCVEADYPADLTGKIALISRGECTFATKSVLSAKAGAAAALVYNNIEGSMAGTLGGATSELGAYAPIAGISLADGQALIQMIQAGTVTANLWIDSQVENRTTYNVIAQTKGGDPNNVVALGGHTDSVEAGPGINDDGSGIISNLVVAKALTRFSVKNAVRFCFWTAEEFGLLGSNYYVNSLNATEQAKIRLYLNFDMIASPNYALMIYDGDGSAFNLTGPAGSAQIERLFEDYYTSIRKPFVPTEFNGRSDYQAFILNGIPAGGLFTGAEAIKTEEQAQLFGGQAGVALDANYHAKGDNMTNLNREAFLINSRATAFAVATYANSLDSIPPRNMTTVVKRSQLEQAMKRTPHTHTGGTGCYKDRVEQ", "text": "FUNCTION: Extracellular aminopeptidase that releases a wide variety of amino acids from natural peptides and contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily."}
{"protein": "MADTDEGFGLARTPLEPDSKDRSCDSKPESALGAPSKSPSSPQAAFTQQGMEGIKVFLHERELWLKFHEVGTEMIITKAGRRMFPSYKVKVTGLNPKTKYILLMDIVPADDHRYKFADNKWSVTGKAEPAMPGRLYVHPDSPATGAHWMRQLVSFQKLKLTNNHLDPFGHIILNSMHKYQPRLHIVKADENNGFGSKNTAFCTHVFPETAFIAVTSYQNHKITQLKIENNPFAKGFRGSDDLELHRMSRMQSKEYPVVPRSTVRHKVTSNHSPFSSETRALSTSSNLGSQYQCENGVSGPSQDLLPPPNPYPLAQEHSQIYHCTKRKDEECSSTEHPYKKPYMETSPSEEDTFYRSGYPQQQGLSTSYRTESAQRQACMYASSAPPSEPVPSLEDISCNTWPSMPSYSSCTVTTVQPMDRLPYQHFSAHFTSGPLVPRLAGMANHGSPQLGEGMFQHQTSVAHQPVVRQCGPQTGLQSPGGLQPPEFLYTHGVPRTLSPHQYHSVHGVGMVPEWSENS", "text": "FUNCTION: DNA-binding protein that regulates the transcription of several genes and is involved in heart development and limb pattern formation. Binds to the core DNA motif of NPPA promoter. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the cytoplasm and the nucleus. Acetylation at Lys-339 promotes nuclear retention."}
{"protein": "MTMFSTRSRLRSAAADTFALVVYCFVIGMIIEIVISGMTFQQSLSSRLVSIPVNILIAWPYGLYRDAFIRFARRHAGEHMWARNLADLLAYVSFQSPVYALILWSVGADLEQITTAVASNALVSMAMGVAYGYFLEYCRKLFRVAGYI", "text": "FUNCTION: Exports L-alanine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AlaE exporter family."}
{"protein": "MARTMTMRVSSLLVAVVLLAALSFQACSGHGGINDGDGQVDAPATPASSSGVRSKGLIAVKVWCLVILLVFTFAGGVSPYFYRWNESFLLLGTQFAAGVFLGTALMHFLADSTSTFKGLTTNQYPFSFMLTCVGFLLTMLSDLVIAAVARRSAAAGVSDNQVSEQQQRQQAEGAVMSRKEEEAAAVAHPAMLVRTSSFEDAVLLIVALCFHSVFEGIAIGVSASKSEAWRNLWTIGLHKIFAAVAMGIALLRMIPKRPFLMTVVYSLAFAVSSPVGVGIGIAIDATSQGRAADWTYAISMGLATGVFIYVAINHLIAKGYRPHHPTAADKPLFKFLAVLLGVAVMAVVMIWD", "text": "FUNCTION: Zinc transporter that may mediate zinc uptake from the rhizosphere. May also transport other divalent cations. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MNVSSDVDFISVGCNCLGDCLVWGQNKLAAYGAQNFIALFDPIQSKVLATLPGHKDRVNHICWVPNINEEYKNRYSSYENELLSCSSDNTIISWKQIKGGLNYQYKVVEVLKGHSDSVTNISVLDFPDGSLLMCSTSADNTVKLWRRESLTKENIDTDTLPKWECIQTIDFTPKCMECSSLAFIPGTTIPLLAVGGLEPKIHIYIQNLDSTTATLQFKKLMSLQGHQDWIRSLSFKTINEGEGEGEEEELILASSSQDFKIRLWKISKFTAEKQKQQQLDESGNGGANLLGSLSTQLSGVTSLSTKGYLFNCNSVKYIILLDAVLSGHDDWVYSIHWSPARRDQETGKKIQEQMLISASMDKTAIVWRPDRTTGIWIDESRVGDMGGNILGQYGAVFSPCSQYILSHGYNGAFHFWKQNTNQKSSFWEPQIVVSGHFGPVQDLMWSPDYSYFISCSTDRTLRLFSEWKRNNNNNNLENNKEQQIISWNEIARPQIHGYDLECFTFINKKTHVIVSGAEEKIMRAFVGSQNFVDTLLNISKVQPVNDGTQRPLAANQPSLGLSNKPYFTGGSDYNENIDNNNNNNNNNGNGEENTEDSIKMKMGGGDEGGGGEGMDTGYFEDEIPFNPEVLSEPPFEEHLLQSSLWPEIHKFYGHGNEIVAVACSADGMYLASTCRASSADQATVRIWNVSNWKECANLKGHTLTVVNLSFSHNSKYLLGVSRDRMWTLWERSASNSEEPFVKVISAPKSHGRIIWSGSWSHDDKFFATGARDKLVKVWNLDNIKDIKNACASTLPAFGSGVTCVEFAPKSSKFTGEHGDHLLAVGEDDGKITIWKSTTSTSNPKSLDWTCVHTISPLISHTLDVRRIRWRDTPTINGNSLTYQIVTCSVDHSVRIFNIKFD", "text": "FUNCTION: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the WD repeat ELP2 family."}
{"protein": "MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLAREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA", "text": "FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H3 family."}
{"protein": "MRIGIFSEAYLPLISGVVTSVVNLKEGLEALGHEVYVITPIPSKDKFENDPSVIRIPGWVIPRKSLKGFRLVLFVKRYVRKMRKLKLDVVHIHTEFSMGKLGLAVAKKERIPSVYTLHTSYQDYTHYVSKLLTRFAPNAAKKLAGKINNQYTKNCHMTIVPTKKIYDKMIRLKHDGEFTIIPSGINLKPFYKSSYTSEQVQALKDKLGIRNDEFVAILVARIAKEKSIGDLVEAFVEFYKSYPNSRFIIIGDGPDKPVLDKLIDSKKASKYINTLGFVKNAEVGLYYQIADVFLNASTTETQGLTYVEALAASLPIIVRYDDVFDAFVEDGKNGIFFNKNEELVKHLIHIRQNPEILGTLSKNAEISTKPYAKEVYAKSCETLYLDLIDKNNKKLNKK", "text": "FUNCTION: Glucosyltransferase involved in the biosynthesis of the non- bilayer-prone membrane lipid alpha-monoglucosyldiacylglycerol. This is a major component for maintaining a certain anionic lipid surface charge density, for balancing the bilayer to non-bilayer phase equilibria and for keeping a constant lipid bilayer spontaneous curvature (curvature packing stress). Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D- glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor and DAG is the preferred substrate. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=The enzyme binds the membrane surface via electrostatic association with anionic lipids and is accompanied by hydrophobic interactions and by a conformational change induced by nonbilayer-prone lipids. The enzyme is supposed to be located on the cytosolic side of the membrane. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MAGDAVTVVLPCLNEEESLPAVLAAIPAGYRALVVDNNSTDDTATVAARHGAQVVVEPRPGYGSAVHAGVLAATTPIVAVIDADGSMDAGDLPKLVAELDKGADLVTGRRRPVAGLHWPWVARVGTVVMSWRLRTRHRLPVHDIAPMRVARREALLDLGVVDRRSGYPLELLVRAAAAGWRVVELDVSYGPRTGGKSKVSGSLRGSIIAILDFWKVIS", "text": "SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MTECKAEVTPSASNGHRVFSYTLESHTAAAFAIMNELRRERQLCDVTLRVRYCPLDTHVDFVAHKVVLASSSPVFRAMFTNGLKECGMEVVPIEGIHPKVMGRLIEFAYTASISVGEKCVIHVMNGAVMYQIDSVVQACCDFLVEQLDPSNAIGIASFAEQIGCTELHQKAREYIYMNFSQVATQEEFFTLSHCQLVTLISRDELNVRCESEVFHACVAWVQYDREERRPYVQALLQAVRCHSLTPHFLQRQLEHFEWDAQSKDYLSQIFRDLTLHKPTKVIPLRTPKVPQLIYTVGGYFRQSLSFLEAFNPCSGAWLRLADLQVPRSGLAACVISGLLYAVGGRNNGPDGNMDSHTLDCYNPMNNCWRPCAHMSVPRNRIGVGVIDGMIYAVGGSHGCTHHNSVERYDPERDSWQLVSPMLTRRIGVGVAVINRLLYAVGGFDGTHRLSSAECYNPERDEWRSIAAMNTVRSGAGVCALGNYIYVMGGYDGTNQLNTVERYDVEKDSWSFSASMRHRRSALGVTTHHGRIYVLGGYDGNTFLDSVECFDPETDSWTEVTHMKSGRSGVGVAVTMEPCHKELIPCQC", "text": "FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting nfe2l2/nrf2 for ubiquitination (PubMed:18057000). Keap1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of nfe2l2/nrf2, a transcription factor regulating expression of many cytoprotective genes (PubMed:18057000). In response to oxidative stress, different electrophile metabolites trigger non- enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting nfe2l2/nrf2 nuclear accumulation and expression of phase II detoxifying enzymes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly cytoplasmic. SIMILARITY: Belongs to the KEAP1 family."}
{"protein": "MYKLEIDNLSVNYGVAGGAKTLALSQVNLTMERGDFVVALGASGCGKTTLLSCIAGFMEPSEGEIRLSGKVVRGPGAERGVVFQKHALMPWLSVADNVALGLRLRGVSRAERMRVAHEKLAAVGLEDVAGKPVYQLSGGMQQRVGIARALACDPAVMLMDEPLGALDALTRESIQALILKLWAKEQKIVFFITHSVEEALFLATRLIVMTPSPGRIAHTYELPFARRFIECGDARAVKADPEFIRYREEIIDLIHATA", "text": "FUNCTION: Part of the ABC transporter complex TauABC involved in taurine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Taurine importer (TC 3.A.1.17.1) family."}
{"protein": "MTGATLTVRVIRNFEYRTLKNVVFHDIDLATTTVDQFKKIIDERIQTDPSLKIYRTTHFDTLKIYVKAQQHKTQNLAINLDHDDWILNDGAKTLSLCGIENETELSYFELAAYKAYQANPVQKWL", "text": "SIMILARITY: Belongs to the UPF0538 family."}
{"protein": "MVANGHFAGVGDVLDAKNYEHGVQVIDEEKEFNPNLSNYLSYENVTPAGFNYHLISVFGSQSTGKSTLLNSLFGTHFSVMSETERRQTTKGIWLSKNKRLKSDKGQDNQTKMADNILVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQVGLYQGANMGLLKTVFEVNLELFLKDKRSNPRSLLFFVIRDFLGTTPLQNLQNTLLQDLNRIWNSLSKPAGLENSSITDYFDFAFAGLPHKNFQPEKFVDEVRKLSTRFCDGHRDPNKTDAKGTGSIEGGIFLPEYHRRIPADGFAVYAEGIWDQIVNNKDLDLPTQQELLAQFRCDEISREVLVAFDEAISPFEAKQAEAVQAGNPQVLGGLGSAMCNARMKSVKNFDTEASRYHKRVYQMKKSELQDKIDSRLKALFLGQLSAAHRSGIQEFTESVTAAVKAGQKRGASYDFAEIVTKERKLAIEKFEKEARAAVVEDTQWSNYQQELSLYQKDLENIGGQLRRDEMRRLATRVGRWVRSRLGESIDLEFNAIGSGRGGSGAPEFGDKPSEKSLWDRVWTLFVDTVLDAERRFTERASSFDASIDEVDVGLWRLRRKSWGVLRAKIDEEMMEGNILLKLRENFEDKFRYDDAGVPRIWRPNDDIESIYTRARESTLTLIPLLSRFRLAETNAPPPLDKWIGHTPSSATPADEEDLTPIGGVDEDEGKSLEEEMTMIGEAKKQDLTVRFKKTADGVYVEAKRSAIGGITQVPLYFYGLLLALGWNEIVAVLRNPAYFLLLFVCAVTAYVTYQLNLWGPIIKMTEAASQQALMEGKTRLREFLEASDTGLQAMAMSKGRNAEEYDMSNMKNRKSAGGFQNNRSHIDDADDDDDF", "text": "FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Enriched in the cortical ER. Concentrated in punctae along the ER tubules. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily."}
{"protein": "MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM", "text": "FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol (PubMed:25732826). Displays N-terminal acetyltransferase activity towards a range of N- terminal sequences including those starting with Met-Lys, Met-Val, Met- Ala and Met-Met (PubMed:21750686, PubMed:25732826, PubMed:27550639, PubMed:27320834). Required for normal chromosomal segregation during anaphase (PubMed:21750686). May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences (PubMed:21981917). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Note=Probably forms an intramembrane hairpin-like structure in the membrane. SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily."}
{"protein": "MACLMAAFSVGTAMNASSYSAAMTEPKSVCVSVDEVVSSNVDEVETDLLNGHLKKVDNNFTEAQRFSSLPRRAAVNIEFKDLSYSVPEGPWWKKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDADYKRDLGGDTDVNPFLWHRPAEEDSASMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMSVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPAYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIAETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER", "text": "FUNCTION: Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta- hydroxycholesterol and this transport is coupled to hydrolysis of ATP (PubMed:14668945). The lipid efflux is ALB-dependent. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cell membrane Note=Predominantly localized in the intracellular compartments mainly associated with the endoplasmic reticulum (ER) and Golgi membranes. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily."}
{"protein": "MDNEDQESLLLQGVPDNYGGVKVNLTEPMTIEDFVPKLRASLVYWSNQGTKGIWLKLADGLDNLIAPAKAEGFVCHHAEREYTMLTSWIADVPSTLPANASHRIGVGAFVLNKKTKEVLVVQEIDGHFKGTGVWKLPTGVVKEGENIWEGALREVEEETGIKTKFVEVLAFRESHQAFLEIKTDIFFLCELEPTTFEIKKQDSEILAAKWMPIEEYVNQPWNQKKELFRFMANICLKRLQEMEYMGFSKVLTTTSSGKESYLYCNTDHANLLNATRGLASTSG", "text": "FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear. SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MNELDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLSQYEHLIDDAIAWGKKNGKTQEQQVVAACDKLAVNFGAEILKIVPGRVSTEVDARLSFDKEKSIEKARHLVDLYQQQGVEKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHHYETIVMGASFRRTEQILALTGCDRLTIAPNLLKELQEKVSPVVRKLIPPSQTFPRPAPMSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL", "text": "FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily."}
{"protein": "MEEQNDFTWAVKNGDIANVKKSVEAKKDLISITDGNKRGPCHWAADFNQVEVLEYLISKGAKFDNTDDYGITPLLAAVYEGHTGAVELLVKKGANKSVVGPDGQTAYDAAEKADIKALLK", "text": "FUNCTION: May regulate NF-kappa-B transcription factor activity. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the myotrophin family."}
{"protein": "MRRMLSPRILLSSLPNASARKLFLIVLIIFVFWVVFMTSKDHTEFMVHLNNRIILRRWSIFKEFLHSEELKNTPASVEAELAVTAILEKLNQQIPPRPFQTHSSTTSAKQSTATIHNPQRTYCVGDQLNVLLVAKDYFGNRKEYGGDFLRARIFSPAMKAGTSGKVTDFNNGTYLVSFTLFWEGPVSLSILLMHPSEGVSALWRARNRGYGKIIFTGQFLNGTSPVLTECGLTLNTSAELCQYLDARDHEAFYCLKLPGVPCEALTHMTSKNSNISYLSLEEKLLFRRFNIGVEVVKNLSIVVSLCNNKTNKKKKKCQIGMETPSPGGYTLKGRWITAHCEQNEFRAIKDINNCLTRKLIYLMGDSTLRQWIYYLPKVVKTLKYFDRHGAGPFKTHILLDTERHIFVQWKKHSHPFVTNKLFSMKDDNYIPREIDQVAGDSGTAIVISFGQHFRPFPINVFIRRAINVKNAIERLFLRSPETKVIIKTENIREINEHVEIFSDFHGSIQNLIIRDIFRDLNVGIIDAWDMTVAYRSEDVHPPESVIESQIGMFLNYIC", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the NXPE family."}
{"protein": "MMSAAICTLLAVIATTSLGLLFLSIIRRGKLPPGPPPKPIVGNLHQFPKVNRAQVFDQWHRTYGPIVGLRLGLKKLILVGSYQVARELLDRRGAIYSSRPRVVMAGEIANRGNHTALMPYGPKWKLHNRVHSALMNPTMVKRYQYLQDIESRQLVHDLLQGSTSDFGARIHRYSSSLLFALAYGRRLPTSDAFEIQENAHIAHQFINNLAAGRWLVDAFPVLNYLPTWLAPWKKIGEQLYQRKFGLLQRHTALALEKPVWNWTKHFHGPKKPAEASWEELLNIIGVLYEAGADTTTSALEAFVMAAVLHPDAVRRVQAEIDALVGGAARMPSFEDVQQLPFVDAFVNETMRWRPIAPEGVPHSLMKEDEYEGFTIPKNSIVIANQWHMAMDPATFTDPQAFRPERWLEDPKLPISAFGFGRRACPGRHIALNSMKIVMCRLLWAYDFDHAYENGRKVTIDPDNFVREGVLSKPAPFKAALRVRSPAHEKTIQSALRESEQDEDKILAHIAAGLA", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aculenes, a unique type of norsesquiterpenes that contain a nordaucane skeleton linked to an L- proline moiety and are of mixed biosynthetic origin (PubMed:31618514). The pathway begins with the synthesis of dauca-4,7-diene by the terpene cyclase aneC using farnesyl pyrophosphate (FPP) as substrate (PubMed:31618514). The cytochrome P450 monooxygenase aneF then performs the initial oxidation at C-12 of dauca-4,7-diene to yield asperaculane D (PubMed:31618514). Asperaculane D is substrate of the cytochrome P450 monooxygenase aneD for C-10 hydroxylation to yield asperaculane E (PubMed:31618514). The cytochrome P450 monooxygenase aneG then converts asperaculane E into aculene D via C-2 oxidation (PubMed:31618514). The monomodular nonribosomal peptide synthtase aneB adenylates L-proline and the thiohydrolase aneE transfers this activated L-proline derivative to aculenes D and C to produce respectively aculenes B and A (PubMed:31618514). The dioxygenase aneA converts aculene D into aculene C, and aculene B into aculene A by introducing the 5,6-alkene moiety (PubMed:31618514). Asperculanes A, B, C and F, as well as 14-prolyl asperculane C, might be shunt products of the pathway (PubMed:31618514). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MFPNSILGRPPFTPNHQQHNNFFALSPSLYSHQQLIDAQFSFHNADLSRAVSLQQLTYGNVSPIQTSTSPLFRGRKRLSDEKNLPLDGKRQRFHSPHQEPTIVNHIVPLSDERRYSMSPLFHTHYVPDIVRCVPPFREISILEPREITLPEAKDKLSQQILELFEACQQQVSDLKKKELCRTELQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHDINDASRGTLSSYSLVLMVLHYLQTLPEPILPSIQKIYPESFSPSIQLHLVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEWRNKYICVEEPFDGTNTARAVHEKQKFDMIKDQFLKSWHRLKNRKDLNSILPLRAAILKR", "text": "FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation. Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2 subfamily."}
{"protein": "MGKAFSQLTSQKDEDKSILPDNPAMASKAANYFSTGNRKPSHSCVPCEKAASTSFVTCPTCQGNGEIPQELEKQLVALIPYGDQRLKPRRTKLSVFLAVTICLLIFSLTIFFLYPRNIVVHPVGLNSSTVAFDETHVQLNMTNVLNITNSNFYPVTVTQLTAEVLHQTSVVGQVTSSLRLHIGPLASKQMPYEVASRILDENTYKICTWPKIRVHHILVNIQGALTCSYLTHPQQLPFESFEYVDCRENMSMPHLELPRPA", "text": "FUNCTION: Activates macrophages and polarizes them into M1-like macrophages through the activation of the MAPK and NF-kappaB signaling pathway. Upon activation, up-regulates the expression of CD80, CD86, CD69 and MHC II on macrophages, and induces the release of pro- inflammatory cytokines such as TNF, IL1B, IL6, CCL2 and nitric oxide (By similarity). May play a role in inhibition of proliferation and migration (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TMEM106 family."}
{"protein": "MSQLTHINAAGEAHMVDVSAKAETVREARAEAFVTMRSETLAMIIDGRHHKGDVFATARIAGIQAAKRTWDLIPLCHPLMLSKVEVNLQAEPEHNRVRIETLCRLTGKTGVEMEALTAASVAALTIYDMCKAVQKDMVIGPVRLLAKSGGKSGDFKVEADD", "text": "FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). SIMILARITY: Belongs to the MoaC family."}
{"protein": "MIRHFLRDDDLSPAEQAEVLELAAELKKDPVSRRPLQGPRGVAVIFDKNSTRTRFSFELGIAQLGGHAVVVDSGSTQLGRDETLQDTAKVLSRYVDAIVWRTFGQERLDAMASVATVPVINALSDEFHPCQVLADLQTIAERKGALRGLRLSYFGDGANNMAHSLLLGGVTAGIHVTVAAPEGFLPDPSVRAAAERRAQDTGASVTVTADAHAAAAGADVLVTDTWTSMGQENDGLDRVKPFRPFQLNSRLLALADSDAIVLHCLPAHRGDEITDAVMDGPASAVWDEAENRLHAQKALLVWLLERS", "text": "FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
{"protein": "MSTAAKQNRSTSRVSKKKTAAPKEGAAKKSDKGHKYEYVELAKASLTSAQPQHFYAVVIDATFPYKTNQERYICSLKIVDPTLYLKQQKGAGDASDYATLVLYAKRFEDLPIIHRAGDIIRVHRATLRLYNGQRQFNANVFYSSSWALFSTDKRSVTQEINNQDAVSDTTPFSFSSKHATIEKNEISILQNLRKWANQYFSSYSVISSDMYTALNKAQAQKGDFDVVAKILQVHELDEYTNELKLKDASGQVFYTLSLKLKFPHVRTGEVVRIRSATYDETSTQKKVLILSHYSNIITFIQSSKLAKELRAKIQDDHSVEVASLKKNVSLNAVVLTEVDKKHAALPSTSLQDLFHHADSDKELQAQDTFRTQFYVTKIEPSDVKEWVKGYDRKTKKSSSLKGASGKGDNIFQVQFLVKDASTQLNNNTYRVLLYTQDGLGANFFNVKADNLHKNADARKKLEDSAELLTKFNSYVDAVVERRNGFYLIKDTKLIY", "text": "FUNCTION: May function as protective capping of the single-stranded telomeric overhang. May also participate in telomere length regulation during DNA replication. Binds specifically to the T4G4-containing extension on the 3'strand and protects this region of the telomere from nuclease digestion and chemical modification. SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. SIMILARITY: Belongs to the telombin family."}
{"protein": "MAEEKKEELFTSIGNAAQNVSTAEDREGNGVQEVESLCMECGKNGTTKLLLTVIPYFREVVLMSFECPHCGFKNAQVQHAETIQPEGSKITFHVEDKEDLNRTVVKSQEAIVSIPEIQLEIPGRLGQLTTIEGILSNVVDDLSKEQESRKESAPQLYDQINAFIEKVNSLRSGSVPFTITVDDITGNSWIEMKPGRDGDRWSQVSYKRTLEQNTKLGLVDTDQPEDVKTQTNNASNTLKHDATAVEVDPNEVHTFHATCPSCSHQCDTHMKLLDIPHFKEVIIMSTVCDRCGYRSNEVKTGGEIPPKGRKITLKVMDAEDLSRDILKSETASLKIPELGLDLFPGTLGGRFTTIEGLLAQVYDELYGRVFSQETDSMTPEQVANWQQFLCNLTAAREGATQFTLILDDPLSQSYLQNYYAPDPDPNMTIEEYERSFQVNEELGLNDMKTENYEKDGGKK", "text": "FUNCTION: Acts as a protein folding chaperone for elongation factor 1- alpha. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the nucleus after nutrient stimulation. SIMILARITY: Belongs to the ZPR1 family."}
{"protein": "MKTPLTEAVSAADSQGRFLSSTAVQVAFGRFRQATSGLAAAKALSEKADSLASGARNAVYSKFPYTTSMTGANYASTQTGKDKCVRDIGYYIRMVTYCCVVGGTGPMDDYLVAGIAEINRTFDLSPSWYVEALKYVKANHGLSGDSAVEANSYIDYAINALS", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=Part of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family."}
{"protein": "MKKTLLASSLAVGLGIVAGNAGHEAHASEADLNKASLAQMAQSNDQTLNQKPIEAGAYNYTFDYEGFTYHFESDGTHFAWNYHATGTNGADMSAQAPTTNNVAPSAVQANQVQSQEVEAPQNAQTQQPQASTSNNSQVTATPTESKSSEGSSVNVNAHLKQIAQRESGGNIHAVNPTSGAAGKYQFLQSTWDSVAPAKYKGVSPANAPESVQDAAAVKLYNTGGAGHWVTA", "text": "FUNCTION: Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the transglycosylase family. SceD subfamily."}
{"protein": "MKKFLVLLIALIMIATLLVVPGVQTSAEGSYADLAEPDDDWLHVEGTNIVDKYGNKVWITGANWFGFNCRERMLLDSYHSDIIADIELVADKGINVVRMPIATDLLYAWSQGIYPPSTDTSYNNPALAGLNSYELFNFMLENFKRVGIKVILDVHSPETDNQGHNYPLWYNTTITEEIFKKAWVWVAERYKNDDTIIGFDLKNEPHTNTGTMKIKAQSAIWDDSNHPNNWKRVAEETALAILEVHPNVLIFVEGVEMYPKDGIWDDETFDTSPWTGNNDYYGNWWGGNLRGVKDYPINLGKYQSQLVYSPHDYGPIVYEQDWFKGDFITANDEQAKRILYEQCWRDNWAYIMEEGISPLLLGEWGGMTEGGHPLLDLNLKYLRCMRDFILENKYKLHHTFWCINIDSADTGGLFTRDEGTPFPGGRDLKWNDNKYDNYLYPVLWKTEDGKFIGLDHKIPLGRNGISISQLSNYTPSVTPSPSATPSPTTITAPPTDTVTYGDVNGDGRVNSSDVALLKRYLLGLVENINKEAADVNVSGTVNSTDLAIMKRYVLRSISELPYK", "text": "FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta- glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MAAAGAGSGRAAVSRSRPPPARFRGCLAGALLGDCLGAVFEGRSVVKLPDLLSFLRGLEPPGGEGEPAGSARRETLSYTDDTAMSRCVVQSLLAKREFDEVDMAKRFAEEYKKEPNRGYGMAVVNVFKKLLSPQCSDVFEPARAQFNGKGSYGNGGAMRVAGIPLTYSDVQDVKKFAKLSAELTHANSLGYNGAILQALAVHLALQGEVSRETFLEQLISHMEDIEADDKSLTDARALGFEDLPFSRRLKKIKEFLELSSVPKEDVLFELGNGIAALRSVPTAIYSFLRCMEADPDIPEHYNNLQRTIIYCISLGGDTNTIATMAGAIAGAYYGEEQVPPSWEQSCEAFQETQKMANSLHELYCQQL", "text": "FUNCTION: ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP- ribose and acts on different substrates, such as proteins ADP- ribosylated on serine and threonine, free poly(ADP-ribose) and O- acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP- ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (By similarity). Also hydrolyzes free poly(ADP- ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl- ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers. SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome Mitochondrion matrix Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family."}
{"protein": "MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVNMVPEELRDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEVFVPSFHLSLDEISQDSPL", "text": "FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 5DNU family."}
{"protein": "MKAPILKKLALISVLSLACTSWVHAAERIAFIPKLVGVGFFTSGGQGAVAAGKTLGVSVTYDGPTEPSVAGQVQLINNFVNQGYDAIVVSAVSPEGLCPALKRAMKRGVKILTWDSDTSPECRSIYINQGTPNQLGGMLVDMTANQVKKEQAKVAFFYSSPTVTDQNQWVXQAKDKIAAEHPGWEIVTTQFGYNDATKSLQTAEGILNAWSDLDAIIAPDANALPAAAQAAENLKRQDVAIVGFSTPNVMRPYLERGTVKQFGLWDVVSQGKISIHVANELLRKGDLNVGDKLDIPDIGTVAVAPNSIQGYSYEAKGNGIVVLPERVIFTKDNINQYDF", "text": "FUNCTION: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Binds AI-2 and delivers it to the LsrC and LsrD permeases (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family."}
{"protein": "MQSLYNSKYAHIFKGPVAKHVTYKFHDLEVTYANIPHLDITVENITPDMIYKSAHLTCSSLFRMYGLSPETDGKLWVLLYRLFTVNEGSYDHRNTIGLELYINHLTAMYEELKVKSELLACVNFALGLGYFYMSYFVMYNHKKGNLLNYLHELCHVIHRYIDQIRLLHMRNPNNYKIEEFMRILRDVFKHYRISQFYDHVMYNHIFGLTRIVSNILCGCSSVCKEHYSIKDRDKSVRGIKTRVKPASAGQSPVLSIPVGFYVNQAISIKTRFPTTGPELFGQAENVIGILRSPVLYHVSQDDVAKIEMCLKTDFYMTEFYNNKEANNYIIPIQSPGCREQEEMMLKLFNNVVFCMYLACQVRQVILSQWKILLTLFRNQFLKIVSLMKGDSFIKICIERLADDIQHHRQSLGAVFKAFLTILPDVLKHVGFPVNDSNALRAHLLVEYLVDDKFAPEIPYDTYVRMARDYRLEILRGNRMPFPIFTLDLAETRNLIFSNEAFHAFYNVISYDDIIPNYSSF", "text": "SIMILARITY: Belongs to the herpesviridae U4 family."}
{"protein": "MAGSLPPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDQAQRRVLRGVDDLDFFIGDEAIDKPTYATKWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKYDVDPRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSICRHNPVFGVMS", "text": "FUNCTION: Plays a role in the organization of the actin cytoskeleton. May function as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. May decrease the metastatic potential of tumors. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection. SIMILARITY: Belongs to the actin family. ARP3 subfamily."}
{"protein": "MIKTLKRIPLVFLIAIMACSNSGDNGKDKVEEQEQAQEQGEKKGQGEERDKEDGIDGLQPTFLADQDPKPDDKKWIKVEGVSDEFNDSELDLTKWSPTPEFIWNGQDRGWYGGSRSLFEADNVSVGNGFLRIEGEKFDSPKYSPKDNTDTPPQRRYGGAYVYGKTLAEPGYYIEARMRASKTAMSAAFWLKTETKPCGENLNDGENLEIDIQECVGVFTGELGDEWTKDDWAVNANWDRIFHYNTHRHNSPCNNIGDRQTKGGKANFDKKNSDEFHIYAAYWHADGSKIDFYIDGELEKSITPVIPFKGALRLIMSSNFYDWIEETSAEDMGFNRPLEDRYTQFDWVRVWQLEDL", "text": "FUNCTION: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6- sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6- sulfate-(1->3)-beta-D-galactose. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 16 family."}
{"protein": "MPSANVSPPCPSGVRGGGMGPKAKAEASKPHPQIPVKLPFVTAPDALAAAKARMRDLAAAYVAALPGRDTHSLMAGVPGVDLKFMPLGWRDGAFDPEHNVILINSAARPERQRFTLAHEIGHAILLGDDDLLSDIHDAYEGERLEQVIETLCNVAAAAILMPEPVIAEMLERFGPTGRALAELAKRAEVSASSALYALTEQTPVPVIYAVCAPGKPPREQAASDEDAGPSTEKVLTVRASSSTRGVKYTLASGTPVPADHPAALALATGMEVREESYVPFRSGRKMKAEVDAYPSRGIVAVSFEFDPARLGRKDSEQADRDEPQDAAQ", "text": "FUNCTION: Plays a central regulatory role in DNA repair and protection pathways in response to radiation stress (PubMed:12804570, PubMed:22051194). Acts as a site-specific metalloprotease that cleaves and inactivates the repressor protein DdrO, resulting in induced expression of genes required for DNA repair and cell survival after exposure to radiation (By similarity). Regulates the expression of dozens of proteins from different pathways, including the important DNA repair proteins RecA and PprA (PubMed:12399492, PubMed:12804570, PubMed:22051194). Binds to the promoters of recA and pprA (PubMed:22051194)."}
{"protein": "MTLNNLQALLRRVAAREDSGHVVVYGMGNTKAFKSYSYQDLLRVAIKASVALRKTSDLHPGSVILLHFDNHWDNIVWFWAASFAGCLPAISASFSNDASQRTAHIERLSTTLMHPLCLTNERIMADFAGQDAVQPLAVETLVLNGDVSFEALPQEHPEPSLSDDALLLFTSGSSGNSKGVCLSHGQILASISGKYAVRPLPDNTSFLNWVGLDHVAAIVEIHLQAMYALKTQVHVPAADILSSPATFLQLLEKHRVSRTFAPNFFLAKLRDLLQENDSLPEPRRWDLRSLEYVASGGEANVTKTCDRLSEYLVAFGAPKDVIVPGFGMTETCAGSIFNTRCPEYDKSRSAEFASVGTCMPGISMRVTDLSNNALPSGEIGHLQLTGPVVFKRYFNNTSATQEAFTPDGWFKTGDMGCIDENGCLTLTGRAKENMIINGVNHSPHEIETALDKIPGLTPSYSCCFSFFPSGGETEEICVVYLPTYSPDDLAARAQTADAISKTVLMSTGSRPHVLPLEREALPKSSLGKLSRAKIKAAYEKGEYATYQNANNELMRRYRESTRAEPQNDLEKTLLEVFTRSLSITDDAFDVKTPIFDVGINSVELIRLKRDIEDHLGMAASAIPMIMLMTHSTVRDLATALEKLQGPREYDPVVTLQSHGHKNPLWLVHPGAGEVLVFINLAQYIVDRPVYALRARGFNDGEQPFETIEEATASYYNGIRSRQPHGPYALAGYCYGSMLAFEVAKMLESHGEEVRFLGSFNLPPHIKMRMRELDWKECLLHLAYFLDLVSQERSREMSVELAGLSHDEILDSVIQNANMERYAELSLNRPLLVRWADVAYELHRMAFDYDPAGCVAGMDVFFSIPLAIAAASKTEWRNVHLSQWEDFTRTVPKFHDVAGEHYSMIGPDHVFSFQKTLRKALDERGM", "text": "FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspulvinones (PubMed:29305695, PubMed:23841722, PubMed:28791090). The nonribosomal peptide synthetase apvA is responsible for the production of aspulvinone E, the core structure of aspulvinones (PubMed:29305695, PubMed:23841722, PubMed:28791090). ApvA first activates 4-hydroxyphenylpyruvate (HPPA) through its A domain to AMP-HPPA (Probable). The HPPA unit is then loaded to the T domain and eventually transferred to the TE domain (Probable). Upon loading of another HPPA unit to the T domain, the TE domain promotes the enolate formation on the unit attached (Probable). The next step involves head to tail Claisen condensation, followed by the keto-enol tautermerization and a nucleophilic attack on the carbonyl carbon to yield the furanone partial structure (Probable). A spontaneous oxidation at the beta-carbon of the thioester might occur in aerobic condition (Probable). The TE domain then catalyzes the hydrolysis of the thioester, followed by spontaneous decarboxylation, dehydroxylation and keto-enol tautermerization to give the aspulvinone core (Probable). Aspulvinone E is highly unstable and converted to isoaspulvinone E in the presence of light (PubMed:29305695). The structural diversity of the aspulvinones suggests that other tailoring enzymes are involved and have still to be identified (Probable). SIMILARITY: Belongs to the NRP synthetase family."}
{"protein": "MSKDIYYSDKYYDEQFEYRHVVLPKELVKMVPKTHLMTEAEWRSIGVQQSRGWIHYMIHKPEPHILLFRRPKTD", "text": "FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases Cdk1 and Cdk2, and is essential for their biological function. SIMILARITY: Belongs to the CKS family."}
{"protein": "MVLSIRSQIIIGVVSSIPLTSTILAIAYILMWFNGHMTLTLTLTTIITSCLTLLICSIFINPLIQKIKQFNIKTKQFANGNYASNDKTFNSPKEIYELNQSFNKMASEITQQMNQIKSEQQEKTELIQNLAHDLKTPLASIISYSEGLRDGIITKDHEIKESYDILIKQANRLSTLFDDMTHIITLNTGKTYPPELIQLDQLLVSILQPYEQRIKHENRTLEVNFCNEIDAFYQYRTPLERILTNLLDNALKFSNVGSRIDINISENEDQDTIDIAISDEGIGIIPELQERIFERTFRVENSRNTKTGGSGLGLYIANELAQQNNAKISVSSDIDVGTTMTVTLHKLDITS", "text": "FUNCTION: Member of the two-component regulatory system SaeR/SaeS involved in the regulation of staphylococcal virulence factors in a strain-dependent fashion. Probably functions as a membrane-associated protein kinase that upon sensing the appropriate signal, autophosphorylates and in turn activates the cytosolic response regulator SaeR. SaeR/SaeS activates the expression of exoproteins involved in adhesion and invasion of host cells, including hemolysins (hla, hlb, hlgC), coa, DNase, spa and cell wall-associated proteins (emp, eap, fnbA, fnbB, efb). Represses the expression of type 5 capsular polysaccharide (cap operon). Also modulates the expression of several other genes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MASAVRGSRPWPRLGLQLQFAALLLGTLSPQVHTLRPENLLLVSTLDGSLHALSKQTGDLKWTLRDDPVIEGPMYVTEMAFLSDPADGSLYILGTQKQQGLMKLPFTIPELVHASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGPSTPRLYIGRTQYTVTMHDPRAPALRWNTTYRRYSAPPMDGSPGKYMSHLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQDGLRQLPHLTLARDTLHFLALRWGHIRLPASGPRDTATLFSTLDTQLLMTLYVGKDETGFYVSKALVHTGVALVPRGLTLAPADGPTTDEVTLQVSGEREGSPSTAVRYPSGSVALPSQWLLIGHHELPPVLHTTMLRVHPTLGSGTAETRPPENTQAPAFFLELLSLSREKLWDSELHPEEKTPDSYLGLGPQDLLAASLTAVLLGGWILFVMRQQQPQVVEKQQETPLAPADFAHISQDAQSLHSGASRRSQKRLQSPSKQAQPLDDPEAEQLTVVGKISFNPKDVLGRGAGGTFVFRGQFEGRAVAVKRLLRECFGLVRREVQLLQESDRHPNVLRYFCTERGPQFHYIALELCRASLQEYVENPDLDRGGLEPEVVLQQLMSGLAHLHSLHIVHRDLKPGNILITGPDSQGLGRVVLSDFGLCKKLPAGRCSFSLHSGIPGTEGWMAPELLQLLPPDSPTSAVDIFSAGCVFYYVLSGGSHPFGDSLYRQANILTGAPCLAHLEEEVHDKVVARDLVGAMLSPLPQPRPSAPQVLAHPFFWSRAKQLQFFQDVSDWLEKESEQEPLVRALEAGGCAVVRDNWHEHISMPLQTDLRKFRSYKGTSVRDLLRAVRNKKHHYRELPVEVRQALGQVPDGFVQYFTNRFPRLLLHTHRAMRSCASESLFLPYYPPDSEARRPCPGATGR", "text": "FUNCTION: Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MSNTGTTGRIPLWLVATVAGLAVIALLGVFFYGSYSGLGSSL", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbJ family."}
{"protein": "MWLPLLLGVLLWAALWLLRDRQCLPASDAFIFITGCDSGFGRLLALRLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDVTDPQSIRQAVKWVETHVGEAGLFGLVNNAGVAGIIGPTPWQTREDFQRVLNVNTLGPIGVTLALLPLLLQARGRVINITSVLGRLAANGGGYCVSKFGLEAFSDSLRRDVAPFGVRVSIVEPGFFRTPVTNLETLEDTLQACWARLPPATQALYGEAFLTKYLRVQQRIMNMICDPDLAKVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARLVDAVLAWVLPKPAQTVY", "text": "FUNCTION: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner (PubMed:7544779, PubMed:7836368, PubMed:9654122). Has no activity towards all-trans retinal (PubMed:9654122). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE) (By similarity). Also recognizes steroids (androsterone, androstanediol) as its substrates (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein; Lumenal side Microsome membrane. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MTAQNPNLAALSAAGVSVWLDDLSRDRLRSGNLQELIDTKCVVGVTTNPSIFQKAFAEGHAYDSQIAELAARGADVDATIRTVTTDDVRNACDVLTREWENSDGVDGRVSIEVDPRLAGDTDKTIAQAVELWKIVDRPNLFIKIPATQAGLPAITAVLAEGISVNVTLIFSVERYRAVMDAYLAGMEKAREAGHDLSKIHSVASFFVSRVDTEIDKRLEKIGGERALALRGQAGVANARLAYAAYQEVFEGGQRYQALKADGARVQRPLWASTGVKNPDYSDTLYVTELVAPNTVNTMPEKTIDAVADHGVIRGDTVTGTGPDAQRVFDELAAVGVDLPDVFVVLENEGVEKFVDSWTELMEETQKQLGSASK", "text": "FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily."}
{"protein": "MKKVIVGTLFALVLVLAGCSSQNSDTKKTGDKLNVVATYSILADIVKNVGGDKIELHSIVPVGVDPHEYDPLPDNIQSAADADLIFYNGLNLETGNGWFDRMLETADKSRDDKDQVVELSKGVKPKYLTEKGKTSETDPHAWLDLHNGIIYTENVRDALVKADPDNANFYKENAKKYIDKLATLDKEAKQKFADLPENQKTLVTSEGAFKYFAARYGLKAAYIWEINTESQGTPDQMKQIISIVEKERVPNLFVETSVDPRSMESVSKETGVPIFAKIFTDSTAKKGEEGDTYLEMMRYNLDKIHDGLAK", "text": "FUNCTION: This protein is probably a component of a manganese permease, a binding protein-dependent, ATP-driven transport system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 9 family."}
{"protein": "MPNKKAARNAYFFFALDMIPELRRRGLQVSGVREAIPLCSEDWALLSADQKEAYAEKARLLKNDPDSTSTYNDGVFGQRKRNATKSSDFSSVGFFQLNDQRNCVTQRTVPAMNIDISFNKNKAPDQHVCYFINIFSHGDMPSLCEQRYVPCEIACVRYSLREGILGSFHDFIDPGELPRGFRYHCQSGSASTHQIPISGFELANSDYHNMFRKLCSFVCPTPCPVVPVYTKANDIYRVDWCLQWLANKAGMENHFRVQEVETLIIKFYQDKLQEEPSRPTVSRLLDVVQWDYSSNTRCKWHEDNDMWCCALASCKKIAYCISKALASVYGVTLTPAHLPNPERSRNQNSVNPKVVVLDAKRFQRVCSSDPKYSTDKSERSSFEPRGVKPYQGPSGGGRGILRLLETLAASQNSSG", "text": "FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with piP-bodies suggests a participation in the secondary piRNAs metabolic process. Required for the localization of germ-cell factors to the meiotic nuage (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs (By similarity). SIMILARITY: Belongs to the maelstrom family."}
{"protein": "MIEPSIIPVLVENTEEKTFKFQPGQVSQWLTGQGLQHQILEPDLLGVELIGVEPSELQKIAEALKSNGFDYLQCQGGYDEGPGGRLVSFYHLIKLGTIADHYLTPNTLPPNSILKEVRLKVFLLRDGNLSVPSLYSIFRGSDWQERETFDMFGISYEGHPHPKRLLMPEDWKGYPLRKDYIQPDFYEMQVAY", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the complex I 30 kDa subunit family."}
{"protein": "MKHLPKHLRPRWRYFAVGIETWPDADLGRRGFQRALWYAAGNLLGDAGSADADLTLLSFSHDGGEGEAIVRARHGHVDDARATIACVSEVDDEPVGVRVRGISGTVRACEERYMGRAGGSSTQRDVAFEGAERSAVVREDAYDVWTGSAYVGAAAFDTE", "text": "FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 2 family."}
{"protein": "MAPWPHGNSSLVPWPDVPTLAPNTANTSGLPGVPWAAALAGALLALAVLATVGGNLLVIVAITRTPRLQTMTNVFVTSLAAADLVMGLLVVPPAATLVLTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRRARAAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCCAFASNMPYVLLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRWELGRFPPEESSPALSRSLAPAPAGTCAPPEGVPACCRRPARLLPLREHRALCTLGLIMGTFTLCWLPFFLANVLRALGGPSLVPDPAFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCHCGGRLPREPCAADRPASSPRAPLRPGPAPRSPGFASGSTGLLGEFLRPEGQEATLR", "text": "FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta- 3 is involved in the regulation of lipolysis and thermogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB3 sub-subfamily."}
{"protein": "MRLTLPRLNAAYIVGAARTPVGKFNGALKSVSAIDLGITAAKAAVQRSKVPADQIDEFLFGQVLTANSGQAPARQVVIKGGFPESVEATTINKVCSSGLKTVALAAQAIKAGDRNVIVAGGMESMSNTPYYSGRGLVFGNQKLEDSIVKDGLWDPYNNIHMGNCCENTNKRDGITREQQDEYAIESYRRANESIKNGAFKDEIVPVEIKTRKGTVTVSEDEEPKGANAEKLKGLKPVFDKQGSVTAGNASPINDGASAVVVASGTKAKELGTPVLAKIVSYADAATAPIDFTIAPSLAIPAALKKAGLTKDDIALWEINEAFSGVALANLMRLGIDKSKVNVKGGAVALGHPIGASGNRIFVTLVNALKEGEYGVAAICNGGGASTAIVIKKVSSVE", "text": "FUNCTION: Essential for n-decane utilization. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MTESIDLNRSESESDNNTDDVTPIFAIDDSSKGRVSGPTRRSTKGGWTAEEDQILTNVVKKYQGRNWKRIAECLPGSEENRRNDVQCQHRWLKVLDPSLQKGAWKKEEDELLSELVKDYMENDRPPWSKISKELPGRIGKQCRERWHNHLNPTIIKSPWTREEELILVQAQRGNGNKWAEIAKLLPGRTENNIKNHWNCSVKKRLEQFPSNLFSGVVYGSKPSSGFEYNFFNQRNTMVESCITSQIKEAAKSPQRDFLDLTLGLNWRSISSSTSSLRGEESVSSSVDSVCARLNACLETPQNSNNDTVCVKEVREMKERLRMAARTFDTPSIISKTSSPASGLKRLRQKYDTPFPTDARSHMSSEEDHSVSASPSSKYRFVKRNTCSGSKPLERRLDFDFLLWDEHGRRNGIVNFSVRILPQKSDLKSGLVRPFWLR", "text": "FUNCTION: Transcription factor that binds 5'-AACGG-3' motifs in gene promoters (By similarity). Required for proper circadian rhythm (PubMed:18426557). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKITRQKHAKKHLGFFRNNFGVREPYQILLDGTFCQAALRGRIQLREQLPRYLMGETQLCTTRCVLKELETLGKDLYGAKLIAQKCQVRNCPHFKNAVSGSECLLSMVEEGNPHHYFVATQDQNLSVKVKKKPGVPLMFIIQNTMVLDKPSPKTIAFVKAVESGQLVSVHEKESIKHLKEEQGLVKNTEQSRRKKRKKISGPNPLSCLKKKKKAPDTQSSASEKKRKRKRIRNRSNPKVLSEKQNAEGE", "text": "FUNCTION: Involved in rRNA-processing and ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP23/FCF1 family. UTP23 subfamily."}
{"protein": "MGTLSCDSTPRLATAPLGRRVTEGQIPETGLRKSCGTATLENGSGPGLYVLPSTVGFINHDCTRVASPAYSLVRRPSEAPPQDTSPGPIYFLDPKVTRFGRSCTPAYSMQGRAKSRGPEVTPGPGAYSPEKVPPVRHRTPPAFTLGCRLPLKPLDTSAPAPNAYTMPPLWGSQIFTKPSSPSYTVVGRTPPARPPQDPAEIPGPGQYDSPDANTYRQRLPAFTMLGRPRAPRPLEETPGPGAHCPEQVTVNKARAPAFSMGIRHSKRASTMAATTPSRPAGHRLPGRCC", "text": "SIMILARITY: Belongs to the ODF3 family."}
{"protein": "MRIKDAIIKIFYTRKDVSEIYLVIRDRVKGTSEIPFSNIERVDNYYIYLNDGETVIPLHRVIEIREKDKTLWKR", "text": "SIMILARITY: Belongs to the UPF0248 family."}
{"protein": "MYEQQQHFMDLQSDSGFGDDSSWLAGDDDLRLSPHQSAAGTNSGNENLDRRLLKDLVEMVPLIEHYMEHKERSSFKRRGSMIYTKMPSKESLSRRGRNASQTVPGRKKRDQEGNDDVMNNSREDDENAKALAGAEKEEMSRLREQVNDLQTKLSEKEEVLKSMEMSKNQVNEIQEKLEATNRLVAEKDMLIKSMQLQLSDTKIKLADKQAALEKTQWEAKTTGTRAIKLQEQLDAVEGDISTFTRVFETLAKTDSKKPDRDYDAVPYEFDHLPYLDDVDETDLRKMEEARLAYVAAVNTAKEREDEESLVMAAQARAYLQSLAFTY", "text": "FUNCTION: Prevents homeodomain proteins (e.g. STM) association to plasmodesmata and, consequently, cell-to-cell transport. Binds to RNA. Alters STM RNA binding capacity (PubMed:17965274). Regulates cytoskeleton (e.g. actin) organization that determinates cell shape (PubMed:8893552, PubMed:19074626). Regulates stomata patterning and drought tolerance (PubMed:19074626). Involved in restricting tobamovirus (e.g. oilseed rape mosaic virus) infectivity, probably by interfering with cell-to-cell virus movement (PubMed:19074626). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Microtubule-associated and stabilizer (PubMed:17965274, PubMed:19074626). Localized in cytosolic punctae when associated with STM (PubMed:17965274). SIMILARITY: Belongs to the microtubule binding protein 2C family."}
{"protein": "MSSLPVMVLFGLSFPPVFFVLMVSLTLFFVVNRLLQPTGIYDFVWHPALFNSALFCCLFYLLFRYGL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AaeX family."}
{"protein": "MTQSNPNEQSVELNRTSLYWGLLLIFVLAVLFSSYFFN", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbL family."}
{"protein": "MMVSSHLGSPDQAGHVDLASPADPPPPDASASHSPVDMPAPVAAAGSDRQPPIDLTAAAFFDVDNTLVQGSSAVHFGRGLAARHYFTYRDVLGFLYAQAKFQLLGKENSNDVAAGRRKALAFIEGRSVAELVALGEEIYDEIIADKIWDGTRELTQMHLDAGQQVWLITATPYELAATIARRLGLTGALGTVAESVDGIFTGRLVGEILHGTGKAHAVRSLAIREGLNLKRCTAYSDSYNDVPMLSLVGTAVAINPDARLRSLARERGWEIRDFRIARKAARIGVPSALALGAAGGALAALASRRQSR", "text": "FUNCTION: Likely catalyzes the dephosphorylation of O-phospho-L-serine into L-serine. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family."}
{"protein": "MAAKLMHAIQYSGYGGGTDALKHVEVAVPDPKSDELLLKIEAATLNPIDWKIQKGVLRPLLPRKFPTIPGTDVAGEVVQAGSAVNRFKTGDKVVAVLSHATGGALAEYAVAKENLTVARPPEVSAAEGAALPVAALTAHQALTQFANIKLDGSGERKNILITAASGGVGHYAVQLAKLGNTHVTATCGARNLDFVKGLGADEVLDYKTPEGASLTSPSGKKYDYVVHGASGIPWSTFEPNLSEAGKVIDLTPGPTAMMTFAWKKLTFSKKQLVPLLLIPKIPNFEYVVNLVKEKKLKTVIDSKHPLSKGEDAWSRIMGGHATGKIIIEP", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
{"protein": "MRNGRCLVTPFVTAQRLANLRNTLWNRQQIAFSTTTASSSTSPIQESSSPLSIRFEYGLPLLDVPLPSRNEPCQFTMRPLSDTIGSLCEFLRQEDRGIDYVAVYGTNGVKLATCTSIEHLLQFGSFRLRLNDKFFDVTVPKTGTMPYDSDKLRQLDDLRATVASLHAALCVDEYKLSREKKLLLQLENAETLLAPLHDAKRKIEQECEAHTDRVMWAGFAAMGVQTGLFARLTWWEYSWDIMEPVTYFATYSTVCATFGYYLYTQQSFEYPSARERVYTKQFYRRAQKQNFDIEKYNRLVTEVDELRNQLKRMRDPLFQHLPVSYLSNLEAEK", "text": "FUNCTION: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria (PubMed:25313960, PubMed:31983639). Constitutes a pore-forming and calcium-conducting subunit (By similarity). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways (By similarity). Required for rapid mitochondrial calcium uptake and mitochondrial reactive oxygen species (mtROS) production after wounding (PubMed:25313960). In addition, together with mitochondrial calcium regulator micu-1, required for mitochondrial calcium uptake following axon injury in PLM touch receptor neurons (PubMed:31983639). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MCU (TC 1.A.77) family."}
{"protein": "MSAPKNEMYYSLLEWFKTLNLNAPHADAESLADGVALAQALNQFAPESFTDAWLSKIKASAVGSNWRLRMSNLKKVTQSVYDYYSDVLNYSLSDFSKPDLQSIAEKCDLGELERLLQLVLGCAVNCAEKQSYITEIMCLEEELQANIMRALQELEATRQASSAEGGVVSSLSRSPRTGILDSKAVQEDRDALAQKCFETEKKMLLLIDEKTNLQQELHKLQQEFARLEQHSTVIGDDGVSLGPVQSGSVRYNELRRQLDLLKEELLQSEGAREDLKLKAQQQDTDLLHMQMRIEELMKSSAEVTTLKDEVDVLRESNDKLKICEAQLDTYKKKLEDYNDLKKQVKILEERSADYVQQNAQFEEDAKRYANTKGQVELFKKEIQDLHAKLDAESSKNVKLEFDNKNLDGKNLALQRAKDSLLKERDNLREAVDELKCGQLSSNTALTGTTVSRELQPSATVEKLQRLEAENKALREGQGGQTALAQLLDDANKRCENLREQLKTANERILSLSHASQSDDPILKESEFGKQIKQLMELNEQKTLQLEEAVTQSTSLQCKVTQLETNLSAREQEILVYDAKYRKCVEKAKEVIKSIDPRIASALDASVLEKSADLVEDEPKPKMSVMEEQLMTSAFYRLGVNAQRDAIDSKLAILMGSGQTFLARQRQSAPRKSLSAMKSK", "text": "FUNCTION: Involved in endocytic trafficking by stabilizing organelles of the endocytic pathway. Probably acts as a cytoskeletal linker protein required to tether endosome vesicles to the cytoskeleton. Involved in modulation of endocytosis at stages required for down- regulation of membrane proteins that control synapse size. Not involved in synaptic vesicle recycling. Required in R7 cells for boss endocytosis into multivesicular bodies (MVBs). Has a role in regulating adult longevity. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Endosome Synapse Note=Enriched at neuromuscular synapses, in both presynaptic and postsynaptic regions. SIMILARITY: Belongs to the hook family."}
{"protein": "MEQTEFKEYIHDNLALVLPKLKENDDLVKNKKMLANGLVFYYLYFSEMTDENKVSEAIKTLIKDEETLTLDQVKKRLDQLDARPVETAKKTIESILNGNCAVFINGLDKAYILTTGKKKTRSLTEPTTEKVVRGPKVAFVEDIDTNLALIRQRTSHPKLITKKIMIGENKLKPAAIMYIEGKAKKSVIKEVKARLKNIQLEDIQDSGTLEELIEDNKYSPFPQIQNTERPDKVSSALFNGRVAILVDSSPFVLLVPVSLGILMQSPDDYYERWISASLIRSLRFASIFITLFLSSIYITLVSFHQGLLPTALAVTISANRENVPFPPIFEALLMEVTIELLREAGLRLPNPLGQTIGLVGGVVIGQAAVEANLVSSILVIVVSVIALASFTVPQYGMGLSFRVLRFISMFSAAILGLYGIILFMLVVYTHLTRQTSFGSPYFSPNGFFSLKNTDDSIIRLPIKNKPKEVNNPNEPKTDSTET", "text": "FUNCTION: Forms a complex at the inner spore membrane which acts as a receptor for L-alanine, thus is involved in the stimulation of germination in response to alanine. Can stimulate germination in the absence of GerD and GerK gene products (fructose and glucose receptors, respectively), but the response is improved in their presence. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GerABKA family."}
{"protein": "MRKYQARIISIILAMIFIMFWDYLFYFIGKNPINWPVDIVYTAVTLVSVWMLAYYIDEKQQLVKKMKDNEWKYKQLSEEKNRIMDNLQEIVFQTNAKGEITYLNQAWASITGFSISECMGTMYNDYFIKEKHVADHINTQIQNKASSGMFTAKYVTKNGTIFWGEVHYKLYYDRDDQFTGSLGTMSDITERKEAEDELIEINERLARESQKLSITSELAAGIAHEVRNPLTSVSGFLQIMKTQYPDRKDYFDIIFSEIKRIDLVLSELLLLAKPQAITFKTHQLNEILKQVTTLLDTNAILSNIVIEKNFKETDGCMINGDENQLKQVFINIIKNGIEAMPKGGVVTISTAKTASHAVISVKDEGNGMPQEKLKQIGKPFYSTKEKGTGLGLPICLRILKEHDGELKIESEAGKGSVFQVVLPLKSDS", "text": "FUNCTION: Phosphorylates the sporulation-regulatory protein Spo0A a transcription factor that also controls biofilm formation (Probable). Requires FloT and FloA for localization to DRMs and for activity (PubMed:20713508). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Membrane raft; Multi-pass membrane protein Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. Lost from DRM in the absence of farnesyl diphosphate phosphatase YisP or when cells are treated with YisP inhibitor zaragozic acid. Colocalizes with FloT in DRMs (PubMed:20713508, PubMed:26297017). Another study shows KinC foci are membrane assemblies of 85-110 nm, but found no evidence of colocalization of these foci with FloA or FloT (PubMed:27362352)."}
{"protein": "MDTSLKNNDGALEADNKNYQDYKDEPDKTSDVLDVTKHNSMVDCCHKNYSTFTSEWYINERKYNDVPEGPKKADVHRCTII", "text": "FUNCTION: May subvert the host innate immune response by interacting with host IL1B and interfering with its function. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the asfivirus L83L family."}
{"protein": "MENMGDSSIGPGHPHLPPGFRFHPTDEELVVHYLKKKADSVPLPVSIIAEIDLYKFDPWELPSKASFGEHEWYFFSPRDRKYPNGVRPNRAATSGYWKATGTDKPIFTCNSHKVGVKKALVFYGGKPPKGIKTDWIMHEYRLTDGNLSTAAKPPDLTTTRKNSLRLDDWVLCRIYKKNSSQRPTMERVLLREDLMEGMLSKSSANSSSTSVLDNNDNNNNNNEEHFFDGMVVSSDKRSLCGQYRMGHEASGSSSFGSFLSSKRFHHTGDLNNDNYNVSFVSMLSEIPQSSGFHANGVMDTTSSLADHGVLRQAFQLPNMNWHS", "text": "FUNCTION: Transcription factor of the NAC family. May be associated with anther development and pollen production (Probable). Required for normal seed development and morphology (PubMed:18849494). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKREHHYLHPRPEPPSVATGSNRESYLNTGKAKLWEEEVQLDGGMDELLAVLGYKVKSSDMAEVAQKLEQLEEAMCQVQDTGLSHLAFDTVHYNPSDLSTWVESMLTELHPPPTSHLDDSSFLAPAESSTIANVDYEPQLQTSSRIFEESSSSDYDLKAITDSAIYSPRESKRLKASESDTDVFSTSAIGASNFATRPVVLVDSQENGIQLVHALMVCAEAVQQNNLNLAEALVKRIDYLAVSQAGAMRKVATFFAEALARRIYRLCPENPLDRSVLDMLQMHFYESCPYLKFAHFTANQAILEAFEGKKRVHVIDFSMNQGIQWPALIQALALRPSGPPTFRLTGIGPPAPDNSDYLQDVGWKLVKFAETLHVEFEYRGFVANSLADLDASMLELRPSEVESVVVNSVFELHQLLARPGAIEKVLSVVKQMKPEIVTVVEQEANHNGPVFVERFTESLHYYSTLFDSLECSPNSQDKMMSEMYLGKQICNVVACEGADRVERHETLTQWRTRLSSAGFDPIHLGSNAFKQASILLALFGSGEGYRVEENEGSLMLGWHTRPLIATSAWKPGNNPVVAH", "text": "FUNCTION: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that represses transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family. DELLA subfamily."}
{"protein": "MDPTIPALGTSQTPINRREETPCYKQTLSLTVLTCIISLVGLTGNAVVLWLLGFRMRRNAVSTYILNLAAVDFLFLSGHIVRSPLRLISIRHPISKIVNPVMTFPYFIGLSMLSAISTERCLSVLWPMWYRCRRPRHLSVVVCVLLWALSLLRSILEWMFCDFLFSGADSVWCETSDFITIAWLIFLCVVLCGSSLVLLVRILCGSRKMPLTRLYVTILLTVLVFLLCGLPFGIQWALFSRIHLDWKVLFCHVHLISVFLSSLNSSANPIIYFFVGSFRQRQNRQNLKLVLQRALQDTPEVDEGGGRLPEETLELSVSRLEQ", "text": "FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain. Potently activated by enkephalins (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily."}
{"protein": "MSKIIPNIVVSMPTQLFTLRRKFQACSNGKIYIGKSNTDPTIPTNQIQVYIENEDGSTVPVAQPIMINHAGFPVYNGQIAKFVTVESHSMAVYDSDGAQQFYFADILKYGPNRFKEQAAQYIAYIEKLKGTTTQTTGDSTTDVMSQKACTDTFAEKNSKEPLKAGRLNLESSNGDTIFNLGGTDGSAGSEFAYVKNSKRTQIYDTATQTTLLFPQKNGTLAVEEDTYTKTEVDAKINSVKWTTNKLENGWMKDPNTGIIIQWGSVYKTDRSRKLFPMAFPNTLAGMGLANFNYDDTLSEMYAPNIMSADKVGFKMRQSLVTDGYKDSPLTDMRWIAIGW", "text": "FUNCTION: Putative tail fiber protein. SUBCELLULAR LOCATION: Virion. SIMILARITY: To phage P22 head-binding domain."}
{"protein": "MGNCCVTPEGSGRGRKKQQQEQKQKQKEPKQQQQQQKKGKKPNPFSIEYNRSSAPSGHRLVVLREPTGRDIAARYELGGELGRGEFGVTYLCTERETGDAYACKSISKKKLRTAVDIEDVRREVDIMRHLPKHPNIVTLRDTYEDDNAVHLVMELCEGGELFDRIVARGHYTERAAALVTRTIVEVVQMCHKHGVMHRDLKPENFLFANKKETAALKAIDFGLSVFFTPGERFTEIVGSPYYMAPEVLKRNYGPEVDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDNAKDLVKGMLNPDPRRRLNAQQVLDHPWLQNIKKAPNVNLGETVKARLQQFSVMNKFKKHALRVIAEHLSVEEVAGIKDMFEKMDLNKDNMINFDELKLGLHKLGHQMADADVQILMDAADVDGNGSLDYGEFVALSVHLRKIGNDEHLHKAFAYFDRNQSGYIEIDELRESLADDLGANHEEVINAIIRDVDTDKDGKISYDEFAAMMKAGTDWRKASRQYSRERFTSLSLKLQKDGSLQLTTTQ", "text": "FUNCTION: May play a role in signal transduction pathways that involve calcium as a second messenger. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily."}
{"protein": "MTGPEHGSASTIEILPVIGLPEFRPGDDLSAAVAAAAPWLRDGDVVVVTSKVVSKCEGRLVPAPEDPEQRDRLRRKLIEDEAVRVLARKDRTLITENRLGLVQAAAGVDGSNVGRSELALLPVDPDASAATLRAGLRERLGVTVAVVITDTMGRAWRNGQTDAAVGAAGLAVLRNYAGVRDPYGNELVVTEVAVADEIAAAADLVKGKLTATPVAVVRGFGVSDDGSTARQLLRPGANDLFWLGTAEALELGRQQAQLLRRSVRRFSTDPVPGDLVEAAVAEALTAPAPHHTRPTRFVWLQTPAIRARLLDRMKDKWRSDLTSDGLPADAIERRVARGQILYDAPEVVIPMLVPDGAHSYPDAARTDAEHTMFTVAVGAAVQALLVALAVRGLGSCWIGSTIFAADLVRDELDLPVDWEPLGAIAIGYADEPSGLRDPVPAADLLILK", "text": "FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. SIMILARITY: In the N-terminal section; belongs to the CofE family. SIMILARITY: In the N-terminal section; belongs to the CofE family."}
{"protein": "MKFKDLRDFIDYLEQEGQLKRIKQPIDPNQEITEICDRTLRAGGPALLFENPIGYDIPILANLFGTPERVAMGMGRQDVKELREVGKLLAYLKEPEPPRGFRDAMDKLPVFKQVFNMPTKRLRKAPCQQVIWQGDDVDLDKIPVMSCWPDDVAPLLTWGLTITKGPNKPRQNLGIYRQQKIAKNKVIMRWLAHRGGALDLRDWMDTHPGEPFPISVAFGADPATILGAVTPVPDTLSEYAFAGLLRGSKTEVVKSLSNDLDIPASAEIVLEGYIDPNEFADEGPYGDHTGYYNEVERHHVFTITHVTMREDPIYHSTYTGRPPDEPAVLGVALNEVFVPILQKQFPEIVDFYLPPEGCSYRMAVVTMKKQYPGHAKRVMMGVWSFLRQFMYTKFVIVLDDDVNARDWNSVIQAMTTRMDPVRDTLLIESTPIDSLDFASPVVGLGSKMGLDATVKWEAETASTPSGTSQAAPDFDIETGTRNLLMQFPEIVDFYLPQEADKNSMAIVSIKKDAAGHATRVMDGVWSFLSQFTDAKFVIVCDDDVNVRDWNDVIWAITTRMDPSRDTLLIANAPIDSLDLTSPVVGLGSKMGLDATNKWQGETAREWGRPITKDPEIVAKVDAIWNELGILD", "text": "FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the UbiD family."}
{"protein": "MAAPVAPSEPQASRAPQPPVCLLVLGMAGSGKTTFVQRLTGHLHNKGCPPYVINLDPAVHEVPFPANIDIRDTVKYKEVMKQYGLGPNGGIVTSLNLFATRFDQVMKFIEKAQNTFRYVLIDTPGQIEVFTWSASGTIITEALASSFPTVVIYVMDTSRSTNPVTFMSNMLYACSILYKTKLPFIVVMNKTDIIDHSFAVEWMQDFEAFQDALNQETTYVSNLTRSMSLVLDEFYSSLRVVGVSAVVGTGFDELCTQVTSAAEEYEREYRPEYERLKKSLANAQSNQQKEQLERLRKDMGSVALDPEAGKGNASPVLDPSDLILTRGTLDEEDEEADSDTDDIDHRVTEESREEPAFQNFMEESMAHWKRNK", "text": "FUNCTION: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. May be involved in nuclear localization of XPA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the GPN-loop GTPase family."}
{"protein": "MTSRSYCVVGGGISGLTAAYRLRVATGDDVAITLFDPGDRLGGVLRTECVGGQPMDLGAEAFLLRRPEVPALLAELGLSERQRATTDARPLIYSQQRLHSLPPDTVAGIPSSATSVAGLVDDATVARIGAEAVRPLSWEPGSDPAMAELVADRFGEQAVARLVDPLLGGVYAGSAATIGLRAGAPSVAAALDCGATSLMEAVRQGLPPVAAGPVFGALDGGYQVLIDELVRRSRLQWVAATVVGLDRGTCGWTLVDDTGACWSADGVILAVPAPRLVRLLQQIAPRTVAAASRIVSASSAVVALSVPRDTTFPQNSGVLVASGERLRAKAVTLSSRKWGLQGDTQLVRLSFGKFGDQVASTASDDELLAWAVSDLAAVFDVTVDPVDVCVQRWIDAMPQYGPGHADLVAEVRAGLPPTLVVAGSHMDGIGVPACISAAGRAIEALQAEVAR", "text": "FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Coproporphyrinogen III oxidase subfamily."}
{"protein": "MKLTDSVLRSFRVAKVFRENSDKINCFDFSPNGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTGLKFSNDGKLILISTNGSFIRLIDAFKGVVMHTFGGYANSKAVTLEASFTPDSQFIMIGSEDGKIHVWNGESGIKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD", "text": "FUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes (PubMed:17998332, PubMed:18838538, PubMed:20516061). Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (PubMed:17998332, PubMed:18838538). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33913806, PubMed:33767452). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452). FUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes (By similarity). Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (By similarity). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (By similarity). Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33767452). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associates with chromatin (By similarity). Recruited at sites of high RNA polymerase II occupancy (PubMed:33767452). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associates with chromatin (PubMed:20516061). Recruited at sites of high RNA polymerase II occupancy (By similarity). SIMILARITY: Belongs to the WD repeat SWD2 family."}
{"protein": "LKFVVLICLVIMASTSAQQCGDETCGAGTCCAVFSQNHCRRLSQMYDLCSDHSDASPSGNYLFFCPCEPGLHCDRNTWTCTEGSSRSE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MIT-like AcTx family."}
{"protein": "MTLTVTDLAIARGGIPVLEGLSFTLTPGRALILRGPNGAGKTTLLRTLAGLQPPLAGRIEGAEDKIAYAGHSDGLKPTLSVTENLLFWAAVFGGRDITPALEGFALGDLADRHAGNLSAGQKRRLGLARLLVTGRPIWMLDEPTVSLDRDAVAMFADTVRAHLGQGGSALIATHIDLGLDAEVLDVGPYRARPAPLDDPDGDFL", "text": "FUNCTION: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. CcmA exporter (TC 3.A.1.107) family."}
{"protein": "MEVNTCNIQVLLQAAEYLERREREAEHGYASVLPFYSNGVSDKRKKQKSKSHSSPGNSRSVHNELEKHRRAQLRHCLEQLKQQVPLSSDSSRNTTLNLLRQAQLHIKKLQEQDERAKLLKDRLRWEQRELRTRLEKLQGGSERMRSDSLGSAVSSERSDSEREDVEIDVESMVWTLEADALGSSHAGVDHSYSTSDHAWL", "text": "FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence- specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3' (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MINSISNTVLLKSVVSKRFFSSSAKMSSQAKPRHLVSMLELSIKELESLVNRAAYHKQQIRSGLVNTTQPLSGKTVSLIFNKRSTRTRVSSEGAAAYLGGCPMFLGKDDIQLGVNESLHDTTKIISSMTSSIFARVNKHSDIQEMCKYSSVPIINALCDTFHPLQAITDILTIKESFGNTTKGLKLAWIGDVNNVINDLCIAALKSGIDVSIAVPSGLKFEELILSGAKEISAENGTTLKITNDPLEAINGANVIVTDTWISMGQEDERLQKLKQFEGFQITKEMISKGKAAENWKFMHCLPRHPEEVHDEVFYDEERSLVFEEGENRLYAAIAVLEGFVVNKGKLL", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
{"protein": "MAKLHDYYKDEVVQKLMSQFGYHSVMQVPRVEKITLNMGVGEA", "text": "FUNCTION: This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uL5 family."}
{"protein": "MTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPPKIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIQTRGEGYAKPNEGAIVEVALEGYYKDKLFDQRELRFEIGEGENLDLPYGLERAIQRMEKGEHSIVYLKPSYAFGSVGKEKFQIPPNAELKYELHLKSFEKAKESWEMNSEEKLEQSTIVKERGTVYFKEGKYKQALLQYKKIVSWLEYESSFSNEEAQKAQALRLASHLNLAMCHLKLQAFSAAIESCNKALELDSNNEKGLFRRGEAHLAVNDFELARADFQKVLQLYPNNKAAKTQLAVCQQRIRRQLAREKKLYANMFERLAEEENKAKAEASSGDHPTDTEMKEEQKSNTAGSQSQVETEA", "text": "FUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. SUBCELLULAR LOCATION: Cytoplasm, cytosol Mitochondrion Nucleus Cytoplasm, cytoskeleton Cell projection, axon Note=Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor (PubMed:21730050). Colocalized with MAPT/TAU in the distal part of the primary cortical neurons (By similarity)."}
{"protein": "MAPGSHLVLAASEDCSSTHCVSQVGAKSLGVYAVNYPASNDFASSDFPKTVIDGIRDAGSHIQSMAMSCPQTRQVLGGYSQGAAVAGYVTSAVVPPAVPVQAVPAPMAPEVANHVAAVTLFGAPSAQFLGQYGAPPIAIGPLYQPKTLQLCADGDSICGDGNSPVAHGLYAVNGMVGQGANFAASRL", "text": "FUNCTION: May have a role in cell wall processes (PubMed:26177502). Does not exhibit cutinase activity (PubMed:19225166). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Secreted, cell wall. SIMILARITY: Belongs to the cutinase family."}
{"protein": "MASGSSKAVIKNADMSEEMQADAVDCATQALEKYNIEKDIAAYIKKEFDRKHNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the dynein light chain family."}
{"protein": "MNTYFRFEWINGEENPCEYNLWRMFQIEPKPKSGANFMKPNLPNTENFSTASSSKIRQLSEQPSCSNSYKKLRHEMGSDNSNIDDPLDDYDDRKKKLAKKKAAFKAKKGYTTGQNKSDNSFEFEVEKSMDRKEPENGDEEESTEDDYRHAYSSVEKSLRKISLLPIQRPSHHTFCVFCSESYPPVEFHFCIFMTAAQKEVNQSVNEFLGKADTINKKMLESLKKFIHTSKVDTIAKHSRMENTSMKKNSDSPKKLKRPSTDPNPISKRFRHISDESTSSSSLAKNKSRSVTPDALPFAMIDSQEHRTQSGRVVKRPNLFCHKEVQIRKETVQKEGLKKKRVNKEKEVEQESTILLGISESERKRNRNMIRRLLANGFELPGDDYVLPPLPADKSTWTREQHKMDIYGPIYCALQSFKPAYTTDMTSEFLEDDGDTEFKSENSESDSDSEDEQKVENDVASSADDIEFIEIVEAERKMDQNLAQQVRSSFVTTAENTENNMLMEDDSSEQGSSKFNRNASRRSTENIEFITIDDDDDDDNDIEIIA", "text": "FUNCTION: May play a role in transgenerational epigenetic inheritance."}
{"protein": "MEVSTSYCTPAVNFKYGSFQDSDVSMREDDLFRMGSYNSQGYYADGTHLDGSIGEEDETSSGSNDQHMDFEEDDFDMESSMTEDLVDEDEEEEDEEDNDEWTNQKRTDNQNSVAYYAAMEMLRIRFPFQSIAIRISDFCCLQEKDLLNDTMIDFYLNHIVEHVLPDSNGSNVTVLPSIFWHNLSLRQHAFDSEDEKMMSDEQKMDLKFGDLHDFVADFDLQDFDYIVVPVNEWEHWSLAVICHPFTAQARTVIFDSQLTADLNNLQNMATLIESFMKYSYEKRTGNAMPFPLPCILPQRMPQQTNNFDCGIFIAEFARRFLLSPPKDLDNFDFAREYPDFSTATKRTEMQRVVLSLSTNRARWRPLVELLNGYSTAAPHRAL", "text": "FUNCTION: Protease required for deconjugation of smo-1 conjugates from target proteins which is necessary for cell cycle progression (PubMed:25475837) (Probable). Required for respiration and the maintenance of normal mitochondrial homeostasis (PubMed:25187565). In response to mitochondrial stress, required for the removal of smo-1 conjugates from the transcription factor dve-1, which promotes the translocation of dve-1 from the cytosol to the nucleus to initiate the mitochondrial unfolded protein response (PubMed:30642431). Furthermore, removes the smo-1 conjugates from the transcription factor atfs-1 to promote its stability and activate the mitochondrial unfolded protein response (PubMed:30642431). Also plays a role in promoting mitochondrial unfolded protein response-mediated innate immunity following infection with P.aeruginosa (PubMed:30642431). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm Mitochondrion matrix Note=Localizes around the metaphase plate and the pericentriolar region and in the surroundings of the central spindle (PubMed:25475837). Translocates from cytoplasm to mitochondrion at late developmental stages (PubMed:25187565). SIMILARITY: Belongs to the peptidase C48 family."}
{"protein": "MWRLLSPTALLLLVSAGTRAADLSKAMVVLEPEWNRVLVSDGVILKCEGAYPPGDNSAQWWHNGSVIPHRAPSYSIEAARSEDSGEYKCQTGLSEASDPVQLEVHTGWLLLQAPRWVFQEGDTIQLRCHSWKNKTVQKVQYFQDGRGKMFFHKNSDFYIPKATSKHSGSYFCRGLIGNKNESSEAVNITVQGPPVPSTSTFLPHWYQIAFFLVTALLFVVDTGLHVAVQRDLQSSVKEWKDGKVTWSHGP", "text": "FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation (By similarity). Fc-binding subunit that associates with FCER1G adapter to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapter with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MPRLERNVYKGLITSLSRKKPSNSLAVKESPLLTKFERWSGKRMKLFFESEDSFEHYGLRDLKLPHNMLANKLASPIRAERNTRYRIPKEFLIKLNLYKDATNNVLQLKANFNGVTGLGTTYIHNNKKCLEMKFCDISRWSSRQPLKVPPLPIVADKSALLKDYENQLIRELNECFSKLKTTSKHDHNTVKLYVSTENNLLMDVDTQGSLCINLQSITDKLPHTMLETVTNAPIHISAYSNMDFLTTLHRLLGYYRHRNR", "text": "FUNCTION: Required for respiratory activity and maintenance and expression of the mitochondrial genome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRG8 family."}
{"protein": "MASATFSVAKPSLQGFSEFSGLRNSSALPFAKRSSSDEFVSFVSFQTSAMRSNGGYRKGVTEAKIKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDSTLGIFDADVKPSGDSALSVDGKIIKIVSDRNPSNLPWGELGIDLVIEGTGVFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNAELYSHEDTIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNAAFRDAAEKELKGILDVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK", "text": "FUNCTION: Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3- diphosphoglycerate by NADPH (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MAETSLPELGGEDKATPCPSILELEELLRAGKSSCSRVDEVWPNLFIGDAATANNRFELWKLGITHVLNAAHKGLYCQGGPDFYGSSVSYLGVPAHDLPDFDISAYFSSAADFIHRALNTPGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHRWVFPNRGFLHQLCRLDQQLRGAGQS", "text": "FUNCTION: Probable protein tyrosine phosphatase. Has phosphatase activity with synthetic substrates (PubMed:15252030, PubMed:29106959). Has a phosphatase activity-independent regulatory role in MAP3K5/ASK1- mediated apoptosis, preventing MAP3K5/ASK1 inhibition by AKT1. Shows no phosphatase activity on MAPK1/ERK2, MAPK8/JNK, MAPK14/p38 and MAP3K5/ASK1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "MEASGTDEVDKLKTKFISAWNNMKYSWVLKTKTYFSRNSPVLLLGKCYHFKYEDESKMLPARSGCAIEDHVIAGNVEEFRKDFISRIWLTYREEFPQIEASALTTDCGWGCTLRTGQMLLAQGLILHFLGRAWTWPDALHIENADSDSWTSNTVKKFTASFEASLSGDRELRTPAVSLKETSGKCPDDHAVRNEAYHRKIISWFGDSPVAVFGLHRLIEFGKKSGKKAGDWYGPAVVAHILRKAVEEARHPDLQGLTIYVAQDCTVYNSDVIDKQTDSVTAGDARDKAVIILVPVRLGGERTNTDYLEFVKGVLSLEYCVGIIGGKPKQSYYFAGFQDDSLIYMDPHYCQSFVDVSIKDFPLETFHCPSPKKMSFRKMDPSCTIGFYCRNVQDFERASEEITKMLKISSKEKYPLFTFVNGHSKDFDFTSTAASEEDLFSEDERKNFKRFSTEEFVLL", "text": "FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE- conjugated forms of ATG8 proteins during macroautophagy. Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity. In contrast to other members of the family, weakly or not involved in phagophore growth during mitophagy (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C54 family."}
{"protein": "MAAVSMSVSLRQALLRQRAVATAAVSVCRVPSRLLNTSTWKLADGQTRDTQLITVDEKLDVTPLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNMVLTFSAKEDAVAFAEKHGWSYDVEGRKVPKPKSKSYGANFSWNKRTRVSTK", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=The interaction with BCAP31 mediates mitochondria localization. SIMILARITY: Belongs to the complex I NDUFS4 subunit family."}
{"protein": "MSAPPPLQIREANAHLAAVHRRAAELERRLLAAERTMRAQAERLACQDQQLRAALDELGRAKDREIFTLQEQLLSSEATVRSLQAAVEQRDQMIQELQPRADLLQDITRQRPPLAALLATLEEAEELGPLPSSHSHGAQLLPDGPGPPLGNSMREEEGQDDQQPAVFGTTV", "text": "SUBCELLULAR LOCATION: Cytoplasm Note=Colocalizes with vimentin-type intermediate filaments."}
{"protein": "GRYTVQNQWGGSSAPWNDAGLWLLGSRANQNVMDVSVTSSDGGATLTGTMTYSGEGPIGFKGTRRGDSNNYDVENQWGGSSAPWHAGGTFVIGSRSGQGVVAVDVNSSDGGKTLTGTMTYANEGPIGFKGTQSGGDSYNVENQWGGSSAPWNKAGAWALGDRDGQGVIGVDVTSSDGGKTLTGTMQYQNEGPIGFKGTSTGGSNYKVENQWGGSSAPWNPAGNWLIGDRHNQNIVAVKVTSSDNGKTLGGTCTYEREGPIGFKGTAI", "text": "FUNCTION: Lectin specific for high mannose N-glycans, recognizes the branched moiety of these glycans. Does not recognize other types of N- glycans or monosaccharides. SIMILARITY: Belongs to the bacterial lectin family."}
{"protein": "MAACRYCCSCLRLRPLSDGPFCLPGRDRALTQLLVRALWSSTGSRAVAVDLGNRKLEISSGKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLSDIPWNGPVGAVRIGIIDGECVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKHTHKLAMERLYAVFTDYEHDKVSRDEAVNKIRLDTEEQLKEKFPQADPYEIIESFNVVAKEVFRNIILNEYKRCDGRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKDKNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESNGSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRTSRKENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSALHEARDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIRHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSSNSQ", "text": "FUNCTION: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (By similarity). Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion matrix Mitochondrion intermembrane space; Peripheral membrane protein. SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase family."}
{"protein": "MSGDAFNMSVAYQPSGMAVPEWLNKGDNAWQMISATLVGMQSVPGLVILYGSIVKKKWAVNSAFMALYAFAAVWLCWVTWGYNMSFGHKLLPFWGKARPALGQSFLLAQAVLPQTTQFYKGGGGADAVVETPWVNPLYPMATMVYFQCVFAAITLILLAGSLLGRMNIKAWMLFVPLWLTFSYTVGAFSLWGGGFLFHWGVMDYSGGYVIHLSSGVAGFTAAYWVGPRSTKDRERFPPNNVLLMLTGAGILWMGWAGFNGGDPYSANIDSSLAVLNTNICAATSLLVWTCLDVIFFKKPSVIGAVQGMITGLVCITPGAGLVQGWAAIVMGILSGSIPWFTMMVVHKRSRLLQQVDDTLGVFHTHAVAGFLGGATTGLFAEPVLCSLFLPVTNSRGAFYPGRGGGLQFVRQVAGALFIICWNVVVTSLVCLAVRAVVPLRMPEEELAIGDDAVHGEEAYALWGDGEKYDSTKHGWYSDNNDTHHNNNKAAPSGVTQNV", "text": "FUNCTION: Involved in ammonium transport. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family."}
{"protein": "MTQEILEDVNPTRMELLKLQDRIELAKKGHKLLKEKRDALIMEFFEMVKRASEIREQAVKKLMEAYSKLAAAKVTVGEIGVERASMATGEEIKVDVGSRNVMGVVVPIIERVSEDGGSKVVYGFADTSGALDEAMRAFTEAIDAVLELAEIEETLRLMAEEIERTKRRVNALEHIVIPRLENTEKYIEMKLDEQERENFVRLKRVKDLIERKKLKEELERVVEEGAELPSFE", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase D subunit family."}
{"protein": "QQMCGRCGGTGQIIKNECKTCHGKKVTK", "text": "FUNCTION: In vitro, inhibits proliferation of the mice ovarian cancer cells ID8. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MATPDQDVRNRKINPEARMELKEHLREFRDRLIKAAIATIIAAIIGTVFLYQPFIEMISAPLQQINIETGRRANLNYGSVASPFDQLLKVGMYIGLVIASPVWLYQALRFLLPALHTKEKKYLFGFLTASIFAFACGVAISYFTLPGVVYALLKFTPVNESNYIDAGVYISFILKFVVTFSCAFIIPVILVGINMLGLIRGKTILKSWRWVVVLVAVIAALTAPGSDIMMMFVLMAPLLIFFFAAIGICMINDKRRDRKLAKLAQGSDEASLNTATSSEDLAKMGYFEEEKTS", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family."}
{"protein": "MESTANALVVKVSYGGVLRRFRVPVKANGQLDLEMAGLKEKIAALFNLSADAELSLTYSDEDGDVVALVDDNDLFDVTNQRLKFLKINVNAGVSTNSAAPESSGSSTPAGMPNPVSKIQKGINDVLMAVPNPMRDTISKVYMDLASKASTSSPVVGEMLDCISKLGQLSIPQESSPCSPVTKPGSSGASLSRDVPSAGGKKDISERTQTGRKPVNLNEPTGAHSKTSGHVPNSSGLGANFNECPFSGSTMNYSCPNPVNLNKHPRRVCHSKKSTNGDYWTSLGVFHKGIRCDGCGVLPITGPRFKSKVKEDYDLCTICYSVMGNEGDYTRMDKPVSVQHLHPFRGPFTQFPNPWLSHPVPRATNGGAPLRCTRPKLDSRFVLDVNVIDGTVVAPSAPFTKIWKMRNSGSLVWPQGTQIVWIGGDRFCNSLSVDLQIPKEGVPIYSELDVKVDFVAPELPGRYISYWRMATSDGAKFGQRVWVLIHVDASLKNSVVNEFHGLNLNASPSLDENFPSEFLGIMNYESAQPGSSSVNPGTVKGTDLEGEVGETQAVEKENLLVGEAHPAIPHGHSPSSSSSSFNMVDFPSMPAVEVLSGGSSSTTKDVPVPLQEDIEKNDVEITMLKELEEMGFKEIDLNKEILRDNEYNLEQSVDALCGVSEWDPILEELQEMGFCDDVTNKRLLKKNNGSIKGVVMDLLTGEKEA", "text": "FUNCTION: Autophagic substrate degraded in the vacuole by non-selective autophagy. Requires ATG8 protein expression to be recognized as an autophagic substrate (PubMed:21606687). Acts probably as a receptor for autophagosomal degradation of ubiquitinated proteins. Targets ubiquitinated protein aggregates derived from denatured or damaged non- native proteins generated under stress conditions (PubMed:23341779). Functions additively with the E3 ubiquitin-protein ligase CHIP for autophagosomal degradation of proteotoxic aggregates formed under stress conditions (PubMed:24497840). SUBCELLULAR LOCATION: Cytoplasm Vacuole Note=Forms large punctated cytoplasmic structures. Recruited to the central vacuole by non-selective autophagy."}
{"protein": "MSDVNASLVDGKKILVTGGAGFIGCAISERLAARASRYVVMDNLHPQIHANAVRPVALHEKAELVVADVTDAGAWDALLSDFQPEIIIHLAAETGTGQSLTEASRHALVNVVGTTRLTDAIVKHGIAVEHILLTSSRAVYGEGAWQKADGTIVYPGQRGRAQLEAAQWDFPGMTMLPSRADRTEPRPTSVYGATKLAQEHVLRAWSLATKTPLSILRLQNVYGPGQSLTNSYTGIVALFSRLAREKKVIPLYEDGNVTRDFVSIDDVADAIVATLAREPEALSLFDIGSGQATSILDMARIIAAHYGAPEPQVNGAFRDGDVRHAACDLSESLANLGWKPQWSLERGIGELQTWIAQELDRKN", "text": "FUNCTION: Catalyzes the interconvertion of dTDP-6-deoxy-L-talose and dTDP-L-rhamnose. The equilibrium is strongly toward dTDP-L-rhamnose. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MFQDNPLLAQLKQQIHDSKEQVEGVVKSTDKAYGFLECDKKTYFIAPPSMKKVMHGDKIKATIEKQGDKEQAEPESLIEPMLTRFIAKVRFNKDKKLQVLVDHPNINQPIGAQQAKSVKEELQEGDWVVANLKTHPLRDDRFFYATINQFICRAEDELAPWWVTLARHEQSRYPVRGAEPYEMLDQKTRENLTALHFVTIDSESTMDMDDALYIEPIAQNSTQTGWKLVVAIADPTAYIALDSQIEQEAKQRCFTNYLPGFNIPMLPRELSDELCSLIANETRPALVCYIETDLAGNITAKPNFVSAYVQSKAKLAYNKVSDYLEQADNAWQPEMPEIAQQIHWLHQFTKARIQWRKTHSLFFKEKPDYTFVLAENGKVQEIKAEYRRIANQIVEEAMIIANICAAQFLHEQAKTGIFNTHSGFDKKFLENAHNFLMANLANEQNQTELAERYSVENLATLNGYCQMRHDIEPIESDYLELRLRRYLTFAEFKSELAPHFGLGLEGYATWTSPIRKYSDMVNHRLIKAVLAKQPYEKPQNDVLARLQEARRQNRLVERDIADWLYCRYLADKVASNAEFEAEVQDVMRAGLRVQLLENGASLFIPAATLHNNKEEIQLNPDELALYIKGDRTYKIGDIVKVKLTEVKEATRSIVGEILQ", "text": "FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily."}
{"protein": "MQSNVIKIIIGASLLIGVGALYLLLSLKTPDKPLAGQVNIYEDNAEIGGDFELIDQNGELFNSDELKGKLSLIYFGFTSCPDICPTSLNKITKAVEILSENKIDIVPVFITIDPSRDTPAVLKEYLKHFHPKFIGLTGDEKQIREVADKFKVYYAKAASENDNDQDYMLDHSSFTYLMDKNGKYLKHFYLDSAPSKIMEFLKSN", "text": "SIMILARITY: Belongs to the SCO1/2 family."}
{"protein": "MFTSKKSLLLLFFLGTINLSLCEEERDADEEERRDDPDEMNVEVEKRFLPLVGKILSGLIGK", "text": "FUNCTION: Antimicrobial activity against the Gram-positive bacterium S.aureus. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily."}
{"protein": "MLLLAAASLVAFVLLLYMVSPLISPKPLALPGAHVVVTGGSSGIGKCIAIECYKQGAFITLVARNEDKLLQAKKEIEKHSINDKQVVLCISVDVSQDYSQVENVIKQAQEKLGPVDMLVNCAGMSLSGKFEDLEVSTFERLMSINYLGSVYPSRAVIATMKERRMGRVVFVSSQAGQLGLFGYTAYSSSKFALRGLAEALQMEVKPYNVYVTVAYPPDTDTPGFAKENQTKPLETRLISETTSVCKPEQVAKQIVKDVQGNFNSSIGSDGYMLSSLTCGMAPVTSIMEGLQQVVTMGLFRTIALFYLGSFDSIVRRCMMQKAKLETVDKTA", "text": "FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MFSRVFVRSMAASAKAGVKPPVQLFGLDGTYATALFTAASKTTSVEAAASSLNALKETVAKDTKLTSILENPALSAEDRNIVVDTLSKKINLDQSVQNLLKVLAENNRLSLLEHVTSQFSKLTDAYHGLVQATVTTAQPLDSKLFKRVEKALAASSLVGKGKSLKLENVVKPEIQGGLIVEVSDRTVDLSIASRINKLNQVLREAI", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase delta chain family."}
{"protein": "MSAFPVHAAFEKDFLVQLVVVDLNDSMDQVAEKVAYHCVNRRVAPREGVMRVRKHRSTELFPRDMTIAESGLNPTEVIDVVFEE", "text": "FUNCTION: Component of the toluene-4-monooxygenase multicomponent enzyme system which catalyzes the O2- and NADH-dependent hydroxylation of toluene to form p-cresol (PubMed:1885512, PubMed:15240250, PubMed:2019563, PubMed:19290655, PubMed:19705873). Also able to convert benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by successive hydroxylations (PubMed:15240250). SIMILARITY: Belongs to the TmoB/XamoB family."}
{"protein": "MALAARLWRLLPFRRGAAPGSRLPAGTSGSRGHCGPCRFRGFEVMGNPGTFKRGLLLSALSYLGFETYQVISQAAVVHATAKVEEILEQADYLYESGETEKLYQLLTQYKESEDAELLWRLARASRDVAQLSRTSEEEKKLLVYEALEYAKRALEKNESSFASHKWYAICLSDVGDYEGIKAKIANAYIIKEHFEKAIELNPKDATSIHLMGIWCYTFAEMPWYQRRIAKMLFATPPSSTYEKALGYFHRAEQVDPNFYSKNLLLLGKTYLKLHNKKLAAFWLMKAKDYPAHTEEDKQIQTEAAQLLTSFSEKN", "text": "SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. SIMILARITY: Belongs to the RMDN family."}
{"protein": "MNELSDESILKYTKKISENATIDNWNDYKWQLSNSIKDVDTLENFLGITFDEKEKTEIQKAIDVFPMSITPYYASLIDIKNLGKDPIYKQSVASSKELILENFEMEDPLSEDEDSPVIGITHRYPDRVLFYINPNCAMYCRHCTRKRKVSEKSSNPSKEEIQKAIDYIKNNNKIRDVLLSGGDPLLLSDEFLDWILSEISSIKHVELIRIGSRVPVVLPQRITDNLVNVLKKYHPIWINTHYNHPVEITKESKKALDKLSDSGIPLGNQTVLLAGVNDCPYVMRKLNQKLVSSRVRPYYLYQCDLSKGISHFRTSVSKGLEIIESLIGHTTGFAVPRYVVDAPGGGGKIPVMPNYVVSWGSDRVILRNYEGIITSYVEPSDYGGCSKNCDTCDRMCIGDFEINQTGIEKLITDVDNSISLIPENNERVARRDD", "text": "FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta- lysine. Is involved in the biosynthesis pathway of N6-acetyl-beta- lysine, a compatible solute produced by methanogenic archaea that helps cells to cope with salt stress. SIMILARITY: Belongs to the radical SAM superfamily. KamA family."}
{"protein": "MSFVSKTIIEADHELRYLNGAELEILRAYLNSSEKRIKVIKTLRDREKEIISKASRKLFQIHPDYIGPGGNASGSRQRALCLRDYGWYLRLITYSIIAGDKNPVERIGLLGVRDMYNSLGVPLIGMVDSIQCLKDAALAELKSEEEVKLAEPYFDFVIQNMAQ", "text": "FUNCTION: Allophycocyanin is a photosynthetic bile pigment-protein complex with maximum absorption at approximately 650 nanometers. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family."}
{"protein": "MGSRNIVQQQNRAEAAVPGAMKQKNIAGEKKNRRALGDIGNLVTVRGVDGKAKAIPQVSRPVTRSFCAQLLANAQTAAADNNKINAKGAIVVDGVLPDRRVAAARVPAQKKAAVVKPRPEEIIVISPDSVAEKKEKPIEKEKAAEKSAKKKAPTLTSTLTARSKAASGVKTKTKEQIVDIDAADVNNDLAVVEYVEDMYKFYKSVENESRPHDYMGSQPEINEKMRAILIDWLVQVHHKFELSPETLYLTINIVDRYLASETTIRRELQLVGIGAMLIASKYEEIWAPEVHELVCISDNTYSDKQILVMEKKILGALEWYLTVPTPYVFLVRFIKASMTDSDVENMVYFLAELGMMNYATLIYCPSMIAAASVYAARCTLNKAPFWNETLQLHTGFSEPQLMDCAKLLVAFPKMAGDQKLKSIYRKYSNLERGAVALLSPAKSVFVFLIELLMNAIEKIQCSLFFTSEIWCRF", "text": "FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily."}
{"protein": "MESTDKLTDTNAILAYLYETFPLCFIAEGETKPLKIGLFQDLAERLADDSKVSKTQLRVALRRYTSSWRYLKGVKAGAKRIDLDGNECAELEQEHIDHAILTLKESQDKAKAKRQALAPKKPAKKVAPKRAPAVKKERPAPVAAPVIKLVPAKLEDLKQKQRVNVKLGATPVPGVVTDINKEDVLVQLDSGLSIKVRAEHILL", "text": "FUNCTION: RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ProQ family."}
{"protein": "MSEIFEDKTENGKVRPWRERKIENVRYAEYLAILEFKRAHDVRGCGEVLRFRKIGEHLKLYQTWFCHKRLCPLCNWRRSMKNSSQLKQIIAEAVAREPKGRFLFLTLTVKNAHSAEELKVSLRALTKAFNKLTRYKKVTKNLLGYLRSTEITVNEQDGSYNQHLHVLLFVKSSYFKNSNNYLAQAEWAKLWQKALKVDYEPVVHVQAVKANKRKGTDSLQASAEETAKYEVKSADYMTADDERNLVVIKNLEYALAGTRQISYGGLLKQIKQDLKLEDVENGDLVHVGDEDYTKEQMEAAEEVVAKWDFNKQNYFIW", "text": "FUNCTION: Produces a single-strand nick in a specific site of the plasmid, and this nick results in single-strand replication by rolling circle mechanism. SIMILARITY: Belongs to the Gram-positive plasmids replication protein type 1 family."}
{"protein": "QDAPTGDAAAGAKVFNKCQTCHMVVAPDGTVLAGKAGKTGNPLYGLDGRAPASYPDFAYGDGIKELGAAGEVWNEADFLQYVADPTKFLKTKTGDTKAKGKMTFKLPNEKEAHDVWAFLNSLAPAPAAAEAAPAADAAAPAAADAAAPAEPAAEGAAT", "text": "FUNCTION: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MGDEDWEAEINPHMSSYVPIFEKDRYSSGENGDNFNRTPTSSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGESNKRDNTSTMGGFGVGKSFGNRGFSNSKFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGGYRDGNNSEASGPSRRGGRSSFRGCRGGFGLGSPNNDLDPDECMQRTGGLFGSRRPALSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGISFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASCFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSSLNTAGFSSSQAPNPVDDESWD", "text": "FUNCTION: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA subfamily."}
{"protein": "MFKHSTGILSRTVSARSPTLVLRTFTTKAPKIYTFDQVRNLVEHPNDKKLLVDVREPKEVKDYKMPTTINIPVNSAPGALGLPEKEFHKVFQFAKPPHDKELIFLCAKGVRAKTAEELARSYGYENTGIYPGSITEWLAKGGADVKPKK", "text": "FUNCTION: Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide. SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MCAYRLQYSLRFNIYDRFENVCFEAQLLQDEIDSLCFLFSKYFNQSLIVDSKGLTFFTEFNKCIVSIKSSFENQANNTDNIHNVKNIFSIFLRDEFIKQVPHFRTIMQYLQKYYNPTPAPDVDAIMCQSCKPANKIQCFECKCKYLASSLSTLDAGLQNGWDIFLRPMFGMPLMLYVLLRTDYKNESDIINENNLITQIFVQFFYNLICDKAYSLYTKRDMCVPFVKECKKATVGLRQEDHERVLSILSAQCNGCSTVANGDRLLLPFKNFMIEMGRNTKMKKVNKIASTVLIGFYLRHYLESLPNKAYPVAELELRNVCRFIMSKYSDENINLLIHKLKLIKIDICNVLMTEMIVPETFIRHIITKYQLDNEISLLIELNHDCFNK", "text": "FUNCTION: Plays an essential role in the production of budded virions (BVs) as well as in the envelopment of occluded derived virions (ODVs). SUBCELLULAR LOCATION: Host nucleus Host cytoplasm. SIMILARITY: Belongs to the baculoviridae p48 family."}
{"protein": "MAKSSFKLEHPLERRQAEAARIREKYPDRIPVIVEKAERSDIPDIDKKKYLVPADLTVGQFVYVVRKRIKLSAEKAIFIFVKNILPPTAAMMSAIYEEHKDEDGFLYMTYSGENTFGSF", "text": "FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation (Probable). May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton (Probable). ATG8CL-mediated selective autophagy contributes to defense against the fungal pathogen Phytophtora infestans (PubMed:26765567, PubMed:29932422). SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Lipid- anchor Vacuole membrane; Lipid-anchor Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the ATG8 family."}
{"protein": "MDNHRRTKQPKTNSIVTSSSEEVSSLEWEVVNMSQEEEDLVSRMHKLVGDRWELIAGRIPGRTAGEIERFWVMKN", "text": "FUNCTION: MYB-type transcription factor involved in epidermal cell fate specification. Acts as a negative regulator of trichome development, including endoreplication, by mediating lateral inhibition. Promotes the formation of hair developing cells in H position in root epidermis, probably by inhibiting non-hair cell formation. May have pleiotropic effects on flowering development and epidermal cell size through the regulation of endoreduplication. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSDQFTLPLRPLIEERDHQDLLPVEIAQISAQWGSFRDVNEETLRAKIEEEKNKEYTIDDEEGEGASVDLDTTERLDQLYKKRAEITQFAMQAHMEAMFALDFISLLLSKYTPRQAETSMSAFLKQVAPLGSLTAELVNPPPKSEAAVRDAKAVSRGWRLQSFNAAADKLLKSAARLETEVASETRYWSEVLAVKDKGWKVCRLPREGQALGVQYGFLEATPIFRDRGLAALRRSEDGGLILDKGLVPAKAKTVRVRVKNRGVVTGCSKPYRSAVQDSESIEGRILQARDTLYEEELFYELVREARIMGSQGVSTGQNLVQFSVSEDEEVLLDLVDPDVAYADDSETSLEHTVVADALAHSIRILLSYAHRQNRRRRTQPPPPLTQKRRHVPEYLLLRPTMAYLQHSFHVRWLESFLGDVYGVLRAAGLESKFTATPYASVDLAHIDRSVPTVEGLVKQFLLPLESTFSADLITPQTSFNVKTRTNLLVPPFGTHFEIALNMPHYPDVQPPSRIGQHDQVAMMVTHFLLLDIVSTISHGQGQPVKSETKTTPLSWEVTYPHHGELLAVASDGRQKKMKVQLSRSELSVQMFETHGTDSYSRLVGAEGGMLPLPSQSQTWTADAATPHPSLMEFVASVSKSA", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 17 family."}
{"protein": "MGKSCKVVVCGQASVGKTSILEQLLYGNHVVGSEMIETQEDIYVGSIETDRGVREQVRFYDTRGLRDGAELPRHCFSCTDGYVLVYSTDSRESFQRVELLKKEIDKSKDKKEVTIVVLGNKCDLQEQRRVDPDVAQHWAKSEKVKLWEVSVADRRSLLEPFVYLASKMTQPQSKSAFPLSRKNKGSGSLDG", "text": "FUNCTION: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small GTPase superfamily. Ras family. KappaB-Ras subfamily."}
{"protein": "MSDINVIRAPLLILSILPCVGDDIEVLRRGEGLS", "text": "FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24050899). SIMILARITY: Belongs to the MSDIN fungal toxin family."}
{"protein": "MSVVVTRYRGGGPQYMNASSTSPKPVVGEPSIRTHALHALAYCERLFYLEEVEELRVADAAVFAGRRLHVQLQEEGEHVELELASEALGLHGRVDAVKTREGTLVVYEHKRGRHAPGGDAPEAWPSDRLQAGAYALLVEERFPGAPVECRVRYHQTDTTVRFPLDAALRGAVVAAVARARLLRASRERPPVTQEERKCAKCSLAPVCLPEEERQVVGEERPRLFPEDDVRQVLHVATPGTRVGRAAEELVVTPPEGEGAPSRQPGRMVSALIAHGAVQVSAQALAYCVENDIGVHWFTSGGRYLGGLGGGAGNVHRRLRQFEALRQASVCLGLARRLVAAKLEGQLRFLLRASRGDSESRQVLASAVRDLRALLPKCEEAPSLEVLLGLEGAGAARYFGALPYLQGEDVDTRLRFEGRNRRPPRDRFNAVLGFLFGLVHREVEAAIRAVGLDVAFGFYHQPRGTAGPLGLDVMELFRVPLADMPLVASVNRRAWDADADFEVTSEHVWLSKAGRAKAIELYERRKRETWKNNVLGYSLSYARLVELEVRLLEKEWTGKPGLFATFRLR", "text": "FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The Cas4 region acts as a ssDNA exonuclease, while the Cas1 region acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated exonuclease Cas4 family. SIMILARITY: In the C-terminal section; belongs to the CRISPR-associated endonuclease Cas1 family."}
{"protein": "MNMTLNKRWCLTAILALSAVVYTSSSFAATDRLVIESGDSAQSRQQASMEKEQWNDTRSLRQKVNKRAEKEWDKTDVAFDAQDNCQKSANVNAYWEPNTLRCLDRRTGRAINP", "text": "SIMILARITY: Belongs to the UPF0482 family."}
{"protein": "MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS", "text": "FUNCTION: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
{"protein": "MYPAHLLVLLAVCVSLLGASAISNRPRNLVQFSELIQCVNKGKRATYHYMDYGCYCGKGGSGTPVDALDRCCKTHDDCYGQAEKKGCFPLLSLYNFACFPGAPQCGKGNTCQRFVCACDLKAALCFAKSPYNNNNYNIDIKKKCQTLIYMRLQTQ", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
{"protein": "MNKEHLLKVDPIPDVTIKRGPLRSFLITKPCDNLSSLRTVTSSKEKLLVGCLLIFTAIVRLHNISLPNSVVFGENEVGTFVSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYGNIGTEYTANVPYVAMRFFSATLGIVSVLVLYLTLRVSGVKIAVAAICAVCFAIENSFVTLSRFTLIEGPFVFFMACAVYFFRRSELYLPNSCKANKSLLAASIALGFAVSSKWAGLFTIAWAGIIVLWRVWFMIGDLSRPIGSSIKYMAFQFTCLLAIPAFIYFLIFSVHIKTLNVNGISSSFFPAEFRKTLKYNNVIKETVAEVAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHIDQNNKWIIELAEHPNENVTSFQNLTDGTIIKLRQLKNGCRLHSHDHKPPVSQNADWQKEVSCYGYEGFEGDINDDWIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPEKLPEWGFGQQEVTCAYFAREDLTSWYIEENENEISLPNPEKVSYKKMSFWQKFVAIHKFMFYLNNYMDTSHAYSSEPKTWPLMLRGIDFWNENGREVYFLGNAVLWWSVTAFICTFIIGVAVELLAWKLGVNILRDKHIINFHYQVFQYLLGFAAHYFPYFFVGQKLFLYDYLPAYYFGILAFGHALDLISTYISNKRNNTGYIVVAIFMVVCFYFFSEHSPLIYATGWSSNLCKRSKWLGSWDFYCNSLLLSDSHYELNAES", "text": "FUNCTION: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT3 and more rarely with PMT2 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 39 family."}
{"protein": "MFGLIGHLTSLEHAQAVAEDLGYPEYANQGLDFWCSAPPQVVDNFQVKSVTGQVIEGKYVESCFLPEMLTQRRIKAAIRKILNAMALAQKVGLDITALGGFSSIVFEEFNLKQNNQVRNVELDFQRFTTGNTHTAYVICRQVESGAKQLGIDLSQATVAVCGATGDIGSAVCRWLDSKHQVKELLLIARNRQRLENLQEELGRGKIMDLETALPQADIIVWVASMPKGVEIAGEMLKKPCLIVDGGYPKNLDTRVKADGVHILKGGIVEHSLDITWEIMKIVEMDIPSRQMFACFAEAILLEFEGWRTNFSWGRNQISVNKMEAIGEASVKHGFCPLVAL", "text": "FUNCTION: Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MKAFSPVRSVRKSSLTEHSLGIARSKAPVDEPMSLLYNMNDCYSKLKELVPSIPPNKKVSKMEILQHVIDYILDLQLTLDSHPTLVSLHHHHLSRVGGNTSRTPLTALNTDISILSLQAVELSSEFTDESKSLCP", "text": "FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Inhibits the activity of both neurogenic (neurod1/neuroD) and myogenic (myod1/myoD) bHLH factors. May play a role in the regulation of the circadian clock (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus."}
{"protein": "MASLPRRLLWSVSYIVRESFPIVSKRNCVSLLQGSWRKVLSVGVGTSLCAIPVGQRSEPTLSSESLIKRAASLVADSSSTFLSQTTYALVESLTEYTTAVYTLISLQQKYSSLLDKINSNEESAIWQVIIGARVQINQLKEQYMKYESSWQRAVSLSEMAAEAAYQSGADQASMTVRNHIQIVQTQVQGARDQAHMAEVQLAASQTEEIKRTITEDKGNPPSGGSPRNSLSEEEDIPEAYLRED", "text": "FUNCTION: Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP) (By similarity). Promotes apoptosis. SUBCELLULAR LOCATION: Mitochondrion Note=Released into the cytosol when cells undergo apoptosis."}
{"protein": "MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHARWDAHRRLQSCSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRALEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVLEIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPPKPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWVCRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPLRGPMSFYNQCLQLTQAARRPDRQQKSWSQ", "text": "FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids without apparent head group selectivity (PubMed:12522102, PubMed:18801741, PubMed:15863501, PubMed:28947740). Contributes to phospholipid remodeling of low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (PubMed:18801741). May act in an autocrine and paracrine manner (PubMed:23624557). Secreted by immature mast cells, acts on nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2 (PGD2), which in turn promotes mast cell maturation and degranulation via PTGDR (PubMed:23624557). Secreted by epididymal epithelium, acts on immature sperm cells within the duct, modulating the degree of unsaturation of the fatty acyl components of phosphatidylcholines required for acrosome assembly and sperm cell motility. Facilitates the replacement of fatty acyl chains in phosphatidylcholines in sperm membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6 PUFAs to generate oxygenated lipid mediators in the male reproductive tract (By similarity). At pericentrosomal preciliary compartment, negatively regulates ciliogenesis likely by regulating endocytotic recycling of ciliary membrane protein (PubMed:20393563). Coupled to cyclooxygenase pathway provides arachidonate to generate prostaglandin E2 (PGE2), a potent immunomodulatory lipid in inflammation and tumorigenesis (PubMed:12522102, PubMed:15863501). At colonic epithelial barrier, preferentially hydrolyzes phospholipids having arachidonate and docosahexaenoate at sn-2 position, contributing to the generation of oxygenated metabolites involved in colonic stem cell homeostasis (PubMed:28947740). Releases C16:0 and C18:0 lysophosphatidylcholine subclasses from neuron plasma membranes and promotes neurite outgrowth and neuron survival (PubMed:17868035). SUBCELLULAR LOCATION: Secreted Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Recycling endosome Note=Localized at pericentrosomal preciliary compartment. SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MEPCEDKCKRGLSLNFFEEDGPSLRLNSDSLDFLARDFKVEGMSQDNFDQKTKLYITEESLQKEVNIFLTKIYIRESEREPPQSHNSVFQLLSKIRNSVPNVSAFRNNLSILSKELSFFSFARHIHNRRLCWAEFIYCIRRGIKAIFKTTVQFLPTRLAKIFEKKASEVLKDNLLQTCNSKREGEVCDVKEPAVASSESSDCFNDMQELNNIVDLRDYSNSRFQQNRLLDRNLKGWIQGESEKALKGRRTTKRNDKENYNYPDFSNDNELLFSLATLIVENNPKKENIIPKYYLRYLQRLSRTEINKEIIEIEKLELEVVQFQMSIANLINTQVEVTNTIEELGLRCRPLPNENE", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAVIPAKKRGRPRKSVVAEVPYDSLASPVSENSGSKRPRRNASKKAVANFAQLVHAGRDDVINTTQVNNVDDTDDDDFVLNDEGDGEESDNVEIEFENELESTKNEVADLNSSGSGASVRPSGRRNTVQKLRLKKNSTKNMKSSSPGSSLGQKGRPIRLLKDLSSARDKIERIYGLNKEKLLLLAKVKEGFETSVFDFPFKNIQPDSPYFVCLDPPCKKESAYNKVIGDKNRTVYHEINKTEFENMIKLRTKRLKLLIGEVDAEVSTGDKIEFPVLANGKRRGFIYNVGGLVTDIAWLNIEENTDIGKDIQYLAVAVSQYMDEPLNEHLEMFDKEKHSSCIQIFKMNTSTLHCVKVQTIVHSFGEVWDLKWHEGCHAPHLVGCLSFVSQEGTINFLEIIDNATDVHVFKMCEKPSLTLSLADSLITTFDFLSPTTVVCGFKNGFVAEFDLTDPEVPSFYDQVHDSYILSVSTAYSDFEDTVVSTVAVDGYFYIFNPKDIATTKTTVSRFRGSNLVPVVYCPQIYSYIYSDGASSLRAVPSRAAFAVHPLVSRETTITAIGVSRLHPMVLAGSADGSLIITNAARRLLHGIKNSSATQKSLRLWKWDYSIKDDKYRIDSSYEVYPLTVNDVSKAKIDAHGINITCTKWNETSAGGKCYAFSNSAGLLTLEYLS", "text": "FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with TFC3 in DNA binding. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKTLRTLKISPNAPDINSVWLYKGTMKYFNNGEWETIGGESEPYVLPAATTSTIGGVKKATNVGNLATGAELATVVTKVNAILSALKVADIMVEDAN", "text": "FUNCTION: Forms short fibers at the surface of the viral capsid. SUBCELLULAR LOCATION: Virion Note=Present in 75 copies in the virion."}
{"protein": "MPAGPVQAVPPPPPVPTEPKQPTEEEASSKEDSAPSKPVVGIIYPPPEVRNIVDKTASFVARNGPEFEARIRQNEINNPKFNFLNPNDPYHAYYRHKVSEFKEGKAQEPSAAIPKVMQQQQQTTQQQLPQKVQAQVIQETIVPKEPPPEFEFIADPPSISAFDLDVVKLTAQFVARNGRQFLTQLMQKEQRNYQFDFLRPQHSLFNYFTKLVEQYTKILIPPKGLFSKLKKEAENPREVLDQVCYRVEWAKFQERERKKEEEEKEKERVAYAQIDWHDFVVVETVDFQPNEQGNFPPPTTPEELGARILIQERYEKFGESEEVEMEVESDEEDDKQEKAEEPPSQLDQDTQVQDMDEGSDDEEEGQKVPPPPETPMPPPLPPTPDQVIVRKDYDPKASKPLPPAPAPDEYLVSPITGEKIPASKMQEHMRIGLLDPRWLEQRDRSIREKQSDDEVYAPGLDIESSLKQLAERRTDIFGVEETAIGKKIGEEEIQKPEEKVTWDGHSGSMARTQQAAQANITLQEQIEAIHKAKGLVPEDDTKEKIGPSKPNEIPQQPPPPSSATNIPSSAPPITSVPRPPTMPPPVRTTVVSAVPVMPRPPMASVVRLPPGSVIAPMPPIIHAPRINVVPMPPSAPPIMAPRPPPMIVPTAFVPAPPVAPVPAPAPMPPVHPPPPMEDEPTSKKLKTEDSLMPEEEFLRRNKGPVSIKVQVPNMQDKTEWKLNGQVLVFTLPLTDQVSVIKVKIHEATGMPAGKQKLQYEGIFIKDSNSLAYYNMANGAVIHLALKERGGRKK", "text": "FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3A complex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230). Involved in pre-mRNA splicing as a component of pre- catalytic spliceosome 'B' complexes (PubMed:29360106, PubMed:30315277). SUBCELLULAR LOCATION: Nucleus Nucleus speckle."}
{"protein": "MTGVVYAFPWNAPRSAIASSYLTYDQQHRRDRMFAALLHARKVLFLQPECVRFDVYRTAAVLEQNQGSQRANAFLISFCKKALPRLELVAKKYECSGINSNVSAAVFDGHFDTQLMQYLASRMVNMVARFNRLPDMSRADIDLLAADIANFIRAELADIDDTGFSELKTLYTWYMRAGFISLQFNVTPPKWERVTKKYFCEDEIAPAVMRMFNEVWWRGRLRRIAAAWREHLQIAVGNVSKKRHAYASKNCVTDWREQKRRTREFLKGLDLEDEEGNRISLIEKYDGSVANPAIRRCELMARIRGFENICNELGYVGEFYTLTAPSKYHATTKAGYRNSKWNGASPSDTQSYLTGLWARIRAKLHREEIRIFGIRVAEPHHDGTPHWHMLMFMLPEDVERVRLIIRDYAWEEDHYELRSDKAKKARFHAEAIDPEKGSATGYVAKYISKNIDGYALDGETDDESGELLKETAPAVSAWAARWHIRQFQFIGGAPVTVYRELRRMADPETARALSVEFAAVHDAAHYGRWADYVNAQGGPFVRRDDLQVRTLYEPRTEFNQYGEETVCIKGVYDASIGAGSPILTRLTQWKIVPKRAVDLAVDVKGASAPSRSSVNNCTGSESDPPILDLTKPLSRRERRELTNRLRKKKPTTRRKFIHGTDKQNVAITKTIDEIHSDNRHHNQPGRSPAPDGRW", "text": "FUNCTION: Endonuclease which induces a single-strand cut at or near ori. May act by forming a covalent link to the 5'side of the nick. SIMILARITY: Belongs to the phage GPA family."}
{"protein": "MKERRAPQPVVARCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDISRPETVDSALKKWRTEILDYCPSTRVLLIGCKTDLRTDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSAFTSEKSIHSIFRTASMVCLNKPSPMPPKSPVRSLSKRLLHLPSRSELISSTFKKEKAKSCSIM", "text": "FUNCTION: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MQGTKIRLLAGSLLMLASAGYVQADALQPDPAWQQGTLANGLQWQVLATPQRPSDRIEVRLQVNTGSLTESTQQSGFSHAIPRIALTQSGGLDAAQARSLWQQGFDPKRPMPPVIVSYDSTLYSLSLPNNRNDLLKEALTYLANVSGKLTITPETVNHALSSEDMVATWPADTKEGWWRYRLKGSALLGHDPAEPLKQPVDAAKIQAFYEKWYTPDAMTLIVVGNIDARSVAEQINKTFGTLKGKRETPAPVPTLSPLRAESVSIMTDAVRQDRLSIMWDTPWQPIRESAALLRYWQADLAREALFWHIQQELTKNNAKDIGLGFDCRVLFLRAQCAINIESPNDKLNTNLSLVANELAKVRDKGLSEEEFTALVAQKNLELQKLFATYARTDTDILTGQRMRSLQNQVVDIAPEQYQKLRQNFLNSLTVDMLNQNLRQQLSQEMALILLQPQGEPEFNMKALKATWDEIMVPATAAAVEADEAHPEVTETPAAQ", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the peptidase M16 family."}
{"protein": "MDTSNHNQDHDSHVAAQRENDNNYMPPSPSMSESSMIFERNVEDPSYLYKTVSNNAANSLSRQSSRTSLFNHNNSSNRNFHNLSQRSSAVNLHLQPSRTNESIASYQTYNPDFVVQTPLDHRRTLENFVPPALDAGCSIVTDDTTGLDDVDMVYSRRPSTIGLDRALGRTRSLSSQSFDNETSPAHPRSPNDHGSRLLRFYSYADMLSDDNNNNVSNATSTSSTANPLRRPPMQGHYSFSSSLLNSPSHLPSPPSASASPPQHMNFTNPFIISRRYSNTTINNANGGTSAGSTTGAALSRSPSNQQYLLKQQRSPSGSARSRRNSNRPGSAANIMIGKPKSKFHMESSGSEGFSSEEEDNTMIERDKLNLKQKLQSQLAQPPSIANMVNDNHNNTNKHKNTINNNIKNSPAFTNSNPSSKSNSNSTITSMNPDTTK", "text": "FUNCTION: Can suppress the synthetic lethality of the hal3 sit4 double mutation when overexpressed, suggesting that it is involved in the G1-S transition. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: To yeast MFL3."}
{"protein": "QGPFGPGCEEAGCPEGSACNIITDRCTCPEVRCRVYCSHGFQRSRYGCEVCRCRTEPMKATCDISECPEGMMCSRLTNKCDCKIDINCRKTCPNGLKRDKLGCEYCECKPKRKLVPRLS", "text": "FUNCTION: This highly disulfide-bonded protein is a potent inhibitor of factor Xa. May have therapeutic utility as an anticoagulant. Also exhibits a strong metastatic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family."}
{"protein": "MSRIGKRLINIPSQVTVSIKDQVFSVKGPKGELSKQIPYGIQVVQQNDHLVVERVAESLLARKLHGLCRTLVSNLVQGVFQGFERRLEIQGVGYRAQMDGKKLVLNIGFSHPVVIEPPTEIQLQVENNTNIIIKGIDKELVGKLAAEIRAVRPPEPYKGKGIRYLGENVKRKVGKAGKK", "text": "FUNCTION: Binds 23S rRNA. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the universal ribosomal protein uL6 family."}
{"protein": "MATAEAQIGVNRNLQKQDLSNLDVSKLTPLSPEVISRQATINIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLGYANAKIYKCDNPKCPRPASFVSDASSKDDSLPCTRLNCSGNFRLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKQILILQNKIDLIKESQAKEQYEEITKFVQGTVAEGAPIIPISAQLKYNIDVLCEYIVNKIPVPPRDFNAPPRLIVIRSFDVNKPGCEVADLKGGVAGGSILSGVLKVGQEIEVRPGVVTKDSDGNITCRPIFSRIVSLFAEQNELQYAVPGGLIGVGTKIDPTLCRADRLVGQVLGAVGQLPDIYQELEISYYLLRRLLGVRTDGDKKGARVEKLQKNEILLVNIGSLSTGGRISATKGDLAKIVLTTPVCTEKGEKIALSRRVENHWRLIGWGQIFGGKTITPVLDSQVAKK", "text": "FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF- 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF- 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily."}
{"protein": "MFDIGFSELLLVFIIGLVVLGPQRLPVAVKTVAGWIRALRSLATTVQNELTQELKLQEFQDSLKKVEKASLTNLTPELKASMDELRQAAESMKRSYVANDPEKASDEAHTIHNPVVKDNEAAHEGVTPAAAQTQASSPEQKPETTPEPVVKPAADAEPKTAAPSPSSSDKP", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein Note=Localizes at the cell poles. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatB family."}
{"protein": "MPQKFEQMQSAEQKHDEDETIAQAGTQIDDTVDALDAVLDDIESVLESNAEEYVGSFVQKGGE", "text": "FUNCTION: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation (By similarity). SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family."}
{"protein": "MDTLRALEPLHRACQVCNLWPWRLAPPPDSEGILLRRSRWLELYGWTVLIAATSFTVYGLFQESSVEEKQDSESTISSIGHTVDFIQLVGMRVAHLAALLEALWQRQAQRGFFAELGEIDRLLSKALRVDVEAMRINMRRQTSRRAVWILWGYAVSQLLILGAKLLSRGDRFPIYWISYLLPLLVCGLRYFQIFNATQLVRQRLDVLLVALQQLQLHQKGPAVDTVLEEQEDLEEAAMDRLIAVRLVYQRVWALVALLNRCYGLSMLMQVGNDFLAITSNCYWMFLNFRQSAASPFDILQIVASGVWSAPHLGNVLVLSLLCDRTAQCASRLALCLHQVSVDLRNESHNALVGTLVRYCAPLIILVPLQITQFSLQLLHQRLHFSAAGFFNVDCTLLYTIVGATTTYLIILIQFHMSESTIGSDSNGQ", "text": "FUNCTION: Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its not yet determined substrates. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Gustatory receptor (GR) family. Gr2a subfamily."}
{"protein": "MATRGHVQDPNDRRLRPIYDYLDNGNNKMAIQQADKLLKKHKDLHCAKVLKAIGLQRTGKQEEAFTLAQEVAALEPTDDNSLQALTILYREMHRPELVTKLYEAAVKKVPNSEEYHSHLFMAYARVGEYKKMQQAGMALYKIVPKNPYYFWSVMSLIMQSISARDENLSKTMFLPLAERMVEKMVKEDKIEAEAEVELYYMILERLGKYQEALDVIRGKLGEKLTSEIQSRENKCMAMYKKLSKWPECNALSRRLLLKNSDDWQFYLTYFDSVFRLIEEAWTPPAEGEHSLEGEVHCSAEDAVKFIEDRITEASQSSRHVRGPHLAKLELIRRLRSQGCNDEYKLGDPEELMFQYFKKFGDKPCCFTDLKVFVDLLPAAQCTQFINQLLGVVPLSTPTEDKLALPADIRGLQQHLCVVQLTRLLGLYHSMDKSQKLDVVKELMLRYQHGLEFGRSCLKTELQFSDYYCLLAVHVLIDVWREAGEETAVWQALTLLEEGLTHSPSNAQFKLLLVRIYCVLGAFEPVVDLYSSLDAKHIQHDTIGYLLTRYAASLGQYAAASQSCNFALRFFHSNQKDTSEYIIQAYKYGAFEKIPEFIAFRNRLNNSLHFAQVRTERMLLDLLLEANISISLAESIKSMNLRPEEDDVPWEDLRDNRDLDVFFSWDPKDRNVSEEHKKLSLEEETMWLRIRSLTLRLISGLPSLTHPVEPKNSEKMSENGVSSRIDILRLLLQQLEVAVETGKRFIEKEIQYPFLGPVPTRMGRFFSSGCCQCQVQSFHLVSDMYELDTSGLEGTVDIQERIENSLASLLELLKGVFSTCKGDLLEVTDGNVKTQPAVLENLVFFVETISVILWVSSYCESVLRPYKLNIQKKKKKKKETSIIMPPIFTSFQDYVTGLQTVISNAVDHIKGLEAHLIALRLEELTLEETSISTEERKFSKTVQGKVQSSYLHSLLETGELLRKRLETTKKLKI", "text": "FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. May play a role in normal cell-cycle progression. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MDM20/NAA25 family."}
{"protein": "MASATAPAAAVPTLASPLEQLRHLAEELRLLLPRVRVGEAQETTEEFNREMFWRRLNEAAVTVSREATTLTIVFSQLPLPSPQETQKFCEQVHAAIKAFIAVYYLLPKDQGITLRKLVRGATLDIVDGMAQLMEVLSVTPTQSPENNDLISYNSVWVACQQMPQIPRDNKAAALLMLTKNVDFVKDAHEEMEQAVEECDPYSGLLNDTEENNSDNHNHEDDVLGFPSNQDLYWSEDDQELIIPCLALVRASKACLKKIRMLVAENGKKDQVAQLDDIVDISDEISPSVDDLALSIYPPMCHLTVRINSAKLVSVLKKALEITKASHVTPQPEDSWIPLLINAIDHCMNRIKELTQSELEL", "text": "FUNCTION: May negatively regulate cell cycle progression. May act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F-dependent transcription. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the CCNDBP1 family."}
{"protein": "AILELPQSPNVFHPEKPSAVG", "text": "FUNCTION: Component of the cytoplasmic filaments that run the length of the organism just underneath the cytoplasmic membrane. SUBCELLULAR LOCATION: Cytoplasm. Note=An array of 4 to 6 filaments lie in close apposition to the inner membrane and are always localized directly underneath the corresponding group of periplasmic flagella."}
{"protein": "VIGDEDTVTGFLLGGIGELNKNRKPNFLVVEKETSVTEIEETFRSFLNRDDIGIILINQFIAEMIRHVIDTHTISIPAVLEIPSKEHPYDATKDSILRRAKGMFTMEDLR", "text": "FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). SIMILARITY: Belongs to the V-ATPase F subunit family."}
{"protein": "RICPRILMECSSDSDCLAECICLEQGFCG", "text": "FUNCTION: Inhibits trypsin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine protease inhibitor) family."}
{"protein": "MTRARKGTLVQCDPSIRALILRMDADRNDIIYEELDDTHLLVDPSKVEFIKYELNRLLSENIYNPLDEEENA", "text": "FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFB5 family."}
{"protein": "MSRSYPGEQVEHAFNSKRLKNWEVPAVDKSQAISTSTGTRFGTLQPRSGRTQFIVDDNGHLKSGVPKLEKSAFNFTQTTPVFMDSAPRWPKENPTWPKNMKATMGYKGIQSNYLPTNTVTLKAVEVPGTTERNFNFM", "text": "FUNCTION: May act as a regulator of cilium basal body docking and positioning in mono- and multiciliated cells. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. SIMILARITY: Belongs to the Flattop family."}
{"protein": "MSLSSLEHKLTYHVRNWLHGSGFAWNTLHMSAFLVALCACIPAGFISQISLYSEPWREHLGYSVVEVNVLFSAVNLGGYITPPLLGLLSDAHGPVMLSWLSFVGFVPTYAYAAWVFASGEPHFYASVLCFTLIGISTNALYFSALFTASKLYPASKLCSISLPATFYGMASVLGSQLLKIPWFRNGLPYLDLSRVFRTLAVAYTLISFCMWFATSIVTMLKVKAATLTFAGMQSPTEPLLPQDIRRRLRNFFHDPAAYFMALVLLLSLGPMEMFLTNMGSLSSLLGQASVLPEFAIASTCSRFLSGLIIDLCIHNGVSTMSVQWAVLLLGVVGQWIVVLATRASDGPLLSLASALSGACYGGLFTVSPILTLAVWGDAVFGTAYGSFMITPAVGSILFGLTYAHIFDANCTPSGVLPVCIQHVFWSSTSALAIALLFSVLMYLVFWRRKV", "text": "FUNCTION: Probable transporter. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MSDLFSFNKEKKTKIINNTYSAKDIEVLEGLEPVRKRPGMYIGGTDLNAMHHLVSEVLDNSMDEAVAGFASIITIKMHQDHSITISDNGRGIPIDNHPKFPNKSALEVILTTLHSGGKFSSNVYQTAGGLHGVGVSVVNALAEHLEIKVYKQGKLYKQSYAKGEKLTELICEEAPKRLKGTSINFIPDPEIFGDKIHFNPKKVYELARSKAYLYRGVTIEWECEIEASSDVPKKALINFPNGLKDYLSSKITPDDLITTEIFSGNVESEQDGIKLEWAICWQNNDSSAFIQSYCNTVPTPLGGTHEQGLKSALLRGLKAYGEMVGNKKTANLAIEDILETASVVLSIFIAEPTFQGQTKEKLVSQGVSKPAENIIKDHFDHFLSSNKTIANNLLEHFIAIAEFRLNKKNEKTISRKNATQKLRLPGKLADCTRTSPEGTELFIVEGDSAGGSAKQARNRETQAVLPLWGKVLNVASSTLEKIVNNQAIQDLEIALACGSMKNYKKENLRYEKIIIMTDADVDGAHIASLLMTFFFLRMPKLVEDGHLYLAKPPLYRLTQSNKTYYANDEEEKAKLTDKLSKSSKAKIEVGRFKGLGEMMPMQLKETTMHPEKRSLLKVTLEDFQNVDKIVDDLMGKKPEKRFQFIYEQALVKMDKIINELDI", "text": "FUNCTION: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. SIMILARITY: Belongs to the type II topoisomerase family. ParE type 1 subfamily."}
{"protein": "MPVKQQIGIVISNKMQKTIVVKIENRYPHPMYSKTLIKTKKYLAHDELGECNIGDQVLVEECRPLSKRKRWKLIKILSKSSLIN", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS17 family."}
{"protein": "MGSLAKIVAVAAVLAALVAGGSCGPPKVPPGPNITTNYNGKWLPAKATWYGQPNGAGPDDNGGACGIKNVNLPPYNGFTACGNPPIFKDGKGCGSCYEIRCNKPECSGQPVTVFITDMNYEPIAPYHFDLSGKAFGAMAKPGLNDKLRHYGIFDLEFRRVRCKYQGGQKIVFHVEKGSNPNYLAMLVKFVADDGDIVLMELKEKSSDWKPMKLSWGAIWRMDTPKALVPPFSIRLTSESGKKVIAQDVIPVNWKPDTVYNSNVQF", "text": "FUNCTION: May cause loosening of the cell walls. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the expansin family. Expansin B subfamily."}
{"protein": "MEKQRLTAQLSSLRVPLFSVPWPGQCSNKAEVIEARMMKWADEHNLLVTDEYRNRVIRTRYGLLAARCYPNAGEELLQAIADCLVWFFLADDLFVDRVEVATDETIRNLTAMVDVLDLNVAGSPPVFGELAWLDVCQRLRRLLQAEAFERFAQGMRLWATTAALQILNHLRPTSVGMREYQTIRRHTSGMNPCTSLADAANKGSVQACEFYDADVQTLVRQTNNIVCWANDIQSLRIEIHQPGQFRNMVTIYAQQGQSLQDAVETTATRVNKEIASFCELADAVTARPISDELHGLIDGLKYWIRGYLDWVVHDTLRYADQFIESDADDRRF", "text": "FUNCTION: Terpene synthase that catalyzes the conversion of (2E,6E)- farnesyl diphosphate (FPP) into sesquiterpenes which are important for fungi-environment interactions (PubMed:31239482). Produces a mixture consisting of 8 sesquiterpenes including corvol ethers A and B, as well as traces of epizonarene, gamma-cadinene, delta-cadinene, alpha- cadinene, alpha-cadinol, and an unidentified sesquiterpene (PubMed:31239482). The major product is corvol ether B (PubMed:31239482). SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MSSEEGKLFVGGLNFNTDERALEDHFSSFGPISEVVVVKDRETQRSRGFGFITFTNPEHASNAMRAMNGESLDGRQIRVDHAGKSARGSRGGAFGSYERGRGYPRGGGDQGYGSGRYDNRPGAYGFGYGYGYGRSRDYGGRSQGGYDRYSGGNYRDNYDN", "text": "FUNCTION: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, dendrite Note=Localizes in mRNA granules in dentrites."}
{"protein": "MSKLSFRARALDAAKPLPIYRGKDMPDLNDCVSINRAVPQMPTGMEKEEESEHHLQRAISAQQVFREKKESMVIPVPEAESNVNYYNRLYKGEFKQPKQFIHIQPFNLDNEQPDYDMDSEDETLLNRLNRKMEIKPLQFEIMIDRLEKASSNQLVTLQEAKLLLNEDDYLIKAVYDYWVRKRKNCRGPSLIPQIKQEKRDGSTNNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRREFSRAITILEMIKRREKTKRELLHLTLEVVEKRYHLGDYGGEILNEVKISRSEKELYATPATLHNGNHHKVQECKTKHPHHLSLKEEASDVVRQKKKYPKKPKAEALITSQQPTPETLPVINKSDIKQYDFHSSDEDEFPQVLSPVSEPEEENDPDGPCAFRRRAGCQYYAPRLDQANHSCENSELADLDKLRYRHCLTTLTVPRRCIGFARRRIGRGGRVIMDRISTEHDPVLKQIDPEMLNSFSSSSQTIDFSSNFSRTNASSKHCENRLSLSEILSNIRSCRLQCFQPRLLNLQDSDSEECTSRKPGQTVNNKRVSAASVALLNTSKNGISVTGGITEEQFQTHQQQLVQMQRQQLAQLQQKQQSQHSSQQTHPKAQGSSTSDCMSKTLDSASAHFAASAVVSAPVPSRSEVAKEQNTGHNNINGVVQPSGTSKTLYSTNMALSSSPGISAVQLVRTVGHTTTNHLIPALCTSSPQTLPMNNSCLTNAVHLNNVSVVSPVNVHINTRTSAPSPTALKLATVAASMDRVPKVTPSSAISSIARENHEPERLGLNGIAETTVAMEVT", "text": "FUNCTION: May play a role in transcription or DNA repair. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the enhancer of polycomb family."}
{"protein": "MKSRYLLFFLPLIVAKYTSAATMQPFHSPEESVNSQFYLPPPPGNDDPAFRYDKEAYFKGYAIKGSPRWKQAAEDADISVENIARIFSPVVGAKINPKDTPETWNMLQNLLKMGGYYATASAKKYYMRTRPFVLFNHSTCRPEDENTLRKDGSYPSGHTAYSTLLALVLSQARPERAQELARRGWEFGQSRVICGAHWQSDVDAGRYVGAVEFARLQTIPAFQKSLAKVREELNDKNNLLSKEERPELNY", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the class A bacterial acid phosphatase family."}
{"protein": "MSSNLANKLRVGTKKAHTMAENVGFVKCFLKGVVEKSSYRKLVANFYYVYSAMEEEMEKHSQHPIVSKINFSQLNRKQTLEQDLSYYYGANWREQIQLSPAGEAYVQRIREISATEPELLIAHSYTRYLGDLSGGQILKNIAVTAMNLNDGQGTAFYEFADISDEKAFKAKYRQTLDELAIDEATGDRIVDEANAAFGMNMKMFQELEGNLIKAIGMMLFNTLTRKRTRGATELATAE", "text": "FUNCTION: Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae (By similarity). Upon overexpression in E.coli with PCB:ferredoxin oxidoreductase, CpeS and either CpcB or PecB permits synthesis of phycocyanin-coupled CpcB or PecB. SIMILARITY: Belongs to the heme oxygenase family."}
{"protein": "MLITQIIMKQIRDYPIVSTISIAVSTVLASEVIWKLVQCSRSKREKASRVHEVIIFNELGEICAAVHMRNSSMGSQKPQVSPCCNTHCSLRNVAKIVEQIDRAVYSIDLAIYTFTSLFLADSIKRALQRGVIIRIISDGEMVYSKGSQISMLAQLGVPVRVPITTNLMHNKFCIIDGFERVEEIRLLRKLKFMRPCYSIVISGSVNWTALGLGGNWENCIITADDKLTATFQAEFQRMWRAFAKTEGSQIQLK", "text": "FUNCTION: Cardiolipin hydrolase present at the mitochondrial outer membrane required for piRNA metabolic process. Acts by catalyzing the hydrolysis of cardiolipin (diphosphatidylglycerol) to form phosphatidate (phosphatidic acid or PA) at the mitochondrial outer membrane surface, promoting the piRNA metabolic process. Plays a key role in primary biogenesis of piRNAs and is required during oogenesis to repress transposable elements and prevent their mobilization. piRNAs mediate the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Involved in trans-silencing effect (TSE), a homology-dependent repression mechanism by which a P-transgene inserted in subtelomeric heterochromatin via its role in piRNA biogenesis. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Note=Was initially reported to localize to the meiotic nuage, also named P granule (PubMed:17543859). However, it was later shown that the EGFP tag at N-terminus used in initial experiments interfered with mitochondrial localization (PubMed:21397848, PubMed:20966047). SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini subfamily."}
{"protein": "MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDWCCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNLGTYNRKYAHYPNKLCTGPTPPC", "text": "FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids (PubMed:10681567, PubMed:11922621, PubMed:28883454). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines (PubMed:10681567, PubMed:28883454). In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver (By similarity). May act in an autocrine and paracrine manner (PubMed:11922621). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (PubMed:11922621). Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis (By similarity). May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes (PubMed:11922621). Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Through binding to heparan sulfate proteoglycan, may be localized to cytoplasmic compartments enriched in anionic phospholipids. SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MATFKDACYHYKRLNKLNHAVLKLGVNDAWRPSPPTKYKGWCLDCCQHTDLTYCRGCSIYHVCQWCNQYGRCFLDDEPHLLRMRTFKNDITKEDLANLIDMYNVLFPVNQKIVNKFINNTKQHKCRNELVPQWYNHLLMPITLQSLSIELSGDIYYIFGYYDDMKNVNQTPFSFVNLIDIYDRLLLDDVNFNRMSFLPLVLQQEYAIRYFSKSRFISEEKRQINHSHFSINILENLHNPNFKIQITRNCSTMFGKWNEACTLVKDIGTYFEILKTSHVEFYDVSPRCRMFTQHKLKAVSKVIKPNYATSNHRALATEVYNCRWCSVNTSFIVWNDFRLRNICDNVLNFIRALVKSNTRIGHCSSQEQIHSYIRDVFDVCDENKWNTSVSGIFNCLESVELDGVHYVLLNHEVNWDVANVLIQNIGKIPQILTLNDVITALHSMIYDWFDIRYMRNTPTTTFTVDKLRQLCARRKIADYDSGLSDVE", "text": "FUNCTION: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complexes, to modulate their activities. Recognizes the host NF-kappa-B regulator BTRC through the presence of a DSGXS motif in the C-terminal substrate recognition domain. SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton. SIMILARITY: Belongs to the rotavirus NSP1 family."}
{"protein": "MGQERLDNANPTLFDSKPRHRPVTGTERDESVEDPIDSWEIFDLIRDINDPEHPYTLEQLNVVQEELIKVFIDEEETFVKVNFTPTIPHCSMATLIGLAIRVKLLRSLHPKVKVSVSITPGSHSTEESINRQLADKERVAAAMENQGLMHAVNECLRVPE", "text": "FUNCTION: May play a role in chromosome segregation through establishment of sister chromatid cohesion. SIMILARITY: Belongs to the MIP18 family."}
{"protein": "MADFDSPPKLSGVQPPSEGVGGGRCSEISAELIRSLTELQELETVYERLCGEEKVVERELDALLEQQNTIESKMVTLHRMGPNLQLIEGDAKQLAGMITFTCNLAENVSSKVRQLDLAKNRLYQAIQRADDILDLKFCMDGVQTALRNEDYEQAAAHIHRYLCLDKSVIELSRQGKEGSMIDANLKLLQEAEQRLKAIVAEKFAVATKEGDLPQVERFFKIFPLLGLHEEGLRKFSEYLCKQVASKAEENLLMVLGTDMSDRRAAVIFADTLTLLFEGIARIVETHQPIVETYYGPGRLYTLIKYLQVECDRQVEKVVDKFIKQRDYHQQFRHVQNNLMRNSTTEKIEPRELDPILTEVTLMNARSELYLRFLKKRISSDFEVGDSMASEEVKQEHQKCLDKLLNNCLLSCTMQELIGLYVTMEEYFMRETVNKAVALDTYEKGQLTSSMVDDVFYIVKKCIGRALSSSSIDCLCAMINLATTELESDFRDVLCNKLRMGFPATTFQDIQRGVTSAVNIMHSSLQQGKFDTKGIESTDEAKMSFLVTLNNVEVCSENISTLKKTLESDCTKLFSQGIGGEQAQAKFDSCLSDLAAVSNKFRDLLQEGLTELNSTAIKPQVQPWINSFFSVSHNIEEEEFNDYEANDPWVQQFILNLEQQMAEFKASLSPVIYDSLTGLMTSLVTVELEKVVLKSTFNRLGGLQFDKELRSLIAYLTTVTTWTIRDKFARLSQMATILNLERVTEILDYWGPNSGPLTWRLTPAEVRQVLALRIDFRSEDIKRLRL", "text": "FUNCTION: Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1. SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the COG4 family."}
{"protein": "ISAEAPLYAEVGMPALSPTMT", "text": "FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family."}
{"protein": "MAHIYRLLLLLLSNLWFSAAAQNQSETEWPLHDNGLSKVVQWDHYSFQVNGQRIFIFSGEFHYWRIPVPELWRDILEKVKATGFTAFAFYSSWAYHAPNNRTVDFSTGARDITPIFELAKELGMYMIVRPGPYVNAEASAGGFPLWLTTGEYGSLRNDDPRYTAAWTPYFANMSQITSKYQVTDGHNTLVYQIENEYGQQWIGDPKDRNPNKTAVAYMELLEASALENGITVPLTSNDPNMNSKSWGSDWSNAGGNVDVAGLDSYPSCWTCDVSQCTSTNGEYVPYKVIDYYDYFQEVQPTLPSFMPEFQGGSYNPWAGPEGGCPQDTGAEFANLFYRWNIGQRVTAMSLYMLYGGTNWGAIAAPVTATSYDYSAPISEDRSIGAKYSETKLLALFTRTAKDLTMTEAIGNGTQYTTNTAVRAFELRNPQTNAGFYVTFHNDTTVGGNQAFKLHVNTSVGALTVPKNEGVIQLNGHQSKIIVTDFTLGKRTLLYSTAEVLTYAVFENRPTLVLWVPTGESGEFAIKGTKSGKVENGDGCSGINFKREKDYLVVNFSQAKGLSVLRLDNGVRVVLLDKAAAYRFWAPALTDDPIVQETETVLVHGPYLVRSASVSKSTLALRGDSVEKTTLEIFAPHSVRKITWNGKEVKTSQTPYGSLKATLAAPPTIKLPALTSWRSNDSLPERLPSYDDSGPAWIEANHMTTSNPSPPATLPVLYADEYGFHNGVRLWRGYFNGSASGVFLNIQGGSAFGWSAWLNGHFLDSHLGTATTSQANKTLTFSSSILNPTENVLLIVHDDTGHDQTTGALNPRGIIEARLLSNDTSSPAPGFTQWRIAGTAGGESNLDPIRGVFNEDGLFAERMGWHLPGFDDSAWTPENSTTSASSALSFTGATVRFFRTVVPLDIPAGLDVSISFVLSTPSAAPKGYRAQLFVNGYQYGRYNPHIGNQVVFPVPPGILDYQGDNTIGLAVWAQTEEGAGIQVDWKVNYVADSSLSVAGFGKGLRPGWTEERLKFA", "text": "FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
{"protein": "MTSQVAAAEVAQPYAQALLSIAQSKNLTEEFGEDARTFLGLLRADKQLHNFFSNPFIQAENKKALIKQILGEGSNPYLRNFLLILVDKRRIAFLESIFQQYLALLRQLNQTVLAEVISAVPLTEAQQQAIIQKVIAISNARQVELETKVDSELIGGVIIKVGSQVIDASIRGQLRRLSLRLTNS", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase delta chain family."}
{"protein": "MQRIPLWLVRSTHCLILLFQDDVQVRKSCLEPFLFLSPERKREIHQLLVAFNQSLVTPTQDEEKILSDIQRACLQIAEDLKHLNPFTGLLLDLNLYTLWTLLRNYKTKQRSQPVNSTVVSRYAHHVVKYIMQRLVYTTDRLFLTAPTSGIVLPVPLANAIFNLLSHCRKKCTGLWRNYGTEKSVLMGLGKEITLCYQALNESGIVSTTLAAFIKLSFPTISIPNLFKPMFQSCKGNQDNFPDICTQGSVIRRPHQGVFGDTFPIPDPLMREISENSFKKFSTANISTLLQNPKEILEMDPFDPRIGGFPLNKEETATPLKDSSFSNPTFINTGAANTLLPAASVTPALESLFSPTHFPCMSDESIASTSHVPLDNNISLPTLVKTNFPLKRKRQSRNIDPNTPRRPRGRPKGSKTKKRPTCSPALFQSSDIPTDSLHVKCPEMLPTVPQNEFCDSSNIQPCTSSSVLENDNLVPINEAETDDNILATILQDLYDLPAPPVLCSHENQTLEIDNNVDIEDLGLSFPMSLQDFLNDE", "text": "FUNCTION: Transcription activation. Regulates the delayed-early 110 kDa promoter. SIMILARITY: Belongs to the herpesviridae TAF50 family."}
{"protein": "MCRRPDCGFSFSPGPVVLLWCCLLLPIVSSVAVSVAPTAAEKVPAECPELTRRCLLGEVFQGDKYESWLRPLVNVTRRDGPLSQLIRYRPVTPEAANSVLLDDAFLDTLALLYNNPDQLRALLTLLSSDTAPRWMTVMRGYSECGDGSPAVYTCVDDLCRGYDLTRLSYGRSIFTEHVLGFELVPPSLFNVVVAIRNEATRTNRAVRLPVSTAAAPEGITLFYGLYNAVKEFCLRHQLDPPLLRHLDKYYAGLPPELKQTRVNLPAHSRYGPQAVDAR", "text": "FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH (By similarity). In human cytomegalovirus, forms two distincts complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA. The gH-gL- UL128-UL130-UL131A pentamer is essential for viral entry in epithelial, endothelial and myeloid cells via interaction with host NRP2 (By similarity). SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein; Extracellular side Host cell membrane; Peripheral membrane protein; Extracellular side Host Golgi apparatus, host trans- Golgi network Note=gL associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the host trans-Golgi where secondary envelopment occurs. SIMILARITY: Belongs to the herpesviridae glycoprotein L family."}
{"protein": "MAEDTDGGIRFNSLCFINDHVGFQGSIKTSPSDFIVIEIDEQGQLVSKATDGSLYEISKIQSEPSNSVKKPKLNIQNVSLEHKNSEGAADLPGCSDGDRSHQSDSEKENSVNSVTSKCEEESVDLLRSLLDEKTHTSLGQFACDIKRMWNSQTELTEPSPELSLGKILDKNRRAVLHSAVRQAFPFLITVGNQGEVVVKPNRECKELCRLVSEEEALGFFKYLDAKKENSKFTFKPDPNKDHRKAVHHFLNKKFGNLVETKSFPGQHHSAGNPDSAITVRFREKARGKRSHPEGCERGKAVYTAFTLQKENLETFEAIGLLAVKLGVIPSDFSYAGLKDKRAITYQSMVVKKVTPERLKSIKEEIEKKRMNVFNIRSVGDCLRLGQLKGNHFEIIIRHLRNQLNDSANLTERILEAIENVKNKGFVNYYGPQRFGKGQKIQTDQIGLALLKNEMVKAIKLFLTPEDVDDPVNKAKQYFLRTEDAKGTLSLMPEFRVRERALLESLHRFGVTEEGCVRAWFSFPHSMRIFYIHAYSSRIWNEAASYRLAAYGPKVVEGDLICSDEDADKHFPSSKVHLVTKEEESAHTYALHQVVLPVLGYNVQYPENQVGRWYQEALSRDGLQACRFRVPALKLNVPGCYRHIVKHPRNVSHRLVHPDPATEEARVEGPHSDDTASSLSLSFDLDASCYATVCLREMMKGDI", "text": "FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family."}
{"protein": "MAHYHNDYQKNDEVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLNSRREYLHGDNSDIIPTDTIKNTVQVLAKFKGIKSIETFAMNICEHFLSSFNHVIRVQVYVEEVPWKRFEKNGVKHVHAFIHTPTGTHFCEVEQLRSGPPVIHSGIKDLKVLKTTQSGFEGFLKDQFTTLPEVKDRCFATQVYCKWRYHQGRDVDFEATWEAVRGIVLKKFAGPYDKGEYSPSVQKTLYDIQVLSLSQLPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGRITGTVKRKLTSRL", "text": "FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the uricase family."}
{"protein": "MHPLQRVFRAQRLSAPLTSMCWVLLRTFRAHNSTSCPDPEGKSSEGVQKDFSSRLATGPTFQHFLRSASVPQEKPSSPEVEDPPPYLSGDELLGRQRKVYLETYGCQMNVNDTEIAWSILQKSGYLRTSNLQEADVILLVTCSIREKAEQTIWNRLHQLKVLKAKRPRSRVPLRIGILGCMAERLKGEILNREKMVDLLAGPDAYRDLPRLLAVVESGQQAANVLLSLDETYADIMPVQTSPSATSAFVSIMRGCDNMCSYCIVPFTRGRERSRPVASILDEVRKLSEQGLKEVTLLGQNVNSFRDNSEVQFSSTGSANLSRGFTTNYKPKQGGLRFSHLLDQVSRIDPEMRIRFTSPHPKDFPDEVLQLIRERHNICKQIHLPAQSGSSRVLEAMRRGYSREAYVALVHHIREAIPGVGLSSDFITGFCGETEDDHLQTVSLLREVQYNTGFLFAYSMRQKTRAYHRLKDDVPEEVKLRRLEELITVFREEASKVNATSVGCTQLVLVEGFSKRSTTDLCGRNDANLKVIFPDAEVEDITDPGLKVRAQPGDYVLVKIISASSQTLKGHILCRTTMKDSSMNCLT", "text": "FUNCTION: Methylthiotransferase that catalyzes the conversion of N6- (dimethylallyl)adenosine (i(6)A) to 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 (adjacent to the 3'-end of the anticodon) of four mitochondrial DNA-encoded tRNAs (Ser(UCN), Phe, Tyr and Trp) (By similarity). Essential for efficient and highly accurate protein translation by the ribosome (By similarity). Specifically inhibits CDK5 activation by CDK5R1 (By similarity). Essential for efficient mitochondrial protein synthesis and respiratory chain (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily."}
{"protein": "MSETSEQMEETVQSGNEPISKSTWMGFIKNLATFTGDLSTLSAPSFILSGTSLLEYMSYWFEFPELFVTIVDFPTPKERMLAVLKWYITGLSREYASRNKNYGTEKKPLNPILGELFYGSWDSSKGKVELTAEQVSHHGPESAAHVVCKEAGITVDTHNKYRSGFSGRTVYVNQLGQLRVHLEKYNETYYITLPNISLEGLWFMAPYIELYGSTYIVSNTNYITKIDYSGRGYFRGTKNSFKATIFEKNEDPDYIVEGVWTGESKLTIPSLKSTIFFLSIPSLEATPITVKPESEMGDWESRNVWKEVSAALASGNYDIVSSKKSTIEQSQRDMRKKEEAEGAVWARRYFKWEEHDSDARNALAQAVLEVIEPGFWIYIGDTHPSLPAGEQPVKRME", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the OSBP family."}
{"protein": "MASPGNHAIVAPGWTRSEDGSLTRPLDLVENWLLARIQRANTPPGREAEGLTYKLKLRLPQDIDDPIPYLRRAWLVFRYVQPLIGAIYPPYSERDETGRYLVTVPLMDPEEWLRLSFHVNQGTQAVFRDVDDAGKIFQPRPTAMAYWFPPSSTLIIRSTHLRFDAVGIYKATNTFMLGLESVFRLGLDANLDCYTTDVKQPSLPPGIDYILGFPPQETPVPHRVERAVDELMRHWHHGLYSLSLPVREGSEDAAPANTQHLVTLFDEPTLEAIVAGCKKLGVSVSAAVHASIVRVWASFPQQQHTGARNMLIPLVANLRPLLDPKWVVPDYALGLCIFVVPFCLTGGFEDLTQRLGAVYSRDLSALPSDPAGDPVSFLELLPLYESREAAFLGSLPVAGCPPFRVPNLSSLGVLERYLARAYGKKGAQAPVCEIEDVALVNATTDPTIEFQLFTFRGTMRLYLYYNDAYYTEDFLAPVMEMVRDSLLQELGLGGS", "text": "FUNCTION: Transcriptional regulator that may regulate the expression of the loline biosynthesis cluster 1, one of the 2 clusters involved in the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 (PubMed:15654104). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAAESSLRVATPTLCNLNGSQRRPTTTTLSPLRFMGFRPRPSSHSLTSSSLSHFFGSTRIHSNSSSSYSSISRQHAPRRNFSVFAMSADDAKRSVPLKDYRNIGIMAHIDAGKTTTTERILYYTGRNYKIGEVHEGTATMDWMEQEQERGITITSAATTTFWNKHRINIIDTPGHVDFTLEVERALRVLDGAICLFDSVAGVEPQSETVWRQADKYGVPRICFVNKMDRLGANFYRTRDMIVTNLGAKPLVIQLPIGSEDNFKGVIDLVRNKAIVWSGEELGAKFDIVDIPEDLQEQAQDYRAQMIENIVEFDDQAMENYLEGIEPDEETIKKLIRKGTISASFVPVMCGSAFKNKGVQPLLDAVVDYLPSPLDLPAMKGSDPENPEATIERLASDDEPFAGLAFKIMSDPFVGSLTFVRVYAGKLGAGSYVLNANKGKKERIGRLLEMHANSRDDVKVALAGDIIALAGLKDTITGETLCDPDNPIVLERMDFPDPVIKVAIEPKTKADVDKMATGLIKLAQEDPSFHFSRDEEINQTVIEGMGELHLEIIVDRLKREFKVEANVGAPQVNYRESISKISEVKYVHKKQSGGQGQFADITVRFEPMDPGSGYEFKSEIKGGAVPREYIPGVMKGLEECMSNGVLAGFPVVDVRAVLTDGSYHDVDSSVLAFQLAARGAFREGIRKAGPRMLEPIMKVEVVTPEEHLGDVIGDLNSRRGQINSFGDKPGGLKVVDSLVPLAEMFQYVSTLRGMTKGRASYTMQLAMFDVVPQHIQNQLATKEQEVAA", "text": "FUNCTION: Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPNNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYALNVPLRDGIDDQSYKHLFQPVINQVVDYYQPTCIVLQCGADSLGRDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVDEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPSDLLSYDRTDEPDPEERGSEENYSRPEAANEFYDGDHDNDKESDVEI", "text": "FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Also functions as deacetylase for non-histone targets. In addition to protein deacetylase activity, also acts as protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2- hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation and de-2-hydroxyisobutyrylation, respectively. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily."}
{"protein": "MSRVQLALNVDDLEAAITFYSRLFNAEPAKRKPGYANFAIADPPLKLVLLENPGTGGTLNHLGVEVGSSNTVHAEIARLTEAGLVTEKEIGTTCCFATQDKVWVTGPGGERWEVYTVLADSETFGSGPRHNDTSDGEASMCCDGQVAVGASG", "text": "SIMILARITY: To B.subtilis YqcK."}
{"protein": "MARGPGDTDMDEASADAAIPSSTPNPTVAFRCTHALSGHTKAVAAVKFSPDGSLLASGSADRTVALWDAATGARVNTLAGHSCGVSDVAWNPNGRYLATAADDHSLKLWDAETGACLRTLTGHTNYVFCCNFDGAAGHLLASGSFDETLRLWDVRSGRCLREVPAHSDPVTSAAFSYDGSMVVTSSLDGLIRLWDTQTGHCLKTLFDRDSPPVSFAAFTPNAKYVLCNTLDGRAKLWDYAAGRTRRTYAGGHVNTQFCISSGFLGGSSSASFDLGCSMVVTGSEDGSLAAYDISTGHVVGRGAAAAAAAEGGGDEGSAAAAAAGGVAGGHTAAVLSVNVHPSAPLVATGGHHPDNSVRVWAASRTEPAAA", "text": "FUNCTION: Part of a complex involved in 'Lys-4' histone H3 methylation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat WDR5/wds family."}
{"protein": "MNNVIPLQNSPERVSLLPIAPGVDFATALSLRRMATSTGATPAYLLAPEVSALLFYMPDQRHHMLFATLWNTGMRIGEARIVTPESFDLDGVRPFVRVLSEKVRARRGRPPKDEVRLVPLTDISYVRQMESWMITTRPRRREPLWAVTDETMRNWLKQAVRRAEADGVHFSISVTPHTFRHSYIMHMLYHRQPRKVIQALAGHRDPRSMEVYTRVFALDMAATLAVPFTGDGRDAAEILRTLPPLK", "text": "SIMILARITY: Belongs to the 'phage' integrase family."}
{"protein": "MFIPVTNICRNRCGYCGFRREPGQPGARLMKPAEVISILKNGVRAGCTEVLFTFGEYAEEMPGYNLMLDEIGYSSTLDYLLFLCETAIETGILPHTNAGVMTRSELEALKPLNASMGLMLESTASLEAHKDCPGKIPERRLETIREAGKLQIPYTSGLLIGIGESREDRIESLEAITSLHREYGHIQEVIIQNFAPKPGTPMESFPEPTVEEMMDAVVLARHVLPSDVSVQVAPNLIDPKALIGKGVTDLGGISPLTIDWINPEAEWPDVRDLQKKLGDIPLRERLPVYPQYVKRGWYSERIGSLIERLSDNEGYRKQPAIENAEDLEK", "text": "FUNCTION: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8- hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D- ribitylimino)-5,6-dihydrouracil. SIMILARITY: Belongs to the radical SAM superfamily. CofG family."}
{"protein": "MLNADLKQQLKQLLELMEGNVEFVASLGSDDKSKELKELLTEISDMSPRLSLSEKSLKRTPSFSVNRPGEETGVTFAGIPLGHEFNSLVLAILQVSGRAPKEKQSIIDQIKNLEGSFHFETFISLTCQKCPDVVQALNLMSVINPNITHSMIDGAVFREESENIMAVPAVFLNGEEFGNGRMTIQDILSKLGSTADASEFENKEPYDVLIVGGGPASGSAAIYTARKGLRTGIVADRIGGQVNDTAGIENFITVKETTGSEFSSNLAAHIDQYDIDAMTGIRATDIEKTDEAIKVTLENGAVLESKTVIIATGAGWRKLNIPGEEQLINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKADNVLQDRLRSLSNVDIKTNAKTTEVVGENHVTGIRYEDMSTGEEHLLNLDGIFVQIGLLPNTSWLKDAVELNERGEIVIDRNNNTNVPGIFAAGDVTDQKNKQIIISMGAGANAALNAFDYIIRN", "text": "FUNCTION: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein (By similarity). SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MFSVPGVSGILNRGGGHKIKGTVVLMRKNVLDFNSVADLTKGNVGGLIGTGLNVVGSTLDNLTAFLGRSVALQLISATKPLANGKGKVGKDTFLEGIIVSLPTLGAGESAFNIQFEWDESMGIPGAFYIKNYMQVEFYLKSLTLEDVPNQGTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAALVGYREEELKNLRGDGKGERKEHDRIYDYDVYNDLGNPDHGENFARPILGGSSTHPYPRRGRTGRYPTRKDQNSEKPGEVYVPRDENFGHLKSSDFLAYGIKSLSQYVLPAFESVFDLNFTPNEFDSFQDVRDLHEGGIKLPTEVISTIMPLPVVKELFRTDGEQVLKFPPPHVIQVSKSAWMTDEEFAREMVAGVNPCVIRGLQEFPPKSNLDPTIYGEQTSKITADALDLDGYTVDEALASRRLFMLDYHDVFMPYIRRINQTYAKAYATRTILFLRENGTLKPVAIELSLPHPAGDLSGAVSQVILPAKEGVESTIWLLAKAYVVVNDSCYHQLMSHWLNTHAVIEPFIIATNRHLSALHPIYKLLTPHYRDTMNINALARQSLINADGIIEKSFLPSKHSVEMSSAVYKNWVFTDQALPADLIKRGVAIKDPSAPHGLRLLIEDYPYAVDGLEIWAAIKTWVQEYVSLYYARDDDVKPDSELQQWWKEAVEKGHGDLKDKPWWPKLQTIEELVEICTIIIWTASALHAAVNFGQYPYGGFILNRPTSSRRLLPEKGTPEYEEMVKSHQKAYLRTITSKFQTLVDLSVIEILSRHASDEVYLGQRDNPHWTSDSKALQAFQKFGNKLKEIEEKLARKNNDQSLSNRLGPVQLPYTLLHPNSEGLTCRGIPNSISI", "text": "FUNCTION: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lipoxygenase family."}
{"protein": "MDVMKGTTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACATLLSNILHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLALNALKSAMERDTFSGNGISLAVITKDGVKIFEDEEIEKILDSMKAKPKKKTTKRSRRKSK", "text": "FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin- like activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MSGTRASNDRSSHPGAGGHKRPRYDVGNKVTVILGAQWGDEGKGKVVDLLATDSDIICRCQGGNNAGHTVVVEGKEYDFHLFPSGIINPKAISFIGNGVVIHLPGLFEEADKNEKKGLKDWEKRLIISDRAHIVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKASRTGLRICDLLSDFDEFSARFKNLAHQHQSMFSNLEVDVEGQLKKLKMYAEKIRPMVRDGVYFMYEALHGSPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNVGDVYGVVKAYTTRVGIGAFPTEQINEIGNILQTRGHEWGVTTGRKRRCGWLDLVILRYAHMINGFTALALTKLDILDVLDEMKIGVAYRLNGKRIPYFPANQEILQKVEVEYEVMPGWKSDTTGARKWEDLPTRAQNYIRFVENHIGVPVKWVGVGKSRESMIELF", "text": "FUNCTION: Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylosuccinate synthetase family."}
{"protein": "MISRRRFLQATAATIATSSGFGYMHYCEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVLFDMSLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFGERHIYTTRGVGSLYGLRLNCRPEVTMLELV", "text": "FUNCTION: Shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP). SIMILARITY: Belongs to the metallophosphoesterase superfamily."}
{"protein": "MASEARSGLGASPLQSARSLPGNAPCLKHFPLDLRTSMDGKCKEIAEELFSRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRGLWERDVVLEREFQRVIISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQSPDTPVSADAPVHPPALEQHPYEHCEPSAMPGDLGLGLRMVRGVVHVYTRRDPDEHCPEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEVGIVMSPGP", "text": "FUNCTION: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family."}
{"protein": "MNATKFVVLLVIGILCAIVTARQVEEVSKETKLGTSLPKSTNKGIGAQLSAAGLTYSGSSVSSSASAFNNPKGPGASASESGYTSTIGQVIAKGRKARVSSASASAATGEAAAAVTRKAAAARAKGKVASASRVKGSSEKKKKDHKGKKD", "text": "SIMILARITY: Belongs to the UPF0540 family."}
{"protein": "MGDRSGVGGEEGEKSVLGASAHSQAGRRQQHTPAARRGAQRAPAATAAAASRPVFAMRWCCGGSYSENGGGGGGSRGAPPTPLLTVAATSSSTAHDTFGPMQVKMLKTAVIVTEGTGESVLLDSLRASGWICTVSFPTQATSDVESICPLAVFIDLRVPHPSQIAKDVSSVSTEEVLIVSIAEKHISEKRRRALAQSNIIHHVTWNTRDVVLFDYVGRLANRIRALPALFAVLDETDQAVEICDEQRVVQYVNRAYENVTGCIRSEVIGQPESEMRRKSLPRARGEEERRRSCDWKFIRVPFANNSQFVYMKRSNTTGDTAAIFRDVSLKSLKSQTGGIEAPISEVLTMLRDVSARVDGEPAQTIKDAMKVLSSHELYAPSINRFRDADRIATQYYDGLIRLHHPARQRKRSVVDAHREKRGSHGERRRVSADVKNALENDNCWKFDILHLEKVSDHHALSQVGMKVFERWKVCDVLGCSDDLLHRWILSIEAHYHAGNTYHNATHAADVLQATSFFLDSPSVAVHVNESHAVAALLAAAVHDLDHPGRGNAYLINTRQSLAILYNDNSILENHHIALAFQLTLQHNANVNIFSSLSREEFIQMRHAMVEMVLATDISRHFEYLAKFNKMHVTDVPEEQRDTNSLTICDMLVKCADISNPAREWGLCQRWAHRIVEEYFEQTREEKEKGLPVTMEVFDRNTCNVPITQCGFIDMFAREAFATFTEFAKLGELSDQLESNYEKWKVMTSQWTPTHNTNLVL", "text": "SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family."}
{"protein": "MAAGFLFHMGSLPAIATVGHKSKVLVIGGTGYLGKRLVTASLAAGHETYVLQRPEIGVDIEKIQLLLSFKKAGASLVSGSFNDYRSLVDAVKLVDVVICAVSGVHIRSHQILLQLKLVDAIKEAGNVKRFLPSEFGTDPATMENAMEPGRVTFDDKMVVRKAIEEAGIPFTYISANCFAGYFLGGLCQPGFILPSREQVTLLGDGNQKAVYVDEDDIARYTIKMIDDPRTLNKTVYIKPPKNVLSQREVVGIWEKYIGKELKKTTLSVEEFLAMMKEQDYAEQVGLTHYYHVCYEGCLTNFEIGDEAGEATKLYPEVGYTTVVEYMKRYV", "text": "FUNCTION: Reductase involved in lignan biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis. SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily."}
{"protein": "MEEAKVEAKDGTISVASAFSGHQQAVHDSDHKFLTQAVEEAYKGVDCGDGGPFGAVIVHNNEVVASCHNMVLKYTDPTAHAEVTAIREACKKLNKIELSECEIYASCEPCPMCFGAIHLSRLKRLVYGAKAEAAIAIGFDDFIADALRGTGVYQKSSLEIKKADGNGAAIAEQVFQNTKEKFRLY", "text": "FUNCTION: Catalyzes the hydrolytic deamination of guanosine, producing xanthosine and ammonia. Deaminates exclusively guanosine and 2'- deoxyguanosine but no other aminated purines, pyrimidines, or pterines. Deamination of guanosine by GSDA is the only source of xanthosine production in Arabidopsis. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes predominantly to the nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MASAMELSLLNPAMHHYGIAAKTASHLPVVPARRASSGAVRFRVRAAAAAPPAPAAKPGSPKKRGKTEVNESLLTPRFYTTDFDEMEQLFNAEINKQLNQDEFDALLQEFKTDYNQTHFIRNPEFKEAADKMQGPLRQIFVEFLERSCTAEFSGFLLYKELGRRLKKTNPVVAEIFSLMSRDEARHAGFLNKGLSDFNLALDLGFLTKARKYTFFKPKFIFYATYLSEKIGYWRYITIFRHLKANPEYQVYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFFCLSVYITMYLNDCQRSAFYEGIGLNTKEFDMHVIYETNRTTARIFPAVPDVENPEFKRKLDRMVDINLKIISIGESNDLPLVKNLKRVPLIAQLVSEIIAAYLMPPIESGSVDFAEFEPKLVY", "text": "FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral membrane protein. SIMILARITY: Belongs to the AcsF family."}
{"protein": "MERFLENAMYASRWLLAPVYFGLSLALVALALKFFQEIIHVLPNIFSMAESDLILVLLSLVDMTLVGGLLVMVMFSGYENFVSQLDISENKEKLNWLGKMDATSLKNKVAASIVAISSIHLLRVFMDAKNVPDNKLMWYVIIHLTFVLSAFVMGYLDRLTRHNH", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0114 family. SIMILARITY: Belongs to the UPF0114 family."}
{"protein": "MIPLKMLLLVTLLLGASLQVTHAARGTNVGRECCLEYFKGAIPISRLTRWYKTSGECPKDAIVFVTVQGKSICSDPKDKRVKKAVRYLQRTWKGGPQES", "text": "FUNCTION: Chemokine, which displays chemotactic activity for T lymphocytes, preferentially Th2 cells, but not monocytes or granulocytes. Therefore plays an important role in a wide range of inflammatory and immunological processes. Acts by binding to CCR4 at T- cell surface. Mediates GM-CSF/CSF2-driven pain and inflammation (By similarity). In the brain, required to maintain the typical, highly branched morphology of hippocampal microglia under homeostatic conditions. May be important for the appropriate adaptation of microglial morphology and synaptic plasticity to acute lipopolysaccharide (LPS)-induced neuroinflammation. Plays a role in wound healing, mainly by inducing fibroblast migration into the wound (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MAARLALRGGPGAAGQRPWLLLAPLLLVPLLARPAEALVEGLYCGTRDCYEVLGVSRSASKAEIARAYRQLARRYHPDRYRPEPGDGPGGAPPSAEAFLLVATAYETLKDEETRKDYDYMLDHPEEYYSHYYHYYSRRLAPKVDVRVVILVSVCAISMFQYFSWWNSYNKAISYLATVPKYRIQATEIAKEQGLLKKAKEKGKNKKSKEEIRDEEENIIKNIIKSKIDIKGGYQKPQVRDLLLFQVILAPVHLCSYIAWYCRWIYNFNIKGKEYGEEERLYIIRKSMKMSQSQFDSLEDHQKEMFLKRELWIKENYEVYKQEQEEELKKKLANDPRWKRYRRWMKNEGPGRLTFVDD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DNAJC25 family."}
{"protein": "MSAVPEQILGASSANDADPQETHEWLDALQGVLAAEGPARAAFLIDKQIEYARVNGVTQPFHAETQYINTIPVEQQARIPGDQDIEHRIRSYTRWNAMAMVLRANKHTNVGGHISSFASAATLYDVGYNHFWRAPSEAGGGDLVFVQGHSAPGVYSRAFLLGRLTQDQLDNFRQEVDGKGISSYPHPWLMPDFWQFPTVSMGLGPIMAIYQARFMKYLDSRGLAKAGDRKVWAFLGDGETDEPESLGAIGMAGREKLDNLVFVINCNLQRLDGPVRGNGKIIQELESEFRGAGWNVIKVVWGSKWDSLLARDTKGLLMKRMMECVDGEYQTMKAKDGAYVREHFFNTPELKAMVADWSDDDIWRLNRGGHDPHKIYAAYKAASEHKGQPTLILAKTIKGYGMGDAGQAMNVAHQQKKMPVDAIRKFRDQFNLPVADDQLEEVPYITFPEGSKELEYMRQARQNLGGYLPARRQKAEALPVPQLSAFDALLKATGEGREVSTTMAFVRILNTLLKDKQIGKHVVPIVPDESRTFGMEGLFRQVGIWNQEGQKYVPEDHDQLMFYKESQTGQVLQEGINEAGAMCDWIAAATSYSTHGVQMIPFYIYYSMFGIQRIGDLCWAAADMRSRGFLLGGTAGRTTLNGEGLQHEDGHSHVFHAAIPNCISYDPTFQYELAVVMQDGLRRMYAEQEDVYYYLTVMNENYEHPEMPAGVEQDIVKGMYQFRKGVENSNAPRVQLLGSGTIFREVIAAADLLKKDWGVESDLWGCPSFTELAREGHDVERFNLLHPTETPRESHVAKSLKSARGPVIASTDYVRAFAEQIRPFVPRRYVVLGTDGFGRSDTREKLRHFFEVDRYWVTLAALKALADEGAIGRDKVAEAIKKYNLDPNKPNPMSV", "text": "FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)."}
{"protein": "MAEQNDSNGNYDDGEEITEPEQLRKLFIGGLDYRTTDDGLKAHFEKWGNIVDVVVMKDPKTKRSRGFGFITYSQSYMIDNAQNARPHKIDGRTVEPKRAVPRQEIDSPNAGATVKKLFVGGLRDDHDEECLREYFKDFGQIVSVNIVSDKDTGKKRGFAFIEFDDYDPVDKIILQKTHSIKNKTLDVKKAIAKQDMDRQGGGGGRGGPRAGGRGGQGDRGQGGGGWGGQNRQNGGGNWGGAGGGGGFGNSGGNFGGGQGGGSGGWNQQGGSGGGPWNNQGGGNGGWNGGGGGGYGGGNSNGSWGGNGGGGGGGGGFGNEYQQSYGGGPQRNSNFGNNRPAPYSQGGGGGGFNKGNQGGGQGFAGNNYNTGGGGQGGNMGGGNRRY", "text": "FUNCTION: This protein is a component of ribonucleosomes. Could be needed to organize a concentration gradient of a dorsalizing morphogen (Dm) originating in the germinal vesicle. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nuclear and/or cytoplasmic."}
{"protein": "MKKIYKRLLFSGLALSMLFFLSGCVQMKNGKPTGEGWVYKFFAAPMGSVIQYLANNLGLGFGFAIIIVTVIVRLLILPLGLSQVRKMTYQSEKMAYLKPVFDPIQERMKNAKTQEEKMAAQTELMQAQRHYGMSMFGGLGCLPLLIQMPFFSALYISTRYTKGIASASFLGIKLGSPNMIITVIIGILYLVQSWVSTLSVPEAQRQQTRNMMFMMPIMMVMISIGAPAGGALYWLVSGIFGLIQQLITNHIIKPKLRKQIDEEFKKNPPKPFKSNARKDITPQANNDKKLITSKKQKSNRNAGKQRHHKQ", "text": "FUNCTION: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins (By similarity). Partially complements an E.coli yidC depletion experiment. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily."}
{"protein": "MESGGKTNRQLRKAICVSTDEKMKKKRSPSVIVIGGGMAGISAARTLQDASFQVVVLESRDRIGGRVHTDYSFGFPVDLGASWLHGVCKENPLAAVIGRLGLPLYRTSGDNSVLYDHDLESYALFDKAGNQVSQELVTKVGENFEHILEEICKVRDEQDEDMSIAQAFSIVFKRNPELRLEGLAHNVLQWYLCRMEGWFAADAETISAKCWDQEELLPGGHGLMVRGYRPVINTLSKGLDIRLSHRITKISRRYSGVKVTTEKGDTFVADAAVIALPLGVLKSGMITFEPKLPQWKQEAINDLGVGIENKIILNFDNVFWPNVEFLGVVAETSYGCSYFLNLHKATSHPVLVYMPAGQLARDIEKKSDEAAANFAFSQLQKILPDASSPINYLVSRWGSDINSLGSYSYDIVNKPHDLYERLRVPLDNLFFAGEATSSSYPGSVHGAYSTGVLAAEDCRMRVLERYGELEHEMEEEAPASVPLLISRM", "text": "FUNCTION: Flavoenzyme involved in polyamine back-conversion (PubMed:18583528, PubMed:20532512, PubMed:21081665). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (PubMed:18583528, PubMed:20532512, PubMed:21081665). Substrate preference is spermidine > spermine > N(1)-acetylspermidine > N(1)-acetylspermine (PubMed:18583528). Plays an important role in the regulation of polyamine intracellular concentration (Probable). Involved in the production of hydrogen peroxide during pollen tube growth (PubMed:20626657). Hydrogen peroxide triggers the opening of the hyperpolarization-activated calcium permeable channels in pollen, and thus regulates pollen tube growth (PubMed:20626657). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the flavin monoamine oxidase family."}
{"protein": "MGKKRAPQKGKTVTKPQEIIVDESKLNWKPVDIPDTLDDFGGFYGLEEIDGVDVKVVDGKVTFVTKKDSKVLKDSNKEKVGDDQESVENESGSDSESELLEFKNLDDIKEGELSAASYSSSDEDEQGNIESSKLTDPSEDVDEDVDEDVLKENVFNKDINIDDISPVNLPEWTNLAPLSMTILQSLQNLNFLRPTEIQKKSIPVIMQGVDVMGKASTGSGKTLAYGIPIVEKLISNFSQKNKKPISLIFTPTRELAHQVTDHLKKICEPVLAKSQYSILSLTGGLSIQKQQRLLKYDNSGQIVIATPGRFLELLEKDNTLIKRFSKVNTLILDEADRLLQDGHFDEFEKIIKHLLVERRKNRENSEGSSKIWQTLIFSATFSIDLFDKLSSSRQVKDRRFKNNEDELNAVIQHLMSKIHFNSKPVIIDTNPESKVSSQIKESLIECPPLERDLYCYYFLTMFPGTTLIFCNAIDSVKKLTVYLNNLGIPAFQIHSSMTQKNRLKSLERFKQQSAKQKTINHSNPDSVQLSTVLIASDVAARGLDIPGVQHVIHYHLPRSTDIYIHRSGRTARAGSEGVSAMICSPQESMGPLRKLRKTLATKNSVSTDLNSRSTNRKPIKWQNTVPLLPIETDILSQLRERSRLAGELADHEIASNSLRKDDNWLKKAADELGIDVDSDEDDISKSNSDTFLLKNKNKKMQKTINKDKVKAMRATLNELLSVPIRKDRRQKYLTGGLVNLADNLVKKRGHNSIIGHEKTNALETLKKKKKRNN", "text": "FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. Required for the maintenance of dsRNA killer plasmid. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily."}
{"protein": "MSLLKERKPKKPHYIPRPPGKPFKYKCFQCPFTCNEKSHLFNHMKYGLCKNSITLVSEQDRVPKCPKSNSLDPKQTNQPDATAKPASSKSVANGLSAFDSKLQHSSAREDIKENLELQARGTHRCLGQKPALHRASPCKSPAPEAALGAQPALEGAARPSAFVPVGEHRLKGPDNAEAPETLALHNPTAKAVSFHTKSAFHTPGYPWKAGSPFLPPEFPHKISSTKGLGAISPYMHPTIPEYPPHFYTEHGLATIYSPYLLAGSSPECDAPLLSVYGTQDPRHFLPHPGPIPKHLAPSPATYDHYRFFQQYPSNLPIPYGFYRPESAFSSYGLRLPPVTGLTRDQSSHLLEEATLVYPASSPSRLNPSDPNRKHVEFESPIPEAKDSSKAGQRDTEGSKMSPRAGSAATGSPGRPSPTDFMQTSQTCEGLYDLSNKAASSALGRLYPPEQSLTAFRPVKKSTECLPAQAAETTAESPVSLNVVNGDPPAPTGSASLVSEAAPSSPDDSSGMGPLNLSKKSEINLAATHEPTYQGSPQAETASFSELQDLPLNLSVKDPCNTQAPRPAFPGRPRAAEPAAAVPQKTGTEGSEDGPSHPETKPGSLDGDGAPPTGPGEEAPDACAVDSSEEQKQTAAVALCQLAAYSPRNIRVGDGDAAAPEPACRQDTPTLSSMESQEAQCDLRPKGQKRTSLRDAGKSQQGAKKAKLQDTARVFTLRRRARVS", "text": "FUNCTION: Transcription factor involved in epidermis differentiation. Required for terminal epidermal differentiation: acts downstream of p63/TP63 and activates expression of late epidermal differentiation genes. Specifically binds to the promoter of KLF4 and promotes its expression. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSVMFDPDTAIYPFPPKPTPLSIDEKAYYREKIKRLLKERNAVMVAHYYTDPEIQQLAEETGGCISDSLEMARFGAKHPASTLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCPVEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGEKIIWAPDTHLGRYVQKQTGADILCWQGACIVHDEFKTQALTRLQEEYPDAAILVHPESPQAIVEMADAVGSTSQLIAAAKTLQHQRLIVATDRGIFYKMQQAVPDKELLEAPTAGEGATCRSCAHCPWMAMNGLQAIAEALEQEGSNHEVYVDERLRERALVPLNRMLDFAATLRG", "text": "FUNCTION: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the quinolinate synthase family. Type 1 subfamily."}
{"protein": "MAEEIVLYYFDARGKAELIRLIFAYLGIQYTDKRFGENGDAFIEFKNFKKEKETPFNQVPILEMDNIIFAQSQAIVRYLSKKYKISGNSELNEFYADMIFCGVQDIHYKFNNTNLFKQNETTFLNEELPKWSGYFENILKKNNCNYFVGDDLTYADLAVFNLYDDIETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNRKESVY", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin). SIMILARITY: Belongs to the GST superfamily."}
{"protein": "METTEPGQADGEERMMDLRPRTRSNPEGAEDRRSSTGSLNSSLPSAPQPAVGSRVEGEGEAASSDSPPVSATAIAATASVPVAAVGNTTTTNTASLPAMSPAVKERPKPSQPTMPTQIPPSAELHLRAPRVNCPEKVIICLDLSEEMSLQKLESINGSKTNALNISQKMIEMFVRTKHKIDKRHEFALVVVNDDAMWLSGFTSDPRELCSCLYDLETNVCESFNLEDLFNVILQKIELPQMENIQTIPPPFVVRTLLVFSRHAGMLQFNPSDAVKKMLQSPYFFFDVVFLHNGTEEQTEDTSWKDVYASFCELDTKGMCYRFEVSLCGPAIELHNCMAKLLCHPLQRPFQSHASYSLLEDEDTLENEATV", "text": "FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'- linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of babam2 and help the 'Lys-63'-linked deubiquitinase activity mediated by brcc3/brcc36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). SIMILARITY: Belongs to the BABAM1 family."}
{"protein": "MANSTVAEPEKMEQSGTCEEDEEEENMEGDEDECDDDEEENMEPAETVTIGSTYKCRRSDNTLHAAEIIKTRKTKENAEEFYVHYVGLNRRQNEWVDKSRVLQAKQIKTEELNNTEDETNGVSDQSEGKAARSNKRKIEDGDGDQKKRKVDDEEDDFTEDLTCPLCRSLFKEPVILECGHNFCKHCIDKSWESASAFSCPECKEVLTERKYTTNRVLANLVKKAAVGVKDKDVKPKEKCDEHDERLKLFCKDDGTLACVICRDSLKHSNHNFLPIQDAVGVYRDQLIALVSPLETTMKENQKLKCDQSQKISLHRENIVDCKKHIECEFEKLHQFLREKEAKMVEDLNAEREGLLKDMEANLVKMTDNCEFIEEAISTTQSRLNESDPIAFLTDIKSFIEKCCEEHRKGVPAESVLVNKELSQGRFKGPLQYIIWKELKSVVQPGLAPLTLDPNTAHPNLVLSEGLTSVKYTDTKQQLPDNPKRFSQCILVLGAEGFDSGKHYWEVEVGNKTAWDVGMASESSNRKGKIKLNPKNGYWAIWLRNGNAFKALESPSKTLNLTSKPSKIGVYLDYEGGQVSFYNADDMSPIYTFNGSFTEKLYPYLSPFLQDSGKNAEPLKLVHTKL", "text": "FUNCTION: May be a nuclear regulatory protein that is stored in the germinal vesicle for use during early embryogenesis and may play a role in the synthesis or processing of pre-mRNA during oogenesis. Binds 3 Zn(2+) ions. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Lampbrush chromosome loops and in some nucleoplasmic particles of the germinal vesicle."}
{"protein": "MAPRRRKAKRRRHTLRSECKDKCKCHVQCYVSPRKRRRKLKPQGDDDINTTHQQQAALTEEQRREEVEEEGEERERRGEEEREGEGGEEGEGREEAEEEEAEEKEAEEEEAEEAEEEAEEEEAEEAEAEEEEAEEEEAEEEEAEEAEEEEAEEAEEEAEEEEAEEEAEEEAEEAEEAEEEAEEEAEEAEEAEEAEEAEEEAEEAEEEAEEAEEEAEEAEEAEEAEEAEEEAEEAEEEEEEAGPSTPRLPHYKVVGQKPSTQPGGVPKLCLKMQPQHRSRLPKGKQSHDKVPKKYQARNKFFSQAAPSVLDLSPKSWCWVVDFWGPTDALYRLSRSLSFPGAVSSGIQTFPKGPHATGPWVYFITVYCRTFQTAKEVIKAQKKYEKKYPRSAKLKASLGKFSKSLPIE", "text": "SIMILARITY: Belongs to the herpesviridae ICP22 family."}
{"protein": "MRCGPLYRFLWLWPYLSYVEAVPIRKVQDDTKTLIKTIVTRINDISHTQSVSSKQRVTGLDFIPGLHPLLSLSKMDQTLAIYQQILTSLPSRNVVQISNDLENLRDLLHLLAASKSCPLPQVRALESLESLGVVLEASLYSTEVVALSRLQGSLQDMLRQLDLSPGC", "text": "FUNCTION: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (By similarity). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (By similarity). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity). May also play an apoptotic role via JAK2-STAT3 pathway and up- regulation of BIRC5 expression. Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells. Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (By similarity). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up- regulation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the leptin family."}
{"protein": "SEKITVFQKNFQVTENSSHFV", "text": "FUNCTION: Catalyzes the hydrolysis of ester bond in chlorophyll to yield chlorophyllide and phytol. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MTGKQHQKHEQKARQAQVKAQINRDKARSKLLRQREKLARRRARNRRQSEVRRGNQSKAQHDTQSETQRGTQSKSQRDNETGGTKNPTAHSTLPPQKTNAENAVRNSHSTVPELPKYSSVPARERLYGLRLHRETTASEDKSVTVAVTRAPKAERQRGGADE", "text": "FUNCTION: May play a structural or regulatory role in gas vesicle synthesis. SUBCELLULAR LOCATION: Gas vesicle."}
{"protein": "MERKKFSSKFIHLLIVFLLLCTFLSRTESALPYHHELFLGRKRMNYYKPNSAIGTPSSTSDHAPGSNGRKLMSIYRPNGDIFTGPSGSGHGGGRTPAP", "text": "FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (PubMed:33514716, PubMed:34535661). Inhibits root growth and regulates root meristems (PubMed:34535661). Promotes ROS production and MAPK (e.g. MPK3, MPK4 and MPK6) activation in a MIK2-dependent manner, thus leading to the up-regulation of immune-related marker genes (e.g. WRKY30, WRKY33 and CYP81F2) (PubMed:34535661). SUBCELLULAR LOCATION: Cell membrane Secreted, extracellular space, apoplast Note=The precursor of SCOOP10, PROSCOOP10, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP10 in the apoplasm. SIMILARITY: Belongs to the serine rich endogenous peptide (SCOOP) phytocytokine family."}
{"protein": "MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFEDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNRRDLNFERGGDITLRCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLTSAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC", "text": "FUNCTION: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cell projection, growth cone Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). SIMILARITY: Belongs to the NDRG family."}
{"protein": "MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAISSWREKVVAEVGDIPTALVQNKIDLLDDSCIKNEEAEGLAKRLKLRFYRTSVKEDLNVSEVFKYLAEKHLQKLKQQITEDPEQTHSSSNKIGVFNASVGSHLGQNSSSLNGGDVINLRPNKQRTKRTRNPFSSCSVP", "text": "FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes (By similarity). Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm Endosome membrane Cytoplasmic vesicle, autophagosome Cytoplasmic vesicle, phagosome Cytoplasmic vesicle, phagosome membrane; Lipid-anchor; Cytoplasmic side Note=Recruited to phagosomes containing S.aureus or Mycobacterium. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MRAIISLLLISAMVFYIIAAVPEEEGLQLSEDERGGCLPHNRFCNALSGPRCCSGLRCKELSIRDSRCLG", "text": "FUNCTION: Insect active toxin causing rapid but reversible paralysis in crickets. No activity shown in mammals. Does not show effect on mammalian voltage-gated calcium channels (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 01 (U2-agtx) family."}
{"protein": "LVKPPYSYIALITMAILQSPQKKLTLSGICEFISNRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPQSEDMFDNGSFLRRRKRFKR", "text": "FUNCTION: Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator (By similarity). Negatively regulates transcription of transcriptional repressor Rhit/Zfp13 (By similarity). Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "GTCKCDDDGPDVRTATFTGSTEFANCNESWEKCLAVYTPVASCCRKKK", "text": "FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type II subfamily."}
{"protein": "MKLAYWMYTGPAHIGTLRIASSFKNVHAIMHAPLGDDYFNVMRSMLERERNYTPVTTSVVDRNVLARGSQEKVIDNILRKDKEEQPDLIVLTPTCTSSILQEDLQNFVEQASLNSMADVLLADVNHYRINELQACDKTLEQIVRFYIEKNRASLTLEKVKTLLPSVNLIGISSLGFHNNHDTRELKKLFELYEIILNCSLPQGTTVKTLINLPKAWLNILPYRELGLLTSKYLNKEFGLLSLVILPMGNINLNRFLKKLLFSLKLENNTITKVINIKLLKLLNLNWIKKEAIKSKLKRKKAIIFGSSNHVATLTKLLSKEIGLEIILCGTYCKSESKWFSEQVQNYCNKILITEDHTMISNEISKLKPDVIFGTQMERHIGKRLGIPCGVISSPIHIQNFPLSYKPMVGYEGVKTIMDLLFNSLNLKDRKNSFTLFNEII", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the ChlB/BchB/BchZ family."}
{"protein": "MPAEVAAGLPPLPPNHFYFYPPDPLLEGDGAITAIEDSDPFDQYVYRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFQWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLDNGPAQALYTRQFYELLHSRLRPGGVVAVQGLEFSHSDDKPHAALARTLRSVFSQVHSYRATVPSFLSSWGFLLASDWLDTNHWQAEDIDRRIERKLGPLWLDHLDGDYLKACFVMDRETRFLLAQPGPVLEDGVPFVAPPDIEEIEFGPAQLPALART", "text": "FUNCTION: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the spermidine/spermine synthase family."}
{"protein": "MTDKEKKPCAIIVVGMAGSGKTTFMQQLNAHLHSKNKPPYILNLDPAVRNLPYEANIDIRDTINYKEVMKQYNLGPNGGIMTSLNLFVTKFDQVLKILEKRAPTVDHILIDTPGQIEIFQWSASGSIICDTLASSWPTCIAYVVDTPRATSTSTWMSSMLYACSMLYKAKLPLIIVYNKCDVQDSEFAKKWMTDFEEFQQAVTKDEGMSSEGATSGYMGSLVNSMSLMLEEFYRHLDFVSCSSVTGEGMDDFLEAVKAKVKEYEEEYVPEMERMKEIQRQTKERQKEAQLSKLMKDMHVSKDKEDVGLTVSDAEDEYNGELVDPDEDDGLTAEDREDMIKQYRVALGISDDISDEKLLEMLTERMKQ", "text": "FUNCTION: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPN-loop GTPase family."}
{"protein": "MGTAKVTTPLVFAITIATIGSFQFGYNTGVINAPEAIIKDFLNNTLREKSKSMPSEVLLTSLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLIVNLLAITGGCLMGFCKISRSVEMLILGRLVIGLFCGLCTGFVPMYIGEISPTALRGAFGTLNQLGIVIGILVAQIFGLKLILGTELLWPLLLGFTIIPAVLQCAALPFCPESPRFLLINRKEEERAKEILQRLWGTQDVAQDIQEMKDESLRMAQEKKVTVLELFRAPNYRQPIIISIMLQLSQQLSGINAVFYYSTGIFKDAGVQEPIYATIGAGVVNTIFTVVSLFLVERAGRRTLHLIGLGGMAFCSLLMTISLLLKDNHTWMSFICIGAILVFVAFFEIGPGPIPWFIVAELFGQGPRPAAMAVAGCSNWTSNFLVGLLFPSAAFYLGAYVFIVFTCFLVVFWVFTFFKVPETRGRTFEEITRAFEVQVPAGSRAEKGPIVEMSSIPPSKDAV", "text": "FUNCTION: Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane. Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate. Does not mediate fructose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Perikaryon Cell projection Note=Localized to densely spaced patches along neuronal processes. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily."}
{"protein": "MACPLDQAIGLLVAIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMDDLDRNKDQEVNFQEYVAFLGALALIYNEALK", "text": "FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). SUBCELLULAR LOCATION: Nucleus envelope Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the S-100 family."}
{"protein": "MDQAKLARMQASVRIGGKGTPRRKVKKVHKSSGTDDKKLQTALKKLNVQPIQAIEEVNMFKSDGNVIHFSAPKVHASVPSNTFAIYGNGEDKELTELVPGILNQLGPDSLASLRKLAESYQSMQKEKGEDGDKKDDDDEDDDDIPELVAGDNFESKTEVE", "text": "FUNCTION: Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic, may also transiently localize to the nucleus. SIMILARITY: Belongs to the NAC-beta family."}
{"protein": "MIERLKKVSLPALSAFILFCSCHYGRILGVICFDIGQRTSDDSLVVRNRHQFKWFCLSCRLISVTAVCCFCAPYVADIEDPYERLLQCFRLSASLICGICIIVVQVCYEKELLRMIISFLRLFRRVRRLSSLKRIGFGGKREFFLLLFKFICLVYELYSEICQLWHLPDSLSLFATLCEIFLEIGSLMIIHIGFVGYLSVAALYSEVNSFARIELRRQLRSLERPVGGPVGRKQLRIVEYRVDECISVYDEIERVGRTFHRLLELPVLIILLGKIFATTILSYEVIIRPELYARKIGMWGLVVKSFADVILLTLAVHEAVSSSRMMRRLSLENFPITDHKAWHMKWEMFLSRLNFFEFRVRPLGLFEVSNEVILLFLSSMITYFTYVVQYGIQTNRL", "text": "FUNCTION: Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Gustatory receptor (GR) family. Gr93a subfamily."}
{"protein": "MVSATRSLLCAALPVLATSRQATGAPVANELRCQCLQTVAGIHFKNIQSLKVMPPGPHCTQTEVIATLKNGREACLDPEAPMVQKIVQKMLKGVPK", "text": "FUNCTION: Has chemotactic activity for neutrophils. Contributes to neutrophil activation during inflammation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
{"protein": "MAKPKSPSRRELLTNGVKAAGVTCLAGLALTAYVESASKAEAKALRPPGALPEDDFLAACVRCGLCVRACPYDTLRLAEMGEEAPLGTPFFVARETPCFMCTDVPCAKACPTGALDRDIPNIRKADMGVAVLVGHESCLNYKGITCSICHRVCPIRDEAITLEVQTIKGRRMVIPTVHSDKCTGCGTCEKHCVLGQAAIRVLPRELGLGGRGRNPAGRAV", "text": "FUNCTION: Involved in electron transfer."}
{"protein": "MAQPGSGCKATTRCLEGTAPPAMAQSDAEALAGALDKDEGQASPCTPSTPSVCSPPSAASSVPSAGKNICSSCGLEILDRYLLKVNNLIWHVRCLECSVCRTSLRQQNSCYIKNKEIFCKMDYFSRFGTKCARCGRQIYASDWVRRARGNAYHLACFACFSCKRQLSTGEEFGLVEEKVLCRIHYDTMIENLKRAAENGNGLTLEGAVPSEQDSQPKPAKRARTSFTAEQLQVMQAQFAQDNNPDAQTLQKLADMTGLSRRVIQVWFQNCRARHKKHTPQHPVPPSGAPPSRLPSALSDDIHYTPFSSPERARMVTLHGYIESQVQCGQVHCRLPYTAPPVHLKADMDGPLSNRGEKVILFQY", "text": "FUNCTION: Probable transcription factor required for the expression of a subset of genes involved in interneurons migration and development. Functions in the specification of cortical interneuron subtypes and in the migration of GABAergic interneuron precursors from the subpallium to the cerebral cortex (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSEDIFDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVTGGRLYAHSLERIIPGFADQAPIERMITHEKLAFMTDNGAMTIDYCNGEDASASQVSYSVLRSKFDAWLMEQAEEAGAQLITGIRVDNVVQRDGKVVGVEADGDILEAKVVILADGVNSLLAEKLGMAKRVEASHVAVGVKELIELPKSVIEDRFQLQGNEGAACLFAGAPTDGLMGGGFLYTNETTLSLGLVCGLHHLKDAKKSVPQMLEDFKQHPAVAPLIAGGKLVEYAAHVVPEAGMNMQPELVGDGVLIAGDAAGMCMNLGFTIRGMDLAISAGEAAAKTVLSAMKRDDFSKQSLGEYRQHLDEGPMRDMRMYQKLPAFLDNPRMFTAYPEMAVSIARDLFTVDGSAPVPMRKKILRHAKKVGFINLMKDGLKGVTVL", "text": "FUNCTION: Could be part of an electron transfer system required for anaerobic carnitine reduction. SIMILARITY: Belongs to the ETF-QO/FixC family."}
{"protein": "MSESVTQQVFNFAVTKSQPFGGYVYSTNLTASTSSAVTSTQLTPLNLSITLGQITLSGNSLVIPATQIWYLTDAYVSVPDYTNITNGAEADGVILIYKDGVKLMLTTPLISSMSISNPARTHLAQAVKYSPQSILTMYFNPTKPATASTSYPNTVYFTVVVVDFSYAQNPARAVVSANAVM", "text": "FUNCTION: VP4 self-assembles to form, together with capsid protein VP10, an icosahedral caspid of 87 nm in diameter, with a T=43 symmetry and composed of 420 hexamers and 12 pentamers (PubMed:31636205). VP4 proteins arrange into hexons, while VP10 proteins form the pentameric densities located at the 5-fold axes in the virion (PubMed:31636205). The stoichiometry of VP4:VP10 is 42:1 (PubMed:31636205). SUBCELLULAR LOCATION: Virion."}
{"protein": "MLQALLDSKDFLALTLAHPEQFDSEFSFRLGDHTQVEVWDTGVIVFEPAQNEGKDVVLSCGVHGNETAPIELCNGLIKQLLQQKIIAKQRTLFLIGNPLAINNGTRIIDENMNRLFSGEHSNPPGLVNPERVRAKKLEAYIDRFYTAVADGRQRIHYDLHTAMRASKHEKFAIYPYRPGRAFSGEQIMFLAASGVDTVLFHHEPTTTFSYFSSERYGADAFTIELGKVYPMGQNDMTRFIATHEMFMRLITAKPLELDAFDADKVNLYQVCRVINKHFDDFEFTFATDVENFRSFPKGFVLAREGGQEIKVEHEFESVVFPNAKVPIGNRTVICLIPAVNADVR", "text": "FUNCTION: Transforms N(2)-succinylglutamate into succinate and glutamate. SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily."}
{"protein": "MITIEQLLDILKKDHNFREVLDADEYHYHYQGFSFERLSYDSRQVDGKTLFFAKGATFKADYLKEAITNGLQLYISEVDYELGIPVVLVTDIKKAMSLIAMAFYGNPQEKLKLLAFTGTKGKTTAAYFAYHMLKESYKPAMFSTMNTTLDGKTFFKSQLTTPESLDLFAMMAECVTNGMTHLIMEVSSQAYLVDRVYGLTFDVGVFLNISPDHIGPIEHPTFEDYFYHKRLLMENSRAVVINSVMDHFSFLADQVADQEHVFYGPLSDNQITTSQAFSFEAKGQLAGHYDIQLIGHFNQENAMAAGLACLRLGASLADIQKGIAKTRVPGRMEVLTMTNHAKVFVDYAHNGDSLEKLLSVVEEHQTGKLMLILGAPGNKGESRRADFGRVIHQHPNLTVILTADDPNFEDPEDISKEIASHIARPVEIISDREQAIQKAMSLCQGAKDAVIIAGKGADAYQIVKGQQVAYAGDLAIAKHYL", "text": "FUNCTION: Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family. MurE subfamily."}
{"protein": "MSATSEMLAEINEVNLSYLLLAQRLLREDKAMGMFRMGISEELADVLVNLTLAQTVKLAASNQMLCRFRFDDHALLSSLADKGRSSAVSHAHSAILMAGQPVESLR", "text": "FUNCTION: Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FlhD family."}
{"protein": "MTELRQRVAREPEAPPEDKESESEAKADGETASDSESRVEAVTQPPSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSGLFRLQEYNIPGVIQSIIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLVQQFLTLRPDQQLHIFNTLKSHLTDKGMLTAATEDK", "text": "FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP- diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (By similarity). Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By similarity). Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDS family."}
{"protein": "MMQDVSSSPVSPADDSLSNSEEEPDRQQPPSGKRGGRKRRSSRRSAGGGAGPGGAAGGGVGGGDEPGSPAQGKRGKKSAGCGGGGGAGGGGGSSSGGGSPQSYEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH", "text": "FUNCTION: Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of pro-inflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-BMAL1 heterodimer (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGDPRISHIELDEATIIWRNADIEQERRIAIFDLIEENTFKPLRAFEAGHEGPYRLKLSVEDGRLALTVSDDDGNGGGQLLETVILGLGRFRRPIREYFAICDSYYQAIRKATATEIETIDMARRGVHNEAAEMLLERLQGKIDTDFATARRLFTLICVLHIRG", "text": "SIMILARITY: Belongs to the UPF0262 family."}
{"protein": "MQKFFVTSALPYPNNSSPHLGNLVGALLSGDVYARFKRNQGHEVIYLCGTDEYGTTTMIRARKEGVTCRELCDKYFELHKKVYDWFNIEFDVFGRTSTTKQTEITWEIFNGLYNNGYIEEKTTVQAFCEKCDMYLADTYLKGYCYHDGCRENRVISNGDQCEICQKMIDVNKLINPFCSICLTPPIQKSTDHLYLSLDKLTPLVQQYLDRVEFDSRIMAISKAWLEIGLNPRCITRDLEWGTPIPINLDPKLEKYADKVFYVWFDAPIGYYSILANERDDWREWLNSGVTWVSTQAKDNVPFHSIVFPASVIGSNIELPLIDRICGTDYLLYEGQKFSKSQGVGLFGDKVAEISPKLGINEDYWRFYLMKIRPETQDSSFNLEEFVRIVKTDLVNNIGNFINRVFSLLEKTPYRDLNYQISPEYIEFIKKYEVSMDEFKFRDGLKICLEMSSRGNKFVQSTKPWTMIKDGLDTQEIMTEAVGICWILLNLLKPIIPKSACDMLSNLDTDNQNIFCLIGGSNINIRILNIIKLPFKNIDLKQLREFIEGKN", "text": "SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MVLCDKGAHELGNREIRKGFCERCLYPEYFDDEEAATTTPTIKKRPPKLTWAPKKKRRKAIHLSCGCSYYGGIDCEDGFTHRGITHVHTVPDWLLLRRHQEPNLLPPPEHNNNGDGEQNNNITNQSQPQPAESVGSPDLLAELGGTFSITSSEWRSIIR", "text": "FUNCTION: Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. Suppresses the host RNA silencing by inhibiting adenosine kinase 2 (ADK2), a kinase involved in a general methylation pathway. Also suppresses the host basal defense by interacting with and inhibiting SNF1 kinase, a key regulator of cell metabolism implicated in innate antiviral defense. Determines pathogenicity (By similarity). SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the geminiviridae transcriptional activator protein family."}
{"protein": "MPLEVVVELQIRAISCPGVFLPGKQDVYLGVYLMNQYLETNSFPSAFPIMIQESMRFEKVFESAVDPGAVVDLLEMWDELAYYEENTRDFLFPEPKLTPSHPRRCREVLMKTALGFPGIAPKIEFSTRTAIRECVFLHRNRFLEERHESRRPLSTSHEPIFPLNTIKMKLKENNLNRLPKGMQARAPSQYSTRHFFQDQPAQLNLGNNFKISGGSKPPFVVRHVDSAKPFGENISEHHLRRSRRKSKFSDFPFPTRRASSLDSLAANVKVIKEPDERIVLRSDSSSCLDSSQFGKSSSSKQGDADFHGKASFATYQHSTSPGPLDQPLLRERFHPGSQSTWKNIHERVCSLLTSHRAQLHQNKEDSTSEVNYIIERPSYPLKKYSLHEQRYF", "text": "SIMILARITY: Belongs to the SPATA6 family."}
{"protein": "MFHCPLCQHAAHARTSRYITDTTKERYHQCQNVNCSATFITYESVQRYIVKPGEVHAVRPHPLPSGQQIMWM", "text": "FUNCTION: This protein may act as an activator of P2 late transcription through an interaction with the alpha-subunit of the host RNA polymerase."}
{"protein": "MPKNKKRNAPHRGGGGGGGSGAATSAATTGGPHRTVQPFSDEDASIETMSHCSGYSDPSSFAEDGPEVLDEEGTQEDLEYKLKGLIDLTLDKSAKTRQAALEGVKNALSSKVLYEFVLERRMTLTDSIERCLKKGKSDGQRAAAALASVLCIQLGPGLESEEILKTLGPILKKIICDGTASIQARQTCATCFGVCCFIATDDITELYSTLECLEGIFTKSYLKEKDTNVPCSTPNTVLHISSLLAWTLLLTICPISEVKKKLELHFHKLPSLLSCDDVNMRIAAGESLALLFELARGMESDFFYEDMDSLTQMLRALATDGNKHRAKVDKRKQRSVFRDVLRAVEERDFPTETVKFGPERMYIDSWVKKHTYDTFKEALGSGMQYHLQTNEFLRNVFELGPPVMLDAATLKTMKIPRFERHLYNSAAFKARTKARSKCRDKRADVGEFF", "text": "FUNCTION: Probably participates in neurogenesis. Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Nucleus Note=Presents a NGF-dependent pattern of intracellular localization. With increasing amounts of NGF and besides being expressed in the cytoplasm, it is also localized in the plasma membrane (inner side) at the onset of NGF-induced differentiation, from where it disappears to reappear in the nuclei of differentiated cells. SIMILARITY: Belongs to the IFRD family."}
{"protein": "MNKCIPMIINGMIQDFDNYAYKEVKLNNDNRVKLSVITESSVSKTLNIKDRINLNLNQIVNFLYTVGQRWKSEEYNRRRTYIRELKTYLGYSDEMARLEANWIAMLLCSKSALYDIVNYDLGSIHVLDEWLPRGDCYVKAQPKGVSVHLLAGNVPLSGVTSILRAILTKNECIIKTSSSDPFTANALVSSFIDVNADHPITKSMSVMYWPHDEDMTLSQRIMNHADVVIAWGGDEAIKWAVKYSPPHVDILKFGPKKSLSIIEAPKDIEAAAMGVAHDICFYDQQACFSTQDVYYIGDNLPLFLNELEKQLDRYAKILPKGSNSFDEKAAFTLTEKESLFAGYEVRKGDKQAWLIVVSPTNSFGNQPLSRSVYVHQVSDIKEIIPFVNKNRTQTVSIYPWEASLKYRDKLARSGVERIVESGMNNIFRVGGAHDSLSPLQYLVRFVSHERPFNYTTKDVAVEIEQTRYLEEDKFLVFVP", "text": "FUNCTION: LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. SIMILARITY: Belongs to the LuxC family."}
{"protein": "MSGILTRWRQFGKRYFWPHLLLGMVAASLGLPALSNAAEPNAPAKATTRNHEPSAKVNFGQLALLEANTRRPNSNYSVDYWHQHAIRTVIRHLSFAMAPQTLPVAEESLPLQAQHLALLDTLSALLTQEGTPSEKGYRIDYAHFTPQAKFSTPVWISQAQGIRAGPQRLS", "text": "FUNCTION: Regulates secA expression by translational coupling of the secM secA operon. Translational pausing at a specific Pro residue 5 residues before the end of the protein may allow disruption of a mRNA repressor helix that normally suppresses secA translation initiation. SUBCELLULAR LOCATION: Cytoplasm, cytosol Periplasm Note=The active form is cytosolic, while the periplasmic form is rapidly degraded, mainly by the tail-specific protease. SIMILARITY: Belongs to the SecM family."}
{"protein": "MTEVRRRGRPGQAEPTAQKGAQALERGIAILQYLERSGGSSSVSDISGSLDLPLSTTFRLLKVLQAADFVYQDSQLGWWHIGLGVFNVGSAYIHNRDVLSVAGPFMHRLMLLSGETVNVAIRNGNEAVLIGQKECKSMVRMCAPLGSRLPLHASGAGKALLYPLTEEELVGIVVNTGLRRFTPTTLVDLPILLKNLEQAREQGYTVDQEEHVVGLNCIASAIYDDAGSVVAAISISGPASRLTEDRFISQGELVRDTAKDISTALGLKPPVA", "text": "FUNCTION: Negative regulator of allantoin and glyoxylate utilization operons. Binds to the gcl promoter and to the allS-allA intergenic region (By similarity)."}
{"protein": "MATTSAAVLNGLSSSFLTGGNKSQALLAAPLAARVGGAATPKRFTVLAAAAKKSWIPAVRGGGNLVDPEWLDGSLPGDYGFDPLGLGKDPAFLKWYREAELIHGRWAMAAVLGIFVGQAWSGIPWFEAGADPGAIAPFSFGTLLGTQLILMGWVESKRWVDFFDPDSQSVEWATPWSKTAENFANFTGEQGYPGGKFFDPLALAGTLNNGVYVPDTEKLERLKVAEIKHARLAMLAMLIFYFEAGQGKTPLGALGL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the ELIP/psbS family."}
{"protein": "MGPGRCLLTALLLLALAPPPEASQYCGRLEYWNPDNKCCSSCLQRFGPPPCPDYEFRENCGLNDHGDFVTPPFRKCSSGQCNPDGAELCSPCGGGAVTPTPAAGGGRTPWRCRERPVPAKGHCPLTPGNPGAPSSQERSSPASSIAWRTPEPVPQQAWPNFLPLVVLVLLLTLAVIAILLFILLWHLCWPKEKADPYPYPGLVCGVPNTHTPSSSHLSSPGALETGDTWKEASLLPLLSRELSSLASQPLSRLLDELEVLEELIVLLDPEPGPGGGMAHGTTRHLAARYGLPAAWSTFAYSLRPSRSPLRALIEMVVAREPSASLGQLGTHLAQLGRADALRVLSKLGSSGVCWA", "text": "FUNCTION: Probable cell membrane receptor for the IGF-like family proteins. Binds IGFL1 and IGFL3 with a higher affinity. May also bind IGFL2. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MATTRFPSLLFYSYIFLLCNGSMAQLFGQSFTPWQSSRQGGLRGCRFDRLQAFEPLRQVRSQAGIIEYFDEQNEQFRCAGVSVIRRVIEPQGLLLPQYHNAPGLVYILQGRGFTGLTFPGCPATFQQQFQPFDQAQFAEGQSQSQNLKDEHQRVHHIKQGDVVALPAGIVHWCYNDGDAPIVAVYVFDVNNNANQLEPRQKEFLLAGNNKREQQFGQNIFSGFSVQLLSEALGISQQVAQKIQSQNDQRGEIIRVSQGLQFLKPFVSQQGPVEHQAYQPIQSQEEQSTQYQVGQSPQYQEGQSTQYQPGQSWDQSFNGLEENFCSLEARQNIENPKRADTYNPRAGRITHLNSKNFPTLNLVQMSATRVNLYQNAILSPYWNINAHSVMHMIQGRARVQVVNNHGQTVFNDILRRGQLLIIPQHYVVLKKAEREGCQYISFKTNPNSMVSQIAGKTSILRALPVDVLANAYRISRQEAQNLKNNRGEEFDAFTPKFTQTGSQSYQDEGESSSTEKASE", "text": "FUNCTION: This is a seed storage protein. SIMILARITY: Belongs to the 11S seed storage protein (globulins) family."}
{"protein": "MYRRLGEALLLSRAGPAALGSAAADSAALLGWARGQPSAAPQPGLTPVARRHYSEAAADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCVGVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKVYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPVVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT", "text": "FUNCTION: Mitochondrial glutamate dehydrogenase that converts L- glutamate into alpha-ketoglutarate (PubMed:20670938). Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (By similarity). Plays a role in insulin homeostasis (PubMed:16959573). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity). SUBCELLULAR LOCATION: Mitochondrion Endoplasmic reticulum Note=Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
{"protein": "MADAPAPAGGRGGFRGGFGGRGRGRGRGRGRGRGRGRGAKDGDKEWVPVTKLGRLVKDMKIKTLEEIYLFSLPIKEFEIIDFFLGDALKDEVLKIMPVQKQTRAGQRTRFKAFVAIGDYNGHVGLGVKCSKEVATAIRGAIILAKLSVVPVRRGYWGNKIGKPHTVPCKVTGKCGSVLVRLIPAPRGTGIVSAPVPKKLLAMAGIDDCYTSARGQTATLGNFAKATYAAIAATYSYLTPDLWRETVFTKSPYQEYTDYLAKHHGRGAVTAHPTEEKPF", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays a role in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
{"protein": "MSSENKEQHDLSPRDLPEEAFGFPSELPLETQRRSGTDLRQSETGHGRRAFRRIHMELREKPDTDIKQFVIRELQKSCQCSAAKVRDGAFDFFPVLRWLPKYDLKKNILGDVMSGLIVGILLVPQSIAYSLLAGQEPIYGLYTSFFASIIYFLFGTSRHISVGIFGILCLMIGEVVDRELHKACPDTDATSSSIAVFSSGCVVVNHTLDGLCDKSCYAIKIGSTVTFMAGVYQVAMGFFQVGFVSVYLSDALLSGFVTGASFTILTSQAKYLLGLSLPRSHGVGSVITTWIHIFRNIRNTNICDLITSLLCLLVLVPSKELNEHFKDKLKAPIPVELIVVVAATLASHFGKLNGNYNSSIAGHIPTGFMPPKAPDWSLIPNVAVDAIAISIIGFAITVSLSEMFAKKHGYTVKANQEMYAIGFCNIIPSFFHCITTSAALAKTLVKESTGCQTQLSAIVTALVLLLVLLVIAPLFYSLQKCVLGVITIVNLRGALLKFRDLPKMWRLSRMDTVIWFVTMLSSALLSTEIGLLVGVCFSMFCVILRTQKPKNSLLGLEEESETFESISTYKNLRSKSGIKVFRFIAPLYYINKECFKSALYKKALNPVLVKAAWKKAAKRKLKEEMVTFRGDPDEVSMQLSHDPLEVHTIVIDCSAIQFLDTAGIHTLKEVRRDYEAVGIQVLLAQCNPSVRDSLARGEYCKKEEETLLFYSLSEAVAFAEDSQNQKGVCVVNGLSLSGD", "text": "FUNCTION: Sulfate transporter which mediates sulfate uptake into chondrocytes in order to maintain adequate sulfation of proteoglycans which is needed for cartilage development (PubMed:24302720). Mediates electroneutral anion exchange of sulfate ions for oxalate ions, sulfate and oxalate ions for chloride and/or hydroxyl ions and chloride ions for bromide, iodide and nitrate ions (PubMed:20219950, PubMed:22190686, PubMed:24302720). The coupling of sulfate transport to both hydroxyl and chloride ions likely serves to ensure transport at both acidic pH when most sulfate uptake is mediated by sulfate-hydroxide exchange and alkaline pH when most sulfate uptake is mediated by sulfate-chloride exchange (PubMed:22190686). Essential for chondrocyte proliferation, differentiation and cell size expansion (PubMed:24302720). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family."}
{"protein": "FKNPECGEPHSLDGSPNGISCRGYFPSWSYNPDAQQCVSFVYGGCGGNNNRFGSQNECEERCI", "text": "FUNCTION: Serine protease inhibitor. This peptide can inhibit, in-vivo, acrosin and, to a lower level, plasma kallikrein. It probably plays a role in Drosophila reproduction."}
{"protein": "MVYKVVVSDEDVTYQLELEDKDAKTVNGLKIGEEFNGGVLGLKGYKLRITGGSDKNGFPMKEDVDGTRRFKSLVNGGTGFKPTKKGLRRRKTVRGNTIADDISQINVKVSERGEQTLAEIFAEPEEEQEE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family."}
{"protein": "MNTVVGRRIINGRRRPRRQTRRAQRPQPVVVVQTSRATQRRPRRRRRGNNRTGRTVPTRGAGSSETFVFSKDNLAGSSSGAITFGPSLSDCPAFSNGMLKAYHEYKISMVILEFVSEASSQNSGSIAYELDPHCKLNSLSSTINKFGITKPGKRAFTASYINGTEWHDVAEDQFRILYKGNGSSSIAGSFRITIKCQFHNPKYVDEEPGPSPGPSPSPQPTPQKKYRFIVYTGVPVTRIMAQSTDDAISLYDMPSQRFRYIEDENMNWTNLDSRWYSQNSLKAIPMIIVPVPQGEWTVEISMEGYQPTSSTTDPNKDKQDGLIAYNDDLSEGWNVGIYNNVEITNNKADNTLKYGHPDMELNGCHFNQGQCLERDGDLTCHIKTTGDNASFFVVGPAVQKQSKYNYAVSYGAWTDRMMEIGMIAIALDEQGSSGSVKTERPKRVGHSMAVSTWETIKLPEKGNSEGYETSQRQDSKTPPTASGGSDTLDVEEGGLPLPVEEEIPDFVGDNPWSDLSTKNSQEEEAMSSESGLRPQLKPPGLPKPQPIRTIRNFDPTPDLVEAWRPDVNPGYSKADVAAATIIAGGSIKDGRSMIDKRNKAVLDGRKSWGSSLASSLTGGTLKASAKSEKLAKLTTSERARYERIKRQQGSTRASEFLESLLAGEDPDSRF", "text": "FUNCTION: [Minor capsid readthrough protein]: Minor component of the viral capsid involved in aphid transmission and virus accumulation in the host (PubMed:7882968, PubMed:20416918, PubMed:26402374, PubMed:10627524). Required for the virus to move through the aphid (By similarity). The RTD domain of the protein is exposed on the surface of the particle and determines the vector specificity and intestinal tropism in the aphid (PubMed:7882968). SUBCELLULAR LOCATION: [Minor capsid readthrough protein]: Virion Host cell junction, host plasmodesma Host periplasm. SUBCELLULAR LOCATION: [Cleaved product]: Virion. SIMILARITY: Belongs to the luteoviruses readthrough protein family."}
{"protein": "MGFIFSKSMNENMKNQQEFMVTHARLQLERHLTMQNEMRERQMAMQIAWSREFLKYFGTFFGIATISLATGALKRKKPAFLVPIVPLSFIFTYQYDLGYGTLLQRMKSEAEDILETEKTKLELPKGLITFESLEKARREQSKLFSDK", "text": "FUNCTION: Receptor for plasminogen. Regulates urokinase plasminogen activator-dependent and stimulates tissue-type plasminogen activator- dependent cell surface plasminogen activation. Proposed to be part of a local catecholaminergic cell plasminogen activation system that regulates neuroendocrine prohormone processing. Involved in regulation of inflammatory response; regulates monocyte chemotactic migration and matrix metalloproteinase activation, such as of MMP2 and MMP9. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Colocalizes on the cell surface with urokinase plasminogen activator surface receptor/Plaur."}
{"protein": "MKMKQFNLLSLFLILITSFGSANSTIVSHDERAITIDGQRRILLSGSIHYPRSTSDMWPDLISKAKDGGLDTIETYVFWNAHEPSRRQYDFSGNLDLVRFIKTIQSAGLYSVLRIGPYVCAEWNYGGFPVWLHNMPDMKFRTINPGFMNEMQNFTTKIVNMMKEESLFASQGGPIILAQIENEYGNVISSYGAEGKAYIDWCANMANSLDIGVPWIMCQQPHAPQPMIETCNGFYCDQYKPSNPSSPKMWTENWTGWFKNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHGGTNFGRVAGGPYITTSYDYDAPLDEYGNLNQPKWGHLKQLHTLLKSMEKPLTYGNISTIDLGNSVTATVYSTNEKSSCFIGNVNATADALVNFKGKDYNVPAWSVSVLPDCDKEAYNTARVNTQTSIITEDSCDEPEKLKWTWRPEFTTQKTILKGSGDLIAKGLVDQKDVTNDASDYLWYMTRVHLDKKDPIWSRNMSLRVHSNAHVLHAYVNGKYVGNQIVRDNKFDYRFEKKVNLVHGTNHLALLSVSVGLQNYGPFFESGPTGINGPVKLVGYKGDETIEKDLSKHQWDYKIGLNGFNHKLFSMKSAGHHHRKWSTEKLPADRMLSWYKANFKAPLGKDPVIVDLNGLGKGEVWINGQSIGRYWPSFNSSDEGCTEECDYRGEYGSDKCAFMCGKPTQRWYHVPRSFLNDKGHNTITLFEEMGGDPSMVKFKTVVTGRVCAKAHEHNKVELSCNNRPISAVKFASFGNPSGQCGSFAAGSCEGAKDAVKVVAKECVGKLNCTMNVSSHKFGSNLDCGDSPKRLFVEVEC", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
{"protein": "MYIYVLGSAAGGGFPQWNCNCPNCHGVRTGTIQAKARTQSSIAVSENGTDWVLLNASPDIRQQLFEFKAAQPARKLRDTGIISVILMDSQLDHTTGLLTLREGCPMNVWCTEMVHQDLTNGFPVFNMLKHWNGGLQYHEINPKQAFKIDGFENLEFLPLIIKSAAPPYSPHRNNPHDGDNIALIIKDHKTQKQLFYAPGLGKIDDQIMQIMQSSDCVMIDGTLWTDDEMQQTGVGTKTGREMGHLYISGEGGSLSYLNKLSTPKKVLIHINNTNPILNENSSQFAELKANGVEVAYDGMQIEL", "text": "FUNCTION: May be involved in the transport of PQQ or its precursor to the periplasm, in association with PQQ biosynthesis, but is not absolutely required for this synthesis. SIMILARITY: Belongs to the PqqB family."}
{"protein": "MTTMESLIGLVNRIQRACTVLGDYGGGTGSNAFNSLWEALPTVAVVGGQSSGKSSVLESIVGRDFLPRGSGIVTRRPLVLQLHKTDDGTEEYAEFLHLPKKQFTDFALVRREIQDETDRITGKNKQISPVPIHLSIYSPNVVNLTLIDLPGLTKVAVEGQPETIAEDIESMVRTYVDKPNCIILAISPANQDIATSDAIKLAKDVDPTGERTFGVLTKLDLMDKGTNALEVLEGRSYRLQHPWVGIVNRSQADINKNVDMMLARRKEREYFDTSPDYGHLASKMGSEYLAKLLSKHLESVIRTRIPSILSLINKSIEELERELDRMGRPVAVDAGAQLYTILEMCRAFDKIFKEHLDGGRPGGDRIYGVFDNQLPAALKKLPFDRHLSLQSVKKIVSEADGYQPHLIAPEQGYRRLIEGALGYFRGPAEASVDAVHYVLKELVRKSISETEELKRFPSLQVELAAAANSSLEKFREESKKSVIRLVDMESAYLTAEFFRKLPQEIERPVTNSKNQTASPSSATLDQYGDGHFRRIASNVSAYVNMVSDTLRNTIPKACVYCQVRQAKLALLNYFYSQISKREGKQLGQLLDEDPALMDRRLECAKRLELYKKARDEIDAVAWVR", "text": "FUNCTION: Microtubule-associated force-producing protein that is targeted to the tubulo-vesicular network of the forming cell plate during cytokinesis. Also plays a major role in plasma membrane maintenance and cell wall integrity with an implication in vesicular trafficking, polar cell expansion, and other aspects of plant growth and development. Has a GTPase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, phragmoplast. Note=Microtubule-associated and localized in the forming cell plate during cytokinesis. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MDISKLTDVKKVDLCKKYFLIGACFLPLVWIVNTFWFFSDAFCKPINAHRRQIRKYVIASIVGSIFWIIVLSAWEIFFQHYRAQGLVWTDFLTFVFPTGRV", "text": "FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch (glp-1 or lin-12). It may represent a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Note=Predominantly located in the endoplasmic reticulum and Golgi region. SIMILARITY: Belongs to the PEN-2 family."}
{"protein": "MSYQRNSARASLDLRSQYQQLEGRMRSEHFNPAYQQQQQKGQNIPLSLPSSLAQRNPIPYPIDAVTSDPTIPAQLNVYDHDRQNSIVDAAAGTNTTHSLNSNNIPSSQNNNINNNNINNVGSFTDPSMLTLPKMSLHSHQKQYDSNQNDPRSPLAILIPTSAQPTDVLSARFSAWRNVIRAILVYLSETASIQDEIVRQQLRLSHAVQFPFFSIENQYQPVSNEDKSMQKFFLPLGSGSVQDLPTMLTKYHDNLASLASKSSKELTSEIIPRLEDLRRDLLVKIKEIKALQSDFKNSCNKELQQTKHLMKLFNESLKECKLGTPKSDPFLIKLQLEKQIKRQLVEENYLHEAFDNLQNSGAQLESVIVMEIQNGLTSYARILGKEAQVVFDSVISKLDSTILNKNTNLEWDSFILRNISNFVPPNLPMRRFKEISYSNQNDPFTFEVKSGFLEKRSKFLKSYSRGFYVLTPSFLHEFKTPDKHKFSTPLMSIPLVECTVTEHSKKTKSNSEQGKNKFILRTNSNGLIHRGHNWVFKVDSYDDMIEWFGNIKALSSLPNYDDKCKYVSKVAKLSKEKAKSNENTTESVTPQVTNEQHTRYDDVSSSNFPLNSIPKLDNLTITNTTSSIPETNDSQIQNRVPEFYIENVDSPRKSNQL", "text": "FUNCTION: Together with SLM1, effector of the TORC2- and calcineurin- signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin, inhibiting interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MSIEEIPEEIPQGADVTILSKNEKKARELIKKLHLKPVPGITRVTFKQKGNLIYAIEQPDVFKSAAGTYVVFGEAKVDDMNKRIAEAQAQQEQQEALTKAAADAETADKSPESITNDLQNASLEDKTVEEDEGEVDETGLDSKDIEIIVEQTQVSRAKAVKALRAHKGDMVNAIMELS", "text": "FUNCTION: Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD2 may also be involved in transcription regulation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic, may also transiently localize to the nucleus. SIMILARITY: Belongs to the NAC-alpha family."}
{"protein": "MAKAEENLRDKCRWSLGGMTALVTGGSKGLGEAVVEELAMLGARVHTCARNETQLQECVREWQAKGFEVTTSVCDVSSRDQREKLMENVASIFQGKLNILVNNAGTGITKPTTEYTAQDYSFLMATNLDSAFHLSQLAHPLLKASGSGSIVLMSSTAGVVHINVGSIYGATKGAMNQLAKNLACEWARDNIRVNSVCPWFIATPLYLNDEELKKEVERKTPMGRVGNANEVSSLVAFLCFPAASYITGQTICVDGGFTVNCFSFKPVL", "text": "SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. SDR65C subfamily."}
{"protein": "MKISRSLSTVEVHTGGEAFRIVTSGLPRLPGDTIVQRRAWLKAHADEIRRALMFEPRGHADMYGGYLTEPVSPNADFGVIFVHNEGYSDHCGHGVIALSTAAVELGWVQRTVPETRVGIDAPCGFIEAFVQWDGEHAGPVRFVNVPSFIWRRDVSVDTPSFGTVTGDIAYGGAFYFYVDGAPFDLPVRESAVEKLIRFGAEVKAAANATYPVVHPEIPEINHIYGTIIANAPRHAGSTQANCCVFADREVDRSPTGSGTGGRVAQLYQRGLLAAGDTLVNESIVGTVFKGRVLRETTVGDFPAVIPEVEGSAHICGFANWIVDERDPLTYGFLVR", "text": "FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C) (By similarity). Does not possess neither proline racemase nor 4-hydroxyproline 2- epimerase activities (PubMed:17849014). SIMILARITY: Belongs to the proline racemase family."}
{"protein": "MELHSLSKRNSPVDPCNALEWSSGETSGDHIEEATIRDAFCYQKNLVSTPRADVVEVCRLSTSPASPTSLLQDSAIQTSFSLSGPPDSGNNQVMADRKVCNCCSQELETSFTYVDENVNLEQRSQRSPSAKGSNHPVDLGWGNPNEWSHETAMSLMSEDDDDTSSEATSSGKSVDYGFISAILFLVTGILLVIISYIVPREVTVDPNTVAAREMERLEKESAMLGAHLDRCVIAGLCLLTLGGVVLSCLLMMSMWKGELYRRNRFASSKESAKLYGSFNFRMKTSTNEDTLELSLVEEDALAVQS", "text": "FUNCTION: Plays an essential role in autophagy. TMEM74-induced autophagy may involve PI3K signal transduction (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM74 family."}
{"protein": "MTNFTFDGAHSSLEFQIKHLMVSKVKGSFDQFDVAVEGDINDFSTLKATATIIPSSINTKNEARDNHLKSGDFFGTDEFDKITFVTKSVSESKVVGDLTIKGITNEETFDVEFNGVSKNPMDGSQVTGVIVTGTINRENYGINFNQALETGGVMLGKDVKFEASAEFSISE", "text": "SIMILARITY: Belongs to the UPF0312 family."}
{"protein": "MGEEKSLLQFRSFPSLKTSDFALTEEPSWRLENNVSSNRRRGNKRSGGVFTNFASLSVAIRRDRRESTFNGRNGGGGGAFASVSVVIPKEEDEFAPTSAQLLKNPIALLSIVPKDAALFFAGAFAGAAAKSVTAPLDRIKLLMQTHGVRAGQQSAKKAIGFIEAITLIGKEEGIKGYWKGNLPQVIRIVPYSAVQLFAYETYKKLFRGKDGQLSVLGRLGAGACAGMTSTLITYPLDVLRLRLAVEPGYRTMSQVALNMLREEGVASFYNGLGPSLLSIAPYIAINFCVFDLVKKSLPEKYQQKTQSSLLTAVVAAAIATGTCYPLDTIRRQMQLKGTPYKSVLDAFSGIIAREGVVGLYRGFVPNALKSMPNSSIKLTTFDIVKKLIAASEKEIQRIADDNRKKASPNTIDEQT", "text": "FUNCTION: Specifically transports adenine nucleotides. Involved in the uptake of ATP into thylakoids in exchange for lumenal ADP. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein Plastid, chloroplast envelope Note=Detected only in low amounts in the chloroplast envelope and in non-photosynthetic plastids. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MISPDPRPSPGLARWAESYEAKCERRQEIRESRRCRPNVTTCRQVGKTLRIQQREQLQRARLQQFFRRRNLELEEKGKAQHPQAREQGPSRRPGQVTVLKEPLSCARRISSPREQVTGTSSEVFPAQHPPPSGICRDLSDHLSSQAGGLPPQDTPIKKPPKHHRGTQTKAEGPTIKNDASQQTNYGVAVLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSWKGQLNEDKLKGKLRSLENQLYTCTQKYSPWGMKKVLLEMEDQKNSYEQKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKRSEAEKLTLVTRVQQLQGLLQNQSLQLQEQEKLLTKKDQALPVWSPKSFPNEVEPEGTGKEKDWDLRDQLQKKTLQLQAKEKECRELHSELDNLSDEYLSCLRKLQHCREELNQSQQLPPRRQCGRWLPVLMVVIAAALAVFLANKDNLMI", "text": "FUNCTION: Adapter protein that plays essential roles in both innate and adaptive immunity. Plays a crucial role in the regulation of thymocyte development (PubMed:26195727). Mechanistically, mediates TCR-stimulated activation through recruiting MAP2K1/MEK1 to the Golgi and, thereby, facilitating the interaction of MAP2K1/MEK1 with its activator BRAF (PubMed:26195727). Also plays an essential role in regulatory T-cell stability and function by recruiting the serine-threonine phosphatase catalytic subunit (PPP2CA) to the lysosome, thereby facilitating the interaction of PP2Ac with the mTORC1 component RPTOR and restricting glycolytic metabolism (PubMed:30115741). Positively regulates TLR4 signaling activity in macrophage-mediated inflammation by acting as a molecular clamp to facilitate LPS-induced translocation of TLR4 to lipid rafts (PubMed:30573680). In response to viral infection, facilitates the recruitment of TRAF3 to MAVS within mitochondria leading to IRF3 activation and interferon production (PubMed:31390091). However, participates in the maintenance of immune homeostasis and the prevention of overzealous innate immunity by promoting 'Lys-48'- dependent ubiquitination of TBK1 (PubMed:32366851). SUBCELLULAR LOCATION: Cell membrane Golgi apparatus membrane; Single-pass type IV membrane protein Lysosome membrane Mitochondrion outer membrane Note=Accumulates on the mitochondria after virus infection."}
{"protein": "MLLRYITFHREKVLYLAIACFFGIYISFHDACILVPAKVGTNVTLNAVHVHDGDYVYWSFGGGGANRLMCRYTPRLDEIHKNTNRSFSCLTNHSLLLINVTEEYTDYYRTMTTFVHQSHNWHNHGNKWTLDTCYYVYVTQNGTLPTTTTKKPTTTTRTTTTTTTKKTTTTSTTTTTTTTKKTTTSTTHHRHSNPKESTTPKTHVELHVGLGATAAETPLQPSPQYQHVATHALWVLAVVIVIIIIIIFYFRIPQKLWLLWQHDKHGIVLIPQTDL", "text": "FUNCTION: Plays a role in the modulation of host immune response by modulating T-cell function. Interacts with host PTPRC/CD45 and thereby reduces host TCR signaling and T-cell proliferation. SUBCELLULAR LOCATION: Host cell membrane; Single-pass type I membrane protein Host endoplasmic reticulum Note=Localizes to the host cell membrane when highly glycosylated while less glycosylated forms are found on the endoplasmic reticulum. SIMILARITY: Belongs to the RL11 family."}
{"protein": "MGSTAPLRLPVIDLSMKNLKPGTTSWNSVRTQVREALEEYGCFEAVIDAVSPELQKAVCNKGHELLNLPLETKMLNGNKPEYDGFTSIPNLNEGMGVGRITDLEKVERFTNLMWPEGNKDFCETVYSYGKRMAEVDHILKMMVFESFGMEKHFDSFCESTNYLLHFMRYQQPGKDGRSPALSLHKDKSILTIVNQNDVKGLEFETKDGEWILPTADNHIVLLGDCFMAWSNGRLHSPLHRVTLVANQARLSTSSFSFPKDIIETPAELVDEEHPLLFNPFEITELLAYCFTKEGAKAVCDLKQYKAYTGA", "text": "FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family (PubMed:26359402). Catalyzes the conversion of yatein to deoxypodophyllotoxin (PubMed:26359402). Can also use, to some extent, demethylyatein as substrate (PubMed:26359402). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family."}
{"protein": "MHTLEMLLLLLLLLPLALGEGDGQAVAGDRNPSEARSTHEHFLQRLIRLIHGSDCQPCGQYVCCPPWKYAEYRRFT", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin Q superfamily."}
{"protein": "MTVTIYDVAREARVSMATVSRVVNGNQNVKAETKNKVNEVIKRLNYRPNAVARGLASKKTTTVGVIIPDISNIYYSQLARGLEDIAIMYKYHSIISNSDNDPEKEKEIFNNLLSKQVDGIIFLGGTITEEMKELINQSSVPVVVSGTNGKDAHIASVNIDFTEAAKEITGKLIEKGAKSFALVGGEHSKKAQEDVLAGLTEVLNKNSLQLGDTLNCSGAESYKEGVKAFAKMKGNLPDAILCISDEEAIGIMHSAMDAGIKVPEELQIISFNNTRLVEMVRPQLSSVIQPLYDIGAVGMRLLTKYMNDEKIEEPNVVLPHRIEYRGTTK", "text": "FUNCTION: Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions."}
{"protein": "MPLNEPSSNAFPRTVLFDLDGTLLDSAPDMLATANAMLAARGRAPITLAQLRPVISIGTFRILAVAFPELDAAAIQGLIPEFLQRYEALIGSVSKPFDGVEMMLDALECAGTVWGIVTNKPEFLARLILPLLGWTSRCAVLIGGDTLAERKPHPLPLLTAAERIGVMPTDCVYVGDDVSDIQAARAAGMPSMVALWGYRSHEDNPMTWQADTLVEQPHLLSRPDVWPST", "text": "FUNCTION: Specifically catalyzes the dephosphorylation of 2- phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family."}
{"protein": "MEILMTVSKLASICTMGANASALEKEIGPEQFPVNEHYFGLVNFGNTCYCNSVLQALYFCRPFREKVLAYKSQPRKKESLLTCLADLFHSIATQKKKVGVIPPKKFITRLRKENELFDNYMQQDAHEFLNYLLNTIADILQEERKQEKQNGRLPNGNIDSENNSTPDPTWVHEIFQGTLTNETRCLTCETISSKDEDFLDLSVDVEQNTSITHCLRGFSNTETLCSEYKYYCEECRSKQEAHKRMKVKKLPMILALHLKRFKYMDQLHRYTKLSYRVVFPLELRLFNTSGDATNPDRMYDLVAVVVHCGSGPNRGHYIAIVKSHDFWLLFDDDIVEKIDAQAIEEFYGLTSDISKNSESGYILFYQSRD", "text": "FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2. SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily."}
{"protein": "MTGISRRTFGLAAGFGAIGAGGLGGGCSTRSGPTPTPEPASRGVGVVLSHEQFRTDRLVAHAQAAEQAGFRYVWASDHLQPWQDNEGHSMFPWLTLALVGNSTSSILFGTGVTCPIYRYHPATVAQAFASLAILNPGRVFLGLGTGERLNEQAATDTFGNYRERHDRLIEAIVLIRQLWSGERISFTGHYFRTDELKLYDTPAMPPPIFVAASGPQSATLAGRYGDGWIAQARDINDAKLLAAFAAGAQAAGRDPTTLGKRAELFAVVGDDKAAARAADLWRFTAGAVDQPNPVEIQRAAESNPIEKVLANWAVGTDPGVHIGAVQAVLDAGAVPFLHFPQDDPITAIDFYRTNVLPELR", "text": "FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of hydroxymycolic acids (H-MAs) to ketomycolic acids (K-MAs), a lipid class making up the mycobacterial pseudo-outer membrane and over one- third of the dry weight of M.tuberculosis (PubMed:24349169). Does not exhibit F420-dependent glucose-6-phosphate dehydrogenase (FGD) activity (PubMed:23110042). SUBCELLULAR LOCATION: Cell envelope Note=The Rv0132c-F420 complex is translocated via the Tat pathway across the cytoplasmic membrane, where Rv0132c is anchored to the cell envelope. SIMILARITY: Belongs to the F420-dependent hydroxymycolic acid dehydrogenase family."}
{"protein": "MCQVGEDYGEPAPEEPPPAPRPSREQKCVKCKEAQPVVVIRAGDAFCRDCFKAFYVHKFRAMLGKNRLIFPGEKVLLAWSGGPSSSSMVWQVLEGLSQDSAKRLRFVAGVIFVDEGAACGQSLEERSKTLAEVKPILQATGFPWHVVALEEVFSLPPSVLWCSAQELVGSEGAYKAAVDSFLQQQHVLGAGGGPGPTQGEEQPPQPPLDPQNLARPPAPAQTEALSQLFCSVRTLTAKEELLQTLRTHLILHMARAHGYSKVMTGDSCTRLAIKLMTNLALGRGAFLAWDTGFSDERHGDVVVVRPMRDHTLKEVAFYNRLFSVPSVFTPAVDTKAPEKASIHRLMEAFILRLQTQFPSTVSTVYRTSEKLVKGPRDGPAAGDSGPRCLLCMCALDVDAADSATAFGAQTSSRLSQMQSPIPLTETRTPPGPCCSPGVGWAQRCGQGACRREDPQACIEEQLCYSCRVNMKDLPSLDPLPPYILAEAQLRTQRAWGLQEIRDCLIEDSDDEAGQS", "text": "FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CTU2/NCS2 family."}
{"protein": "MASNFWTSTHYKELKDPEEVNVVHPLDAQRGISVEDFRLIKLHMSNYISKLAQHIKIRQRVVATAVTYMRRVYTRKSLTEYEPRLVAPTCLYLACKAEESVVHAKLLVFYMKKLYADEKFRYEIKDILEMEMKVLEALNFYLVVFHPYRSLPEFLQDSGINDTSMTHLTWGLVNDTYRMDLILIHPPFLITLACIYIASVHKEKDIKTWFEELSVDMNIVKNIAMEILDFYENHRLFTEERVHAAFNKLATNP", "text": "SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily."}
{"protein": "MANEHSPLLVHGVYSMMGNAEDSRGGSAGTGEASNPKTDPRKLNTFFGVMVPTILSMFSIVLFLRTGFVVGHAGLLHGLLMLFVAYFIISLTILSICAISTNGAVEGGGAYFMISRSLGPEFGGSIGLMFYLAKVCACGVYVLGLVEAIMDVFGQDPGSSVAQGLRVLPQGYWYTVLYSSVVLLLCMLVCLVGAHIYAKASFLILLVVTVSLISIIISPLIVSPQGFNITHTYGNNHSVTVSPSYTGFNSTTLKNNLGPRYSLDYSTNTMMSFATVFAVMFTSCTGIMAGANMSGELKNPSESIPKGTIMAVAYTFTVYVLLYLLLSSTCDRSLLLNDYAVFQRVNVWPPFVTIGVYCASLSAAMCSMIGASRILHALALDQLFGLPLAPAAVTSSSGNPWVSVLYTWALVQCTLFAGQLNVIAGIVTVFYLLAYAAVDLACLALEWASAPNFRPTFQFFSWHTCLLGIISCVVMMFVINPVYSSASIVLLLLLLLFLHYRSPTSSWGYISQALIFHQVRKYLLMLDSRKDHVKFWRPQVLLMVSNPRSSCQLICFVNQLKKGGLFVLGHVQIGDLDVLPADPVQPQYNFWLSLVDKLGVKAFVDLTLSPSVRQGTQHLLRITGLGGMKPNTLVLGFYDNSYPEDYFLQDPVFCKGDRSEGDNFGVDLPSLQAHFPPVRHAESPRALQPQEYVSIIQDAIKMGKNICLARYFFQLPPESKGATYMWGKDSMDTIDVWPTNLLTPGSASYADVGSLFLLQMACVLNMASGWRRARLRIFVCVESESEDQGWLAKEEQFRELLGKLRIRAAIKIVAWDNVARMVRGPNTESQPVSEDFLCAVNGLLKEHSSTAAVRFLYLPDPPSSCELSQQYLTQLDTLTRDLGPTLLIHGVTPVTCTEL", "text": "FUNCTION: Seems to correspond to a subunit of a multimeric transport system and thus, additional subunits may be required for its function. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC12A transporter family."}
{"protein": "MDFLNKKIQKILFICILSFLIVNLTKSEISEVKDVSKFLSVGGGGTGGCQHPIYCNGTLLKTIQLTQVFNDSKTFVDMPMRTSIENVNELFNQLLLNTSKNGGPNKEELAAFLSENFYPAGYEVEPVTPVDWVPNPSFLDEITDPNLVDFARSIHGKWLELTRVFNTSGLCDGCYSSIPVNNPFVIAGSRFREFYYWDSYWIIQGLLVSDMTTTAKGMLRNFGDMITEFGFIPNGGRIYYLNRSQPPLFTQMVNKYFEATNGSDIEFLQEILPILDQEYQWWMTHRTTELTNGETGESVILNLYNVSNNSPRPESYYEDFTDAQSFSSVEEKDYFYSSIASGAESGWDFSSRWMSPSDNTNLTTIQTVDVVPVDLNSILYLNEKILSSFHRTLGNNSMAVYYQAQSESRVDAMQQVFFNEDTYQWNDYNLKTSTNNEAWYTSNILPLFADIQSSIDMDNQEIDLIFKSLANVLIAYPGGVPTSLISAQSLQWDGLNVWPPLQYWIIESIMTPNTTFSNMIGKNLIDRWITTNFCGWNSTLESEGGMMFEKYNANYIGVPGGGGEYVVQNGFGWTNGVDLYLLKKYGKSITLNSC", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 37 family."}
{"protein": "MAREQDSINSHPLDKYIDENSANESEIIKSSSQFSHEDQQKIDKLSKQIKPMDNDGLLNYGTEAQSNMSQFSHRILNEVKTTDVGPVGDSLNGLMSKLKSVNPEELNPENQSKLKRIFKRTKASVNEIFSKMQSVGSQIDRISIELDKHKNNLKKDIDMLDELYDMNKDYFDELSIYIEAAKHKQYVLQQDEIPKLREQAKSTGNQMDVQAASDMEQFVDRLDKRIYDLQLSRQIAIQTAPQIRMIQNVNQALAEKIQSSILTSIPLWKNQMSIALTLMRQRNAVSAQKAVTDTTNDLLLKNSELLKQNALATATENERGVVDIETLKTTQKDIIETIEQTLQIQEHGRTKRKQAESELNELETELQNQLLDMKENK", "text": "SIMILARITY: Belongs to the TelA family."}
{"protein": "MSNSFSFQRQNPGSPLQQHSPIHNINTGGNSNSVSNQSNNHPQTPGHHVPSRKPSIVEMLSSPPPLPNTPDQEDIHSFSLSRNTSVSSRASSIYGNVNGGTSKGSIVGVDWAEIPLVELTESNKLVSINSGFSVQKAFETLMEHNLTSVPVSLSKTDSTDLTNCLTFDYSDVNTYLLLIMNKINLNDLSIYEGGDDVLSNQQKDSITKSINKAKKGEEVPVDFIVKLHPKNPFVKFSEQDTLYKAMESLGNGVHRVAITNMNGTKITGILSQRRLIKYMWENARRFPSLDFYINSTLQDLKIGSNNPITIYEDQLLIEALLKMFTERVTSLAVVDKTMALIGNISIVDVKNVTSSKNSHLLFKSVLGFIGYNLTQKGIEEGQDQFPIFHVNNQSSLGRVIAKLVATKSHRLWVVENRGSVHHGSVSSTSSSNSNSNSKSVTQSPKASPSTIESTLNQSVSTPSNVQNIPPGSEPGGLPGKLVGVVTLTDILGLFASSKSNKKIDPQFARNQRRRSSTSTTRSSFEGSSAGQDLFRKSYTTSAPAKTEGKR", "text": "FUNCTION: Involved in DNA replication and cell separation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SDS23 family."}
{"protein": "MVLELYLDLLSQPCRAIYIFAKKNNIPFQMHTVELRKGEHLSDAFAQVNPMKKVPAMKDGGFTLCESVAILLYLAHKYKVPDHWYPQDLQARARVDEYLAWQHTTLRRSCLRTLWHKVMFPVFLGEQIRPEMLAATLADLDVNVQVLEDQFLQDKDFLVGPHISLADVVAITELMHPVGGGCPVFEGRPRLAAWYRRVEAAVGKDLFLEAHEVILKVRDCPPADPVIKQKLMPRVLTMIQ", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Also binds steroids, bilirubin, carcinogens and numerous organic anions. Has dichloromethane dehalogenase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Theta family."}
{"protein": "MGFSDVYACNPFPSAAFVTQRFFVPINLAHTQKVSWLHGHENAGLHHKTFIQHAKLLAIAQLTYRINLKTKQLQIKFCSMAALVFSLEDLESVVPEVLGVD", "text": "FUNCTION: Not required for CRPV to induce papillomas, but may facilitate the functioning of other viral or cellular factors involved in the induction of papillomas. SIMILARITY: Belongs to the papillomaviridae E5 protein family."}
{"protein": "MARFTIVLAVLFAAALVSASAHKTVVTTSVAEEGEEENQRGCEWESRQCQMRHCMQWMRSMRGQYEESFLRSAEANQGQFEHFRECCNELRDVKSHCRCEALRCMMRQMQQEYGMEQEMQQMQQMMQYLPRMCGMSYPTECRMRPIFA", "text": "FUNCTION: Seed storage protein. SIMILARITY: Belongs to the 2S seed storage albumins family."}
{"protein": "MEELELPLPTEKLAVDPGREGGKRGVAVLVATGSFNPPTYMHLRMFELAKDELQQRGYSVLGGYMSPVNDAYKKKGLLSAAHRIRLCELACESSSFVMVDRWEAMQKGFQRTLTVLSRIRNALSKDGLADGGSPNVMLLCGSDLLESFSTPGVWIPDQVRIICKDFGVICIRREGKDVEKIISSSEILNECRDNIISVDEIVPNQISSSRVRECIKKCLSIKYLVCDEVIQYIGEHKLYKEADGSDTRK", "text": "FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate. SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family."}
{"protein": "MSYPGYPPPAGGYPPAAPGGGPWGGAGYPPPSMPPIGLDNVANYAGQFNQDYLSGMAANMSGTFGGANVPNLYPGAPGGGYPPVPPGGFGQPPPAQQPVPPYGMYPPPGGNPPPGMPSYPAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPPGQQPVPSYPGYSGSSTITPAVPPAQFGNRGTITAASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLVQRDVQELYAAGENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMTGRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLYHDITGDTSGDYRKILLKICGGND", "text": "FUNCTION: Required for midbody formation and completion of the terminal phase of cytokinesis (By similarity). Binds specifically to calcyclin in a calcium-dependent manner. SUBCELLULAR LOCATION: Cytoplasm Melanosome Nucleus envelope Nucleus, nucleoplasm Cytoplasm, cytoskeleton, spindle Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus. Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. SIMILARITY: Belongs to the annexin family."}
{"protein": "MGRELQKKKNRSGNAKIKLKPKSKRVNPLGNAIIAANWRQEETLTQNYRRLGLTSRLNTVTGGIEKKKAGPESKTSTANKLAISNTIPKSLAPTEARVERDPETGKIIRVIHDEKKTNPLNDPLDSEAEDGEGEGFEGFGDEEGSASKNEIVKMLEEQASRAGEKRERQQSEREKEWIERLVKRWGENYGAMVRDRRLNPMQQTESDIKRRVQKWKDAGGSVTTEA", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP16 family."}
{"protein": "MALVVQKYGGSSLESAERIRNVAERIVATKKAGNDVVVVCSAMGDTTDELLDLAAAVNPVPPAREMDMLLTAGERISNALVAMAIESLGAEAQSFTGSQAGVLTTERHGNARIVDVTPGRVREALDEGKICIVAGFQGVNKETRDVTTLGRGGSDTTAVALAAALGADVCEIYSDVDGVYTADPRIVPNAQKLERLSFEEMLELAAVGSKILVLRSVEYARAFNVPMRVRSSYSNDPGTLIAGSMEDIPMEEAVLTGVATDKSEAKVTVLGIPDKPGEAAKVFRALADAEINIDMVLQNVSSVEDGTTDITFTCPRSDGPRAMELLKKMQQQGDWTNVLYDDQVGKVSLVGAGMKSHPGVTAEFMEALRDVNVNVELISTSEIRISVLIREDDLDKSAKALHEKFQLGGDEEATVYAGTGR", "text": "FUNCTION: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine. SIMILARITY: Belongs to the aspartokinase family."}
{"protein": "MAKTGMYVGLDIGTTSVKVVVAEYIDSQMNIIGVGNAKSEGINRGIIVDIDKTVQAIQRAVRQAEEKAGIQIKGVSVGLPANLLEVENCQGMIAVNGDSKEITDEDVRNVASAALVRSIPPERQIVSILPQDFTVDGFEGIKDPRGMIGVRLEMYGLLFTGPKTIVHNIRKCVENAGLVVNELVITPLALTETILSDGEKDFGTIVIDMGGGQTTTAVMHDKQLKFTSLDQEGGEFVTKDISIVLNTSFNNAEALKINYGDAYPERTSANEEFPVDVIGQSEPVKVDERYLSEVISARMEQIFNKAKEALDQIEALELPGGIVLTGGAASLPGVVDLAQEIFGVNVKLYVPNQMGLRNPVFTNVISIVDYSANLSEVYQLAKIAVTGETVVAHHTTVEQEVTSYDNDSYDAPEETVYDEPEQKKSDEDVTTKIKGFFSKIFD", "text": "FUNCTION: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to the membrane through a conserved C-terminal amphipathic helix. SIMILARITY: Belongs to the FtsA/MreB family."}
{"protein": "MADLEEQLSDEEKVRIAAKFIIHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNLDQFTPVKIEGYEDQVLITEHGDLGNGKFLDPKNRICFKFDHLRKEATDPRSCEVENAIESWRTSVETALRAYVKEHYPNGVCTVYGKKIDGQQTIIACIESHQFQAKNFWNGRWRSEWKFTITPSTTQVVGILKIQVHYYEDGNVQLVSHKDIQDSLTVSNEVQTAKEFIKIVEAAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA", "text": "FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (By similarity). SIMILARITY: Belongs to the F-actin-capping protein alpha subunit family."}
{"protein": "MFGSCQAYSRELVMATTFSPSATAWIIQRWQTEPGSVMIRTLNRTSGSLEQLLDTANAENVDLILTSSPMLLQHLQEHQKLALLDSAPAASQKLVPRSIRSTSVAVAVSGFGLLINRSALAARHLPPPADWQDMGLPSYQGALLMSSPSRSDTNHLMVESLLQQKGWTAGWATLLAISGNLVTISSRSFGVADKIKSGLGVAGPVIDNYANLLLNDPNLAFTYFPYSAVSPTYVAVLKNSRHADEARAFIHYLLSPKGQRILADANTGKYPVAPLSADNPRAAQQQRLMAQPPLNYRLILKRQQLVQRMFDTAISFRLAQLKDAWRALHSAETRLKRPLPEIRALLTSVPVDAASSEDETWLAQFDNKSFAEQKMMEWQIWFLNNQRLAIHKLEELK", "text": "FUNCTION: Required for pgtP expression, it may act jointly with the PgtA/PgtB signaling proteins. FUNCTION: Required for PgtP expression, it may act jointly with the PgtA/PgtB signaling proteins. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MFTIALAQLNPTIGAIAENAEKIVTAALQAQARGADLLLTPELALCGYPPKDLLLNPSFVEQLEEELQWLAEKMPPSIAILVGTVTPHHQAERQGQKKLWNSAVLIEQGQIKQWFHKCLLPTYDVFDEDRYFASAAKSEYFIYKNVKIGVTICEDLWNDEAFWGQKFYQVNPLMDLIDQGVNLVVNLSASPYSCGKHYLRESLISHSAKRFNVPLIYVNQVGGNDDLIFDGGSFAVNSQGKIIGRSPLFQEDLALLSYDLSSGELTGQKLASLPMVDTEELWQALVLGVGDYLHKCGFSKAILGLSGGIDSSLVAAIAVEALGKENVLGILMPSPYSSDHSIQDALALAKNLGMNTQTIPIGPIMATYDQALVPLFQDAPFGLAEENLQSRIRGNLLMAIANKFGHLLLSTGNKSELAVGYCTLYGDMNGGLAAIADVPKTQVFELCRWLNREQTIIPPSVLTKPPSAELKPGQVDTDSLPPYDVLDGILGRLVEKHQSPQEIINAGFEREVVLKICQLVQKSEFKRRQAAPGLKVTDRAFGSGWRMPIAQAFHPQGS", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. SIMILARITY: In the C-terminal section; belongs to the NAD synthetase family."}
{"protein": "MICRSLLLLRSNAASKASNIVKHVAATGCLPKYSSEAPARYFSSEPSLQVDSTEENGFKGHGMLAPFTAGWQSTDLHPLVIDRSEGSYVYDINGKKYIDALAGLWSTALGGNEPRLIKAATDQLNKLPFYHSFWNRTTKPSLDLANEILSMFTAREMGKIFFTNSGSEANDSQVKLVWYYNNALGRPNKKKFIARSKSYHGSTLVSASLSGLPALHQKFDLPAPFVLHTDCPHYWRFHLPDETEEEFATRLATNLENLILKEGPETIAAFIAEPVMGAGGVIPPPKTYFEKIQAVLKKYDILLIADEVITAFGRLGTMFGCDMYDIKPDLVSIAKALSSAYMPIGAILVSPEITDVIYSQSNKLGSFAHGFTYSGHPVSCAVAIEALKIYKERNIIEHVQKIAPRFQEGIKAFSGSPIVGEIRGLGLILGTEFVDNKSPNDPFPAEWGVGSLFGAECEKRGMLIRVAGDNIMLSPPLIMTPDEVEEIICKYGDALKATEERIAELKAKRG", "text": "FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MFVESAKKALLALSLLAASAQAVPRVRRQGASSSFDYKSQIVRGVNLGGWLVTEPWITPSLYDSTGGGAVDEWTLCQILGKDEAQAKLSSHWSSFITQSDFDRMAQAGLNHVRIPIGYWAVAPIDGEPYVSGQIDYLDQAVTWARAAGLKVLVDLHGAPGSQNGFDNSGHRGPIQWQQGDTVNQTMTAFDALARRYAQSDTVTAIEAVNEPNIPGGVNEDGLKNYYYGALADVQRLNPSTTLFMSDGFQPVESWNGFMQGSNVVMDTHHYQVFDTGLLSMSIDDHVKTACSLATQHTMQSDKPVVVGEWTGALTDCAKYLNGVGNAARYDGTYMSTTKYGDCTGKSTGSVADFSADEKANTRRYIEAQLEAYEMKSGWLFWTWKTEGAPGWDMQDLLANQLFPTSPTDRQYPHQCS", "text": "FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MAYDEVREVDPEVADALTGERHRQNDTLAMIASENHVSEAVMEAQSSELTNKYAEGYPGSRYYGGCEYADDVEELAVARAKELFGADHVNVQPHSGSSANMGVYFATLAPGDKILSLDLTHGGHLSHGHPANFAGQLYEVEQYEVDAETGRLDYEALREHADAFEPDMIVSGFSAYPREVEWERIQAAADAVGALHMADIAHITGLVAAGEHASPVGVADFVTGSTHKTIRAGRGGIVMCDEAFADDIDSAVFPGAQGGPLMHNIAGKAVGFNEALDPAFEEYAAQVVENAAVLGERLQEHGFSLVSGGTDTHLVLVDLRESHPDISGGDVEGELEDVGIVLNANTVPDETRSAFDPSGIRIGTPALTTRGFDADAMETVADCIARVIDNLGDESVYADVADTVADLCEQYPQYE", "text": "FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. Also exhibits THF-independent aldolase activity toward beta- hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family."}
{"protein": "MTQQITLIKDKILSDNYFTLHNITYDLTRKDGEVIRHKREVYDRGNGATILLYNTKKKTVVLIRQFRVATWVNGNESGQLIESCAGLLDNDEPEVCIRKEAIEETGYEVGEVRKLFELYMSPGGVTELIHFFIAEYSDNQRANAGGGVEDEDIEVLELPFSQALEMIKTGEIRDGKTVLLLNYLQTSHLMD", "text": "FUNCTION: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP- mannose as its preferred substrate, yielding GMP and mannose-1- phosphate. FUNCTION: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP- mannose as its preferred substrate, yielding GMP and mannose-1- phosphate. Can also hydrolyze the pyrophosphate bond of other sugar nucleotides such as IDP-ribose, GDP-glucose, and to a lesser extent, ADP-ribose, ADP-glucose and UDP-glucose. Shows no activity toward Nudix substrates FAD, CDP-ethanolamine, CDP-choline, NAD(+), diadenosine pentaphosphate, GTP, UTP, ATP, or CTP. SIMILARITY: Belongs to the Nudix hydrolase family. NudK subfamily."}
{"protein": "MDQGYGGYGAWSAGPANTQGAYGTGVASWQGYENYNYYGAQNTSVTTGATYSYGPASWEAAKANDGGLAAGAPAMHMASYGPEPCTDNSDSLIAKINQRLDMMSKEGGRGGSGGGGEGIQDRESSFRFQPFESYDSRPCLPEHNPYRPSYSYDYEFDLGSDRNGSFGGQYSECRDPARERGSLDGFMRGRGQGRFQDRSNPGTFMRSDPFVPPAASSEPLSTPWNELNYVGGRGLGGPSPSRPPPSLFSQSMAPDYGVMGMQGAGGYDSTMPYGCGRSQPRMRDRDRPKRRGFDRFGPDGTGRKRKQFQLYEEPDTKLARVDSEGDFSENDDAAGDFRSGDEEFKGEDELCDSGRQRGEKEDEDEDVKKRREKQRRRDRTRDRAADRIQFACSVCKFRSFDDEEIQKHLQSKFHKETLRFISTKLPDKTVEFLQEYIVNRNKKIEKRRQELMEKETAKPKPDPFKGIGQEHFFKKIEAAHCLACDMLIPAQPQLLQRHLHSVDHNHNRRLAAEQFKKTSLHVAKSVLNNRHIVKMLEKYLKGEDPFTSETVDPEMEGDDNLGGEDKKETPEEVAADVLAEVITAAVRAVDGEGAPAPESSGEPAEDEGPTDTAEAGSDPQAEQLLEEQVPCGTAHEKGVPKARSEAAEAGNGAETMAAEAESAQTRVAPAPAAADAEVEQTDAESKDAVPTE", "text": "FUNCTION: Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II) (PubMed:9473338). Acts as an anchor for a PKA-signaling complex onto mitotic chromosomes, which is required for maintenance of chromosomes in a condensed form throughout mitosis. Recruits condensin complex subunit NCAPD2 to chromosomes required for chromatin condensation; the function appears to be independent from PKA-anchoring (PubMed:10601332, PubMed:10791967, PubMed:11964380). May help to deliver cyclin D/E to CDK4 to facilitate cell cycle progression (PubMed:14641107). Required for cell cycle G2/M transition and histone deacetylation during mitosis. In mitotic cells recruits HDAC3 to the vicinity of chromatin leading to deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3; in this function may act redundantly with AKAP8L (PubMed:16980585). Involved in nuclear retention of RPS6KA1 upon ERK activation thus inducing cell proliferation (PubMed:22130794). May be involved in regulation of DNA replication by acting as scaffold for MCM2 (PubMed:12740381). Enhances HMT activity of the KMT2 family MLL4/WBP7 complex and is involved in transcriptional regulation. In a teratocarcinoma cell line is involved in retinoic acid-mediated induction of developmental genes implicating H3 'Lys-4' methylation (PubMed:23995757). May be involved in recruitment of active CASP3 to the nucleus in apoptotic cells (PubMed:16227597). May act as a carrier protein of GJA1 for its transport to the nucleus (PubMed:26880274). May play a repressive role in the regulation of rDNA transcription. Preferentially binds GC-rich DNA in vitro. In cells, associates with ribosomal RNA (rRNA) chromatin, preferentially with rRNA promoter and transcribed regions (PubMed:26683827). Involved in modulation of Toll- like receptor signaling. Required for the cAMP-dependent suppression of TNF-alpha in early stages of LPS-induced macrophage activation; the function probably implicates targeting of PKA to NFKB1 (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus matrix Nucleus, nucleolus Cytoplasm Note=Associated with the nuclear matrix in interphase and redistributes mostly to chromatin at mitosis. However, mitotic chromatin localization has been questioned. Upon nuclear reassembly at the end of mitosis, is sequestered into the daughter nuclei where it re-acquires an interphase distribution. Exhibits partial localization to the nucleolus in interphase, where it colocalizes with UBTF/UBF, suggesting localization to the fibrillary center and/or to the dense fibrillary component. Colocalizes with GJA1 at the nuclear membrane specifically during cell cycle G1/S phase. SIMILARITY: Belongs to the AKAP95 family."}
{"protein": "MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPVASWLCAMLHCFGSYILADLLLGEPLIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFIMIATGWVKGSGVALLSNVEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVLEAYVCPVLFGTGSGGDHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD", "text": "FUNCTION: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Multi-pass membrane protein Nucleus membrane. SIMILARITY: Belongs to the TMEM38 family."}
{"protein": "MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV", "text": "FUNCTION: Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney. Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein Note=CLDN4 is required for tight junction localization in the kidney. SIMILARITY: Belongs to the claudin family."}
{"protein": "MLTGVTDGIFCCLLGTPPNAVGPLESVESSDGYTFVEVKPGRVLRVKHAGPAPAAAPPPPSSASSDAAQGDLSGLVRCQRRITVYRNGRLLVENLGRAPRADLLHGQNGSGEPPAALEVELADPAGSDGRLAPGSAGSGSGSGSGGRRRRARRPKRTIHIDCEKRITSCKGAQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGPTALEPSFCSIFNMPTCVLHCLSPCLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFVLRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNTLLHEFLLWEPEPSPKALPEPLPAPPEDKK", "text": "SIMILARITY: Belongs to the AB hydrolase superfamily."}
{"protein": "MLSVDYENFDLISYLYNLVRQIPDGMVSTYGDLAEALGDPVAARSVGFMLSINKEPDYIPCYKVVPHDGSVGNYTHPLGSAEKMRRLIRDGITITNGHISNFEKVRFREFKTDYPLRKLRELQFKIGRLYDDRNDYSLDTIAAFDVSYKETRGYASKVVYNKGKIGAYVYSSDSMFPYIPGYLAFKEFKFIRALYDNETMILIDGNGILHPRFAGLATHAGVSLKTASIGIAKHLINCTVKGSDLLISGVVAGKMIGHHTIVSPGNRINVEEAGRLIEQREGKEMRSLLRLAHNLTRLHIETNGNIARYDFSTRNTAIQSS", "text": "FUNCTION: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the endonuclease V family. SIMILARITY: In the N-terminal section; belongs to the MGMT family."}
{"protein": "MLFRSVMNKPRLGYGQKGAPFTYPLQSLLQCYQCVKQDEHISYGELGMPVPPFGCAFSTVPDMSHVLAVANEEGIVRLYDTECRDMQRLLMKEFMAHTNAVFDIAWVPGEHKLVTASGDQTAKLWDVMAGELIGECRGHQCSLKSVSFSKFERAVFSTGGRDGNIMMWDTRCSKKDGFYRQVNQITGAHNAIDKQTPSKMKKRKPSIRGLAPSVDSQQSVTVVIFQDEYTIISAGAVDGVVKIWDLRKNYSAYRQDPVPVKHFPYPGNSTRKLGYSSLVLDPTGTNLFASCTDDNVYMFNATGLKTDPVSIFRGHQNSTFYIKASVSPDGQFLLSGSSDHSAYIWQVSDPMAAPVTLMGHCQEVTSVAWCQSDFTKIATCSDDNTVRVWRLKRSCEDSSESDKRDSVGWACKKKFEPSSMAANLCTPGKPSVMSSSSLTSSPTPASCAPSNTGDLPMPSSTPISALLPDPKLQTPKRINNGGLGVSPKQMSSSKMSIKDWVTRTPKSSTRTDTKTPSPRKAFTPVEQYPSVSSARVQLPYEKRAKRRLETSSEYAEHVCPDNCNCVRELEPGLKKAKLDVCFIDKERDSSDDKCLRLSDLSKGFDQELSPSPSTSLHMNATENLLQLGPLSELKSVLLDKENSSPEKNWLSALGHKFKSSPQNKASGSPSSRTSTTKKQQPRNAPNSPVSVPTPPGSMRKICTYFFKKSE", "text": "FUNCTION: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), KMT5A and SDE2. CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis. May play a role in the regulation of the circadian clock (By similarity) (PubMed:19595719). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome. SIMILARITY: Belongs to the WD repeat cdt2 family."}
{"protein": "MAFLRSFLGAKQIIRRESSSTPRGFMAVYVGENDQKKKRYVVPVSYLNQPLFQQLLSKSEEEFGYDHPMGGLTIPCHESLFFTVTSQIQ", "text": "FUNCTION: Functions as a positive effector of cell expansion through modulation of auxin transport. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ARG7 family."}
{"protein": "MSVTHGKMGLSLTQEILSHLGLANKTAAWGTLGTLRTFLSFSADKDVQRLLKAIAGQGVDRIAILDVLTNRSREQRQLISRAFHERTQQDLLKSLQAALSGNLERIVVALLQPAAHLDARELRTALKGSGSAEDVALEILATRTPPQLQECLAVYKHNFQVDAAEDIKSETRGILRDLLLALAKGGREAYTGIIDYNLAAQDVQALKQAEGPSTERTWVLVFTQRNPEHLVRVLNQYQWYTGHGLEKTVRARFHGAACVALLNLASVIRNTPLYFADKLHQALQETEPNYQALMRILISRSETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCRSALLALCRAEDL", "text": "FUNCTION: May act as a low affinity receptor for acetylcholine. SIMILARITY: Belongs to the annexin family."}
{"protein": "MTYAAEDFDYEGLPIGSPMYAHLLAGAFSGILEHSVMYPVDAIKTRMQMLNGVSRSVSGNIVNSVIKISSTEGVYSLWRGISSVIMGAGPSHAIYFSVLEFFKSKINASPDRPLASALAGACAITISDAFMTPFDVIKQRMQLPSRKYKSALHCATTVFRNEGLGAFYISYPTCIAMSIPFTAIQVATYDTCMSFLNPNAVYDPTSHIISGGLSGAIASSLTTPLDVVKTLLQTRGSSSIPEVRKCKGSLDVVRFIYNYGGIPSFFKGIRPRMVVAMPATAVSWAAYEAGKEILIRVSKTSQA", "text": "SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MAPSHLSVREVREDEKPLVLEMLKAGVKDTENRVALHALTRPPALLLLAAASSGLRFVLASFALALLLPVFLAVTAVKLGLRARWGSLPPPGGLGGPWVAVRGSGDVCGVLALAPGTNAGDGARVTRLSVSRWHRRRGVGRRLLAFAEARARAWAGGMGEPRARLVVPVAVAAWGVAGMLEGCGYQAEGGWGCLGYTLVREFSKDL", "text": "FUNCTION: Probable acetyltransferase. FUNCTION: May act as a transcription factor regulating the expression of coproporphyrinogen oxidase by binding to a promoter regulatory element. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the camello family."}
{"protein": "MNEILKILNNIRTLRVHSRECSLEILEEILEKFKVVINERKKEEKKIKEEIAQRAIKLKKYREMLIADGINPNELLTKTNSIKSSEKRKRPKRPAKYKYINKNGDFKTWTGQGRTPSVIKNAILERKKILEDFLL", "text": "FUNCTION: A DNA-binding protein implicated in transcriptional repression and chromosome organization and compaction. Binds nucleation sites in AT-rich DNA and bridges them, forming higher-order nucleoprotein complexes and condensing the chromosome. A subset of genes are repressed by H-NS in association with other proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the histone-like protein H-NS family."}
{"protein": "MSLSKKLTLDKLDVRGKRVIMRVDFNVPMKKNQITNNQRIKASIPSIKYCLDNGAKAVVLMSHLGRPDGVPMPDKYSLQPVAAELKSLLGKDVLFLKDCVGAEVENACANPAPGSVILLENLRFHVEEEGKGQDPSGKKIKAEPDKIEGFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPHKASGFLMKKELDYFAKALENPVRPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAYTFLKVLNNMEIGASLFDEEGAKIVKDIMTKAQKNGVRITFPVDFVTADKFDENAQVGKATVASGIPPGWMGLDCGPESNKNHAQVVAQARLIVWNGPLGVFEWDAFAKGTKALMDEIVKATSKGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKILPGVEALSNM", "text": "FUNCTION: Essential for sperm motility and male fertility but is not required for the completion of spermatogenesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MAAFRTTAWRLISGVLGVICLVLMAALGVLLKNSLTKRSVQPGPSADLQEEYNLHEEEESCLGCLGSGCYSCQEKWIGYQCNCYFISNELKTWKDGRDFCVSHNSSLLQIQTRNEPAFMKFSTSFYWIGLSYDEEHHAWLWEDNSTLSQDLLPFFKSVNPKNCIMYNPRGRILDAYCEKKFRYICKQQLI", "text": "FUNCTION: Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule MHC-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal. FUNCTION: KLRD1-KLRC2 acts as an immune activating receptor. On cytotoxic lymphocyte subsets recognizes MHC-E loaded with signal sequence-derived peptides from non-classical MHC class Ib MHC-G molecules, likely playing a role in the generation and effector functions of adaptive NK cells and in maternal-fetal tolerance during pregnancy. Regulates the effector functions of terminally differentiated cytotoxic lymphocyte subsets, and in particular may play a role in adaptive NK cell response to viral infection. Upon MHC-E- peptide binding, transmits intracellular signals via the adapter protein TYROBP/DAP12, triggering the phosphorylation of proximal signaling molecules and cell activation. FUNCTION: KLRD1-KLRC1 acts as an immune inhibitory receptor. Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions. Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity. On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens. In MHC-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion. Upon MHC-E- peptide binding, transmits intracellular signals through KLRC1 immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHIP-1 and INPPL1/SHIP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
{"protein": "MLYGFSGVILQGALVTLELAISSVVLAVIIGLIGAGGKLSQNRLSGLIFEGYTTLIRGVPDLVLMLLIFYGLQIALNTVTEAMGVGQIDIDPMVAGIITLGFIYGAYFTETFRGAFMAVPKGHIEAATAFGFTRGQVFRRIMFPSMMRYALPGIGNNWQVILKSTALVSLLGLEDVVKATQLAGKSTWEPFYFAIVCGVIYLVFTTVSNGVLLFLERRYSVGVKRADL", "text": "FUNCTION: Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Probably responsible for the translocation of the substrate across the membrane. Required to relay the ATPase-inducing signal from the solute-binding protein to HisP (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily."}
{"protein": "MEDDGKSSPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVYARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWFGISFDKFGRTSTPEQTEVCQAIFNKLWDNKWLSENTMQQLYCDTCKKFLADRLVEGSCPFEGCNYDSARGDQCEKCGKLLNPTELKDPKCKVCQNTPRIRDTDHLFIELPLLKDRLEAYIKKTSVTGSWSQNAIQTTNAWLRDGLRQRCITRDLKWGVPVPHEKYKDKVFYVWFDAPIGYVSITSCYTSEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTQLGTEENWTLMKTISVTEYLNYEDGKFSKSKGVGVFGNDVKDTNIPVEVWRYYLLTNRPEVSDTSFSWTDLQAKLNGELLSNLGNFVNRVLSFIAKPDNAGYGSVIPDAHDAESHSLTKSLAEKVEKFVAEYVEAMEKVKLKQGLKTAMLISSEGNYYLQASQFWKLYKEDKPLCAVVIRTAAGLVHLLAQLLEPFMPSFSCEVFKQLNLPPQFSLSDERGEVLLASRPWDILPPSHRIGTPQPLFKELENDEVARYREKFAGSQSDRRARDEAANLADQLNKTKLSDAKKQKASSKGGGKPKPQPAADREITMARLDIRVGKIVKAEKHPKADALYVEEIDVGGGEIRTVVSGLVKYIPLEEMQNRMVCVLCNLKPAKMRDIVSQAMVLAASSSDGSKVELVEPPKTANIGERVTFPGFEGEPDDVLNPKKKVWETLLVDLNTKENLVACYKDVPFTTSAGVCKVSSISNGTIR", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MTAEPTVAARPQQIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKALAARTDTRPEALLRLIRHLVAIGLLEEDAPGEFAPTEVGKLLADDHPAAQRAWHDLTQAVARADISFTRLPEAIRSGRPTYESVYGKPFYEDLAGRPDLRASFDSLLACDQDVAFDAPAAAHDWTNVRHVLDVGGGKGGFAAAIARRAPHVSATVLEMAGTVDTARSYLRDAGLSDRVDVVEGDFFEPLPRRADAIILSFVLLNWPDHDAVRILTRCAEALEPGGRILIHERDDLHENSFNEQFTELDLRMLVFLGGALRTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPASTGA", "text": "FUNCTION: Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 4-O- position of carminomycin to form daunorubicin. In vitro, it also methylates the anthracyclines rhodomycin D (10-carbomethoxy-13- deoxycarminomycin), 10-carboxy-13-deoxycarminomycin, 13-deoxy- carminomycin and 13-dihydrocarminomycin at the 4-hydroxyl position. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family."}
{"protein": "MLSFQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCNFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVCLDPNTLSDDGTVALRGYAFSEDGEYVAYGLSASGSDWVTIKFMKVDGAKELADVLERVKFSCMAWTHDGKGMFYNAYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIREGCDPVNRLWYCDLHQEPNGITGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRHSPNYRLINIDFTDPEESRWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNTLQLHDMATGALLKTFPLEVGSVVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVCRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVATCANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYGCSDNKQHFEWLIKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSPKFIATLQHLVGRSRKQNNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIDWIQ", "text": "FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S9A family."}
{"protein": "MELSITTSIALATIVFFLYKLATRPKSTKKQLPEASRLPIIGHMHHLIGTMPHRGVMDLARKHGSLMHLQLGEVSTIVVSSPKWAKEILTTYDITFANRPETLTGEIIAYHNTDIVLAPYGEYWRQLRKLCTLELLSVKKVKSFQSIREEECWNLVKEVKESGSGKPINLSESIFTMIATILSRAAFGKGIKDQREFTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSIHKKLDNLINNIVAEHHVSTSSKANETLLDVLLRLKDSAEFPLTADNVKAIILDMFGAGTDTSSATVEWAISELIRCPRAMEKVQAELRQALNGKEKIQEEDIQDLAYLNLVIRETLRLHPPLPLVMPRECREPVNLAGYEIANKTKLIVNVFAINRDPEYWKDAEAFIPERFENNPNNIMGADYEYLPFGAGRRMCPGAALGLANVQLPLANILYHFNWKLPNGASHDQLDMTESFGATVQRKTELLLVPSF", "text": "FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:20351109). Catalyzes three consecutive oxidations of germacrene A to produce germacrene A acid (PubMed:20351109). Could also catalyze the three-step oxidation of non- natural substrate amorphadiene to artemisinic acid (PubMed:20351109). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MHGNGGQPAAGGSESALSREGQPGPSGAAQGQVISNERSPRRYSTRTINGVQATNKFTAVGNPSLQRDPDWYRWNYNHSIAVWLRECSRSHAKICNCGQFRKHWFQECAGLEDRSTQASLEEAILRPLRVQGKRAKRKLDYHYSQPTPNRKKVYKTVRWKDELADREADFTPSEEDGGTTSSDFDEDINFDIGGDSGIVDELLGRPFTTPAPVRIV", "text": "FUNCTION: May act as a scaffold protein in virion assembly. May also play a role in intracellular signaling during viral replication (By similarity). SIMILARITY: Belongs to the gyrovirus protein VP2 family."}
{"protein": "MIKNLSTFFVGIALSCLAGCTPIPKETTATKEYAPLEVPVPERPAGQQDVIELTTPKLDTVRVGFIGLGMRGPSAVERWTHIPGTKIVALCDLLPENAEKAQKIVTNAGMEAPALYSGSEDAWKQLCERNDIDLVYIATDWKHHTEMGIYAMEHGKHAAIEVPAAMSLDEIWALINTSEKTRKHCMQLENCVYDFFELTTLNMAQKGLFGEVLHVEGSYIHNLEEFWPYYWNNWRLDYNREFRGDVYATHGLGPACQLLNIHRGDRMKTLVAMDTKAVTGPELVKQYQKEEAPDFQNGDHTMTFIRTENGKTIHIQHDVMNPRPYSRMYQLTGTKGFANKYPIEQYCFRPDQIDSTSIPDHENLSMHSAVPEKVKEALMSQYKHPIHQELEETAKKIGGHGGMDFIMDYRLVYCLRNGLPLDMDVYDLAEWCCMADLTRLSIENGNAPVAVPDFTRGNWNKVDGYHHAFAQ", "text": "FUNCTION: Glycosidase. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109 subfamily."}
{"protein": "MDVKHIKDYLSWLYYQYLLITCSYVLEPWEQSIFNTLLLTIIAMVIYSSYIFIPIHVRLAVEFFSRIFGGQHESTVALMS", "text": "FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SPTSS family. SPTSSB subfamily."}
{"protein": "MAQIRIHEVNTRIENEVEVSKFLQEEGVLYEKWNISKLPPHLNENYSLTDENKAEILAVFSKEIADVSARRGYKAHDVISLSNSTPNLDELLINFQKEHHHTDDEVRFIVSGHGIFAIEGKDGTFFDVELEPGDLISVPENARHYFTLQDDRQVVAIRIFVTTEGWVPIY", "text": "FUNCTION: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway. SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family."}
{"protein": "MTKKLHIKTWGCQMNEYDSSKMADLLDATHGYQLTDVAEEADVLLLNTCSIREKAQEKVFHQLGRWKLLKEKNPDLIIGVGGCVASQEGEHIRQRAHYVDIIFGPQTLHRLPEMINSVRGDRSPVVDISFPEIEKFDRLPEPRAEGPTAFVSIMEGCNKYCTYCVVPYTRGEEVSRPSDDILFEIAQLAAQGVREVNLLGQNVNAWRGENYDGTTGSFADLLRLVAAIDGIDRIRFTTSHPIEFTDDIIEVYRDTPELVSFLHLPVQSGSDRILNLMGRTHTALEYKAIIRKLRAARPDIQISSDFIVGFPGETTEDFEKTMKLIADVNFDMSYSFIFSARPGTPAADMVDDVPEEEKKQRLYILQERINQQAMAWSRRMLGTTQRILVEGTSRKSIMELSGRTENNRVVNFEGTPDMIGKFVDVEITDVYPNSLRGKVVRTEDEMGLRVAETPESVIARTRKENDLGVGYYQP", "text": "FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily."}
{"protein": "MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRIGPNIRLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQGSLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIQPSSREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKSPLTPEKEVGYLEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLELKNELCQLPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEECKRQMLTASHTLAVDAKNLLDAVDQAKVLANLAHPPAE", "text": "FUNCTION: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, focal adhesion. Cell projection, lamellipodium. Cytoplasm, cell cortex. Nucleus. Note=Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with integrins at the cell periphery. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily."}
{"protein": "MSSLQQPIPPNSTLATTASSNQSGSNDFVKKLFLMLQEDSYKEVVRWTVKGDSFVVINTNEFTKDILPKHFKHSNFASFVRQLNKYDFHKVKISNEAKASYPYGEDAWEFKHPEFRINDAEALENIKRKGPTAKKSASNVTIKTEANNNGTQPTCNHNYSQLVSATNHLKEQVESLKNDKHSLYQEISVLERKYKTVVENIVAINTFNERYYRSMNVLINSIVQNGMKLPPLDFPPPVQLGPDSGIGSNLGPISSDTALPSISHHLSSPLPHHQQLLNRTIRPISSPIDGIPLVKLQQQSLGQNLQAPIGTPSAVPFSEEASSSIQAATPAPLAQPVAQPINQPPPPPPPPATQQQPLPPPPPPATATSQIPSAPPPPTQQQVGTSSSSVPTISPKSQGIVVSNSASPTTSAQISTTSVPNPKFHVLLVEDDNVCIQLCRKFLVKYGCSVTVVTDGLNAISTVEHTKYDLVLMDIVMPNLDGATATSVIRSFDTKTPIIAMTGNIEDNDLVTYLQNGMSDILAKPFTKDDLYAILSKHLLDPKENKQDNEPTVKKQKLS", "text": "FUNCTION: Transcription factor that is part of a SLN1-YPD1-SKN7 two- component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in response to oxidative stress, independent on the two-component regulatory system. Regulates heat shock genes in response to oxidative stress and genes involved in cell wall integrity in response to osmotic changes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SKN7 family."}
{"protein": "MKFIIVLLLFFFFKVIDRVICVTPQKLICLKEDVYLGDFFFFLKRKKYIMYDVNIGEGFNLQKEIFYRLSLVIYNLNKKDKINIYYLVLPPWCYVTHWNIRKGNNLRWEFFFNTDIMKKVIPIIEYEEYEKLYGNYSDIMINSKYILDNYKEKSFLILPFEECNINVNRFKQFCKKCEHKYNVLYSGYCTTINTKQSECYSYNMISNYFITSILENLFLYNITSVLIKQSTNILVPFVNELYQSNLEDILLFNNKLLSYGNNYISNILKTNHYISSHLRYTDFKYISRYNVPPIHIALLKLLYIMFINNCRIIFIASDEKVEIQKVINKDFHQYKKHFYFYNNQNNLHEGEFSIIEQWICTRSYIFIGNIFSRFTMNINWERHLINKGQINQNIDLCSYHINDDNDQDIKNSYKKIVHIFNHKALQKIKNIYDNYSDRDKKYINTICYNFLSHFPNNRSIYRKEYITNT", "text": "FUNCTION: Catalyzes the reaction that attaches fucose through an O- glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively (By similarity). O-fucosylates sporozoite proteins CSP and TRAP (By similarity). O-fucosylation regulates stability and intracellular trafficking of TRAP but not of CSP (PubMed:28916755). Probably by regulating protein O-fucosylation, may play a role in parasite transmission to the mosquito vector and/or infection of the vertebrate host hepatocytes; however, POFUT2 involvement in transmission/infection is controversial (PubMed:28916755, PubMed:31334132). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 68 family."}
{"protein": "MKKWIVLFLVLIAAAISIFVYVSTGSEKPFYNDINLTQYQKEVDSKKPKFIYVYETSCPPCQEIKPELNEVIKKEKLKVQALNIEEKENYNTEFLDKYNLNKTPTILYYKDGKEKDRLEGYRSASQIEKFFDKNGDR", "text": "FUNCTION: Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the thioredoxin family."}
{"protein": "MVERMKKDTGDETKTKVQEEPPSPSPPPPPPPRRERQKQHYWVPEREKKQIERHIHRTSHAREFTDKPWRQPRLFSETTLPKIVLEEESIPQAQKRRQAHERELLQIKDHRERMIRGRELLQQRLKDRILRKSPSQIPLPEKRDQVKKQKKEFEKVVAYPLVQPSCTSRIKVDVLMEKSQDEEDLSTIIKPFGRRFLAVPPFLRTQIGKIKDL", "text": "FUNCTION: May be involved in male sterility."}
{"protein": "MSASKFIKCVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSANVAVDGQIVNLGLWDTAGQEDYSRLRPLSYRGADIFVLAFSLISKASYENVLKKWMPELRRFAPNVPIVLVGTKLDLRDDKGYLADHTNVITSTQGEELRKQIGAAAYIECSSKTQQNVKAVFDTAIKVVLQPPRRKEVPRRRKNHRRSGCSIASIVCGGCTAA", "text": "FUNCTION: Acts as a negative regulator of abscisic acid (ABA) responses. SUBCELLULAR LOCATION: Membrane; Lipid- anchor. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MIIGYVVGSATTQEANVLLEKKVRSGYYVTLEYDDEKVLGLVTLITTGSPLVDDSLNDIELVQRIKQMGNKIPIYMKAKVKLLCKLDGKLSQPDLPPVAGTPVRLATNEELSTIFSEGTIRIGKLIGSDVEVRIRVNALTRHLAILAATGSGKSNTVAVLSSRLSEVFGSVLIFDYHGEYYESEIKNLNNIEPKINPLNLTPDEFATLLEIRENATIQYRILRRAFKSFLEETKEKLKNGNVNYNELNNNFRNLILKKVDEVSKNEKRKDSKDEVINKIEDFLDRYSEIIDFTAGDVVDKIKIGKVNVINLSSLDEDAIDAIVSHYLRKILTSRKENKMKRKIGLKFPVLVVIEEAHVLLSKDSNTLTKHWAGRIAREGRKFGVGLIIVSQRPKGIDENILSQMTNKIILKMVEPSDKKYVLETSDNLSEDIVEGLSALDTGEAVIVGNIVRMPAIVKIDKFEGKLAGSDPNLIEEWKKAKEEIEEHADVLNWGE", "text": "FUNCTION: Involved in DNA double-strand break (DSB) repair (PubMed:18243819). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (PubMed:18243819). Loads on either a 3' or a 5' DNA tail for subsequent DNA unwinding (PubMed:18243819). Can also unwind blunt-ended dsDNA, Holliday junction and splayed-arm DNA (PubMed:18243819). SIMILARITY: Belongs to the HerA family."}
{"protein": "MTSSYMRLKAAAIAFGVIVATAAVPSPASGREHDGGYAALIRRASYGVPHITADDFGSLGFGVGYVQAEDNICVIAESVVTANGERSRWFGATGPDDADVRTTSSTQAIDDRVAERLLEGPRDGVRAPCDDVRDQMRGFVAGYNHFLRRTGVHRLTDPACRGKAWVRPLSEIDLWRTSWDSMVRAGSGALLDGIVAATPPTAAGPASAPEAPDAAAIAAALDGTSAGIGSNAYGLGAQATVNGSGMVLANPHFPWQGAERFYRMHLKVPGRYDVEGAALIGDPIIEIGHNRTVAWSHTVSTARRFVWHRLSLVPGDPTSYYVDGRPERMRARTVTVQTGSGPVSRTFHDTRYGPVAVVPGTFDWTPATAYAITDVNAGNNRAFDGWLRMGQAKDVRALKAVLDRHQFLPWVNVIAADARGEALYGDHSVVPRVTGALAAACIPAPFQPLYASSGQAVLDGSRSDCALGADPDAAVPGILGPASLPVRFRDDYVTNSNDSHWLASPAAPLEGFPRILGNERTPRSLRTRLGLDQIQQRLAGTDGLPGKGFTTARLWQVMFGNRMHGAELVRDDLVALCRRQPTATASNGAIVDLTAACTALSRFDERADLDSRGAHLFTEFLAGGIRFADTFEVTDPVRTPAPFWNTTDPRVRTALADACNGSPASPSTRSVGDIHTDSRGERRIPIHGGRGEAGTFNVITNPLVPGVGYPQVVHGTSFVMAVELGPHGPSGRQILTYAQSTNPNSPWYADQTVLYSRKGWDTIKYTEAQIAADPNLRVYRVAQRGR", "text": "FUNCTION: Catalyzes the hydrolysis of the palmitoyl moiety of the antifungal antibiotic, aculeacin-A, giving a hexapeptide moiety and a long chain fatty acid. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S45 family."}
{"protein": "MAMETQDIIKRSATNSITPPSQVRDYKAEVAKLIDVSTCIGCKACQVACSEWNDIRDEVGHCVGVYDNPADLSAKSWTVMRFSETEQNGKLEWLIRKDGCMHCEDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFNIPRLNKEDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIHFGTKKEMLELAEQRVAKLKARGYEHAGVYNPEGVGGTHVMYVLHHADQPELYHGLPKDPKIDTSVSLWKGALKPLAAAGFIATFAGLIFHYIGIGPNKEVDDDEEDHHE", "text": "FUNCTION: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). FUNCTION: Formate dehydrogenase allows the bacterium to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar) (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein."}
{"protein": "MKFAVAIAFTLLVCVFAQEEEEPVTCGGKQCKPNSCCVQNSHGKGKDSPRCHPLGKLNNPCEVEPNENGIYSQHCPCGEGLSCTKVGEPNKLRCQEESGKSDKSKESQGSDESEESEGSKESSG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 32 family."}
{"protein": "MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLRSNTYDLQESNVGLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKSDAISKSELTKFKIKITSELVNNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMKARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHSRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKN", "text": "FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore Cleavage furrow Midbody Cell projection, cilium, flagellum Note=In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle. Found in the sperm annulus (By similarity). SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
{"protein": "MAWFDDTYYFEQAQLRIAHITDCHLFSDKQGEYFGVNTAEHFTRALTDIAKQQPDALIFGGDLTQDHSFNSYLLFAELIHNSDLDCPVFWVPGNHDEIDQLNLISGGQIQRAKHIVAQGFELILINSKGNTPAGWVTPSHLEEIMACLVDSDNRHIAFCHHNPLPINGYLDKHMLENGPQLLNLLVNNGRVDALFHGHVHNDYQQQFRELDIYATPASSVQFTKHSATWQQEDKGAAYRMLHLNAEQQKVHIRTDVVWLNE", "text": "SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class- III family."}
{"protein": "MIEVLLVTICFTVFPYQGSSIILESGNVNDYEVVYPQKVPALPKGGVQNPQPETKYEDTMQYEFHVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAAISACDGLKGHFKHRGETYFIEPLKLSNSESHAIYKDEHVEKEDEIPKICGVTQTTSESDEPIEKISQLTNTPEQDRYLQVKKYIELYVVVDNRMYRNYNSNRDAINERVYEMVNTLNVMYRPLNFFIALIGLEIWSNQDEINIEPEVAVTLRSFGEWRNTTLLPRKRNDNAQLLTGIDFNGATVGLAYVGTLCSPTQSVAVIQDHSKRTSMVASTMAHELGHNLGINHDSASCNCNAGPCIMSATISNQPFSKFSSCSVQEHQRYLLRVRPQCILNKPLSTDIVTPPVCGNYFVERGEECDCGSPQDCQSACCNATTCKPQHEAQCDSGECCEKCKFKKAGAECRAAKDDCDLPESCTGQSAKCPTDSFQRNGHPCQNNEGYCYNGKCPIMTNQCIALGGPGVNVSPDECFTLKQNVPECGFCRIENGRKIPCAEKDKMCGKLLCEKGNATCICFPTTHDPDYGMVEPGTKCGDGKVCINRQCVDVQTAY", "text": "FUNCTION: Snake venom zinc metalloproteinase that may impair hemostasis in the prey. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily."}
{"protein": "MDEKELIERAGGPVTRGRLVRDLEALGVGAGDTVMVHTRMSAIGYVVGGPQTVIDAVRDAVGADGTLMAYCGWNDAPPYDLAEWPPAWREAARAEWPAYDPLLSEADRGNGRVPEALRHQPGAVRSRHPDASFVAVGPAAHPLMDDHPWDDPHGPDSPLARLAGAGGRVLLLGAPLDTLTLLHHAEARAEAPGKRFVAYEQPVTVGGRRVWRRFRDVDTSRGVPYGRVVPEGVVPFTVIAQDMLAAGIGRTGRVAAAPVHLFEAADVVRFGVEWIESRMGGAAGGA", "text": "FUNCTION: Resistance to neomycin. SIMILARITY: Belongs to the antibiotic N-acetyltransferase family."}
{"protein": "MGMVSSQATPVEAYKVQQVQINDQTVEQLVRVQTSAGTTVTTIDAATAERLVKLREEDLIKFSAQGMSQAQMMAKPGMTSPRPIELCAVCGDKASGRHYGAISCEGCKGFFKRSIRKHLGYTCRGNKDCQIIKHNRNRCQYCRLQKCLDMGMKSDSVQCERSPLKTRDKTPGNCAASTDKIYIRKDIRSPLTATPTFVTGSVLAGGDMKSPQGNRQGLFDQGILLNVQTTPTSSPSASTSDSTTDLSTLASVVTSLANMNKKTEEGPSHSQQIYSPSQTLQIISNGDQDVQGGGDNVSKAFDALTKALNTSGDSEAGDLSIDQSANGGSSEVELVKLDSPMLSDHHMQFKLTTPSPMPQFLNVHYICESASRLLFLSMHWARSLPAFQVLSADTHTSMVQKCWSELFTLGLAQCAQAMALSTILTAIVNHLQTSLQQDKLSADRVKAVMEHIWKLQEFVTTTSKLDVDQTEFAYLKTIVLFSPDHPGLSNVRQIEKFQEMAISELHDYEAQTYPSKLNRFSKLLLRLPTLRLLSPAIMEELFFAGLIGNVQIDSIIPYILRMETADYNSAQITMSASPGSLIG", "text": "FUNCTION: Orphan nuclear receptor. Binds to the hormone response element in the upstream promoter region of the CYIIIB gene in vitro. Both isoform 1 and isoform 2 bind DNA. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The subcellular location of isoform 1 alters throughout development. In the unfertilized egg, isoform 1 expression is cytoplasmic and concentrated around the pronucleus. Following fertilization, the cytoplasmic protein rapidly enters the embryonic nuclei where it appears as speckles. From the fourth cleavage stage onwards it resides as speckles in the cytoplasm and the nucleus. The cytoplasmic localization also differs between cells, maintaining an apical position in polarized ectodermal and endodermal cells, whereas in non-polarized cells the cytoplasmic distribution is uniform. In contrast, isoform 2 resides in the nucleus in both 4-cell and 16-cell embryos. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily."}
{"protein": "MLKPSIICLFLGILAKSSAGQFYFPNEAAQVPNYGRCITPNRERALCIHLEDCKYLYGLLTTTPLRDTDRLYLSRSQCGYTNGKVLICCPDRYRESSSETTPPPKPNVTSNSLLPLPGQCGNILSNRIYGGMKTKIDEFPWMALIEYTKSQGKKGHHCGGSLISTRYVITASHCVNGKALPTDWRLSGVRLGEWDTNTNPDCEVDVRGMKDCAPPHLDVPVERTIPHPDYIPASKNQVNDIALLRLAQQVEYTDFVRPICLPLDVNLRSATFDGITMDVAGWGKTEQLSASNLKLKAAVEGSRMDECQNVYSSQDILLEDTQMCAGGKEGVDSCRGDSGGPLIGLDTNKVNTYYFLAGVVSFGPTPCGLAGWPGVYTLVGKYVDWIQNTIES", "text": "FUNCTION: Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo (PubMed:9477324, PubMed:2107028, PubMed:12493753). Three proteases; ndl, gd and snk process easter to create active easter (PubMed:9477324). Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo (PubMed:9477324). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily."}
{"protein": "MSRRLRRTKIVTTLGPATDRDNNLEKVIAAGANVVRMNFSHGSPEDHKMRADKVREIAAKLGRHVAILGDLQGPKIRVSTFKEGKVFLNIGDKFLLDANLGKGEGDKEKVGIDYKGLPADVVPGDILLLDDGRVQLKVLEVQGMKVFTEVTVGGPLSNNKGINKLGGGLSAEALTEKDKADIKTAALIGVDYLAVSFPRCGEDLNYARRLARDAGCDAKIVAKVERAEAVCSQDAMDDIILASDVVMVARGDLGVEIGDPELVGIQKALIRRARQLNRAVITATQMMESMITNPMPTRAEVMDVANAVLDGTDAVMLSAETAAGQYPSETVAAMARVCLGAEKIPSINVSKHRLDVQFDNVEEAIAMSAMYAANHLKGVTAIITMTESGRTALMTSRISSGLPIFAMSRHERTLNLTALYRGVTPVHFDSANDGVAAASEAVNLLRDKGYLMSGDLVIVTQGDVMSTVGSTNTTRILTVE", "text": "FUNCTION: Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis. SIMILARITY: Belongs to the pyruvate kinase family."}
{"protein": "IKITTMLAKLGKVLAHV", "text": "FUNCTION: Mast cell degranulating peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MCD family. Bombolitin subfamily."}
{"protein": "MTVEEVSDGSVWSREDDIAFERALANNTDESEERWEKIAADVPGKSVEQIKEHYELLVEDVTRIESGCVPLPAYGSPEGSNGHAGDEGASSKKGGNSHAGESNQAGKSKSDQERRKGIAWTEDEHRLFLLGLDKYGKGDWRSISRNFVVTRTPTQVASHAQKYFIRLNSMNKDRRRSSIHDITSVGNADVSTPQGPITGQNNSNNNNNNNNNNSSPAVAGGGNKSAKQAVSQAPPGPPMYGTPAIGQPAVGTPVNLPAPPHMAYGVHAAPVPGSVVPGAAMNIGQMPYTMPRTPTAHR", "text": "FUNCTION: Transcription activator that coordinates abscisic acid (ABA) biosynthesis and signaling-related genes via binding to the specific promoter motif 5'-(A/T)AACCAT-3'. Represses ABA-mediated salt (e.g. NaCl and KCl) stress tolerance. Regulates leaf shape and promotes vegetative growth. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSKQECMEFKAVVYSNTLQSILAIVKAMTTLGIDYVNPRSREDQQLLLSMANTLEDGDMTPQLAEIIKRLWGDPGIQACFERASEYQLNDSAAYYLNDLDRLTAPGYVPNEQDVLHSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFATTSIVLFLNKKDLFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF", "text": "FUNCTION: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP- phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications for the prevention and treatment of malabsorption syndromes and diet- related disorders including diabetes and obesity. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with microvilli, the presumed sites of sensory transduction in taste cells. SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily."}
{"protein": "MSENKKFRPKKVGNTEQVSEKQHTDTALNISQDNKTSSSSAKRGAKGRRGTKGKSGPANSSQTSNIEGSNALELEFDRDSQLSVLQELFPSWTIDDLSFALEEADRDLELTILHITEGHASKWGEVKKKPIPKTKSKPTSHAPVSDNVSSTFRNATRKSKKPSASKDTSRGVRKSKAGAPSDPSSVHAPSSLEKPAGTGDLPSSEISTKAPASTTVSSSVDPGTINEDSSMKDHTTSNEQASVLTSANTAASTNTNGTAGGTSASAKSTSAADQAVASSKPIKKAWASVAKSKKKVTPAPAPAPESEPSKPSIAPSQPSKTNVSAAYEKPAELSSSSVPFPHKSQDSATPANVETTPSTATSAPKKSTAPFAINAVKPAPGLSNISSASLPKPSFAKQAAVGSQSSTTSMTTARLLSDRFPVVMPVANTAAIPEKVQVRFGSLTLGGEDKKSTKSSSDNIAQSGPRSSYFPKKTVSPKPEAKKEASKVAESTKIPKKQHTSAYESRAPQSKVPENLKESHVNETPYRGLHDVNLPASGNASSVSAIPPQVSAQTTIPAASTSATSGPVVGKQSAGYGGIYSPATHGISPQPYAGASLIPPSTGAAFNNETASSNAGETTALPYSSRFMNPVENRSANSPFDNFQHIDHSTELGYASNTSQQYQQTSHPAYTTMSPIEYGQAAPAAHYYNERNQYSQYDNVAGSASNTPDVHSVMHNKVASSNATSLPAAGTATPSPVVSQQQPQPYAFPPMYPIPYVSYGYGTMPYNNNKFGQPQQGYMSQSGFNDFPPIFGGHSNVYNRQQPGNVSGMSGTQTSNPINNATANTSGMTEKAAGHRDSVIGNGGVTGANSMSSTLGGLSSMSGMGRAAPGMFMGNVGSFENLSANAASPYGLPPQQTPLTNAATQQTTSFQSNANKVNNANSQPAGFPFNSGASTNAGSNGLGGYNAYNQSFINRPGGWYGNA", "text": "FUNCTION: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor rhp26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, telomere Note=During transcription stress, localizes to the nucleus following proteolytic cleavage by the proteasome. SIMILARITY: Belongs to the DEF1 family."}
{"protein": "MDTSGNPNGYYSAHLNPESDDLWSVLPKKYPGQLTEGILEEILEIESRLSRSKKNLKDAQKENRAFLVGVYPERSVGRHPSLSMEELKELCRTAEVHVVDTFIQRKNRLDPSTVLGKGKLEEIILKAIQKHVELLVFDLELTPSQAKKISDIADIKVIDRTQLILDIFARNAKSRDGKLQVELAQLKYLKGRLTELDDNMSRLTGGIGGRGPGETKLEIGKRRVEERITRLEVELKSLKKRREINRRQRKRNELPAVGIVGYTNAGKSTFLNALTNSEILSENKLFATLDPTTRRIRFPEEREIIISDTVGFIHDLPPELSNAFKATLEELGDSDLLVHVVDVSNPDYKLQMEAVEKILEELELSHIPMIQVFNKIDNLEKFKTWKIESDSNGYKTFSHPSINHGPGLEAIADLKEELGIDVHSDTVLVSAYQGWGLKAFLDLLEEKIYNLPRLNYSIAEKL", "text": "FUNCTION: GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. SUBCELLULAR LOCATION: Cytoplasm Note=May associate with membranes. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family."}
{"protein": "MSGLLIAAPASGSGKTTVTLGLMRALKRRGVAIAPGKAGPDYIDPAFHAAATGEPCFNYDPWAMRPELLLANASHVASGGRTLIVEAMMGLHDGAADGSGTPADLAATLNLAVILVVDCARMSQSVAALVRGYADHRDDIRVVGVILNKVGSDRHEMMLRDALGKVRMPVFGVLRQDSALQLPERHLGLVQAGEHSALEGFIEAAAARVEAACDLDAIRLIATIFPQVPAAADAERLRPLGQRIAVARDIAFAFCYEHLLYGWRQGGAEISFFSPLADEGPDAAADAVYLPGGYPELHAGQLSAAARFRSGMHSAAERGARIFGECGGYMVLGEGLVAADGTRYDMLGLLPLVTSFAERRRHLGYRRVVPVDNAFFDGPMTAHEFHYATIVAEGAADRLFAVSDAAGEDLGQAGLRRGPVAGSFMHLIDVAGAA", "text": "FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L- glutamine or ammonia as the nitrogen source. To a much lesser extent, can also use cobyrinate as substrate in vitro, but the physiological substrate is indeed hydrogenobyrinate, as part of the aerobic pathway for cobalamin biosynthesis. SIMILARITY: Belongs to the CobB/CbiA family."}
{"protein": "MASIMEGPLSKWTNVMKGWQYRWFVLDYNAGLLSYYTSKDKMMRGSRRGCVRLRGAVIGIDDEDDSTFTITVDQKTFHFQARDADEREKWIHALEETILRHTLQLQGLDSGFVPSVQDFDKKLTEADAYLQILIEQLKLFDDKLQNCKEDEQRKKIETLKETTNSMVESIKHCIVLLQIAKDQSNAEKHADGMISTINPVDAIYQPSPLEPVISTMPSQTVLPPEPVQLCKSEQRPSSLPVGPVLATLGHHQTPTPNSTGSGHSPPSSSLTSPSHVNLSPNTVPEFSYSSSEDEFYDADEFHQSGSSPKRLIDSSGSASVLTHSSSGNSLKRPDTTESLNSSLSNGTSDADLFDSHDDRDDDAEAGSVEEHKSVIMHLLSQVRLGMDLTKVVLPTFILERRSLLEMYADFFAHPDLFVSISDQKDPKDRMVQVVKWYLSAFHAGRKGSVAKKPYNPILGEIFQCHWTLPNDTEENTELVSEGPVPWVSKNSVTFVAEQVSHHPPISAFYAECFNKKIQFNAHIWTKSKFLGMSIGVHNIGQGCVSCLDYDEHYILTFPNGYGRSILTVPWVELGGECNINCSKTGYSANIIFHTKPFYGGKKHRITAEIFSPNDKKSFCSIEGEWNGVMYAKYATGENTVFVDTKKLPIIKKKVRKLEDQNEYESRSLWKDVTFNLKIRDIDAATEAKHRLEERQRAEARERKEKEIQWETRLFHEDGECWVYDEPLLKRLGAAKH", "text": "SUBCELLULAR LOCATION: Late endosome membrane Golgi apparatus, trans-Golgi network membrane Note=Localizes at the Golgi- late endosome interface. SIMILARITY: Belongs to the OSBP family."}
{"protein": "MSKKQEYIAPIKYQNSLPVPQLPPKLLVYPESPETNADSSQLINSLYIKTNVTNLIQQDEDLGMPVDLMKFPGLLNKLDSKLLYGFDNVKLDKDDRILLRDPRIDRLTKTDISKVTFLRRTEYVSNTIAAHDNTSLKRKRRLDDGDSDDENLDVNHIISRVEGTFNKTDKWQHPVKKGVKMVKKWDLLPDTASMDQVYFILKFMGSASLDTKEKKSLNTGIFRPVELEEDEWISMYATDHKDSAILENELEKGMDEMDDDSHEGKIYKFKRIRDYDMKQVAEKPMTELAIRLNDKDGIAYYKPLRSKIELRRRRVNDIIKPLVKEHDIDQLNVTLRNPSTKEANIRDKLRMKFDPINFATVDEEDDEDEEQPEDVKKESEGDSKTEGSEQEGENEKDEEIKQEKENEQDEENKQDENRAADTPETSDAVHTEQKPEEEKETLQEE", "text": "FUNCTION: The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of the RAD6/UBC2-BRE1 ubiquitin ligase complex, which ubiquitinates histone H2B to form H2BK123ub1. Also required for the methylation of histone H3 by the COMPASS complex to form H3K4me, by SET2 to form H3K36me, and by DOT1 to form H3K79me. RNA polymerase II associated protein important for transcription of a subset of genes. Required for both positive and negative regulation. Negatively regulates MAK16 expression. Also required for efficient CLN2 transcription in late G1 and may be involved in transcription of galactose-inducible genes. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the PAF1 family."}
{"protein": "MAPSSSPLRTTSETDEKYANVKWEELGFALTPIDYMYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDIDPCQG", "text": "FUNCTION: Converts 2-oxo acids to branched-chain amino acids. Acts on leucine, isoleucine and valine (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MIWKQPPRRMGEMGGSLSRRFGNAAASWAVWRVSRSCFSLLFFFYFFLFFSSSSLLPTTNNYQHLQLHSLIPTLNTTAHLPHQQASSASMKASLFLACSALGLALATPTQDAPETVNNPLGIVYQAKLPETSRTGIRGTINATAHSSGRGVVFNLDLWGFDNTEGPFRKLHTCFDQTNKQTNKIVKLTTTTAYHIHVDPVPTDGSCGPTKDHLDPFGRGQTPPCDDSLPQTCEPGDLSGKFGRLTTSSMEEHFNQTFHDLYTSTRPGLGTFFGNRSIVIHHRNSTRLTCANFTLVEQPGTSTTYVPRPTGTGIISSIFPTGTGAISTSGHAPTISATYTPTPTPSPPAQNNGAGRLVGFSLGAIMAALVPLAL", "text": "FUNCTION: Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action (By similarity). Degrades host-derived reactive oxygen species to escape innate immune surveillance (By similarity). Involved in the occurrence of miconazole- tolerant persisters in biofilms (By similarity). Persisters are cells that survive high doses of an antimicrobial agent. The unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Secreted Cell membrane; Lipid-anchor, GPI-anchor Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGKNGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYDTCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNSQRAACICAEEEKEEL", "text": "FUNCTION: Not known; does not seem to have catalytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MAVPRANTSKARTRRRRAVNMRLEAPHLVECGNCGNFVQSHRVCGRCGFYRGRQVINPDDLC", "text": "SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family."}
{"protein": "MLVTLEGLDGSGKTTVWESLRASHDDGVTFTAEPTDSQYGQAVRRSESAADADPIAELFLFTADHADHLSRVVSPALDRGDVVISDRYSDSRYAYQGATLADTVPRAMEYVRGIHQPWTRPPDVTLYFDVDPDTGAARSGATNKFETAAFLADVRANYEQLIDYTPERFVRIDATQSPEAVIADAEAALADALPDDAWA", "text": "SIMILARITY: Belongs to the thymidylate kinase family. SIMILARITY: Belongs to the thymidylate kinase family."}
{"protein": "MNRIFGRGKPKGPPPNLTDCISGVDSRAESVDKKIARLDAELMKYKDQMKKMRDGPSKNMVKQKAMRVLKQKRMYEGQRDQLMQQSFNMEQANYTIQTLKDTKTTVEAMKIGAKEMKKAYKNVKIDQIEDLQDQLEDMMEDANEVQEALSRSYGTPEIDEDDLEAELDALGDELLLDDDNSYLDEASSAPAIPEGAPGDRTTNRDGVLVDEFGLPQIPAT", "text": "FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNF7 family."}
{"protein": "MIIVISGPPGSGKSTVAKILSKNLSLKYISAGHIFRELAEKEGLSLLELNKKAEENFEIDKKIDREIFRIASTEKNIIIESHIGGWLLKDIADITVYLNASIEIRAMRIAKRDNIPFTKAIEQIIEREESHSRRFLAYYGIDLSDLSVFDLVINTDNLQPDEISKIIEAYLNFMLAKNIH", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily."}
{"protein": "MSKKVLVFGGTGYQGGSVVRELLKDDSFKVITLSRNPESEKCKELKKLGADVIKCDESQPKEEIEKVMKGCDCVYLVTNSQGYCEKEIEYGIKVADVALKCGVKHFIFSTVPGPNKLSNGKFKSPDLDNKVEIEQHIRQLSKSNPEFISSFVIAPWYFQNFINYYQPEKESSTSDKYILKWACDPKVSLDYGDIDELGLLVREIFKNPIKFSGETVPFSSEILTPIQIVEIISKVTNKKVSYQFIDPVEYGKSYDLEVSLMLAFFNEYGGFNIYGGDRSIAHNIKKLTSFEEYLKKINYKLD", "text": "FUNCTION: May be a redox sensor protein. SIMILARITY: Belongs to the NmrA-type oxidoreductase family."}
{"protein": "MIDQNRSYEQESVERALTCANCGQKLHVLEVHVCEHCCAELMSDPNSSMHEEEDDG", "text": "SIMILARITY: Belongs to the ninF family."}
{"protein": "MEEFLSTLRDHDASSVLSSCEPELQELMRQIDIMMGHKRHEWEAEVRAMELSLHNTQEELQSAKALLDKRNSEIRVLGKQLEELHTGKQELVVKYEEQLLHVKEELSKLKRSYEKLQRKHLKESRDGALSREEDRTELSRLNSKIEEFRQRSAEWEQQRLQYQRQVSLLEEQRKTLAEQFSLIQSQGVGRPQEQGQGELQRLRSQLQRAQDSLHAQELELERLRLLQDELGDSIKEQQVSCHAAAHRRGQVLSEEREELKATLDAQDQFVRSTGVQQQQLRREVNRLNQTLQAKEQVIRSLEECLSSPGSAPNLASLRQDLEKVTARLNSSQTCESHLKAEVMRLRDKLESMRKYKAEMSRREHEWKQMEEEHSRCTAENKRLRDELERAEQTRCGEQEGMRKEVFQLTSELHQRDITIATLTGSTSSIERQLRAEVERAERRASELKVTQVQLETLKLENQHLNDLLERVESQSPKRGDGELASLRDSYVSSLKSLEEENRQLRLEMTELRARMEASNQTWQDKYERALLQNQNKNHLYNEQNRADEDVQRRHQEELQAMETQMQERASHYEEQIQTLLTQLENLSRTSPYRPDGQTQESKTSVSPARSSASSASSSSSTRKAQRVATLLSAVANGEEAQASSSDSTGSPNTSVTTRFLEEETLRSQELLQRLDAHIQSMKLENSNTVCKYLGKTGNPQNDVFWQGTHSFCKMID", "text": "FUNCTION: Required for normal spindle assembly. Plays a key role in mother-centriole-dependent centriole duplication. Plays a role in DNA damage response. Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the CEP63 family."}
{"protein": "MGAVVSRWRAKPSTVEVLEGLDKDIQVLEEYREKNHKQLKLWVYRLLLYSALLYLMACAVVYAWYIPERMIGKLIVASPFLLFPLLIWLLRKLLIILYNKRTERNNEKLEELKAEKKKILEQVMETETYKNAKLILERFDPDSKKKLELETQPIGPTVTPRQGQELRHRLVSPRPTGRPPPVPVPGPSVPGTPLSAPGGPPEKGLSASTPQALIRRPGTPVGTPIPVMGMHPPGPPLARPVLPRERGAVDRVIEYLVGDGPQNRYALICQQCLSHNGMALKEEFEYIAFRCAYCYFLNPARKTRPQAPRLPEFAAEAKTSQDPPAVAMETDLPVSPPAPESKEAGPEPVKAGDGDPQTDEIPTEEMKPGDPEPHTDIPDKSDGEQDVSAMEVE", "text": "FUNCTION: Endoplasmic reticulum (ER)-shaping membrane protein that plays a role in determining ER morphology. Involved in the stabilization of nascent three-way ER tubular junctions within the ER network. May also play a role as a curvature-stabilizing protein within three-way ER tubular junction network (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein; Cytoplasmic side Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions, which represent crossing-points at which the tubules build a polygonal network. SIMILARITY: Belongs to the lunapark family."}
{"protein": "MTLFHFGNCFSLAYFPYFITYKCSGLSEYNAFWRCVQAGATYLFVRLCKMLFLATFFPTWEGGAGVYDFVGEFMKATVDMADLLGLHLVMSRNAGKGEYKIMVAAMGWATAELIMSRCIPLWVGARGIEFDWKYIQMSFDSNISLVHYIAMAAVVWMFTRYDLPKSFRLPVAILLGLCVYKGFLMELFVHVFLLGSWTALLVKAVLTGAISLCSLFLFVTLVHSN", "text": "FUNCTION: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM147 family."}
{"protein": "MCLSPVKGAKLILIFLFLGAVQSNALIVNLTDSKGTCLYAEWEMNFTITYETTNQTNKTITIAVPDKATHDGSSCGDDRNSAKIMIQFGFAVSWAVNFTKEASHYSIHDIVLSYNTSDSTVFPGAVAKGVHTVKNPENFKVPLDVIFKCNSVLTYNLTPVVQKYWGIHLQAFVQNGTVSKNEQVCEEDQTPTTVAPIIHTTAPSTTTTLTPTSTPTPTPTPTPTVGNYSIRNGNTTCLLATMGLQLNITEEKVPFIFNINPATTNFTGSCQPQSAQLRLNNSQIKYLDFIFAVKNEKRFYLKEVNVYMYLANGSAFNISNKNLSFWDAPLGSSYMCNKEQVLSVSRAFQINTFNLKVQPFNVTKGQYSTAQDCSADEDNFLVPIAVGAALGGVLILVLLAYFIGLKRHHTGYEQF", "text": "FUNCTION: Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live (PubMed:10972293). Functions by binding target proteins, such as GAPDH, NLRP3 and MLLT11, and targeting them for lysosomal degradation (By similarity). In the chaperone-mediated autophagy, acts downstream of chaperones, such as HSPA8/HSC70, which recognize and bind substrate proteins and mediate their recruitment to lysosomes, where target proteins bind LAMP2 (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed:27628032). Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes (PubMed:27628032). Required for normal degradation of the contents of autophagosomes (PubMed:10972293, PubMed:12221139). Plays a role in lysosomal protein degradation in response to starvation (PubMed:27628032). Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endosome membrane; Single-pass type I membrane protein Cytoplasmic vesicle, autophagosome membrane Lysosome membrane; Single-pass type I membrane protein Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane. SIMILARITY: Belongs to the LAMP family."}
{"protein": "MKSLIFVLLLGAVFAEEDKIVGGYECTKHSQAHQVSLNSGYHFCGGSLVSKDWVVSAAHCYKSVLRVRLGEHHIRVNEGTEQYISSSSVIRHPNYSSYNINNDIMLIKLTKPATLNQYVHAVALPTECAADATMCTVSGWGNTMSSVADGDKLQCLSLPILSHADCANSYPGMITQSMFCAGYLEGGKDSCQGDSGGPVVCNGVLQGVVSWGYGCAERDHPGVYAKVCVLSGWVRDTMANY", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MQAAQLSWELENAVTLIDPQRDSLYRYDEETHKYLSDTRPWTKDPHYFKSVRISAVALLKMVMHARSGGSLEVMGLMQGYILPNTFVVTDAFRLPVEGTETRVNAQDEANEYMVSYLQSCREAGRMENAVGWYHSHPGYGCWLSGIDVSTQDMQQMSGPFVAVVIDPERTISAGKVDIGAFRTFPKDYTPPKEEQEEDEYQTVPLNKAEDFGAHASHYYSLEVSLFKSALDTEILSLLWNKYWVATLSQSPLFTTRDYGSKQMLDLSQKTRRVARGIESNPPRGGAPTQVRDQQLERVVKDGQRIVSEEVKGLLAAEVKMQLFQGIGGKQTVEST", "text": "FUNCTION: Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex seems to link protein degradation to sexual development. Required for fruit body formation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily."}
{"protein": "MVSEKVLAIIAVALGTYLARFLPLKIKFATSDKIKSFLSLSSTSVISALFVTSVFTPDAAEFGVRVAALFPLILSFYRWRNFGLSIFAAVLSYYLLRLAV", "text": "SIMILARITY: To M.jannaschii MJ1155.1."}
{"protein": "MAALDLRAELDSLVLQLLGDLEELEGKRTVLNARVEEGWLSLAKARYAMGAKSVGPLQYASHMEPQVCLHASEAQEGLQKFKVVRAGVHAPEEVGPREAGLRRRKGPTKTPEPESSEAPQDPLNWFGILVPHSLRQAQASFRDGLQLAADIASLQNRIDWGRSQLRGLQEKLKQLEPGAA", "text": "FUNCTION: Accessory component of the proton-transporting vacuolar (V)- ATPase protein pump involved in intracellular iron homeostasis. In aerobic conditions, required for intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. Necessary for endolysosomal acidification and lysosomal degradation (PubMed:28296633). May be involved in Golgi homeostasis (PubMed:26833332). SUBCELLULAR LOCATION: Endosome Lysosome Endoplasmic reticulum-Golgi intermediate compartment Cytoplasmic vesicle, COPI-coated vesicle Endoplasmic reticulum."}
{"protein": "MKLSRLALLSVFALASAPSWAESVVTVYSIDGLHDGDNSWYQVQFDAFTKATGITVRYVEGGGGVVVERLAKERTNPQADVLVTAPPFIQRAAAEKLLANFNTDAASAIPDANNLYSPLVKNYLSFIYNSKLLKTAPASWQDLLDAKFKNKLQYSTPGQAADGMAVMLQAFHSFGSKDAGFAYLGKLQANNVGPSASTGKLTALVNKGEIYVANGDLQMNLAQMERNPNVKIFWPANDKGERSALAIPYVIGLVQGAPQSENGKKLINFLLSKEAQTRVSELSWGMPVRSDVTPSDEHYKAATAALEGVQSWQPNWDDVAVSLSADISRWHKVTESE", "text": "FUNCTION: Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved in 2-aminoethylphosphonate import. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
{"protein": "MKALILVGGFGTRLRPLTLSLPKPLVDFANKPMILHQIEALKAIGVDEVVLAINYEPEQLLVMSKFSNDVEATLGIKITCSQETEPLGTAGPLALARDKLVDGSGQPFFVLNSDVISDYPLEEMIAFHNAHGGEASIMVTKVDEPSKYGVVVMEEATGRVERFVEKPKLFVGNKINAGIYLLNPSVLDRIELRPTSIEKEIFPQIAEAEKLYAMLLPGFWMDIGQPRDYITGLRLYLDSLRKKSPSKLATGPHILGNVLVDETAEIGEGCLIGPNVAIGPGCVVESGVRLSHCTVMRGVHVKRYACISSSIIGWHSTVGQWARVENMSILGKNVYVCDEIYCNGGVVLHNKEIKSDILKPDIVM", "text": "FUNCTION: Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
{"protein": "MANPVKYESLIVVCNGLERLFGNIVKVISYPFHALFPKLRFTIPEYSPAKIKSKQNTRITKTIWQTNYSNKVTLPVYANYLFNRLMSLSYDYRYVSTEERETYIKENADTRTFNAYSKLTDGAAQADFWRVFTLLQEGGVYIDIDGHLVFPISQIIRENDQEVLIKRRDKYTNFFLACEERSPS", "text": "SIMILARITY: Belongs to the glycosyltransferase 32 family."}
{"protein": "MEMYETLGKVGEGSYGTVMKCKHKNTGQIVAIKIFYERPEQSVNKIAMREIKFLKQFHHENLVNLIEVFRQKKKIHLVFEFIDHTVLDELQHYCHGLESKRLRKYLFQILRAIDYLHSNNIIHRDIKPENILVSQSGITKLCDFGFARTLAAPGDIYTDYVATRWYRAPELVLKDTSYGKPVDIWALGCMIIEMATGNPYLPSSSDLDLLHKIVLKVGNLSPHLQNIFSKSPIFAGVVLPQVQHPKNARKKYPKLNGLLADIVHACLQIDPADRISSSDLLHHEYFTRDGFIEKFMPELKAKLLQEAKVNSLIKPKESSKENELRKDERKTVYTNTLLSSSVLGKEIEKEKKPKEIKVRVIKVKGGRGDISEPKKKEYEGGLCQQDANENVHPMSPDTKLVTIEPPNPINPSTNCNGLKENPHCGGSMTMPPINLTNSNLMAANLNSNLFHPSVRLTERAKKRRTSSQSIGQVMPNSRQEDPGPIQSQMGKGIFNERTGHSDQMSNENKRKLNFSRSDRKEFHFPELPVTIQPKDTKGMEVKQIKMLKRESKKTDSSKIPTLLNVDQNQEKQENTGNAQTERKKNLPDVE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MQFSGRTRKKLRLAGDQRNACYPHSLQFYLQPPTENISLTEFESLAFDRVKLLKAIENLGVSYVKGTEQYQSKLEAEIRKLKFSYRENLEDEYEPRRRDHISHFILRLAYCQSEDLRRWFIQQEMDLLRFRFSILPKDKVQSFLKDTHLHFEAISDEEKTLREQDIMASSPSLSGVRWESESVYKVPFADALDLFRGRKVYLEDGFAYVPLKDIVAIILNEFRATLSKALALTARSLPAVQSDERLQPLLSHLSHSYTGQDYSTQKSTGKISLDQIDSLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWKQEFIKGKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCMKIILTNPPSQGDFHGCPFRHSDAELLKQKMQTYKIPASGISQILDLVKGNHYQVACQKYFEMTHNVDDCGFSLNHPNQFFFESQRILTGGKDIKKEASHPETPQHKPSTQKTKDATSALASLDSSLEMDLEGLEDYFSK", "text": "FUNCTION: Regulatory subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which play an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity). These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. In the primase complex, both subunits are necessary for the initial di- nucleotide formation, but the extension of the primer depends only on the catalytic subunit (By similarity). Binds RNA:DNA duplex and coordinates the catalytic activities of PRIM1 and POLA2 during primase- to-polymerase switch. SIMILARITY: Belongs to the eukaryotic-type primase large subunit family."}
{"protein": "MSKKIIQVVLKENIQKLGKSNDVVKVATGYARNFLIPNKMASVATVGMLNQQKLYAAIKEKKIIFAKENARKTQQLLEEIQKFSISKKTGDGETIFGSVTEKEISQIIKNTTNVDIDKQNILIPEIKTIGLYNIEIKLFNQVTANIQLQVLPESN", "text": "FUNCTION: Binds to the 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family."}
{"protein": "MTYSEKALIFCISVNLKFILVHINFQSKRKEGNICGKKPTYSVRMRASRNAPHEQGGKHISGGERLITYSGLQEAVDGLLHKGFSHSRGIPDFMQIQLESINEPIETIRPLPVAFHQSDTPEKGQAIARKLLQKAGIPPHMIEKAYENIAEYAEARGAVLFDIRAGERIDGRGNRGVRVSRMDWPSHDFQKWAFTHNMPENSRIKEAHAIAAKVCAHPGIIAELCWSDDPDYITGYVAAKKLGYQRIAKMKNAGDESGCRIFFTDGSIDTESCIHFLEKQPVFIQREENI", "text": "FUNCTION: Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. SIMILARITY: Belongs to the BioW family."}
{"protein": "MALLPDKEKLLRNFLRCANWEEKYLYIIELGQRLTELRDEDRSPQNSIQGCQSQVWIVMRQNAHGIIELQGDSDAAIVKGLIAVVFILYDQMTPQDIVSFDVRPWFEKMALTQHLTPSRSQGLEAMIRAIRAKAAALS", "text": "FUNCTION: Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L- alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SufE family."}
{"protein": "MKILVLAVHPHMETSVVNKAWAEELSKHDNITVRDLYKEYPDEAIDVAKEQQLCEEYDRIVFQFPLYWYSSPPLLKKWQDLVLTYGWAFGSEGNALHGKELMLAVSTGSEAEKYQAGGANHYSISELLKPFQATSNLIGMKYLPPYVFYGVNYAAAEDISHSAKRLAEYIQQPFV", "text": "SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family."}
{"protein": "MTKVLVTGAGGQLGLELCRQLKQAGYEVIALTKKMMNIADQRSVRHSFGHYQPDIVVNSAAFTSVDQCEKELDKAYLINGIGAYYTALESTRIGAQYVHISTDYVFNGKGTQPYREDDPLDPKTIYGKSKRLGEELIRLTTKDSTIIRTSWVYGHGGSNFVETMLKLAETKQELRVVSDQIGSPTYTKDLAEAVIKLFSHPPGIYHVSNSGICSWYEFATAIMEESGLETAILSVTTEEYGNKTPRPAYSVLSHRAIEEAGIRPRHWREALREYLQERSSACD", "text": "SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family."}
{"protein": "MMEFTIKRDYFINQLNDTLKAISPRTTLPILTGIKIDAKENEVILTGSDSEISIEITIPKQVDGEEIVEITETGSVVLPGRFFVDIIKKLPGKEVKLSTNEQFQTLITSGHSEFNLSGLDPDQYPLLPEVSRDDAIQLSVKVLKNIIAQTNFAVSTSETRPVLTGVNWLIQDNELICTATDSHRLAVRKLQLEDESENKNVIIPGKALSELNKIMSDSDEDIDIFFASNQVLFRVGNINFISRLLEGHYPDTTRLFPENYEIKLGINNGDFYHAIDRASLLAREGGNNVIKLSTGNELVELSSTSPEIGTVKEEVNANDVEGGNLKISFNSKYMMDALKAIDNDEVEVEFFGTMKPFILKPKDDDSVTQLILPIRTY", "text": "FUNCTION: Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the beta sliding clamp family."}
{"protein": "MIDRYSREEMANIWTDQNRYEAWLEVEILACEAWSELGHIPKEDVKKIRQNAKVDVKRAQEIEQETRHDVVAFTRQVSETLGDERKWVHYGLTSTDVVDTALSYVIKQANEIIEKDIERFIKVLEEKAKNYKYTLMMGRTHGVHAEPTTFGVKMALWYTEMKRNLKRFKEVRKEIEVGKMSGAVGTFANIPPEIEQYVCDHLGIDTASVSTQTLQRDRHAYYIATLALVATSLEKFAVEIRNLQKTETREVEEAFAKGQKGSSAMPHKRNPIGSENITGISRVIRGYITTAYENVPLWHERDISHSSAERIMLPDVTIALDYALNRFTNIVDRLTVFEDNMRNNIDKTFGLIFSQRVLLALINKGMVREEAYDRVQPKAMESWETKTPFRQLIEKDESITNVLSKEELDECFNPEHHLNQVDTIFKRAGLE", "text": "FUNCTION: Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N- succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta- D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4- carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate. SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily."}
{"protein": "MSNGLVILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMDSESGLTASVACCNCCRHPSEACLYILNKRKVMSQHGLVPPAMLVGNGIEKLLLHSNIKLVPESHLITERSMKTQIKWKEILYQNPINLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIESFDNKSHSSTCAVATSGTGEHISNTCFACRSSQLLVSEDNVVSSLNKLINDFHEHPSATLYSDLQVGIIFAKVETSNSHNKRIIFGLAHSSPDMVFGFMKGDHSKPTTEISRKGSKRSSVQLYAERL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Ntn-hydrolase family."}
{"protein": "MTAHNPVQGTLPRSNEEIAARVKAMEAILVDKGLISTDAIDHMSSVYENEVGPQLGAKIVARAWVDPEFKQRLLTDATSACREMGVGGMQGEEMVVLENTGTVHNMVVCTLCSCYPWPVLGLPPNWYKYPAYRARAVRDPRGVLAEFGYTPDPDVEIRIWDSSAELRYWVLPQRPAGTENFTEEQLADLVTRDSLIGVSVPTTPSKA", "text": "FUNCTION: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. SIMILARITY: Belongs to the nitrile hydratase subunit alpha family."}
{"protein": "MPYIITQSCCNDGSCVFACPVNCIHPTPDEPGFATSEMLYIDPVACVDCGACVSACPVGAIASDTRLAPKQLPFIEINASYYPARPIDLKLPPTSKLAPVIPAAQVHVRRRPLTVAIVGSGPAAMYAADELLTQPGVWVNVFEKLPTPYGLVRAGLAPDHQNTKKVTELFDRVAEHRRFRFFLNVEIGRHLSHDELLAHHHAVLYAVGAPDDRRLNIDGMGIPGTGTATELVAWINAHPDFAYLPVDLSHERVVVIGNGNVALDVARLLTADPDNLARTDISEFALHVLGGSAVREVVVAARRGPAHSAFTLPELIGLKATSEVVLDAGDRKLVEGDFATVSDSLTRKKLEVLSSLVDSSKPTSRRRIRLAYQLTPKRVLGNQRATGVEFSVTGTEESRRFDAGLVLTSVGYRGKRIRDLPFDEEAAVIPNDGGRVVDPSRGRPMPGAYVAGWIKRGPTGFIGTNKLCSVQTVQAVVADFNAGWLTDPVAEPAELAKLVHARQPDTVDSVGWRAIDAAEIAQGSTEGRPRRKFTDVADMLAVAAGAPPLRLRALS", "text": "SIMILARITY: In the C-terminal section; belongs to the ferredoxin--NADP reductase family."}
{"protein": "MGKRWDSNSSGSWDHIWSGNDTQHPWYSDINITYMNYYLHQPHVTAVFISSYFLIFFLCMVGNTVVCFVVIRNRYMHTVTNFFIFNLAISDLLVGIFCMPITLLDNIIAGWPFGSSMCKISGLVQGISVAASVFTLVAIAVDRFRCVVYPFKPKLTVKTAFVMIVIIWGLAITIMTPSAIMLHVQEEKYYRVRLSSHNKTSTVYWCREDWPNQEMRRIYTTVLFATIYLAPLSLIVIMYARIGASLFKTSAHSTGKQRLEQWHVSKKKQKVIKMLLTVALLFILSWLPLWTLMMLSDYADLSPNKLRVINIYVYPFAHWLAFCNSSVNPIIYGFFNENFRSGFQDAFQFCQKKVKPQEAYGLRAKRNLDINTSGLLVHEPASQNPSGENLGCRKSADNPTQESLMEETGEATNSTET", "text": "FUNCTION: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTPWLGLVVLLSCWSLGHWGTEACTCSPSHPQDAFCNSDIVIRAKVVGKKLVKEGPFGTLVYTIKQMKMYRGFSKMPHVQYIHTEASESLCGLKLEVNKYQYLLTGRVYEGKMYTGLCNFVERWDHLTLSQRKGLNYRYHLGCNCKIKSCYYLPCFVTSKKECLWTDMLSNFGYPGYQSKHYACIRQKGGYCSWYRGWAPPDKSISNATDP", "text": "FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family."}
{"protein": "MRGIIKGVSNDGLGVLGEVLVPFAYPGDVVEVISTRERFGRTIARDFKLVKSSPIRVPGKCRYFGRCGGCLWQGLKYREQLKLKEEIFKRVTGVEAEIKGSPRIWFFRNISNFIVTVNGIGFKEFGMPRTVVSVDECPVFSERTKLYIRAMKRFLRETGLNPWNWKNGDVHYLQVREGKFTGEVMINVIAHIPPSGREELTEAFGFADSVYWSLKRDKRDDPKGIPTLIKGNEFIRESIEGLVYLIHPSTFFQTNSYALPILLKAVESFAEGSKVLDLYSGVGTFSLYLAKKGFEVTGVEVNEESVRVAKKSAEVNSLDVSFIPGRAEDAKLKGYETLIVDPPRKGLKDFSKRIAKEGPENLIYVSCNPSKFVLDYRNYLSKAYKIEDAVLIDMFPHTPHVEAVVKLRRR", "text": "FUNCTION: Catalyzes the formation of 5-methyl-uridine at position equivalent to 747 (m5U747) in 23S rRNA (m5U859 in the P.abyssi numbering). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family."}
{"protein": "MSEVEFSHEYWMRHALTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVMQNYRLIDATLYVTLEPCVMCAGAMIHSRIGRVVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGILADECAALLSDFFRMRRQEIKAQKKAQSSTD", "text": "FUNCTION: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2). FUNCTION: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2). Essential for cell viability. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MPRSLKKGPFIDLHLLKKVEKAVESGDKKPIRTWSRRSTVFPNMIGLTIAVHNGRQHVPVFVSDEMVGHKLGEFAPTRTYRGHAADKKAKKR", "text": "FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SIMILARITY: Belongs to the universal ribosomal protein uS19 family. SIMILARITY: Belongs to the universal ribosomal protein uS19 family."}
{"protein": "MSHFTNIETRFQNLFYLEKALNKLDINHKPQKKVTNINSKSYDIDINLMISQPNGYDIEFCWNGQEYELIADTSFWQQKDSIKGFINNIAKQYAGEVIIGESKKIGFQPIKYQQNKDGSNTCYFTTLE", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf35 family."}
{"protein": "MQQAQQKPFIPTIPAYQALKLDEDLINKCNYSIEQLMEIAGTAVAQATTHYIESTSSVSKAGVLVVCGPGNNGGDGLVAARHLSSGSMSSATVRVWLPKEPSSSVNKRMLSIAKHAGVVFIKDTNEEALHAILEFINSCESFYLVDAIFGFSFHGGPIKPPYDTVINTLLQMQTSMAIGPKTRIVSVDVPSGWSVDAQEWGLNTDKELIPDGLLRPDALISLTVPKNCSLWLPPGTAHYLGGNFLTPLLAMEYDVQEIQHYWSGVSSLFVVLS", "text": "FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX (By similarity). SIMILARITY: Belongs to the NnrE/AIBP family."}
{"protein": "MTSLPLGVKVEDSAFGKPAGGGSGQAPSAAAATAAAMGADEEGAKPKVSPSLLPFSVEALMADHRKPGAKESSLAASESAQAAGGLTQPLGVPPGSLGAPDAPSSPRPLGHFSVGGLLKLPEDALVKAESPEKPERTPWMQSPRFSPPPARRLSPPACTLRKHKTNRKPRTPFTTAQLLALERKFRQKQYLSIAERAEFSSSLSLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPPAAFGLSFPLGSPAAVAAAAGASLYGASGPFQRAALPVAPVGLYTAHVGYSMYHLT", "text": "FUNCTION: Acts as a transcriptional repressor. May play a role in limb- pattern formation. Acts in cranofacial development and specifically in odontogenesis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Msh homeobox family."}
{"protein": "MSAAIEKETGMLDVGKHCAYCRQLDFLPFHCSFCNEDFCSNHRLKEDHHCRWLLEHEEVHKTEKSPSKSRDGSSSNDEAYFKSLLPERASVRIQRVSETREPLRGSNTAKVSSTLNSKTLDKIFKFFQRNEKRKSNNKSKKNFGSSSNKIIQLANLKKIAKGDPKIPMQNRIYIWCYLVDGDETDIAKEDTRMPLYINKMWPVGRAMDYLSIQLNVKSSTLTNSSSNDKFQLCKLKEGKQVSFYNIGASLRVTNEIKDLDTLYLVHNNADEKSN", "text": "FUNCTION: Promotes efficient arsenite-induced clearance of stress granules (SGs) (PubMed:29804830). May have a role in the ubiquitin- proteasome system (UPS) protecting cells from metalloid-induced proteotoxicity (PubMed:24121501, PubMed:24297164). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MELPLGSDLARLVRVWRALVDHRLKPLELTQTHWVTLHNIYHLPPGQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHVCAHDRRAKRIMLTESAEPIIQAVDGVISHTRSEVLFGITPEQVDELALLVARLEKNILALHENQA", "text": "FUNCTION: Transcription regulator that can specifically activate or repress expression of target genes. SIMILARITY: Belongs to the SlyA family."}
{"protein": "MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQEKRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGSHYSYSENRVEKDGLILTSRGPGTSFEFALKIVEVLVGKEVADQVKAPLVLKD", "text": "FUNCTION: Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox- sensitive chaperone and protease. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Has been described as a protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. But this function is rebuted by other works. As a protein deglycase, repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin. Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels. Displays a very low glyoxalase activity that may reflect its deglycase activity. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells. In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal- binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity. In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Cytoplasm Nucleus Membrane raft Mitochondrion Endoplasmic reticulum Note=Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage. Membrane raft localization in astrocytes and neuronal cells requires palmitoylation. SIMILARITY: Belongs to the peptidase C56 family."}
{"protein": "MSPNLQEGARLVEGKPSSTSFSIESILGLDQKKDDAPSMKPHRPWADTCSSLGKDANLRLHVPSFPNGISFPHPGDHPMPEERAMKYENYFSASERASLKRELNWYRGRRPRTAFTQNQVEVLENVFRVNCYPGIDIREDLARKLNLEEDRIQIWFQNRRAKLKRSHRESQFLMA", "text": "FUNCTION: Required for the normal development of the forebrain, eyes and other anterior structures such as the olfactory placodes and pituitary gland. Possible transcriptional repressor. Binds to the palindromic PIII sequence, 5'-AGCTTGAGTCTAATTGAATTAACTGTAC-3'. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ANF homeobox family."}
{"protein": "MSAQTGSAAAIGDKGKGKSAAEPQDVTMGEGGDDSSSEEEVDDDAPPPAEEVEEEASDNEIDKSNIIQGRRTRGKQIDFAAAAKDLPADDDEDEDDDFQSEGEEDDEMGGN", "text": "FUNCTION: Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CHZ1 family."}
{"protein": "MSRRKENEEVDKQTRIAIVSDDKCKPKRCRQECKKTCPVVRMGKLCIEVTPTSKIASLSEELCIGCGICVKKCPFEAITIINLPSNLEKHTTHRYSKNSFKLHRLPIPRPGEVLGLVGQNGIGKSTALKILAGKQKPNLGKYANPPDWTEILSYFRGSELQNYFTKILEDNLKALVKPQYVDQIPKAVRGAVGDLLDKKDERELQTKICEMLDLSHIRDREIAQLSGGELQRFAIAMVCIQNADIFMFDEPSSYLDVKQRLNAALTIRSLLHPTKFIIVVEHDLSVLDYLSDFICCLYGVPGCYGVVTMPFSVREGINIFLDGFVPTENMRFRTESLTFKVSESATEEEIKRMNHYVYPAMVKTLGKFELTVEKGHFSDSEILVLLGENGTGKTTFIRMLAGNLQPDGEVELPMLNISYKPQKISPKFQNHVRHLLHDKIRDAYVHPQFIADVMKPMKIEEIMDQEVQNLSGGELQRVALVLCLGKPADVYLIDEPSAYLDSEQRLVAAKVIKRYILHAKKTGFVVEHDFIMATYLADRVIVIEGQPSVKTTAFSPQSLLNGMNRFLELLGITFRRDPNNFRPRINKNNSVKDTEQKRSGQFFFLEDEACN", "text": "FUNCTION: Plays a role in translation initiation and quality control of translation (PubMed:16291791, PubMed:17392269, PubMed:29861391). Together with pelo and HBS1, is required for 48S complex formation from 80S ribosomes and dissociation of vacant 80S ribosomes (PubMed:17392269). Stabilizes core components of eIF3 complex promoting their assembly into translation initiation-competent complexes (PubMed:17392269). Together with pelo and HBS1, recognizes stalled ribosomes and promotes dissociation of elongation complexes assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and to degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway (PubMed:25128630). Plays a role in the regulation of mRNA turnover (By similarity). Plays a role in quality control of translation of mitochondrial outer membrane- localized mRNA (PubMed:29861391). As part of the Pink1-regulated signaling, ubiquitinated by Cnot4 upon mitochondria damage; this modification generates polyubiquitin signals that recruits autophagy receptors to the mitochondrial outer membrane to initiate mitophagy (PubMed:29861391). Required in the wing disk for cell division and growth as well as cell survival (PubMed:16291791). During muscle embryogenesis, required for the recruitment of Pak to muscle attachments in the embryo, hence may play a role in proper muscle morphogenesis and proper guidance and targeting of subsets of myotubes (PubMed:18996366). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family."}
{"protein": "MYSANRSHRAETRNRSKDELRKVINSLEKVRRWEKKLVLIKDTNIRIYKWVPVSAQNIMAPPKIKEVKEVDEESNQVPSAENSQDSTSVTQPPPQFDINEDSNFSTGDHFDSDSNQTFEPQNYQGGATGSTDFSSMRDAEMTSKQP", "text": "FUNCTION: Required for the terminal differentiation of seam cells, and the differentiation of distal tip cells important for normal somatic gonad and germ cell development. Plays a role in the Wnt signaling pathway, regulating the expression of beta-catenin homologs wrm-1, bar- 1 and sys-1, and the localization of wrm-1 and the wnt signaling pathway component pop-1 during asymmetric cell division of seam cells and the Z-cell lineage of the somatic gonad, respectively. May have a pro-apoptotic role, possibly linked to the negative regulation of expression of anti-apoptotic factor ced-9. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BCL7 family."}
{"protein": "MDDAGSSGGSGGFRPGVDSLDEPPNSRIFLVISKYTSESVLREHFSPFGDIQDIWVVRDKHTKESKGIAFVKFARSSQACRAMEEMHGQCLGPNDTKPIKVFIAQSRSSGSHRDVEDEELTRIFVMIPKSYTEEDLREKFKVYGDIEYCSVIKNKVTGESKGLGYVRYLKPSQAAQAIENCDRSFRALLAEPKNKVLESPEQDYYSSVRQETLGHEPRGNLFPFVGEQQSEFSTFDKNDSRGQEAISKRLSVASRVPFTEEQLFSIFDIVPGLEYCEVHRDPYLNYGHGVVQYFNVASAVYAQYKLHGFQYPPGNRIAVSFLDDGSNSADLIRKMATQMVAAQLASTVWSNPSHQQFLQFGGSAGSQVPQIQTDVVLPSCRKKAPPETPVKERLFIVFNPHPLPLDVLEDIFCRFGNLIEVYLVSGKNVGYVKYADRMSANDAITTLHGKILNGVRLKVMLADSPREVSKKRQRTY", "text": "FUNCTION: RNA-binding protein with binding specificity for poly(C). May play an important role in neural development. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. May shuttle between cytoplasm and nucleus."}
{"protein": "MAAKSDGGGVGVGFAQLHNLDEAVGSGGEEDGEPGGGGCGGGGDGSEPGESSSMHICHCCNTSSCYWGCRSACLRSLLGRKPRRSAAADGGDQPLQPPAAPGAGRQPPTPSAARPEPPPPQVERPWLDCLWIVLALLVFFGDVGTDLWLALDYYRKGDYVYFGLTLFFVLVPSLLVQSLSFRWFVQDYTGGGLGAVEGLTSRGPPMMGAGYVHGAARGGPGVRVSPTPGAQRLCRLSVWIWQSVIHLLQMGQVWRYIRTMYLGIQSQRRKEHQRRFYWAMMYEYADVNMLRLLETFLESAPQLVLQLYIMLQKNSAETLPCVSSVTSLMSLAWVLASYHKLLRDSRDDKKSMSYRGAIIQVFWRLFTISSRVISFALFASIFQLYFGIFVVVHWCAMAFWIIHGGTDFCMSKWEEILFNMVVGIVYIFCWFNVKEGRTRYRMFAYYTIVLTENAALTFLWYFYRDPETTDSYAVPALCCVFISFVAGIAMMLLYYGVLHPTGPRAKILASSCCAELLWGIPLPPDVEPMAPEIPGYRGTQVTPTRAVTEQQEDLTADTCLPVFQVRPMGPPTPLGRPYLPEGPLIKIDMPRKRYPAWDAHFVDRRLRRTINILQYVTPTAVGIRYRDGPLLYELLQYESSL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the XK family."}
{"protein": "MRSIASKVLVIGVVVVLAFFVTQYVLLNTTVFNSIMERKKEEAKHLVESVYGILERAYEMEQKGELTREQAQELAKSLIGKIRYDDNNYFWINDTHPRMVFHPIKPEMNGQDLSNYKDPNGVYLFNEMVKVAKEKGEGFVSYSWPKAGSDKPEPKISYVKLFEPWGWIVGTGIYVDDVKVTVGNLIFRNVLTVSVIGIAVIIMIFFYGRVLSRKTKAVLSALEKISSGDLSVSVDIKSKDEFGLIAQKLNETVGNLRKMVQEIDKSQDEVERVSEELFALSQQLRSALEEIARASDTISKEVQNASASIEEVTSGSEEVSANSQNISKLIQEISENADNIADFARNGQRVLEEAVKKVEDVSENSRETADVVSNVTESARNIEEIVRTIQSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESQKATEEISQILENIREGVERTNEMSKKNVEITKDARRLVEESYESFNQIVTRIEDLAARIEGIAASAQELSAASEEMSSALDAVAKTTTTVADEVEEVSENITEQEKAAKRIADIGTELKKLSDELKEDVERFKI", "text": "FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family."}
{"protein": "MKEACSSSSHVPVSDSKYILKSELLSLLKTYNCYHEGRSFQLRHREEEGTLIIEGLLNIAWGLRRPIRLQMQDDRERVHLPSATWVPERLSYLQKEASPQDSKVPTEEPGTQPANKAEVSGDSSGALEGEEEEVPQLMRTKSDASCIIQRRSKSRAPSEAQKIRRHRFSINGHFYNHKTSVFTPAYGSVTNVRVNSTMTTQQVLTLLLNKFRVEDGPSEFALYTVHESGEQTKLKDCEYPLISRILHGPCEKIVKIFLMEADLSEEVPHDVAQYIKFEMPVLDSFVEKLKEEEEREIIKLTMKFQALRLTMLQRLEQLVEAK", "text": "FUNCTION: Potential tumor suppressor. May act as a KRAS effector protein. May promote apoptosis and cell cycle arrest."}
{"protein": "MDDFSSISLLSLSMLIGCYVAGTIPLAVNFSEEKLKLVTVLGAGLLCGTALAVIIPEGVHALYEEMLEGVHNHGHGQVEAEVSEQKVAEGVVRPSGEHGHGHEQLHAYIGISLVLGFVFMLLVDQIGSAHMHSSDDPEAARAASSKITTTLGLVVHAAADGVALGAAASTSQTSVQLIVFVAIMLHKAPAAFGLVSFLMHAGLERNRIRKHLLVFALAAPVLAMVTYVGLSQSSKEALSDVNATGVAMLFSAGTFLYVATVHVLPEVGGMGGHSHSPGGSAGKGLSKLEVGALVLGCLIPLVLSIGHQH", "text": "FUNCTION: Has dual functions as membrane-bound androgen receptor and as an androgen-dependent zinc transporter both of which are mediated through G protein activation and are required for the androgen- dependent apoptotic response. Upon androgen binding, mediates apoptosis by directly activating a stimulatory G protein that leads to increased cAMP levels and MAP kinase activity and which is accompanied by increased intracellular free zinc levels (By similarity). May play a role in the proper zinc modulation during egg activation (PubMed:32973303). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm, perinuclear region Golgi apparatus, trans-Golgi network membrane Mitochondrion Nucleus. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MSSLPKTDFNVSKYQLIAQKREANAVEIEAALEVVREFIIKKKLILYGGIAIDYALHLKGSSIYPEGERPDFDMFSPNHVEDAYELADILYEKGFKQVGTVRAIHVQTMRVRTDFVWVADLSYMPPNIFDTIPTLTYKNLKIIHPDYQRAGLHLAFCFPFDNPPREDVFSRFKKDLQRYNLIEKYYPIPVVPVKTTYESKTFSVPFKQVAIHGFAAYALLYQTLNELRITCKAPEWKTEFPQPSYSYHKNDKNITLTVDMPRAYPSLVLATYNPEEVIKEMGLHLTEICEPYMDYSPPIFKTKDIHFFSTMFKELAISMIQDNIIVVSPQYLLLYFLYGAFATPADKSLFLFYYNATLWILEKADSLLNMIQKQTSPEEFTRFANTSPFVLTTRVLSCSQERCTFSPAYRISLANDVQQSQLPLPKTHFLSNFLPDISTLPYNYYPGKGKDRPTNFSYEKNLLFNIGGKCIPFAM", "text": "FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic subunit family. Highly divergent."}
{"protein": "MTAKIFSLDEVSKHKTKSDLWVVIHNKVYDITRFVVEHPGGEEVLVDEGGKDATEAFEDIGHSDEAREMLEEYLIGSLDEASRTKEYNVNVIRAGELPEEKKGSSLRIILPALAIIGALVYKYVIVPKAHQ", "text": "FUNCTION: Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side Microsome membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the cytochrome b5 family."}
{"protein": "MVSVPTAWCSVALALLVALHEGKDQAAATLEQPASSPRARAAHLRLRRCSCSSWLDKECVYFCHLDIIWVNTPGQTAPYGLGNPPRRRRRSLPGRCECSSARDPACATFCHQRSRADAVGVPGSQSSADAFQAGKTWATPGELLRTLRDISAAKTHFAKRQQEATREPRTTHSRHRKR", "text": "FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the endothelin/sarafotoxin family."}
{"protein": "ELVTLSGAHTIGQAR", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. SUBCELLULAR LOCATION: Secreted Secreted, cell wall. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MSIRTPPRLLELAGRSLLRDEALAISTLEELPTELFPPLFMEAFSRRHCEALKLMVQAWPFLRLPLGSLMKRPCPETFQAVLDGLDALLTHRVRLRRWKLQVLDLQDVSENFWMVWSEAMARRCLPNAMMNRKPLQDCPRMRGQQPLTVFIDLCLKNRTLDEYFTCLFLWVKQREGLVHLCCKKLKMLGMLFHNIRNILKTVNLDCIQEVEVNCNWTLPVLAEFTPYLGQMRNLRKLVLSDIDSRYISPEQKKEFVTQFTTQFLKLRCLQKLYMNSVSFLEGHLDQMLSCLKTSLNILAITNCVLLESDLKHLSKYPSIGQLKTLDLSGTRLANFSLVPLQVLLEKVAATLEYLDLDDCGIVDSQVNAILPALSRCFELTTFSFRGNPISTATLENLLCHTIRLNNLCLELYPAPRESYDVRGIVCRSRFAQLGAELMGRVRALREPERILFCTDYCPQCGNRSLYDLEVDRCCC", "text": "SIMILARITY: Belongs to the PRAME family."}
{"protein": "MSYESGRSSSSSESTRPPTLKEEPNGKIAWEESVKKSRENNENDSTLLRRKLGETRKAIETGGSSRNKLSALTPLKKVVDERKDSVQPQVPSMGFTYSLPNLKTLNSFSDAEQARIMQDYLSRGVNQGNSNNYVDPLYRQLNPTMGSSRNRPVWSLNQPLPHVLDRGLAAKMIQKNMDARSRASSRRGSTDISRGGSTTSVKDWKRLLRGAAPGKKLGDIEAQTQRDNTVGADVKPTKLEPENPQKPSNTHIENVSRKKKRTSHNVNFSLGDESYASSIADAESRKLKNMQTLDGSTPVYTKLPEELIEEENKSTSALDGNEIGASEDEDADIMTFPNFWAKIRYHMREPFAEFLGTLVLVIFGVGGNLQATVTKGSGGSYESLSFAWGFGCMLGVYVAGGISGGHINPAVTISMAIFRKFPWKKVPVYIVAQIIGAYFGGAMAYGYFWSSITEFEGGPHIRTTATGACLFTDPKSYVTWRNAFFDEFIGASILVGCLMALLDDSNAPPGNGMTALIIGFLVAAIGMALGYQTSFTINPARDLGPRIFASMIGYGPHAFHLTHWWWTWGAWGGPIAGGIAGALIYDIFIFTGCESPVNYPDNGYIENRVGKLLHAEFHQNDGTVSDESGVNSNSNTGSKKSVPTSS", "text": "FUNCTION: Channel protein that mediates glycerol entry under ethanol stimulation (PubMed:12832087). Does not seem to mediate glycerol uptake under standard conditions (PubMed:12832087). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MELEVRHLRALCAIADAGSLHRAARRLGVAQPTLSTQLTRIEQALGGPLFTRERTGCRPTPLGRTVLGRARPLLTDMNTLVREARAAAAGGDSRLRVGSTASRALAGWLRRLRRPGLEPTLQMDVSANALLRRVTDGQLDVAFVHEVEGCALHIPEDLRLRVLVEREPQFVMLPADHPAAARPVVRLADLADDRWMVDPTVDGEWDGVHRMLRAVGLNPRVLHGDYHTAASLVATGEVVTVCQPSSQSRPDTAVRRLYGDPLGVRLLLAGTRAELDAVFPALEDAYWEAARQSTAYREWLEGGGIRTLPRCPVAATGGGRVSCGRAEGSRSRRPRDVAPPRPIG", "text": "FUNCTION: Transcriptional activator of the gene (snpA) for the small neutral protease. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MAKPEPDVVVPEGDPAKGAKLFKSKCAQCHTINKGGSVKQGPNLFGFYGRKSGSTDYAYSDANKNSGIVWSDKHLFVYLVNPKQYIPGTKMVFAGLKKEQDRADLIAYLKEASSK", "text": "FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Note=Loosely associated with the inner membrane. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MAQQLTGEQTLDHYEDSTQASIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSTWMILVVIASVFTNGLVLAATMRFKKLRHPLNWILVNLAVADLAETIIASTISVVNQIYGYFVLGHPLCVIEGYIVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLATVGIVFSWVWAAVWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIFPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYAFHPLVASLPSYFAKSATIYNPIIYVFMNRQFRNCILQLFGKKVDDSSELSSTSKTEVSSVSSVSPA", "text": "FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MQTAATSTFFANPHVKHLPGPFLRPSPHYGALVHLPSFRNKTPISIAMAASPSPPPLQELTITRPDDWHLHLREGDVLAAVLPHSAMHFGRAIVMPNLKPPVTTTARALEYREEILRALPPGSNFVPLMTLYLTDNTSPEEIKLAKKSGVVFAVKLYPSGATTNSQDGVTDIFGKCLPVLEEMARQEMPLLVHGEVTDQHVDTFDREKVFIEKILAPLVQRLPQLKIVMEHITTMDAVNFVESCKEGHVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKRETHRQAIVSAVTSGSKQYFLGTDSAPHDKRRKECSCGCAGIYSAPVALSLYAKVFEQAGALDKLEAFTSFNGPDFYGLPRNTSKIVLRKSAWKVPDTYSYSSGEIVPMFTGNTLEWLPSDQLEE", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily."}
{"protein": "MLRAPRTLAPATAQPTKSLPALNPTELWPSGLSSPQLCPATTATTYYTSLYTQTVPSSVALGTCLDATPHGPEGQIVRCAPAGRLPAKRKLDLEGIGRPTVPEFRTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKSKNNIQWVGRELFEDPTRPSRQQQLGQELKELMNAEQTLDQLIQSCSLSFKHLTEDNANKKLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRAEENLQIYLKSTQGPIEVYLCPEEGQEPDSPAKEALPSTSALSPIPDCAQPGCSTDSGIAETIEPSVLIPQPIPPPPPPPLPPAPSLVPLEATDNMLELSHPLLQQTEDQFLSPILAANSPLISFSPPLDQDEYLWGMDEGEGISDLFDSYDLGDLLIN", "text": "FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the E2F/DP family."}
{"protein": "PAGPFRIPKCRKEFQQAQHLRACQQWLHKQAMQSGSGPSWTLDDEFDFEDDMENPQGPQQRPPLLQQCCNELHQEEPLCVCPTLKGASKAVKQQVRQQLGQQGQQGPHLQHVISRIYQTATHLPKVCNIRQVSVCPFKKTMPGPS", "text": "FUNCTION: This is a 2S seed storage protein. SIMILARITY: Belongs to the 2S seed storage albumins family."}
{"protein": "MVAQGFTVDLKKPLVFQVGHLGEDYEEWVHQPIATKEGPRFFQSDFWEFLTLTVWWAVPVIWLPVVVWCISRSVSMGCSLPEIVPIVVMGIFIWTFFEYVLHRFVFHIKTKSYWGNTAHYLIHGCHHKHPMDHLRLVFPPTATAILCFPFWNIAKAISTPSTAPALFGGGMLGYVMYDVTHYYLHHAQPTRPVTKNLKKYHLNHHFRIQDKGFGITSSLWDIVFGTLPTTKAPRKEQ", "text": "FUNCTION: Fatty acid 2-hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long-chain fatty acids (VLCFA). Probably involved in the resistance response to oxidative stress. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MIKPDGVQRGLVGEIISRGDFAIDIGR", "text": "FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. SIMILARITY: Belongs to the NDK family."}
{"protein": "MIKRLPDDFIFGGATAAYQAEGATTIDGKGAVAWDRYLKDNYWYTAEPASDFYHQYPVDLALAEQFGINGIRISIAWSRIFPEGFGEVNAKGVAFYHSLFAECHKHHVEPFVTLHHFDTPEALHSRGDFLNRENIDHFVAYAAYCFKEFPEVTYWTTFNEIGPIGDGQYLVGKFPPGISYDLAKVFQSHHNMMLAHARALVHYKEQAYPGEIGIVHALPTKYPLDPKKPGDVLAAELDDIIHNKFILDATYLGQYSEKTMAGVKHILAENGGSLDLRPEDFELLQAAKDLNDFLGINYYMSDWLRAFDGETEIIHNGKGEKGGSKYQIKGVGQRVFDVDVPRTDWDWMIYPQGLYDQIMRIKADYPGYKKIYITENGLGYKDTCIDGRIDDDARIDYIKQHLAVIADAISTGANVKGYFIWSLMDVFSWSNGYDKRYGLFYVDFETQKRYPKKSAYWYQQLAATKTISM", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MNIVDQQTFRDAMSCMGAAVNIITTDGPAGRAGFTASAVCSVTDTPPTLLVCLNRGASVWPVFNENRTLCVNTLSAGQEPLSNLFGGKTPMEHRFAAARWQTGVTGCPQLEEALVSFDCRISQVVSVGTHDILFCAIEAIHRHTTPYGLVWFDRSYHALMRPAC", "text": "FUNCTION: Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family. RutF subfamily."}
{"protein": "GIWDTIKSMGKVFAGKILQNL", "text": "FUNCTION: Antimicrobial peptide with activity against Gram-negative and Gram-positive bacteria (MIC=13 uM against E.coli, MIC=25 uM against S.aureus) and fungi (MIC=25 uM against C.albicans) (PubMed:15556063). Also shows hemolytic activity (HC(50)=50 uM) (PubMed:15556063). In vitro, shows moderate inhibitory activity against HIV (PubMed:20086159). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MSSTAVPRPKPWETSASLEEPQRNAQSLSAMMTSNQQDSRPTEESNNSNSASESAPEVLPRPAALNSSGTYGESNTIPGIYGNSNYGIPYDNNPYSMNSIYGNSIGRYGYGGSYYGNNYGSFYGGGYGAGAGYGMNNGSGLGESTKATFQLIESLIGAVTGFAQMLESTYMATHNSFFTMISVAEQFGNLKEMLGSFFGIFAIMKFLKKILYRATKGRLGIPPKNFAESEGSKNKLIEDFQKFNDSGTINSNEKATRRKISWKPLLFFLMAVFGFPYLLNKFITKLQTSGTIRASQGNGSEPIDPSKLEFARALYDFVPENPEMEVALKKGDLMAILSKKDPLGRDSDWWKVRTKNGNIGYIPYNYIEIIKRRKKIEHVDDETRTH", "text": "FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX21 receptors (PubMed:8858167, PubMed:20154681). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (PubMed:20154681). Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:20154681). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peroxin-13 family."}
{"protein": "MKKKQQQHPGGGTDPWPHGAPVGGAPPCLGSCKRRIPLLPFLRFSLRDYGFCMATLLVFCLGSLFYQLSGGPPRFLLDLRQYLGNSTYLDDHGPPPSKVLPFPSQVVYNRVGKCGSRTVVLLLRILSEKHGFNLVTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSRFGGDQPVYINIIRDPVSRFLSNYFFRRFGDWRGEQNHMIRTPSMRQEERYLDINECILENYPECSNPRLFYIIPYFCGQHPRCREPGEWALERAKLNVNENFLLVGILEELEDVLLLLERFLPHYFKGVLSIYKDPEHRKLGNMTVTVRKTVPSPEAVQILYQRMRYEYEFYHYVREQFHLLKRKLGLKSRVSGPPVRPQFFIPTPLETEEPIDDEEQDDEKWLEDIYKR", "text": "FUNCTION: Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N- resulfated heparin (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 3 family."}
{"protein": "MEPSATPGAQPGVPTSSGEPFHLPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFLIALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGQALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAVMVPQAAVMECSSVLPELANRTRLFSVCDEHWADELYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSEQLEAQHQGLCTEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVLKRVFGMFRQASDREAVYACFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSCCLPGLGPGSSARHKSLSLQSRCSVSKVSEHVVLTTVTTVLS", "text": "FUNCTION: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSKSLKKLVEESREKNQPEVDMSDRGISNMLDINGLFTLSHITQLVLSHNKLTTVPPNIAELKNLEVLNFFNNQIEELPTQISSLQKLKHLNLGMNRLNTLPRGFGSLPALEVLDLTYNNLNENSLPGNFFYLTTLRALYLSDNDFEILPPDIGKLTKLQILSLRDNDLISLPKEIGELTQLKELHIQGNRLTVLPPELGNLDLTGQKQIFKAENNPWVTPIADQFQLGVSHVFEYIRSETYKYLYGRHMQANPEPPKKNNDKSKKISRKPLAAKNK", "text": "FUNCTION: Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro (By similarity)."}
{"protein": "MLKKYLISLDKDIQRRELFFSQKNTEDFQVFSAINTMQKDWDELAAIFNIEQFKAHYFRNVTKGEIGCTLSHLSVYQKIVEDNDIAEDSYALVCEDDALFHSDFQQNLTALLSEKLEAEIILLGQSKINDFNDFDLEINYPTTFSFLCKKTGDVNYAFPYKSYFAGTVGYLIKKSAARRFIQQISQNKPFWLADDFLLFEQNFNIRNKVVRPLIVIENPVLISNLESVRGSLSNNLLKKLMKYPLKKIFAIKKNLAN", "text": "SIMILARITY: Belongs to the glycosyltransferase 25 family."}
{"protein": "METIIESRQRINSPGVLPPPLSPLIVDVTPKERASISNVANILLKAFGHYEHPDFISALHLNAFQLLPERIAGILSRFGTDFSRHQYGALVFRGLTEVDQEALGPTPPSWKETDYSKLVKYGFICSLLHGAIPSKPVQYYAQRKGGGLLHAVIPDEKMSHTQTGSGSRTDLFVHTEDAFLFNQADFLSFLFLRNEEQVPSTLYSIRSHGDTNAIMAELFKPIYKCPKDANYADDENAGEEVTTSILYGNRERPFIRFDAAEQIYNEKAGQTPEAMHNLVRFWDEAKQLIYNDFVPDSGDLIFVNNHLCAHGRNSFVAGYRNENGQLVKCERRLMLRMMSKTSLINIQSVTQLNDPYFIMEEHYGKLFHSQQ", "text": "FUNCTION: Alpha-ketoglutarate-dependent dioxygenase that in vitro catalyzes the regio- and stereoselective hydroxylation of L-lysine, leading to (4R)-4-hydroxy-L-lysine. SIMILARITY: Belongs to the clavaminate synthase family."}
{"protein": "GDGTGPGPGP", "text": "FUNCTION: Has antifungal activity. Inhibits mycelial growth of wood rotting fungi P.chrysosporium MTCC 787, S.commune ITCC 3751, G.trabeum MTCC 355, P.agaricans ITCC 761, C.versicolor MTCC 138, P.versicolor ITCC 13, P.placenta MTCC 144 and P.friabilis ITCC 335. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MSESLHLTRNGPILEITLDRPKANAIDAKTSFAMGEAFLNFRDDPELRVAIITGGGEKFFSAGWDLKAAAEGEAPDADFGPGGFAGLTEIFDLDKPVIAAVNGYAFGGGFELALAADFIVCAENASFALPEAKLGIVPDSGGVLRLPKLLPPAIVNEMVMTGRRMSAEEALRWGVVNRVVSQSELMESARELAQQLVNSAPLAIAALKEIYRATSEMPVEEGYRYIRSGVLKHYPSVLHSEDALEGPQAFAEKRDPVWKGR", "text": "FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "GKLQAFLAKMKEIAAQTL", "text": "FUNCTION: Inhibits growth of Gram-positive (S.aureus, B.subtilis) and Gram-negative (E.coli, P.aeruginosa) bacteria and fungi (C.albicans). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 05 subfamily."}
{"protein": "MSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEDKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY", "text": "FUNCTION: Its physiological role is not yet clear. SIMILARITY: Belongs to the acylphosphatase family."}
{"protein": "MKAGCSIVEKPEGGGGYQFPDWAYKAESSPGSRQIQLWHFILELLQKEEFRHVIAWQQGEYGEFVIKDPDEVARLWGRRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVMPNYPFINIRSSGVVPQSAPPVPTASSRFHFPPLDSHSPTGDVQPGRFSASSLSASGPESGVTTDRKVEPSDLEDGSASDWHRGMDFMPSRNALGGGAVGHQKRKPDILLPLFTRPAMYPDPHSPFAISPVPGRGGVLNVPISPALSLTPTMFSYSPSPGLSPFTSSSCFSFNPEEMKHYLHSQACSVFNYHLSPRTFPRYPGLMVPPLQCQMHPEEPSQFSIKLQPPPAGRKNRERVESREEAVRGSVPASAPVPSRIKVEPATEKDPDSLRQSTQGKEEQTQEVDSMRSRTIEEGKGTGFAHPSPTWPSVSISTPSDEPLEGTEDSEDRSVREPGVPEKKEDALMPPKLRLKRRWNDDPEARELNKTGKFLWNGAGPQGLATTATAAADA", "text": "FUNCTION: Transcriptional repressor that contribute to growth arrest during terminal macrophage differentiation by repressing target genes involved in Ras-dependent proliferation. Represses MMP1 promoter activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family."}
{"protein": "MSEDVKKYFTTGEFSKLCRVKKQTLFHYDEIGLFSPEIKKENGYRYYSYHQFETFQVISLFKELGVPLKEIKCLIKGKTPDKILHVLKEKSIEIDKKINELKQLQTILQTKVTLTEQALETDFSSISFEYLNEETFMLSRKTLNLPERKYVAAISELIHEVQQYELDEGYPIGGIFAREQILEKDFYNYSYFYIKVKDGAENINYHVRPKGLYAVGYEIGGNTEEAYRRIIEFIERNGMQIGENAYEEYMLDEMVVDGYENTYAKILLQVKEV", "text": "FUNCTION: Activates transcription of the blt gene in response to structurally dissimilar drugs."}
{"protein": "MAIDGSGVATPAPSGITVIIVGLGPTGLAAAIECHRRGHKVICFEKNPKSYRLGDLISVTGNAVRVLQEWGNGSVIKELQAFQCNLDTLEVYNETGDLKLSAPYNATQAKDEYMLRRSRLLDIFLQHLKSLGVEIHLGIQVADYWETESSAGVTVGGEKIVGDCVVVADGVHSKGRPQVSGEPFALEATDGIAFRAFFNASEISQDPEASWILRDAGEKDCFKTFYGKGLVMMVGTAENHEYVFWSCGHKENVMAHPSSVATVLDLIRDWPVSTRLAPLISKTPGDNCLNQTLYTRPPLKKWVSSNGRMIVLGDAAHPFLPHAGQGANQGIEDGAVLALCLEITSKKDVPLALRVTEKLRYQRVAAIQQRGVEARDQSLNVDWGNGGFSKKLTLHPAWLHDHDCIKQVYEEFDKAADAVTKGHEHTFGGIPVG", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:20722388). The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F (PubMed:20722388). The reverse prenyltransferase notF then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core (PubMed:20722388). Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG, to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC for normal prenylation at C-7 to produce 6- hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (PubMed:20722388). As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH cytochrome P450 monooxygenase or the notD FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation- initiated pinacol-like rearrangement catalyzed by the notB FAD- dependent monooxygenase leading to the formation of notoamide C and notoamide D (PubMed:22188465). On the other hand notoamide S is converted to notoamide T by notH (or notD), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (+)-notoamide T (Probable). To generate antipodal (-)- notoaminide T, notH' (or notD') in Aspergillus versicolor is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD (or notH) likely catalyzes the oxidative pyran ring formation to yield (+)- stephacidin A (Probable). The FAD-dependent monooxygenase notI is highly similar to notB and is predicted to catalyze a similar conversion from (+)-stephacidin A to (-)-notoamide B via the 2,3- epoxidation of (+)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
{"protein": "MPRLVLVSFLFLAIFSVFIGGFAKSKCPRNEIFTRCHAACQPSCARLARKPFCIKICKPGCICTSGYLRNKNNVCVPRSRCFSGRLL", "text": "FUNCTION: Antifibrinolytic and antimicrobial serine protease inhibitor. Inhibits trypsin, plasmin and microbial serine proteases but not chymotrypsin, thrombin and elastase. Inhibits the plasmin-mediated degradation of fibrin to fibrin degradation products. Also binds to bacterial and fungal surfaces and exhibits antimicrobial activity against fungi as well as Gram-positive and Gram-negative bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain- containing) family."}
{"protein": "MSATEPHTDQPRTLADLCKVCNIPMHSLQLPCAFCKKTVCTAEIYAFQYKDLFVVWRHGFPHAACALCLELHGQINYRRHRDRACLWETVEQECGKPLEEIFIRCWLCHKPLCNVEKQRHVDYNRRFHCVRGYWKGRCLHCWKP", "text": "FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin- protein ligase and modulates its activity. Sequesters tumor suppressor TP53 in the host cytoplasm and modulates its activity by interacting with host EP300 that results in the reduction of TP53 acetylation and activation. In turn, apoptosis induced by DNA damage is inhibited. E6 protects also host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the papillomaviridae E6 protein family."}
{"protein": "MEQIWLLLLLTIRVLPGSAQFNGYNCDANLHSRFPAERDISVYCGVQAITMKINFCTVLFSGYSETDLALNGRHGDSHCRGFINNNTFPAVVIFIINLSTLEGCGNNLVVSTIPGVSAYGNATSVQVGNISGYIDTPDPPTIISYLPGLLYKFSCSYPLEYLVNNTQLASSSAAISVRENNGTFVSTLNLLLYNDSTYNQQLIIPSIGLPLKTKVFAAVQATNLDGRWNVLMDYCYTTPSGNPNDDIRYDLFLSCDKDPQTTVIENGRSQRGRFSFEVFRFVKHKNQKMSTVFLHCVTKLCRADDCPFLMPICSHRERRDAGRRTTWSPQSSSGSAVLSAGPIITRSDETPTNNSQLGSPSMPPFQLNAITSALISGMVILGVTSFSLLLCSLALLHRKGPTSLVLNGIRNPVFD", "text": "FUNCTION: Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ. SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1, secreted form]: Secreted, extracellular space, extracellular matrix. SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1]: Cytoplasmic vesicle membrane; Single-pass type I membrane protein."}
{"protein": "MAGGEAGVTLGQPHLSRQDLATLDVSKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD", "text": "FUNCTION: Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily."}
{"protein": "MVPRDRVNAAAAGGGGEGRLVQSGIVNKKCDKKAPKRIHKSEREKLKRDKQNDLFNELGNLLEPDRQNNGKACVLGETTRILKDLLSQVESLRKENSSLKNESHYVALERNELHDDNSMLRTEILELQNELRTRMEGNPVWSHVNTRPALRVPYPTTGVFPVQHLPHLPVTTTAAFPQQLPVIIEQHYAATPRELQLFPESATSEDSEPSQEHGISDHVTRPQPRYPTPTATLPVNLFPVFPGRQDQQCSSGTSGTNEEDRIGRS", "text": "FUNCTION: Transcription factor that plays a positive role in salt stress tolerance. Interacts with TIFY11A/JAZ9 and binds to the promoter of some potassium ion transporter genes to regulate potassium homeostasis during salt stress. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bHLH protein family."}
{"protein": "ADIENGERIFTANCAACHAGGNNVIMPEKTLKKDALEANGMNAVSAITYQVTNGKNAMPAFGGRLSDSDIEDVANYVLSQSEQGWD", "text": "FUNCTION: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily."}
{"protein": "MNDADVSKQIQQMVRFIRQEAEEKANEISVSAEEEFNIEKLQLVEAEKKKIRQEYERKEKQVEIRKKIEYSMQLNASRIKVLQAQDDLVSNMMEAASKEVLNVSRDHNSYKKLLKGLIVQSLLRLKEPAVLLRCRKDDHHLVESVLESAKEEYAQKLQVHPPEIIVDHHIYLPPGPGHHNAHGPSCSGGVVVASRDGKIVCENTLDARLDVVFRKKLPEIRKQLVSQVAA", "text": "FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity). SIMILARITY: Belongs to the V-ATPase E subunit family."}
{"protein": "MIIPWQELEEETLNNIVESFILREGTDYGQCELSLEQKKQALLSQIQQGTVVIVWSELHESIDIKDKMDLLK", "text": "SIMILARITY: Belongs to the UPF0270 family."}
{"protein": "MASNNDPTVISMIERHLCDLPETNTSDLKTLTEEAVLSFHNISYQETVQSGFPLRKKAYVIERLSNISGIMKPGLNAIMGPQDGSRSLLLDVLAARRDPRGLSGDILINGKPRPANFKCTSGYVPQNDVVLGTVTVRDNLEFSAALRLPVTITRDEKRRRINEVLELLHLNKEQNIKPRSKELRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVILVLRRMSKKGRTIIFSINQPQYSIFKFFDSLTLVASGKVMFHGPAQDALEYFRSAGYNYESHNNPADFFLDVINGGFSNILDTEEDGHEDDKYEELFERQYQVTGKLANMYAQSPLYSETRAILDQLLGEQKLERSSAVETTCVTPFCHQLKWIICQSFKNFKGFPWVTVIQAIITVILATAVGTAFRVLKNDCIEVQMRAGLLYLLTIFQCITSVSAGELFVIDRVRFLHEHTSGYYRVSSYFFGKLLAELIPRRLLPSTVFSLITYVIAGVKMSMKCFFTMICTIMVLAYSASSLPLSIGAGENAVAVPTLLVTIYFVFMLFFSGLSLYSGSFLPKLSWIQYFSIPHYGFRALLHNEFLGQNFCPEHNTEEVSRCHNYVICTGEEFLMIQGIDLSSWGFWENHLALVCTMIILLTITYVQLLQVKNIRNF", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily."}
{"protein": "MDTEFAILDEEKYYDSVFKELNLKTRSELYEISSKFMPDSQFEAIKRRGISNRKRKIKETSENSNRMEQMALKIKNVGTELKIFKKKSILDNNLKSRKAAETALNVSIPSASASSEQIIEFQKSESLSNLMSNGMINNWVRCSGDKPGIIENSDGTKFYIPPKSTFHVGDVKDIEQYSRAHDLLFDLIIADPPWFSKSVKRKRTYQMDEEVLDCLDIPVILTHDALIAFWITNRIGIEEEMIERFDKWGMEVVATWKLLKITTQGDPVYDFDNQKHKVPFESLMLAKKKDSMRKFELPENFVFASVPMSVHSHKPPLLDLLRHFGIEFTEPLELFARSLLPSTHSVGYEPFLLQSEHVFTRNISL", "text": "FUNCTION: Methylates DNA on the 6th position of adenine (N(6)- methyladenosine) (PubMed:25936839). N(6)-methyladenosine (m6A) DNA is involved in epigenetic transgenerational inheritance (PubMed:25936839). SIMILARITY: Belongs to the MT-A70-like family."}
{"protein": "MDSEDETVEETVEGLLDDDGLPHGFCTVNYSSTDRFEGHFVHGEKNGRGKFYFFDGSTLEGFYVDDALQGQGIYTYEDGGSLHGTYVEGELNGPAQEYDTDGRLIFKGQYKDNVRHGVCWIYYPDGGSLVGEVNEDGDMTGDKVAYVYPDGRMALYGKFIDAEMLEGKLAILTSVDEGKPHFELVPNGPVYNFDKSTPSCISVNPLFPDPYESERVYVNDSLIHNAGEGLFAKVASAAQTVMSFYNGVRITHQEVDSREWALNGNTISLDDETVLDVPAPYNSYYKYCASLGHKANHSFSPNCMYDTFVHPRFGPIKCIRTMKAVEKDEELTVAYGYDHSVTGKNGPEAPEWYQQQLTAFQATQQK", "text": "FUNCTION: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes. Has also methyltransferase activity toward non-histone proteins. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET7 subfamily."}
{"protein": "MLQTSIKKIHGKLKGSNLNTAEVIVNSFKRAEQVLELNSFISMNNNAGLQVESSNEYFKNGKPRSLLEGIPIAVKDNFCVKDTLTTCGSKMLQNFRPKYTATVVQKLLDSGAILVGKTNMDEFAMGSGTTTSIFGPTKNIWGSRFSNLCIQEKNDWFIPGGSSGGSAVAVASGICLGALGSDTGGSCRNPASYCGIVGLKPTYGLLSRYGLIPLVNSMDVPAIMALNVEDTACLLGIMMGRDENDSTTVSKNLNLALNYSSSSVKGLKIGIPAEYNCQGLSDEIRSAWNDIAKVLYQGGASIVPVSMPHTKYSIVCYSILNQCEVASNMARYDGIEFGLRSKEKGNRKNSYVTTRYSGFNEVVRSRIIAGNFFLLSSNSNKYYEKALKVRRLIADDFNNAWRKGINILLTPTTLTDAPKYSEYIKKDEREQSAIQDYCTQPANMAGCPAISIPIELSKKGFPISLQLMAPKFEEKTLLGCALYIENAVNFKNMNEQ", "text": "FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the amidase family. GatA subfamily."}
{"protein": "MTSRYWVVSLPVKDSASSLWNRLQEQISKHSFDTPVYRFNIPNLRVGTLDSLLALGDDLLKSNSFVEGVSQKIRRQIEELERISGVESNALTVDGVPVDSYLTRFVWDEAKYPTMSPLKEVVDNIQSQVAKIEDDLKVRVAEYNNIRGQLNAINRKQSGSLAVRDLSNLVKPEDIVESEHLVTLLAVVPKYSQKDWLACYETLTDYVVPRSSKKLFEDNEYALYTVTLFTRVADNFRIAAREKGFQVRDFEQSVEAQETRKQELAKLVQDQESLRSSLLQWCYTSYGEVFSSWMHFCAVRTFAESIMRYGLPPAFLACVLSPAVKSEKKVRSILERLCDSTNSLYWKSEEDAGAMAGLAGDSETHPYVSFTINLA", "text": "FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein. SIMILARITY: Belongs to the V-ATPase C subunit family."}
{"protein": "MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQLLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLLDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTCLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEDAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEAAEPSAGGQFESLTFDMELTSECATSPM", "text": "FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6- responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA (By similarity). Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (By similarity). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (By similarity). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation. May play an apoptotic role by transctivating BIRC5 expression under LEP activation (By similarity). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion. Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus (By similarity). The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. SIMILARITY: Belongs to the transcription factor STAT family."}
{"protein": "MFILRLFVYNVVIFFVFLFIFGFLPNDSGRNPGREE", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbI family."}
{"protein": "MGSLGAILKHPEDFYPLLKLKIAARHAEKQIPSEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSISTEVKVPILMAFHRHIYDNDWHFSCGTKEYKVLMDEFHHVSNAFLDLGSGYKEAIEDITMRMGAGMAKFICKEVETIDDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAKVIDQTKTMSDVYGAFFDFSCLLKSKVDNNDPNATKTLSRLEAIQKICKNSGALTTKRKSYIIENESGYNSTLIVILFIILAILYAYLSSNLPNSL", "text": "FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:29378087). Catalyzes the biosynthesis of squalene (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phytoene/squalene synthase family."}
{"protein": "MDNSAPDSLSRSETAVTYDSPYPLYAMAFSSLRSSSGHRIAVGSFLEDYNNRIDILSFDSDSMTVKPLPNLSFEHPYPPTKLMFSPPSLRRPSSGDLLASSGDFLRLWEINEDSSTVEPISVLNNSKTSEFCAPLTSFDWNDVEPKRLGTCSIDTTCTIWDIEKSVVETQLIAHDKEVHDIAWGEARVFASVSADGSVRIFDLRDKEHSTIIYESPQPDTPLLRLAWNKQDLRYMATILMDSNKVVILDIRSPTMPVAELERHQASVNAIAWAPQSCKHICSGGDDTQALIWELPTVAGPNGIDPMSVYSAGSEINQLQWSSSQPDWIGIAFANKMQLLRV", "text": "FUNCTION: May regulate MYC transcription factors. Involved in epidermal cell fate specification such as trichome and root hair development, seed mucilage production, and anthocyanin biosynthesis by acting at the dihydroflavonol-4-reductase (DFR) step. Together with GL1 and GL3, promotes trichome formation. Activates the transcription of GL2. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MQFKNALTATAILSASALAGTNSTTSIPSSCSIGTSATATAQADLDKISGCSTIVGNLTITGDLGSAALASIQEIDGSLTIFNSSSLSSFSADSIKKITGDLNMQELIILTSASFGSLQEVDSINMVTLPAISTFSTDLQNANNIIVSDTTLESVEGFSTLKKVNVFNINNNRYLNSFQSSLESVSDSLQFSSNGDNTTLAFDNLVWANNITLRDVNSISFGSLQTVNASLGFINNTLPSLNLTQLSKVGQSLSIVSNDELSKAAFSNLTTVGGGFIIANNTQLKVIDGFNKVQTVGGAIEVTGNFSTLDLSSLKSVRGGANFDSSSSNFSCNALKKLQSNGAIQGDSFVCKNGATSTSVKLSSTSTESSKSSATSSASSSGDASNAQASVSASASSSSSSSKKSKGAAPELVPATSFMGVVAAVAVALL", "text": "FUNCTION: Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall. Important for apical bud growth (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted, cell wall Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. SIMILARITY: Belongs to the SPS2 family."}
{"protein": "MFLSTLFLVSLATCVICGNPSSPPVVDTAHGKVLGKHVNVEGFSQPVAVFLGIPFAKPPLGSLRFAPPQPAEPWSSVKNATTYPPMCSQDAARGQAVNDLITNRKEKIHLEFSEDCLYLNIYTPADFSKNSRLPVMVWIHGGGLKLGGASSFDGRALSAYENVVVVAIQYRLSIWGFFSTGDEHSRGNWGHLDQVAALHWVQDNIANFGGDPGSVTIFGESAGGYSVSILILSPLSKNLFHRAISESGVAFIPGMFTKDVRPITEQIAVTAGCKTTTSAVIVHCMRQKTEEELLEIMHKLNLYKLSLQGDTKNSDQFVTSVLDGVVLPKDPKEILAEKNFNTVPYIVGINKQECGWLLPTMTGFLPADVKLDKKKAIALLEQFASMTGIPEDIIPVAVEKYTKGSDDPDQIREGVLDAMGDVAFGVPSVIVSRGHRDTGAPTYMYEYQYYPSFSSPQRPKNVVGDHADDVYSVFGAPILREGASEEEINLSKMVMKFWANFARNGNPNGKGLPHWPKYDQKEGYLHIGGTTQQAQRLKEEEVTFWTQSLAKKQPQPYHNEL", "text": "FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes retinyl esters (By similarity). Hydrolyzes p-nitrophenyl butyrate (PNPB), triacylglycerol and monoacylglycerol. Shows higher activity against PNPB, a short-chain fatty acid ester, than against triolein, a long-chain fatty acid ester. Shows no detectable activity against diacylglycerol, cholesterol ester or phospholipids. May play a role in adipocyte lipolysis. SUBCELLULAR LOCATION: Lipid droplet Cytoplasm, cytosol Endoplasmic reticulum Microsome. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "MGERKAVIKNADMHEDMQETAVHTAAAALDKYEIEKDVAAYIKKEFDRKYNPNWHCIVGKHFGSYVTHETQHFIYFYLQERAFLLFKSG", "text": "FUNCTION: Acts as a non-catalytic accessory component of a dynein complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the dynein light chain family."}
{"protein": "MVSLRLQKRLAASVLKCGQKRLWLDPNESSEISMANSRASIRKLIKDGLVMKRSTVIHSRSRARAFLEAKRKGRHTGSGKRKGTRNARMPTKVLWMRRQRVLRRLLRKYRAAKKIDKHQYHEFYLGSKGNLYKNKTVLIEAIHVSKADKIKSDKLTSQQEARRAKNTASRAKRNEKAQIVAKVDV", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family."}
{"protein": "MSFIFDWIYSGFSSVLQFLGLYKKTGKLVFLGLDNAGKTTLLHMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHIQARRVWKNYLPAINGIVFLVDCADHERLLESKEELDSLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQTTGKGSVSLKELNARPLEVFMCSVLKRQGYGEGFRWMAQYID", "text": "FUNCTION: GTP-binding protein involved in transport from the endoplasmic reticulum to the Golgi apparatus (PubMed:11149932, PubMed:8138575). Activated by the guanine nucleotide exchange factor PREB (PubMed:11149932, PubMed:8138575). Involved in the selection of the protein cargo and the assembly of the COPII coat complex (PubMed:11149932, PubMed:8138575). Synergizes with the cargo receptor SURF4 to mediate the export of lipoproteins from the endoplasmic reticulum, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Golgi apparatus, Golgi stack membrane; Peripheral membrane protein Note=Associated with the endoplasmic reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi region. SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family."}
{"protein": "MFTAKNPFEDIVLKATSDELTSENWELNLEVCDKVSSGGDTAARNCIAAIQKRLVHRNANVQLYALTLADAVAKNCGLAAHQEIASRSFTQTLARICLDRNTHSTVKKRCSALVKEWAGEFDDQSLGLMKETYESLKSQDAVAEDETPAEPPREPTSEQLRAEDEELRRALELSIQDQGGRNAWPSYNTEQAETSGSSAPAAASSSSSAYQPTSQSLAPAQQQQQQQHDANHTNGTSSSAHAQPLSAATPPAVASRVRALYDFSPTEPGELAFSRGEVIRVLDSVYEHWWRGEVRGEAGIFPVNYVEVLPDPTPDELQREAQMEARIFSQAADIDRLLSKLRSLDPARDNLADDDELQELYQKSLAMRPKIVKLIDRYSNKITELKAMNDKFVHARGSFDEMMEQSLSRYNPGGHSSQDYLRPRPELQQHFSASSADYAQHPSYPTAHAYSVQQAQSASSAHDQIQYPFNPEQRHGYAQSAGAEPADPSYVQGSRLPSGPQPPQQITMAHQQQPHEQQYSSAPHDDEKRRLFERARAESEAFQQQHFQSQAHTSRSGYSGAYPSQPDASVLNQQMGNMNIGGSSSYASHPTGH", "text": "FUNCTION: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB). SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the STAM family."}
{"protein": "MFRSALVRSSASAKQSLLRRSFSSGSVPERKVAILGAAGGIGQPLALLMKLNPLVSSLSLYDIANTPGVAADVGHINTRSQVVGYMGDDNLAKALEGADLVIIPAGVPRKPGMTRDDLFNINAGIVKNLWSAIAKYCPHALVNMISNPVNSTVPIAAEIFKKAGMYDEKKLFGVTTLDVVRVKTSYAGKANVPVAEVNVPAIVGHAGVTILPLFSQATPQAILSGDALTVTTKRTQDGGTEVEEAKAGKGSATLSMAYAGALFADACLKGLNGVPDVVECSYVQSTITELPFFASKVRLGKNGVEEVLDLGPLSDFEKEGLEALRPGIKSTIEKGVKFANQ", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family."}
{"protein": "MAFLKKSLFLVLFLGMVSLSICEEEKRENEDEEEQEDDEQSEEKRALWKTLLKGAGKVFGHVAKQFLGSQGQPES", "text": "FUNCTION: Antimicrobial peptide with activity against Gram-positive and Gram-negative bacteria, and fungi. Has hemolytic activity. SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily."}
{"protein": "MRDQERTLNQDVERCINVLQDFLDTGSAKAISVFSNKTSENEDWLEEIRVKYRIKDNDELQAIKMLKQKRLDQLEALESKVDYYEKLCDELEEFQDEMEVKAKLEQNRRSRFDSMTRK", "text": "FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting. SUBCELLULAR LOCATION: Endosome. SIMILARITY: Belongs to the BLI1 family."}
{"protein": "MLTKFLSLLLLLLLLGCAFCNSDGSQSLHMLQISYFPDPYHGRHQGNASLGKLLTHTLEGPSNNVTILQLQDWQDPDSWARTESGLKIYLSQFNSLVQLIYRERKNDVVFPLTVSCSVGCELPPEEGSEPHVFFDVAVNGSAFVSFQPKTAIWVTGSQEPSEAINFTLKQLNTYNRTRYELQEFLQDTCVQYLENHITTQNTKGSQTGRSYTSLVLGILMGCFIIAGVAVGIFLCTGGRRC", "text": "FUNCTION: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MSLRLLIPLLFLPGLALADHRPCPDWPAQRARAEVSQLLKTLSHWDDHYHRQGVALVADELYDQSRQHLRHLQGCFDLASNDAPLATARGQVPHPVPHTGVDKLRDEPAVQRWLQGRQGMWIQPKVDGVAVSLVYQQGQLTQLLSRGDGVLGHDWSRHIPQLGRIVRQLPQPLDTVFQGELYWRLADHVQAEAGSANARGIVAGLLARKQLSDEQGSGIGLFVWDWPAGPGSQAERLAQLTALGFIDSQRFSVAIEGFDAAAHWRQHWYRTALPFATDGVILRQDARPPAQRWRAQAPYWIAAWKYPFSQALAQVRDIHFRIGRTGRITPLLQLEPIQLDDRRISQVSLGSLARWTQLDIRPGDQVAVSLAGLTIPRVESVVHRSPLRAPVLVPDPADHHLLSCWQASPACQEQFLARLAWLGGNKGLDMAGVGSGVWHQLVESGKVATLSDWLELTREDLLEVPGIAQARAERLLQAFSLGRRQPFERWLRGLGLPAPSHFSPGADWSALASRNIEQWLAEPGVGAVRAAQLQAFLSHEQVQALARRLRAHEIEGF", "text": "FUNCTION: Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB subfamily."}
{"protein": "MAKEPMRVLVTGAAGQIGYALVPMIARGVMLGADQPVILHMLDIPPAAEALNGVKMELVDAAFPLLKGVVATTDVVEACTGVNVAVMVGGFPRKEGMERKDVMSKNVSIYKSQASALEAHAAPNCKVLVVANPANTNALILKEFAPSIPEKNVTCLTRLDHNRALGQISERLNVQVSDVKNVIIWGNHSSSQYPDVNHATVKTSTGEKPVRELVSDDEWLNGEFITTVQQRGAAIIKARKFSSALSAASSACDHIRDWVLGTPEGTFVSMGVYSDGSYGVPSGLIYSFPVTCSGGEWKIVQGLPIDEFSRKKMDATAQELTEEKTLAYSCLE", "text": "FUNCTION: Malate dehydrogenase; catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL", "text": "FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding. SIMILARITY: Belongs to the peptidase C2 family."}
{"protein": "MNLSLSDLHRQVSRLVQQESGDCTGKLRGNVAANKETTFQGLTIASGARESEKVFAQTVLSHVANIVLTQEDTAKLLQSTVKHNLNNYELRSVGNGNSVLVSLRSDQMTLQDAKVLLEAALRQESGARGHVSSHSHSVLHAPGTPVREGLRSHLDPRTPPLPPRERPHTSGHHGAGEARATAPSTVSPYGPEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCCRQTAVRADLNANYIQVGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTIREAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYESKGSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNSQLSVEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS", "text": "FUNCTION: Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages. SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion system. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily."}
{"protein": "SCVGEYGRCRSAYEDCCDGYYCNCSQPPYCLCRNNN", "text": "FUNCTION: Insecticidal neurotoxin that induces irreversible neuromuscular blockade in house crickets (A.domesticus). Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neurons. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 04 (aga-5) subfamily."}
{"protein": "MQVNNLGFIASILFVLVPTVFLLILFIQTRQETEG", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbM family."}
{"protein": "MTTAALQTQLQGYLDYLIIERSIAANTLSSYRRDLIRYSKHLSDRGIEDLAKVGEHDVSEFLVALRRGDPDSGVAALSAVSAARALIAVRGLHRFAVAEGLVDLDVARAVRPPTPGRRLPKSLTVDEVLALLESVGGESRADGPLVLRNRALLELLYSTGSRISEAVGLDVDDVDTQARTVLLQGKGGKQRLVPVGRPAVQALDAYLVRGRSDLARRGPGMLATPAIFLNARGGRLSRQSAWQVLQDAAEHAGITSGVSPHMLRHSFATHLLEGGADIRVVQELMGHASVTTTQIYTLVTVQALREVWAGAHPRAK", "text": "FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily."}
{"protein": "MEVPGSSKKMIATQEEMSAAKIALGSRDMCAHLLIPLNKCRQAEFYLPWKCEDERHVYEKCEYELVMERMLAMKKIREEEALAKQNKLQGNAAVPLIPKTANA", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane; Peripheral membrane protein Mitochondrion intermembrane space. SIMILARITY: Belongs to the complex I NDUFB7 subunit family."}
{"protein": "MPLDGVKNIVLVLSGKGGVGKSSVTLQLALALTLQGKSVGILDIDLTGPSIPRLVGLEDAKITQSPAGWVPVPVHSATDNATGPATGSLRCISLGFLLRDRGDAVIWRGPKKTAMIRQFLSDVSWGETDYLLVDTPPGTSDEHIALAEQLLTTATTDAAAAAAGGRPRLAGAVLVTTPQAIATSDVRKEVNFCVKTRIPTLGVIENMSGYACPCCGEVSNIFSSGGGRAMAQEMGIKFLGVVPVDVKFGELVEGGKIQDGSDSEDEGETARQEPEPEAVDDRPLVERYKDCWSYPRFEEFARTLIADIDGA", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nbp35-cfd1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily."}
{"protein": "MIMETESPLSITSPSPSDSTFQVDMEKTMHALPSSLLDSPLLSTNEHYPPKSTLLLSGPSPIRNIQLSATKSSESNSIDYLTDTQNIFPNFVNNENNYQFSTAPLNPIDACRVGERKVFTTGNVLLSADRQPLSTWQQNISVLSESPPQNGIQSYISSSEQAAQALTRKPSVTGFRSSSLNSNSDDIDIFSHASRYLFVTNLPRIVPYATLLELFSKLGDVKGIDTSSLSTDGICIVAFFDIRQAIQAAKSLRSQRFFNDRLLYFQFCQRSSIQKMINQGATIQFLDDNEGQLLLNMQGGSVLSILQLQSILQTFGPLLIMKPLRSQNVSQIICEFYDTRDASFALDELDGRIIHNCCLQVAYYDAMADSVSTSSASSLSVPRGFSGMLNNNSEWNNSMTMSSNQETPTAASCAVSRIGSSYGMSNNFGSVPLGRTESSPAWGTSGYYDVSSTSPVAPSDRNPSRQYNSIRYGLDVNPIAPPNSSRLKQRNSDLLNGINPQWSPFSSNTGKVFDSPTGSLGMRRSLTVGANASCSNPTNLSFASLTLHDSKADSTLSASSLNPDLNLQRYTPTVEKHASDRNSVDYAQIASGIDTRTTVMIKNIPNKFTQQMLRDYIDVTNKGTYDFLYLRIDFVNKCNVGYAFINFIEPQSIITFGKARVGTQWNVFHSEKICDISYANIQGKDRLIEKFRNSCVMDENPAYRPKIFVSHGPNRGMEEPFPAPNNARRKLRSIASAQQIGLFPPTASKC", "text": "FUNCTION: Crucial for commitment to meiosis but it is not sufficient itself for the commitment. May be a splicing regulator."}
{"protein": "MRILCDACESAAAIVFCAADEAALCCSCDEKVHKCNKLASRHLRVGLADPSNAPSCDICENAPAFFYCEIDGSSLCLQCDMVVHVGGKRTHRRFLLLRQRIEFPGDKPNHADQLGLRCQKASSGRGQESNGNGDHDHNMIDLNSNPQRVHEPGSHNQEEGIDVNNANNHEHE", "text": "FUNCTION: Acts as negative regulator of seedling photomorphogenesis (PubMed:18540109). Acts as a negative regulator of blue light-mediated inhibition of hypocotyl elongation through increase of bioactive gibberellin levels (PubMed:20872270). Acts as a repressor of thermotolerance by modulating expression of a set of heat shock- responsive genes (PubMed:23238922). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MVKKLLTILSIAATAGSLSIGTASAQDAKAGEAVFKQCMTCHRADKNMVGPALGGVVGRKAGTAAGFTYSPLNHNSGEAGLVWTADNIINYLNDPNAFLKKFLTDKGKADQAVGVTKMTFKLANEQQRKDVVAYLATLK", "text": "FUNCTION: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "NLFQFAKMINGKLGAFSVWNYISYGCYCGWGGQGTPKDATDRCCFVHDCCYGRVRGCNPKLAIYSYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNKNTYNKNYKFLSSSRCRQTSEQC", "text": "FUNCTION: Heterodimer: postsynaptic neurotoxin. FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas saturated fatty acids induce a slight activity). The inhibition of platelet aggregation is almost maximal when aggregation is induced by collagen, and arachidonic acid, whereas it is only of 30% when the aggregation is induced by ADP. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
{"protein": "MTSSATSPTNGVDKNKNEEMVATPANCPYQLFNQEVVWNGKWIQTRQVGFKTHTGQVGVWQSVHRNTKPVEASADGVSIIARVRKQGKLYIVLVKQYRIPCGKLCLELPAGLIDAGETAQQAAIRELKEETGYVSGKVVMESKLCFLDPGLTDDSQCLVVVDVDGDAPENQNPVQVLDSTESIEVLLVEQSALMAYVTNLDSSSIVVESTLLAYAMGIQFATI", "text": "FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MFNKIIKLGQKKFNKSDQHHQDNNNNNNNTSTNTVVRGSRTTTPAPSSVSNGESQTTAQSPSQTPNHPMFTTTPILEVLPLLKDVSSSDRPLLFMKKAHMCSCHCDFSDTLIMPREKEIKRQTLLELVDFLHSSSGKVNETMQSELIRMVSANIFRCLPPAYHENTGAPPEGNDPEEEEPYLEPWWPHLQLVYELLLRYVVSSEIEPKTAKKFINHTFVSRLLDLFDSEDPREREYLKTVLHRIYGKFIFHRPFIRCSIYNIFYKFLYETERCIGIGELLEILGSVINGFTVPMREEHRLYLVKAILPLHKSKGISIYHQQLAYCVTQFVEKDYKLADTVIRGLLKFWPLTNCQKEVLFLGELEEVLDATEPSEFQQCVVPLFTQIGKCLNSAHFQVAERALFLWNNEHIVGLIAQNKDVIFPIIFEALERNMKGHWNQAVHGLSENVRRMFLEMDTELFEECEKQYLENEAKACELLEQRELTWKRLEEAASLAAN", "text": "FUNCTION: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 family."}
{"protein": "MSEPKTSATSETQTGTMTVKTGLAQMLKGGIIMDVINADQARVAEEAGACAVMALEKVPADIRKDGGVARMADPRKIKEIMDTVTVPVMAKCRIGHFAEAQILQNLGVDFIDESEVLSPADDENHVDKQPFNVPFVCGARSLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHARQINREIRVAQCLSSAELYGYAKQLGVPLDLLQKTAKLGRLPVVNFAAGGLATPADVSLLMQLGVDGVFVGSGIFKSGNPEKRAKAMVQAVTHYNDPKVLADVSEDLGDPMVGLNCEHLSEKWAQRESVHKS", "text": "FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme- catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers. SIMILARITY: Belongs to the PdxS/SNZ family."}
{"protein": "MYNSWFVLKQKSNILLTILTSSLLAKFSYPSTLFFFLEMALMKVMTILVLFVSVSSTLAQSNNGGHISIIVSETGLEFAKDYLIKKVITTTLPLQLPDIENKVKIPLIGKVRMGLSNIQIDAVHVQSSKMETRKDGIILSVLGATANLSMDWSYTYRASFFEISDHGDASVEVKGMNVRITATLVNDNGSLKIASRENDCTVKNIDIHINGGASWLYQGVVDAFQKMIISTVEKTVSTKIVEKMKKLDSFLQSLPKQRKIDDSAAVNLTFTGNPVLGNSSVEVDINGLFMPKGDDIKVAGSRSSSFFGGVNKRMVTISVEEGVFNSATLVYFNAKVMHLVMEETKNGSILSTSDWKLILPELYKHYPDNKMVLNMSVTSPPAVKITENGIDATIQLDIAFDVQDSGENLSVARLSTILSVACSTEIVKNNLIGSLRLNDFNATMKWSKIGEFQTNYVQAATSRILEALFLPYVNTRLKRGFPLPIPGDFTIKNIKIVYVNSGILVCTDIGTSTNQ", "text": "SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP (TC 1.C.40) family."}
{"protein": "MAKLARASALQFGANVTQTFVGAIITIYVINELGVGAFGIFALSAALVKWASIPAVGIRGAVITRMNESDDISPSEYFTTASVLTGAIILVGLLALLGYSPFVEQYLDYSGTQLVGGMFVSNVSFRLVLGGLRGENRVEMSSLYEALWGILSSLVKLALVYTGVGVDALFYGEITSSIVIGIFGVYSLNISFVSPTRSAAISLYSWARYGWLDNLKRMSYSWLDTIILGFFVSTSLVGIYEVAWRISALFVLLPTAISKSTFPTISSLRDTDKLNKVRRILTRGLSVAGVLAIPGLVGSVLVGGDILALYGPSVSSVGVAVSVLVSLSVVRLVECYETLVMQALNALDLPDRTFRIGVIFITTNIILNVSLIPMFGVIGAAIATLLSMTLGSILAVRALPKAVQTLPPVSAIGSQFVSAGAMAVVLFTILNYRPIGQPIEVVLYVLAGATTYGFVLLSLSSNFRERVQQLLSESLG", "text": "FUNCTION: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Probably mediates or contributes to the translocation of the dolichol-phosphate-mannose across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AglR/Agl15 family."}
{"protein": "MAALLLLLPLLLLLPLLLKLDVWPQLRWLPADLAFTVRALRCKRALRARALAAAAADPESSESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLRARGWTGGRRGSGRGSTEEGARVAPPAGDAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSVLSDPLYVLDQDIGAYLPLTPARYSALLSGDLRI", "text": "FUNCTION: Mainly functions as an acyl-CoA ligase catalyzing the ATP- dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:15469937, PubMed:15699031). Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes (PubMed:15699031). SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MTRLSEILDQMTTVLNDLKTVMDAEQQQLSVGQINGSQLQRITEEKSSLLATLDYLEQQRRLEQNAQRSANDDIAERWQAITEKTQHLRDLNQHNGWLLEGQIERNQQALEVLKPHQEPTLYGADGQTSVSHRGGKKISI", "text": "FUNCTION: Required for the efficient initiation of filament assembly. FUNCTION: Required for the efficient initiation of filament assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FlgN family."}
{"protein": "MRSTAYLTALLSFLGATHAAPEGPRCRCTPDQSCWPSPGLWQTLNKTLSGNLVAVKPVGTVCHDPTYNGGLCDSVKGMQTDSSWRSAQPGAVQSINWETWPEKNESCYIDGPRQVPCGQGRIPLYSAVVQSPLDIQKTVRFASKYNLRLVIKNTGHDFLGRSTGPQSLQILTHNMKSINFTDNFVPEGKPDGRGIGQAVTIGAGVQLNELYEAAGKRGLTQVIGLSTTVGAAGGYIQGGGHSPLGPWKGMSTDHVLEYKVVTAGAKFVTANEYQNSDLFWALRGGGGGTFGVVTSVTLRTFKDPPTIVSQVNVTMDGKANESYWAAVEKFQAYLPTLSDGGCSGYYYMLPNVTLGPQSAAVIIAAFYYANKTDKAHVDNLYRPLFASLSSIPGINVASVSVPVSSSTEAFRSAFDQKPPRDGGGVNILGSRLFSRKLLEAPGGAANLTAALSKLDFKNLQPAIGHLVAGGQVAKNTHIQSALNPSWRKALVHLVISRDWSIDSTFAEQEKISTKLTAEEIPLLAAVEPDMGAYTNEADVNEPRFQQTFWGTNYNTLLRVKNRWDPRGLFFVRSGVGSEAWDKQGLCRA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MAYNQEDSKRLSDKYKKEGHFDKLKREILSNPWNNTEENSESFEQALRKRVASTVKEMVNEDEELIFKNRGLTSALIESQLVKDNYLKLGSKMEGDNGDGEKKFDLDVYVRSKLQDPKLLEMIKGQLQETLNSYEEEANGST", "text": "FUNCTION: The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SHG1 family."}
{"protein": "MVDPLCNYNVLEAIFSYLELNDLYRCSQVCKSWYHFLNDENSDVWRWHCLRKLPKESVKSDLLASVSTYKTKLRAYLHAWSPNDCSRNVYIKPNGFTLHRNPVAQSTDAARGKIGFRQGRHAWEVIWEGPLGTVAVIGISTKEAALQCHGYVALLGSDDQSWGWNLVENHLLHNGDMQGNYPLLNNAPKYQVGERIRVILDCDDNTLSFEKNYEFLGVAFRGLPDKKLYPTVSAVYGNTEVSMVYLGTPLDG", "text": "FUNCTION: Required in the presynaptic motoneuron to down-regulate the levels of wnd and restrain synaptic terminal growth at the neuromuscular junction (NMJ). SUBCELLULAR LOCATION: Synapse. SIMILARITY: Belongs to the FBXO45/Fsn family."}
{"protein": "MGPWEAKWIRHSDVRPFPQPEPMTVEEKVAVMLKPELHVSSGCHPYPAVNDLGETNGGLKTTGAPSGMCKGSGWGSQVYGRHASFRGVWAIMYVWYFPKDMPSAHFGHRHDWEHVIVWIEKPVVENVKILAVTPSFHDGYSKQVPPDPSHLNGLAAKFIYESEWPINHALRPTRKGGKKQDLILWEQMSSNARHALNIVPWGAANTPFNDFVFMGRLEKAFPF", "text": "FUNCTION: Probable secreted effector that may act as a pathogen- associated molecular pattern (PAMP) recognized by the plant immune system (PubMed:32117400). Seems not to induce necrosis, neither in several susceptible or resistant Vitis species nor in the dicot model plant Nicotiana benthamiana (PubMed:32117400, PubMed:35152834). SUBCELLULAR LOCATION: Secreted Host cytoplasm. SIMILARITY: Belongs to the Necrosis inducing protein (NPP1) family."}
{"protein": "MALPKNLIPMPRSRFLRVKCIDCGNEQIVFSHPATKVRCLVCGATLVEPTGGKGVIKAKILEVLE", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family."}
{"protein": "MATPPKRRAVEATGEKVLRYETFISDVLQRDLRKVLDHRDKVYEQLAKYLQLRNVIERLQEAKHSELYMQVDLGCNFFVDTVVPDTSRIYVALGYGFFLELTLAEALKFIDRKSSLLTELSNSLTKDSMNIKAHIHMLLEGLRELQGLQNFPEKPHH", "text": "FUNCTION: [Isoform 1]: Plays a role in protecting cells against TNF- alpha-induced apoptosis by preventing the recruitment of FADD and caspase 8 to the apoptotic complex I, composed of TRADD, TRAF2 and RIPK1/RIP. FUNCTION: Involved in gene transcription regulation (PubMed:28106301, PubMed:21730289). Acts in concert with the corepressor URI1 to regulate androgen receptor AR-mediated transcription (PubMed:11854421, PubMed:21730289). Together with URI1, associates with chromatin to the NKX3-1 promoter region (PubMed:21730289). Negatively regulates the transcriptional activity of the estrogen receptor ESR1 by inducing its translocation into the cytoplasm (PubMed:28106301). May act as nuclear chaperone that facilitates the formation of the NF-kappa-B enhanceosome and thus positively regulates NF-kappa-B transcription activity (PubMed:17620405, PubMed:21307340). Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling (PubMed:17554592). Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC (PubMed:17554592). Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM (PubMed:17635584). SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Note=Predominantly localizes to the nucleus (PubMed:16221885). Localizes to spindle pole during mitosis (PubMed:16221885). SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. SIMILARITY: Belongs to the UXT family."}
{"protein": "ATFFLLSWTHCWSLPLPYGDDDDDDLSEEDLEFAEHYLKSYYHPVTLAGILKKSTVTSTVDRLREMQSFFGLDVTGKLDDPTLDIMRKPRCGVPDVGVYNVFPRTLKWSQTNLTYRIVNYTPDISHSEVEKAFRKAFKVWSDVTPLNFTRIHDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNLGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEPELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDIMEGYPRKISDLGFPKEVKRLSAAVHFEDTGKTLFFSGNHVWSYDDANQTMDKDYPRLIEEEFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC", "text": "FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the peptidase M10A family."}
{"protein": "MHLDWTLVLASRIRKVKCDEKKPCCQKCIDTGRTCDGYESPFRVVTSRSIINGARASGIPGAASRPVRPALTEISPADIDLLNRYFSTKTMFDVKLGCDEEAREVLEASLTDPTVRHAVSSLRSLREHLETSGDVSASAAQQSPSYGYDYGVQQYCMALGGLASNLSSPGSNALKSALLCCQIFISIEQVRGNYGTMAQHIIQGLGIMHEYRARPTLDDANNLVPAHHAQLPLLDAFVIKLFAAPCKFAEPSATADKEGGKAVSMCAISRHEQTVGSRNLRTIVPDMRTELTRISTSTLDFLVKVSSVDSAGNALRLLPEKTALLESLKSWLMDLELVHADIKSPGTEPLAVSFLRLFHQILKIILVEALNSSSNLQAELRTENDRLQGIGSIIDERVQSQRKNSSALDLIDNRLKCPA", "text": "FUNCTION: Transcription factor that may coregulate the expression of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDTKEEKDKDDQEWESPSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHPSPRTQHIQQPRK", "text": "FUNCTION: Ribosome-binding protein involved in ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with eiF5a (EIF5A and EIF5A2) at the polypeptide exit tunnel of the ribosome, preventing mRNA translation (By similarity). Involved in ribosome hibernation in the mature oocyte by preventing mRNA translation, leading to ribosome inactivation (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also acts as a negative regulator of autophagy (PubMed:20537536). Involved in mediating interferon-gamma-induced cell death (PubMed:7828849). SIMILARITY: Belongs to the DAP-DAPL1 family."}
{"protein": "MGNRLNGSYLSNTDMSIEDKQNKYNEAIEDCKICNKVYIKQSGKIDKKELTRIKKLDFFYSQKSDHEIERMFFNVPNGTFLLTDDATNENLFIAQKDLENGSLNIAKLEFKGKALYIDGKDYFSLENYLKTFEDFYKYPLIYNKNE", "text": "FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. SIMILARITY: Belongs to the asfivirus MGF 100 family."}
{"protein": "MEDDGQSSVAETLDPALQKKHHDMLERLSARHQARKSDSPDSSSSSSSTLESTSSFLAKFSDSKRSIESRIAESRLASSSTDSSKLKSDLAEISVAIDNLEKLLAENSYFLPSYEVRSSLKIVSDLKQSLDILSGELVPKKKFSFKSKSTTKKPESKLPEIQKPDVVLPPKLVPVRDSPGLRNKHGETLVKSFEGSSIGEFTLSDLDSCQVKLTGTVNALFLHRLKKCSVYTGPVIGSILIDDVEDCVLVLASHQIRIHCARKSDFYLRVRSRPIIEDSNGVRFAPYCLDYKGIDEDLKTAGLEEETNNWANVDDFRWLRAVQSPNWSLLPEEERVSLLTISGDS", "text": "FUNCTION: Essential tubulin-folding protein involved in the final step of the tubulin folding pathway. Required for continuous microtubule cytoskeleton organization, mitotic division, cytokinesis, and to couple cell cycle progression to cell division in embryos and endosperms. Not essential for cell viability. Binds probably to the multimeric supercomplex, stimulating GTP hydrolysis by the bound beta-tubulin and the release of the alpha-/beta-tubulin heterodimer. SUBCELLULAR LOCATION: Cytoplasm Note=Not associated with microtubular arrays. SIMILARITY: Belongs to the TBCC family."}
{"protein": "MLRFLVFASLVLYGHSTQDFPETNARVVGGAEARRNSWPSQISLQYLSGGSWYHTCGGTLIRRNWVMTAAHCVSSQMTFRVVVGDHNLSQNDGTEQYVSVQKIMVHPTWNSNNVAAGYDIALLRLAQSVTLNNYVQLAVLPQEGTILANNNPCYITGWGRTRTNGQLSQTLQQAYLPSVDYSICSSSSYWGSTVKTTMVCAGGDGVRSGCQGDSGGPLHCLVNGQYSVHGVTSFVSSMGCNVSKKPTVFTRVSAYISWMNNVIAYT", "text": "FUNCTION: Acts upon elastin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily."}
{"protein": "MQPLHGNCLIAYARHKYILTMVNGEYRYFNGGDLVFADASQIQVDKCVENFVLVSRDTLSLFLPMLKEEALKLHAHKKVPSLLVHHCTRDIPVFQEVAQLSQNKNLRYAEMLRKRALIFALLSVFLEDTQFIPLLLNVLQPNMRTRVCTVINNNIAHEWTLARIASELLMSPSLLKKKLREEGTSYSQLLTECRMQRALQLIVIYGVSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERSAQELPNCGPAASMAAQGNFYGTDRSAEGIRL", "text": "FUNCTION: Positively regulates the expression of about fifteen genes involved in acid resistance such as gadA, gadB and gadC. Depending on the conditions (growth phase and medium), can repress gadW (By similarity). Negatively regulates perA expression in acidic conditions and positively regulates it in alkaline conditions."}
{"protein": "VSGSGIMAKRVVVDA", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL13 family."}
{"protein": "MSTLGRSKTPSRDEPKKPGVFEKLSGTLSRKKKAPEDEHGNQGGAHHATDEDEVLELELEGREALDQSLVPVLARNIWLEEGEIRRYLTKETARDQKLAQVVDLLIYWLNEELADQRIVVRHLQEDLFDGQIIQKLLEKLEQIRIEVPEVSQSEEGQRQKLQIVVQTANRILGQPREQEKWSADLIHQKDFTAIIQLLVLLALHYRAPVRFPDNVVANVVVAQKEHGQVKTHRITEQITTVQTELAPKGTRDAFDTLFDYGPDKLAHVKTSLLAFCNKHLNKINLEVSDLDNQFQDGVFLVLLVGLLEGYFVPLYHFNLQVQSHEEKVKNVQFAFKLMEDTGLEKPRSRVQDIANGDVKSTLRLLHLLFTKYKHI", "text": "FUNCTION: Involved in the regulation of cell adhesion and cytoskeleton organization. Component of an integrin containing attachment complex, which is required for muscle development and maintenance (PubMed:22253611). During embryonic development, required to recruit cpna-1, unc-89 and myofilaments to newly forming integrin attachments composed of integrins pat-2/pat-3, pat-4 and unc-112 (PubMed:12781130, PubMed:23283987). Also required to reposition the integrin-based attachments so that they form the highly ordered array of dense body and M-line attachments that are characteristic of mature muscle cells (PubMed:12781130, PubMed:23283987). During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles (PubMed:16495308). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, myofibril, sarcomere, M line Perikaryon Cell projection, axon Note=Colocalizes with integrins and pat- 4/ILK (PubMed:12781130). Colocalizes to M line and dense bodies with cpna-1 (PubMed:23283987). SIMILARITY: Belongs to the parvin family."}
{"protein": "MERFVLKFLLIDKVIAVCLDQKISNERLNPLTEYFFWPQRDAWEDMKNFIDNNDWIDPKDAVNILNRITEVINFWEESAQLKKEDIKNLNIKFPDCVFIVM", "text": "FUNCTION: Probably a ribosomal protein or a ribosome-associated protein. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cS23 family."}
{"protein": "MAQLSAQRRMKLMALQLLLWQSALWSGREAVPLVTVSALPPSLPLPRSFLLKSLEQVRKIQASGSVLLEQLCATYKLCHPEELVLLGHSLGIPKASLSGCSSQALQQTQCLSQLHSGLCLYQGLLQALSGISPALAPTLDLLQLDVANFATTIWQQMENLGVAPTVQPTQSAMPAFTSAFQRRAGGVLAISYLQGFLETARLALHHLA", "text": "FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily."}
{"protein": "MKEGRASQKLSSKSIMDPNQNVKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSALQSENSVRDIFHVATLACVNKTNKNVKRNKSQRATKRISHMPSRPELSAVATDLRKDKAKSCTVM", "text": "FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MSSSKPTIAFFGATGGSTISCLAPALKAGYRCAALARTPSRLRDLLVQRGVSESTIADNLTIVSGTATDLQPVKQTLQMGRPASDMADLIVSGIGGKLIMSNPLSPTLDNPTICQDVVRNILTAIRELRDTGTTKAPFLITLSTTGISEVKRDLPIAMMPMYHWMLKVPHDDKKVMERLIVDDAERDPAARALGGYVIVRPSLLTDGDRDKGGDLKKIRVGVEEAPAVGYTISREDVGRWVFEHLVKKGRESEYAGKAVTITY", "text": "FUNCTION: Reductase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA (PubMed:32077283). The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA (PubMed:32077283). A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively (PubMed:32077283). The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo- methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable). SIMILARITY: Belongs to the avfA family."}
{"protein": "MVRPSSSSSASASAARSGAAKRKRNLPTATNPTTRASVAANVKGKGKTKALELDLVVSDDGEEDGELDLESDSGDDDANDDDDNDNEQDDFPEIDLEDSDDDQDVEDEDEPGAQEEVDSDNNKQASTQVHDIQVEEDDSSEEGYNSSDIDNSDFDDDADEGDLAYDSADEDERASAFAARSDASQTSIDEELSRMMSRYSSKPDEHSGSLSATNKLGIPRSQAAQAFDLRVRNPDGSAKGVFKRSEITGEMKRVYPEIDAAYDSDSSTEDPENRIGNVPLEWYDDLPHIGYDINGRKVMKPATKDELDKFLDTVDGDGEAWFSARDKSTGKDVRLSDEELAIIRKLQNAEIPDDAYDPYEDYVDWFTGEDKVMQTALSGRPEPKSRFVPSKWEHKKVMKIVRAIREGRIVPGAAANKDAKPKFYNIWADAHENDTRSPWAVMAAPKLALPGHAESYNPPAEYLFNEQEQKEWQEAEAEDRKQNFLPTKHDSLRRVGAYQNFVQERFERCLDLYLAPRMMRKKLDIHNPENLLPKLPSPKELRPFPITTSVVYVHPDGGRVRCLSVDPTGNWLVTGGDDGRARLWDVAIGRCTASWDVCEGMPKAERSAVHSIAWCPTKNYSLFTAVVHGRVAVIAPPQTQNYAKTSANAISSKSASSSSGATATSTASFLYATSAAATSMPSKPDARSPVAWTRPSEAERRTGVAMHLNITSPSAANLKTVVWHNKGDYFATVCPDSAAGSAGLLIHQLSKHRSQSPFRKASKGSSIQKLVFHPTKPWIFVATQRYIRIYDLMAQSLIKTLQSGFKWISTLDVHPSGDHLMVGSYDKKLAWFDLDLSARPYKVLKYHARAIRSVHFSTSWNLVADASDDGTLQLFYAKVGADYGENLTLVPLKVLRGHEVKNGLGVLDVKWHPNQPWLFSAGADGNALLWTT", "text": "FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family."}
{"protein": "MTINSIYILNKAGTLIYQNDFGNTEKLSHNSYIRLGSTFHSLHAIASNLSPVSGSSSGIEVIETEAFKLQCFQTHTGIKFYVIADPNHQQLEELLHGVYELYTDYVLKNPFYEIEMQIRCDLFDYKLNRLLGVRE", "text": "FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. SUBCELLULAR LOCATION: Golgi apparatus membrane Endoplasmic reticulum. SIMILARITY: Belongs to the TRAPP small subunits family. TRAPPC4 subfamily."}
{"protein": "MAGFTDLREKLKSMTPHRDKVFEYSNGEKRKYRESDDDESEYEERRDAEARRVKSGIKQASIFTLEECARIEAKIDEVVAKADKGLYREHTVDRAPLRNKYFFGEGYTYGAQLEKRGPGQERLYSKGEVDDIPDWVHELVIDRLVTHGVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFLFKPIRVSEPVLHLPVRRGSVTVLSGYAADDITHCIRPQDIKERRAVIILRKTRADAPRLDSNSLSPSIVSPKRRHILKAKRSHRKADPDAAHRPRVLEMDKELQRRSLSSRQRRHDDGSSENSWRRADDREPAARYTHDHAPTRRVKMRRH", "text": "FUNCTION: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:24561204). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (By similarity). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:24561204). SUBCELLULAR LOCATION: Nucleus speckle. SIMILARITY: Belongs to the alkB family."}
{"protein": "MSQETDNKRLVVLVPNDAVFNPRRAYTSEDEAWKSYLENPLTAATKAMMSINGDEESAAAIGLLYDYYKVPREKRLLSLNKINEGHEDQDKRNCLPANETPSNLSTGENRVQVLKTVPVNLSLNNDTVESSNREKYTTSLSESPQPAPASAVTVVKAEEFTPVFMAPSVPYRSDGEEPRGVIFEQTHFGVHSITTHSDYLKDDQRSTPDSTYNESFKETTEKYRTPSVGTEEFLYEQTASSTFQYTLEATKSLRQKQGEGPMTYLNKGQFYAITLSETGANKCFRHPISKVRSVIMVVFSEDKNRDEQLKYWKYWHSRQHTAKQRVLDIADYKESFNTIGNIEEIAYNAVSFTWDVNEEAKIFITVNCLSTDFSSQKGVKGLPLMIQIDTYSYNNRSNKPIHRAYCQIKVFCDKGAERKIRDEERKQNRKKGKSQAAQAQCNNSADGKLSAVPLQKKSDITFFKTMTDLDVQPVLFIPDVHFGNLQRTGQVFYNTDDDIEGGVLVKRLLRPVDEDYGPPAPKQMKEGSRKVLLYVRKETDEVFDALMLKYPTVKGLLEAISEKYGIPVEKIVKIYKKSKKGILVNMDDNIIEHYSNEDTFILNVESLAEQGYKITLTEI", "text": "FUNCTION: Transcription factor playing an important role in primary neurulation and in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. SUBCELLULAR LOCATION: Nucleus Membrane Note=detected at cell-cell contact areas. SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily."}
{"protein": "MNFIHDYRSPRVIFGPDSLARLPQELERLGIDRALVLTTPEQAPLGRQVAEPVIGHVAAFYDGATMHVPALVAEEACKIARTSEANGVIAIGGGSTIGLAKIVALRTELPIVAVPTTYAGSEMTSIFGITEGGVKKTGRDARVMPRAVIYEPRLTLELPLSISVTSAINAIAHAVEGLYAPDATPLLTIMAQEGIAATVRAISRMYQSPRDLQARGDALYGAWLCASVLGNVSMALHHKLCHTLGGTLDLPHAQTHTVVLPHALAYNARAVPDAMRVLRIALGHDDPPTALYELARDNGAPVALRDLGMREEDIEHVGDLALQDRYPNPRELDRDALLALLRDAYHGRPPSA", "text": "SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family."}
{"protein": "MFIINKNLPHFKNDFSDYYSKLDNDLSISSPKFESPVLSQPKVKPLSHDIISICSTKITPLDDFNFLKVISKGGFGKVYLAENKITKKTVAIKVIKKSDTIKKMMVDQVNIEKTILSNYKCNFIVELFSSFQTDKKLFFVMEFLNGGDCASLLRSFNNNMPEDLTKNIIAQIIICLEYLHNHGIIHRDLKPDNILIDSNGHIKLADFGLSKFDFVDESCNIKILKNSFTLYNTNNNNTTENQKILGTPYYIPPEVILGKGYGKTIDWWSLGIILYEFLIGYPPFQEDEPNESINPKSDNDEKNVRIIFNKITNHKKKLYFPKKLYPVAIDLIEKLLDPNPSVRLGANGVDEVKCHPFFSEINWKIYEDQKVLVFQPFVENDCDTSYFIERKEENNKNKINDDIDSLILNQNNQNIYKNNNNNNNNNNNNNNNNNNNNNNDDNDDENNIIDQNLFIDFDFPTY", "text": "SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family."}
{"protein": "NSVPTERLRMATLDVDPEASCSKLSTSPSNTSLTHRFLDNKFYLLVVIGEIVTEDHLRCAISDIERGIRSWDTDLISCNLDQELKLFVSRHSARFSADVRGQKILHHRSDVLETVVLINPSDEAVSTEVRLMITDAARHKLLVLTGQCCENTGELILQSGSFSFQNFIEIFTDQEIGELLSTTHPANKANLTLFCPEEGDWKNANLKKHNLQDFINIKLNSVSILPEMEGLSEFTEYLSESVEVPSSFDVLEPPASGGFLKLSKPCCYIFPGGRGDSALFAVNGFNMLINGGSDRRSCFWKLVRHLDRVDSILLTHNGADNLPGVNSLLQRKIAELEEEQSQGSTANSDWMKNLISPELGVVFLNVPENVTNLQPNFRVRRNTEETCLTLQYLNKLCVKPEPLFRTVGNVIDPVILFQKMGVGRLEMYILNSVKGSKELQFFMQHWSSNNKAKTGLILPNGKDAEISFPYLTSISSLIVWHPANPSEKIVRALFPGNAPQYNILDGLEKLKHLDFLKHPVVTQKELIASSAAPTVKQAKLKQWSDSKESLKSNSRPSVGKGVKKDVKEETPELTKPTAVSHQEAVNEKPQKVEKKEKPVVKKERPRTELQSKPEEKDAKAKADAAKQELEEKMQKDEKLKSESKPKPLKEKIVKKEVKAKKPEEKKKEEKDVKKESAKPDRKEEKAVIKKEKVKKEEKPKKEEVKKDVKKDVKKEVKKKGN", "text": "SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Note=Associated with membranes of intracellular organelles. SIMILARITY: To T.californica electromotor neuron-associated protein 2."}
{"protein": "VKSTNLMAFVATKMLERQEDLDTCTEMQVEKMKTSTKARLRTESSFAPRTWEDAIKDGELLFNGTILQAESPTMTPASVEMKGKKFPIDFAPSNIAPIGQNPIYLSPCIPNFDGNVWEATMYHHRGATLTKTMNCNCFQRTIWCHPNSSRMRLSYAFVLYCRNTKKICGYLIARQVAGIETGIRKCFRCIKSGFVMATDEISLTILQSIKSGAQLDPYWGNETPDIDKTEAYMLSLRETGP", "text": "FUNCTION: Suppresses the RNA silencing-based antiviral response in Drosophila cells. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus."}
{"protein": "MAIKKRNKIRLPSGSPEEVGIDGSAHKPMQQIKPLVSNDSEDDDNDICVLQPIKFKKVPKRDITFDGEQAIKEDNSHYEDLYHSKKNTNASTRNKDDLLILNMEDLMEGNHHLLSDSSEAGSSSEGEHISSIPTRGEIAKLKAQKSLSRRKISESDVTTERDYVKLLDSEDKREIMETIRLNGGLKRNNEKEITNFSDDEMQGFQDEMLALTDNQIAIQKDSKRKIIEKAINEVPYRTNEEWETQLLSKGNINKSNEKIITPLPVLFPDDDESGNSIERINEMVSKICLQRKKVEMRLQALEKTKIDLEKSKASLINKLIGN", "text": "FUNCTION: Involved in pre-mRNA splicing and spliceosome disassembly. Promotes release of excised lariat intron from the spliceosome by acting as a receptor for PRP43. This targeting of PRP43 leads to disassembly of the spliceosome with the separation of the U2, U5, U6 snRNPs and the NTC complex. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MGGFQRGKYGTMAEGRSEDNLSATPPALRIILVGKTGCGKSATGNSILGQPVFESKLRAQSVTRTCQVKTGTWNGRKVLVVDTPSIFESQADTQELYKNIGDCYLLSAPGPHVLLLVIQLGRFTAQDTVAIRKVKEVFGTGAMRHVVILFTHKEDLGGQALDDYVANTDNCSLKDLVRECERRYCAFNNWGSVEEQRQQQAELLAVIERLGREREGSFHSNDLFLDAQLLQRTGAGACQEDYRQYQAKVEWQVEKHKQELRENESNWAYKALLRVKHLMLLHYEIFVFLLLCSILFFIIFLFIFHYI", "text": "FUNCTION: Plays a role in T lymphocyte development and the optimal generation of CD4/CD8 double-positive thymocytes (By similarity). Inhibitor of GSK3A, possibly by sequestering GSK3A in cytoplasmic vesicles and impairing its translocation to the nucleus. Consequently, impairs GSK3A-dependent transcriptional program and regulation of the DNA damage response occurring during T cells proliferation (PubMed:29382851). Required for the survival of peripheral T cells, natural killer (NK) and NK T-cell development and the maintenance of normal liver function (By similarity). May promote the survival of mature T lymphocytes upon cytokine withdrawal (By similarity). May regulate Ca(2+) homeostasis by modulating lysosomal Ca(2+) stores, preventing its accumulation in the absence of T cell activation (By similarity). May play a role in mitochondrial DNA segregation in hematopoietic tissues (By similarity). Is a regulator of liver endothelial cell homeostasis (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type IV membrane protein Endosome, multivesicular body membrane; Single-pass type IV membrane protein Endosome membrane; Single-pass type IV membrane protein Note=The mitochondrial localization originally reported was observed with C-terminally tagged protein and was not confirmed in later publications. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family. IAN subfamily."}
{"protein": "MSRVSQARNLGKYFLLVDNMLVVLGFFVVFPLISIRFVDQMGWAALMVGIALGLRQFVQQGLGVFGGAIADRFGAKPMIVTGMLLRAAGFATMGIAHDPWLLWFSCFLSGLGGTLFDPPRTALVVKLIRPRQRGRFFSLLMMQDSAGAVIGALLGSWLLQYDFRLVCATGAALFILCAAFNAWLLPAWKLSTVKAPVREGLGRVMADKRFVTYVLTLTGYYMLAVQVMLMLPIMVNDIAGSPAAVKWMYAIEACLSLTLLYPIARWSEKRFRLEHRLMAGLLVMTLSMMPIGLVSSVQQLFVLICTFYIGSIIAEPARETLGAGLADPRARGSYMGFSRLGLALGGALGYAGGGWLFDSGKAMNQSELPWVMLGVVGFITLIALWWQFSPKRSASGMLEPGA", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. MdtH (TC 2.A.1.2.21) subfamily."}
{"protein": "MAEKQAGLVGEPDPEGSSPGTSESWNYDSNCVFCRVAAGQEPKTELFHCENEDLVCFKDIKPAALYHYLVVPKKHIGSCKDLNKDHIEMVESMVAAGKTMLERNNFTDFTDVRMGFHVPPFCSISHLHLHVIAPVKEFGFLSKLVYRQDSYWFVTVDYLLEKLRK", "text": "FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha- acetyl lysine methyl ester)) generated by lysine tRNA ligase (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HINT family."}
{"protein": "MDFKDYYKILDVEPAADDKAIKTAYRKLARKYHPDVSKEAGAEDKFKEASEAYEVLSSPEKRAEYDELRKYGRQGRPFQTPPGWQSRAGAGAGGFEETADFSEFFSSIFGGRPQQGGRTRNPGRKGQDVEMELAVFLEETLSGESKQVSFKVPQHSPNGQRMGDITKTLNVKIPAGVVDGERIRLKGQGAPGIGGGANGDLYLIIRLAPHPMFEVEGHDLVITVPLAPWEAALGTKVAVPTLTSRLNLTIRPDSQNGQRLRIKGNGLMNKSGERGDLYAQLKIVMPKQTDEAARALWQKLADSAAFDPRAQWKG", "text": "FUNCTION: DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. SUBCELLULAR LOCATION: Cytoplasm, nucleoid."}
{"protein": "MSEYREIITKAVVAKGRKFTQCTNTISPEKKPSSILGGWIINHKYDAEKIGKTVEIEGYYDINVWYSYADNTKTEVVTERVKYVDVIKLRYRDNNYLDDEHEVIAKVLQQPNCLEVTISPNGNKIVVQAEREFLAEVVGETKVVVEVNPDWEEDDEEDWEDELDEELEDINPEFLVGDPEE", "text": "FUNCTION: Morphogenic protein required for the assembly of the outer coat of the endospore. Is also a regulatory protein for the expression of cotA, cotB, cotC, cotH and other genes encoding spore outer coat proteins. SUBCELLULAR LOCATION: Spore coat Note=Localizes between the two coat layers in the mature spore. SIMILARITY: Belongs to the CotE family."}
{"protein": "MAFSDLTSRTVHLYDNWIKDADPRVEDWLLMSSPLPQTILLGFYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGIGYSFRCDIVDYSRSPTALRMARTCWLYYFSKFIELLDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYSYYGLSALGPAYQKYLWWKKYLTSLQLVQFVIVAIHISQFFFMEDCKYQFPVFACIIMSYSFMFLLLFLHFWYRAYTKGQRLPKTVKNGTCKNKDN", "text": "FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the ELO family. ELOVL7 subfamily."}
{"protein": "MSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLKDVEEGDEKFE", "text": "FUNCTION: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation (By similarity). FUNCTION: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm Cytoplasm, cytoskeleton, spindle Note=Primarily detected in the cytoplasm, and at low levels in nucleus. Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Primarily detected in the cytoplasm, and at low levels in nucleus and nucleolus (PubMed:19602484, PubMed:17475909). Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (PubMed:19759903). SIMILARITY: Belongs to the SDO1/SBDS family."}
{"protein": "MRVSVPGPAAAAAPAAGREPSTPGGGSGGGGAVAAASGAAVPGSVQLALSVLHALLYAALFAFAYLQLWRLLLYRERRLSYQSLCLFLCLLWAALRTTLFSAAFSLSGSLPLLRPPAHLHFFPHWLLYCFPSCLQFSTLCLLNLYLAEVICKVRCATELDRHKILLHLGFIMASLLFLVVNLTCAMLVHGDVPENQLKWTVFVRALINDSLFILCAISLVCYICKITKMSSANVYLESKGMSLCQTVVVGSVVILLYSSRACYNLVVVTISQDTLESPFNYGWDNLSDKAHVEDISGEEYIVFGMVLFLWEHVPAWSVVLFFRAQRLNQNLAPAGMINSHSYSSRAYFFDNPRRYDSDDDLPRLGSSREGSLPNSQSLGWYGTMTGCGSSSYTVTPHLNGPMTDTAPLLFTCSNLDLNNHHSLYVTPQN", "text": "FUNCTION: Lysosomal integral membrane protein that may regulate MTORC1 complex translocation to lysosomes. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GPR137 family."}
{"protein": "MVVRIRLSRFGCKNRPFFRVMAADSRSPRDGKHLEVLGYFNPLPGQDGGKRMGLKFDRIKYWLSVGAQPSDPVQRLLFRSGLLPPPPMVAMGRKGGARDTRPVDPMTGRYVDAENKTVNANDNQPKEEDTEAKSA", "text": "SUBCELLULAR LOCATION: Mitochondrion Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family."}
{"protein": "MTELAQLQASAEQAAALLKAMSHPKRLLILCMLSGSPGTSAGELTRITGLSASATSQHLARMRDEGLIDSQRDAQRILYSIKNEAVNAIIATLKNVYCP", "text": "FUNCTION: Functions as transcription repressor."}
{"protein": "MEIVIRTGSGDVRGSKENGIAVFRGIPYAEPPVGAHRFTAPRPPRPWDGVRDATEFSATAPRPPYPEAIGALLIERFIPGDDYLTLNVWTPDPNAVGLPVMVWIHGGAFTNGSGSEPVYDGAAFARDGVVFVSFNYRLGIIGFADLPDAPSNRGLLDQIAALEWVRDNIARFGGDPGNVTVFGESAGAMSVCTLMATPRARGLFRRAILQSGAGNMAVAAEDATTIAAVIAHRLGVEPTAAALAHVPVAQLLDVQQQVAQEIQGAPDPAVWGERIAGGSVLLPFAPVIDGELLSQRPAEAIAGGAGHDVDLLFGTTTDEYRLFLAPTGLLPFITSDYVTAHLAKSGLDADAAKAYTAEGRGEEPGDILASIITDQVFRIPALRIAESRVDAPARTFGYEFAWRTPQLDGILGACHAVELPFVFRTLDRAASLVGTNPPEELAETVHNAWVRFATSGDPGWPAWNPETRSVMRFDHPVSEMVTDPYPATRALWDGVPL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "DVSGTVCLSALPPEATDTLNLIASDGPFPYSQDGVVFQNRESVLPTQSYGYYHEYTVITPGARTRGTRRIITGEATQEDYYTGDHYATFSLIDQTC", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ribonuclease N1/T1 family."}
{"protein": "MYKMNICNKPSNKTAPEKSVWTAPAQPSGPSPELQGQRSRRNGWSWPPHPLQIVAWLLYLFFAVIGFGILVPLLPHHWVPAGYACMGAIFAGHLVVHLTAVSIDPADANVRDKSYAGPLPIFNRSQHAHVIEDLHCNLCNVDVSARSKHCSACNKCVCGFDHHCKWLNNCVGERNYRLFLHSVASALLGVLLLVLVATYVFVEFFVNPMRLRTNRHFEVLKNHTDVWFVFLPAAPVETQAPAILALAALLILLGLLSTALLGHLLCFHIYLMWHKLTTYEYIVQHRPPQEAKGVHRELESCPPKMRPIQEMEFYMRTFRHMRPEPPGQAGPAAVNAKHSRPASPDPTPGRRDCAGPPVQVEWDRKKPLPWRSPLLLLAMWGPQAPPCLCRKRGRGACIKCERLRPRIRRRGLGPPAAAPARRRIPRTPALCTPLALPAPTTRRRQSPWTRFQWRRRAWAAPLWPPRGAGADSPRWRGRRVRPPFS", "text": "FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (By similarity). Has a palmitoyltransferase activity toward NCDN and regulates NCDN association with endosome membranes through this palmitoylation. FUNCTION: Has also a palmitoyltransferase activity-independent function in DNA virus-triggered and CGAS-mediated innate immune response (PubMed:25299331). Functions as an activator of STING1 by promoting its cGAMP-induced oligomerization and the recruitment of downstream signaling components (PubMed:25299331). SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MAVFPSSGLPRCLLTLILLQLPKLDSAPFDVIGPPEPILAVVGEDAELPCRLSPNASAEHLELRWFRKKVSPAVLVHRDGREQEAEQMPEYRGRATLVQDGIAKGRVALRIRGVRVSDDGEYTCFFREDGSYEEALVHLKVAALGSDPHISMQVQENGEICLECTSVGWYPEPQVQWRTSKGEKFPSTSESRNPDEEGLFTVAASVIIRDTSAKNVSCYIQNLLLGQEKKVEISIPASSLPRLTPWIVAVAVILMVLGLLTIGSIFFTWRLYNERPRERRNEFSSKERLLEELKWKKATLHAVDVTLDPDTAHPHLFLYEDSKSVRLEDSRQKLPEKTERFDSWPCVLGRETFTSGRHYWEVEVGDRTDWAIGVCRENVMKKGFDPMTPENGFWAVELYGNGYWALTPLRTPLPLAGPPRRVGIFLDYESGDISFYNMNDGSDIYTFSNVTFSGPLRPFFCLWSSGKKPLTICPIADGPERVTVIANAQDLSKEIPLSPMGEDSAPRDADTLHSKLIPTQPSQGAP", "text": "FUNCTION: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Secreted. SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family."}
{"protein": "MLIPFLFKLTLPLASGIALSSCGTLPEADLGTAAGNQTSSEPTNSVEIVQANQPEIKAVPVIDGLEHPWGMAWLPNGDILITERPGRLRIVRDGVLDPEAIAGVVAVSTVSAQQLFASQQGGLLDIALHPRFAENRFVYFTYSHGTQQANRTRVARAVFDGEKLTDWQVIFEVGQTKPGGQHFGSRLTWLPDETLLVSIGDGGNPPVELEGDFIRQQAQNRASHLGKIIRINDDGTVPADNPFRNDPKAAPEVWSYGHRNIQGLAYDPVTQKVWATEHGSRGGDELNLIQKGKNYGWPVVSFSKEYSTDQPVAPATSRPDMVDPLQIWTPAIAPSGLTIYNGDRHPEWQGTIFAGGLVDRGIRHLRLDENNQIIDETTISIGQRVRDVRQGPDGHVYVLTDQNNGQLLRLES", "text": "SIMILARITY: Belongs to the PQQ oxidoreductase GdhB family."}
{"protein": "MEPVNDFQEGISTEHAFEAEPVPSLSETITPRSMVVSFILSVTLSIVAMKVTLSSGFIPSFSIPAGLLGFCVSRASIRILDYFAVAQLPFTRQENTIIQTCVVACTSITFTGGFGTYILAMGKKAAVGDVNAQNNVEEPSFARMITFLFLISFAGMFIIMPFRKVMIIRHRLTFPSGTATAHLINSFHTPQGVKQARKQVTLLFKSFGGTIAWSLFQWFFASGPGCGFKFFPTFGLEAYKHGFFFDFTMANVGIGMMCPYMIVFSVFIGTIISCGVIWPYIESKEGIWYPSNLGPNSLNGIRGYKVFIGLSMIMADCLFVFLCIMVRTTCAMIKRRRQAMQGGGGNAQPFQGIDIADQPVKSFDDRRRAQVFLRDEIPDSVTIGCYVLLSIISIAAIPHLYPQMRYSHVALIYLAAPVFAFCNAYGFGVTDMNLASTYCKIAMFAFGSWVGIKSGGVVAALVAGGITMSILGNAADVAQDLKTGYLTLTSPRAVFISEAIGTALGCVVNPTVFWVFYRVYKMGSGDMGDMPYAKLYRGFAMLSVGDGEQGLPRHSMLLFKVFFVLALALSVFREVASRKEWRIRRYIPSTIGMAITFFMPPRVPVGMCIGSLVAYLWEKMDAGRGRMLSPALASGLICGDGVGSILLSMLTLMGARAPICIKFLSRGDNVKLDAFLATLHDMR", "text": "FUNCTION: May be involved in the transport of nicotianamine-chelated metals. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the YSL (TC 2.A.67.2) family."}
{"protein": "MAPGGSALKEALESNSTGVDYEVKMAKVEANSKPTKSGSGSIGKFHSSNGVYELLECPVCTNLMYPPIHQCPNGHTLCSSCKLRVQNTCPTCRYELGNIRCLALEKVAESLEVPCRYQNLGCQDIFPYYSKLKHEQHCRFRSYSCPYAGSECSVTGDIPTLVDHLKDDHKVDMHDGCTFNHRYVKSNPHEVENATWMLTVFNCFGRQFCLHFEAFQLGMAPVYMAFLRFMGDENEAKKFSYSLEVGAHSRKLTWQGIPRSIRDSHRKVRDSQDGLIIPRNLALYFSGSDKEELKLRVTGRIWKEE", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:28351989, PubMed:32786047). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:28351989, PubMed:32786047). It probably triggers the ubiquitin- mediated degradation of different substrates (PubMed:28351989, PubMed:32786047). Mediates the proteasomal-dependent degradation of ATG6, a component of the autophagosome complex (PubMed:28351989). Requires TRAF1A/MUSE14 and TRAF1B/MUSE13 to target ATG6 for ubiquitination and subsequent regulation of autophagosome assembly (PubMed:28351989). Modulates directly the ubiquitination and proteasomal-dependent degradation of FREE1, a component of the ESCRT-I complex (PubMed:32786047, PubMed:32753431). Modulates directly the ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a component of the ESCRT-I complex (PubMed:32753431). SUBCELLULAR LOCATION: Endosome, multivesicular body Cytoplasmic vesicle, autophagosome. SIMILARITY: Belongs to the SINA (Seven in absentia) family."}
{"protein": "MTVRKNPAGGWICELYPNGAKGKRIRKKFATKGEALAFEQYTVQNPWQEEKEDRRTLKELVDSWYSAHGITLKDGLKRQLAMHHAFECMGEPLARDFDAQMFSRYREKRLKGEYARSNRVKEVSPRTLNLELAYFRAVFNELNRLGEWKGENPLKNMRPFRTEEMEMTWLTHDQISQLLGECNRHDHPDLETVVRICLATGARWSEAESLRKSQLAKYKITYTNTKGRKNRTVPISKELYESLPDDKKGRLFSDCYGAFRSALERTGIELPAGQLTHVLRHTFASHFMMNGGNILVLQRVLGHTDIKMTMRYAHFAPDHLEDAVKLNPLVHITNSK", "text": "FUNCTION: Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. SIMILARITY: Belongs to the 'phage' integrase family."}
{"protein": "MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC", "text": "FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis. SUBCELLULAR LOCATION: Host cell membrane; Lipid-anchor; Cytoplasmic side Virion Secreted Host Golgi apparatus membrane Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. SIMILARITY: Belongs to the lentivirus primate group Nef protein family."}
{"protein": "MPGLKRILTVTILALWLPHPGNAQQQCTNGFDLDRQSGQCLDIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSNPYSTSYSGPYPAAAPPVPASNYPTISRPLVCRFGYQMDEGNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQLCANVPGSYSCTCNPGFTLNDDGRSCQDVNECETENPCVQTCVNTYGSFICRCDPGYELEEDGIHCSDMDECSFSEFLCQHECVNQPGSYFCSCPPGYVLLDDNRSCQDINECEHRNHTCTSLQTCYNLQGGFKCIDPISCEEPYLLIGENRCMCPAEHTSCRDQPFTILYRDMDVVSGRSVPADIFQMQATTRYPGAYYIFQIKSGNEGREFYMRQTGPISATLVMTRPIKGPRDIQLDLEMITVNTVINFRGSSVIRLRIYVSQYPF", "text": "FUNCTION: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (By similarity). Stabilizes and organizes elastic fibers in the skin, lung and vasculature. Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:11805835). May act as an adapter that mediates the interaction between FBN1 and ELN (By similarity). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space, extracellular matrix Note=co-localizes with ELN in elastic fibers. SIMILARITY: Belongs to the fibulin family."}
{"protein": "MRPLTEEETRVMFEKIAKYIGENLQLLVDRPDGTYCFRLHNDRVYYVSEKIMKLAANISGDKLVSLGTCFGKFTKTHKFRLHVTALDYLAPYAKYKVWIKPGAEQSFLYGNHVLKSGLGRITENTSQYQGVVVYSMADIPLGFGVAAKSTQDCRKVDPMAIVVFHQADIGEYVRHEETLT", "text": "FUNCTION: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. FUNCTION: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NIP7 family."}
{"protein": "MIEPLDSPASDSDFLDYPSALGNCTDEQISFKMQYLPVIYSIIFLVGFPGNTVAISIYIFKMRPWRGSTVIMLNLALTDLLYLTSLPFLIHYYASGENWIFGDFMCKFIRFGFHFNLYSSILFLTCFSLFRYVVIIHPMSCFSIQKTRWAVVACAGVWVISLVAVMPMTFLITSTTRTNRSACLDLTSSDDLTTIKWYNLILTATTFCLPLVIVTLCYTTIISTLTHGPRTHSCFKQKARRLTILLLLVFYICFLPFHILRVIRIESRLLSISCSIESHIHEAYIVSRPLAALNTFGNLLLYVVVSNNFQQAFCSIVRCKASGDLEQGKKDSCSNNP", "text": "FUNCTION: Receptor for alpha-ketoglutarate. Seems to act exclusively through a G(q)-mediated pathway. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTAALAAARAAATMASGSSGLAAARLLSRAFLLQQNGIRHCSYTTSRKHLYVDRNTKIICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGKTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAVAAIDEAIEAEVSLVVCITEGIPQQDMVRVKHKLLRQGKTRLVGPNCPGVINPGECKIGIMPGHIHKKGRVGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFTDCLEIFLNDPATEGIILIGEIGGNAEENAAEFLKQHNSGPKAKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKIAALQSAGVVVSMSPAQLGTTMYKEFEKRKML", "text": "FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family."}
{"protein": "MEDSDSAAKQLGLAEAAAVAAAAAVAAAAAAAAGGEAEEPVLSRDEDSEEDADSEAERETPRVTAVAVMAAEPGHMDMGAEALPGPDETAAAAAFAEVTTVTVANVGAAADNVFTTSVANAASISGHVLSGRTALQIGDSLNTEKATLIVVHTDGSIVETTGLKGPAAPLTPGPQSPPTPLAPGQEKGGTKYNWDPSVYDSELPVRCRNISGTLYKNRLGSGGRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDNMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTFTVTPSGQITTSGALTFDRASTVEATAVISESPAQGDVFAGATVQEASVQPPCRASHPEPHYPGYQDSCQIAPFPEAALPTSHPKIVLTSLPALAVPPPTPTKAAPPALVNGLELSEPRSWLYLEEMVNSLLTTAQQLKTLFEQAKHASTYREAAANQAKIHADAERKEQSCVNCGREAMNECTGCHKVNYCSTFCQRKDWKDHQHICGQSAAVTVQADEVHVAESVMEKVTV", "text": "FUNCTION: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. Regulates epithelial cell proliferation and side-branching in the mammary gland. Required for neural tube closure and skeletal patterning. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Transcriptional activator of EIF4G3. May also involved in behavior (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSDLPRISVAAPRLDGNERDYVLECMDTTWISSVGRFIVEFEKAFADYCGVKHAIACNNGTTALHLALVAMGIGPGDEVIVPSLTYIASANSVTYCGATPVLVDNDPRTFNLDAAKLEALITPRTKAIMPVHLYGQICDMDPILEVARRHNLLVIEDAAEAVGATYRGKKSGSLGDCATFSFFGNKIITTGEGGMITTNDDDLAAKMRLLRGQGMDPNRRYWFPIVGFNYRMTNIQAAIGLAQLERVDEHLAARERVVGWYEQKLARLGNRVTKPHVALTGRHVFWMYTVRLGEGLSTTRDQVIKDLDALGIESRPVFHPMHIMPPYAHLATDDLKIAEACGVDGLNLPTHAGLTEADIDRVIAALDQVLV", "text": "FUNCTION: Catalyzes the synthesis of GDP-perosamine from GDP-4-keto-6- deoxy-D-mannose and L-glutamate. Can use only L-glutamate as amino donor. In vitro, can also use GDP-4-keto-3,6-dideoxymannose to produce GDP-3-deoxyperosamine. Involved in the formation of S-LPS, which is required for attachment of the protein S-layer to the outer membrane surface. SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family."}
{"protein": "MLSVGRGIADITGEAADCGMLGYGKSDQRTAGIHQRLRSRAFVFRDDSQDGDARLLLIVAELPLPMQNVNEEVLRRLADLYGDTYSEQNTLITATHTHAGPGGYCGYLLYNLTTSGFRPATFAAIVDGIVESVEHAHADVAPAEVSLSHGELYGASINRSPSAFDRNPPADKAFFPKRVDPHTTLVRIDRGEATVGVIHFFATHGTSMTNRNHLISGDNKGFAAYHWERTVGGADYLAGQPDFIAAFAQTNPGDMSPNVDGPLSPEAPPDREFDNTRRTGLCQFEDAFTQLSGATPIGAGIDARFTYVDLGSVLVRGEYTPDGEERRTGRPMFGAGAMAGTDEGPGFHGFRQGRNPFWDRLSRAMYRLARPTAAAQAPKGIVMPARLPNRIHPFVQEIVPVQLVRIGRLYLIGIPGEPTIVAGLRLRRMVASIVGADLADVLCVGYTNAYIHYVTTPEEYLEQRYEGGSTLFGRWELCALMQTVAELAEAMRDGRPVTLGRRPRPTRELSWVRGAPADAGSFGAVIAEPSATYRPGQAVEAVFVSALPNNDLRRGGTYLEVVRREGASWVRIADDGDWATSFRWQRQGRAGSHVSIRWDVPGDTTPGQYRIVHHGTARDRNGMLTAFSATTREFTVV", "text": "FUNCTION: Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid. Also catalyzes the synthesis of Cers from Sph and fatty acid. Cers containning C6-C24 fatty acids are well hydrolyzed, and Cers with mono unsaturated fatty acids are much more hydrolyzed than those with saturated fatty acids. SIMILARITY: Belongs to the neutral ceramidase family."}
{"protein": "MLGSSGRRLLTTVLQAQRWPFQPSRDMRLVQFQAPHLAGPHLGLESGNGGGVIDLNAFEPTLPKTMVEFLEQGEATLSVVRRALATQLPVLPRSEVTFLAPVTRPDKVVCVGMNYADHCREQNVPVPKEPIIFSKFASAIVGPYDNIILPPESQEVDWEVELAVVIGKRGKYIKATDAMAHVAGFTVAHDVSARDWQMGRNGKQWLLGKTFDTFCPLGPALVTKDSVADPHNLKICCRVNGELMQSSNTNQMVFKTEELITWVSQFVTLYPGDIILTGTPPGVGVFRKPPVFLKKGDEVQCEIEELGVIINKVV", "text": "FUNCTION: May have hydrolase activity. SIMILARITY: Belongs to the FAH family."}
{"protein": "MNAKRPVNLDLTKFHFPPMAILSIGHRISGFVLFLCMPLMFYLLHRATASAESFYHLHQLLLHNGWIKLAVWIMLSATLFHLFAGIRHLAMDLGFWESVPEGRISAYTVFVVSFIAIVLAGVWIW", "text": "FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b560 family."}
{"protein": "MQTPRPAMRMEAGEAAPPAGAGGRAAGGWGKWVRLNVGGTVFLTTRQTLCREQKSFLSRLCQGEELQSDRDETGAYLIDRDPTYFGPILNFLRHGKLVLDKDMAEEGVLEEAEFYNIGPLIRIIKDRMEEKDYTVTQVPPKHVYRVLQCQEEELTQMVSTMSDGWRFEQLVNIGSSYNYGSEDQAEFLCVVSKELHSTPNGLSSESSRKTKSTEEQLEEQQQQEEEVEEVEVEQVQVEADAQEKAQSSQDPANLFSLPPLPPPPLPAGGSRPHPLRPEAELAVRASPRPLARPQSCHPCCYKPEAPGCEAPDHLQGLGVPI", "text": "FUNCTION: Is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. It acts as a substrate- adapter for CUL3-RING ubiquitin ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of TCHP, a protein involved in ciliogenesis down-regulation (PubMed:25270598). May be involved in endoplasmic reticulum calcium ion homeostasis (PubMed:25983243). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MHKKKHIKHGTNKQEIINIGTKSPTFQEKQRPSKTDQRSTVWREEQKKQELKVHRIFHPQPRTGFDVGKGIDPWLTTWQMITVILATLCIILVTKVGFLIPSLFSKGEKQSRKFSLLDPLCDRNDDSSCDFCSSDWIAFGNNFYCVFRENSKTWVESQSACEELNSHLVIIDSKAEVENLLLFEMDGWILHRMDGTNSSRLWGNDIKIRNTLMNDSEKKNHSCHYLRGNIFMPDECSAKKTYICEFNI", "text": "FUNCTION: Lectin-like receptor for natural killer (NK) cells. Heterodimer formation with KLRE1 mediates NK cell cytolytic activity. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
{"protein": "MPKVVSRSVVCSDTRDREEYDDGEKPLHVYYCLCGQMVLVLDCQLEKLPMRPRDRSRVIDAAKHAHKFCNTEDEETTYLRRPEGIERQYRKKCAKCGLPLFYQSQPKNAPVTFIVDGAVVKFGQGFGKTNIYTQKQEPPKKVMMTKRTKDMGKFSSVTVSTIDEEEEEIEAREVADSYAQNAKVIEKQLERKGMSKRRLQELAELEAKKAKMKGTLIDNQFK", "text": "FUNCTION: Stimulates membrane curvature formation and subsequent endoplasmic reticulum exit site (ERES) establishment by recruiting PI3K complex I, leading to COPII vesicle-mediated transport (By similarity). Promotes endoplasmic reticulum (ER) exit of cGAMP-activated STING1 oligomers (PubMed:32690950). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Detected in the nucleus and cell soma of pyramidal neurons in the brain cortex and Purkinje cells, as well as in neurons in the granular layer in the cerebellum. SIMILARITY: Belongs to the STEEP1 family."}
{"protein": "MNTSPGTVGSDPVILATAGYDHTVRFWQAHSGICTRTVQHQDSQVNALEITPDRTMIAAAGYQHIRMYDLNSNNPNPIISYDGVNKNVASVGFHEDGRWMYTGGEDCTARIWDLRSRNLQCQRIFQVNAPINCVCLHPNQAELIVGDQSGAIHIWDLKTDHNEQLIPEPEVSITSAHIDPDASYMAAVNSTGNCYVWNLTGGIGDEVTQLIPKTKIPAHTRYALQCRFSPDSTLLATCSADQTCKIWRTSNFSLMTELSIKSSNPGESSRGWMWGCAFSGDSQYIVTASSDNLARLWCVETGEIKREYGGHQKAVVCLAFNDSVLG", "text": "FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR- mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser- 657' (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the WD repeat LST8 family."}
{"protein": "MAVAYADKPNHFINFPLTQFQGFVLNYKGLQFQLLDEGVDCKIQTAPHISLAMLDIQPEDYRSVDVAIQEVIDDMHWGEGFQIKFENPHILGRCIVLDVKGVEELHDDLVNYIRDKGCVADQSRKWIGHCTIAQLTDAALSIKENVDFINSMQFNYKITINPSSPARLEIVKLGAEKKDGFYETIASHWMGIRFEYNPPTDKLAMIMGYCCSEVVRKELEEGDLPENDDDAWFKLSYHYENNSWFFRHVYRKSSYFRKSCQNLDCNCLGFYESSVEED", "text": "SIMILARITY: Belongs to the coronaviruses ns2a protein family."}
{"protein": "MTVLAWCIAWLLDFVIGDPQNWPHPVRWIGNLISATQRVVRRYCHSDRSLRIGGAVMWLVVVGVTWAVSWGVLALASEIHPWFGWLVEIWMIFTVLAGRCLANAARDVERPLRAGDLAESREKLSWIVGRDTSQLQPEQVNRAVVETVAENTVDGIIAPLFFLFLGGAPLAMAYKAVNTLDSMVGYKHEKYRAIGMVSARLDDIANVIPARLSWLLLSIAAALCRYDGYRALHIGWRDRYNHSSPNCAWSEASVAGALGIRLGGPNDYFGERVEKPWIGDAQRGISVDDISRTIRLMWVASTLALALFIAVRCLLVGAA", "text": "FUNCTION: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CobD/CbiB family."}
{"protein": "MAKSKNHTTHNQSRKWHRNGIKKPRSQRYESLKGVDPKFLRNMRFAKKHNKKGLKKMQANNAKAVSARAEAIKALVKPQAVKPKMPKGSSRKLSRLAFIAHPKLGKKIRSYMAKGRRLCQPKPKVQTKAEAKAPAKAQAKAPAQAPKGAQAPVKAP", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family."}
{"protein": "MKRPCEETTSESDLDETIDVGSENNYPGHATSSVMRSNSPTTTSQIMARKKRRGIIEKRRRDRINNSLSELRRLVPTAFEKQGSAKLEKAEILQMTVDHLKMLQATGGKGYFDAHALATDFMSIGFRECLTEVARYLSSVEGLDPSDPLRVRLVSHLSTCASQREAAVMTSSMAHHHHPLHPHHWAAAFHHLPTALLQPNGLHTSESTPCRLSTSSEVPSAHGSALLTATFAHADSALRMPSGGTVAPCVPPLSTSLLSLSATVHAAAAAATAAAHSFPLSFAGAFPMLPSNAAAAAAVAAATAISPPLSVSAASSPQQTSTGTNNKPYQPWGTEVGAF", "text": "FUNCTION: Transcriptional repressor which functions as a downstream effector of Notch signaling in cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY1 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HEY family."}
{"protein": "MKYRFIDHTADIAFEVYGSNLRELFENAALAFYDAFVDTSGIGIEREVGVECEGEDVEITLYRWLNELLYLFDTEFFAAKDVEVEVEEGDGVKASGKLRGGRFSAEMVKVEPKAITLHKFRVEKTDKGYVAFVVVDI", "text": "FUNCTION: Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). SIMILARITY: Belongs to the archease family."}
{"protein": "MRKLCGNGSTSMISTDSYKNTTFFVIAFSTFLISCIDYTKLFSSLSTPEAVGRLEDVLIGQCITKGSFAHTLFLIILSAFFIFQVANFAMSVPRLLDMYRFYTHLLGVPDADIQTLPWPEIVRLIGDIRKHNPVTSLSNGQATALADMVGNDAKAPVKKLDAHDIANRILRQENYLIALFNKDLLDLRVRIPVPHIFTAFIPSSMLILSADPPLPSLQSEPERKFLSFGANHLTKALEWNLRFCLLGYLFDRRGQVRKEFVREKRRKDLVQGLRRRFVFMGILNAIFAPFIILYLLIYSFFRYFEEYHKNPSSIGSRQYTPYAQWKFREFNELPHLFERRLDRSYETAKEYVDQFPKERTALVMRFVAFVAGSFAAVLLVASLIDPDLFLHFEITPHRTVLFYLGVFGSVLAISRGMVPQENMVFDPEASLNEVVRWTHYLPVEWRGQLHSQMVHQEFSKLFALKIMIFFSELLSVILTPFILFFSLPPCAAAIIDFFREFTVHVDGVGYVCSFAVFDFARHGNIDSNRPETGVQGATGPDAGDSGGGGGGGGGGFAAGKSGRQTTRRAASASPSRFKQKDWRSNENKMEQSFLHFKATHPDWQPSDPSSSLFLDRLMGAGARNRPAGGISGSIYGGGGGGGGGGGRGLGIDGSVMAEMEEERLRAKSQSYERAWAKSSHLHRPDISNPLRHPHSAASEIIEEEEGGEGDKGDDSIDGWSKRMKTDGESDDEQEEHGRLWKDDGVQIDIKQ", "text": "FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATG9 family."}
{"protein": "MGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQCLEDLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLATEAGVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLISKMEPLEIPVETITSEVIEKCTTPLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGFGRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASRLNIERMKQIYQQLSRYRGLGLLASVPSNPNGNGGFMGYSAENIPGCSSSGSCSQGSGILHYAHGDSQQTHLLKQGRSSMGTGLSGGKRPSQEEDTQSIGPKVQRQSTN", "text": "FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post- translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-BMAL1 independently of PER proteins and is found at CLOCK-BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-BMAL1 induced transcription of ATF4, MTA1, KLF10 and NAMPT (By similarity). May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon-mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Inhibits hepatic gluconeogenesis by decreasing nuclear FOXO1 levels that down-regulates gluconeogenic gene expression (By similarity). Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4 (By similarity). Represses PPARD and its target genes in the skeletal muscle and limits exercise capacity (By similarity). Plays an essential role in the generation of circadian rhythms in the retina (By similarity). Represses the transcriptional activity of NR1I2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus Note=Translocated to the nucleus through interaction with other clock proteins such as PER2 or BMAL1. SIMILARITY: Belongs to the DNA photolyase class-1 family."}
{"protein": "MDPLGATANLVDINSLPKWSTTPVPNYEPGSNESQSSSFLSPFPVDEEINAKVVLWNGDITKLAADAIVNTTNESLSDRGALSERVHRAAGPELMQECRQQLLGCRTGEAKISEGYNLPARYVIHTVGPRYNTKYKTAAESALFSCYRNTMRLVRENKISTIGVCVVNTTKRGYPPEDGAHIALRTVRRFLEKYGSAVDTVAFVVEGAEAVVYAKVMPIYFPRDKLEEAHALTLMPDDIGNEEGEPIIPERQIRIVPKPPSLQHGEDVEEAEEAEGHLDMTELHVGKHAFAVMAGDHDQMTKQRAHRSDDGMKVVEQQRVYQRWLRRARTENFADFSRQKILYQSGVDFLGRPVVVFVARHFTAQNTDLGKAVAYFISVLDRIVNRDYVVVYFHTHSTEENQPPMSFLKELYHIVDNKYRRNLKAFYIVHPTVWARIVTWFFTTFTASSVKEKVHFLSGVQYLYDWINPDQLDIPAYVLEYDMKENGTNYHTPASTYRTGGL", "text": "SIMILARITY: Belongs to the GDAP2 family."}
{"protein": "MRLISKRRIRFIVFILFGVLTVFVVSRLVVHFQYNQEIKFYKKYFQQRKDGLHEIYNPLEIKQIPKETIDDLYTARLDKELKNGEVIEWSKFAYVNYVTNADYLCNTLIIFNDLKQEFETKAKLVLLISKDLLDPNTSSNVAYISSLLNKIQAIDEDQVVIKLIDNIVKPKDTTPWNESLTKLLVFNQTEFDRVIYLDNDAILRSSLDELFFLPNYIKFAAPLTYWFLSNSDLEKSYHETRHREKQPINLQSYTKVLTKRIGKGQMIYNHLPSLPHSLYLNSNNIAQDIISSTSSLSPLFDFQSSKKVGKLKFASNLMVINPSKEAFDEIVNVMLPKILNKKEKYDMDLINEEMYNLKKIIYKQFIFFRKVRKLFKPEVLVLPFARYGLLTGSLRNPRHYSIIYNDVLGYKTLDNDGNDIPVGLNDSVAYSKYIHFSDYPLAKPWNYPSMKEFECIVKEEDAEDSKLEHQACDLWNSVYASYIQSREICLV", "text": "FUNCTION: N-acetylglucosaminyltransferase involved in the Golgi- specific modification of N-linked glycans. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein Vacuole membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the GNT1 family."}
{"protein": "MRRSVCYVTPSVARAGQISTWRFEYSSANFLPEGTLLKFDLGIDGRPIDWEIPSTDLSQPCNTIYLETPSESIVTAKAVYAPGSYIPTFEFILPCEIEAGDTFSIILGSSPNFPQEDASGNGAQLFTQRRKPFSLYVDPTGKGNFEDPDIFTIDIRGNVLKNIRIFAPSYVVKNKRFDITVRFEDEFGNLTNFSPEETQIELSYEHLRENLSWQLFIPETGFVILPNLYFNEPGIYRIQLRNQATKEIFTSAPIKCFTETSPHLLWGLLHGESERVDSEGNIESCLRYFRDDCALNFFATSSFEIQDGLTPETIKSINQTVSDFNEEDRFIALSGAQYVSEEPGEGIREVLLIKEPKSPGKHKECKLFPLSKLYKQSTSHELISIPSFTASKKFGCDFQNFHAEFERVVEIYNAWGCSERTEAEGNPFPIKGSIDSENPEGTILSALKRNLRFGFVAGGLDDRNLYSNFFDSDQQQYSPGLTAVICNKYSRDSLLEALYQRQCYATTGQRIIVSFQITSAPMGSELSTAIKPGLMINRHISGYVAGTAKISTIEIIRNGDTLHTFYPDGNNFEYEYDDLTPFAQATLADPKNGAPFAFYYLRVTQENGAMAWSSPIWIDLN", "text": "SIMILARITY: Belongs to the chlamydial CPn_0512/CT_425/TC_0708 family."}
{"protein": "MESKALLLLALSVCLQSLTVSRGGLVAADRITGGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG", "text": "FUNCTION: Key enzyme in triglyceride metabolism (PubMed:9188470, PubMed:16179346, PubMed:10727238). Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:9188470, PubMed:16179346, PubMed:10727238). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:9188470). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side Secreted Secreted, extracellular space, extracellular matrix Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:9188470). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (PubMed:9555944). SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MPCVQAQYGSSPQGASPASQSYSYHSSGEYSSDFLTPEFVKFSMDLTNTEITATTSLPSFSTFMDNYSTGYDVKPPCLYQMPLSGQQSSIKVEDIQMHNYQQHSHLPPQSEEMMPHSGSVYYKPSSPPTPSTPGFQVQHSPMWDDPGSLHNFHQNYVATTHMIEQRKTPVSRLSLFSFKQSRPGTPVSSCQMRFDGPLHVPMNPEPAGSHHVVDGQTFAVPNPIRKPASMGFPGLQIGHASQLLDTQVPSPPSRGSPSNEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKSPQDPSPPSPPVSLISALVRAHVDSNPAMTSLDYSRFQANPDYQMSGDDTQHIQQFYDLLTGSMEIIRGWAEKIPGFADLPKADQDLLFESAFLELFVLRLAYRSNPVEGKLIFCNGVVLHRLQCVRGFGEWIDSIVEFSSNLQNMNIDISAFSCIAALAMVTERHGLKEPKRVEELQNKIVNCLKDHVTFNNGGLNRPNYLSKLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPAIIDKLFLDTLPF", "text": "FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons (By similarity). May confer liver- specific regulation of delayed-early genes induced later in the G1 phase of regeneration along with HMR. SUBCELLULAR LOCATION: Cytoplasm Nucleus. Note=Mostly nuclear; oxidative stress promotes cytoplasmic localization. SIMILARITY: Belongs to the nuclear hormone receptor family. NR4 subfamily."}
{"protein": "MLSRIVTCFLFLLSSLPLFAEEEAAQSKNTFVQPAVMLAIAILFFYFILWRPEQKRRKAMEKRKNDLAKGDKVTAMGIIGTVDDIREHTVILNIASGKVEVLKGAISEILKPNDNKS", "text": "FUNCTION: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the YajC family."}
{"protein": "MDKNKIEYWLNSSWLSRENQNYIETIYKSFLTNAQSIDDMWHKAFLEFSEEQKNTYERNNTKNNKYLLIKKIDHMIHAFRSEGYQQSLIDPLKLKKRTKIHDLDLSFYNFTEEETRQTVEINFKNCTNFRTNIISLYKILYKKYCGSIGFEYMYVNNLLEKQWITNHIESFFNENVFTIEEKINFLKELTYAETLEKYIGKKFPGAKRFSLEGAETLIPVLHEVIRFSKKNNISKIVLGMAHRGRLNVLINVLNKSPKVLFDEFSNLNLFQKISGDVKYHMGGTAEIQYEKKIIFHMACNPSHLEIINPVVSGISRSYIDNMKNIDNEVLPISIHGDASVIGQGVVQETLNMSQTEGYKVGGTVHIIINNQIGFTTSNPKHLRSSEYCTDVAKIIQAPVFHVNADDLEASIFAIQLALHFRKIFKKDVFIDLVCYRRNGHNEVDEPSVTQPIMYQKIKNHPTSRTIYSDVLISKKIITSEKNQEIMNQYLSKLQKGHYIFSKSKNIHFKNEFFLEEKKIKKIKKDVNFSDLKNLACLINQIPDSVKMHQRVKKIYEERLEMAQRLKLFDWGAAETLAYATILNEGISCRISGEDVSRGTFFHRHAFIHNQINGSIYIPLNNISKKQGKFQIWDSVLSEEAVLAFEYGYSLSSPNTLTIWEAQFGDFINGAQIVIDQFISSGEQKWNKKSNLVVLLPHGYEGQGPEHSSSRIERFLQLCAEENMQICIPTTSSQIFHIFRKQIFDKILKPLIIFTPKSLLRNPMASSSFDDLVYGKFQKILDEVDNVNKKEIRLIFCSGKIYYDLLRNRREKKINSIILIRIEQLYPFPEGEILKILKNYFYIKDFIWCQEEPYNQGAWFYIKDCLSNILPLDASLKYIGRSSSASPAVGYISIHKKQQEKIIYNALNIN", "text": "FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family."}
{"protein": "MRSWLLLLVGLSSYFALSTSVNRAKNSGSDFDLESRASTTNVNSILSKRKLRAPGGDTNTLKDSGKARREKKVWKLFCRVFLQLDDEKKCMFETNQVSSHQPEPRPALSFMPGPKPAHSLVPESKPVRSLMTGNAPVRSIATKLKLVLPRITETVKNPSKSQVVMLWLHKVAEFSRSEHGVNTMSYRTLYEWLSPSFSDAKLAKFFVGLREDEALRETAEKMLAYMLIKSTSTEAVGRAWLKSGEHPSRLFESMNFKEADFKDTVFLGWLKYASLYEKHYFSQSELTDYRRQLFFYRMYDYIKPMYSYEKTQGFLEYKFEGLTSIPGMQDFGQNLADIARRERKISFYLDSEFTPEALFNYLKVSDENLLTNVFQWLRYCRRYTMAYKYVPFDELEFLEEKLGEISLWIYQVYGKL", "text": "FUNCTION: Effector that partially suppresses the tobacco programmed cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVEFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAMKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEKRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRKSETSGRYASYRICM", "text": "FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerase complexes are composed of mobile elements that move relative to each other. In Pol II, RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family."}
{"protein": "MMAAASDSCLSLWEGSASSPNRQLTPEAVNCLTEALTEDVAVLRLIRSDPRVKIFMAVSVLTPRLARFAPPPPKLTHTAKCAVIMIYLTRPKALALQPKQFHMLVTFNKASVYSLVVRVKTKPFPVGTQRFRAVFQDPEFIGLPSDIPDPAAENIPTEINDRLDVSNFATPAQPPKDKYDCCVLAPGVWWSNANKAIYFLQMDVALLALCPAGWKARGLGIILGRLLNHQEGCATCRFTEHSDPLNATADSVATPESCLCWAPCLWRKAHQRELTVEGDRYLFRVLFMDAVERVRLTGLRRSPKITANLADLVVGIGPHGQQIPVNNAGWKLVALDADISRLIVCGCYALRYICPPTNSKHQPSSPDEYA", "text": "FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparing capsid uncoating. SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 2 family."}
{"protein": "MAVLLLLLRALRRGPGPGPRPLWGPGPAWSPGFPARPGRGRPYMASRPPGDLAEAGGRALQSLQLRLLTPTFEGINGLLLKQHLVQNPVRLWQLLGGTFYFNTSRLKQKNKEKDKSKGKAPEEDEEERRRRERDDQMYRERLRTLLVIAVVMSLLNALSTSGGSISWNDFVHEMLAKGEVQRVQVVPESDVVEVYLHPGAVVFGRPRLALMYRMQVANIDKFEEKLRAAEDELNIEAKDRIPVSYKRTGFFGNALYSVGMTAVGLAILWYVFRLAGMTGREGGFSAFNQLKMARFTIVDGKMGKGVSFKDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLKSLKLTQSSTFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNFEYAVERVLAGTAKKSKILSKEEQKVVAFHESGHALVGWMLEHTEAVMKVSITPRTNAALGFAQMLPRDQHLFTKEQLFERMCMALGGRASEALSFNEVTSGAQDDLRKVTRIAYSMVKQFGMAPGIGPISFPEAQEGLMGIGRRPFSQGLQQMMDHEARLLVAKAYRHTEKVLQDNLDKLQALANALLEKEVINYEDIEALIGPPPHGPKKMIAPQRWIDAQREKQDLGEEETEETQQPPLGGEEPTWPK", "text": "FUNCTION: ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function (PubMed:26387735). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the AAA ATPase family. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family."}
{"protein": "MKTLILHICIFALVAFASASRDSAKKIGSQYDNYETCLTELSVTEDELFSIGEVTSGQHKTNHEDTELHKNGCVMQCMLEKDGLMTGADYDEEKMREDYIKETGAQPGDQRVEALNACMQETKDLEDKCDKSLILVACVLAAEAVLADSSEGA", "text": "FUNCTION: Colony queen number, a major feature of social organization, is associated with worker genotype for Gp-9. Colonies are headed by either a single reproductive queen (monogyne form) or multiple queens (polygyne form). Differences in worker Gp-9 genotypes between social forms may cause differences in workers' abilities to recognize queens and regulate their numbers (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the PBP/GOBP family."}
{"protein": "MSLGIRYLALLPLFVITACQQPVNYNPPATQVAQVQPAIVNNSWIEISRSALDFNVKKVQSLLGKQSSLCAVLKGDAYGHDLSLVAPIMIENNVKCIGVTNNQELKEVRDLGFKGRLMRVRNATEQEMAQATNYNVEELIGDLDMAKRLDAIAKQQNKVIPIHLALNSGGMSRNGLEVDNKSGLEKAKQISQLANLKVVGIMSHYPEEDANKVREDLARFKQQSQQVLEVMGLERNNVTLHMANTFATITVPESWLDMVRVGGIFYGDTIASTDYKRVMTFKSNIASINYYPKGNTVGYDRTYTLKRDSVLANIPVGYADGYRRVFSNAGHALIAGQRVPVLGKTSMNTVIVDITSLNNIKPGDEVVFFGKQGNSEITAEEIEDISGALFTEMSILWGATNQRVLVD", "text": "FUNCTION: Amino-acid racemase that catalyzes the interconversion of L- lysine and D-lysine. To a lesser extent, is also able to interconvert arginine enantiomers (Ref.1, PubMed:23118975). Cannot use methionine, asparagine, alanine, leucine, glutamine, phenylalanine and histidine as substrates (Ref.1). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Periplasmic side Periplasm. SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily."}
{"protein": "MNPLRKKRLVIILAILVGVGAAVGLALSALQQNINLFYTPTQIANGEAPKDTRIRAGGMVEKGSLVRSGDSLDAKFNVTDFNKTVTITYRGILPDLFREGQGIVALGKLNADDVVVADEVLAKHDEKYMPPEVAKALKDSGQSAPAPGKEG", "text": "FUNCTION: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the CcmE/CycJ family."}
{"protein": "MPVLPWLAAAATTPVRRSPPLPATPRALLRLPASSFPPWSNCAKSGLPPRGPFATAADTPLGGSLPEPEEERDTLLDGALRAARFRDEESRRPDPLFIDPYAAVLLSLDVASEDKDLLALHLMPSAEHYRLVTRYIDDKLQHFISNSDDLRQIVLLTDGMDTRPYRLSWPRLSVVYDVSPRRVFITASQQLRGAGAKISRNCVVLHTSSESPDLQAGLNKNGFNGNRPSLWVLQGLPLFTFKSLEDLLLVIGNLAMKGSIFIGEVPRFTQWGAATDMASEQDRLENLFFTQGFRVSFVHYEEVAKDVGLGLDSPPEIHGRAIFIAEQLRFSDAQMESFRMHFERIEDDADEDGFEEL", "text": "FUNCTION: Involved in melatonin biosynthesis (PubMed:29901843). Can function as acetylserotonin O-methyltransferase (PubMed:29901843). Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine) (PubMed:29901843). Involved in the regulation of jasmonate- and brassinosteroid-mediated plant growth and defense responses (PubMed:26864209). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family."}
{"protein": "MMFHFLGTAGLGIALSWLVFTHFLQSSCRCQPWEPCWPSDEQWELLNRSMEFTLVRLQPIASVCYNHSLDHTLCEDVMRMSRDSGWRASQPGALQDWVWESGQSPGDACPLGSQMNGHTQCHQGRIPLYSAMVNSTKHVQEAVMFAKRHDLRLIIRNTGHDLAGRSSSPNALQIHTHRLQDIKFHDNVQLHGFEKSFGPAVSVGAGVMMGDLYARSAQNGYIVVGGDCPTVGVVGGFLQGGGISDFLSLHHGLAVDNVLEFEVVTASVSLPEPDAIQYCGFLTLRQGDIVLANAIRNPDLFWALRGGGGGTFGIVTRATMRVFPDVPAIAAELGVQTSQSHGEYSRSLAAFFTVLQSLNRENVGGQLIITVISEHSIEAKLKMFFLNQTNTADVDQRMQPFVEDMRRIETHVTYESTSLPKLSMNYRQVPDIHTDNDYGVLGSTVAISNDLFNASKGPAYVADGLAQLPTRPGDLLFTSNLGGQVMRNGDLMETSMHPAWRNATQLINFVRPVEPTIEGKAGALQNLTNIHMPLLYAIDPRFRLSYRNVGDPNEKDFQQVYWGQSYARLLQLKRRWDREGLLISKLGVGSEEWDSEGMCRTGRRSLENLAIDTLSSLAHLIHVTYRCIW", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids (PubMed:28620689). The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4- dimethylallyl-L-tryptophan (PubMed:28620689). The second step is catalyzed by the methyltransferase ifgB that methylates 4- dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan (PubMed:28620689). The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:28902217). The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7- didehydroergoline (PubMed:28620689, PubMed:28902217). The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8- dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689). Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A (PubMed:28620689). Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689, PubMed:28902217). The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions (PubMed:28902217). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MPNARVFKILAAAKLNNIALEIPAYQHGVTNKSAEFLLKFPAGKVPAFEGPDGFCLVESDAIAQYVAQSGPQASQLLGQDAMSSAKIRQWISFFAEEIYPTVLDLVMWRVGLGAFDETTETKALTQLVYGLSVLEKHLGTGALLVGDKLTLADLTGASTLLWAFMHIVDEPMRQQYPNVVAWYLKVVQNEEVEEVFGKPNFIEKRRLGAK", "text": "FUNCTION: Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (PubMed:23932525). The other FUS cluster members are not essential for fusarin C biosynthesis (PubMed:23932525). SIMILARITY: Belongs to the GST superfamily."}
{"protein": "MSDCLLPSSDMDAFRKILKKANSVVILTGAGVSAESGVPTFRGAGGLWRTYSAQNLATPSAFRSNPSLVWEFYHHRRENMASKSPNNAHNAIAEFEHRMTKEGRHVSVITQNIDELHQRAGSVNVLELHGSLFKTRCLKCKKIEPNHDSPICEALRGKGSPSPNEVGELVPESLLPRCKVSSCGGLLRPHVVWFHENLDSAVLKKADEELNSCDLCLVVGTSSVVYPAAMFAPQVAERGVPVAEFNMETTAATHHFGFHFSGPCGELLPKALAP", "text": "FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the sirtuin family. Class III subfamily."}
{"protein": "MVQRLTYRRRLSYNTASNKTRLSRTPGNRIVYLYTKKVGKAPKSACGVCPGRLRGVRAVRPKVLMRLSKTQKHVSRAYGGSMCAKCVRDRIKRAFLIEEQKIVVKVLKAQAQSQKAK", "text": "FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eL34 family."}
{"protein": "MMTIRPTKSTDFEVFTPAHHDILEAKAAGIEPSFPDASECVTLSLYGFPLAIGGNCGDQCWFVTSDQVWRLSGKAKRKFRKLIMEYRDKMLEKYDTLWNYVWVGNTSHIRFLKTIGAVFHEEYTRDGQFQLFTITKGG", "text": "FUNCTION: May act as an organizer for the correct association of several proteins in the surrounding of the head-tail connector protein gp8."}
{"protein": "MNLWLLVCLVASLMGAWSTVHTQGVSEDCCLAYHHRARPRLLMRAQGYQRQEVSGSCNLPAVIFFFPKNKMLCVNPRVNWLPNVFKFLDNRNNTHSKQHLGSRRNLQDSHLGGQRSNTGMSRLAHSKSKSSRSTRSNKKKTSFLNMANPGP", "text": "FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MNKRAMLGAIGLAFGLMAWPFGASAKGKSMVWNEQWKTPSFVSGSLLGRCSQELVYRYLDQEKNTFQLGGQARERLSLIGNKLDELGHTVMRFEQAIAASLCMGAVLVAHVNDGELSSLSGTLIPNLDKRTLKTEAAISIQQAEMIAKQDVADRVTKERPAAEEGKPTRLVIYPDEETPRLAYEVNVRFLTPVPGNWIYMIDAADGKVLNKWNQMDEAKPGGAQPVAGTSTVGVGRGVLGDQKYINTTYSSYYGYYYLQDNTRGSGIFTYDGRNRTVLPGSLWADGDNQFFASYDAAAVDAHYYAGVVYDYYKNVHGRLSYDGSNAAIRSTVHYGRGYNNAFWNGSQMVYGDGDGQTFLPFSGGIDVVGHELTHAVTDYTAGLVYQNESGAINEAMSDIFGTLVEFYANRNPDWEIGEDIYTPGVAGDALRSMSDPAKYGDPDHYSKRYTGTQDNGGVHTNSGIINKAAYLLSQGGVHYGVSVTGIGRDKMGKIFYRALVYYLTPTSNFSQLRAACVQAAADLYGSTSQEVNSVKQAFNAVGVY", "text": "FUNCTION: Extracellular zinc metalloprotease. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family."}
{"protein": "MSTDDQKVGLIPVTLMVAGNIMGSGVFLLPANLASTGGIAIWGWLVTIIGALALSMVYAKISSLDDSPGGSYAYARRAFGPFLGYQTNVLYWLACWIGNIAMVVIGVGYLSYFFPILKEPMVLTITCVVFLWIFVGLNIIGPKMITRVQAVATSLALIPIVGIALFGWFWFKGETYMAAWNVSGLGTFGAIQSTLNVTLWSFIGVETASVAAGVVKNPKRNVPIATVGGVLIAAVCYVLSSSAIMGMIPNAELRLSASPFGDAARLALGDTAGAVVSLCAAAGCLGSLGGWTLVAGQTAKAAADDGLFPPIFGKVNKAGTPVAGLLILGVLMTIFQISSISPNAAKEFGLVSSVSVIFTLVPYLYTCSALLLVGHGHLGNQVKTYVGITLIAFVYCIWAVVGSGAEEVMWSFVTLMVITALYTFNYNRTHKNPFPLDAPVKNGQ", "text": "FUNCTION: Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach. Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons. Probably undergoes several conformational states in order to translocate the substrate across the membrane; keeps the substrate accessible to only 1 side of the membrane at a time by opening and closing 3 membrane-internal gates. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family."}
{"protein": "MMRPWTILIASSWLSLAAASASASACAAKPSVAAEIASIDHDNCEHGPNSRGCWGDYSINTNYYEQAPDTGVTREYWFVVENITMAPDGYEQHVLAINRSIPGPLIEANWGDEVVIHVTNNMERNGTAIHWHGIRQLNNNAHDGVPGVTQCPIPPGGSYTYRWKAEQYGTSWYHSHFSLQYSVGLQGPMIIHGPATANYDEDLGTVMLQDWSHVSPFAMWWYARVPSGPPSLSNSLINGKNIFRCTDPLDKNCLGTGERSEWHFEKGKRYRMRLVNTGLYSNFRFAIDGHNLTVIANDFVPIEPYTTDNVIISMGQRYDVIVEANAPEDNYWLRAIWQTSCCPNDYANDTLGIIRYDPQSTALPNTTHPALHYPDNCDDEPAEKLVPHVKVDAGPPARTDVFNLYRHTYDMPRGFMWTLNDTYLWIDWSKPTNLLVAENDTTIFPPNYLLYHTPDGPNQWVYIVFNDISERNRSHPMHLHGHDFFLLGTGEGNFTKDSPLQLKNPPRRDTASWPKRGYMVFAYKTDNPGAWLIHCHIAWHSSQGLGMQMLERPGEMTYTEDEDQALHQTCQSWNKFYESPEQYIQEDSGI", "text": "FUNCTION: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects (PubMed:26305932). The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensing acetyl- CoA with 3 malonyl-CoA units (PubMed:26305932). Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase OpS4 (PubMed:26305932). The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy- oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932). The latter is further dimerized to oosporein by the catalase OpS5 (PubMed:26305932). OpS6 probably functions en route for protecting cells against oxidative stress by scavenging any leaked free radical form of benzenetetrol by activating the thiol group of glutathione (PubMed:26305932). SIMILARITY: Belongs to the multicopper oxidase family."}
{"protein": "MPQQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAATLGILPAGVRQTAGEILADGKPVSPYALRGIKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAAIEAVGLENAARVLKLYPFEMSGGMLQRMMIAMAVLCESPFIIADEPTTDLDVVAQARILDLLESIMQKQAPGMLLVTHDMGVVARLADDVAVMSQGKIVEQGDVETLFNAPKHTVTRSLVSAHLALYGMELAS", "text": "FUNCTION: Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Nickel importer (TC 3.A.1.5.3) family."}
{"protein": "MLGIMDHHQDTVRKCKSEALPPERRKRTVEDFNKFCSFVLTYAGYIPPQKEESSWSPSSSPCTHDLSELSGEGSVKDSWTDSHSDLNNIHNLVYKAETDSSSSREFSHLPSDNSLDKMTLKDSLNHVHSKAERKKVKKLDRLSLGGPRKSISEARAHKQSKAALKKIKTSIKAERHFTSSSPLNEGFEKEELTEQAIHMHEAGLKLESNQETDLSSCETDTLVTDEDIMVESGDDSWDLITCYCGKPFAGRPMIECEECSIWVHLSCAKIKKSNVPDIFYCYRCLDSRGSTVKRDH", "text": "FUNCTION: Acts as a negative regulator of autophagy. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the PHF23 family."}
{"protein": "MQVDELLKPFPIKEFHPFPRALLGPGAHEMIGPEALKLGFKKTLVMTSGLRGSDIVHKITESMKYHGLEVVLYDKVESNPKDYNVMDAVKLYQENKCDSFVSIGGGSSHDACKGARISVAHDGRNVNDFEGFNKSENPRNPPHIAVSTTAGTGSETSWAYVITDTTTDPDNPHKYVAFDDASVATLAIDDPVLYYSCPIDYTAQCGFDVLAHASEPYVSRLNFEPSLGNALRAIKLTAENLRQATWNPSELSGREGMMYAQYIAAQAFNSGGLGIIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFADMAEAMGVDTHGMTDVQAADALAAAIRLLRDVGIPEKFTDVTQDSYSKNRLGQGPTKFYEQASVIKGDDEDVDRITNHVLGDACTPGNAKECTFETVRPVVDHCMNGDLDDLLS", "text": "FUNCTION: Catalyzes the oxidation of methanol to yield formaldehyde. While the in vivo electron acceptor is not known, N,N-dimethyl-4- nitrosoaniline (NDMA) can serve this function in vitro and is reduced to 4-(hydroxylamino)-N,N-dimethylaniline. It can also use various other primary alcohols, polyols and formaldehyde. In addition, MNO is able to produce methylformate from methanol plus formaldehyde, and possesses a formaldehyde dismutase and a NADH-dependent formaldehyde reductase activity. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family."}
{"protein": "MGSDWDEIKRLAADFQKAQLTSTLQKLSERNCVEIVTLLLEKQMLEVVFTNDGKEYITPDHLEREIQDELYVNGGRANLVEVSKTLNVDLSRIELLAERISAENQSVHLVLGQLIDEDYISHIAQEINEKLVQRGEVSISELASQFDLPSDFLQHDVVEKHLGKIIKGRQDASNPRVFFTQAYIQRCKAKIRGALAAITRPINVAVILQKIGVQEKIFYSLLDEIAPAGQVTSKQANSQYVPHIYAKTQADWVNSFYKQNSFLEYDAIQKLGISDAKSYIRKQFPNEEFLYLKRVALGARLVELTVVTALNECSATKQYLDLTTILPSNLSEEDIEEVFSTIMAQKHSNPSNFVYLDGIVFSQPYLAQLVQPCQALAESQAKAAIDGGVYQQYIVEKTLAQKGNVSTQELEDEGKVDKRDERRKKASSGKAGGGAQGRETKTKSTKKHQRGKAAAQFDSDDEDDAQQGSRGGGGASKKAVKPLELVKTADIVKLITASLEEEGLEHLSKSIASLYTNQFNQTALARAQELFEATPQTNRRQTHAAIQDRINTLLIDIRLYEKGLKLFPQDTQTQLVKYLLKSLGNEICNELSLYVASECNLTVKNTNLNVDQRNKLAQECEAQYRAALLEQNKALNKSIDDFELATETVLKTCSMIIKKVDKKKDRLLIADHKKKLQKQLLECNEPALLLHLAALILFTTITGSILHASGKFVSAILQHIRGSLNEDQNALLLRYHDLVLQVLQAIPDSNESKLANEHLQTMQNQVVELAQNFSRASISKAD", "text": "FUNCTION: E3 UFM1-protein ligase that mediates ufmylation of target proteins. SIMILARITY: Belongs to the UFL1 family."}
{"protein": "MPPPGKVPRKENLGLQCEWGSCSFVCSAMEEFCEHVTQHLQQHLQGSGEEEEEEEDLLEEEFSCLWRECGFCSPDNSADLIRHVYFHCYHTKLKQWGLQALQSQADLSPCILDFQSRNLIPDIPDHFLCLWEHCENSFDNPEWFYRHVEAHSQCCEYQVVGKDNNVVLCGWKGCTCTFKDRFKLREHLRSHTQEKVVACPTCGGMFANNTKFLDHIRRQSSLDQQHFQCSHCSKRFATERLLRDHMRNHVNHYKCPLCDMTCPLPSSLRNHMRFRHSEARPFKCDCCDYSCKNLIDLRKHLDTHSKEPAYSCDFENCTFSARSLYSIKSHYRKVHEGDSEPRYRCHVCDKCFTRGNNLTVHLRKKHQFKWPSGHPRFRYKEHEDGYMRLQLVRYESVELTQQLLRQPQEGSGLGASLNESSLQDIILETVPGEPGPQEEAEEEGGGGEGIALPASQGTSSPIIHVVNQTNAQGEREVVYYVLFEAPGEPPPASEPPSGGVMGELQGAAEEPEVQMV", "text": "FUNCTION: Transcriptional repressor that binds to the consensus sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional activator that promotes histone H4 gene transcription at the G1/S phase transition in conjunction with NPAT. Also activates transcription of the ATM and PRKDC genes. Autoregulates its expression by associating with its own promoter (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Associated with discrete nuclear foci."}
{"protein": "MQDNWPTRLAITCLLVAIERLGMYIPVGLISNPQANWLNGGGWFVLGIIPTINASIVMQILISIVPALTRLQKEEGEMGQKQIQKYTRYLTFFLAGIQAFTLSQQWCTWLLIVSGAMLVMWLAEQMTHKGIGNGTSIFVCSNIAANFLHHPIEAPWSLAMVVLIFTMLGMIALQEAVRAIPILSAKQLIQSIAQVYLLPMRLNQGGVMPIIFASSTLALLHTWSIWWLYVACIIFFSHFYNLVIANPKELSENLNKMAVVIPSIRPGAETQQYLNRTLNRMSWIGGIALSLIALLPWLFSSLKIFSGFGATSLLIVIGVSIDTMRQIRTYFIANAYEKMI", "text": "FUNCTION: The central subunit of the protein translocation channel SecYE. Consists of two halves. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family."}
{"protein": "MVYGVSKMANKNRKNLKPVKSDRKDRISKNHSKKKVNKNSLKKVATTDITVNANELNWKSVDIPDTLDDFGGFYGLEEIDGVDVKVVDGKVQFITKDNKNVKKEPEQVEEKDNIVFQEDDEDVNMDELIEFKNFDDIKEGELSAASDDEESEFHVSTEEEGEEGEEAEDQEEERSEKENVKGEAGTVVTEDQTNDDLLQSNVFSSNVDIDDQEPPVLPEWSENMDLSFTVLKGLSGLGFTRPTEIQLKSIPLALKGHNIMGKASTGSGKTLAYGIPIIEQLIKDTSNDRSIGLIFTPTRELAHQVTDHLQKVWTKMNKLNKYTILSLTGGLSIQKQERILKYDGSGRIIVATPGRFLELLERNPDLIPRFAKIDTLVLDEADRLLQDGHFDEFEKILKLLGKARKIKTSIDGKPTGSGWQTMIFSATFSLDLFTKLDKTSWKILKTAGGENNEMEQVLNHLMKKIQFKSKPVIIDTNPEHKVTSQVKESLIECLPMERDLYVYYFIMMYPGTTLVFCNAIDSVKKLNAFLNNLKISSFQIHSSMAQKNRLRNLEKFKEQSEKNSKVGKPTILIASDVAARGLDISGIKHVLHYHLPRSADVYIHRSGRTARGDNEGVSVMICSPQESMGPLRKLRKVLSTKKSSNPRKTKWQNDVPMLPLEPDIVSQLRERSKIASELADDEIATKSLHKDDNWLKKAAEELDIELDSEEEEKDQFLARNKTKKLNKQLEKNENKALKYQLNELLKMPLRKDLRKSYLTGGLTNLADTLVKHKGHNSIIGHDKVDALQTLKGKKHK", "text": "FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily."}
{"protein": "MDPKFQRVALSDGHFIPVLGFGTYAPEEVPKSKAMEATKIAIDAGFRHIDSAYFYKNEKEVGLAIRSKIADGTVKREDIFYTSKLWCTFHRPELVRPSLEDSLKNLQLDYVDLYIIHFPTALKPGVEIIPTDEHGKAIFDTVDICATWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQGKLLEFCKSKGIVLVAYSALGSHREPEWVDQSAPVLLEDPLIGALAKKHQQTPALIALRYQLQRGIVVLAKSFTEKRIKENIQVFEFQLPSEDMKVIDSLNRNFRYVTADFAIGHPNYPFSDEY", "text": "FUNCTION: Can convert prostaglandin E2 to prostaglandin F2-alpha. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MYMELYLMFSNFFKSIRWCKVPAFMQAKVEMGLVNEVELKSLLEQETDSPQTNAASLMEQGSLRERRAKAPRNSVVQSFKIVILSNKLNLLLPFGPLAILVHYLTDNKGWFFLLSLVGITPLAERLGYATEQLSCYTGATVGGLLNATFGNVIELIISIIALKNGMIRVVQLTLLGSILSNILLVLGCAFFCGGLVFPGKDQVFDKRNAVVSSGMLLMAVMGLLFPTFLHYTHSEVHAGSSELALSRFISCIMLVAYAAYLFFQLKSQPSFYTEKTNQNEETSNDDEDPEISKWEAIIWLSIFTAWVSLLSGYLVDAIEGTSVSWKIPISFISVILLPIVGNAAEHAGAIMFAMKDKLDLSLGVAIGSSIQISMFAVPFCVVIGWMMGAQMDLNLQLFETATLLITVIVVAFFLQLEGTSNYFKRLMLILCYLIVAASFFVHEDPHQG", "text": "FUNCTION: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/proton exchanger (CAX) subfamily."}
{"protein": "MCLRVLDLRIPKVIITYCPKCRTHTEHSVTIYKHGKRRSLSEGERRYARKKKGYGSKRKPEQKRFAKVTKKTVLKLKCSKCGYIIHREGIRLKKAELVEVGGR", "text": "FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family."}
{"protein": "MMEIAYQPRIDSEIESLVERINPPRVCVDNDSDPECTLIKVDSANKYGILLDMVQVLADLDLVISKCYISSDGEWFMDVFHVTDQLGNKLTDRSLILYIQQAICSSRTGGITKEMQSNLKREVQQRHVSTEHTAFEITGINRPGLLSEISAVLSDIGCHVTAAVAWTHHERAAMVIYLEDGFNGGPIIDPIRKAQVKDHLDTVMEAHHIVGDVSHVVVRVVEAKGVPVGWAHTERRLHELMYGEGDYENCFDCDCFGDRCDALWRGRCERIHVTIEACNGYSMVNVKCRDRPKLLFDTVCALKELQFVVFHAVAGAKGSTAEQEYFIRKKNGGTLETEGQRERLRHCLVAAISRRASQGLKLEIRTENKMGLLSDVTRVVRENGLSITRAEMCTQGEIAVGSFYVTDVNGGETGPSEVEAVVRELGGAVVSAVKGVGMMPRRIGSTSDSVEQDKAKSSIGRMFWSKLERLSTSIRSL", "text": "FUNCTION: May bind amino acids. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MEGESTTAVLSGFVLGALAFQHLNTDSDTEGFLLGEVKGEAKNSITDSQMDDVEVIYTIDIQKYISCYQLFSFYNSSGEVNEQALKKILSNVKKDVVGWYKLRRHSDQIMTFRERLLHRNLQQHLSSQELVFLLLTPSIITESCSTHRLEHALYKPQKGLFHRIPLVVANLGMSEQLGYKTTSGSCTSAGFSRAVKTHSSEFFKEDGSLKEVQKINEMYTSLQDELKSICEKVEHSERAVEKLLNDVNRLKGEIKKRKQAQMQATREKNVQKDPQENILLCQALRTFFPDCELLHSCVISLKNRRISGSSCTTTHPLSGVDNLTLMVEYTDFPEASPARSALLVTKRKASDTDDGWQFKKSRLGGIQNRPSKTDTNSSNQEQASTVSSPETDEEIERMKGSGEYPQSPTF", "text": "FUNCTION: Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. SUBCELLULAR LOCATION: Nucleus Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). SIMILARITY: Belongs to the FAM175 family. Abraxas subfamily."}
{"protein": "SEGRSRLLGAPVPVRENDEGLQRALQFAMAEYNKASNDKYSSRVVRIISAKQQLVSGIKYIMEVEIGRTTCPKSSADLQSCEFHDEPEMAKYTTCNFVVYSIPWLNQIKLLKSSCQ", "text": "FUNCTION: This protein binds tightly to and inhibits papain and cathepsin B. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cystatin family."}
{"protein": "MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEELKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGKIFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGKFPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPTYVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYFLFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFMFFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVRPRSWTCRYVF", "text": "FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol (PubMed:16154994, PubMed:16647063, PubMed:9020103, PubMed:32433614, PubMed:32433613, PubMed:32944968). Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:16154994, PubMed:9020103). Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions (PubMed:11294643, PubMed:32433614). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily."}
{"protein": "MAPSGPTGAQPSPAEPLSRSIFRKFLLMLCSLLTSLYVFYCLAERCPPGSGPVAGVPGRGVPAGPRELAMWPAGAPRKRLLQLRQRRRRGRSGPGDSSDQEEQSPGLAAAPGGSGAGSSVAEAQPGTLALLLDEGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYHKGLAWYRDLMPRTLEGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPSFESLTFRNRSAGLIDTSWSAIQIGLYAKHLEPWLRHFPLGQMLFVSGERLVSDPAGELRRVQDFLGLKRIITDKHFYFNQTKGFPCLKKAEGSGKPHCLGKTKGRAHPTIAREVLRQLRDFYRPFNRKFYQMTGRDFGWDG", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. Unlike HS3ST1/3-OST-1, does not convert non- anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family."}
{"protein": "MNPSFFLTVLCLGVASAAPKLDPNLDAHWHQWKATHRRLYGMNEEEWRRAVWEKNKKIIDLHNQEYSEGKHGFRMAMNAFGDMTNEEFRQVMNGFQNQKHKKGKLFHEPLLVDVPKSVDWTKKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRAQGNQGCNGGLMDNAFQYIKDNGGLDSEESYPYLATDTNSCNYKPECSAANDTGFVDIPQREKALMKAVATVGPISVAIDAGHTSFQFYKSGIYYDPDCSSKDLDHGVLVVGYGFEGTDSNNNKFWIVKNSWGPEWGWNGYVKMAKDQNNHCGIATAASYPTV", "text": "FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (PubMed:12869695). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity). SUBCELLULAR LOCATION: Lysosome Apical cell membrane; Peripheral membrane protein; Extracellular side Cytoplasmic vesicle, secretory vesicle, chromaffin granule Secreted, extracellular space Secreted Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MNKKILLVIFIVTMLIVDEVNSFKFGSFIKRMWRSKLAKKLRAKGKELLRDYANRVLSPEEEAAAPAPVPAKRRR", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Long chain multifunctional peptide (group 2) family."}
{"protein": "MWQIVFLTFGCDLVLASAYNNFRKSVDSTGRRQYQVQNGPCSYTFLLPETDSCRSSSSPYMSNAVQRDAPLDYDDSVQRLQVLENILENNTQWLMKLENYIQDNMKKEMVEIQQNVVQNQTAVMIEIGTSLLNQTAAQTRKLTDVEAQVLNQTTRLELQLLQHSISTNKLEKQILDQTSEINKLQDKNSFLEKKVLDMEDKHSVQLQSMKEQKDQLQVLVSKQSSVIDELEKKLVTATVNNSVLQKQQHDLMETVNSLLTMMSSPDYKSSVAVPKEEKTTFRDCAEIFKSGLTTSGIYTLTFPNSTEEVKAYCDMDMGGGGWTVIQHREDGSVDFQRTWKEYKEGFGSPLGEYWLGNEFVSQLTSGHRYVLKIQLKDWEGSEAHSLYEHFYLSGEESNYRIHLTGLTGTAGKISSISQPGSDFSTKDSDNDKCICKCSQMLTGGWWFDACGPSNLNGQYYPQKQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF", "text": "FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Involved in the regulation of lymphangiogenesis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MGNKFTNISTNLRNSWLTAKSGLNNAGQSLAKAGQSLKTGAKKIILYIPKDYQYDTDKGNGLQDLVKAAEELGIEVQKEESNDIAKAQTSLGTIHNVLGLTERGIVLSAPQLDKLLQKTKVGQAIGSTENITKGFSNAKTVLSGIQSILGSVLAGMDLDEALQNNSNELTLAKAGLELTNSLIENIANSVKTLDAFGDQINQLGSKLQNVKGLSSLGEKLKGLSGFDKTSLGLDIVSGLLSGATAALVLADKNASTSRKVGAGFELANQVVGNITKAVSSYILAQRVAAGLSSTGPVAALIASTVSLAISPLSFAGIADKFNHAKSLESYAERFKKLGYDGDNLLAEYQRGTGTIDASVTAINTALAAIAGGVSAAAAGSVVASPIALLVSGITGVISTILQYSKQAMFEHVANKIHNKIVEWEKNNPGKNYFENGYDARYLANLQDNMKFLLNLNKELQAERVIAITQQQWDNNIGDLAGISRLGEKVLSGKAYVDAFEEGKHLKADKLVQLDSANGIIDVSNSGKAKTQHILFRTPLLTPGTEKRERVQTGKYEYITKLNINRVDSWKITDGEASSTFDLTNVVQRIGIELDNAGNVTKTKETKIIAKLGEGDDNVFVGSGTTEIDGGEGYDRVHYSRGNYGALTIDATKETEQGSYTVNRFVETGKALHEVTSTHTALVGSREEKIEYRHSNNRQHAGYYTKDTLTSIEEIIGTSHNDIFKGSQFNDAFNGGDGVDTIDGNGGNDRLFGGKGDDIIDGGDGDDFIDGGKGNDLLHGGRGDDIFVHRQGDGNDSITEAGGHDRLSFSDSNLKDLTFEKVNHHLVITNTKQEKVTIQNWFREEEFAKTVKNYVATRDEKIEEIIGQNGERITSKQVDELIAKGKDNKIDKNDLANVVNSYELLKNSRNVTNSLDKLISSVSSFTSSNDSRNVLATPTSMLDTSLSSLQFARAA", "text": "FUNCTION: Pasteurella leukotoxins are exotoxins that attack host leukocytes and especially polymorphonuclear cells, by causing cell rupture. The leukotoxin binds to the host LFA-1 integrin and induces a signaling cascade leading to many biological effects, including tyrosine phosphorylation of the CD18 tail, elevation of the intracellular Ca(2+) and lysis of the host cell (By similarity). This leukotoxin is a major contributor to the pathogenesis of lung injury in ovine pneumonic pasteurellosis. It has also weak hemolytic activity. FUNCTION: Pasteurella leukotoxins are exotoxins that attack host leukocytes and especially polymorphonuclear cells, by causing cell rupture. The leukotoxin binds to the host LFA-1 integrin and induces a signaling cascade leading to many biological effects, including tyrosine phosphorylation of the CD18 tail, elevation of the intracellular Ca(2+) and lysis of the host cell (By similarity). This leukotoxin is a major contributor to the pathogenesis of lung injury in bovine pneumonic pasteurellosis. It has also weak hemolytic activity. SUBCELLULAR LOCATION: Secreted Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family."}
{"protein": "MPRSYKEECSFLERLSDSAFLIKKGFVPNMKVEGKFYINEHLEKLMFDELRHWCGAQGIGGFLPGVKQIANVAALPGIVGYSVGLPDVHSGYGFAIGNMAAFDMSLPEAVVSPGGVGFDINCGVRLLRTNLEEKDVQPVKERLAQSLFDHIPVGVGSKGVIPMGAKDLEDALEMGVDWSLREGYAWAEDKEHCEEYGRMLQADSAKVSAKAKKRGLPQLGTLGAGNHYAEIQVVDEIYNEFAAKKMGIDHKGQVCVMIHSGSRGLGHQVATDALVAMEKAMKRDKIEVNDRQLACAHIKSPEGQDYLKGMAGAANYAWVNRSSMTFLTRQAFAKVFNSTPDDLDMHLIYDVSHNIAKVEEHFLDGRQRQLLVHRKGSTRAFPPHHPLIPVDYQLTGQPVLIGGTMGTCSYVLTGTEKGMTETFGTTCHGAGRALSRAKSRRNLDYQDVLENLAQKGISIRVASPKLVMEEAPESYKNVTDVVDTCHSAGISKKAIKLRPIAVIKG", "text": "FUNCTION: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs. SIMILARITY: Belongs to the RtcB family."}
{"protein": "LQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEMGREPTPEELAERMLMPEDKIRKVLKIAKEPISMETPIGDDEDSHLGDFIEDTTLELPLDSATSESLRSATHDVLAGLTAREXKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEVLRSFLDD", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily."}
{"protein": "MAHTSESVNPRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQVDYYEINEAFAVVALANQKLLGIAPEKVNVNGGAVSLGHPLGCSGARILITLLGILKKRNGKYGVGGVCNGGGGASALVLELL", "text": "FUNCTION: Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA (PubMed:22332816). Generates the bulk of the acetoacetyl-CoA precursor required for the cytosol-localized, mevalonate-derived isoprenoid biosynthesis (PubMed:22332816). The generated isoprenoids are required for normal growth and development (PubMed:22332816). Essential protein during embryogenesis (PubMed:15266054). SUBCELLULAR LOCATION: Cytoplasm Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MGDLENLLLEAAGRTNSAGRSRHPPSSRRREGSYSDGSSDSRDDSDEDRGYASRKPSGSQVPLKKRLEAEREDRAARVEGGYGDGPSDREGDSSEESDFGDDLYKNEEDRQKLAGMTEFQREMILSERADKKGDKNFTEKLRSKRESEKTPVSKKETQPLPASRGVRSSARSADRAAAKDDALNELRAKRMKQQDPAALRKLRDASKGGSGSRDFSSTKRKPLASSNLSSSSQSDSDSRSQSDDEGSNGGMLDSDDDRSDVPTFEDVKEVTIRRSKLAKWLMEPFFEELIVGCFVRVGIGRSKSGPIYRLCWVKNVDATDPDKTYKLENKTTHKYLNVVWGNETSAARWQMAMISDGHPLEEEYRQWIREVERTNGRMPTKQDISEKKEAIQRTNSFVYSAETVKQMLQEKKSASVRPMNVAAEKDRLRKELEIAQSKNDEAGVERIKSKIKQLDASRNKKGVDKKALKLAEMNKKNRAENFKNASEVKSITASLKAGEAGYDPFSRRWTRSSNYYNGKNKGKDGEENEAAVAAAVETNGADAGAGVEATEAALEAAAEAGKLIDTRAPIGQGAEHNQLHNFELSLSLTALQKYGGPQGVQKAFMARKQLTEATVGCRVAENDGKRHGLTLTVSDYKRRRGLL", "text": "FUNCTION: Component of the PAF1 complex (PAF1C) which is involved in histone modifications such as methylation on histone H3 'Lys-4' (H3K4me3) (PubMed:20363855). Involved in regulation of flowering time. Required for the expression of the flowering repressors and FLC and MADS-box genes of the MAF family (PubMed:15472079). Involved in the control of seed dormancy and germination (PubMed:21799800). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTKLEVCCYSVDCAQIAEKAGADRVELCCGQSEGGLTPSVGALMQARETVTIPVHPIVRPRGGDFCYSSNDFTIMKNDIARIRDLGFAGVVVGVLDTDGHIDMPRMREIMSVSGSLAVTFHRAFDMCQNPMIALKQLAELNVARILTSGQQQNAELGLALLKDLVAATKDQGPIIMAGAGVRLTNMQKFIDAGIRELHSSAGRTVPSTMRYRKAGVTMCADSDVDEFSHYCVDGEVVEAMKSLLVMGAPLAKHT", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutC family."}
{"protein": "MAMDGYLWMVILGFIIAFILAFSVGANDVANSFGTAVGSGVVTLRQACILASIFETTGSVLLGAKVGETIRKGIIDVNLYNETVETLMAGEVSAMVGSAVWQLIASFLRLPISGTHCIVGSTIGFSLVAIGPKGVQWMELVKIVASWFISPLLSGFMSGVLFILIRMFILTKEDPVPNGLQALPLFYAATIAINVFSIMYTGAPVLGLSLPIWAIALISFGVALLFAFFVWLFVCPWMKRKIAGRLEKESALSRASDESLRKVQEAESPGFKELPGAKPSDDSAVPLTSLAGEAVGASEGTSAGNHPRASYGRALSMTHGSAKSPISNGTFGFEGHMRNDGHVYHTVHKDSGLYKDLLHKIHVDRGSEEKPTQENNYRLLRRNNSYTCYTAAICGMPVHTTFRASDTSSAPEDSEKLVGDSVSYSKKRLRYDSYSSYCNAVAEAEIEAEEGGVEMRLASELADPDRPHEDPTEEEKEEKDSAEVHLLFHFLQVLTACFGSFAHGGNDVSNAIGPLVALWLIYQQGGVTQEAATPVWLLFYGGVGICTGLWVWGRRVIQTMGKDLTPITPSSGFTIELASAFTVVIASNIGLPVSTTHCKVGSVVAVGWIRSRKAVDWRLFRNIFVAWFVTVPVAGLFSAAIMALLMYICGLFSSSR", "text": "FUNCTION: Sodium-phosphate symporter which preferentially transports the monovalent form of phosphate with a stoichiometry of two sodium ions per phosphate ion (PubMed:11003594, PubMed:23968976, PubMed:26822507, PubMed:30721528). Plays a critical role in the determination of bone quality and strength by providing phosphate for bone mineralization (PubMed:30721528). Required to maintain normal cerebrospinal fluid phosphate levels (PubMed:26822507). Mediates phosphate-induced calcification of vascular smooth muscle cells (VCMCs) and can functionally compensate for loss of SLC20A1 in VCMCs (PubMed:23968976). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family."}
{"protein": "MNPRLAACQALAAVLAGRASLSGALPPQLDKVAPRDRGLTQELAFGAARWQPRLQALAARLLQKPFKAADTDIHALLLIGLYQLLYTRIPPHAAIGETVGCADKLKKGWAKGVLNAVLRRAQREGETLLAEVDRDPSARLGHPRWLLKALKQAWPEQLDALCAANNAHPPMTLRVNRRHGERDAYLAELAEAGIKARACDYSRDGIQLAAPRDVRELPGFAEGRVSVQDEAAQLAAEQLESAPGQRVLDACCAPGGKTCHLLETQPELAEVVAVDLEESRLVRVRENLQRLGLQASLVAADARATGEWWDGKPFQRILLDAPCSATGVIRRHPDIKLARKPEDIAALAHLQGELLDALWPTLEVGGVLLYATCSVMPAENSDSIAAFLARTPGARELDLPGPWGMKQPHGRQLLPQVEGHDGFYYAKLIKISAR", "text": "FUNCTION: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family."}
{"protein": "MTTRFKKNRKKRGHVSAGHGRIGKHRKHPGGRGNAGGMHHHRILFDKYHPGYFGKVGMRYFHKLRNKFFCPIVNLDKLWSLVPEDVKAKSTKDNVPLIDVTQHGFFKVLGKGHLPENKPFVVKAKLISKTAEKKIKEAGGAVVLTA", "text": "SIMILARITY: Belongs to the universal ribosomal protein uL15 family."}
{"protein": "MFGWHWLLEWQTPYEFHGHLIEKVLAEEKTPYQHVTLVEFTRFGKGLIIDGKVQSTLYDEHIYHELLVHPLLLSLTKPPKSVLILGGGEGATLREVLKYKSVEKAVMVDIDEKVIEFAKKYLYEWHQGAFEDKRTNLVITDGLKFIKETKEKYDAIILDLTDPIKNSTSYMLYTKEFYEKLREILNERGGIVTQATSPSFSLEVYVTIYNTIKEVFKEASASYTYMASFDGLWGFVYGGVRPDLLSEDEVDSKINERIDGQLRFYDGYSHKISFSLPKNIKSEFQKITKISTEKDPIYVPA", "text": "FUNCTION: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to various amine acceptors such as putrescine (1,4-diaminobutane), 1,3-diaminopropane, sym- norspermidine and spermidine. The biosynthesis of caldopentamine from norspermine has been also observed, but with a very low activity. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet. S-adenosylmethioninamine is the only amino donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the spermidine/spermine synthase family."}
{"protein": "MIGGLFIYNHKGEVLIYRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVDAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKSDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC", "text": "FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface (By similarity). AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules (By similarity). AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6- regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (By similarity). The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs (By similarity). The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at Thr-156 in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity). SUBCELLULAR LOCATION: Cell membrane Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. SIMILARITY: Belongs to the adaptor complexes medium subunit family."}
{"protein": "MASILPASNRSMRPDKNTYERKRSVYVKNPYLEGMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGDGEDIEDICAGTDRYCMFKTGPVLSVSHGMGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELANDLFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLRAAVVCVTLLDRLESDQINLSHDVLVEYQQRPQLLISNFIKKQLGLCDQMS", "text": "FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate (PubMed:14715930). The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable). SIMILARITY: Belongs to the PNP/UDP phosphorylase family."}
{"protein": "MIVIVGPSGAGKDTLMDYAAAQLSGRPGFHFTRRVITRSCDAGGENHDAVSMHEFNQLEDAGAFAVSWQAHGLKYGIPAAVYRHLEAGDVVIANGSRSALPHFGTAFSRLKVVNIVARPDVLARRLEQRGRESRDDILRRLERSSLAVAGDFDVTTVDNSGAIEDAGKTIMQVLQQSAGSSQP", "text": "FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family."}
{"protein": "MKLCAVIIASLLVCVAVASSSDNQKEFAQEKEMTREETQSLGEHEKDDEVTGSEERSCIEEWKTCENDCECCGMSTLCAASWVDGHQIKLCRNEGGKLKKVLHFIQKSVSKIKSCRK", "text": "FUNCTION: Putative ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 02 subfamily. HNTX-XV sub-subfamily."}
{"protein": "YCCHPACGPNFSC", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin inhibits fetal and adult muscle-type nAChR (IC(50)=52.1 nM towards alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND, and IC(50)=102.8 nM towards alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1- CHRND-CHRNE). Shows potent activity on the synthetic AChR alpha-1-beta- 1-delta/CHRNA1-CHRNB1-CHRND (IC(50)=16.9 nM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
{"protein": "MGITLIWCLALVLIKWITSKRRGAISYDSSDQTALYIRMLGDVRVRSRAGFETERRGSHPYIDFRIFHSQSDIEASVSARNIRRLLSFQRYLRSSRVFRGATVCSSLDILDEDYNGQAKCMLEKVGNWNFDIFLFDRLTNGNSLVSLTFHLFSLHGLIEYFHLDMVKLRRFLVMIQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLASSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNSSVLENHHWRSAVGLLRESGLFSHLPLESRQEMEAQIGALILATDISRQNEYLSLFRSHLDKGDLHLDDGRHRHLVLQMALKCADICNPCRNWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRQTESIANIQIGFMTYLVEPLFTEWARFSDTRLSQTMLGHVGLNKASWKGLQRQQPSSEDANAAFELNSQLLTQENRLS", "text": "FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:11027622). May have a role in muscle signal transduction (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE7 subfamily."}
{"protein": "MDVRVGGKYRLGRKIGSGSFGDIYLGTNISTGDEVAIKLESVRSRHPQLIYESKLYKILTGGIGIPTLYWYGIEGDYNVMIIELLGPSLEDLFSICNRKLSLKTVLMLADQMLNRIEFVHSRHFIHRDIKPDNFLIGRGKKMSIVFAIDFGLAKKYRDPRTQSHIPYREGKNLTGTARYASVNTHLGIEQSRRDDLEALGYVLMYFNRGSLPWQGLKATTKKDKYDKIMEKKMSTPIEVLCKQFPFEFITYLNYCRSLRFEDRPDYSYLRRLFKDLFFREGYQYDFIFDWTFLHAERERERQRRSMVNQGAESGNQWRRDASGRDPLGRLPQLEP", "text": "FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
{"protein": "MEQLFQFLEHHTDFVILGLLGLLSVICLWKAIERIMFYSKVDISKYDTLEELDIDLTHNLTTISTIGSNAPYIGLLGTVVGILLTFYHLGQSGGDIDAASIMVNLSLALKATAVGILVAIIAMVFYNGFGRKVEENKLKWLALQSKKPHQAV", "text": "FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ExbB/TolQ family."}
{"protein": "TDCGILQRIKVKQQWAQVYSVGESRTDFAIDVFNNFFRTNPDRSLFNRVNGDNVYSPEFKAHMVRVFAGFDILISVLDDKPVLDQALAHYAAFHKQFGTIPFKAFGQTMFQTIAEHIHGADIGAWRACYAEQIVTGITA", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the globin family."}
{"protein": "MKRLWLTGYRSYELGVFGDSGEKLKVIKYSLKKQLNNYLDDGLEWLITGGQMGIEQWGIQVAQELKIDYPELKVAMMLPFSDFGQQWNEQNQGTLMTLKAQVDFCEPVIKAPYSGPQQLRQYQQFMLTHTDGALLYYDREAPGKPEYDAKAIETYQEQHEYPNNQVDFFELQDLANELAELENQAF", "text": "SIMILARITY: Belongs to the UPF0398 family."}
{"protein": "MIQKPQMYVYIYLFVLIAAGPVDLNEDSEREANVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRAVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS", "text": "FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MEYLKRLALLISVIILTIFIMGCDSQSDTAENPKEGSKEAQIKKSFSKTLDMYPIKNLEDFYGKEGYRDGEFKKDDKGTWLIRSEIVKQPKGKVMKTRGMQLYINRNTETAKGFFVLKEISENNNRVNKDKEEKYEVKMVGNKIIPTEQINDEKIKKEIENFKFFVQYGNFKNFEKYNNGEFSYNPEAPIYSAKYQLHNDDYNVRQLRKRYDISTKETPKLLLKGGGDLKNSSVGQNDIEFTFVERKGENIYFNDSVEFIPSK", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the staphylococcal tandem lipoprotein family."}
{"protein": "MAFLKKSLFLVLFLGLVSLSICDEEKRENEDEEEQEDDEQSEEKRGMWGSLLKGVATVVKHVLPHALSSQQS", "text": "FUNCTION: Possesses a potent antimicrobial activity against Gram- positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family."}
{"protein": "MYDVTEWKHVFKLDPNKDLPDEQLEILCESGTDAVIIGGSDGVTEDNVLRMMSKVRRFLVPCVLEVSAIEAIVPGFDLYFIPSVLNSKNADWIVGMHQKAMKEYGELMSMEEIVAEGYCIANPDCKAAALTEADADLNMDDIVAYARVSELLQLPIFYLEYSGVLGDIEAVKKTKAVLETSTLFYGGGIKDAETAKQYAEHADVIVVGNAVYEDFDRALKTVAAVKGE", "text": "FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Cannot use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor. SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I subfamily."}
{"protein": "MMEEEELEFVEELEAVLQLTPEVQLAIEQVFPSQDPLDQADFNAVEYINTLFPTEQSLANIDDVVNKIRLKIRRLDDNIRTVVRGQTNVGQDGRQALEEAQKAIQQLFGKIKDIKDKAEKSEQMVKEITRDIKQLDHAKRHLTTSITTLNHLHMLAGGVDSLEAMTRRRQYGEVANLLQGVMNVLEHFHKYMGIPQIRQLSERVKAAQTELGQQILADFEEAFPSQGTKRPGGPSNVLRDACLVANILDPRIKQEIIKKFIKQHLSEYLVLFQENQDVAWLDKIDRRYAWVKRQLVDYEEKYGRMFPREWCMTERISVEFCHVTRAELSKIMRARAKEIEVKLLLFAIQRTTNFEGFLAKRFSGCTLTDGTLKKLESPPPSTNPFLEDETTPEMEELALEKGELEQPKKPKAPDNPFHGIVSKCFEPHLYVYIESQDKNLSELIDRFVADFKAQGPPKPNTDEGGAVLPSCADLFVYYKKCMVQCSQLSTGEPMIALTTIFQKYLREYAWKILSGNLPKTSSSSGGLTISSLLKEKEGSEVARFTLEELCLICSILSTAEYCLATTQQLEEKLKEKVDVSLTERINLTGEMDTFSTVISSSIQLLVQDLDAACDPALIAMSKMPWQNVEHVGDQSPYVTSVILHIKQNVPIIRDNLASTRKYFTQFCIKFANSFIPKFITHLFKCKPISMVGAEQLLLDTHSLKMVLLDLPSIGSQVVRKAPASYTKIVVKGMTRAEMILKVVMAPHEPLVVFVDNYIKLLTDCNSETFQKILDMKGLKRSEQSSMLELLRQRLPAPPSGTEGSSTLSLIAPTPEQESSRIRKLEKLIKKRL", "text": "FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4- positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Recycling endosome Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex. SIMILARITY: Belongs to the VPS53 family."}
{"protein": "MSASVELSSYRDQHFKGSRSEQERSLRDSCTLYVGNLSFYTTEEQIHELFSRCGDVRVIVMGLDKYKKTPCGFCFVEYYIRSEAEAAMRFVNGTRLDDRLIRVDWDAGFIEGRQYGRGKTGGQVRDEYRTDYDAGRGGYGKLLSQKIAPNTDNR", "text": "FUNCTION: Component of the cap-binding complex (CBC), which binds co- transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference via its interaction with Ars2 and is required for primary microRNAs (miRNAs) processing. Also involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. In the CBC complex, Cbp20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires Cbp80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap- binding state with the cap structure (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RRM NCBP2 family."}
{"protein": "MHITNLGLHQVSFQSGDSYKGAEETGKHKGVSVISYQRVKNGERNKGIEALNRLYLQNQTSLTGKSLLFARDKAEVFCEAIKLAGGDTSKIKAMMERLDTYKLGEVNKRHINELNKVISEEIRAQLGIKNKKELQTKIKQIFTDYLNNKNWGPVNKNISHHGKNYSFQLTPASHMKIGNKNIFVKEYNGKGICCASTRERDHIANMWLSKVVDDEGKEIFSGIRHGVISAYGLKKNSSERAVAARNKAEELVSAALYSRPELLSQALSGKTVDLKIVSTSLLTPTSLTGGEESMLKDQVSALKGLNSKRGGPTKLLIRNSDGLLKEVSVNLKVVTFNFGVNELALKMGLGWRNVDKLNDESICSLLGDNFLKNGVIGGWAAEAIEKNPPCKNDVIYLANQIKEIVNNKLQKNDNGEPYKLSQRVTLLAYTIGAVPCWNCKSGKDRTGMQDAEIKREIIRKHETGQFSQLNSKLSSEEKRLFSTILMNSGNMEIQEMNTGVPGNKVMKKLPLSSLELSYSERIGDPKIWNMVKGYSSFV", "text": "FUNCTION: Converts phosphatidylinositol 4,5-bisphosphate (PtdIns 4,5- P2) to PtdIns 5-P. IpgD is injected by Shigella into the host cell and is required for invasion. The accumulation of PtdIns 5-P causes membrane ruffling and actin cytoskeleton rearrangements at the entry site. Acts in concert with IpaA to coordinate and control the membrane and cytoskeletal rearrangements induced early after invasion of the host cell. SUBCELLULAR LOCATION: Secreted Note=Secreted via the Mxi-Spa type III secretion system. It is stored in the bacterial cytoplasm associated with the chaperone IpgE before being secreted in response to activation of the type III secretion system. SIMILARITY: Belongs to the phosphatase IpgD/SopB family."}
{"protein": "MKYTIVPAPRNLHDYVLELLEEWQPDCLDCEYSHGSPSPPTLHDLFDVELETSHSPFVGLCDSCAEADTDSSASTEADSGFSPLSTPPVSPIPPHPTSPASISDDMLLCLEEMPTFDDEDEVRSAATTFERWENTFDPHVGPIFGCLRCAFYQEQDDNALCGLCYLKALAEEPASAGAEEEDDEVIFVSAKPGGRKRSAATPCEPDGVSKRPCVPEPEQTEPLDLSLKPRPN", "text": "FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF- mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the adenoviridae E1A protein family."}
{"protein": "MQQEADVNVFQQDLADMKGEHKALEQRVSALERVSDRQDQQIMTLNEKLNKIEENTTWIKRTITGAIITAVSTGIIGGAIAIMYSLLQH", "text": "FUNCTION: Associated with cell lysis upon induction of PbsX. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: To B.licheniformis xpaF1 and xpaL1."}
{"protein": "MACGAAERGPEPPAFQRHLEASTQRLAHGYGLRSMSELRDQEFGRLAGTVYLDHAGATLFPQSQLTNFTKDLMENVYGNPHSQNITSKLTHDTVEQVRYRILTHFHTTPEDYIVIFTAGSTAALRLVAEAFPWVSRSPENSGSHFCYLTDNHTSVVGMRKVAAAMSVTSIPVKPEDMWSAEGKDAGACDPDCQLPHLFCYPAQSNFSGTRYPLSWVEEVKSGRRSPVNAPGKWFVLLDAASYVSTSPLDLSAHQADFIPISFYKIFGLPTGLGALLVNKHVAPLLRKGYFGGGTAAAYLAGEDFYVPRSSVAERFEDGTISFLDVIALKHGFDALEHLTGGMVNIQQHTFALVQYTHSALSSLRYLNGAPVVRIYSDSEFSSPDVQGPIINFNVLDDGGKIIGYSQVDKMASLYNIHLRTGCFCNLGACQRHLGLSDEMVKKHFQAGHVCGDDVDIIDGRPTGSVRISFGYMSTLEDAQAFLRFISTIYLRSPSDQPVPQASISDAGALTSKSDCHSPQEGSCTDPSVCNGSYPDTNIMDLHPSLSKASSAQQTPQDKAAGILNGDPGSHIVTNIYLYPIKSCAAFEVTKWPVGSQGLLYDRSWMVVNHNGICMSQKQEPRLCLIQPFIDLQQRIMVIKAEGMEPIQVPLEEDGEQTQICQSRVCADRVNTYDCGENVSRWLSKFLGRLCHLIKQSPHFQRNARKTPKKGQPPGTTVALSLVNEAQYLLVNTSSILELQRQLNASDEHGKEESFSMKDLISRFRANIITKGARAFEEEKWDEISIGSLHFQVLGPCHRCQMICINQQTGQRNQDVFQTLSESRGRKVNFGVYLMHSYLDLSSPCFLSVGSEVLPVLKDCGVS", "text": "FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily."}
{"protein": "MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRXXC", "text": "FUNCTION: Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. EIF2S1/eIF2-alpha is a key component of the integrated stress response (ISR), required for adaptation to various stress: phosphorylation by metabolic-stress sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF2-alpha in a global protein synthesis inhibitor, leading to a attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1- mediated reprogramming. SUBCELLULAR LOCATION: Cytoplasm, Stress granule Note=Colocalizes with NANOS3 in the stress granules. SIMILARITY: Belongs to the eIF-2-alpha family."}
{"protein": "MFAGLQDLGVANGEDLKETLTNCTEPLKAIEQFQTENGVLLPSLQSALPFLDLHGTPRLEFHQSVFDELRDKLLERVSAIASEGKAEERYKKLEDLLEKSFSLVKMPSLQPVVMCVMKHLPKVPEKKLKLVMADKELYRACAVEVKRQIWQDNQALFGDEVSPLLKQYILEKESALFSTELSVLHNFFSPSPKTRRQGEVVQKLTQMVGKNVKLYDMVLQFLRTLFLRTRNVHYCTLRAELLMSLHDLDVSDICTVDPCHKFTWCLDACIRERFVDSKRARELQGFLDGVKKGQEQVLGDLSMILCDPFAINTLSLSTIRHLQELVSQETLPRDSPDLLLLLRLLALGQGAWDLIDSQVFKEPKMEAELITKFLPMLMSLVVDDFTFNVDQKLPAEEKASVTYPNTLPESFTKFLQEQRMACEVGLYYVLHITKQRNKNALLRLLPGLVETFGDLAFSDIFLHLLTGSLVLLADEFALEDFCSSLFDGFFLTASPRKENVHRHVLRLLLHLHARVAPSKLEALQKALEPTGQSGEAVKELYSQLGEKLEQLDHRKPSPTQAAETPALDLPLPSVPAPATL", "text": "FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (Pol II) (PubMed:25773599). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (By similarity). May be able to induce chromatin unfolding (By similarity). Essential for early embryogenesis; plays an important role in maintaining the undifferentiated state of embryonic stem cells (ESCs) by preventing unscheduled expression of developmental genes (PubMed:19340312). Plays a key role in establishing the responsiveness of stem cells to developmental cues; facilitates plasticity and cell fate commitment in ESCs by establishing the appropriate expression level of signaling molecules (PubMed:25773599). Supports the transcription of genes involved in energy metabolism in cardiomyocytes; facilitates the association of transcription initiation factors with the promoters of the metabolism-related genes (PubMed:24656816). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NELF-B family."}
{"protein": "MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLLTGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRWEHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLGVWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLLALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLIMMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQIRYHTNNYASSSTSLPCQCSSTLMWSDHLER", "text": "FUNCTION: Receptor for prostaglandin E2 (PGE2) (PubMed:8307176, PubMed:7883006, PubMed:8117308, PubMed:8135729, PubMed:7981210). The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G(i) proteins, and to an elevation of intracellular calcium (PubMed:7883006, PubMed:8117308, PubMed:8135729, PubMed:7981210). Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation. Required for increased HCO3(-) secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid- induced ulceration. Not required for normal kidney function, normal urine volume and osmolality (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MERGVRVFGEPKVELHIHLDGAIRPETILHFGKKRGVPLPGSTVDELMKHVSYQTPLSLKLFLEKFNHYMPAIAGDREAVRRIAYELVETKAKEGVVYVEVRYSPHLLANCRVEPIPWGQAEGDLTPEEVVNLVNQGLQDGERNFRIKARSILCCMRHMPSWSPEVVELCKKYQNNSVVAIDLAGDELLMASSDHKAAYEEAERCGIHRTVHAGEAGPATMIKEAVYLLKAERIGHGYHVLEDPELYRELLRTRMHFEVCPWSSYLTGACLPDFRKHPVVQFKKDQANYSINTDDPLIFNSNIDKDYGIVKEYMDFTEEDFKRVNINAAQSSFLPEKEKQELLNTLYEAYGMVPATS", "text": "FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. May act as a positive regulator of T-cell coactivation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side Cell junction Cytoplasmic vesicle lumen Cytoplasm Lysosome. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family."}
{"protein": "MTSLDPAPNKTWELSLYELQRKPQEVITDSTEIAVSPRSLHSELMCPICLDMLKKTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRADPNFDLLISKIYPSREEYEAIQEKVMAKFNQTQSQQALVNSINEGIKLQSQNRPQRFRTKGGGGGGGGGGNGNGAANVAAPPAPGAPTAVGRNASNQMHVHDTASNDSNSNTNSIDRENRDPGHSGTSAASAITSASNAAPSSSANSGASTSATRMQVDDASNPPSVRSTPSPVPSNSSSSKPKRAMSVLTSERSEESESDSQMDCRTEGDSNIDTEGEGNGELGINDEIELVFKPHPTEMSADNQLIRALKENCVRYIKTTANATVDHLSKYLAMRLTLDLGADLPEACRVLNFCIYVAPQPQQLVILNGNQTLHQVNDKFWKVNKPMEMYYSWKKT", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-118' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-118' ubiquitination gives a specific tag for epigenetic transcriptional repression. Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. PcG complexes act via modification of histones, such as methylation, deacetylation, ubiquitination rendering chromatin heritably changed in its expressibility. May play a role in meiotic sister chromatid cohesion. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with ubiquitinated histone H2A. Colocalizes with Pc, Pcl, Psc, ph at many sites on polytene chromosomes. Colocalizes with ORD on the chromatin of primary spermatocytes during G2 of meiosis."}
{"protein": "MGVPRTPSRTVLFERERTGLTYRVPSLLPVPPGPTLLAFVEQRLSPDDSHAHRLVLRRGTLAGGSVRWGALHVLGTAALAEHRSMNPCPVHDAGTGTVFLFFIAVLGHTPEAVQIATGRNAARLCCVASRDAGLSWGSARDLTEEAIGGAVQDWATFAVGPGHGVQLPSGRLLVPAYTYRVDRRECFGKICRTSPHSFAFYSDDHGRTWRCGGLVPNLRSGECQLAAVDGGQAGSFLYCNARSPLGSRVQALSTDEGTSFLPAERVASLPETAWGCQGSIVGFPAPAPNRPRDDSWSVGPGSPLQPPLLGPGVHEPPEEAAVDPRGGQVPGGPFSRLQPRGDGPRQPGPRPGVSGDVGSWTLALPMPFAAPPQSPTWLLYSHPVGRRARLHMGIRLSQSPLDPRSWTEPWVIYEGPSGYSDLASIGPAPEGGLVFACLYESGARTSYDEISFCTFSLREVLENVPASPKPPNLGDKPRGCCWPS", "text": "FUNCTION: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Efficiently hydrolyzes gangliosides including alpha- (2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3 (PubMed:15847605, PubMed:21521691, PubMed:15213228). Hydrolyzes poly- alpha-(2->8)-sialylated neural cell adhesion molecule NCAM1 likely at growth cones, suppressing neurite outgrowth in hippocampal neurons (By similarity). May desialylate sialyl Lewis A and X antigens at the cell surface, down-regulating these glycan epitopes recognized by SELE/E selectin in the initiation of cell adhesion and extravasation (PubMed:21521691). Has sialidase activity toward mucin, fetuin and sialyllactose (PubMed:15847605). SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Lysosome lumen Note=According to PubMed:15213228, isoform 2 is soluble, N-glycosylated and found in the lumen of lysosomes. However, no signal sequence nor N-glycosylation site is predicted from the sequence. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Mitochondrion membrane; Peripheral membrane protein. Cell projection, neuron projection Note=Predominantly associates with endoplasmic reticulum membranes. Only a small fraction associates with mitochondrial and plasma membranes. SIMILARITY: Belongs to the glycosyl hydrolase 33 family."}
{"protein": "MYVWPCAVVLAQYLWFHRRSLPGKAILEIGAGVSLPGILAAKCGAEVILSDSSELPHCLEVCRQSCQMNNLPHLQVVGLTWGHISWDLLALPPQDIILASDVFFEPEDFEDILATIYFLMHKNPKVQLWSTYQVRSADWSLEALLYKWDMKCVHIPLESFDADKEDIAESTLPGRHTVEMLVISFAKDSL", "text": "FUNCTION: Histone methyltransferase that dimethylates histone H3 at 'Arg-17', forming asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling (By similarity). Maternal factor involved in epigenetic chromatin reprogramming of the paternal genome in the zygote: mediates H3R17me2a, promoting histone H3.3 incorporation in the male pronucleus, leading to TET3 recruitment and subsequent DNA demethylation (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localizes in male and female zygote pronucleus and cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. METTL23 family."}
{"protein": "MSRPIDTYRQVGSAQDVPPYQVVKLLLDGALERIALARRAVLERNPALRGEAVGTTLSIIGALQAGLDHQQGGEIAGNLDALYDYMTRRLAGVALDDTPRPLDEVEALLGQIKQAWDAIGSAEAQGEDSERR", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the FliS family."}
{"protein": "MKPVPLVLLITSVLLTTHIPLSTCRPRDLSLVNSQLDDVLSNGAGDDAMSYLVGEKLLQYLQRNLGAQKASGVLHLPHFPAAQLRSPHEDSSLEELTEFSKRNDDPPISIDLTFHLLRNMIEMARNENQREQAGLNRKYLDEVGK", "text": "FUNCTION: Urotensin is found in the teleost caudal neurosecretory system. It has a suggested role in osmoregulation and as a corticotropin-releasing factor. The non-hormonal portion of this precursor may be a urotensin binding protein, urophysin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family."}
{"protein": "INWKKIAEVGGKILSSL", "text": "FUNCTION: Shows antimicrobial activity against the Gram-positive bacteria B.subtilis ATCC 6633 (MIC=2 ug/ml), and the Gram-negative bacteria E.coli JM109 (MIC=8 ug/ml). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MCD family. Mastoparan subfamily."}
{"protein": "MSAAAGLIPPPVSWAQRNDLIYVIIDVECKDIEHKVTEKTFTFKGVNVLDPSKKYEVTLNFLHEVDPEKVTSKNIGRCLEFTIPKKAAGPYWSSLTTDKTKLHFLKANFAKWRDESDDEEGDQKDNSMFGNFLNSPGGDWNNKFDDFNVDDEEEDSDDNIPSLSQNDEDDEEGGEGDKEKKPAA", "text": "SIMILARITY: Belongs to the p23/wos2 family."}
{"protein": "MNVQRKLASTQLKPVLLGVLLATSAWSQAAPPEQARQSAPPTLSSKQYSVTSASIEALKLDPPKLPDLSGYTHAAVEAKIRRKPGGRIAAAMLQQTALKDFTGGSGRLREWIVRQGGMPHAIFIEGGYVELGQLARQLPANQFAETTPGVYVARVPIVVAPGATLHIGKNVKELRLSEERGAFLVNDGKLFITDTKLVGWSEKNNAPSAYRGPESFWAFLVSWGGTETYISRRPVASLGYNTSKAYGVSITQYTPEMHKRLKRPRPTGWLIDSVFEDIYYGFYCYEADDVVLKGNTYRDNIIYGIDPHDRSERLVIAENHVYGTKKKHGIIVSREVNNSWIINNRTHDNKLSGIVLDRNSEHNLVAYNEVYQNHSDGITLYESSNNLIWGNRLINNARHGIRMRNSVNIRIYENLSVVNQLTGIYGHIKDLSSTDRDFKLDPFDTKVSMIVVGGQLTGNGSSPISVDSPLSLELYRVEMLAPTKSSGLTFTGILEDKQEEILDLLVRRQKAVLIDPVVDLAQAEL", "text": "FUNCTION: Catalyzes the epimerization of beta-D-mannuronate to alpha-L- guluronate during the synthesis of the linear polysaccharide alginate (PubMed:8830682). In addition, is part of a periplasmic protein complex that protects alginate from degradation by AlgL by channeling the newly formed alginate polymer through a scaffold that transfers the alginate polymer through the periplasmic space to the outer membrane secretin AlgE (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the D-mannuronate C5-epimerase family."}
{"protein": "MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPAFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKCKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEPVGALHLIQAAKLGNVKAQNILRTAGTALGLGVVNILHTMDPSLVILSGVLASHYIHIVKDVIRQQASSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIH", "text": "FUNCTION: Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Plays an essential role in early development (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the UDP-N- acetylglucosamine 2-epimerase family. SIMILARITY: In the C-terminal section; belongs to the ROK (NagC/XylR) family."}
{"protein": "MNKKSILKKPKNAQSTQEKQLITWSKSLIDEARSRLQYDFFALEWIEKLVDPVSLETLEEARKYLRKSDYDQVVKERKLVNLCGYPVCPYEPKQQTRYKLEDSGMKVYGGLNYYCSKDCFLKSCQYMVELSDEPLWIREDAREAMKQHLDPRQDEAFRKELENKKIEDVRLLLQALPVGYKAKVGEIVEHPLANEQS", "text": "FUNCTION: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the RPAP2 family."}
{"protein": "MAEADFKMVSEPVAHGVAEEEMASSTSDSGEESDSSSSSSSTSDSSSSSSTSGSSSGSGSSSSSSGSTSSRSRLYRKKRVPEPSRRARRAPLGTNFVDRLPQAVRNRVQALRNIQDECDKVDTLFLKAIHDLERKYAELNKPLYDRRFQIINAEYEPTEEECEWNSEDEEFSSDEEVQDNTPSEMPPLEGEEEENPKENPEVKAEEKEVPKEIPEVKDEEKEVPKEIPEVKAEEKADSKDCMEATPEVKEDPKEVPQVKADDKEQPKATEAKARAAVRETHKRVPEERLQDSVDLKRARKGKPKREDPKGIPDYWLIVLKNVDKLGPMIQKYDEPILKFLSDVSLKFSKPGQPVSYTFEFHFLPNPYFRNEVLVKTYIIKAKPDHNDPFFSWGWEIEDCKGCKIDWRRGKDVTVTTTQSRTTATGEIEIQPRVVPNASFFNFFSPPEIPMIGKLEPREDAILDEDFEIGQILHDNVILKSIYYYTGEVNGTYYQFGKHYGNKKYRK", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family."}
{"protein": "MENWDLSSDEMQDGNAPELDVIEEHNPVTRDDENANPEEVVGDTRSPVQNILGKFEGDINKRLHIKRKRMETYIKDSFKDSNVKLEQLWKTNKQERKKINNKFCEQYITTFQKFDMDVQKFNEEQEKSVNNYQKEQQALKLSKCSQSQTLEAIKDMHENYMEGLMNLETNNYNMLFDVDGELRKEMSVFKKDLMKHTLKYSSSFPSSD", "text": "SIMILARITY: Belongs to the XLR/SYCP3 family."}
{"protein": "MLLRSLVGSLTRQWSQFARCAASLSLPAVGAQRCLSTITAAAVPFRAVVNPMFKPHTAFLSPLLGRCQQLLCVQPSAGMKTKSALKKRCNECFFVRRRGRLFVFCKAHPRHKQRQG", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family."}
{"protein": "MMLAQKQNFMNQFYKKYHYSIQKYQITDLLFFLFLYPFSTSYGNEQFSFDSRFLPSGYNYSLNSNLPPEGEYLVDIYINKIKKESAIIPFYIKGNKLVPCLSKEKLSSLGININNNDNAECAETSKAGISNISFEFSSLRLFIAVPKNLLSEIDKISSKDIDNGIHALFFNYQVNTRLANNKNRYDYISVSPNINYFSWRLRNRFEFNQNNDKKTWERNYTYLEKSFYDKKLNLIVGESYTSSNVYNNYSFTGISVSTDTDMYTPSEIDYTPEIHGVADSDSQIIVRQGNTIIINESVPAGPFSFPITNLMYTGGQLNVEITDIYGNKKQYTVSNSSLPVMRKAGLMVYNFISGKLTKKNSEDGDFFAQGDINYGTHYNSTLFGGYQFSKNYFNLSTGIGTDLGFSGAWLLNVSRSNFKDKNGYNINLQQNTQLRPFNAGVNFDYIYRKKGYVELSGIGWHGNLYNQLKNSFSLSLSKSLDKYGNFSLDYNKIKYWDNAYDSNSMSIRYFFKFMRAMITTNYSLNKYQSYEKKDKRFSINISLPLTKDYGHISSNYSFSNANTGTATSSVGVNGSFFNDARLNWNIQQNRTTRNNGYTDNTSYIATSYASPYGVFTGSYSGSNKYSSQFYSALGGIVLHSDGVAFTQKAGDTSALVRIDNISDIKIGNTPGVYTGYNGFALIPHLQPFKKNTILINDKGIPDDIALANIKKQVIPSRGAIVKVKFDAKKGNNILFKLTTKDGKTPPLGAIAHEKNGKQINTGIVDDDGMLYMSGLSGAGIINVTWNGKVCSFPFSEKDISSKQLSVVNKQCNRPENSGD", "text": "FUNCTION: Involved in the export and assembly of C6 fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
{"protein": "MDLTLLQWGDAGWGDELARGAMMTVVVAACSYFFGIIFGSLFAAAKLSRFWSLRLLGDVYTTVVRGVPELLIIFLVFFGGGTLLRTIANGLFGYEGYIEPPIFVIGVLCISVSAGAYATEVIRAAVLAVPPGQIEAAKSIGMGPWLRLRRVLIPQAARFALPGLGNVWQFTLKDTSLISVVGLVEIMRTAAMGAGSTKQPFTFYITAFVIFLLLSSVSNRGFLKAEKWANRGVRSQ", "text": "FUNCTION: Component of the nopaline active transport system probably consisting of four subunits: Q, M, P and T. This system is also capable of transporting octopine provided that catabolic functions are induced with nopaline. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily."}
{"protein": "MSSLLLNKEIFSKSISIVGLKVNKTLLKTLAQEFKGYLLIRDRVKHIVDDSDSKDKKLVLLSESIENGNVGAYGVNKQLPDNLQSFLKTHSIEVVKHQVQLNYNNFSYEEVMKELIPTGLPIPHAFEKIGHIAHLNLKEELLPYKNMIGQVILDKKGPQIRTVLNKVGKIDTVFRTFNFELLAGDNDLLAQVVYWNSRLQFEHSNLIQTFKSHDIVVDMFAGVGPFAVPASKLVKCKVYANDLNPNSVKYMRENATRNKASTIEISNLDARDFVRELVSRDPPVAFTQAIMNLPSTSIEFLDVFREIFLNPEKAPPIPAPTIHCYTFTPVSETAGGDLKELTIKNVEAIIKHPLPADTTVYEVRDVSPNKRMMRISFKMPTLKKRKDTENNDDQENNNNSSNNNNNNKIDYNEAVSSGGEGKKIKH", "text": "FUNCTION: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Cytoplasm Note=Predominantly in the mitochondria and in the nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family."}
{"protein": "MFNFFKKNKLNKFQNTINEIHQIGNTVKNYSDAELKKQTHKLKKKIIQNSNLTEILPESFAIVKEAIKRSTGMILFDVQLVGSIVLHQGQIAEMKTGEGKTIVAITTGYLNALTSKGVHIITVNDYLAKRDSELAQKICSYIDLKVGLITQSMTYEEKKRAYDCDITYITNSELGFDYLRDNMAIEFNQIVQRGFNFAIIDEVDSILIDEARTPLIISGPFEIEINKYKKSTSIANTLQKDLDYEIDEKTKNITLTEKGISRCENMLNIDNLYDIHDSWIQYLLNSLKAKDLFLKNQHYIVKNNEIIIVDEFTGRVMQGRRWSDGLHQAIESKENIPIQQENKTLASITYQNLFLLYEKLSGMTGTAKTEETELDKIYNLEVLEIPTNKICKRQDLPDLVYKTEYKKWQAIADECFDMYHIGRPTLIGTTNVEKSELLAKILMELQIPFNLLNAKPENVSREAEIITQAGRKNTITISTNMAGRGTDIILGGNPEALSKLALTYYLQNKLGLKVNYLLNNIETQITTIINNYVLDMQELDIYKYKNIDLKKIQYYIEKIIKNEHTKYSEEEKLQKLYLKILSEYKNICYQEKQEVLKLGGLYVIGTERHESRRIDNQLRGRAGRQGDIGASRFFLSLEDNLLRIFGGDKISQLMDNLNIDEHTPIESIILSKSLDSAQKKVESYFYDIRKQLFEYDEVINNQRQAIYAERKRILQSSFTRDCIIEYAESTIDEILTAFYREDNINNKNHIIKKIYQLLNLTENFHFNTLYDMNYKQIQEFLYEQLRISYDLRESYLEQLRPGLIRKLEKYYLLQQIDKAWQDHLDKMALLRESIGWRSYGQQDPLVEYKNEAFSLFINMVRYIRQTVTYLTMRSRLIINVNN", "text": "FUNCTION: Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane. SUBCELLULAR LOCATION: Plastid, chloroplast stroma Plastid, chloroplast thylakoid membrane; Peripheral membrane protein Note=A minor fraction is associated with the chloroplast thylakoid membrane. SIMILARITY: Belongs to the SecA family."}
{"protein": "MEEELKSFVKVWGSAIISVSYCYYIPSKIKSGVHRLLSVLPVCVLFLVLPLFFVFTIFSSTTAFCLSILANFKLILFAFDKGPLLPLPANLFRFICFTCLPIKIQKNPNSQNHLPKWVFFCKAAIFGVLLNVHNYKSSLPPILLICLYPLHLYLVLDVLLTIVNALLTIILGCDLEPHFNEPYLATSLQDFWGRRWNLMVPAIFRPGVYHPMRSVCQPQMRSDWARFMGCWTTFFVSGLIHELVYFYINRETPTWEVTWFFVLQGVCTAMEKAVKRKTRWSLSPMLSRLITVGFLVVTGYFLFFRQIERSNMLERRATEASLIIDFVKHKLSNFLL", "text": "FUNCTION: Catalyzes the final step in the synthesis of long-chain linear esters (waxes). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the wax synthase family."}
{"protein": "MKFLSFKYNDKTSYGVKVKREDAVWDLTQVFADFAEGDFHPKTLLAGLQQNHTLDFQEQVRKAVVAAEDSGKAEDYKISFNDIEFLPPVTPPNNVIAFGRNYKDHANELNHEVEKLYVFTKAASSLTGDNATIPNHKDITDQLDYEGELGIVIGKSGEKIPKALALDYVYGYTIINDITDRKAQSEQDQAFLSKSLTGGCPMGPYIVTKDELPLPENVNIVTKVNNEIRQDGNTGEMILKIDELIEEISKYVALHPGDIIATGTPAGVGAGMQPPKFLQPGDEVKVTIDNIGTLTTYIAK", "text": "SIMILARITY: Belongs to the FAH family."}
{"protein": "MCVCQTMEVGQYGKNASRAGDRGVLLEPFIHQVGGHSSMMRYDDHTVCKPLISREQRFYESLPPEMKEFTPEYKGVVSVCFEGDSDGYINLVAYPYVESETVEQDDTTEREQPRRKHSRRSLHRSGSGSDHKEEKASLSLETSESSQEAKSPKVELHSHSEVPFQMLDGNSGLSSEKISHNPWSLRCHKQQLSRMRSESKDRKLYKFLLLENVVHHFKYPCVLDLKMGTRQHGDDASAEKAARQMRKCEQSTSATLGVRVCGMQVYQLDTGHYLCRNKYYGRGLSIEGFRNALYQYLHNGLDLRRDLFEPILSKLRGLKAVLERQASYRFYSSSLLVIYDGKECRAESCLDRRSEMRLKHLDMVLPEVASSCGPSTSPSNTSPEAGPSSQPKVDVRMIDFAHSTFKGFRDDPTVHDGPDRGYVFGLENLISIMEQMRDENQ", "text": "FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family."}
{"protein": "MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL", "text": "FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Host endosome membrane; Single-pass type I membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. SIMILARITY: Belongs to the HIV-1 env protein family."}
{"protein": "MKYTSYILAFQLCVVLGSLGCYCQDPYVKEAENLKKYFNAGDSDVADNGTLFLDILRTWREEGDRKIMQSQIISFYFKLFKNFKDNQSIQKSMETIKEDMNVKFFNSNKRKQDDFERLTNYSVNDLNVQRKAIHELIQVMAELSPAPKIGKRRRSQTLFRGRRASQ", "text": "FUNCTION: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By similarity). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type II (or gamma) interferon family."}
{"protein": "MSQVTTSYSYDAPTDFINFSSLTDEEDMQHIDSWFDEKANLENKFTGKDGTGGLYQGKTPLRKANLHRDVTPLRPVDNTYNKQAEKENLVEESIPSNECPSMKVKETTSRNNPVQPQRRSLRLSAKKNLEQKEKQHVKMKAKRCGTPVIINEFPPSKKMKVQKILKSTEEQELEKRMKMQQEVVEMRKRNEEFKKFALAGAGQPVKKSVSQVTKAVDFHFRTDERVKQHPKNQEEYKEVNFTSELRKHPPSPARVTKGCTIVMPFNLSQGKKRTFDETASTYVPLAQQVEAFHKRTPTRYHLRNRKDDIMPLPSKSVVRICRDPQTPVLQTKHRTRPVTCKSAADLEAEELEKQQQYKFKAQELDPRILEGGPILPKKPPVKPPTQPVGFDLEIEKRIQERESKKKLEEEHYEFHSRPCPTKILEDVVGVPEKKELPITVPKSPAFALKNRIRMPTKEDKEEEEPVMIRAQPVPYFGMPFKPQIPVGRTVEVCPFSFDSRDKERQLQKEKKIKELQKGEVPKFKAHPLPHFDTINLPEKKVKNTTQVEPFCLETDRRGALKAQTWKHQLDEELKQQKEAACFKARPNTVISQEPFVPKREKKSVIEGLSGSLVQEPFQLATEKRAKERQELEKRMAEVEALKAQQLEEARQQEEEQQKEELARLRKELVHKANPIRRYQGVEVKSSDQPLTVPVSPKFSTRFHC", "text": "FUNCTION: Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation. TPX2 is inactivated upon binding to importin-alpha. At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin- alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=During mitosis it is strictly associated with the spindle pole and with the mitotic spindle, whereas during S and G2, it is diffusely distributed throughout the nucleus. Is released from the nucleus in apoptotic cells and is detected on apoptotic microtubules. SIMILARITY: Belongs to the TPX2 family."}
{"protein": "MAKVYKDLREFLEVLEQEGQLIRVKEEVNPEPDIAAAGRAAANLGKNQPAVFFEKIKGYKYSVVTNVHGSWQNHALMLGLDKNTSTKDQFYELNRRWDKFPVPPNVVKREAAPCKENVIDKDINLFEILPLYRINEQDGGFYISKASVVTADPEYPDDFNKLNVGTYRIQVKDRDRVGIQALAMHDIAVQLEKAEAENKPLPIAITIGNNPLVTFMASTPVGYNQNEYEFVGALQDGVPMDIVKSDLYDHLYVPAGSEVVLEGHIIPRVRTVEGPFGEFPGSYSGARLQCEVKIDRITHRTNPIFENLYLGIPWTEIDYLMALNTSVPLYKQLKETMPEVVAVNAMYTHGIGVIISTKVRYGGYAKGVAFRLLSTPHGMPYSKIVIVVDEFVDPFNLEQVMWALTTRVHPGKDVSIIENCPGMPLDPSTNPPGMHTKMIIDATTPVPPEPNPRETQLLDPPDGTEEWEEKLKELLKNQNR", "text": "FUNCTION: Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under anaerobic conditions (PubMed:10438791, PubMed:7744052, PubMed:24193968, PubMed:15979273). Oxygen-sensitive phenolic acid decarboxylase that catalyzes the reversible decarboxylation of 4-hydroxybenzoate and 3,4- dihydroxybenzoate (PubMed:10438791, PubMed:7744052, PubMed:15979273). SIMILARITY: Belongs to the UbiD family. YclC subfamily."}
{"protein": "MNIIQGNLVGTGLKIGIVVGRFNDFITSKLLSGAEDALLRHGVDTNDIDVAWVPGAFEIPFAAKKMAETKKYDAIITLGTVIRGATTHYDYVCNEAAKGIAQAANTTGVPVIFGIVTTENIEQAIERAGTKAGNKGVDCAVSAIEMANLNRSFE", "text": "FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. Is able to use the non-natural R enantiomer of 3,4- dihydroxy-2-butanone 4-phosphate as a substrate, but with less efficiency than the natural S enantiomer. Cannot use unphosphorylated 3,4-dihydroxy-2-butanone, 3,4-dihydroxy-2-butanone 3-phosphate or diacetyl as substrates. SIMILARITY: Belongs to the DMRL synthase family."}
{"protein": "MPIRVFDELPAVNFLRNENVFVMTSSRASTQEIRSLKVLILNLMPKKIETENQFLRLLSNSPLQVDIQLLRIDSRESKNTPAEHLNNFYCNFEDIQHDNFDGLVVTGAPLSLVDFHDVVFWPQIDRVLHWARDHVTSTLFVCWAVQAALNILYGIPKMTRQQKLAGVYQHHLLKPHALLTRGFDETFLAPHSRNADFPTAMIRQHTDLEILAESDEAGAYLFASHDKRLAFVTGHPEYDALTLASEYHRDRENGLNPSLPVNYFLQDNPDLTPKASWRSHGHLLVANWLNYYVYQITPYDLRRMNPTLE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MetA family."}
{"protein": "MVRVRAVVMARDDSSGGWLPVGGGGLSQVSVCRVRGARPEGGARQGHYVIHGERLRDQKTTLECTLRPGLVYNKVNPIFHHWSLGDCKFGLTFQSPAEADEFQKSLLAALAALSRGSLTPSSSSSSSSPSQDTAETPCPLTSHVDSDSSSSHSRQETPPTAPIATVESAAAFPLATRPQRRRSSAQSYPPLLPFTGIPEPSESLAGAGSQGWGSRGYEDYRRSGPPPPPLALSTCVVRFAKTGALRGAALGPPVSLPAPLTEAAPPAPPARPPPGPGPTPAPAKASPEAEEAARCVHCRALFRRRADGRGGRCAEAPDPGRLLVRRLSCLWCAESLLYHCLSDAEGDFSDPCACEPGHPRPAARWAALAALSLAVPCLCCYAPLRACHWVAARCGCAGCGGRHEEAAR", "text": "FUNCTION: Tyrosine kinase substrate that inhibits growth-factor- mediated activation of MAP kinase (PubMed:12646235). Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (PubMed:29501879). Inhibits TGFB-induced epithelial-to- mesenchymal transition in lens epithelial cells (PubMed:25576668). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein."}
{"protein": "MSIGLLCCVAFSLLWAGPVNAGVTQTPKFHILKTGQSMTLQCAQDMNHGYLSWYRQDPGMGLRRIHYSVAAGITDKGEVPDGYNVSRSNTEDFPLRLESAAPSQTSVYFCASSY", "text": "FUNCTION: V region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). SUBCELLULAR LOCATION: Cell membrane."}
{"protein": "MRESTWVSLLLLLLLPAPQRGGPQDGRGSPEPEPERGPLQPFDLLYASGVAAYYSGDYEGAVRDLEAALRSHRRLRDIRTRCARHCAARRPLAPPGAGPGAELPFFRAVLERARCSRSCQSQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLDKAMEAAHTFFMANPEHMEMQQNIEDYKATARVEAPLVDREAKPHLESYNAGVKHYEADDFEAAIKYFEQALREYFNEDMVCRALCEGPQRFEEYEYLGSKGSLYEAIADHYMQVLVCQHECVRELATRPGRLSPIENFLPLHYDYLQFAYYRVGEYVKALECAKAYLMFHPDDQDVLDNVDFYESLLDDSTDPASIEAREDLTAFVKRHKLEAELIKSAAEGLGFSYSEPNYWISYGGRQDENRVPSGVNMDGAEVHGLSMGKKSPPKIGRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELHSVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKFGYEGRVPLKSARLFYDISEKARKIVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAYTFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTRGQRCAVALWFTLDPLYRELERIQADEVIAILDQEQHGKHGLNINPKDEL", "text": "FUNCTION: Prolyl 3-hydroxylase that catalyzes the post-translational formation of 3-hydroxyproline on collagens (PubMed:21757687). Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (By similarity). Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline. Has no activity on substrates that lack 4-hydroxyproline in the third position (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum Sarcoplasmic reticulum Golgi apparatus. SIMILARITY: Belongs to the leprecan family."}
{"protein": "MTWLSGLYSIFVASAAFCSLGLILVAVILLSRKFLIKVHPCKLKINNDDSLTKTVDSGKTLLSSLLDSGIAIPSPCGGKAACKQCKVRITKNADEPLETDRSTFSKQQLEQGWRLSCQTKVQHDLCLEVEERYFNASSWEGTVVSNENVATFIKELVLSVDPSRPIPFKPGGYLQITVPPYKTNTSDWKQTMDPQYYSDWETFHLFDQIIDNLSLDTDSANKAYSLASYPAELPLIKFNVRIATPPFVDQAPDPTIPWGVCSSYIFSLKPGDKVMVSGPYGESFMKEDNRPVIFLIGGAGSSFGRSHILDLLLNKHSDRELTLWYGARSLKENIYQEEYEKLEKEFPNFHYHLVLSQPLQEDLDQGWDKNDPIKTNFLFKAFELGQLSHLPNPEDYLYYVCGPALHNSSILTLLDNYGVERSSIVLDDFGS", "text": "FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the NqrF family."}
{"protein": "MFLKVHEIAFLFGLLGNIVSFGVFLSPVPTFYGIYKKKSSKGFQSIPYICALASATLLLYYGIMKTHAYLIISINTFGCFIEISYLFLYILYAPREAKISTLKLIVICNIGGLGLLILLVNLLVPKQHRVSTVGWVCAAYSLAVFASPLSVMRKVIKTKSVEYMPFLLSLSLTLNAVMWFFYGLLIKDKFIAMPNILGFLFGVAQMILYMMYQGSTKTDLPTENQLANKTDVNEVPIVAVELPDVGSDNVEGSVRPMK", "text": "FUNCTION: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane (By similarity). Nectary-specific sugar transporter required for nectar production by mediating the secretion of sucrose from the nectary parenchyma to the extracellular space. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane Golgi apparatus, trans- Golgi network membrane. SIMILARITY: Belongs to the SWEET sugar transporter family."}
{"protein": "MKTHKTKNDLPSNAKSTVIGILNESLASVIDLALVTKQAHWNLKGPQFIAVHELLDTFRTQLDNHGDTIAERVVQLGGTALGSLQAVSSTTKLKAYPTDIYKIHDHLDALIERYGEVANMIRKAIDDSDEAGDPTTADIFTAASRDLDKSLWFLEAHVQEKS", "text": "FUNCTION: Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. It efficiently inhibits hydroxyl radical production by the Fenton reaction. Does not bind DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Dps family."}
{"protein": "MALEKSLETGDGQEKVRKQTAVYVYEAPLRLWHWVTALSIVVLGVTGYFIGAPLPTMPGEAMDNYLMGYIRFAHFAAGYVLAIGFLGRVYWAFVGNHHARELFLVPVHRKAWWKELWHEVRWYLFLEKTPKKYIGHNPLGQLAMFCFFVVGAVFMSVTGFALYAEGLGRDSWADRLFGWVIPLFGQSQDVHTWHHLGMWYLVVFVMVHVYLAVREDIVSRQSLISTMVGGWRMFKDDRPD", "text": "FUNCTION: Probable b-type cytochrome. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HupC/HyaC/HydC family."}
{"protein": "MCSIGEDDFGDDGAAHAMAVESLPLGIVLSPGNCSKCDVNSDELYKLNFRTAECRECFLAYARHKFRAALGAAKILPRNAEVLLVLDGSAESLVLLDMLHFAQTQNTFKRLHCNARVVYVEEQQVQGRDPVHLEALQNLSTQYAPFDFYVIELGALPSSMQRIKDYSPSLNANNELIHKLQKLRSLTARQDYLQQQRKNLICSVAQCLRCTHVFESNISVDLATQLLTAIALGRGGSAALDVALLDDRLSGDVKLLRPLKDLNEQEIQFYIHAQRLKPLFQKGSRYGREHGQTASLQNLTSAFVANLQQNYASTVSTVFRTGDKIAANSNPEQSSCVHCRSTLDTELSDTLLAIEYSRSVSEAGVSLYKSGQDLEDLAKKRLENKDGLCHACRAIQAELDSGNLL", "text": "FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6/CTU1 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CTU2/NCS2 family."}
{"protein": "MWSRNVRLLGSWTRSYMVPATKRKTIPVYPPVQRIASSQIMKQVALSEIESLDPGAVKRKLISKKNKDRLKAGDVVRIVYDSSKCSYDTFVGYILSIDRKQLVQDASLLLRNQIAKTAVEIRVPLFSPLIERIDLLTPHVSSRQRNKHYYIRGTRLDVGDLEAGLRRKK", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:24675956). bL19m is essential for respiration (PubMed:8771712). SUBCELLULAR LOCATION: Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family."}
{"protein": "MPGIPLVSRETSSCSRSTEQMCHEDSRLRISEEEEIAAEESLAAYCKPVELYNIIQRRAIRNPLFLQRCLHYKIEAKHKRRIQMTVFLSGAIDAGVQTQKLFPLYILLARLVSPKPVAEYSAVYRFSRACILTGGLGVDGVSQAQANFLLPDMNRLALEAKSGSLAILFISFAGAQNSQFGIDSGKIHSGNIGGHCLWSKIPLQSLYASWQKSPNMDLGQRVDTVSLVEMQPCFIKLKSMSEEKCVSIQVPSNPLTSSSPQQVQVTISAEEVGSTEKSPYSSFSYNDISSSSLLQIIRLRTGNVVFNYRYYNNKLQKTEVTEDFSCPFCLVKCASFKGLRYHLPSTHDLLNFEFWVTEEFQAVNVSLKTETMISKVNEDDVDPKQQTFFFSSKKFRRRRQKSQVRSSRQGPHLGLGCEVLDKTDDAHSVRSEKSRIPPGKHYERIGGAESGQRVPPGTSPADVQSCGDPDYVQSIAGSTMLQFAKTRKISIERSDLRNRSLLQKRQFFHSHRAQPMALEQVLSDRDSEDEVDDDVADFEDRRMLDDFVDVTKDEKQMMHMWNSFVRKQRVLADGHIPWACEAFSRLHGPIMVRTPHLIWCWRVFMVKLWNHGLLDARTMNNCNTFLEQLQI", "text": "FUNCTION: Polycomb group (PcG) protein. Involved in flowering processes by repressing unknown target genes and preventing reproductive development. Participates in polycomb group (PcG) protein complex- mediated (probably in complex with EMF1) silencing of the flower homeotic genes AGAMOUS (AG), PISTILLATA (PI), and APETALA3 (AP3), as well as of some regulatory genes such as ABSCISIC ACID INSENSITIVE3 (ABI3), LONG VEGETATIVE PHASE1 (LOV1), and FLOWERING LOCUS C (FLC) during vegetative development, by mediating trimethylation of histone 3 lysine 27 on the AG chromatin (H3K27me3). PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family."}
{"protein": "MSPLWWGFLLSCLGCKILPGAQGQFPRVCMTVDSLVNKECCPRLGAESANVCGSQQGRGQCTEVRADTRPWSGPYILRNQDDRELWPRKFFHRTCKCTGNFAGYNCGDCKFGWTGPNCERKKPPVIRQNIHSLSPQEREQFLGALDLAKKRVHPDYVITTQHWLGLLGPNGTQPQFANCSVYDFFVWLHYYSVRDTLLGPGRPYRAIDFSHQGPAFVTWHRYHLLCLERDLQRLIGNESFALPYWNFATGRNECDVCTDQLFGAARPDDPTLISRNSRFSSWETVCDSLDDYNHLVTLCNGTYEGLLRRNQMGRNSMKLPTLKDIRDCLSLQKFDNPPFFQNSTFSFRNALEGFDKADGTLDSQVMSLHNLVHSFLNGTNALPHSAANDPIFVVLHSFTDAIFDEWMKRFNPPADAWPQELAPIGHNRMYNMVPFFPPVTNEELFLTSDQLGYSYAIDLPVSVEETPGWPTTLLVVMGTLVALVGLFVLLAFLQYRRLRKGYTPLMETHLSSKRYTEEA", "text": "FUNCTION: Plays a role in melanin biosynthesis (PubMed:33100333). Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2- carboxylic acid (DHICA). SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane protein Melanosome Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. SIMILARITY: Belongs to the tyrosinase family."}
{"protein": "MKDTIVLYPNLGRGHLVSMVELGKLILTHHPSLSITILILTPPTTPSTTTTTLACDSNAQYIATVTATTPSITFHRVPLAALPFNTPFLPPHLLSLELTRHSTQNIAVALQTLAKASNLKAIVIDFMNFNDPKALTENLNNNVPTYFYYTSGASTLALLLYYPTIHPTLIEKKDTDQPLQIQIPGLSTITADDFPNECKDPLSYACQVFLQIAETMMGGAGIIVNTFEAIEEEAIRALSEDATVPPPLFCVGPVISAPYGEEDKGCLSWLNLQPSQSVVLLCFGSMGRFSRAQLKEIAIGLEKSEQRFLWVVRTELGGADDSAEELSLDELLPEGFLERTKEKGMVVRDWAPQAAILSHDSVGGFVTHCGWNSVLEAVCEGVPMVAWPLYAEQKMNRMVMVKEMKVALAVNENKDGFVSSTELGDRVRELMESDKGKEIRQRIFKMKMSAAEAMAEGGTSRASLDKLAKLWKQS", "text": "FUNCTION: Involved in the biosynthesis of isoflavonoids. Specific for UDP-glucose. Can use genistein > daidzein > formononetin > quercetin > kaempferol > 4,2',4',6'-tetrahydroxychalcone > apigenin > aureusidin > esculetin > naringenin as substrates, but not cyanidin, trans-p- coumaric acid, caffeic acid, benzoic acid, m- and p-hydroxybenzoic acids, salicylic acid, salicyl alcohol, and hydroquinone. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MGGLPTLRIEPVPLERKVRPGDDLAELIAESAELEEGDVLAIAHTVVSKAEGALISLDEIEPSPFAKTLAERTGKDPRVVEVILREAESIVRVGPDFIITEVRGGMVCANAGVDESNAPPGYVIVLPEDPDRSARELRRRLRELVGVDVGVIITDTQGRPFREGVVGVAIGASGVPVLADRRGDRDLYGRELKITIVALGDLLASAAELVMGQADEGTPAVIFRGLKPELERFEGPRKARAIIRSPSRDIFR", "text": "FUNCTION: Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8- didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420- 0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives. SIMILARITY: Belongs to the CofE family."}
{"protein": "MKTITTARLPWAAQSFALGICLIALLGCNHAANKSSASRADVKPVTVKLVDSQATMETRSLFAFMQEQRRHSIMFGHQHETTQGLTITRTDGTQSDTFNAVGDFAAVYGWDTLSIVAPKAEGDIVAQVKKAYARGGIITVSSHFDNPKTDTQKGVWPVGTSWDQTPAVVDSLPGGAYNPVLNGYLDQVAEWANNLKDEQGRLIPVIFRLYHENTGSWFWWGDKQSTPEQYKQLFRYSVEYLRDVKGVRNFLYAYSPNNFWDVTEANYLERYPGDEWVDVLGFDTYGPVADNADWFRNVVANAALVARMAEARGKIPVISEIGIRAPDIEAGLYDNQWYRKLISGLKADPDAREIAFLLVWRNAPQGVPGPNGTQVPHYWVPANRPENINNGTLEDFQAFYADEFTAFNRDIEQVYQRPTLIVK", "text": "FUNCTION: Catalyzes the endo hydrolysis of beta-1,4-linked mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall (PubMed:11382747). Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides (PubMed:7848261) (PubMed:8973192). It displays tight specificity for mannose at both the -2 and the -1 subsites (PubMed:19441796). Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan (PubMed:11064195). SIMILARITY: Belongs to the glycosyl hydrolase 26 family."}
{"protein": "MTTTLQQRGSASLWEKFCQWITSTENRIYVGWFGVLMIPTLLTATTCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVIFHFLIGVFCYMGREWELSYRLGMRPWICVAFSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTETESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVVGIWFTALGVSTMAFNLNGFNFNQSILDSQGRVINTWADILNRANLGFEVMHERNAHNFPLDLAAGEQAPVALQAPAING", "text": "FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family."}
{"protein": "MEREGIWHSTLGETWEPNNWLEGQQDSHLSQVGVTHKETFTEMRVCGGNEFERCSSQDSILDTQQSIPMVKRPHNCNSHGEDATQNSELIKTQRMFVGKKIYECNQCSKTFSQSSSLLKHQRIHTGEKPYKCNVCGKHFIERSSLTVHQRIHTGEKPYKCNECGKAFSQSMNLTVHQRTHTGEKPYQCKECGKAFHKNSSLIQHERIHTGEKPYKCNECGKAFTQSMNLTVHQRTHTGEKPYECNECGKAFSQSMHLIVHQRSHTGEKPYECSQCGKAFSKSSTLTLHQRNHTGEKPYKCNKCGKSFSQSTYLIEHQRLHSGVKPFECNECGKAFSKNSSLTQHRRIHTGEKPYECMVCGKHFTGRSSLTVHQVIHTGEKPYECNECGKAFSQSAYLIEHQRIHTGEKPYECDQCGKAFIKNSSLTVHQRTHTGEKPYQCNECGKAFSRSTNLTRHQRTHT", "text": "FUNCTION: Probable transcription factor involved in neuronal differentiation and/or phenotypic maintenance. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MKKLLIASLLFGTTTTVFAAPFVAKDIRVDGVQGDLEQQIRASLPVRAGQRVTDNDVANIVRSLFVSGRFDDVKAHQEGDVLVVSVVAKSIISDVKIKGNSVIPTEALKQNLDANGFKVGDVLIREKLNEFAKSVKEHYASVGRYNATVEPIVNTLPNNRAEILIQINEDDKAKLASLTFKGNESVSSSTLQEQMELQPDSWWKLWGNKFEGAQFEKDLQSIRDYYLNNGYAKAQITKTDVQLNDEKTKVNVTIDVNEGLQYDLRSARIIGNLGGMSAELEPLLSALHLNDTFRRSDIADVENAIKAKLGERGYGSATVNSVPDFDDANKTLAITLVVDAGRRLTVRQLRFEGNTVSADSTLRQEMRQQEGTWYNSQLVELGKIRLDRTGFFETVENRIDPINGSNDEVDVVYKVKERNTGSINFGIGYGTESGISYQASVKQDNFLGTGAAVSIAGTKNDYGTSVNLGYTEPYFTKDGVSLGGNVFFENYDNSKSDTSSNYKRTTYGSNVTLGFPVNENNSYYVGLGHTYNKISNFALEYNRNLYIQSMKFKGNGIKTNDFDFSFGWNYNSLNRGYFPTKGVKASLGGRVTIPGSDNKYYKLSADVQGFYPLDRDHLWVVSAKASAGYANGFGNKRLPFYQTYTAGGIGSLRGFAYGSIGPNAIYAEYGNGSGTGTFKKISSDVIGGNAIATASAELIVPTPFVSDKSQNTVRTSLFVDAASVWNTKWKSDKNGLESDVLKRLPDYGKSSRIRASTGVGFQWQSPIGPLVFSYAKPIKKYENDDVEQFQFSIGGSF", "text": "FUNCTION: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the BamA family."}
{"protein": "MSKLNWNVEGVTESLKAKATALGVDVISQEQVAAIAAELAAETGKDVTARSVGSKLRKEGFEVQKANEVQKSPWTPEQEAELVDFLNAHAGQYTYAEIAAAVAGGQFGAKQVQGKILSLEMTASVKPTEKAAAVRSFTPDEETDFVNQVVAGATIEAIAAHFGRNIKQIRGKALSLLREGRIAAMPVQETSSAKTREDLLEGLDLVNMTVAEIAEKTGKSERGVKSMLSRRGLVAKDYDGAAKRAKLDAKAAAAE", "text": "FUNCTION: Putative transcription factor required for the expression of viral late genes."}
{"protein": "MKPSIAEMLHRGRMLWIILLSTIALGWTTPIPLIEDSEEIDEPCFDPCYCEVKESLFHIHCDSKGFTNISQITEFWSRPFKLYLQRNSMRKLYTNSFLHLNNAVSINLGNNALQDIQTGAFNGLKILKRLYLHENKLDVFRNDTFLGLESLEYLQADYNVIKRIESGAFRNLSKLRVLILNDNLIPMLPTNLFKAVSLTHLDLRGNRLKVLFYRGMLDHIGRSLMELQLEENPWNCTCEIVQLKSWLERIPYTALVGDITCETPFHFHGKDLREIRKTELCPLLSDSEVEASLGIPHSSSSKENAWPTKPSSMLSSVHFTASSVEYKSSNKQPKPTKQPRTPRPPSTSQALYPGPNQPPIAPYQTRPPIPIICPTGCTCNLHINDLGLTVNCKERGFNNISELLPRPLNAKKLYLSSNLIQKIYRSDFWNFSSLDLLHLGNNRISYVQDGAFINLPNLKSLFLNGNDIEKLTPGMFRGLQSLHYLYFEFNVIREIQPAAFSLMPNLKLLFLNNNLLRTLPTDAFAGTSLARLNLRKNYFLYLPVAGVLEHLNAIVQIDLNENPWDCTCDLVPFKQWIETISSVSVVGDVLCRSPENLTHRDVRTIELEVLCPEMLHVAPAGESPAQPGDSHLIGAPTSASPYEFSPPGGPVPLSVLILSLLVLFFSAVFVAAGLFAYVLRRRRKKLPFRSKRQEGVDLTGIQMQCHRLFEDGGGGGGGSGGGGRPTLSSPEKAPPVGHVYEYIPHPVTQMCNNPIYKPREEEEVAVSSAQEAGSAERGGPGTQPPGMGEALLGSEQFAETPKENHSNYRTLLEKEKEWALAVSSSQLNTIVTVNHHHPHHPAVGGVSGVVGGTGGDLAGFRHHEKNGGVVLFPPGGGCGSGSMLLDRERPQPAPCTVGFVDCLYGTVPKLKELHVHPPGMQYPDLQQDARLKETLLFSAGKGFTDHQTQKSDYLELRAKLQTKPDYLEVLEKTTYRF", "text": "FUNCTION: Suppresses neurite outgrowth. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the SLITRK family."}
{"protein": "EDIWKKFELLPTPPLSPSRAALPGDPGELGAVAGDCSLMGFGLTDPLDWASELLLLPGDDIWGASDGDLFGSVLDTTDNSIIIQDCMWSGFSA", "text": "FUNCTION: May function as a transcription factor. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSTRDHVKQSPMPVQEGYPRSSKEFSPPSSRSRKRTWVRNLTMSLLIAAGAATFSKYIFPLGSILGAGSLQPIDPHDYAARADRILSTTPLIDGHNDLPYLIRLETKNKIYDHEKLPFEAGLLSHTDAKKIRQGKLGGQFWSVYVECPADPSAGIDDPSWAVRDTLEQIDVAKRLVDEYPDLLEYCETASCARSAFKKGRVGSFLGIEVHDLGVRYITVTHNCDNAFATAASTVAAGKPDHGLTDFGREFVKEMNRLGMLIDLSHVSHQTMRDVLSVTNAPVIFSHSSSYALSKHLRNVPDDVLRTVTKNGGVVMVTFVPLFLKVNDPASVTIHDAVDHILHVAKVAGWDHVGIGSDFDGTAVVPKGLENVSKYPRLVELLLERGVTDEQARKLVGENLLRVWSKAEDIAYAIQASGQKPNEETWSGRKWTAAADIPMPSMFNDSAERRKQLE", "text": "FUNCTION: Hydrolyzes a wide range of dipeptides. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family."}
{"protein": "MGTSIVNLNQKIELPPIQVLFESLNRENETKPHFEERRLYQPNPSFVPRTNIAVGSPVNPVPVSSPVFFIGPSPQRSIQNHNAIMTQNIRQYPVIYNNNREVISTGERNYIITVGGPPVTSSQPEYEHISTPNFYQEQRLAQPHPVNESMMIGGYTNPQPISISRGKMLSGNISTNSVRGSNNGYSAKEKKHKAHGKRSNLPKATVSILNKWLHEHVNNPYPTVQEKRELLAKTGLTKLQISNWFINARRRKIFSGQNDANNFRRKFSSSTNLAKF", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/CUP9 homeobox family."}
{"protein": "MSLSEQYEEKVRPCIDLIDSLRALGVEKDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLELKMKKSRKADFWHGKIKYEDYEEEIEDPADVEQMIRKAQNEIAGTGMGISDKLISLEVTSSNVPDLTVIDLPGITRVAVKDQPENIGDQSKRLIKKFITKQETINLVVVPCNVDIATTEALKMALEVDPNGERTFGVLTKPDLVDKGSEETVVSIINNEIVYLNKGYIIVRCRGQQEIKDRVSLNETVKRERDFFEDHPHFRTLYDNRKATIPNLAEKLTLELVFHIGRCLPRLEERIQVKLSETQAELDRYGSGTPTEPEQRIYFLTDKITAFIQDVLNLTTGEEVKSMLYMNIFPDLRKQFDLWKNDLDSVGETFNKKIEKEMKAYEEKYRGRELPGFLKYNTFEVIVKGQIKQLEEPAIRRLKEISDLIKREFSQLAHSNFPGFPNILKMAKTKIDNIKQVKESETESILRTQFKMEMMIYTQDKTHHDNLKMLKSKEEGKERQKLGVAHSPSHKLYDHSDSEGIREELTCHLKSYFSIVTKRLADQVPMVIRYMMLQESAAQLQREMIQLIQDRHNIEELLKEDHDIASKRNNLHSCQKRLTEALKYLAKF", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MFHLQGPQLLQMLEKSLRKSLPESLKVYGTVFHMNQGNPFNLKALVDKWPDFKTVVIRPQEQEMADDFDHYTNTYQIYSKDLNNCQESLATSDVINWKQHLQIQSSQSSLNEVVQNLAATKFVKVEHTQCILYVMPETARKLLPSLPETKNLPVGYGAPKAINQEMFKLSSMDPTHAALVNKFWHFGGNERSQRFIERCIRAFPTFCLLGPEGTPASWSLMDQTGEIRMGATLPEYRGHGLISHMLAVHTRALDQLGIPVYNHTDKANKIVQKVSHNLHHIAIPHGWNQWNCEPL", "text": "FUNCTION: Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines. Catalyzes the conjugation of arylacetic acids with glycine but does not have activity towards any alkyl-CoA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the glycine N-acyltransferase family."}
{"protein": "MTIEFSNFSFRYESLDKPTLKNINLRIEKGEKIVIIGPSGSGKSTLGQCLNGLIPHAIKGETSGTLTIYGQDTAPFDMHQYTEQVGTVLQDTDSQFVGLSIGEDIAFALENQLTSNIDMYPLVKATAKMVDLEQMLDRSPHDLSGGQKQRVSLAGILVDDVDILLFDEPLAALDPKTGKKTIEIIDDLHRETGKTIVIIEHRLEDVLHRSVDRIILMESGEIIADTTPDEILASPLLEDYGIREPLYISALKEAGCAIEGDAKPSSLTTLPLEQYKPTVQAWFDGSTAQPPKTPAETLLEVRGLTYSYDGEKNALEDVSFDIKRGEFVSVLGKNGSGKSTITKLIMGVIEADSGSMSMNGQDLNELTIFERSQKVGVVMQNPNHMISHHMIFDEVAFGLRNRGIKEKQIEAKVLEVLELCGLSKYRHWPIEALSYGQKKRVTIASILVLEPELLILDEPTAGQDYRNYTSMLSFIEKLNRELGVTVMIISHDMHLVLEYTTRSIVIADSKLVADAPMTQVFSSPELLDQANLTTTSLFDLATKVGIEDTNGFMQHFINVEKAHRQQKSGEVNQPEKAVA", "text": "FUNCTION: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MTSSISWGLLLLAGLCCLVPSFLAEDAEKTDSSHQDHIMASNLADFAFGLYRVLSHQSNTTNIFLSPLSIATALAMLSLGSKDDTKAQLLQGLHFNLTETSEADIHKGFQHLLKTLNRPDNELQLTTGSSLFVNNSLNLVEKFLEEVKNHYHSEAFFVNFADSEEAKKTINSFVEKATHGKIVDLVKDLEIDTVLALVNYIFFRGKWEKPFDPELTEEADFHVDKSTTVKVPMMNRMGMFDVHYCDTLSSWVLLMDYLGNATAIFILPDEGKMQHLEQTLTKEHIYKFLQNRHTRSANVHLPKLSISGTYNLKKVLSPLGITQVFSNGADLSGITTDVPLKLSKAVHKAVLTLDERGTEAAGTTVLEAVPMSIPPDVCFKNPFVVIICDKHTQSPLFVGKVVNPTQ", "text": "FUNCTION: Inhibitor of serine proteases. Can inhibit elastase, trypsin, chymotrypsin and plasmin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
{"protein": "MEKMSRPLPLNPTFIPPPYGVLRSLLENPLKLPLHHEDAFSKDKDKEKKLDDESNSPTVPQSAFLGPTLWDKTLPYDGDTFQLEYMDLEEFLSENGIPPSPSQHDHSPHPPGLQPASSAAPSVMDLSSRASAPLHPGIPSPNCMQSPIRPGQLLPANRNTPSPIDPDTIQVPVGYEPDPADLALSSIPGQEMFDPRKRKFSEEELKPQPMIKKARKVFIPDDLKDDKYWARRRKNNMAAKRSRDARRLKENQIAIRASFLEKENSALRQEVADLRKELGKCKNILAKYEARHGPL", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. PAR subfamily."}
{"protein": "MSRQAKDDFLRHYTVSDPRTHPKGYTEYKVTAQFISKRDPEDVKEVVVWKRYSDFRKLHGDLAYTHRNLFRRLEEFPAFPRGQVFGRFEASVIEERRKGAEDLLRFTVHIPALNNSPQLKEFFRGGEVTRPSEVSGDLHILPPPLIPTPPPDEPRVQPHETWLPQPLPAERRGLEELEVPADPPPSSPAQEALDLLFNCGSTEEASSSPARGPLTEAELALFDPFSKEEGAGPSPTHIGELAALEAGSGRPDQEPWEPGGQAEEDDEEGEPAPAYLSQATELITQALRDEKAGAYPAALQGYRDGVHILLQGVPGDPSPARREGVKKKAAEYLKRAEEILHLHLS", "text": "FUNCTION: May be involved in several stages of intracellular trafficking. Overexpression of SNX15 disrupts the normal trafficking of proteins from the plasma membrane to recycling endosomes or the TGN (By similarity). SIMILARITY: Belongs to the sorting nexin family."}
{"protein": "MLRKQAGEEDSVVLIDMTSPEAGNGCSYGSTAQASEAGKQQVAPSRVGSSANPPIDFVLVWEEDLRSRENPTQDKTDTHEIWRETFLENLRVAGLKIDQRDVQDEAAAVHYILLSAPWAVLCYYAEDLRLKLPLQELPNQASNWSATLLEWLGIPNILLENVPDTPPEYYSCQFKASKLQWFLGSDNQDTFFTSTKRHQILFEILAKTPYGHQKKGLFGIDQLLAEGVFSAAFPLHDGPFSVVPESSQVLGLTQRQVLFKHWARWGKWRKYQPLDHVRRYFGEKVALYFAWLGFYTGWLLPAAVVGTVVFLAGCFLVFSDVPTQELCHSSDTFDMCPLCSDCSFWLLSSACTLAQAGRLFDHGGTVFFSLFMALWAVLLLEYWKRKNATLAYRWDCSDYEDIEERPRPQFAATAPMTALNPITGEDEPYFPEKNRVRRMLAGSVVLLMMVAVVIMCLVSIILYRAVMAIIVSKSNNAFLSAWASRIASLTGSVVNLVFILILSKVYVILAQVLTRWEMHRTQTAFEDAFTLKVFIFQFVNFYASPVYIAFFKGRFVGYPGNYHTLFGVRNEECPAGGCLSELAQELLVIMVGKQIINNVQEVLVPKLKGCWQKLCSRRKKAGMGANPAPWEADYELLPCEGLFHEYLEMVLQFGFVTIFVAACPLAPLFALLNNWVEIRLDARKFVCEYRRPVAERAQDIGIWFHILAGLTHLAVISNAFLLAFSSDFLPRVYYSWTRAPDLRGFLNFTLARAPPTFTSAHNRTCRYRAFRDDDGHYSPTYWTLLAIRLAFVIVFEHVVFSTGRFLDLLVPDIPESVEIKVKREYYLAKQALADNEALLGATGVKGEQPPSSEPSLGLPA", "text": "FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity (By similarity). May play a role in cell-cell interactions (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum Note=Concentrates at sites of cell-cell contact. Shows an intracellular localization. SIMILARITY: Belongs to the anoctamin family."}
{"protein": "MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLYAVKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSVGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPLSCSLSQGLQALLTPVLANILEADQEKCWGFDQFFAETSDVLHRMVIHVFSLQHMTAHKIYIHSYNTAAVFHELVYKQTKIVSSNQELIYEGRRLVLELGRLAQHFPKTTEENPIFVTSREQLNTVGLRYEKISLPKIHPRYDLDGDASMAKAVTGVVCYACRTASTLLLYQELMRKGVRWLVELVKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKVNLEAAELGEISDIHTKLLRLSSSQGTIESSLQDISSRLSPGGLLADTWAHQEGTHPRDRNVEKLQVLLNCITEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMSHFSEECVRKYEAFKDKSEEWMRKMLHLRKQLLSLTNQCFDIEEEVSKYQDYTNELQETLPQKMLAASGGVKHAMAPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL", "text": "FUNCTION: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:15210742, PubMed:15661922). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (By similarity). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB (By similarity). In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli (By similarity). Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1- containing-complexes (By similarity). Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (By similarity). Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus (By similarity). Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (By similarity). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (By similarity). Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes (By similarity). Phosphorylates and activates AKT1 (By similarity). Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity (PubMed:23396211). SUBCELLULAR LOCATION: Cytoplasm Note=Upon mitogen stimulation or triggering of the immune system, TBK1 is recruited to the exocyst by EXOC2. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily."}
{"protein": "MASSASSLHFLSLTPQTLLLPKPTSQTTSLSFFSLPPSSLNLSLSSPSSCFSSRFVRKVTLPDFDQIEDVEDGDEGVEEERNFSPDLKIFVGNLLFSADSAALAELFERAGNVEMVEVIYDKLTGRSRGFGFVTMSSKEEVEAACQQFNGYELDGRALRVNSGPPPEKRENSSFRENSSFRGGSRGGGSFDSSNRVYVGNLAWGVDQDALETLFSEQGKVVDAKVVYDRDSGRSRGFGFVTYSSAEEVNNAIESLDGVDLNGRAIRVSPAEARPPRRQF", "text": "FUNCTION: Could be involved in splicing and/or processing of chloroplast RNA's. SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MVLASRTTALAQRRKAARATGMSRPAFMTIIMAILALLTLSAFMSPASSAGGMGVAAAADKRSEYGTVIGIDLGTTYSCVGAQVNGRVEIITNDQGNRITPSYVAFTPWGESDLKKDAKHLPFKLVEKNGKPAIQVTVNGEKKVFTPEEVSAMVLQKMKETAEAYLGHKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKKDGESQIIVYDLGGGTFDVSLLSIDSGVFEVLATAGDTHLGGEDFDNRVSEYILKQFKKKTGLDASSNKRSVGKLKREVERAKRTLSSQMSTKIEIDGFFEGNDLDETLTRAKFEELNMDLFRKTMKPVEQVLKDAGVKKDEIDDVVLVGGSTRIPKVQAMLKEYFGREPSKGINPDEAVAWGAAVQGGVLAGDESLGDVVLIDVNPLTLGIETNGGVMTKLIPRNTVVPTKKSQIFSTAADNQNTVLIQVFEGERSMTKDNNLLGKFELTGIPPAPRGTPQIEVTFELDANGIMKVSAADKGTGKSESITISNDKGRLTPEEIERMVAEAEEFAEQDEAVRKRIEALNNLQNFIASLRSQLSDKEGLGGKLDKEDKETIKQSLKDAEAWLDENSQTAEGSDIEEQLSELQAAVAPITAKIYQGGAAAGGDDEPLNYGHDEL", "text": "FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (By similarity). Is required for secretory polypeptide translocation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "GVPINVPCTGSPQCIKPCKDAGMRFGKCMNRKCHCTPK", "text": "FUNCTION: Potent inhibitor of shaker potassium channels as well as the mammalian homologs of shaker. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 03 subfamily."}
{"protein": "MNSKVFAALLLLALSTCVLSEKYCPTPRNTSCKKMNIRNNCCRDSDCTSNAFCCAEPCGNFCHKASDKPGGRRVDPNASCQTGYVYW", "text": "FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom protein 11 family. 01 (wap-1) subfamily."}
{"protein": "MIEVLMIEDDIELAEFLSEFLLQHGIHVTNYDEPYTGISAANTQNYDLLLLDLTLPNLDGLEVCRRISKQKHIPIIISSARSDVEDKIKALDYGADDYLPKPYDPKELLARIQSLLRRSHKKEEVSEPGDANIFRVDKDSREVYMHEKKLDLTRAEYEILSLLISKKGYVFSRESIAIESESINPESSNKSIDVIIGRLRSKIEKNPKQPQYIISVRGIGYKLEY", "text": "FUNCTION: Member of the two-component regulatory system ArsS/ArsR that regulates genes involved in biofilm formation and acid adaptation by acting on major ammonia-producing pathways (PubMed:22865848, PubMed:25997502, PubMed:27432830). Upon phosphorylation by ArsS, functions as a transcription regulator by direct binding to promoter regions of target genes including ureA, amiE and amiF to positively regulate their expression in response to acidic pH (PubMed:11751811, PubMed:16672598). Negatively autoregulates its expression (PubMed:11751811)."}
{"protein": "MDGHSNFTQPSDTSHASHTIPSSSSSQRRRLTKKPPPSTSARHHHSSLSIDSRVDAQSLVGKRSSTSLRRAPSAPPARTPTSTHASNSSSPRNPSSSTRLNNHSPIIPAASEFAASSLSPSARDRDSDPARNDHGHQLQNNNNYYYSAFTNAHHHNQYSAASHRRSNSYGHPHGPQSSNSLTFNHSEDFIGAPFDGSAILNRIEATKASPTLGSGAFPHISNPIPVGAAAPAQYSRGSPALEQSFTFPSAAMSEKSQQVRGMEAQLPTSKRYSDETKEPKPGVLRKKSGFSGFMSGLVGTPKKPLISAPENPVHVTHVGYDSATGQFTGLPKEWQRLISESGITEKERRENPETLVNVIKFYKETTEKPAEDQVLEKFHDARPGLPSAPSAGSMISPGLAPHHYNPMSPMISPPASPRFPQVGHEGNFENPRSPPPVPKNKDVTLMPSRPAPRPPVSLPTRTAPHAPYAAKDSGIDMPPQHDDLTPTTYQPPKESQPILPEEHRSRSNSRVNGNTAYPASQQSPAVQAAYQQQLMQQQQEQALAQAQASMSGSMSRAPSKRQPQAQQPTPPQSQHQYSRPTDANGAQQTQRPQQPQIGPVPQSRPRHRSRQSNGLDVVAALKRICSEGDPREIYRSFTKIGQGASGGVYTGHERGSNRLVAIKQMNLEQQPKKDLIINEILVMKDSSHPNIVNFIDSYLCGGELWVVMEFMEGGSLTDVVTFNIMTEGQIASVCRETLLGLQHLHSKGVIHRDIKSDNILLSMEGNIKLTDFGFCATINEAQNKRTTMVGTPYWMAPEVVTRKEYGRKVDIWSLGIMAIEMIEGEPPYLTESPLRALWLIATNGTPQIKDEGNMSPVFRDFLYFALKVDPDKRASAHDLLRHEFMNLCVDLSHLSPLVRAAREARAQEKARKGQ", "text": "FUNCTION: MAP4K component of the MAPK pathway required for the mating pheromone response and the regulation of cell polarity and cell cycle. Phosphorylates histone H2B to form H2BS10ph (By similarity). Is involved in conidiation, aerial hyphal growth and infection-related morphogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MADPKYADLPGIARNEPDVYETSDLPEDDQAEFEAELEELTSTSVEHLIINPNAAFEKFKDKRLGTDGVDFSDRISKSRTTGYESGEYEILGEGLGAKETPQQRYQRLQHEVQELIRDVEQIQSAVKESAAEEELTPMALARQLEGLKQQLVSCHLQKLLGPTAAIDFADPEGALAKRLQQQLEVPSVKKAAPAKSPPKAPGPTTDALTFELFWRRPEQDQFSQTAKIAELEKRLAQLEAMVRCEPDSQNPLLVGAEGTSLVETVQILQAKVNILDAAVLDQVEARLQRRPGSKVNEIAKHKAIVQDADTQSKIHQVVYEMMQRWDHMASSLPDVVQRLLTLRDLHEQASRFVQVLVHLDTTQQEVDVVQRLLAEVQKTMKENLAVVEDNFAEVEARIKRLQ", "text": "FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (By similarity). Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Membrane; Peripheral membrane protein Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the dynactin subunit 2 family."}
{"protein": "MLVSSSFASSIDSVMSHETMSLRRNPPFIDTPEKMPNPTASPNGTIHHLIDPSLPLLSSTTSSSRSTLSSTLNSPPPPPLTTSYSSYNSSACQSITSSPTDNTALAHNSKCYFPHSLSPTPLSSNSSSHVILPPISSFTNLITVAEREFNGRSNSLHANFTSPVPRTVLDHHRHELTFCNPNNTTGFKTITPSPPTQHQSILPTAVDNVPRSKSVSSLPVSGFPPLIVKQQQQQQLNSSSSASALPSIHSPLTNEHTSRYSSSLKDSAKITKQRKKKECPICHNFYANLSTHKSTHLTPEDRPHKCPICQRGFARNNDLIRHKKRHWKDEFMQIYARESDNNSGADDQDDTARTSANNDSDDSNDKLAASSSSEETKLLKKNQLKSLYKIKGAFKCPYNSTLINLDMEVYPHKSRSLYFEPINCHQTGVFSRCDTFKNHLKALHFEYPPKTKKEDRGVVPGKCKHCGLQFPNVDVWLNKHVGKGCGYSYH", "text": "SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Nucleus."}
{"protein": "MASLYVGDLPQDVNESGLFDKFSSAGPVLSIRVCRDVITRRSLGYAYVNFQQPADAERALDTMNFDLVRNKPIRIMWSQRDPSLRRSGVGNVFIKNLDRAIDNKAIYDTFSAFGNILSCKVATDEKGNSKGYGFVHFETEEAANTSIDKVNGMLLNGKKVYVGKFIPRKEREKELGEKAKLFTNVYVKNFTEDFDDEKLKEFFEPYGKITSYKVMSKEDGKSKGFGFVAFETTEAAEAAVQALNGKDMGEGKSLYVARAQKKAERQQELKRKFEELKQKRHESVFGVNLYVKNLDDTIDDDRLRIAFSPYGNITSAKVMTDEEGRSKGFGFVCFNAASEATCAVTELNGRVVGSKPLYVALAQRKEERKAHLASQYMRHMTGMRMQQLGQIYQPNAASGFFVPTLPSNQRFFGSQVATQMRNTPRWVPQVRPPAAIQGVQAGAAAAGGFQGTAGAVPTQFRSAAAGARGAQPQVQGTHAAAAAANNMRNTGARAITGQQTAAPNMQIPGAQIAGGAQQRTSNYKYTSNMRNPPVPQLHQTQPIPQQLQGKNSEKLIASLLANAKPQEQKQILGERLYPMIEHMHANLAGKITGMLLEIENSELLHMIEDQEALKAKVEEAVAVLQVHRVTEPAN", "text": "FUNCTION: Binds the poly(A) tail of mRNA (PubMed:2125288). Since it interacts with the cap-associating translation initiation factor eIF4G, it is likely that it functions by linking Atx2 to the cap-binding complex (PubMed:28388438). Forms a complex with tyf and Atx2 which functions in adult circadian pacemaker neurons to sustain circadian rhythms likely by switching between activator and repressor modes of post-transcriptional regulation via interaction with Lsm12a or me31B, respectively (PubMed:28388438). The activator complex (Atx2-tyf activator complex) activates the TYF-dependent translation of per to maintain 24 hour periodicity in circadian locomotor behaviors, whereas the repressor complex (Atx2-Not1 repressor complex) promotes Not1- dependent post-transcriptional gene silencing and supports high- amplitude circadian rhythms in a per-independent manner (PubMed:28388438). In 0-1 hour embryos, forms a ribonucleoprotein complex (RNP) with me31B, eIF4E1, tral and cup which binds to various mRNAs including maternal mRNAs, and down-regulates their expression during the maternal-to-zygotic transition (PubMed:28875934). SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family."}
{"protein": "MTINTDDQYGDAESKTTISSSRRYSSSSYQDQSMDDALNTTLTNDKATLIQVWKPKSYGSVKGQIPQCERLTYTWKEIDVFGEAPTDGKPREPLCTRLRNCCTRQRKDFNPRKHLLKNVTGVAKSGELLAVMGSSGAGKTTLLNALAFRSPPGVKISPNAVRALNGVPVNAEQLRARCAYVQQDDLFIPSLTTREHLLFQAMLRMGRDVPASVKQHRVQEVLQELSLVKCADTIIGAPGRIKGLSGGERKRLAFASETLTDPHLLLCDEPTSGLDSFMAHSVLQVLKGMAMKGKTIILTIHQPSSELYCLFDKILLVAEGRVAFLGSPYQSAEFFSQLGIPCPPNYNPADFYVQMLAIAPAKEAECRDMIKKICDSFAVSPIAREVLETASVAGKGMDEPYMLQQVEGVGSTGYRSSWWTQFYCILWRSWLSVLKDPMLVKVRLLQTAMVATLIGSIYFGQVLDQDGVMNINGSLFLFLTNMTFQNVFAVINVFSAELPVFLREKRSRLYRVDTYFLGKTIAELPLFIAVPFVFTSITYPMIGLRTGATHYLTTLFIVTLVANVSTSFGYLISCASSSISMALSVGPPVVIPFLIFGGFFLNSASVPAYFKYLSYLSWFRYANEALLINQWSTVVDGEIACTRANVTCPRSEIILETFNFRVEDFALDIACLFALIVLFRLGALLCLWLRSRSKE", "text": "FUNCTION: May be part of a membrane-spanning permease system necessary for the transport of pigment precursors into pigment cells responsible for eye color. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily."}
{"protein": "MARVKRGVIARKRHKKILKLAKGYYGARSRVFRVAKQAVIKAGQYAYRDRRQKKRQFRALWIARINAGARVNGLSYSRFIAGLKKASIEIDRKVLADLAVNEKAAFAAIVEKAKATLA", "text": "FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity). SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
{"protein": "MLVILAFIIVFHIVSTALLFISTIDNAWWVGDSFSADLWRVCTNSTNCTEINELTGPEAFEGYSVMQAVQATMILSTILSCISFLIFLLQLFRLKQGERFVLTSIIQLMSCLCVMIGASIYTDRRQDLHQQNRKLYYLLQEGSYGYSFILAWVAFAFTFISGLMYMILRKRK", "text": "FUNCTION: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (PubMed:31550239). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (PubMed:17609206, PubMed:14978215). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (PubMed:14978215). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity (PubMed:12763482). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (PubMed:12189152). Also regulates many processes through PTK2. Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation (By similarity). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A- dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (PubMed:16487956, PubMed:16216233). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (PubMed:28295343). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (PubMed:30773261). May play a role in glomerular filtration (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cell membrane Apical cell membrane Membrane raft Cytoplasm Nucleus Cytoplasm, perinuclear region Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney (By similarity). Localizes to the apical cell surface in the luminal epithelium and glandular epithelium (PubMed:16487956). Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane (PubMed:12189152) (PubMed:14978215). SIMILARITY: Belongs to the PMP-22/EMP/MP20 family."}
{"protein": "MKRPAYMSEVPVNHTSGQEARCVYLTFDDGPNPFCTPQILDVLAEHRVPATFFAIGSYVKDHPELIRRLVAEGHDVANHTMTHPDLATCDPKDVKREIDEAHQAIVSACPQALVRHLRAPYGVWTEDVLSASVRAGLGAVHWSADPRDWSCPGVDVIVDEVLAAARPGAIVLLHDGCPPDEVEQCSLAGLRDQTLIALSRIIPALHSRGFEIRSLP", "text": "FUNCTION: Is involved in generating a small heat-stable compound (Nod), an acylated oligomer of N-acetylglucosamine, that stimulates mitosis in various plant protoplasts. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the polysaccharide deacetylase family."}
{"protein": "MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL", "text": "FUNCTION: Unknown for isoform 4. Csen is involved in calcium-dependent transcriptional repression, regulation of potassium channels, and perhaps in processing of PSEN2 and apoptosis."}
{"protein": "MLSKQIPLGIYEKALPAGECWLERLQLAKTLGFDFVEMSVDETDDRLSRLDWSREQRLALVNAIVETGVRVPSMCLSAHRRFPLGSEDDAVRAQGLEIMRKAIQFAQDVGIRVIQLAGYDVYYQEANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMNSISKALGYTHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGIGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFETLKQSGYCGPYLIEMWSETAEDPAAEVAKARDWVKARMAKAGMVEAA", "text": "FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to L- ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization. SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase family."}
{"protein": "MKPRRSMLFIPGANAAMLSTSFVYGADAVMFDLEDAVSLREKDTARLLVYQALQHPLYQDIETVVRINPLNTPFGLADLEAVVRAGVDMVRLPKTDSKEDIHELEAHVERIERECGREVGSTKLMAAIESALGVVNAVEIARASPRLAAIALAAFDYVMDMGTSRGDGTELFYARCAVLHAARVAGIAAYDVVWSDINNEEGFLAEANLAKNLGFNGKSLVNPRQIELLHQVYAPTRKEVDHALEVIAAAEEAETRGLGVVSLNGKMIDGPIIDHARKVVALSASGIRD", "text": "FUNCTION: Represents a citryl-ACP lyase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase beta subunit subfamily."}
{"protein": "MSITITYRIETPGSIEAMADKIASDQSTGTFVPVPGETEELKSRVAARVLGIRQLEDAKRPTWPEVAEGHGPLRRADVDIAFPLDAIGTDLSALMTIAIGGVFSIKGMTGIRIVDMKLPNAFRGAHPGPQFGVAGSKRLTGVEGRPIIGTIVKPALGLRPVETAELVGELINSGVDFIKDDEKLMSPAYSPLKERVAAIMPRILDHEQKTGKKVMYAFGISHADPDEMMRNHDLVLEAGGNCAVVNINSIGFGGMSFLRKRSGLVLHAHRNGWDVLTRDPGAGMDFKVYQQFWRLLGVDQFQINGIRVKYWEPDESFIESFKAVSTPLFDPSDCPLPVAGSGQWGGQAPETYQRTGRTTDLLYLCGGGIVSHPSGPAAGVRAVQQAWEAAVADIPLANYAKDHPELAASIAKFSDGKGA", "text": "FUNCTION: Involved in catabolism of D-apiose. Catalyzes the decarboxylation of 3-oxo-isoapionate 4-phosphate to L-erythrulose 1- phosphate. SIMILARITY: Belongs to the RuBisCO large chain family."}
{"protein": "MSSCPAIVNMKDDDGIGAMGAAVAFAAMGVFGIYFLWPVVGPTSAGMMMKAPGAAGWVICRAVFEANPQLYFTILRTAGAAAAAATFAACSIAS", "text": "FUNCTION: Involved in short-range signaling required for pollen tube attraction by the female gametophyte. Required for female fertility. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein."}
{"protein": "MRLAASIAVALPVIGAASAQGFPPPVMGVTVVKSKYDENVKITYKENDICETTEGVRSFTGHVHLPPDNDYFGVYQNYSINTFFWFFEAREDPKNAPLSIWLNGGPGSSSMIGLFQENGPCWINDDSKSTTNNSFSWNNRVNMLYIDQPNQVGFSYDELTNITYSTINDTISVADFSSGVPAQNLSTLVGTGSSQKPWATANNTVNAARSIWHFAQVWFQEFPEHKPNNNKISIWTESYGGRYGPSFASYFQEQNEKIKNHTITKEGEMHILNLDTLGVINGCIDLMFQAESYAEFPYNNTYGITAYTKEKRDAIIRDIHRPDGCFDKLAKCREAAKEGDPHFYSNNATVNAICAEANSDCDKYLMEPFQEANLGYYDIAHPLQDPFPPPFFKGFLSQSSVLSDMGSPVNFSHYSQAVGKSFHGVGDYARPDVRGFTGDIAYLLESGVKVALVYGDRDYICNWLGGEQVSLGLNYTGTEAFRKAGYADVKVNSSYVGGLVRQHGNFSFTRVFEAGHEVPGYQPETSLKIFERIMFNKDIATGELDIAQKQDYGTTGTESTFQVKNEIPPSPEPTCYLLSADGTCTPEQLNAIENGTAVVENYIIKSPAASKGNPPPTTTSSPTASPTAGSAMLKAPVAMLAISALTVLAFYL", "text": "FUNCTION: Extracellular serine carboxypeptidase that contributes to pathogenicity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the peptidase S10 family."}
{"protein": "MKVSVLAAVAAFAAATAIAGPVRPAGVGNDKYLIELAPGKTQWVTKNEKHQMKAAGQTFIDITDEFGTGFTASQPVSANYPKNSRHSSIVAPIIANLSKENLMRDLKAMIEFNNRYYESQTGVESATWLMEQVQKAIDASGIQGAKVEKFENQFQQFSIIATIPGSESTVVIGAHQDSINEQDPEGGRAPGADDNGSGSVVVLEALRGVLGSKALQAANNTNTMEFHWYAGEEGGLLGSNAIFKKYKSDGRQIKAMLNQDLAGFVKKGGPEQFGLITDNTNQELNQFCKMIVKKYASIPIVDTKCGYACSDHASADRSGFPASMVAETAFRDSNPHIHSADDVTDYLDFDHMLEHAKVAVGFMTELAMASNL", "text": "FUNCTION: Probable extracellular aminopeptidase which contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily."}
{"protein": "MSESELRQRQAEFTKELHGEGAESRTGLTALLSKNRNAQREAVSKYLRHWDGKTDKEAEDRRLEDYNEATHSYYNVVTDFYEYGWGSSFHFSRFYKGENFQAAMARHEQYLAYMAGIKKGDLVLDVGCGVGGPARTIARFTGCNIIGLNNNDYQIQKAKYYAKKYNLQDHMDFVKGDFMNMEFEPNSFDKVYAIEATCHAPKLEGVYGEIYKVLKPGGTFAVYEWVMTENYDENNEEHRKIAYEIELGDGIPKMFTVDVAKQALKNVGFEVEVSKDLADEDDEIPWYYPLTGEWKYVQSLSDIATFFRTSYFGRKFTNCMVSIMEKVGVAPQGSVEVTAALENAAVGLVEGGRKKLFTPMFLFVAKKPEDAK", "text": "FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family."}
{"protein": "MAISPRDEQNRSVDLWFAYKVPKLTKDADSDSASGYEYVYYDRQVGAVQKSPNLMNDPKGALFYTLDSVFGDPGDTTGWILYNDEMPADANRSNNATLGHTKGVIAFDIASSSALWLLHSWPKYASPSVPGVPTPLYGQTFLCLSLDLATAGKLAAQMALHQQPQVYLPRTGGLDHTSPLYALTQPLNASAPGDSDSLDFKTRGGVPFKVIAKNRKWGKDFWNDLVGPTLKADMYVETWIRGKIPPVLDSDGVHKTYDIKFIDLRKLGAPWAWPETQDHAKWGITTTDNWVCVGDINRMVTQEKRGGGTIAFQDPKLWKALCETDLIIPPPGKTDAQARAMIRKTHEPAE", "text": "SIMILARITY: Belongs to the DNase II family."}
{"protein": "MDLMDMDAINDLHFSGHSSLTNTPTSDEDYGCTWNHWSPIVNWDTFTGAPDDFHHLMDTIIEDRTTVLEQLSPSITTTTTTTTTTDEEEEEMETTTTTTTTAIKTHEVGDDSKGLKLVHLLMAGAEALTGSTKNRDLARVILIRLKELVSQHANGSNMERLAAHFTEALHGLLEGAGGAHNNHHHHNNNKHYLTTNGPHDNQNDTLAAFQLLQDMSPYVKFGHFTANQAIIEAVAHERRVHVIDYDIMEGVQWASLIQSLASNNNGPHLRITALSRTGTGRRSIATVQETGRRLTSFAASLGQPFSFHHCRLDSDETFRPSALKLVRGEALVFNCMLNLPHLSYRAPESVASFLNGAKTLNPKLVTLVEEEVGSVIGGFVERFMDSLHHYSAVFDSLEAGFPMQNRARTLVERVFFGPRIAGSLGRIYRTGGEEERRSWGEWLGEVGFRGVPVSFANHCQAKLLLGLFNDGYRVEEVGVGSNKLVLDWKSRRLLSASLWTCSSSDSDL", "text": "FUNCTION: Transcriptional regulator essential for Nod-factor-induced gene expression (PubMed:15961668). Acts downstream of calcium spiking and DMI3, a calcium/calmodulin-dependent protein kinase (CCaMK) (PubMed:15961668). Transcription factor involved in the control of strigolactone biosynthesis in roots through the activation of the beta- carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones (PubMed:22039214, PubMed:26503135). SUBCELLULAR LOCATION: Nucleus membrane Endoplasmic reticulum Note=Mainly localized to the nuclear envelope. Also found in the endoplasmic reticulum. Upon Nod-factor application, the nuclear envelope localization disappears and the protein accumulates in the nucleus. SIMILARITY: Belongs to the GRAS family."}
{"protein": "MAEERQDALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEEEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGERRRHSGQDVHVVLKLWKTGFSLDNGDLRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLNTSSPAQQAENEAKASSSILINEAEPTTNIQIRLADGGRLVQKFNHSHRISDIRLFIVDARPAMAATSFVLMTTFPNKELADENQTLKEANLLNAVIVQRLT", "text": "FUNCTION: Reduces the ATPase activity of VCP (PubMed:9824302, PubMed:9214505). Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis (PubMed:12411482). May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (PubMed:10930451). Inhibits the activity of CTSL (in vitro) (By similarity). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase (By similarity). Also, regulates spindle orientation during mitosis (By similarity). SUBCELLULAR LOCATION: Nucleus Golgi apparatus, Golgi stack Chromosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Predominantly nuclear in interphase cells (PubMed:12810701). Bound to the axial elements of sex chromosomes in pachytene spermatocytes (PubMed:1495983). A small proportion of the protein is cytoplasmic, associated with Golgi stacks (PubMed:12810701). Localizes to centrosome during mitotic prophase and metaphase (PubMed:23649807). SIMILARITY: Belongs to the NSFL1C family."}
{"protein": "MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLCAIHAKRVTIQKKDIQLARRLRGERS", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H3 family."}
{"protein": "MKTLLLTLVVVTIVCLDLGYTMQCKTCSFYTCPNSETCPDGKNICVKRSWTAVRGDGPKREIRRECAATCPPSKLGLTVFCCTTDNCNH", "text": "FUNCTION: Exhibits M2 muscarinic acetylcholine receptor (CHRM2)- blocking activity, but has a weak binding activity toward nicotinic AChR. Moreover, it inhibits collagen-induced platelet aggregation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Orphan group V sub-subfamily."}
{"protein": "MLQSMGDGEISISPYDTAWVALVEDDGGGRRQPQFPSSLEWISSNQLADGSWGDAGTFSIFDRILNTLACVVALRSWNIHPHKTDKGIWFMKKNMCRIDEENLEHMPIGFEVALPSLIDIAKKLEIDIPTQTRGLQEIYARREIKLKKIPRDIMHQVPTTLLHSLEGMAGLKWEKLLKLQSQDGSFLFSPSSTAFALQQTRDHGCLKYLTNHIHKFNGGVPNVYPVDLFEHLWAVDRLQRLGLSRYFQPEIEECIAYVHRQWTEKGICWARNSQVEDIDDTAMGFRLLRLHGYEVSADVFRHFKSDGGEFFCFKGQSTQAVTGMYNLYRASQLMFPGENILVDAARFSANFLQLKRANNDLLDKWIITKDLPGEVGYALDVPWYASLPRVETRFYLDQYGGDDDVWIGKTLYRMPYVNNNKYLELAKLDYNNCQALHQQEWQNIQKWYRSCSLGEFGMTERSLLQTYYVAAASVFEPEKSQERLAWAKTAILMETISSHFEFQQLSRDQKRAFITEFEHDSILKYTNGGRYKRRSSLVGTLVRTLNHLSLDILLAHGRDIHQPLKNAWCKWLNSWEEGGDAELLLRTLNLMSGGGRRRRWASEELLSSNPKHEQLLKATIGVCDKLRLFQRRKVQGGNGCMNATGITTVEIESEMRELVKLVVTRSSSEDLDSEIKQNFLTIARSFYYAAYCNQGTINFHIAKVLFEKVL", "text": "FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones (PubMed:22284743). Catalyzes the conversion of (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP) (PubMed:22284743). SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily."}
{"protein": "MAPPSITKTATQQDVISTVDIGNSPLLSISLDQSRNFLVNGHPFLTQVPPNITTTTTSTPSPFLDFKSNKDTIANNNNTLQQQGCFVGFNTTEAKSHHVVPLGKLKGIKFTSIFRFKVWWTTHWVGTNGHELQHETQILILDKNISLGRPYVLLLPILENSFRTSLQPGLNDYVDMSVESGSTHVTGSTFKACLYLHLSNDPYRLVKEAVKVIQTKLGTFKTLEEKTPPSIIEKFGWCTWDAFYLKVHPKGVWEGVKALTDGGCPPGFVIIDDGWQSISHDDDDPVTERDGMNRTSAGEQMPCRLIKYEENYKFREYENGDNGGKKGLVGFVRDLKEEFRSVESVYVWHALCGYWGGVRPKVCGMPEAKVVVPKLSPGVKMTMEDLAVDKIVENGVGLVPPNLAQEMFDGIHSHLESAGIDGVKVDVIHLLELLSEEYGGRVELAKAYYKALTSSVNKHFKGNGVIASMEHCNDFFLLGTEAISLGRVGDDFWCCDPSGDPNGTYWLQGCHMVHCAYNSLWMGNFIHPDWDMFQSTHPCAEFHAASRAISGGPVYVSDCVGNHNFKLLKSFVLPDGSILRCQHYALPTRDCLFEDPLHNGKTMLKIWNLNKYAGVLGLFNCQGGGWCPETRRNKSASEFSHAVTCYASPEDIEWCNGKTPMDIKGVDVFAVYFFKEKKLSLMKCSDRLEVSLEPFSFELMTVSPLKVFSKRLIQFAPIGLVNMLNSGGAVQSLEFDDSASLVKIGVRGCGELSVFASEKPVCCKIDGVSVEFDYEDKMVRVQILWPGSSTLSLVEFLF", "text": "FUNCTION: Transglycosidase operating by a ping-pong reaction mechanism. Involved in the synthesis of raffinose, a major soluble carbohydrate in seeds, roots and tubers. Able to utilize D-ononitol and D-pinitol as acceptors. May also act as a glycoside hydrolase. SIMILARITY: Belongs to the glycosyl hydrolases 36 family."}
{"protein": "MAEFVRAQIFGTTFEITSRYSDLQPVGMGAFGLVCSAKDNLTGSNVAVKKIMKPFSTPVLSKRTYRELKLLKHLKHENVISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDVWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIHTIASENTLRFVQSLPKRERQPLASKFTQADPLAIDLLEKMLVFDPRARIKAAEGLAHEYLSPYHDPTDEPAAEERFDWSFNDADLPVDTWKIMMYSEILDYHNVINDAQNLTESQ", "text": "FUNCTION: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity). Involved in vegetative and pathogenic development like conidia formation, sclerotial development, and in penetration into unwounded plant tissue. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily."}
{"protein": "MGLVGWGLLLGCLGCGILLRARAQFPRVCMTLDGVLNKECCPPLGPEATNICGFLEGRGQCAEVQTDTRPWSGPYILRNQDDREQWPRKFFNRTCKCTGNFAGYNCGGCKFGWTGPDCNRKKPAILRRNIHSLTAQEREQFLGALDLAKKSIHPDYVITTQHWLGLLGPNGTQPQIANCSVYDFFVWLHYYSVRDTLLGPGRPYKAIDFSHQGPAFVTWHRYHLLWLERELQRLTGNESFALPYWNFATGKNECDVCTDELLGAARQDDPTLISRNSRFSTWEIVCDSLDDYNRRVTLCNGTYEGLLRRNKVGRNNEKLPTLKNVQDCLSLQKFDSPPFFQNSTFSFRNALEGFDKADGTLDSQVMNLHNLAHSFLNGTNALPHSAANDPVFVVLHSFTDAIFDEWLKRNNPSTDAWPQELAPIGHNRMYNMVPFFPPVTNEELFLTAEQLGYNYAVDLSEEEAPVWSTTLSVVIGILGAFVLLLGLLAFLQYRRLRKGYAPLMETGLSSKRYTEEA", "text": "FUNCTION: Plays a role in melanin biosynthesis (PubMed:33100333). Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2- carboxylic acid (DHICA) (PubMed:1537333, PubMed:1537334). SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane protein Melanosome Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. SIMILARITY: Belongs to the tyrosinase family."}
{"protein": "MAIPKKLRLFTLYVDGTNHIGKIPSVTLPKVTRKTEDYQGGGMQGAVAVDLGLDGGALDASMVVGGVVEELILKYGGDIDEMRLRFVGEIYSGGTSSLMEVEMRGRITEIDPGEAKQGDDTNHTYAIKNTYYKLSVDDKALLEIDLLNFIYKRDGKNLYPDRIVSALGLGG", "text": "FUNCTION: Forms the virus tail tube. SUBCELLULAR LOCATION: Virion."}
{"protein": "MADEDGEGIHPSAPHRNGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNGVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPTYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFEVINHSFVRKLAPNEFPHKLYVQNYTSAVPGTCLTIRKWLFTTEEEVLLNDNDLAVTYFFHQAVDDVKKGYIKAEEKSYQLQKLHEQRKMVMYLNMLRTCEGYNEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIAFEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHECFERVFCELKWRKENIFQMARSQQRDVAT", "text": "FUNCTION: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C- terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes. SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein Cytoplasm, cytosol Note=Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3- kinase products (By similarity)."}
{"protein": "MMKCVVLVILGLTLLLGTQAMPSSRLSCYRKLLKDRNCHNLPEGRADLKLIDENVQHHFWEGKGCEMICYCNFSELLCCPKDVFFGPKISFVIPCNSH", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SCRG1 family."}
{"protein": "MVKEKYTRFERARIVGARALQIAMGAPVLVDDDGRLDPLGVAIAELKAEIIPITVKRKKS", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family."}
{"protein": "MDGDISTGKMASPACAMAPLDSMEVLDLLFDGQDGILRNVDLAESWILTREEQKVLPNSDSDEFLNSILGPGDSDPSSPIWSPADSDSGISEDLPSDSQDTPPGSGPGSANVAARCHPSKQGEGPCPSYLPSTACPEPPRTQVHESSVAIDLDMWSTDTLYPEEQAGSPSRFNLTVKELLLSGGGGDLQQHPLAASQLLGPGSGHCQELVLTEDEKKLLAKEGVTLPTQLPLTKYEERVLKKIRRKIRNKQSAQESRKKKKEYIDGLENRMSACTAQNQELQRKVLHLEKQNLSLLEQLKHLQALVVQSTSKPAHAGTCIAVLLLSFVLIILPSISPFTANKVDSPGDFIPVRVFSRTLHNHAASRVAPDVTPGPEVPGPHKGSSGGLSADWGNFLEIPMLDDPTEELDNTTLVLANSTEDLGRATLLDWVASEPLLGQMGLEIPGEEIWLSWVPRWLRVRVVQDALGVL", "text": "FUNCTION: Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. Binds the cAMP response element (CRE). Activates transcription through box-B element and CRE. Seems to function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes (By similarity). May be involved in growth suppression. Regulates FGF21 transcription (By similarity). Plays a crucial role in the regulation of triglyceride metabolism and is required for the maintenance of normal plasma triglyceride concentrations (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 3]: Nucleus Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. SIMILARITY: Belongs to the bZIP family. ATF subfamily."}
{"protein": "MSSKRVTWLSLTWVLVFLCLSVELEAQLQVGFYRTSCGLAEFIVKDEVRKGFIRDSGVAPGLVRMHFHDCFVRGCDGSVLIDSTPSNTAEKDSPANNPSLRGFEVIDSAKARLEAVCKGVVSCADIVAFAARDSVEITGGLGYDVPAGRRDGRISLASEASTNLPPPTFTVDQLTQFFSNKGLTQDEMVTLSGAHTIGRSHCSSFSNRLYNFNGTSGQDPTLDPQYAASLKTQCPQGSTNTNLVVPMNPSSPSITDVGYYVDVLRNRGLFTSDQTLLTDTTTATQVRQNAGNPFLWKNKFASAMVKMGQLGVLIGEAGQIRANCRVINS", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MKFNFKLILIILIINQILIINCKENKILEIYKSGNICPYPLHYRERTGSDDHDFDLGFVYARNDSNCLLPCPSPIYTSQEVNTLSLMIKITGTISFIASLILLLIYSPLINRMGYNRHTIGIFFLTFSVFLIMLTDIIYVHHGNDLICPQSHRYSRQNDSGCTITGILFQYGCIAAVLFWATLSLDLYLTLKKISTKKVEKWYLIILTLIALILTFVPLVKKSYGYLVTGLACWILDSTDQIIFFWAPFTAILGIGSILIVLVVYEIYKISKITKQNRGIFQSHIRPLLMVLFIFGQFLFILAFNALINNKYDEYSARMDSYIDCLFSSSSYSYLCRLKTFPFEMEFIVLFFLRLIGIEVLIFYGFTQQTKKILLHSFLVNNIFFKKYFIRLDGASLDFSTVDEELKVVNFSCNNNNNNNNSNSNSNSNLNNNLNNNLNNNNLNNNNNLNNLNNLNINNNLKNSQNNLNNSQQNEPLSSQKLSENGNVNVFMVESFDNNNSMINQFKHLEEKNNIILNSIISPVQEEQYEEDEINNKNINNNSNNDENN", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family."}
{"protein": "MANVDDVHTKPIPAFYCCYLLRSTVRQTSLYIGSTPHPSRRLAQHNGVSRGGARKTANDKRPWEMVLIVEGFMSRTAALQFDTIYTTWAWQKPGKSRHLGDDDNTESAREKGKTRPRGPARSLKGHLENLHALLRSTYFSGLPLRVRFFADDVHQLWRVWSDRIDGFIPEHIKVIPDGSCFENRQPGIEYLRVGSVEHIQVDYSKIHSYLEKTTFQLDDPEDLQCKVCQAPVVPKEELVLVCPQTRCYCVSHLLCLSARFLDSTKDRGRLIPISGKCPGCHKTIQWSLMMQELSFRTRGAKELQAILRKKKRGDCRVKDVPEKDTDDVGTVTAECCDFPESVGGSIEGPGDASDESTHDDVRLDDDWYESLGIESDHEIADWSESHPAMPTRVEIVIEDSDCDNTG", "text": "FUNCTION: Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX1 family."}
{"protein": "MDTLAPESTRQNLRSQRLNLLTNEPHQRLESLVKSKEPFASRDNFARFVAAQYLFQHDLEPLYRNEALARLFPGLASRARDDAARADLADLGHPVPEGDQSVREADLSLAEALGWLFVSEGSKLGAAFLFKKAAALELDENFGARHLAEPEGGRAQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLERTFA", "text": "FUNCTION: Involved in heme degradation. Catalyzes the degradation of heme to biliverdin, with the release of iron. Forms biliverdin delta (70%) and beta (30%). SIMILARITY: Belongs to the heme oxygenase family."}
{"protein": "MSAQVSLELHHRISQFLFHEASLLDDWKFRDWLAQLDEEIRYTMRTTVNAQTRDRRKGVQPPTTWIFNDTKDQLERRIARLETGMAWAEEPPSRTRHLISNCQVSETDIPNVFAVRVNYLLYRAQKERDETFYVGTRFDKVRRLEYDNWRLLERDIVLDQAVITSHNLSVLF", "text": "FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family."}
{"protein": "MASPGSGFWSFGSEDGSGDPENSGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGGSQPPRTTSRKATCACNQKPCNCPKAEVNYAFLHATDLLPACDGERPTLAFLQDVMDILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMLIARFKMFPEVKEKGMAAVPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHIDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWYVPPSLRVLDNNEERMSRLSKVAPVIKARMMESGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL", "text": "FUNCTION: Catalyzes the production of GABA. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasmic vesicle Presynaptic cell membrane; Lipid- anchor Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Note=Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Golgi membranes and presynaptic clusters (By similarity). SIMILARITY: Belongs to the group II decarboxylase family."}
{"protein": "MQYSHHCEHLLERLNKQREAGFLCDCTIVIGEFQFKAHRNVLASFSEYFGAIYRSTSENNVFLDQSQVKADGFQKLLEFIYTGTLNLDSWNVKEIHQAADYLKVEEVVTKCKIKMEDFAFIANPSSTEISSITGNIELNQQTCLLTLRDYNNREKSEVSTDLIQANPKQGALAKKSSQTKKKKKAFNSPKTGQNKTVQYPSDILENASVDLFLDANKLPTPVVEQVAQINDNSELELTSVVENTFPAQDIVHTVTVKRKRGKSQPNCALKEHSMSNIASIKSPYEAENSGEELDQRYSKAKPMCNTRGKVFSEASSLRRHMRIHKGVKPYVCHLCGKAFTQCNQLKTHVRTHTGEKPYKCELCDKGFAQKCQLVFHSRMHHGEEKPYKCDVCNLQFATSSNLKIHARKHSGEKPYVCDRCGQRFAQASTLTYHVRRHTGEKPYVCDTCGKAFAVSSSLITHSRKHTGERPFICELCGNSYTDIKNLKKHKTKVHSGADKTPDSSAEDHTLSEQDSIQKSPLSETMDVKPSDTTLPLALPLGTEDHHMLLPVTDTQSPTSDTLLRSTVNGYSEPQLIFLQQLY", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MPREYAPAHRKRKSHDISDDADAAAAPGAGAGPRKKILLPKKEHKYPSVNELKKRIRDVKRLLNKADLPADARIVQERALSGYEKELEDELKRRDRSKMIKKYHFVRFLDRKTATKDVNRLVRREKEVSSAGPDAMDTKTKEKKLASLAEKLRVARVNLNYTIYYPLDEKYIALYAEQKKKVKGDGAEDGGDGADSDGDARFGMVHATVADKPAMWHVVEKCMKDGTLDMLRDGKLESGAKAGEKDRKKEERSQRAGDKAKKSQERGVSSSQAGKSRDRSRKVDDRKRSRGPAEDHVMRDAGNDDGDESDGGFFEM", "text": "FUNCTION: Involved in rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the EFG1 family."}
{"protein": "MSRRSPKLELKLNLSPPTSSQRRMVRSPSRSATTSPTSPPSSCVSSEMNQDEPSVRYSTSPETTSMVLVGCPRCLMYVMLSEDDPKCPKCKSTVLLDFLHENATNANANAAAASSGRKTRRN", "text": "FUNCTION: Acts as negative regulator of root hair development redundantly with GIR2 (PubMed:28526410). GIR1 and GIR2 may function as adapter proteins that associate with GL2 and participate in the control of root hair formation (PubMed:28526410). GIR1 and GIR2 may function as adapter proteins that associate with TPL and participate in the repression of root gene expression (PubMed:28526412). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLRINQRLLVRSLRDAQYQYLKSTALRFLSSSTQSNVETTPRRSGRLFELNKEYTGKLAQPDGKANIESLYNEFKNDLDKISEFSNGRQGMAPKYGRSRSLSFINRLFQSITNAKNTSSLDPYVVLEQLSKYNLIGPAQYEMILRYYLLVKDAPKDVISLWVKYLEQFTTSNENLMAYTTIAYLKLPDMNEPDCSMLQQILQTERFHTDIPFGRIISIVEQNEVLKRDQELSNRFAYLLNLYATQNKTWFINQLDICYTESRLRSFYNIYSAQRDINNCDIEIITKFMEQFNKLNANSSFPMQVFNEYKDKLSDADGFKLKLGLLDIVSKYPAPSKIQKLQRLLAVWNSYLKPEFGKVGIDASLAYASLIKALNTSGNIEELQNIWEKEIPTEYKNNQVVFEAFLLAIIRRTKITYSQIQNRIDATKFGKLKSVDLAEAIALKIFNENPNDSKVFDDFYQQNSLDSFGSNTSILALKTYGDYIYKTKTDDETYVIANDVRSKVLKLKPQISTQSWKQEVNLILEKFIDIAPSIIPVRVLFEQRGIYQLNFTLQKKILFSEFRKPDGDVQNAEKIFEELMKTDNNKVSQPMRINSPQLMGTMIKGLCQVIGRTHDVSLYPELSKYLEMLPGLEVHMSINWMEQVLRTIRMVFRSGSTKTIPKELLEFSEFIIEKLPAIDPDFNYQFRNDDIAMFKKIGAKSFSKLKSTST", "text": "FUNCTION: May be involved in the control of meiotic sister-chromatid recombination. SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MSEAPQARRVGSVDDHSVYDDAKTYYTSEERHNNSRSGPRQRTYSQNSLLGQMERLGLKEPFRRGSHDESNHNRRFLIQVDPTLESLKSQEDTDGNMQITIEDNGPKVLTLRTAGSNGHNRFDIRGTYMLSNLLQELTLAQEYGRKQVILDEARLNENPVNRLSRLIRDHFWDALTRRIDASSIEVAAKDPKDWTDDPRPRIYVPKGAPEQLEYYKKLAADKPDIRLDVVELPETITPEYVVGINKAPGLLAVDMEETVDPKTGERVMSGRPFVVPGGRFNELYGWDSYMESLGLLVNDKVYLAKSMVLNFCFCIKHYGKILNATRSYYLCRSQPPFLTDMALRVYDKIRHEPDATEFLRTAILAAIKEYHSVWVAEPRLDPVTGLSRYRPEGTGVPPETEADHFLHILEPYYKKHNMTFKEFVEAYNFGRIREPELDKYFLHDRAVRESGHDTSYRLEGVCADLATVDLNTLLFKYETDIARTIRNVFGDKLVIPAEYCVGSLQPGQVETSAIWDRRSKRRKLAIDKYLWNEEAGMYFDYDTAKRQQCNYESCTTFWALWAGVASPKQAAIMVTRALPKFEAYGGLLSGTEESRGQIGLDRPNRQWDYPYGWAPQQMLAWTGLYRYSFTEEAERLAYKWLFMITKAFSDFNGVVVEKYDVTRPVDPHRVDAEYGNQGLGFKGVAKEGFGWVNASYIYGLQIINAHMRRALGTLTPYDTFIKALEDNRNRALSEMV", "text": "FUNCTION: Hydrolyzes intracellular trehalose to glucose (By similarity). Plays a role in pathogenicity, specifically in proliferation of invasive hyphae in rice blast disease (PubMed:12514128). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 37 family."}
{"protein": "MGRSPCCDENGLKKGPWTPEEDQKLIDYIHKHGHGSWRALPKLADLNRCGKSCRLRWTNYLRPDIKRGKFSAEEEQTILHLHSILGNKWSAIATHLQGRTDNEIKNFWNTHLKKKLIQMGIDPVTHQPRTDLFASLPQLIALANLKDLIEQTSQFSSMQGEAAQLANLQYLQRMFNSSASLTNNNGNNFSPSSILDIDQHHAMNLLNSMVSWNKDQNPAFDPVLELEANDQNQDLFPLGFIIDQPTQPLQQQKYHLNNSPSELPSQGDPLLDHVPFSLQTPLNSEDHFIDNLVKHPTDHEHEHDDNPSSWVLPSLIDNNPKTVTSSLPHNNPADASSSSSYGGCEAASFYWPDICFDESLMNVIS", "text": "FUNCTION: Transcription factor that acts as negative regulator of lateral root (LR) development. Required for normal auxin responses during LR development. May be part of a negative feedback loop stimulated specifically in the endodermis upon LR initiation to ensure that LRs are formed only in the correct place. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQANYPAADSSLYTNPKGSTISAFDGGSDSSSDSEPDEPQSRKKLRMEAS", "text": "FUNCTION: Transcription regulator. Forms a sequence-specific DNA- binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MAX family."}
{"protein": "MNSVTVSHAPYTITYHDDWEPVMNQLVEFYNEVASWLLRDETSPIPDKFFIQLKQPLRNKRVCVCGIDPYPKDGTGVPFESPNFTKKSIKEIASSISRLTGVIDYKGYNLNIIDGVIPWNYYLSCKLGETKSHAIYWDKISKLLLHHITKHVSVLYCLGKTDFSNIRAKLESPVTTIVGYHPAARDRQFEKDRSFEIINVLLELDNKAPINWAQGFIY", "text": "FUNCTION: Plays an essential role in viral replication as a component of the DNA polymerase processivity factor. Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family."}
{"protein": "MDIDPYKEFGASVELLSFLPSDFFPSIRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMNLATWVGSNLEDPASRELVVSYVNVNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSESPRRRRSQSRESQC", "text": "FUNCTION: Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions. SUBCELLULAR LOCATION: Virion Host cytoplasm. SIMILARITY: Belongs to the orthohepadnavirus core antigen family."}
{"protein": "MKFLPTTKEEMKNLGWDSIDVLLISGDTYLDTSYNGSVLVGKWLVEHGFKVGIIAQPEVDVPDDITRLGEPNLFFAVSGGCVDSMVANYTATKKRRQQDDFTPGGVNNKRPDRAVLVYSNMIRRFFKGTTKKIVISGIESSLRRITHYDYWTNKLRKPILFDAKADILSYGMGEMSMLQLANALKNGEDWKNIKGLCYLSKEMKQDYLSLPSHSECLADKDNFIEAFHTFYLNCDPITAKGLCQKCDDRYLIQNPPSESYSEEIMDKIYSMEFARDVHPYYKKMGAVRALDTIKYSVTTHRGCYGECNFCAIAIHQGRTIMSRSQSSIVEEVKNIAGTPKFHGNISDVGGPTANMYGLECKKKLKLGACPDRRCLYPKKCLHLQVNHNNQVELLKKLKKIPNIKKIFIASGIRYDMILDDNKCGQMYLKEIIKDHISGQMKIAPEHTEDKILGLMGKDGKSCLNEFKNQFYKINNELGKKQFLTYYLIAAHPGCKDKDMMDLKRYASQELRVNPEQVQIFTPTPSTYSTLMYYTEKDPFTNQKLFVEKDNGKKQKQKDIVTEKRKNRK", "text": "SIMILARITY: Belongs to the UPF0313 family."}
{"protein": "MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDFEGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPRTTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQMMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVKDDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVKSKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDCGPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANSVTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGLNFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYEGENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFHIMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIAILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGLEGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPMLMGPPPKTGLFCSLVKRTRNRSKE", "text": "FUNCTION: [Isoform 2]: Does not associate with membranes but has a diacylglycerol kinase activity. FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:11719522). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Has a higher activity with long-chain diacylglycerols like 1,2-di-(9Z-octadecenoyl)-sn-glycerol compared to 1,2-didecanoyl-sn-glycerol (By similarity). Specifically expressed in brain, it regulates neuron-specific morphological changes including neurite branching and neurite spine formation (By similarity). SUBCELLULAR LOCATION: Postsynaptic cell membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein Cytoplasm Note=Translocation to the plasma membrane is induced by phorbol esters. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family."}
{"protein": "MTTSYAKIEITGTLTVLTGLQIGAGDGFSAIGAVDKPVVRDPLSRLPMIPGTSLKGKVRTLLSRQYGADTETFYRKPNEDHAHIRRLFGDTEEYMTGRLVFRDTKLTNKDDLEARGAKTLTEVKFENAINRVTAKANLRQMERVIPGSEFAFSLVYEVSFGTPGEEQKASLPSSDEIIEDFNAIARGLKLLELDYLGGSGTRGYGQVKFSNLKARAAVGALDGSLLEKLNHELAAV", "text": "FUNCTION: This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals. FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities (Probable). This CRISPR-Cas system protects bacteria against transformation with plasmids containing DNA homologous to its spacer regions (PubMed:29979631). SIMILARITY: Belongs to the CRISPR-associated Csm3 family."}
{"protein": "MDEYEAQLLVVEQALLVTTDEQQREELSALRTNLEELLALTRSSETEATNNISTAQTNGDLDDELKRFQSELNDLKEQEQEETDTTDDKQQLEELRAKYNALLGEKCSAPHEHSWGALSYHNALICGVDDELIIDGNGILDVRLRVLFTNPTHREMLPCNYYLEGECRFDEIRCRFSHGALVPGASIKEYNAPDFHKLARNCPVLAKLQDRLWHRGRVLCVNFVEQQCRVRLDGQEHKERERDFPFEELFPLIADEDDELSSDSSESHSTEDSDAANDSDMDDLEAARQARMVELSLFTFKPTEKLGAWEQYTRGIGSKLMANMGYIHGTGLGSDGRGIVTPVSAQILPQGRSLDACMELREAANGDKNYFSVERKLKRAQRRQQAANEKAYARESKRTDVFAFLNGSVLGQAQNSTKTTKTSNLQQHSNKTLNVETVRIADDIRRKQRDIAKVQQSLARNATDAQLQKRLNGQLRAHQQELATLQAQESSLSKEQQTRKSKNKMFAF", "text": "FUNCTION: Transcription repressor. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTTGNNDFYYSNKYEDDEFEYRHVHVTKDVSKLIPKNRLMSETEWRSLGIQQSPGWMHYMIHGPERHVLLFRRPLAATQKTGGNVRSGNAVGVR", "text": "FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function (By similarity). Has a role in the exit from M phase during early mitotic cell division. More specifically, thought to act by degrading B-type cyclins that causes breakdown of nuclear envelope and exit mitosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CKS family."}
{"protein": "MKLFLYHTPELTPTDKAPECAIAVDVLRATSTIATVLASGGEAVQVFSDLDRLIEVSEKWPHEKRLRAGERGGAKVAGFELGNSPLDCTPELVQGRRLFISTTNGTRALQRVQDSPNVLAAALINRAAVVQFLLDKQPETVWIVGSGWEGSFSLEDTVCAGAIAHSIWQQTQLSPEEIAGNDEVISAIALYSQWQDNLLGLLHQASHGQRLLRLDCHEDLKYCSQTDILDVLPIQHETGVLKSQKK", "text": "SIMILARITY: Belongs to the ComB family."}
{"protein": "MAAAAPPAGPGLYSDIGKKARDLLYRDYHTDQKFTLTTYAANGAAITVAGTKKNESIFSEIQSQVKNNNVSVDVKATSDSKLITTFTVHDLGTPGLKGILSIPFPYQKSAKAEVQYLHPHAGLNAIVGLNANPLVSFSGVFGTGAFAVGTDVAFDTATGDFTKYNAGLSHTTPDLTAALLLNNKGDSLAASYYHKVSKTSAVGAELAHSFSSNENTLTFGTQHALDELTTVKARFNNFGMASALIQHEFRPKSLVTISTEVDTKAIDKSSKVGLSLVLKP", "text": "FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane. SIMILARITY: Belongs to the eukaryotic mitochondrial porin (TC 1.B.8.1) family."}
{"protein": "MSVRVSGKHMEIGDSFRVRIGEQIEQAVTKYFDGGYSSQVTVEKSGSRFSADCKLHLDTGVVLQANGQANEPQSAFDAASERIEKRLRRYKRKLKDHHNGNGQNSTEVAYRVMDSVPFEDEEVPDDYAPTIVAETTKQLRTMSVANAVMALDMTDEPVLMFRSPGKDDLNIVYRRNDGNIGWIDAANIKA", "text": "FUNCTION: Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family. Long HPF subfamily."}
{"protein": "MIIKVQKTFEKRLINAFMRKGNYIKAEKIYLKVVNRLSTIGIKNSYQFIRETLLKMTPIMGVVKKKRGVKELIYPKYLEPEMGEKLAIKWLKKTVAKFKGELLIENIVEEFVKASKDQGEVVKEKWALYKEVRYAISCNTRKGHHKSFVEQKLKATQRRKWY", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S-like rRNA where it nucleates assembly of the head domain of the small subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MPRKNYIYNLKPFFNPSKNERKKSTFICYAMKKVSEIDVARSHLNRALLPIDPKTGNVLPRFRRLNKHRACAMRAIVPAMLYYFNINSKLVEASIEKLADECGLSTLSDSGNKSITRASRLISEFLEPMGFVKCKKINSKSMSNYIPKKIFLTPMFFMLCGISPSEINHFLSKKIKPLKKLKKQEKSAFISFTDMKIISQLDERSARTKILNALINYYTASELTKIGPKGLKKKIDIEYSNLCNLYKKKS", "text": "FUNCTION: This protein is essential for plasmid replication; it is involved in copy control functions. SIMILARITY: Belongs to the IncFII RepA family."}
{"protein": "MLSNPLHRFSGYHAMPSNTLMSNGHMSQGHLHNNGLDGLGQSSHYALQQLQQHVGVHNPHLARAAPHMKHHRQHPYGPAVRTAGIAGPIRRRISRACDQCNQLRTKCDGNHPCAHCIEFGLGCEYIRERKKRGKASRKDLAQQAAAQAATTGSSSGQKSPTHSANTTKKDDQKVDGGSSTGNAPNSEQHSPDDKDLDNDAMQRSQRMGSMDSLDEMDHQGHISGHHHQQAALDREHHTMSNPSALDPNSYGGVHNGYERQGGMGTATSHIMGGAAHGGYGSQGGMSSYPELPYLQTQSPTGYSGGGASYRIGTSPLSAYPLSGETASPGWGLPIPSPPASHGQYHSQHMQQQSSASYGAGTSGGLASGHPQHLRYPVLDPLVPHLGNIIPLSLACDLIDLYFASSSSAQVHPMSPYVLGFVLRKRSFLHPSKPRLCQPALLASILWVAAQTSDAPFLTSVPSARGKICQKLLELTVSLLKPLIHTPSGDVSPVSSPVIDGAALGGLGVAMPGSISMEALSGETGAFGAAGTLDDVVTYIHLATVVSASEYKGASLRWWNAAWSLARELKLGRELPQNAPSAMSDTAGNERNDNDDTTEALGGGPNVITDEEREERRRIWWLVYIVDRHLALCYNRPLFLLDIECDGLLQPLDDTAYQNGEFRPHQVVTDPDMLGEDRRSSQKSETALIRGPSFECTGHGIFGYFLPLMTILGEIVDLNHARNHPRFGINFRSHSEWDEQTSEIARHLELYEQSLRRFEQQHLSAAAQAQAQAADAAKAAAAAQAQAHAQAQAQQTSSDDSAISADNISVTDVGTPSALSVHSVAHSAHTTSSSRLTESDVQTRIVLAYGTHVMNVLHILLTGKWDPINLLDDNDLWISSQGFITATGHAVDAAEAIGSILEFDPGLEFMPFFFGIYLLQGSFLLLLIADKLQSEASPSVVKACETIIRAHEACVVTLNTEYQRNFSKVMRSALAQVRGRVPEDLGEQHQRRRELLALYRWTGDGTGLAL", "text": "FUNCTION: Transcriptional activator of the pentose catabolic pathway (PCP). Involved in the induction of a variety of PCP enzymes during growth on D-xylose. Has no effect on cellulolytic and xylanolytic enzyme activities. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the xlnR/xlr1 family."}
{"protein": "ENEDPFYYDYETVRNGGLIFAALAFIVGLVIILSKRFRCGAKKKHRQIPEDGL", "text": "FUNCTION: May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase. SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the FXYD family."}
{"protein": "MSRYRGPRFKKIRRLGALPGLTNKRPRAGSDLRNQSRSGKRSQYRIRLEEKQKLRFHYGITERQLLKYVRIARKAKGSTGQVLLQLLEMRLDNILFRLGMAPTIPGARQLVNHRHILVNGRIVDIPSYRCKPQDTIMARDEQKSIALIQNSLDLSPREELPKHLTLNPFPYKGLVNQIIDSKWVGLKINELLVVEYYSRQT", "text": "FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
{"protein": "MGSSGLLSLLVLFILLVNVQGPGLTDWLFPRRCPTIREECEFRERDVCTRHRQCPDNKKCCVFSCGKKCLDLKQDVCEMPNETGPCLAFFIRWWYDKKNNTCSTFVHGGCQGNNNNFQSEANCLNTCKNKRFP", "text": "FUNCTION: Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility (By similarity). SUBCELLULAR LOCATION: Secreted Note=Bound to the surface of testicular and on the head and tail of ejaculate spermatozoa."}
{"protein": "MSNETNCTLDFEQSVELFKEYNLFITAFLLFLTIILQYGYATRSKFIYILKMIVLWCFWPLNIAVGVISCIYPPNTGGLVAAIILTVFACLSFVGYWIQSIRLFKRCRSWWSFNPESNAVGSILLTNGQQCNFAIESVPMVLSPIIKNGVLYCEGQWLAKCEPDHLPKDIFVCTPDRRNIYRMVQKYTGDQSGNKKRFATFVYAKQSVDTGELESVATGGSSLYT", "text": "FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Host Golgi apparatus membrane; Multi-pass membrane protein Note=Largely embedded in the lipid bilayer. SIMILARITY: Belongs to the gammacoronaviruses M protein family."}
{"protein": "MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK", "text": "FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta- catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development (PubMed:16826533). Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:30026314). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes (By similarity). Required for normal neural stem cell proliferation in the hippocampus dentate gyrus (By similarity). Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation (By similarity). Promotes formation of synapses via its interaction with FZD5 (By similarity). FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta- catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self- renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5 (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
{"protein": "MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS", "text": "FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:26387735). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
{"protein": "MGHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGGAIKHLDDLKGTFAQLSELHCDKLHVDPENFRLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTAVASALSSRYH", "text": "FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination with alpha chains. SIMILARITY: Belongs to the globin family."}
{"protein": "MTIKAPTLNVPGLGVDPLTQRIKEKEKKWKYKIAVLSGKGGVGKSTVAVNLTAALAKMGYFVGILDADIHGPNVAKMFGIGNTDIYAEKFEDGHFEMIPPTVDFMGQVTPIKVMSMGMMVPEDQPIIWRGSLVTKAIKQLLGDVMWGELDFMIIDFPPGTGDEILTVVQSIQLDAAIVVTTPQEVALLDTGKAVNMMKKMEVPYIAVIENMSYLICPHCGNKIDIFGEGGGEKLAEKEGVDFLGKVPIDLKAREASDLGIPIVLYGDTPAAKAFMEIAEKLVNKLKEIKGDGREK", "text": "FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family."}
{"protein": "ILLDEHIRLLGIDPYSIDGYSRECFSHLAVASTVARGGADLAIGSEKMGLQVKNIDFIPLQKERYELVIKKEDMNKPFFKVLMDIINSNNFKMELEGLGGYDLSETGKIVTEL", "text": "SIMILARITY: To M.jannaschii MJ0886 C-terminal region."}
{"protein": "MSWSGPLRGLNTSLTCGPALVPRLWATCSMATLNQMHRLGGPPKRPPQKLGPTEGRPQLKGVVLCTFTRKPKKPNSANRKCCRVRLSTGQEAVCFIPGEGHTLQEHQIVLVEGGRTQDLPGVKLTVVRGKYDCGHVQKK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
{"protein": "MSQPPKVLLLYAHPESQDSVANRVLLRPAQQLEHVTVHDLYAHYPDFFIDIHHEQQLLREHQVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRYPIEDILRPFELTAAMCHMHWLTPMLVYWARRQKPEVLESHATAYGDWLRNPLPHGGR", "text": "FUNCTION: Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. KefG subfamily."}
{"protein": "QKKDKKDRFY", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the tachykinin family."}
{"protein": "MQAVANKPVAELVDYRTEPSKYRHWSLATDGEIATLTLNIDEDGGIRPGYKLKLNSYDLGVDIELHDALQRVRFEHPEVRTVVVTSGKPKIFCSGANIYMLGLSTHAWKVNFCKFTNETRNGIEDSSQYSGLKFLAACNGTTAGGGYELALACDEIVLVDDRNSSVSLPEVPLLGVLPGTGGLTRVTDKRRVRRDHADIFCTISEGVRGQRAKDWRLVDDVVKQQQFAEHIQARAKALAQTSDRPAGAKGVKLTTLERTVDEKGYHYEFVDATIDADGRTVTLTVRAPAAVTAKTAAEIEAQGIKWWPLQMARELDDAILNLRTNHLDVGLWQLRTEGDAQVVLDIDATIDANRDNWFVRETIGMLRRTLARIDVSSRSLYALIEPGSCFAGTLLEIALAADRSYMLDAAEAKNVVGLSAMNFGTFPMVNGLSRIDARFYQEEAPVAAVKAKQGSLLSPAEAMELGLVTAIPDDLDWAEEVRIAIEERAALSPDALTGLEANLRFGPVETMNTRIFGRLSAWQNWIFNRPNAVGENGALKLFGSGKKAQFDWNRV", "text": "FUNCTION: Catalyzes the ring opening of 2,3-epoxy-2,3-dihydroxybenzoyl- CoA to form 3,4-didehydroadipyl-CoA semialdehyde. SIMILARITY: Belongs to the benzoyl-CoA oxygenase component C family."}
{"protein": "APWLVPSQITTCCGYNPGTMCPSCMCTNTC", "text": "FUNCTION: May specifically activate neuronal voltage-gated sodium channels (Nav) at the resting membrane potential. Causes a marked contraction and extension of the caudal and dorsal fins in fish and noticeable spontaneous contractions of isolated frog neuromuscular preparations. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSTLGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ", "text": "FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein A1/A4/E family."}
{"protein": "MAEKENTKRNRREEILQALAQMLESSDGSQRITTAKLAANVGVSEAALYRHFPSKTRMFDSLIEFIEDSLMSRINLILQDEKETFNRLRLILLLVLGFAERNPGLTRIMTGHALMFEQDRLQGRINQLFERIEVQLRQVLREKKLRDGQGFIHDEALLATQLLAFCEGMLSRFVRSEFRYRPTQEFDARWPLIVAQLQ", "text": "FUNCTION: Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the nucleoid occlusion factor SlmA family."}
{"protein": "MLIKDIILTPMSLSAVAGLLPLLFVAFLVLHEPIWLLWYRYAARRHKCSMPRFIEKSFPLGIQRTMDMIKTAKSYTLLEVQYDRVFNKFKARTYLRQAPLQYQIFTIEPENIKTILATKFNDFGLGARFHTVGKVFGQGIFTLSGNGWKQSRSMLRPQFTKDQVCRIDQISSHAAELIKEMNRAMKVDQFIDVQHYFHKLTLDTATEFLFGESCESLNPENQSCIVARDGSEITAEQFVESYNFLLNYAFKRTLSSKVYWLFNSKEFRDHKKRAQSYIDYYVDKALYATSFAAENSIAEKDAAAESSGIYVFSLEMAKVTRDPVTIRDQIFNILIAGRDTTAATLSFAIHFLARNPDVFNKLREEVLDHFGTKEEQRPLSFELLKQAPYLKQVINEVLRLAPVLPLNFRTAVRDTTLPIGGGPEQKDPIFVPKGTAVYYSIYMVHRDIKYWGPDAHEFNPNRWENLKLDNVWAFLPFNGGPRICLGQQFALTELSLTLVRLLQEYSKIEMGPDFPESPRFSTTLTAQHAPPGVVVRFS", "text": "FUNCTION: Catalyzes the first step of sophorolipid biosynthesis. Catalyzes the terminal (at the omega-position) or subterminal (at the omega(-1)-position) hydroxylation of a fatty acid. This converts the fatty acid to a substrate for the subsequent glycosyltransferase reactions (PubMed:23516968, PubMed:24242247). Oleic acid is the preferred substrate, but it acts on various other C-16, C-18 and C-20 saturated and unsaturated fatty acids, namely palmitic, palmitoleic, stearic, linoleic, cis-9,10-epoxystearic, trans-9,10-epoxystearic and arachidonic acid (PubMed:24242247). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MIKIPRGTQDILPEDSKKWRYIENQLDELMTFYNYKEIRTPIFESTDLFARGVGDSTDVVQKEMYTFKDKGDRSITLRPEGTAAVVRSYIEHKMQGNPNQPIKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSVDAEVLAMVMHIYQSFGLKHLKLVINSVGDMASRKEYNEALVKHFEPVIHEFCSDCQSRLHTNPMRILDCKVDRDKEAIKTAPRITDFLNEESKAYYEQVKAYLDDLGIPYIEDPNLVRGLDYYTHTAFELMMDNPNYDGAITTLCGGGRYNGLLELLDGPSETGIGFALSIERLLLALEEEGIELDIEENLDLFIVTMGDQADRYAVKLLNHLRHNGIKADKDYLQRKIKGQMKQADRLGAKFTIVIGDQELENNKIDVKNMTTGESETIELDALVEYFKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family."}
{"protein": "MDPATNSPIMPIDLPIMHDSDRYDFVKDIGSGNFGVARLMTDRVTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRFKEVILTPSHLAIVMEYAAGGELYERICNAGRFSEDEARFFFQQLISGVSYCHAMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEILLRQEYDGKLADVWSCGVTLYVMLVGAYPFEDPQEPRDYRKTIQRILSVTYSIPEDLHLSPECRHLISRIFVADPATRITIPEITSDKWFLKNLPGDLMDENRMGSQFQEPEQPMQSLDTIMQIISEATIPTVRNRCLDDFMADNLDLDDDMDDFDSESEIDVDSSGEIVYAL", "text": "FUNCTION: Together with SRK2I, key component and activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as seed germination, Pro accumulation, root growth inhibition, dormancy and seedling growth, and, to a lesser extent, stomatal closure (PubMed:17307925). In response to ABA, phosphorylates the ESCRT-I complex component FREE1, which is required for ABA-induced FREE1 nuclear import (PubMed:30962512). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MLCLSLNSSSTSPPKLPLHHSFSRRGIRSWVRSPCVQRKKLGFWSSPKAVLSAVSGAGSEAGKVEEAEEYDAIVIGSGIGGLVAATQLAVKGARVLVLEKYVIPGGSSGFFQRDGFTFDVGSSVMFGFSDKGNLNLITQALEAVDCKLRTIPDPTTVHFHLPDNLSIRVHREYDMFISELVNYFPHEKEGIRRFYNECWKIFNSLNSLELKSLEEPMYLFGQFFRKPVECLTLAFYLPQNAGDIARKFIKDPQLLSFIDAECFIVSTVKALHTPMINASMVLCDRHFGGINYPVGGVGGIAKALANGLVNKGSKLLYKANVTKILLKDGKAVGVKLSNGREFFAKTVISNATRWDTFGKLLKVEDIPQEEKNFKKIYLKAPSFLSIHMGVKAFVLPPDTDCHHFILEDNWGRLELPYGSIFLSIPTVLDPSLAPEGHHIFHIFTTSSIENWEGLSHKEYEEKKELVADEIITRLEKKLFPGLKDSVVLKEVGTPKTHRRFLARDSGTYGPMPRKVPKGLLGMPFNTTAINGLYCVGDSCFPGQGVIAVAFSGVMCAHRVAADLGFEKKAPVLDAALLRLLGWLRTVA", "text": "FUNCTION: Carotene cis-trans-isomerase that converts 7,9,9'-tri-cis- neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene (also known as prolycopene) into all-trans-lycopene. Isomerization requires redox-active components, suggesting that isomerization is achieved by a reversible redox reaction acting at specific double bonds. Isomerizes adjacent cis-double bonds at C7 and C9 pairwise into the trans-configuration, but is incapable of isomerizing single cis- double bonds at C9 and C9' (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral membrane protein. SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family. CrtISO subfamily."}
{"protein": "MHKTHSTMSGKSMKVIGVLALQGAFLEHTNHLKRCLAENDYGIKIEIKTVKTPEDLAQCDALIIPGGESTSMSLIAQRTGLYPCLYEFVHNPEKVVWGTCAGLIFLSAQLENESALVKTLGVLKVDVRRNAFGRQAQSFTQKCDFSNFIPGCDNFPATFIRAPVIERILDPIAVKSLYELPVNGKDVVVAATQNHNILVTSFHPELADSDTRFHDWFIRQFVSN", "text": "FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform. SIMILARITY: Belongs to the glutaminase PdxT/SNO family."}
{"protein": "MECLRSLPCLLPRAMRLPRRTLCALALDVTSVGPPVAACGRRANLIGRSRAAQLCGPDRLRVAGEVHRFRTSDVSQATLASVAPVFTVTKFDKQGNVTSFERKKTELYQELGLQARDLRFQHVMSITVRNNRIIMRMEYLKAVITPECLLILDYRNLNLEQWLFRELPSQLSGEGQLVTYPLPFEFRAIEALLQYWINTLQGKLSILQPLILETLDALVDPKHSSVDRSKLHILLQNGKSLSELETDIKIFKESILEILDEEELLEELCVSKWSDPQVFEKSSAGIDHAEEMELLLENYYRLADDLSNAARELRVLIDDSQSIIFINLDSHRNVMMRLNLQLTMGTFSLSLFGLMGVAFGMNLESSLEEDHRIFWLITGIMFMGSGLIWRRLLSFLGRQLEAPLPPMMASLPKKTLLADRSMELKNSLRLDGLGSGRSILTNR", "text": "FUNCTION: Magnesium transporter that mediates the influx of magnesium into the mitochondrial matrix (PubMed:11401429, PubMed:18384665). Required for normal expression of the mitochondrial respiratory complex I subunits (PubMed:18384665). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family."}
{"protein": "MKNPMLEAASLLLEKLLLISNFKLFSVSVPGGGTGKNRPYEISSFVRGDVLEVSRTHFIHYGIYLGENRVAHLMPDILLALTNDKERTQKVVSNKRLLLGVICKVASIRVDTVEDFAYGADILVNHLDGTLKKKSLLNEEVARRAEQQLGLTPYSLLWNNCEHFVTYCRYGSRISPQAEKFYDTVKIIIRDQRSSLASAVLGLASIVYTGLASYMTLPAICIPFCLWMMSG", "text": "FUNCTION: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A (PubMed:28758396). LRAT plays a critical role in vision (By similarity). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis- retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (By similarity). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (PubMed:25416279). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Rough endoplasmic reticulum Endosome, multivesicular body Cytoplasm, perinuclear region Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). SIMILARITY: Belongs to the H-rev107 family."}
{"protein": "ATAGPASGKIRAVIGAVVDVQFEQGELPAILNALTIDQGNNQKLVLEVAQHLGENAVRAIAMDGTEGLVRGQTVVDTGAPISVPVGRGTLGRIINVVGEPIDERGPIECKQRNPIHADPPSFVEQSTEAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTRKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDVSVVGQEHYDVATGVQQTLQAYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIEGKLVRLKDTIASFKAVLEGKYDHLPENAFYMVGGIEDVVAKAEKIAAEAN", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27791192). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (By similarity). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MRSLISVAVLSALPTAFSQANTSYTDYNVEANPDLFPLCLQHLNASFPDCASGPLSLTPVCDRSLSPKDRATALVSLFTFDELVNNTGNTGLGVSRLGLPNYQVWGEALHGVGRANFVESGNFSWATSFPMPITMMAALNKTLIHQIGTIVSTQLRAFSNAGLGGVDVYSPNINTFRHPVWGRGQETPGEDAFLTSVYGYEYITALQGGVDPETLKIIATAKHYAGYDIESWNNHSRLGNDMQITQQELSEYYTPPFIVASRDAKVRSVMCSYNAVNGVPSCANKFFLQTLLRDTFEFSEDGYVSGDCGAVYNVWNPHGYASNEAAASADSILAGTDIDCGTSYQWHSEDAFEDSLVSRSDIERGVIRLYSNLVQAGYFDGEDAPYRDITWDDVLSTDAWNIAYEAAVEGIVLLKNDETLPLSKDIKSVAVIGPWANVTEELQGNYFGPAPYLISPLTGFRDSGLDVHYALGTNLTSHSTSGFEEALTAAKQADAIIFAGGIDNTIEAEAMDRENITWPGNQLDLISKLSELGKPLVVLQMGGGQVDSSSLKDNDNVNALIWGGYPGQSGGHALADIITGKRAPAGRLVTTQYPAEYAEVFPAIDMNLRPNETSGNPGQTYMWYTGTPVYEFGHGLFYTTFEESTETTDAGSFNIQTVLTTPHSGYEHAQQKTLLNFTATVKNTGERESDYTALVYVNTTAGPAPYPKKWVVGFDRLGGLEPGDSQTLTVPVTVESVARTDEQGNRVLYPGSYELALNNERSVVVKFELKGEEAVILSWPEDTTSDFVSSIDGGLDRKQDVIA", "text": "FUNCTION: Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 3 family."}
{"protein": "MLRLSLLRSTATLPVKCQRRGLILPAAAMYTLGSLIFGKEARLADAMERGELHNKNVDYAKEAEERTELRIRALANTRPMEPRYNGHVPLHRYEKLLLFAISGWNSFFHPEDGYNIVQLGEATALPVFLENLKQTMLSDSSGRRILKEQPNITTEILHMDKLAKLPHNTLGYVYYQWLKRENVSPDTRAPVKFIDDPMHAYIFKRYRQCHDFYHAITNMPIIIEGEITIKALEGANLGVPMAILGGILAPLRLKKVQRKRLYNIYLPWAVRTGLSCKPLINVYWEEMLEKDVTALRKELKITLPPDLRTMRKERAALRKEIDAKYNSQKRATTPA", "text": "FUNCTION: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of COQ3, COQ4, COQ6, COQ7 and COQ9 polypeptides. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ4 family."}
{"protein": "MPNFWILENRRSYTSDTCMSRIVKEYKVILKTLASDDPIANPYRGIIESLNPIDETDLSKWEAIISGPSDTPYENHQFRILIEVPSSYPMNPPKISFMQNNILHCNVKSATGEICLNILKPEEWTPVWDLLHCVHAVWRLLREPVCDSPLDVDIGNIIRCGDMSAYQGIVKYFLAERERINNH", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis (By similarity) (PubMed:17550898, PubMed:18644345). Required for UBC4-independent ubiquitination of PEX5 (PubMed:17550898, PubMed:18644345). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MDICGVDSEGKEFNSVQEMWREEIGEGDETKKTQWYRDGVSYWEGVEASVDGVLGGYGHVNDADIIGSEVFLKTLLQERLVNNVGANQHLVALDCGSGIGRITKNLLIRYFNEVDLLEPVAQFLDAARENLASAGSETHKATNFFCVPLQEFTPAAGRYDVIWVQWCIGHLTDNDFVSFFNRAKGYLKPGGFFVVKENLAKNGFVLDKEDHSITRSDPYFKQLFRQCGLHLYRTKDQKGLPQELFAVKMYALTVDTPPKIHRTRSKTRSNRPQIIK", "text": "FUNCTION: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (By similarity). SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family."}
{"protein": "MKNKWYKPKRHWKEIELWKDVPEEKWNDWLWQLTHTVRTLDDLKKVINLTEDEEEGVRISTKTIPLNITPYYASLMDPDNPRCPVRMQSVPLSEEMHKTKYDLEDPLHEDEDSPVPGLTHRYPDRVLFLVTNQCSMYCRYCTRRRFSGQIGMGVPKKQLDAAIAYIRETPEIRDCLISGGDGLLINDQILEYILKELRSIPHLEVIRIGTRAPVVFPQRITDHLCEILKKYHPVWLNTHFNTSIEMTEESVEACEKLVNAGVPVGNQAVVLAGINDSVPIMKKLMHDLVKIRVRPYYIYQCDLSEGIGHFRAPVSKGLEIIEGLRGHTSGYAVPTFVVDAPGGGGKIALQPNYVLSQSPDKVILRNFEGVITSYPEPENYIPNQADAYFESVFPETADKKEPIGLSAIFADKEVSFTPENVDRIKRREAYIANPEHETLKDRREKRDQLKEKKFLAQQKKQKETECGGDSS", "text": "FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta- lysine. SIMILARITY: Belongs to the radical SAM superfamily. KamA family."}
{"protein": "MPHTKKILVIGASIAGPALCYWLNHYGFQPTLVEKNQSTRKGGYAIDLRGIAVDVAKQMGIYDSVCAMRTSLQCVRYVDAAGNLLFEEHGEKGGFRQGDEVEIVRGDLVDILMKTITDIPCFYDHAIESLTQHDDHVTVQFKNGKTENYDLVIAADGLHSATRRMVFSKDDYHLRNLGCYISVFSIPNYLQLDHCETLLEAKQKLVSITSDKDSTKAFAGFMFRSSNSPNYIRDEASQKDFLRENFTNHGWESNKLLSLMNDANDFYFDAIMQVKMKDWTKGRIALVGDAGYTPSPLSGQGTSLALVGAYILAGELKTATDHVAAFARYNELLKPYVEANQAFGVWVSESFLADEPLSAEQAEERNNIVLGIMKKATHAIELPEY", "text": "FUNCTION: An FAD-requiring monooxygenase active on tetracycline antibiotic and some of its derivatives, which leads to their inactivation (PubMed:26097034). Expression in E.coli confers high resistance to oxytetracycline, slightly less resistance to tetracycline, moderate resistance to minocycline but no resistance to tigecycline. Degrades tetracycline and oxytetracycline; the reaction requires NADPH (PubMed:26097034). Degrades and confers resistance to chlortetracycline (PubMed:28481346). SIMILARITY: Belongs to the aromatic-ring hydroxylase family."}
{"protein": "MVQSETSMEKYKNLSDFLKKFFIPSYVLSPEDEPEAQISCTTAPENPILVFINSKSGGQLGAELILTYRTLLNDKQVFDLEVETPDKVLQRIYLNLERLKDDSLASKIRDKLKIIVAGGDGTAGWLLGVVSDLNLSNPPPIATVPLGTGNNLPFAFGWGKKNPGTDRSSVESFLGKVINAKEMKIDNWKILMRMKHPKEGSCDITLKLPHSLPRIFPSDQENMEGYHTYRGGFWNYFSLGMDAQVSYAFHSQRKLHPERFKNQLVNQSTYLKLSCTQGWFFASLFHPSSQNIAKLAKIQICDRNGQWNDLHIPQSIRSIVCLNLPSFSGGLNPWGTPNPKKQRDRSLTAPFVDDGLIEIVGFRNAWHGLILLSPNGHGTRLAQANRVRLEFKKGAAKHAYMRIDGEPWKQPLPSNDETVMVEISHHGQVNMLATQNCRSKSMYESSSIIRFSNDEDDSSVVENEEF", "text": "FUNCTION: Phosphorylates the second messenger diacylglycerol (DAG) to generate phosphatidic acid (PA), another important signaling molecule. PA is required for plant development and responses to abiotic stress and pathogen attack. May be involved in the accumulation of PA during cold stress. SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family."}
{"protein": "MTMPKIMILPDKYPCSITSILITSRCRVTMYNRKNTLYFNQNNPNNHMYSPNQTFNEIHWTSQDLIDTIQNFLQHLGVIEDIYTIYILVS", "text": "FUNCTION: Mediates the regulatory switch from transcription to RNA replication. Acts late in infection by inhibiting viral transcription and up-regulating RNA replication. Inhibition of transcription by protein M2-2 requires phosphorylation of the phosphoprotein. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the orthopneumovirus M2-2 protein family."}
{"protein": "MKNFYYFILILLFFNEVCYSLKDGEIKLHLIPHSHCDSGWTSTMNEYYMGQVKSIISSMVQSLNVESNPPRKFVWSEIGFLEQWWDDMPIEIKNDFIKHVKNDRIEFVNGGWVMNDEACASLESVIRQLSNGHKFIREKFGKQPESGWQIDPFGHSSLTPTLQAQFGYKHVVLNRIHYELKKKFKEEKNLQFKWRGSPEGVGPKSDILAHVFDDFYTSPPHMSFDGYNFLAYGLPRLTMEMIELARNRSVFYKSPHVLIPMGGDFAFKNAYKSFEQMDQLVASINGQHANGESNVICQYSTLADFFSDTINWHNENKVSFNYYDSDFFPYADDSNTYWTGYYTSRPLLKGYERHVSSKLRSAEILSALQNDEKYYPNQLLNASKQVSILQHHDAISGTSKKHVVQDYFSRLQKADILVSEQSEKLLASALSQHSPTKLDIIDIGGSLNFPKNNDAISFILFNQLSWSKEELISIKVQSVGDHGESLNSPTNNACPYVLAQEDFLNEIEIDCSPRSDFKSDQSDDHKEFIQIDFPAKLKPFSSKLYYLKRKSNPNKSNWVLPKTNHFNSIENSIYTANLDENYLIKSLKSKSSRHGGGANQITEINQQLLTYSDIGGAYIFRTNKQVFQPPRQVYSTFTYIGKFYQEAQSILQDTHQISNRNGYYYYYGNNQQQQQQQQTISTFNYNSIKLINTGNEMIDKKINFNFHIRGINGTTTINRFTTDIDNNRELYSDNGLEMMHRKSISSQSVEVGRETQSYYPTINSVYIESQSTGKRFVCNNDRSRGVSSQGQGCLEMALHRSLTYEDGKGLEIPAIDESSINARFECYLDEVPSNSQQSNGGGGGDDIRKQSINYQHKFQIYQGQDSSYMSSKSFMLKPLPEFIHILSMERSGPRSIKLRIHNIENNNQSPITFDLNGLFSFIKSIKSIKEYNLSLINRFVDNNIDNIISSHRSIVGKNLFPIKDTPTRFNPINTKQTKITLYPSEIKAIEITYH", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 38 family."}
{"protein": "MYVEKILQSLQKKYPYQKEFHQAVYEAITSLKPLLDSDKSYEKHAVLERLIEPEREIFFRVCWLDDNHQIQVNRGCRVEFNSAIGPYKGGLRFHPSVNESVIKFLGFEQVLKNSLTTLAMGGAKGGSDFDPKEKSEHEIMRFCQAFMNELYRHIGATTDVPAGDIGVGEREIGYLFGQYKKLVNRFEGVLTGKGLTYGGSLCRKEATGYGCVYFAEEMLQERNSSLEGKVCSVSGSGNVAIYTIEKLLQIGAKPVTASDSNGMIYDKDGIDLELLKEIKEARRGRIKEYALEKTSAKYTPTENYPKGGNAIWHVPCFAAFPSATENELSVLDAKTLLSNGCKCVAEGANMPSSNEAIELFLQAKISYGIGKAANAGGVSVSGLEMAQNASMHPWSFEVVDAKLHHIMKEIYKNVSQTAKEFKDPTNFVLGANIAGFRKVASAMIAQGV", "text": "FUNCTION: Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family."}
{"protein": "MNYFPIFANLAGRPVLVVGGGAVAARKISLLLKAGAEVRVAAKHLNAELSALAAENKILWLAEEFRAEHIRTVFLIIAASSDQALNRRVFHLAESCQKPVNVVDDRDHCSFIFPSVIDRNPVQIAVSSSGSAPVLARLLRERLEALLPPSLGDMAEISGRWRDAVKGKLKSVTERRRFWEKQFNGRFAALVKNRQNTLAERELAGQLEQSRQNDQGGSVSLVGAGPGDAGLLTLKGLQEIQQADVVLYDALVSDGILSLVRRDAERIFVGKRARGERTPQEDTNALMVRLAREGRRVVRLKGGDPFVFGRGGEELETLARHQIPFSVVPGITAAVGATAYAGIPLTHRDYAQSAVFVTGHRKADAPDIEWQTLARSRQTLVIYMGALKAALIAERLQQHGRSPDTPAAVISQGTLPAQKTATGTLANLAELAETAPNPALIVIGEVVGLHEKLAWFGENGEGENRVGQTYPALGGLNAGQRAA", "text": "FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. SIMILARITY: In the C-terminal section; belongs to the precorrin methyltransferase family. SIMILARITY: In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family."}
{"protein": "MSAPIVHGGGITEAAARYGGRPEDWLDLSTGINPCPVALPAVPERAWHRLPDRQTVDDARSAAADYYRTNGVLPLPVPGTQSVIQLLPRLAPANRHVAIFGPTYGEYARVLEAAGFAVDRVADADALTAEHGLVIVVNPNNPTGRALAPAELLAIAARQKASGGLLLVDEAFGDLEPQLSVAGHASGQGNLIVFRSFGKFFGLAGLRLGFVVATEPVLASFADWLGPWAVSGPALTISKALMQGDTKAIAAGILERRAGLDAALDGAGLNRIGGTGLFVLVEHPRAALLQERLCEAHILTRKFDYAPTWLRVGLAPDAAGDRRLADALARMEL", "text": "FUNCTION: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRISLTQTRAA", "text": "FUNCTION: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. FUNCTION: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. CcmA exporter (TC 3.A.1.107) family."}
{"protein": "MRGGQRRASRLRPPTYRRRPPPAASILEVAPVQTQTLTQTDTAAGGAEPDAERGVLLAMPAQPGAGAALPHPGAPVDVPEHPEPPPPTRTESGGPSSDLFRQYLREIGRIPLLSAAEEVDLARRVEAGLFAEEKLRCSPGLDDRLALDLDRLVVLGRLAKRRLIEANLRLVVSVAKRYVGRGLTMLDLVQEGNLGLIRAVEKFDYARGYKFSTYATWWIRQAMSRALADQARTIRVPVHVVELINRVVRVQRRMLQERGCEPTPQEVAAHLDLAPERVGEVLRLAQEPVSLHAPVGEEDDVALGDLIEDGDAASPVESAAFLLLRQHLEAVLSTLGERERKVVQLRYGLADGRPRTLEEIGRLFGVTRERIRQIESKTLSKLRDHAYADQLRGYLD", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. SIMILARITY: Belongs to the sigma-70 factor family."}
{"protein": "MENEKENLFFEPHKRGLMKTPLKESTAANIVLADIQPDFGPLTTPTKPKEISQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRNGLSDVKDCLHEHFSGDEYEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNQILETLKSVGEENKYAEQIMMIKKKEYEQEFEVSKSYNTEDPIIKSNTGQNGHPDMCCAERPGVELRAASVNSRKDKSLKVMSQKFVTLFLVSTPQIVSLEIAAKILTWEDHVEDLDRSKFKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNPSGLSPVLPCAASDLEARQSSKENCAKNLFSTRGKPNFTRHPSLIKLVKSIESDRRKINSAPSSPIKTHKAESTQNSVPFRSKMAQLAAICKMQLEEQSSEPRKNVTVQLAGSGHCKSVAPLDTPANAEPEMMAPSLIQPLGVVPLLPSPLSPAVPVILPQTPSGTSYAIYLQPAQAQTITPPPGLSPTVCPTTSSNAMISEDSTDATGENADSDAPKSSVSTRPGSLLPGPERQGAKNREREPAREKGSKRASMLEDSGSKKKFKEDQKAPENVSTTLFPSGYLIPLTQCSTLGAESILSSNENSGTLSPNHSIYSSPIAGVIPVTSSELTAVNFPSFQVTPLKLMVSPTSMAAVPVGNSPALSSSHPLPIQNPSSAIVNFTLQHLGLISPGVQVSTSPGPGTIAVSPRIEAVSVTPENAGAEQGRATKCDASILSQNQTNGQSFAGTGAQQPVPVTPKGSQPVAESFFRTPGGPTKPTGSPCTDFDGANYTSVGTLLVPQRKLEVSVEDVH", "text": "FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the E2F/DP family."}
{"protein": "MRVIMKPLRRTLVFFIFSVFLCGTVSARQIEWQSCMTSPYSDWFGKESSSPELLCGYLSVPLKYTDTGKDVSDENIPLVRLAMTKLPAKSKRKGSVIIISGGPGLPGINPYINFDWPVTNLRESWDIIGFDPRGVGQSFPAINCQQSNQERLVNVSEKQLILQKINACIHNTGAEVIRHIGSHEAVYDIERIRQALGDKQLTAVAYSYGTQIAALYAERFPSSIRSIVFDGVVDIDDLNDNFSWKLRQAHSYQETFDRFAAWCARTKSCPLSSDRNQAIHQFHQLLLKLHNSPLTDSRGESISSDDLISLTTELLLWRSSWPTLATAVRQFSQGIVSNEIETALNSSIASEKVSDALGVILCVDQSDEQLSQEQRKSRKKALADAFPAVNFEREQSDLPEFCELWPIHRDLQQTRLKNTVLPSGLLFVAHKYDPTTPWINARKMADKFSAPLLTINGDGHTLALAGTNLCVDEAVVRHLLFPGKSEDITCQGSGTGDTN", "text": "SIMILARITY: Belongs to the peptidase S33 family."}
{"protein": "MADQEADTNIEIWKIKKLIKGLESARGNGTSMISLIMPPRDQVSRVTKMLGDEYGTASNIKSRVNRQSVLSAITSAQQRLKLYNKVPTNGLVLYTGTIVNDDGKEKKVTFDFEPFRPINASLYLCDNKFHTGALNELLESDDKFGFIVMDGNGTLFGTLSGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKTAELATQFYINPATSQPNVAGLILAGSADFKTELSQSELFDPRLQAKILNVVDVSYGGENGFNQAIELSAEILSNVKFIQEKKLIGKYFEEISQDTGKYVFGVEDTLKALEMGAIETLIVWENLDINRYELKNSTSGEIVVKHFGKDQETDQSNFHDAETNAELEVQEKMPLLEWFANEYKRFGCTLEFVTNKSQEGSQFCRGFGGIGGMLRYQLDMRTFDELSDGEVYEDSD", "text": "FUNCTION: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (By similarity). Modulates plant growth and development (PubMed:21175633). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family."}
{"protein": "MTAIRKNDMNYTLDDFTKLEKIGEGTYGVVYKGRNRRTQAMVAMKKIRLESEDEGVPSTAVREISLLKELQHPNVVGLEAVIMQENRLYLIFEFLSYDLKRYMDTLSKEEYLPSETLKSYTFQILQAMCFCHQRRVIHRDLKPQNLLVDEKGAIKLADFGLARAIGIPIRVYTHEVVTLWYRAPEILMGAQRYSMGVDMWSIGCIFAEMATKKPLFQGDSEIDELFRIFRILGTPTELEWNGVESLPDYKATFPKWRENFLRDKFYDKKSGNYLMDEDAFSLLEGLLIYDPALRISSKKALHHPYFNDIDTSKLPAGNYRGELQLE", "text": "FUNCTION: Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MLYASQRGRLTENLRNALQQDSTTQGCLGAETPSIMYTGAKPDRWAHPLVGTIHASNLYCPMLRAYCRHYGPRPVFVASDESLPMFGASPALHTPVQVQMCLLPELRDTLQRLLPPPNLEDSEALTEFKTSVSSARAILEDPNFLEMREFVTSLASFLSGQYKHKPARLEAFQKQVVLHSFYFLISIKSLEITDTMFDIFQSAFGLEEMTLEKLHIFKQKASVFLIPRRHGKTWIVVAIISLILSNLSNVQIGYVAHQKHVASAVFTEIIDTLTKSFDSKRVEVNKETSTITFRHSGKISSTVMCATCFNKNSIRGQTFHLLFVDEANFIKKEALPAILGFMLQKDAKIIFISSVNSADQATSFLYKLKDAQERLLNVVSYVCQEHRQDFDMQDSMVSCPCFRLHIPSYITMDSNIRATTNLFLDGAFSTELMGDTSSLSQGSLSRTVRDDAINQLELCRVDTLNPRVAGRLASSLYVYVDPAYTNNTSASGTGIAAVTHDRADPNRVIVLGLEHFFLKDLTGDAALQIATCVVALVSSIVTLHPHLEEVKVAVEGNSSQDSAVAIASIIGESCPLPCAFVHTKDKTSSLQWPMYLLTNEKSKAFERLIYAVNTASLSASQVTVSNTIQLSFDPVLYLISQIRAIKPIPLRDGTYTYTGKQRNLSDDVLVALVMAHFLATTQKHTFKKVH", "text": "FUNCTION: Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM1 and TRM2 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM3 carries an RNase H-like nuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes. SUBCELLULAR LOCATION: Host nucleus Note=Responsible for the nuclear localization of the two others subunits TRM1 and TRM2. SIMILARITY: Belongs to the herpesviridae TRM3 protein family."}
{"protein": "MSLKIPGLADMHVHLRQDNMLKAVVPTVAEGGVSVAYVMPNLIPPITTVDACLQYKKEIEQLDSKTTYLMSLYLSPETTPEVIYEAAKKGIRGVKSYPKGATTNSESGVESYEPFYPTFAAMQETGMILNIHGEVPPSKDNTVFTAEPKFLPTLLDLHQRFPKLKIVLEHCTTADAVEAVKACGESVAGTITAHHLYLTQKDWQDDPYCFCKPVAKTERDRRALIEAATSKNPKFFFGSDSAPHPRSSKLKTPPAAGVFTQPFAASYLAEVFDKEGRLDALKDFACIFGRKFYCIPLDFKESNIVLKKESFRVPESVANDLVPFHPNEVLQWHCSWE", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily."}
{"protein": "VQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEVFTGAPGKYVDLKESITSFQGVLDGKFDDLPEQSFYMVGGIEEVIAKAEKISKESAA", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MANAGLQLLGFILAFLGWIGSIVSTALPQWKVYSYASDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVATVGMKCMKCMEDDEAQKMRMAVFGGVIFLISGLAILVATAWYGNRIVQEFYDPMTPVNARYEFGQALFIGWAAASLCLLGGALLCCSCPRKTTSYPTPRPYPKPAPSSGKDYV", "text": "FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions (By similarity). SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein Basolateral cell membrane Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. SIMILARITY: Belongs to the claudin family."}
{"protein": "MDKSLFYNPQKMLSYDRILNFVIGARGIGKSYAMKVYPINRFIKYGEQFIYVRRYKPELAKVSNYFNDVAQEFPDHELVVKGRRFYIDGKLAGWAIPLSVWQSEKSNAYPNVSTIVFDEFIREKDNSNYIPNEVSALLNLMDTVFRNRERVRCICLSNAVSVVNPYFLFFNLVPDVNKRFNVYDDALIEIPDSLDFSSERRKTRFGRLIDGTEYGEMSLDNQFIGDSQVFIEKRSKDSKFVFSIVYNGFTLGVWVDVNQGLMYIDTAHDPSTKNVYTLTTDDLNENMMLITNYKNNYHLRKLASAFMNGYLRFDNQVIRNIAYELFRKMRIQ", "text": "FUNCTION: ATPase required for the genome encapsidation reaction. Part of the active packaging motor via the binding to the packaging RNA (pRNA), itself fixed to the head-tail connector at the unique portal vertex of the prohead. Binds and supercoils the DNA-gp3 to produce an initiation complex for DNA packaging. Provides the energy to actively pump the viral DNA into the prohead. Approximately one molecule of ATP is used in the packaging of 2 bp of viral DNA. After packaging, the ATPase and the pRNA are released from the prohead. SIMILARITY: Belongs to the phi29likevirus gp16 family."}
{"protein": "MDSAAAAFALDKPALGPGPPPPPPALGPGDCAQARKNFSVSHLLDLEEVAAAGRLAARPGARAEAREGAAREPSGGSSGSEAAPQDGECPSPGRGSAAKRKKKQRRNRTTFNSSQLQALERVFERTHYPDAFVREELARRVNLSEARVQVWFQNRRAKFRRNERAMLASRSASLLKSYSQEAAIEQPVAPRPTALSPDYLSWTASSPYSTVPPYSPGSSGPATPGVNMANSIASLRLKAKEFSLHHSQVPTVN", "text": "FUNCTION: May play a role in the scarless healing of cutaneous wounds during the first two trimesters of development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family."}
{"protein": "MKANKLSAITLCILGYAHTVYAESNMQTEKLETIVVSSEDDSVHNKNVGEIKKNAKALSKQQVQDSRDLVRYETGVTVVEKGRFGSSGYAIRGVDENRVAVVVDGLHQAETISSQGFKELFEGYGNFNNTRNGVEVENLKQAVIQKGADAIRTGSGSLGGTVSFESKDARDYLIDKNYHFGYKTGYSSADNQKLHSVTAAGRYSDFDLLAVHTQRHGNELRNYGYRHYDGSVVRKEREKADPYKITKQSSLIKIGYQLNDTNRFTLGYDDSRNTSRGTDWSNAFTSYNGGPFLKDVRHTNDQSNRKNISFVYENFDTNDFWDTLKITHNHQKIKLKARLDEYCDVNGEIDCPAIANPSGLYINDKGIFLDKHDGEITHKKEGEFNNYFDSKGKEVRVKGFNVDSILINCDQYDCSKPMQLLSSTNNGYGGSPNKYIYKTYELFEKTMNNGNGKYAVLEIRSSGHEKFSRVYLPSEKGYVENQWKDRDLNTDTQQYNIDLTKSFKLKSVEHNATYGGLYSEVKKSMTNRAGYEAYNRQWWANIFFGKENNKPNKCQPYNGNSFTTLCSHEDRLFSFLIPVKTKTGALYVTDKIKLNDKVNLDVAYRYDRIKHDPKYIPGTTPKLPTDLILGRFIEFKPKNTYATQDEKNENAEKNAVYLASKKTKFSANSYSATFSFDPMDFLKIQAKYATGFRAPTSDEIYFVFQHPSFSIYPNLYLKAERSKNKEVAITLHKQKSFLTVNLFQTDYKDFLDLAYLKKGSLPYGNGGSQLETLLYQNVNRDKARVKGLEVNSKLHLGDVWRTLDGFNLSYKLSLQKGRMSSKVGEEGKQRDTNKLDTPMNAIQPQTHVVGVGYEHPQEKFGVDMYLTHASAKKEKDTFNMFYDGKDQKDQHIKWRSDRYTLVDLIAYVKPVKNVTLRAGVYNLTNREYGTWDSIRSIRPFGTTNLINQETGKGIKRFNAPGRNFRVNAEITF", "text": "FUNCTION: Acts as a receptor for hemoglobin or the hemoglobin/haptoglobin complex of the host and is required for heme uptake. May be involved in virulence. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family. Hemoglobin/haptoglobin binding protein subfamily."}
{"protein": "MAFPELLDRVGGRGRFQLLQAVALVTPILWVTTQNMLENFSAAVPHHRCWVPLLDNSTSQASIPGDFGRDVLLAVSIPPGPDQRPHQCLRFRQPQWQLIESNTTATNWSDADTEPCEDGWVYDHSTFRSTIVTTWDLVCDSQALRPMAQSIFLAGILVGAAVCGHASDRFGRRRVLTWSYLLVSVSGTIAALMPTFPLYCLFRFLVASAVAGVMMNTASLLMEWTSAQAGPLMMTLNALGFSFGQVLTGSVAYGVRSWRMLQLAVSAPFFLFFVYSWWLPESARWLITVGRLDQSLRELQRVAAVNRRKAEADTLTVEVLRSAMQEEPNGNQAGARLGTLLHTPGLRLRTFISMLCWFAFGFTFYGLALDLQALGSNIFLLQALIGIVDLPVKMGSLLLLSRLGRRLCQASSLVLPGLCILANILVPREMGILRSSLAVLGLGSLGAAFTCVTIFSSELFPTVIRMTAVGLGQVAARGGAMLGPLVRLLGVYGSWLPLLVYGVVPVLSGLAALLLPETKNLPLPDTIQDIQKQSVKKVTHDIAGGSVLKSARL", "text": "FUNCTION: Electroneutral antiporter that translocates urate across the apical membrane of proximal tubular cells in exchange for monovalent organic or inorganic anions (PubMed:21074513). Involved in renal reabsorption of urate and helps maintaining blood levels of uric acid (PubMed:21074513). Mediates urate uptake by an exchange with organic anions such as (S)-lactate and nicotinate, and inorganic anion Cl(-) (PubMed:21074513). Other inorganic anions such as Br(-), I(-) and NO3(-) may also act as counteranions that exchange for urate (By similarity). Also mediates orotate tubular uptake coupled with nicotinate efflux and to a lesser extent with lactate efflux, therefore displaying a potential role in orotate renal reabsorption. Orotate transport is Cl(-)-dependent (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family."}
{"protein": "MEKETTFLGLKLSEKGPGNDMVKKALGYSLKYLEIETFMDVIGFVKDPVMTDYFWHIMVDNHCRHLATVLLECLGYEGTYNKQQYAIKRFLKSNRINYSELSSDDPQIDLYPTIKEEMKNMKPNAIACRKWLIIEPREFKKVIMKLNTKNGDNIREYYIRLEELIKLYLEYSLYFKEREAQIEKQKSQFHIETLEKKLDEMKLEAEKRHDELLDKVEEVQYDLNVVGEKLDIAVEDRAPKVKAELLRERFVVLNRNDKRASCQYYVMRGQDHYINGKIFSYKNLHPNLKIIFDISCQPNPRNLFVRFKELKDNRFKVVGNNIQTLDEKALLEVFNKLNDDKRNIQLM", "text": "SIMILARITY: Belongs to the IIV-6 006L/238R/313L/468L family."}
{"protein": "MTSTQNHPLQTQDDQQRFGQSPESVRETDHYQQEYIEDFTDRWDRLIDWNARAEAEGDFFIRLLKEHGARSVLDVATGTGFHSIRLLEEGFDVVSADGSPNMLARAFRNARNRDQLLRTSQADWRFLNRDIHGEFDAVICLGNSFTHLFKERDRRKALAEYYAVLKHNGILILDHRNYDRLLEGGSAVRQGKGNVYCGKDVEVGPEHVDEGLARFRYSFSDGGVYHLNMFPLRYGYVRRLMSEVGFQQITSFGDYQRDFENPDFYVHVAEKEYRFDVDTTMH", "text": "FUNCTION: Catalyzes the methylation of glycine and sarcosine to sarcosine and dimethylglycine, respectively, with S-adenosylmethionine (AdoMet) acting as the methyl donor. It has strict specificity for glycine and sarcosine as the methyl group acceptors. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Glycine N-methyltransferase family."}
{"protein": "MDGKVAVQECGPPAVSWVPEEGEKLDQEDEDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFVCGIPVFFLEVALGQYTSQGSVTAWRKICPLFQGIGLASVVIESYLNVYYIIILAWALFYLFSSFTSELPWTTCNNFWNTEHCTDFLNHSGAGTVTPFENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWVICYFCIWKGVKSTGKVVYFTATFPYLMLVILLIRGVTLPGAYQGIIYYLKPDLFRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYKDCIALCFLNSATSFVAGFVVFSILGFMSQEQGVPISEVAESGPGLAFIAFPKAVTMMPLSQLWSCLFFIMLIFLGLDSQFVCVECLVTASIDMFPRQLRKSGRRELLILTIAVMCYLIGLFLVTEGGMYIFQLFDYYASSGICLLFLSLFEVVCISWVYGADRFYDNIEDMIGYRPWPLVKISWLFLTPGLCLATFLFSLSKYTPLKYNNVYVYPPWGYSIGWFLALSSMVCVPLFVVITLLKTRGPFRKRLRQLITPDSSLPQPKQHPCLDGSAGRNFGPSPTREGLIAGEKETHL", "text": "FUNCTION: Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A12 subfamily."}
{"protein": "MFKSGSGSLKRSGSISSVKSFSGDSEKGLPPISRGSVSITSQNYEPLIVPANSSSFAAASDFVPEKTKSEGNLKNKSSVITGNFESSGPTNAHYNQNADGDRLVENLLLKEIAKGRGPSTSDARHTATDSRLSQEVKQPFSEENAGGNDLNTGRGSHGTGDGIEQYHKSDCEERMSAYHKRVVDTFFKYFEYSAEDGHSTLYSDVAFLFGCGDLDLLVMSRYQEVMTLRARSAIYGIFCYLQALTAYLTYLGAKVGQVIMLDEELEKYEIRLDVAQDDDPIVFQITTGVFTSGVAHDLRKLTQILEAFSLER", "text": "FUNCTION: Constituent of viral factories. SUBCELLULAR LOCATION: Host cytoplasm Note=Constituent of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the phytoreovirus non-structural protein Pns12A family."}
{"protein": "MSKRSLDPSDDFKGQKRLAIDPESTALEQDRQMLQQLSEQNSELEPQNVAPNAEIPLGFDLSGIQFNMTPDFYLRMNQGMDYAFNQPNPIATPQQLLRTSLIPTLGNLSNIILSILGKPVQEASAIVTNPASEMGMAFTKVMNMFRMVKDIYTEESFIYSSAIGMRTPSQRSTTRRANLAIFLAAVYGALQIGFFHLNENFLEVFAPDESNILTNQGTLYMELKTQAYISAMAQAERPKGDILNDLFPSDMAHRFLIRRNAKLDDKLTYVEKQIIEKCTARKERLANFSPQEALNEVYPWGKFLSEIACYIHNNYSSISAIPIPANSFKRRSKKNGLRFKAGEAESSPSESGSDLTDSLAFGIPSSTFDGSSETQNVSSVVLYDQVRHMTNNNLNNKRTRRVANRRSWTKEEEEALLDGLDLVKGPRWSQILELYGPGGKKSEVLKYRNQVQLKDKARNMKLFFLKSGQVVPAALQCVTGDLRRD", "text": "FUNCTION: Binds the telomeric double-stranded TTACAGG repeat and regulates telomere length. SUBCELLULAR LOCATION: Nucleus Note=Enriched throughout the euchromatic hemisphere."}
{"protein": "MVRILRKIKSAAVNPLKSSQPLGAAFAFLGVEGAMPLFHGSQGCTSFALVLFVRHFKEAIPLQTTAMDEVATILGGADHLEEAILNLKTRTKPKLIGVCTTALVETRGEDCASDIANVKLKHVEELAGTEVVLANTPDFDGAIEEGWAKAVAAMIEGITRSGERTRQPKKIAILPGCNLTVADVEHLRDMVESFGLKPVILPDVSGSLDGTVPDRWVTTTYGGTSVEEIRELGTAAQCIVIGEHMRHPAKTLHGLTGVPYAVFQSLTGLKAVDRFVSLLSAVSGAAVPDRVRRHRAQLEDALLDGHFHFGGKKIAIAAEPDQLYQLATFFTGMGCDIAAAVTTTDMSKILQKVPAEWVQIGDLGDLEALAAGADLLVTHSHGRQASRRLEIPLMRVGFPIFDRLGSQHKLTILYRGTRDLIFDVANIFQANQHAPTPEALDPFRKREMPDELRSSPLTRH", "text": "FUNCTION: This protein may play a role in the biosynthesis of the prosthetic group of nitrogenase (FeMo cofactor). SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family."}
{"protein": "MRTIIALETHDVRFPTSRELDGSDAMNPDPDYSAAYVVLRTDGAEDLAGYGLVFTIGRGNDVQTAAVAALAEHVVGLSVDKVIADLGAFARRLTNDSQLRWLGPEKGVMHMAIGAVINAAWDLAARAANKPLWRFIAELTPEQLVDTIDFRYLSDALTRDEALAILRDAQPQRAARTATLIEQGYPAYTTSPGWLGYSDEKLVRLAKEAVADGFRTIKLKVGANVQDDIRRCRLARAAIGPDIAMAVDANQRWDVGPAIDWMRQLAEFDIAWIEEPTSPDDVLGHAAIRQGITPVPVSTGEHTQNRVVFKQLLQAGAVDLIQIDAARVGGVNENLAILLLAAKFGVRVFPHAGGVGLCELVQHLAMADFVAITGKMEDRAIEFVDHLHQHFLDPVRIQHGRYLAPEVPGFSAEMHPASIAEFSYPDGRFWVEDLAASKAKA", "text": "FUNCTION: Plays a role in the catabolism of L-fucose. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. L-fuconate is the preferred substrate with 15-fold lower activity observed for L-galactonate and 8- fold lower activity with D-arabinonate. No activity detected with D- fuconate. Can also catalyze the epimerization of L-talonate and D- ribonate, but at slow rates. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
{"protein": "GKPDGAFXDNITVVESVXFXI", "text": "FUNCTION: Binds and precipitates antigens of the parasite Echinostoma paraensei. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MLPRLGGPALPLLLPSLLLLLLLGAGGCGPGVRAEVLFRCPPCTPERLAACGPPPDAPCAELVREPGCGCCSVCARQEGEACGVYIPRCAQTLRCYPNPGSELPLKALVTGAGTCEKRRVGATPQQVADSEDDHSEGGLVENHVDGTMNMLGGSSAGRKPPKSGMKELAVFREKVNEQHRQMGKGAKHLSLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDDRGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKPIQGAPTIRGDPECHLFYNEQQENDGAHAQRVQ", "text": "FUNCTION: Inhibits IGF-mediated growth and developmental rates (By similarity). IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTIDQMTIDQMTKIFLADKESTLNLGILLGETLTAGSVILLEGDLGAGKTTLVQGLGKGLSITEPIVSPTFTLINEYTEGRIPLYHLDLYRLEPQEVLSLNLEIYWEGIEIIPGIVAIEWSERMPYKPSTYINVLLTYGDEGSRQAEITPFNCTISDLIATK", "text": "FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TsaE family."}
{"protein": "MATSSCFLLVTLGLLLHVQQAFLHEHTCSPSEPAAPGGICGSNLAELHSFLCEKELEDYSGSALKKRGRPSRRMKRRDFLSALKTRVKRKEGRSVKRSPTSGMSCECCKNSCDAEEILEYCPPLPSS", "text": "FUNCTION: This venom insulin facilitates prey capture by rapidly inducing hypoglycemic shock. Intraperitoneal injection of this peptide into zebrafish lowers blood glucose with the same potency than human insulin. In vivo, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
{"protein": "MSEGQKFQLGTIGALSLSVVSSVSIVICNKALISTLGFTFATTLTSWHLLVTFCSLHVALWMKMFEHKPFDPRAVMGFGILNGISIGLLNLSLGFNSVGFYQMTKLAIIPCTVLLETLFFRKKFSRKIQFSLTILLLGVGIATVTDLQLNMLGSVLSLLAVVTTCVAQIMTNTIQKKFKVSSTQLLYQSCPYQAITLFVTGPFLDGLLTNQNVFAFKYTSQVVFFIVLSCLISVSVNFSTFLVIGKTSPVTYQVLGHLKTCLVLAFGYVLLRDPFDWRNILGILVAVIGMVVYSYYCSIETQQKASETSTQLPQMKESEKDPLIAAENGSGVLSDGGGGVQQKTVAPVWNSNKDFQA", "text": "FUNCTION: Nucleotide-sugar transporter that transports UDP-xylose and UMP in a strict counter-exchange mode. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9) subfamily."}
{"protein": "MAAVAAASAELLIIGWYIFRVLLQVFLECCIYWVGFAFRNPPGTQPIARSEVFRYSLQKLAHTVSRTGRQVLGERRHRAPN", "text": "FUNCTION: May participate in the maintenance of segment identity in the hindbrain and pituitary development, and maturation or maintenance of the overall structure of the nervous system. SIMILARITY: Belongs to the neuronatin family."}
{"protein": "MVSIAFYGGIPGGISTPITQQSEKSKCEENTMFQPYCYNNDSKNSMAESKEARDQEMNLKEESKEEKRRNDWWEIGMFLLCLAGTTGGILWWYEGLPQQHYIGLVAIGGRLNGSGQSNAIECWGSFPGCRPFQNYFSYETNRSMHMDNNTATLLEAYHREIAFIYKSSCTDSDHCQEYQCKKVNLNSSDSSNSVRVEDVTNTAEYWGFKWLECNQTEHFKTILVPENEMVNINDTDTWIPKGCNETWARVKRCPIDILYGIHPIRLCVQPPFFLVQEKGIADTSRIGNCGPTIFLGVLEDNKGVVRGDYTACNVRRLNINRKDYTGIYQVPIFYTCTFTNITSCNNEPIISVIMYETNQVQYLLCNNNNSNNYNCVVQSFGVIGQAHLELPRPNKRIRNQSFNQYNCSINNKTELETWNLVNTSGLTPLPISSEANTGLIRHKRDFGISAIVAAIVAATAIAASATMSYVALTEVNKIMEVQNHTFEVENSTLNGMDLIERQIKILYAMILQTHADVQLLKERQQVEETFNLIGCIERTHVFCHTGHPWNMSWGHLNESTQWDDWVSKMEDLNQEILTTLHGARNNLAQSMITFNTPDSIAQFGKDLWSHIGNWIPGLGASIIKYIVMFLLIYLLLTSSPKILRALWKVTSGAGSSGSRYLKKKFHHKHASREDTWDQAQHSIHLAGVTGGSGDKYYKQKYSRNDWNGESEEYNRRPKSWVKSIEAFGESYISEKTKGEISQPGAAINEHKNGSGGNNPHQGSLDLEIRSEGGNIYDCCIKAQEGTLAIPCCGFPLWLFWGLVIIVGRIAGYGLRGLAVIIRICIRGLNLIFEIIRKMLDYIGRALNPGTSHVSMPQYV", "text": "FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N- terminus of Gag (By similarity)."}
{"protein": "MAELACFCYPHLENDSYKFIPFNSLAIKCMLTAKVDKKDQDKFYNSIVYGIAPPPQFKKRYNTNDNSRGMNYETPMFNKVAILICEALNSIKVTQSDVANVLSRVVSVRHLENLVLRKENHQDVLFHSKELLLKAVLIAIGQSKEIETTATAEGGEIVFQNAAFTMWKLTYLDHKLMPILDQNFIEYKITLNEDKPISDICVKELVAELRWQYNRFAVITHGKGHYRVVKYSSVANHADRVFATYKNNAKSGNVTDFNLLDQRIIWQNWYAFTSSMKQGNTLDVCKKLLFQKMKQEKNPFKGLSTDRKMDEVSHVGI", "text": "FUNCTION: Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. SUBCELLULAR LOCATION: Host cytoplasm Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus NSP2 family."}
{"protein": "MPSRRRTLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVQFEDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNSAKSFEDLNNWREEFLIQASPSDPENFPFVVIGNKIDVDGGSSRVVSEKKARAWCASKGNIPYYETSAKVGTNVEDAFLCITTNAMKSGEEEEMYLPDTIDVGTSNPQRSTGCEC", "text": "FUNCTION: Intracellular vesicle trafficking and protein transport. May play a role in adaptation to stress by recylcing macromolecules in specific cellular compartments. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MRAVLLPGSGEQPTAFCYQVNGSCPRTVHPLAIQVVIYLACAVGVLITVLGNLFVVFAVSYFKVLHTPTNFLLLSLALADMLLGLLVLPLSTVRSVESCWFFGDFLCRLHTYLDTLFCLTSIFHLCFISIDRHCAICDPLLYPSKFTVRTALRYIVAGWGIPAAYTAFFLYTDVVERALSQWLEEMPCVGSCQLLFNKFWGWLNFPAFFVPCLIMISLYLKIFVVATRQAQQIRTLSQSLAGAVKRERKAAKTLGIAVGIYLVCWLPFTVDTLVDSLLNFITPPLVFDIFIWFAYFNSACNPIIYVFSYRWFRKALKLLLSREIFSPRTPTVDLYHD", "text": "FUNCTION: Olfactory receptor specific for trimethylamine, a trace amine enriched in the urine of male mice, playing a role in social behavior. Trimethylamine is present at high concentration in the urine of male mice after puberty and acts as an attractant. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRYITVEDLSFYYDKEPVLEHINYCVDSGEFVTLTGENGAAKTTLIKASLGILQPRIGKVAISKTNTQGKKLRIAYLPQQIASFNAGFPSTVYEFVKSGRYPRKGWFRRLNAHDEEHIKASLDSVGMWEHRDKRLGSLSGGQKQRAVIARMFASDPDVFILDEPTTGMDAGSKNEFYELMHHSAHHHGKAVLMITHDPEEVKDYADRNIHLVRNQDSPWRCFNVHENGQEVGHA", "text": "FUNCTION: Part of the ATP-driven transport system AdcABC for zinc. Required for transformability. FUNCTION: Part of the ATP-driven transport system AdcABC for zinc. Required for transformability (By similarity). SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MSTKLDTILENPQYAILCGITVFTLFIVQLSLFDRGRNYPLLNPKGSFEISTNRVVREFISDSRNLLEKGKSLFKGQPYRANTDWGEVVVIPPQFLDALKSHKDLDFTIPAQDDSHCYIPGFEPFDADPNLSKVVIKYLTKALNRVTGPLSEEASIAFRTVISDSPEWHEIQPQPAFVRIISRMSSRVFMGEELCRNEEWVKLAGDYTVQSFKTGDELRMYPRWSRPFVHHFLPSCKEVRRTLNAARNCLNPLLERRNAIKAEAKAKGEPCPYDNSFEWFEKEYSTHDPAVAQLNLSLVAIHTTTDLLMETVFNIAQHPELLAPLREEIVRVLSTEGLKKTALLNLKLMDSVLKESQRLRPALLGSFRRLAMADVTLPNGDVIKKGTKIVCSTSHMWSADSHESGEEFDGYRFLRMREKEETEQGKTSHPHLVSPSSDHLGFGFGNHACPGRFFAANELKIALCHMLLKYDWKLAKDAVPRSASFGMILMPDLRTKLLIRRRSEELDIDSVES", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of equisetin, a trans-fused decalin- containing tetramic acid with antimicrobial activity (PubMed:23614392). The PKS module of eqxS together with the enoylreductase eqxC catalyze the formation of the polyketide unit which is then conjugated to L- serine by the condensation domain of the eqxS NRPS module (PubMed:23614392). Activity of the Dieckmann cyclase domain (RED) results in release of the Dieckmann product intermediate (PubMed:23614392, PubMed:18652469). Diels-Alderase eqx3 is involved in endo-selective Diels-Alder cycloaddition to form the decalin ring, leading to the production of N-desmethylequisetin also called trichosetin (By similarity). Subsequent N-methylation is carried out by eqxD to give equisetin (PubMed:23614392). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MKYSLWALLLAVLGTQLLGSLCSTVRSQRFRGRIQQERKNIRPNIILVLTDDQDVELGSLQVMNKTRKIMEQGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNVLQRKRLQTLMSVDDSVERLYNMLVESGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSIEPGSIVPQIVLNIDLAPTILDIAGLDSPSDVDGKSVLKLLDLEKPGNRFRTNKKAKIWRDTFLVERGKFLRKKEESGKNIQQSNHLPKYERVKELCQQARYQTACEQPGQNWQCIEDTSGKLRIHKCKGPSDLLTVRQNARNLYSRGLHDKDKECHCRDSGYRSSRSQRKNQRQFLRNKGTPKYKPRFVHTRQTRSLSVEFEGEIYDINLEEEELQVLPPRSIAKRHDEGHQGFIGHQAAAGDIRNEMLADSNNAVGLPATVRVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEVLQDKIKNLREVRGHLKKRKPEECGCGDQSYYNKEKGVKRQEKLKSHLHPFKEAAAQEVDSKLQLFKEHRRRKKERKEKKRQRKGEECSLPGLTCFTHDNNHWQTAPFWNLGSFCACTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTVERSILNQLHIQLMELRSCQGYKQCNPRPKSLDIGAKEGGNYDPHRGQLWDGWEG", "text": "FUNCTION: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity (By similarity). It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin (By similarity). Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation (By similarity). SUBCELLULAR LOCATION: [Extracellular sulfatase Sulf-2 secreted form]: Secreted. SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus, Golgi stack Cell surface. SIMILARITY: Belongs to the sulfatase family."}
{"protein": "MAPRPPTATPQESVTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSLGYQVSKPEVIFKLEQGEEPWISERELQRPFCPDWKTRPDIKSWSSQQGVSEVSHSANVWSHATFGDIWGVNTQRHQESWRRHLGPEASSQKKITALEKIAEQNKFGEDSGLSTDLVPQLDVSSSIRPSECKTFGNNLEYNSELVTQSGIPAKKKPYKCDKCRKSFIHRSSLNKHEKIHKDDAYSNGTDQGVPSGRKHHECTDCGKTFLWRTQLTEHQRIHTGEKPFECNVCGKAFRHSSSLGQHENAHTGEKPYQCSLCGKAFQRSSSLVQHQRIHTGEKPYRCNLCGRSFRHSTSLTQHEVTHSGEKPFQCKECGKAFSRCSSLVQHERTHTGEKPFECSICGRAFGQSPSLYKHMRIHKRSKPYQSNNFSIAFEPNIPLTQGESVLTDVKSYHCIDCGKDFSHITDFTEHQRIHAGENSYDSEQALRQQSLSHPREKPYQCNVCGKAFKRSTSFIEHHRIHTGEKPYECNECGEAFSRLSSLTQHERTHTGEKPYECIDCGKAFSQSSSLIQHERTHTGEKPYECNECGRAFRKKTNLHDHQRIHTGEKPYACKECGKNFSRSSALTKHHRIHSRNKL", "text": "FUNCTION: Inhibits the transcriptional repressor activity of REST by inhibiting its binding to DNA, thereby derepressing transcription of REST target genes. SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with REST in the nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MSKIYIDERSNAEIVCEAIKTIGIEGATAAQLTRQLNMEKREVNKALYDLQRSAMVYSSDDIPPRWFMTTEADKPDADAMADVIIDDVSREKSMREDHKSFDDVIPAKKIIDWKGANPVTVINEYCQITRRDWSFRIESVGPSNSPTFYACVDIDGRVFDKADGKSKRDAKNNAAKLAVDKLLGYVIIRF", "text": "FUNCTION: RNA-binding protein that plays a role in the inhibition of multiple cellular antiviral responses activated by double-stranded RNA (dsRNA), such as inhibition of PKR activation, necroptosis, and IFN- mediated antiviral activities (PubMed:1350676, PubMed:1681618, PubMed:18604270, PubMed:24257616, PubMed:25740987). Recognizes and binds Z-RNA structures via its Z-binding domain and dsRNA via its DRBM domain: RNA-binding activity is required to escape host ZBP1-dependent necroptosis (PubMed:29073079, PubMed:34192517). Mechanistically, the Z- binding domain binds Z-RNAs that are produced during vaccinia virus infection, thereby competing with Z-RNA detection by host ZBP1, suppressing ZBP1-dependent necroptosis (PubMed:34192517). Acts as a key inhibitor of the interferon response by blocking the phosphorylation and subsequent activation of IRF3 and IRF7 kinases that are required for interferon-alpha gene expression (PubMed:22419806). Inhibits NF- kappa-B activation and the ubiquitin-like protein ISG15, which is an early antiviral protein (PubMed:18604270, PubMed:24257616). The binding with host ISG15 subsequently blocks host ISGylation (PubMed:18604270, PubMed:24257616). SIMILARITY: Belongs to the orthopoxvirus OPG065 family."}
{"protein": "MRISYTPQQEELRRELRSYFATLMTPERREALSSVQGEYGVGNVYRETIAQMGRDGWLALGWPKEYGGQGRSAMDQLIFTDEAAIAGAPVPFLTINSVAPTIMAYGTDEQKRFFLPRIAAGDLHFSIGYSEPGAGTDLANLRTTAVRDGDDYVVNGQKMWTSLIQYADYVWLAVRTNPESSGAKKHRGISVLIVPTTAEGFSWTPVHTMAGPDTSATYYSDVRVPVANRVGEENAGWKLVTNQLNHERVALVSPAPIFGCLREVREWAQNTKDAGGTRLIDSEWVQLNLARVHAKAEVLKLINWELASSQSGPKDAGPSPADASAAKVFGTELATEAYRLLMEVLGTAATLRQNSPGALLRGRVERMHRACLILTFGGGTNEVQRDIIGMVALGLPRANR", "text": "FUNCTION: Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA (3-OCS-CoA) to yield (24E)-3-oxo-cholest-4,24-dien-26-oyl-CoA (PubMed:26348625, PubMed:26161441). Also able to dehydrogenate steroyl-CoA such as 3-oxo- chol-4-en-24-oyl-CoA (3-OCO-CoA) as well as 3-oxo-4-pregnene-20- carboxyl-CoA (3-OPC-CoA) (PubMed:26161441). It dehydrogenates only (25S)-OCS-CoA diastereomer (Probable). SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MMRIPYRAVVPRATLLHARFSRPPAVPSLTKAFIVSRRTSSHASFIETGHIDVKDDEGLVFVNNIFPSKLQWLLQGPLSGNKTYEEALKRINRPHLAASDPLHIIRRVFPQSLNVDIREVIPRFREGGAFVKYVRKDGVRDNDIVTAVQHHLEHNPIRPWFNPFQQVKVAHVHGRPWIEDLYRIPSQRLRVEFLPGSVDGAATELTTETLYSFFRRYGKLRDIERQPTDSKIAPRYAFVSFTRQKYAVMAKNCMHGFTIPEEEGGGKSGTRIKIKYERKIKFSVIKDWILNHPRIVIPAIAALIAAITVTIFDPIRTFFIEMKIKATLQTEENSVLQWIRNQANKANIIYFGRQRTDPRRLTAIWEDRQGDIKQLQSWLMENAETFIVIHGPRGTGKRELVLDRALENYKYKVVIDCKQIQDAKGDTAKIARAASQVGYRPVFSWMNSMSSFIDLAAQGMIGTKAGFSETLDAQLSKIWQNTATALKRVALSNRKKDDKEAHLSDEEYLEAHPEQRPVVVIDNFLHNATESSVVYDKITEWAAGLTTGNIAHVVFLTTDVSFSKPLSKALPNSVFRTISLGDCSLDVGRKFVLSHLEHGAKDGANSGQNMEEVGDLGTLDSCIEVLGGRVTDLEFMARRIESGETPRAAVNRIIEQSASEILKMFVFDPDIESKQWSHEQAWHLIKTLAHSQDGTLPYNQVLLSDLFKENGETTLRALEQAELIAISSVNGCPDAVKPGKPVYRAVFKRLTENKTLSSRLDLDIVKQLLSSENKSIGKYEQELQVLGSLPKQPRELSARIQWLLQKVASSQNKISQYEHESAILQKVLRREH", "text": "FUNCTION: Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the YME2 family."}
{"protein": "MDTSRVRMLLSLLALLQLVAAGSPPRPDTMPRGCPSYCHCELDGRMLLRVDCSDLGLSELPSNLSVFTSYLDLSMNNISQLPASLLHRLRFLEELRLAGNALTHIPKGAFAGLHSLKVLMLQNNQLRQVPEEALQNLRSLQSLRLDANHISYVPPSCFSGLHSLRHLWLDDNALTDVPVQAFRSLSALQAMTLALNKIHHIADHAFGNLSSLVVLHLHNNRIHSLGKKCFDGLHSLETLDLNYNNLDEFPTAIKTLSNLKELGFHSNNIRSIPERAFVGNPSLITIHFYDNPIQFVGISAFQHLPELRTLTLNGASQITEFPDLTGTATLESLTLTGAKISSLPQTVCDQLPNLQVLDLSYNLLEDLPSLSGCQKLQKIDLRHNEIYEIKGGTFQQLFNLRSLNLARNKIAIIHPNAFSTLPSLIKLDLSSNLLSSFPVTGLHGLTHLKLTGNRALQSLIPSANFPELKIIEMPYAYQCCAFGGCENVYKIPNQWNKDDSSSVDDLRKKDAGLFQVQDERDLEDFLLDFEEDLKVLHSVQCSPPPGPFKPCEHLFGSWLIRIGVWTTAVLALSCNALVAFTVFRTPLYISSIKLLIGVIAVVDILMGVSSAILAVVDTFTFGSFAQHGAWWEGGIGCQIVGFLSIFASESSVFLLTLAALERGFSVKCSSKFEMKAPLSSLKAIILLCVLLALTIATVPLLGGSEYNASPLCLPLPFGEPSTTGYMVALVLLNSLCFLIMTIAYTRLYCSLEKGELENLWDCSMVKHTALLLFTNCILYCPVAFLSFSSLLNLTFISPEVIKFILLVIVPLPACLNPLLYIVFNPHFKEDMGSLGKQTRFWTRAKHPSLLSINSDDVEKRSCDSTQALVSFTHASIAYDLPSDSGSSPAYPMTESCHLSSVAFVPCL", "text": "FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Note=Rapidly and constitutively internalized to the trans-Golgi network at steady state. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSAADMARKNSLINRQLEKEKIDSKKMLKILLLGGPECGKSTIFKQMKIIHMNGFSDLDYVNFRYLIYSNIMQSMDQLLEAAEFFHFPPDDSPSIRRALNHYKSYKVRYSTSEVELNRELADSLSKLYNAEFIKSVLNRKNELKLLDSAVYFLDDIDRISAHEYKPTEMDVLRARVPTTGITEIEFPFKQASLRMVDVGGQRSEQRKWIHCFDNVNGVLFIAAISGYNLYDEDEENRKDDGTPTKTNRLRYSMELFKRIANHQCFSKKTAMILFLNKIDIFKEKIGKYPLTTCFKNYKGVNAFEPACKYVTDRFSRLVSGDIQHEKPLYTHITNATDTRNIDRVFDSCMDVIFKISMEKVGFM", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Mediates the transduction of food and serotonin signals, which modulates the avoidance response to the odorant octanol. Has a role in lifespan to promote longevity. SIMILARITY: Belongs to the G-alpha family."}
{"protein": "MTTVYTLVSWLAILGYWLLIAGVTLRILMKRRAVPSAMAWLLIIYILPLVGIIAYLAVGELHLGKRRAERARAMWPSTAKWLNDLKACKHIFAEENSSVAAPLFKLCERRQGIAGVKGNQLQLMTESDDVMQALIRDIQLARHNIEMVFYIWQPGGMADQVAESLMAAARRGIHCRLMLDSAGSVAFFRSPWPELMRNAGIEVVEALKVNLMRVFLRRMDLRQHRKMIMIDNYIAYTGSMNMVDPRYFKQDAGVGQWIDLMARMEGPIATAMGIIYSCDWEIETGKRILPPPPDVNIMPFEQASGHTIHTIASGPGFPEDLIHQALLTAAYSAREYLIMTTPYFVPSDDLLHAICTAAQRGVDVSIILPRKNDSMLVGWASRAFFTELLAAGVKIYQFEGGLLHTKSVLVDGELSLVGTVNLDMRSLWLNFEITLAIDDKGFGADLAAVQDDYISRSRLLDARLWLKRPLWQRVAERLFYFFSPLL", "text": "FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsA sub-subfamily."}
{"protein": "MSDIRHSLLRRDALSAAKEVLYHLDIYFSSQLQSAPLPIVDKGPVELLEEFVFQVPKERSAQPKRLNSLQELQLLEIMCNYFQEQTKDSVRQIIFSSLFSPQGNKADDSRMSLLGKLVSMAVAVCRIPVLECAASWLQRTPVVYCVRLAKALVDDYCCLVPGSIQTLKQIFSASPRFCCQFITSVTALYDLSSDDLIPPMDLLEMIVTWIFEDPRLILITFLNTPIAANLPIGFLELTPLVGLIRWCVKAPLAYKRKKKPPLSNGHVSNKVTKDPGVGMDRDSHLLYSKLHLSVLQVLMTLQLHLTEKNLYGRLGLILFDHMVPLVEEINRLADELNPLNASQEIELSLDRLAQALQVAMASGALLCTRDDLRTLCSRLPHNNLLQLVISGPVQQSPHAALPPGFYPHIHTPPLGYGAVPAHPAAHPALPTHPGHTFISGVTFPFRPIR", "text": "FUNCTION: Probable component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKVGELNVSEKIKEILRERGIEELYPPQAEALTSGVLEGENLLVAIPTASGKTLIAEIAIANKLLEEGGKAVYIVPLKALAEEKFREFKDWERLGLKVAMATGDYDSKDEWLGKYDIIIATAEKFDSLLRHGSSWIRDVKMLVIDEIHLIGSRDRGATLEFIITQMLGRAQIIGLSATIGNPEELAEWLNAKLIRSDWRPVKLRKGVFYQGFVFWEDGGSERYNSWEELVYDAVKKGKGALVFVNMRRKAEKTALELAKKVKNYLDRKELRELRELAESLEENPTNEKLAKALLSGVAFHHAGLGRDERVLVEDNFRKGLIKVVVATPTLSAGINTPAFRVIIRDTWRYSEFGMERIPVLEVQQMMGRAGRPRYDEVGEAIIVSTTEEPSLVIDHYIKGKPEKLFSQLSNESILRSQILALIATFGYSEFKEIYDFLERTFYAHQGKDPYMLEEKIRRIIYFLLENEFIEVTLEDEIKPLPLGVRTTKLYIDPMTAKIFKDTLPRIEKNPNPLGIFHMISLAPDLTPLSYSKRETSMLEDEYYSLMDRLYFELDYENERKFFRAFKTALVLNAWINEVPEGEIVERFNVEPGDIYRIVETAEWLIYSLGEIAKVLEASQEVVDYVNTLRLRVKHGIREELIPLMELPMVGRKRARALYNAGFKDLESIRNAKPSELLRIEGIGAKIVEGIFKYLGKEVKITERPRKGTLDYFLNP", "text": "FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. SIMILARITY: Belongs to the helicase family. Hel308 subfamily."}
{"protein": "MSTTGTPKTTAEIQQDWDTNPRWKGVTRNFTAQQVSDLQGTVVEEATLARRGSEILWDLVNNEDYINSLGALTGNQAVQQIRAGLQAIYLSGWQVAGDANLSGHTYPDQSLYPANSVPSVVRRINNALLRADEIAKIEGDTSVKNWVAPIVADAEAGFGGALNAYELQKAMIVAGAAGVHWEDQLASEKKCGHLGGKVLIPTQQHIRTLTSARLASDVADVPSVIIARTDAEAATLITSDVDERDREFLDGTRTAEGFFGVKNGIEPCIARAKAYAPYADLIWMETGVPDLEVAKKFSESVRSEFPDQLLAYNWSPSFNWKAHLDDATIAKFQKELGAMGFKFQFITLAGFHSLNYGMFDLAHGYAREGMTAFVDLQEREFKAAEERGFTAIKHQREVGAGYFDRIATTVDPNTSTAALKGSTEEGQFH", "text": "FUNCTION: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family."}
{"protein": "MSSTVSYWILNSTRNSIATLQGGRRLYSRYVSNRNKLKWRLFSRVPPTLNSSPCGGFTLCKAYRHTSTEEDDFHLQLSPEQINEVLRAGETTHKILDLESRVPNSVLRFESNQLAANSPVEDRRGVASCLQTNGLMFGIFDGHGGHACAQAVSERLFYYVAVSLMSHQTLEHMEGAMESMKPLLPILHWLKHPGDSIYKDVTSVHLDHLRVYWQELLDLHMEMGLSIEEALMYSFQRLDSDISLEIQAPLEDEVTRNLSLQVAFSGATACMAHVDGIHLHVANAGDCRAILGVQEDNGMWSCLPLTRDHNAWNQAELSRLKREHPESEDRTIIMEDRLLGVLIPCRAFGDVQLKWSKELQRSILERGFNTEALNIYQFTPPHYYTPPYLTAEPEVTYHRLRPQDKFLVLASDGLWDMLSNEDVVRLVVGHLAEADWHKTDLAQRPANLGLMQSLLLQRKASGLHEADQNAATRLIRHAIGNNEYGEMEAERLAAMLTLPEDLARMYRDDITVTVVYFNSESIGAYYKGG", "text": "FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the PP2C family."}
{"protein": "MWLLLITSVISTFGGAHGLFGKLGPGNPEANMNISQMITYWGYPCQEYEVVTEDGYILGVYRIPHGKNNSENIGKRPVVYLQHGLIASATNWIANLPNNSLAFMLADAGYDVWLGNSRGNTWSRKNVYYSPDSVEFWAFSFDEMAKYDLPATINFIVQKTGQEKIHYVGHSQGTTIGFIAFSTNPTLAKKIKTFYALAPVATVKYTQSPLKKISFIPTFLFKLMFGKKMFLPHTYFDDFLGTEVCSREVLDLLCSNTLFIFCGFDKKNLNVSRFDVYLGHNPAGTSVQDFLHWAQLVRSGKFQAFNWGSPSQNMLHYNQKTPPEYDVSAMTVPVAVWNGGNDILADPQDVAMLLPKLSNLLFHKEILAYNHLDFIWAMDAPQEVYNEMISMMAED", "text": "FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:3839077). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MNNMNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGDKYGDGITLIKYIKRHFPSLSIIVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQKGKKFTPESVSRLLEKISAGGYGDKRLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDIALLNYLSSVTLSPTDKE", "text": "FUNCTION: Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. SIMILARITY: Belongs to the RcsB family."}
{"protein": "MATYSFRQTTSSVAGGPCGRSLRLGGGSFRAPSIHGGSGGRGVSVSSARFVSSGLGSGLGGGYGGAFSSSFSAGFGGGYGGGLGSGDGLLSGNEKTTMQNLNDRLASYLDKVRALEEANSDLETKIREWYLKQGPGPARDYSPYYKAIEDLRDQILAATIDNSKVVLQIDNARLAADDFKTKFETEQALRMSVEADINGLRRVLDELTLARTDLELQIENLKEELAYLKKNHEEEMSALGGQVASQVSVEVDSAPGIDLSKILADMRDQYEHMAEKNRKDAEAWFHSKTEELNRELAVNTEQLQSSKSEVTDLRRTLQGLEIELQSQLSMKGALESTLADTEGRYGAQLAQIQDMIGSIEAQLAELRADMERQNSEYKMLMDIKTRLEQEIATYRQLLEGQESQLFGSLSGSPDKRDKPADGK", "text": "FUNCTION: Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle (By similarity). SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MLKMEQSAPPRYEEDWADVYEFIERDSSRKNVPAIEAIERRLAFSPLITPNPGAKQFAPIHVPGREPPRMLLPPTPHFQAPFSPHPPPVQQVPSYSPPHAPPSYETYPEVYYPPHIICNPYDVPTTSDRNPPYYTEVTTVSAVTLHSMTPPTHKIETPPSSPENSFGPLASQLPAIKMEIPMHPLPHNGELDSTRSSPSSTTSSERSPLQRKSRIESNKRNPTDKKFVVHACTYPGCFKKYSKSSHLKAHERTHSGEKPFVCKWQNCSWKFARSDELTRHMRKHTGDKPFRCSLCDRNFARSDHLSLHMKRHSTI", "text": "FUNCTION: Probable transcription factor which regulates lipid catabolism, storage, and secretion, probably by modulating genes involved in fatty acid desaturation and beta-oxidation, and lipoprotein assembly and secretion (PubMed:19427851, PubMed:23639358). Involved in reproduction, perhaps indirectly (PubMed:19427851, PubMed:23639358). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MKVASSSAAATAGPSCSLKAGRTAGEVVLGLSEQSVAISRCAGTRLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVATAGGRGLPVRAPLSTLNGEISALAAEVRSESEYYIILLWETKATGGGCPPYFSGA", "text": "FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MPFGCLTLGEKKDYNSPSEVTDKYDLGQVVKSEEFCEIFRAKDRNTLKMYTCKKFNKKDGRKVRKAAKNEIMILKMVKHHNILQLVDAFETKKEYFIFLELATGREVFDWILDQGYYSERDTSNVMRQVLEAVAYLHSLKIVHRNLKNLVYFNRLKHSKIVISDFQLAKLENGLIKDPCGTPEYLAPEVIGRQRYGRPVDCWAIGVIMYILLSGNPPFYDDGDEEDSDSRDKNLFLKILSGDYEFDSPYWDDISDSAKTLVASLMEVDQDQRLTAQEAIAHEWISGNAASDKNIKDGVCAQIEKNFAKAKWKKAVRVTTLMKRLRASEQGDTGASGLAAGATGGPPDPNMPGGSLLAASIKTALSEKAADAQTSTIPSLPQPPAARPEEQQQAQQQQQAQQQQQARCNGDVPQMLPQRKGY", "text": "FUNCTION: Does not appear to have detectable kinase activity. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein. Note=May be associated with vesicular structures. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
{"protein": "MAPRLGIFLLWAGVSVFLPLDPVNGDQHLPGRFLTPAITSDDKCVFPFIYKGNLYFDCTLHDSTYYWCSVTTYYMKRWRYCRSTDYARCALPFIFRGKEYDSCIKEGSVFSKYWCPVTPNYDQDRAWRYC", "text": "FUNCTION: May form a complex with spermadhesin AQN-1 which possesses phosphorylcholine-binding activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the seminal plasma protein family."}
{"protein": "MSLPAISLYTSPPPGAVYSSEFDPSSRGSSPPCSTAPPSTSHRPPAAAGGLSCLFSSPAAAASPPRAPPHDELGALWQDRSDEPAFAGGGGGYSSSPLKWRDLHHHHHHSPVSVFQGPSSSPAASRSPPASWLAGRDRDRERLFAGFVRNALGSCVDYAPALSPRSEVGGGELAFELDENLAEASPACEPCARELLAGAQARHRIFHEELVVKTFFEAEKAHRGQTRASGDPYLQHCVETAVLLANIGANSTVVSAGLLHDTIDDSFIDYDHIFHMFGAGVADLVEGVSKLSHLSKLARDNNTASRIVEADRLHTMLLAMADARAVLIKLADRVHNMKTLEALPLGKQQRFAKETMEIFVPLANRLGIASWKDQLENLCFKHLNPEEHKDLSSKLTKSFDEVLITSAVDKLDRGLRDAGLSYHNLSGRHKSLYSIHNKMLKKNLTMDEIHDIHGLRLVFEKEEDCYRALDVVHELWPQVPGRFKDYISRPKLNGYRSLHTVVMSENVHPFEVQIRTKEMHLQAEYGFAAHWRYKEGTCRHSFVLQMVEWARWVLTWQCEAMNKERPASLGDSDAIRPPCPFPMHSEDCPYSYTRQCDHDGPIFVILLEHDKMSVQEFQANSTVMNLMDRVGTNTPRWSPYRIPMKEDLRPKVNHEPISDLNRKLSMGDVVELTPALPHESLPNYREEIQRMYDRGGFALATRGGSSRR", "text": "FUNCTION: Probable ppGpp (guanosine 3'-diphosphate 5'-diphosphate) synthetase that may be involved in a rapid plant ppGpp-mediated response to pathogens and other stresses. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RelA/SpoT family."}
{"protein": "MADKGSGGSRLPLALPPASQGCSSGGSGSSAGGSGNPRPPRNLQGLLQMAITAGSQEPDPPPEPMSEERRQWLQEAMSAAFRGQREEVEQMKNCLRVLSQATPAMAGEAELATDQQEREGALELLADLCENMDNAADFCQLSGMHLLVGRYLEAGAAGLRWRAAQLIGTCSQNVAAIQEQVLGLGALRKLLRLLDRDSCDTVRVKALFAISCLVREQEAGLLQFLRLDGFSVLMRAMQQQVQKLKVKSAFLLQNLLVGHPEHKGTLCSMGMVQQLVALVRTEHSPFHEHVLGALCSLVTDFPQGVRECREPELGLEELLRHRCQLLQQREEYQEELEFCEKLLQTCFSSPTDDSMDR", "text": "FUNCTION: Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of target proteins (By similarity)."}
{"protein": "MINNVSSLFPTVNRNITAVYKKSSFSVSPQKITLNPVKISSPFSPSSSSISATTLFRAPNAHSASFHRQSTAESSLHQQLPNVRQRLIQHLAEHGIXPARSMAEHIPPAPKWPAPPPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPXWXAPTPPVQNEQSRPLPDVAQRLMQHLAEHGIZPARSMAEHIPPAPNWPAPPPPVQNEQSRPLPDVAQRLXQHLAEHGIQPARNMAEHIPPAPNWPAPXXPVXNEQSRPLXDVAXRLMQHLAEHGIQPARNMAEHIPPAPNWXAPTPPVQNEQSRPLPDVAQRLMQHLAEHGINTSKRS", "text": "FUNCTION: Required for efficient pedestal formation in host epithelial cells during infection. Acts as an intermediate between Tir (via host BAIAP2) and host WASL/N-WASP. Directly binds and activates WASL/N-WASP, which stimulates actin polymerization and leads to the formation of actin pedestals at the sites of bacterial adhesion. SUBCELLULAR LOCATION: Secreted Host cytoplasm Note=Secreted via the type III secretion system (TTSS) (PubMed:15527496, PubMed:15296718). In host cells, localizes to the tip of the actin pedestal (PubMed:15527496, PubMed:15296718). SIMILARITY: Belongs to the EspF(U)/TccP family."}
{"protein": "MEMEEAQEMSQMPGRDSPPPNDVSEENDEAMPIPEDLSASSNLQHNNRGDKEGLACNIKVEARCDEENGLAIDMMMNGEEEEECAEDLRVLDASGAKVNGSHAGGPDSKGPYSSAGGIRLPNGKLKCDICGIVCIGPNVLMVHKRSHTGERPFQCTQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALSGHLRTHSVGKPHKCAYCGRSYKQRSSLEEHKERCHNYLQCMGLQNSIYTVVKEESNQNEQREDLSQMGSKRALVLDRLANNVAKRKSTMPQKFVGEKRFSNISFEGGPGELMQPHVIDQAINSAINYLGAESLRPLIQTSPTSSDMGVMGSMYPLHKPPAEGHGLSAKDSAAENLLLLAKSKSASSEKDGSPSHSGQDSTDTESNNEEKAGVGASGLIYLTNHITSGVRNGVLPLVKEEQQRQYEAMRASIEIASEGFKVLSGEGEQVRAYRCEHCRILFLDHVMYTIHMGCHGFRDPFECNLCGHRSQDRYEFSSHMTRGEHRY", "text": "FUNCTION: Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Functions in the specification and the maturation of the T-lymphocyte. Also interacts with a critical control element in the TDT (terminal deoxynucleotidyltransferase) promoter as well as with the promoters for other genes expressed during early stages of B- and T- cell development. Function is isoform-specific and is modulated by dominant-negative inactive isoforms (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family."}
{"protein": "MRIAVICFCLLGMAYALPVKHADSGSSEEKQLYHKHPDALATWLNPDPSQKQNLLTPQNAMSSEEKDDLKQETLPSKSIESHDHMDDIDEDEDDDHVDNRDSNESDDADHPDDSHHSDESHQSDESDEVTVYPTEDAATTVFTEVVPTVETYDGRGDSVAYRLKRSKSKMFHVSNAQYPGASEEDLSSHVDSEDLDDTPRAIPVAQHLNVPSDWDSQEKDSHDVSQVDDHSVETQSHEQARQYKREANDNSVEHSHSIDSQESSKVSQESQSREFRSHEDKLAIEPKSEEDEEHRQLRVSHELDSTSSEIN", "text": "FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity. FUNCTION: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the osteopontin family."}
{"protein": "MSETFLRPKVSSTKVTDWVAPAFDDFEANTAITTITASSLTFSNSSHRRKYLPSTLESNRLSARKRGRLSLEQTHGLETSRERLSDNEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKQGGSVLLITGPPGCGKTTTIKILSKELGIQVQEWVNPILPDFQKDDYKELLSLESNFSVVPYQSQIAVFNDFLLRATKYSKLQMLGDDLTTDKKIILVEELPNQFYRDPNALHEILRKHVQIGRCPLVFIVSDSVSGDNNQRLLFPRNIQEECSVSNISFNPVAPTIMMKFLNRIVTIEASKNGEKIIVPNKTSLELLCQGCSGDIRSAINSLQFSSSKGENSSWSKKKRMSLKSDAAISKSKQKKKHNSTLENQEIQAIGGKDVSLFLFRALGKILYCKRAPLTELDSPRLPAHLSEHDRDTLLVQPEEIVEMSHMPGDFFNLYLHQNYIDFFAEVDDLVPASEFLSFADILGGDWNTRSLLREYSTSVATRGVMHSNKARGFAHCQGGSSFRPLHKPQWFLIQKKYRENCLAAKALFVDFCLPALCLQTQLLPYLALLTIPMRNKAQISFIQDVGRLPLKRSFGRLKMEALTDRELGLIDPDSGDESPHSGGQPAQEAPGEPAQAAQNADPETWSLPLSQNSGSDLPASQPQPFSSKVDMEEEEEEEEDIIIEDYDSEET", "text": "FUNCTION: Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination (By similarity). Essential for embryonic development. May be involved in homologous recombination. SUBCELLULAR LOCATION: Nucleus Note=Phosphorylated form redistributes to discrete nuclear foci upon DNA damage. SIMILARITY: Belongs to the rad17/RAD24 family."}
{"protein": "MNPIINFILLSSMIAGTVLTMTSHHWVSAWLGLELNTLAIIPIISKTHHPRATEASTKYFLIQAASSALMLFAGIINAHLYGTWDITQISNNPTKILLTAALATKLGLAPIHFWLPEILQGVPMLTALIITTWQKIAPMALLITTWNTIPTPMTLTMGFLSVIIGGLGGLNQTQLRKMMAFSSIAHLGWMIVIITITPSLTLFNLVLYITFTSSTMLIMHLTMSKTLQNAMLMSSHSSTTANLFLLSLLSLGGLPPLSGFSPKWLILQELITHNLVPLATTMAITTLFSLMFYLRTTYISAMTLPPSTTPIKNIWRLKPNSSTTMLSMFSLATLFLLPITPTMTQ", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."}
{"protein": "MDRTETRFRKRGQITGKITTSRQPHPQNEQSPQRSTSGYPLQEVVDDEMLGPSAPGVDPSPPCRSLGWKRKREWSDESEEEPEKELAPEPEETWVVEMLCGLKMKLKQQRVSPILPEHHKDFNSQLAPGVDPSPPHRSFCWKRKMEWWDESEESLEEEPRKVLAPEPEEIWVAEMLCGLKMKLKRRRVSLVLPEHHEAFNRLLEDPVIKRFLAWDKDLRVSDKYLLAMVIAYFSRAGFPSWQYQRIHFFLALYLANDMEEDDEDSKQNIFHFLYRKNRSRIPLLRKPWFQLGHSMNPRARKNRSRIPLLRKRRFQLYRSTNPRARKNRSRIPLLRKRRFQLYRSMNSRARKNRSQIVLFQKRRFHFFCSMSCRAWVSPEELEEIQAYDPEHWVWARDRAHLS", "text": "SIMILARITY: Belongs to the Speedy/Ringo family."}
{"protein": "MKVPFVNFMISSFPAAVLVGAVVGFMIGRKYSVADASRGYSSKNANKASNPEKESPVSVSNDEDSESETELLDMLKGNSSLAALALAEGQTKMVLVVRTDLGMTKGKIAAQCAHAALACYKIASAVDPDLVRIWENAGQAKITLQAQTEETLELLQAQAMSLGLCARVIHDAGRTQIASGSATVLGIGPGPVSVINEVTGSLKLF", "text": "FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. SIMILARITY: Belongs to the PTH2 family."}
{"protein": "MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRTALAAERKFFLSHPAYRHIADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAVPNQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHYELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD", "text": "FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. Regulates maturation of apoptotic cell corpse- containing phagosomes by recruiting PIK3C3 to the phagosome membrane. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cell junction Membrane, clathrin-coated pit Postsynaptic density Synapse Midbody Cell projection, phagocytic cup Cytoplasmic vesicle, phagosome membrane; Peripheral membrane protein Note=Colocalizes with CTTN at the basis of filopodia in hippocampus neuron growth zones. Microtubule- associated. Also found in the postsynaptic density of neuronal cells. Co-localizes with PIK3C3 and RAB5A to the nascent phagosome. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MNITWNWYEQLESAHARAFTVAKATKAEVLDTIRWATEQAIANGTGEREYIKKLEPMLKELGWWGKAKDENGNEVQLGSPRRLRTILRTNKITAYHAARYAQQMENVDEQPYWRYVAVNDSRTRASHLALHGKIYRADDPIWQTMYPPNDWGCRCRVEALSEYAVQSRGLKISSSDGEMEMEEAVVGIDKDTGEEIRTTVSKIKTDQGEMKVGAGWNYNVGSAAFGTDVAVLRKLQQVKNRELRQQTIQAINNSEARHKAFADWVLANLGKRGASARYMSAGLVTTEIAEAVTEITQGGKNAELVLVMSEKRLAHANSDKHHEGGVGLTAEEYASISRIVANPSLVLWDTLEGHNNLIYINQERTIQVIVDVPNKHSIKPKEKVDAIINAYKVDMNNVKRQLSGGNYVLLKGKL", "text": "FUNCTION: Involved in virion morphogenesis. SIMILARITY: To phage Mu protein F."}
{"protein": "MSFAAGLLNATVQAATVLLLAGLGELISERAGVLNLGVEGMMLVGALGGFVVTAVTGNYWLGFGVGIACGMALAAVHAFLCISLKSNQVISGVMLTLLGTGLTTFFGSGWVQESITGFPQMTFPIVGRYLVHLPLVGEAFFRSTATDYLALLAVPVVWFFLYRSNLGLEIIAVGEDPEMADTMGVPVFKFRYLAVIIGGGFAGAAGAHLSLAFSQLWVPGMTVGRGWIAVALVVFAQWRPSRMLVGAYLFGLLDALQLRSQSLSLALDPNAPLAGVLNPLVNTLMNPQIMSTYPYLTTIAVLSYAVIRTESVRLAVPSALLQSYNREMD", "text": "FUNCTION: Part of an ABC transporter complex involved in glucose import (Potential). Responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family."}
{"protein": "MNRQQNDLILQFAAVIIFFMVMVFGFSLFLAGHYTPGGGFVGGLLFASSLVIITIAFDIETMRKIFPLDFKILIGIGLVFCIATPIASWFLGKNFFTHVTFDIPLFILEPVHMTTAVFFDFGVLCAVVGTVMTIIISIGENE", "text": "FUNCTION: Mnh complex is a Na(+)Li(+)/H(+) antiporter involved in Na(+) and/or Li(+) excretion. Na(+)/H(+) antiport consumes a transmembrane electrical potential, and is thus inferred to be electrogenic. Does not transport K(+), Ca(2+) or Mg(2+). FUNCTION: Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit B family."}
{"protein": "GDDVKSACCDTCLCTKSNPPTCRCVDVGETCHSACLSCICAYSYPPKCQCFDTQKFCYRACHNSEKEEVIKG", "text": "FUNCTION: Inhibits trypsin (IC(50)=0.9 nM) and alpha-chymotrypsin (IC(50)=1.1 nM). SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor family."}
{"protein": "MVAFTPEEVRNLMGKPSNVRNMSVIAHVDHGKSTLTDSLVQKAGIISAAKAGDARFMDTRADEQERGVTIKSTAISLFAEMTDDDMKDMKEPADGTDFLVNLIDSPGHVDFSSEVTAALRVTDGALVVVDTIEGVCVQTETVLRQALGERIRPVVVVNKVDRALLELQISQEELYQNFARVVESVNVVISTYYDKVLGDCQVFPDKGTVAFASGLHGWAFTVRQFANRYAKKFGIDRNKMMQRLWGENYFNPKTKKWSKSATDANGNSNQRAFNMFILDPIYRIFDAVMNSRKDEVFTLLSKLEVTIKPDEKELEGKALLKVVMRKFLPAADALMEMIVLHLPSPKTAQQYRAETLYEGPMDDECAVGIRNCDANAPLMIYVSKMVPTSDRGRFYAFGRVFSGTVRSGLKVRIQGPNYVPGKKDDLFIKAIQRTVLMMGSRIEPIEDCPAGNIIGLVGVDQFLVKSGTLTTSEVAHNMKVMKFSVSPVVQVAVEVKNGNDLPKLVEGLKRLSKSDPCVLCTTSESGEHIVAGAGELHLEICLKDLQEDHAGIPLKISPPVVSYRESVSEPSSMTALSKSPNKHNRIFMTAEPMSEELSVAIETGHVNPRDDFKVRARIMADEFGWDVTDARKIWCFGPDTTGANVVVDQTKAVAYLNEIKDSVVAAFAWASKEGPMFEENLRSCRFNILDVVLHADAIHRGGGQIIPTARRVVYASTLLASPIIQEPVFLVEIQVSENAMGGIYSVLNKKRGHVFSEEQRVGTPLYNIKAYLPVNESFGFTGELRQATAGQAFPQLVFDHWSPMSGDPLDPTSKPGQIVCEARKRKGLKENVPDYTEYYDRL", "text": "FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MGLPPLLSLPSNSAPRSLGRVETPPEVVDFMVSLAEAPRGGRVLEPACAHGPFLRAFREAHGTAYRFVGVEIDPKALDLPPWAEGILADFLLWEPGEAFDLILGNPPYGIVGEASKYPIHVFKAVKDLYKKAFSTWKGKYNLYGAFLEKAVRLLKPGGVLVFVVPATWLVLEDFALLREFLAREGKTSVYYLGEVFPQKKVSAVVIRFQKSGKGLSLWDTQESESGFTPILWAEYPHWEGEIIRFETEETRKLEISGMPLGDLFHIRFAARSPEFKKHPAVRKEPGPGLVPVLTGRNLKPGWVDYEKNHSGLWMPKERAKELRDFYATPHLVVAHTKGTRVVAAWDERAYPWREEFHLLPKEGVRLDPSSLVQWLNSEAMQKHVRTLYRDFVPHLTLRMLERLPVRREYGFHTSPESARNF", "text": "FUNCTION: A gamma subtype methylase that recognizes the double-stranded sequence 5'-TCGA-3', methylates A-4 on both strands and protects the DNA from cleavage by the TaqI endonuclease. SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MEKFAPEFVGEDANKKAEEFLKHRSFPSEKPLAGIPNTATHVTKYNMPPILRSSFKLPSPRVAANLTEPSAPPTTPPPTPPQNKEEQPKESDVDIETMHVCKVPDNPEHSKKPCCSDDTDTKKTRKPMVTFVEPEEKFVGLGASLYRETMQTFAADGYDEESNLSFEETNQEPGSSSVEQRLDRIEEKLSYIIGLLNTIMVATAGPTTARDEIRDALIGTREELIEMIKSDILTVNDRIVAMEKLRDEECSRADTDDGSACYLTDRARILDKIVSSNAEEAKEDLDVDDIMGINF", "text": "FUNCTION: Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins. Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex. Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA. Acts as a chaperone for neo- synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs. Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Localizes in cytoplasmic inclusion bodies. SIMILARITY: Belongs to the pneumoviridae phosphoprotein P family."}
{"protein": "AAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEITAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGG", "text": "FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 14-3-3 family."}
{"protein": "MSSFKEFKIKWGMVIDLDKCTGCGACMVACQAENNIAPQPDASNKLKSLNWLVVYELNNGKPFPEHDVAYLPRPCMQCGKPSCVSVCPVVATDKNEEGGIVSQVYPRCIGCRYCMASCPYHARYFNWFDPTWPEGMDKTLTPDVSVRPRGVVEKCTFCHHRFMQAKDKARVEGRDPSALRDGDYVTSCTEACPNGAIIFGDFNNPEHRVHELHKSKYAFRLLERLGTDPQVYYLSRREWVRRLGDNYLEHEKVKG", "text": "FUNCTION: Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. QrcC is an electron- transferring subunit; its cubane iron sulfur clusters form a pathway for electron transfer between the hemes of QrcA and the membrane quinone pool. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MRSEVPSSTSPSFLSPPFIHLPLLSLSSPTPLPHSSSSTFSLFSTMAASQIGLVGLAVMGQNLALNIAEKGFPISVYNRTASKVDETLDRAKSEGDLPLSGHYTPRDFVLSIERPRSIVILVKAGSPVDQTIASLASFMEPGDTIIDGGNEWYQNTERRLSDAHSNGLLYLGMGVSGGEEGARFGPSLMPGGDFQAYDNIQHILKKVAAQVDDGPCVTYIGEGGSGNFVKMVHNGIEYGDMQLISEAYDVLKNVGGLSNEELGQIFDEWNKSELESFLVEITADIFKVKDDLADGGLVDKILDKTGMKGTGKWTVQQAAELSVAAPTIAASLDCRYLSGLKEERENAAKILEAAGMKEEVNAIRGGVDKKRLIDDVRQALYASKICSYAQGMNLLRAKSAEMGWDLNLGELARIWKGGCIIRAVFLDSIKQAYQRNPNLASLVVDPEFAKEMVQRQAAWRRVVGLAVSAGISTPGMCASLAYFDTYRRARLPANLVQAQRDYFGAHTYERVDLPGSYHTEWSKLARKSDPNVAAALH", "text": "FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family."}
{"protein": "MSPVAIIACVCLAVTLTSISPSEAIVPTRELENVFLGRCKDYEITRYLDILPRVRSDCSALWKDFFKAFSFKNPCDLDLGSYKDFFTSAQQQLPKNKVMFWSGVYDEAHDYANTGRKYITLEDTLPGYMLNSLVWCGQRANPGFNEKVCPDFKTCPVQARESFWGMASSSYAHSAEGEVTYMVDGSNPKVPAYRPDSFFGKYELPNLTNKVTRVKVIVLHRLGEKIIEKCGAGSLLDLEKLVKAKHFAFDCVENPRAVLFLLCSDNPNARECRLAKRFYRIA", "text": "FUNCTION: Synthesizes cyclic ADP-ribose (cADPR), a second messenger for calcium mobilization from endoplasmic reticulum; ADP-ribose is a minor product (PubMed:1650254, PubMed:10861229). Synthesizes the Ca(2+) mobilizer nicotinate-adenine dinucleotide phosphate from 2'-phospho- cADPR and nicotinic acid as well as from NADP(+) and nicotinic acid; with NADP(+) as substrate preferentially catalyzes NADP(+) hydrolysis rather than NAADP(+) synthesis, about 70-fold better at pH 7.4 (PubMed:11829748, PubMed:16690024). Has cADPR hydrolase activity at very high enzyme concentrations, which is probably not physiological (PubMed:10861229). The conversion of NAD(+) into ADP-ribose is also only observed at high enzyme concentrations and results from the hydrolysis of cADP-ribose (PubMed:10861229). SUBCELLULAR LOCATION: Cytoplasmic vesicle Note=Localized to vesicles or granules within ova of all stages. SIMILARITY: Belongs to the ADP-ribosyl cyclase family."}
{"protein": "MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGTLLVIFCVELACGVWTYEQEVMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNYFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMLSLKNDASQHLSCHSVELLKPSLSRIFEHTSMANSFNTHFEMEEL", "text": "FUNCTION: Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt- dependent activation of FZD4, suggesting the existence of a Wnt- independent signaling that also promote accumulation the beta-catenin (CTNNB1). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family."}
{"protein": "MRNVKGLFSYMTKTKSFYISIIVIIFIIFIVNRMGPRNYNYKQIGTEINCVKHKVDEQRYLLFPMITILYKYGLGNQLFEVFSLLGSAQTLNRTAIFNADDDILQSKLDLLQKQVPQVAARIISIPIEIAESTRYLFLPACCHYQFPSLFSCERSKFLVIDGQYFQSFKYFSAIDSLIRKLLKPPIDEEIILKKMIGRKDELRFKNCVHIRRGDYVNDFDHAETSSYFTIRAIDYVHTLHPGLVYLISDDPKWVRKQIAEHLDYHDDVKIMETPINAAIRDLYFSQAHCDSVLITAPSSTFGWWIGYMSKNQSNVYYRDIQETDDMVKYKMVEEDFFPPTWKKLGMSRNGSIISK", "text": "FUNCTION: Selectively catalyzes the addition of fucose in alpha 1-2 linkage to Gal-beta-(1->4)-Xyl-beta-R, Gal-beta-(1->6)-GlcNAc-R, Gal- beta-(1->3)-Gal-beta-(1->4)-Glc and Gal-beta-(1->3)-Gal-beta-(1->4)- Xyl-R acceptors but not Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta- (1->4)-Glc. Unlike in mammals, unable to fucosylate Gal-beta-(1->4)- Glc-beta-R. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 11 family."}
{"protein": "MPKAPKTKLHHAPLYKDIAESSESGVLRQKPSKQKKSKESNTGNGFLDAKTSKKILQLAREQKEELDEEENGKPSQISAFISNGHQKDTLENPAIESSYEESEHARNVSDSESITSQEEEEYEELEIDDADRDLFDRFLPTVSGEEGDLTEEKTTSLSDLIMQKINEAEARARGEYIPSAEEEENALPPLPPKVIEVYSKVGVLLSKYRSGKIPKAFKIIPTLSNWEDILYLTRPDMWTPHACYEATRIFISNLKPVQAQHFLTVIILERVRDDIRENKKLNYHLYMALKKALYKPSSWFKGFLFPLVQENCTLREAAIIGSILQKVSVPVLHSAAALLRLTEFDLSGATSVFIRILLDKKYALPYKVLDSLVFYFMRWKSLERPLAVLEHQSMLVFAQRYKFDITPEQKDALLEVVRLKGHYSIGPEIRRELLNSASRGEEIPVEMEY", "text": "SIMILARITY: Belongs to the bystin family."}
{"protein": "MAILPLLLCLLPLAPASSPPQSATPSPCPRRCRCQTQSLPLSVLCPGAGLLFVPPSLDRRAAELRLADNFIASVRRRDLANMTGLLHLSLSRNTIRHVAAGAFADLRALRALHLDGNRLTSLGEGQLRGLVNLRHLILSNNQLAALAAGALDDCAETLEDLDLSYNNLEQLPWEALGRLGNVNTLGLDHNLLASVPAGAFSRLHKLARLDMTSNRLTTIPPDPLFSRLPLLARPRGSPASALVLAFGGNPLHCNCELVWLRRLAREDDLEACASPPALGGRYFWAVGEEEFVCEPPVVTHRSPPLAVPAGRPAALRCRAVGDPEPRVRWVSPQGRLLGNSSRARAFPNGTLELLVTEPGDGGIFTCIAANAAGEATAAVELTVGPPPPPQLANSTSCDPPRDGDPDALTPPSAASASAKVADTGPPTDRGVQVTEHGATAALVQWPDQRPIPGIRMYQIQYNSSADDILVYRMIPAESRSFLLTDLASGRTYDLCVLAVYEDSATGLTATRPVGCARFSTEPALRPCGAPHAPFLGGTMIIALGGVIVASVLVFIFVLLMRYKVHGGQPPGKAKIPAPVSSVCSQTNGALGPTPTPAPPAPEPAALRAHTVVQLDCEPWGPGHEPVGP", "text": "FUNCTION: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon Cell projection, dendrite Synapse Presynaptic cell membrane Postsynaptic cell membrane. SIMILARITY: Belongs to the LRFN family."}
{"protein": "MATQEAGKLEWRISVDNGTTERLVPRSGLSKRIFLWLKDLVMKVIMERVAKFMRKAWRIGADDPAKVVHCLKVGLALSLVSIFYYMRPLYDGVGGNAMWAIMTVVVVFESNVGATFCKCVNRVVATILAGSLGIAVHWVATQSGKAEVFVIGCSVFLFAFAATYSRFVPSFKARFDYGAMIFILTFSLVSVGGYRVDKLVELAQQRVSTIAIGTSICIIITVFFCPIWAGSQLHRLIERNLEKLADSLDGCVAEYFKENEVSTNRNEDENTNMKLQGFKCVLNSKGTEEAMPLIRFSGFSFSQANLARWEPAHGSFNFRHPWKLYVKIGAAMRRCAYCLENLSICINYETEAPDQVKNHFGEACMKLSSASSKILRELADMMKNTRKSSKMDFLVFDMNSAVQELQETLKNVPIETNKPEEVPSEEENKVDSEERTTSMSLHEVLPVATLVSLLIENAARIQTAVEAVDELANLADFEQDSKKKTGDNNTKQPPLSS", "text": "FUNCTION: Malate transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic acid exporter (TC 2.A.85) family."}
{"protein": "MEPPAISQQSTPTAPGGTQGTRKLRESCISCSRSKVKCNKEKPTCSRCVRRGLPCEYMVSRRTGRTRVIGVEQPKTAPSPTTPTNTTAATTATKAGPPVTTDSAVHTPVITTAPSPKPVQIQSPPAEPDLWGAILSPNTSTSTDLSSLLSVNTNFSQLFASLSPSLLEGMDGMDAEMHAPELGALSVADPSSSMMQGLEAPNAAQPPSSNTTSHSYCLSICLDTLMRLFPNAGANCERPGHESNPGKLFTIESVIEDNKQILDTAQTILACRCAEDEYVVTLVSLIVFKVLGWYVAAARDRSSDPGREEDFNWSTAQDSRRGSVSSFEEQVLHLPTVVGSYCIDGHHQSRMAAQLVLSELYRVQRLVTQVSRRLESIRRRSSSSSSSASSNTTDSDGGMSTPLSSTTLVHLEDDLRKRLRAVSSETISILRHA", "text": "FUNCTION: Transcription factor; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646, PubMed:8662194). Binds to the palindromic sequence 5'-TCG(N5)CGA-3'found in the promoter regions of several sterigmatocystin cluster genes to induce their expression (PubMed:9680223). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLRNKSQKELLHLSRQLIQPLLPNFHKGQAGKIVVIGGNEDYTGAPFFASHSAALVGADLSHVICEKAAGPVIKSYSPDLMIHPYLMDLDNPHLNLNNSELEKLKNLPIDEIIKTNDNAVLNKLIDELILPKVTSLLNRIDIVVVGPGFGRDPLMLKSLIRIIEEVKVLNLPIILDADSLYLVSLSPKIIANYPKAIITPNVVEFQRIAKALSIDVDLSESNKDKLIDQTIEVSRKLGDIIVFRKGEHDLIVKSSKFLINEITGSNKRVGGQGDTLTGAIATLVNWSNNYILRLWDNQVDLDQEDANLLACFAASSVVRNASSKAFNKYGRSMQTSNVHEYLHESFTELFGDSIFRTSNI", "text": "FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NnrD/CARKD family."}
{"protein": "MDAIKKKMVAMKMEKKNALDRAEQLEQKLRETEEAKAKIEDDYNSLVKKNIQTENDYDNCNTQLQDVQAKYERAEKQIQEHEQEIQSLTRKISLLEEGIMKAEERFTTASGKLEEASKAADESERNRKVLENLNSGNDERIDQLEKQLTEAKWIAEEADKKYEEAARKLAITEVDLERAEARLEAAEAKVIDLEEQLTVVGANIKTLQVQNDQASQREDSYEETIRDLTNRLKDAENRATEAERTVSKLQKEVDRLEDELLTEKEKYKAISDELDATFAELAGY", "text": "FUNCTION: Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. SIMILARITY: Belongs to the tropomyosin family."}
{"protein": "MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTRKDEQERGITIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQTFARTVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKAKMMDRLWGDSFFNPKTKKWTNKDTDAEGKPLERAFNMFILDPIFRLFTAIMNFKKDEIPVLLEKLEIVLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGPADDANCIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVPGKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTSETAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEICLQDLEHDHAGVPLKISPPVVAYRETVESESSQTALSKSPNKHNRIYLKAEPIDEEVSLAIENGIINPRDDFKARARIMADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIKDSVVAAFQWATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLADPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGMKEEVPGWQEYYDKL", "text": "FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:16950777, PubMed:29069440, PubMed:14976550, PubMed:17082187). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site- bound deacylated tRNA move to the P and E sites, respectively (PubMed:16950777, PubMed:14976550, PubMed:17082187). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:16950777, PubMed:14976550, PubMed:17082187). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MPHRNDRRKSASKAPNAIIHGRVASKKTIKKQLRNGKYSLKRLAEKGIHLDDIAMEIDNASKKNISKDKSLNENLFGKTEAGKQKDFMNIEPTCKGTILGAPPAL", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the ALB1 family."}
{"protein": "MTKPSVHEHPGVLADNGLCEPKTPAGRRLLDLLERYLPALEAESRDNDREATLPVHLFDRMRKEGVLGATVPEDLGGLGVHSLHDVALALARIAGRDAGVALALHMQFSRGLTLDFEWRHGAPSTRPLAEDLLRQMGAGEAVICGAVKDVRGTTVLTRATDGSYRLNGRKTLVSMAGIATHYVVSTRLEEAGAPVRLAAPVVARTTPGLTVLDNWDGMGMRSSGSVDIVFDGCPVDRDRVLPRGEPGVRDDAALAGQTVSSIAMLGIYVGIAEAARRIALTELRRRGGAPAGVRTTVAEIDARLFALHTAVASALTTADRLADDLSGDLAARGRAMMTPFQYAKLLVNRHSVGVVDDCLMLVGGAGYSNSHPLARLYRDVRAGGFMHPYNFTDGVDYLSEVALGR", "text": "FUNCTION: Nitrososynthase involved in the biosynthesis of baumycin (PubMed:23885759). Catalyzes the double-oxidation of TDP-L-epi- vancosamine to TDP-L-epi-vancosonitrose (PubMed:23885759). The rapid turnover of TDP-L-epi-vancosamine suggests that this compound, or a closely related analog, is the natural substrate for DnmZ (PubMed:23885759). Can also catalyze the double-oxidation of TDP-L- evernosamine to TDP-L-evernitrosose (PubMed:23885759). SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MKHNNVIPSSHFRKHWQNYVKTWFNQPARKTRRRVARQKKAVKIFPRPTSGPLRPVVHGQTLKYNMKVRAGKGFTLEELKVAGIPKKLAPTIGISVDHRRKNRSLEGLQSNVQRLKTYKAKLVVFPRRSRQVKAGDSTPEELANATQVQGDYMPIASVKAAMELVKLTADLKAFKAYDKIRLERTNARHAGARAKRAAEAEKEEKK", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family."}
{"protein": "MSFNLQSSKKLFIFLGKSLFSLLEAMIFALLPKPRKNVAGEIVLITGAGSGLGRLLALQFARLGSVLVLWDINKEGNEETCKMAREAGATRVHAYTCDCSQKEGVYRVADQVKKEVGDVSILINNAGIVTGKKFLDCPDELMEKSFDVNFKAHLWTYKAFLPAMIANDHGHLVCISSSAGLSGVNGLADYCASKFAAFGFAESVFVETFVQKQKGIKTTIVCPFFIKTGMFEGCTTGCPSLLPILEPKYAVEKIVEAILQEKMYLYMPKLLYFMMFLKSFLPLKTGLLIADYLGILHAMDGFVDQKKKL", "text": "FUNCTION: Oxidoreductase with strong preference for NAD (PubMed:18926804). Active in both the oxidative and reductive directions (PubMed:18926804). Oxidizes all-trans-retinol in all-trans- retinaldehyde (PubMed:18926804). No activity was detected with 11-cis- retinol or 11-cis-retinaldehyde as substrates with either NAD(+)/NADH or NADP(+)/NADPH (PubMed:18926804). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSQQGESSDPKSGKKDFSTAILERKKSPNRLVVDEAVNDDNSVVTMHPQTMEKLQLFRGDTILIKGKKRKDTICIALADENCEEPKIRMNKVVRSNLRVRLGDVVSVHQCPDVKYGKRVHILPIDDTIEGVTGNLFDAFLKPYFLEAYRPVRKGDLFLVRGGMRSVEFKVVETDPGEYCVVAPDTEIFCEGEPLKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVIGATNRPNSIDPALRRFGRFDREIDIGVPDEVGRLEVLRIHTKNMKLSDDVDLERIAKDTHGYVGADLAALCTEAALQCIREKMDVIDLEDETIDAEVLNSMAVTNEHFQTALGTSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGSSVGDAGGAADRVLNQLLTEMDGMSAKKTVFIIGATNRPDIIDPALLRPGRLDQLIYIPLPDEDSRHQIFKACLRKSPIAKNVDLRALARHTQGFSGADITEICQRACKYAIRENIEKDIERERKSRENPEAMDEDTVDDEVAEIKAAHFEESMKFARRSVSDADIRKYQAFAQTLQQSRGFGSEFRFPESGDRTTTGSDPFAASAGGADEDDLYS", "text": "FUNCTION: Probably functions in cell division and growth processes. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MAANYSSTGSRKEHVKVTSDPQPGFLERLSETSGGMFVGLVTFLLSFYLIFTNEGRALKTANLLAEGLSLVVSPDSIHSVAPENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESNEYTEDGQVKKETKYSYNTEWRSEIVSSKNFDREIGHKNPSAMAVESFTATAPFVQIGRFFLSAGLIDKIDNFKPLSLAKLEDPHVDIIRRGDFFYHSENPKYPEVGDVRVSFSYAGLSSDDPDLGPAHVVTVIARQRGDQLIPYSTKSGDTLLLLHHGDFSAEEVFRREQKSNSMKTWGLRAAGWMAMFMGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWAALLGCLALVPIIIARTRVPTKKLE", "text": "FUNCTION: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (By similarity). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (By similarity). Contributes to passive conductance current in cochlear glia-like supporting cells, mediated by gap junctions and necessary for hearing (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane Nucleus inner membrane; Multi-pass membrane protein Cell membrane Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen (By similarity). SIMILARITY: Belongs to the TMEM43 family."}
{"protein": "MAESDWDTVTVLRKKGPSAAQAKSKQAVLAAQRRGEDVETSKKWAAGQNKQHFITKNTAKLDRETEELHHDRVPLEVGKVIQQGRQSKGMTQKDLATKINEKPQVIADYESGRAIPNNQVMGKIERAIGLKLRGKDIGKPLETGPKGK", "text": "FUNCTION: Probable transcriptional coactivator. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MPRLTVGTKNMLYPLQKTLAVGSCKPEQVPIRSLASVVESSSKILDKSGSDREVDINVSEKIYKWTKAGIEQGKEHFKVGGNKVYFPKARIILLRPNAKHTPYQAKFIVPKSFNKLDLRDYLYHIYGLRAMNITTQLLHGKFNRMNLQTTRFREPQIKKMTIEMEEPFIWPEEPRPDENSFWDSTTPDNMEKYREERLNCLGSDANKPGTAFDGVVGPYERVAQPFIPRFLKREIDNKRERHAAELQRADKLIALNRYIEDLH", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
{"protein": "MPLPEPLNIKAWVEENEHLLKPPVNNFCLHRGGFTVMIVGGPNERSDYHINQTPEYFYQYKGTMCLKVVDEGKFRDIYIREGDTFLLPPNVPHNPCRFENTVGIVVEQDRPKGVNDRIRWYCARCESIVCEEEFYLTDLGTQIKDAIVAFDSNIEAKTCKNCGHVNSSKREPAEF", "text": "FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 3-HAO family."}
{"protein": "MAHGEPYYSSKPDKDFNFGSTMARRQMTPTMVAKLPNFVRNSPQAYDWIVRGLIFPTTGKTYFQRVVVITGGLEDGTYGSFVFDGREWVEIYPIEHLNLMSSLKLIHKANALQERLRLSQEEKATLALDVQFLQHENVRLKELIPKPEPRKIQMKWIIVGAVLTFLSLIPGGYAQSQINNTIFTDMIAACKYSTETLTENLDLRIKLALANITISDKLDAVRQILNFAFVPRAHWLRTVFYYIHYYEMWNIFMFVLAIGTVMRSARPGTDLITLATSHLSGFRMAVLPTIPFHTTMTLWVMNTLMVCYYFDNLLAITLAILAPILGIIFLCFMEDSNYVSQIRGLIATAVLIAGGHACLTLTGTTTSLFVVILTCRFIRMATVFIGTRFEIRDANGKVVATVPTRIKNVAFDFFQKLKQSGVRVGVNEFVVIKPGALCVIDTPEGKGTGFFSGNDIVTAAHAVGNNTFVNVCYEGLMYEAKVRYMPEKDIAFITCPGDLHPTARLKLSKNPDYSCVTVMAYVNEDLVVSTAAAMVHGNTLSYAVRTQDGMSGAPVCDKYGRVLAVHQTNTGYTGGAVIIDPTDFHPVKAPSRVELLKEEIERLKAQLNSAAENPATAVTQQPVVTLEQKSVSDSDVVDLVRTAMEREMKVLRDEINGILAPFLQKKKGKTKHGRGRVRRNLRKGVKLLTEEEYRELLEKGLDRETFLDLIDRIIGERSGYPDYDDEDYYDEDDDGWGVVGDDVEFDYTEVINFDQAKPTPAPRTVKPKTCPEPEAETQPLDLSQKKEKQLEHEQQVVKSTKPQKNEPQPYSQTYGKAPIWESYDFDWDEDDAKFILPAPHRLTKADEIVLGSKIVKLRTIIETAIKTQNYSALPEAVFELDKAAYEAGLEGFLQRVKSKNKAPKNYKGPQKTKGPKTITH", "text": "FUNCTION: [Non-structural polyprotein 1A]: Contains the viral protease participating in the cleavage of the polyprotein into functional products. FUNCTION: [VPg]: Protein covalently attached to the 5' extremity of the genomic and subgenomic RNAs. SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the astroviridae polyprotein 1A family."}
{"protein": "MATQKKKTSGRKKSSTRSKKKQSASFRLEITGVILIAIGVIGLLQLGFVGRGFFALAEMFVGLLSYVLLAGSVILGGYMVIRRKMPHLFSKRLVGIYLIVLGFLTYIHMYFIIHNLGANASVVSSTWKLVLENLFRPNQVGFVGGGMIGAAITSITYFLLDRLGTNLIAVLLIIYGFSLVSGISIRQFFSKIAEFVRYLFTKGKVATEKGKEVKAKRDKKKAEKIVDVEPDEVIDVIEPLQEEKTPPIISNFSSKVEQEKAPVEEKISQKEQDLEMFQQESFENEIYQLPPVDILAPAKVTDQSKEYDQIKVNAKKLEDTFESFGVKAKITQVHLGPAVTKYEVQPSVGVKVSKIVSLSDDIALALAAKDIRIEAPIPGKSAIGIEVANQNVAMVSLREVLENNPKNNPDEKLQIALGRDISGEAMMANLDKMPHLLVAGATGSGKSVCINGIITSILLRAKPHEVKMMMIDPKMVELNVYNGIPHLLAPVVTNPKKAAQALQKVVAEMERRYDLFSHTGTRNMQGYNDYVKKHNELNEEKQPELPFIVVIVDELADLMMVASNDVEDAITRLAQMARAAGIHLIIATQRPSVDVITGVIKANIPSRIAFAVSSSIDSRTILDMGGAEKLLGRGDMLLLPVGSSKPTRIQGAFLSDAEVEDVVNYVISQQKAQYSEEMIPDDIPEVEGEVTDELYHEAVELVVEMQTASVSMLQRKFRIGYNRAARLIDEMEQRGVVGPHEGSKPRRVNVEVSPEHE", "text": "FUNCTION: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Required for activation of the Xer recombinase, allowing activation of chromosome unlinking by recombination (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Located at the septum. SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family."}
{"protein": "MAAFLHHCPFLKSMPKPALRRRVPALLSLADRCPVIVHQVCISRLHILETKLDVSPTQPKRQRLSLLDQKRLFAQTATQVAVSVSKGCPFVSSQIGMVRASPEVQEDVQADLKSPVLPTPPQTGITQLLKDNMVGPSFDYDNFFNEKIAEKKRDHTYRVFKTVNRNAVVFPFAEDYSVSDRQGSQVSVWCSNDYLGMSRHPRVLEAIREVLERHGAGAGGTRNISGTSKYHVTLEKELAHLHQKDAALVFSSCFVANDSTLFTLAKMLPGCHIYSDAGNHASMIQGIRNSGAKRFIFRHNDSRHLEELLQQSDPKTPKIVAFETVHSMDGAICPLEELCDVAHRHGALTFVDEVHAVGLYGAHGAGVGERDNVMHKIDIVSGTLGKAFGCVGGYVASSAALVDTVRSFAAGFIFTTSLPPMILAGALESVRVLKSPEGQLLRRAHQRNVKYMRQLLMDKGLPVVNCPSHIIPIRVGNAELNTKVCDSLLEKHNIYVQAINYPTVPRGQELLRLAPSPHHHPAMMEYFVDKLVEVWQEAGLLLNGPATVSCTFCDRPLHFDLMSEWEKSYFGNMEPQYITMSA", "text": "FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (By similarity). Contributes significantly to heme formation during erythropoiesis (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein Note=Localizes to the matrix side of the mitochondrion inner membrane. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MRLISPALVVSTAIQARHVNSSAPVDSAMTEANPLASAHPPDVGYDGVPAGRVRNPDDPTTEERTPGESFMEAINFKIFKLVQEAQGRILGLPEQPRGDMEWLERYGQDAILHYLETGDKDPSQLEKKYDQLLDELKNAPNLEVEILESIHALFLAYMEEVAKPAVQTTPKLNEQPDKFAWAMINKARRNAKPGIRNPYKSLNIPLVENYIKKYNAFIELRQRELTLLDTFSCAFNHNTVKLAKFLAMVDTFSPKRTFVLAMRIELSEIWIEEKRTIAEVASILGISTITGYAKNRLSAGTFVRFIYQLAKTNEQLGPDIVKDLVKTFGPDRTTELLTRMKTVSPRMFTILKDHMDVRLKETGVTPN", "text": "FUNCTION: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RPP5. SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MQPTQYVGIQDIKSLGTLLDKVAEHKGCGTSSEGGKASCGSSDGPADMAPEVWEKVKNHPCYSEEAHHHYARMHVAVAPACNIQCNYCNRKYDCANESRPGVVSEKLTPEQAAKKVFAVASTIPQMTVLGIAGPGDPLANPAKTFKTFELISQTAPDIKLCLSTNGLALPDHIDTIAAFNVDHVTITTNMVDPEIGQHIYPWIYYQNKRWTGIDAARILHERQMLGLEMLTARGILCKVNSVMIPGINDQHLVEVNRAVKSRGAFLHNIMPLISAPEHGTVFGLNGQRGPSAQELKALQDACEGEMNMMRHCRQCRADAVGLLGEDRSAEFTTEKIEAMEVAYDGATRKAYQELVEQERQAKSAAKAAEQQELAQMADQSGLSLLVAVATKGQGRVNEHFGHVSEFQIYEVSSAGSKFVGHRRVDQYCQGGYGEEDALETVIRAINDCHAVLVAKIGGCPKDDLQKVGIEPVDRYAHEFIEQSVIAYFMDYLERVRSGQIEHRPRGDADIRQGAYTSVQSTSAAA", "text": "FUNCTION: Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster. SIMILARITY: Belongs to the radical SAM superfamily. NifB family."}
{"protein": "MCNRQPKAVDLPPNYSCPHLLSFQSVEFNTNPTACDDVFCKRIESEKKYNDFLESLFKKYGRDTSDIADEVDLATGEIIVNNGHLEALKTKDDIWDPTFNNLEISASNGYEKKLDSSIGNPGEKAVSPVHIEDFQSPQIYKFKNLSLRDEMVSDCVFADEVPLASLFVENVCNETIPSQSCVRLKINDKTRKVDASALEKKSCLLPNSSGTLTDQRGLDTIKHKSIEQNEILHVISDTLSSPRRRNPLLSSPKTPLRRSFSKSKVRNSNSTKRRNFISLISMISPRPNLSTHHFNLGFQPLSQQTSFSGSSTQNPHSSSTCKKAFCFQCISESKKC", "text": "FUNCTION: Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MAAYKLVLIRHGESTWNLENRFSCWYDADLSPAGHEEAKRGGQALRDAGYEFDICLTSVQKRVIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSYESPKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLQGIAKHVEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVCKAIEAVAAQGKAKK", "text": "SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily."}
{"protein": "MNDALKTYLNGICWFLLSLVTSSINDVMSKYLGTRLHSFEVAFFRFFFSSIVLLPFVVYYGKNALKTSRPFVHVLRGLLLFFGMTSWTYGLTIAPVTTATVVSFAIPLFTLILAVFILNENIIWQRWVVTVVGFIGLVVMLKPHTKDFNPEILYLILAAISFAMLDIINKKFVVKESMLSMLFYSAIVTAMVSLPVAMQYWITPSSFELALLFVLGSSGSFILFFLLKAFSIVDATATAPYRYLELVISAIAAYFIFNEFPDKSTVHGAVIIIPATLFIIYSEKKSMSSKHESQ", "text": "FUNCTION: Transports S-adenosylmethionine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. 10 TMS drug/metabolite exporter (DME) (TC 2.A.7.3) family."}
{"protein": "MSMMTSTPTKRSVKLDDIWPELEEGIYKIITDLNKGFPKQKWIALYTHVYDYCAASQSKSSAKVGMPKQQASGANYVGEDLYNRLNLFLKKHMSQLLKLTETKMDEPLLNYYYTEWDRYTSAMKYINNIFQYMNRYWIKREIDDGKKEVYEIFILSLVIWRDCLFTPLKQRLTNSLLDIIESERNGYQINTHLIKGVINGYVSLGLNREKPKETILQVYKSGFEELFLTATENYYTNESAKFISENSVADYMKKVETRLNEEVKRVQQYLHQNTESELIAKCEKVLIEKHVEVIWNEFQTLLEKDKIPDLTRMYSLLSRIPRGLEPLRTTLEKHVQNVGLQAVSSIATNGVIEPKVYIETLLKVFKKYNELVTGAFRSDTGFVASLDKACRRFINENAVTIAAKSSSKSPELLARFTDFLLKKSPNNPEESEMEQLLNDVMIVFKYIEDKDVFQDFYSKMLAKRLIHGTSTSEDLEGTMIGKLKSTCGYEYTSKLQRMFTDMSLSRELLDRFNNHIEQVERSSLNIDFSVLVLATGSWPLQPPSTNFSIPKELQACEQLFQKFYQNQHSGRKLNWLHHLSKGELKTKYLQTSKSGYTLQCSTYQIGVLLQFNQYETLTSEEIQESTQLIDSVLKGTLTSLAKSKILLADPPLDDEEIAKTTKFSLNKQFKNKKTKIFINVPVLTQVKEEIDSIHKTVEEDRKLQIQAAIVRIMKMRKQLAHSGLMTEVISQLQTRFNPKVNIIKKCIDILIEKEYLMRVEGKKDHYSYVA", "text": "FUNCTION: Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit (By similarity). Required at several stages during development. CulA and fbxA regulate multicellular development by targeting regA for degradation via a pathway that requires erkB function, leading to an increase in cAMP and PKA activity. SIMILARITY: Belongs to the cullin family."}
{"protein": "MRRNDGERHCVQWSRGARKFFGKNPEIIDIPDLIEVQKASYDQFLMMNTAPEDRPNEGLQAAFKSVFPIKAFSGAAMLEFVSYEFDPPKFDVDDCLRRDLTYAVPLKIILRLIVFDVDEFTGAKSIKDIKEQSIYMGDVPLMTKDG", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the RNA polymerase beta chain family."}
{"protein": "MSSAAVAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRIEFVIETARQLKRAHGFQEGRSPGPVGKPGKDMQSINHAEPGSRPPQPLDRYPLTSDRPPRLGAEYQRQANGIPVPNGFPKPDEPPELNRQSPNPRRTGAIPPNLVPLVNGSMPPVHALNGRSVQMGIPPGALAEHVGKRADDMKDKHRADSMSDPSDGHKRVDEWTQKGKTVREMMTLQTLDSRFKKEHAALPHRMSYESSSGALKTDRGKHSRGIKRKTSPEPDGEGIAVKLNGEGQPWLPSPSEVLKMPSAALPGFAAAPPSTISPHSRTTPPEAATAVQNSQSPMAALILAADNAGTGSPKDAGNQVHSTTTSAAGRRNSGSPQSPSAGQRRPALGATGTAHIPGMDPQAGHPHSIPDSSVPPSSVPLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRESIKQQGATGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP", "text": "FUNCTION: Acts as a transcriptional repressor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IRF2BP family."}
{"protein": "MRMLLHLSLLALGASYMYAIPTEIPTSALVKETLTLLSTHRTLLIGNETLRIPVPVHKHHQLCTEEIFQGIGTLESQTLQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES", "text": "FUNCTION: Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils. Acts also on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation (By similarity). Mechanistically, exerts its biological effects through a receptor composed of IL5RA subunit and the cytokine receptor common subunit beta/CSF2RB. Binding to the receptor leads to activation of various kinases including LYN, SYK and JAK2 and thereby propagates signals through the RAS-MAPK and JAK-STAT5 pathways respectively (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-5 family."}
{"protein": "MGVNAVHWFRKGLRLHDNPALRECIRGADTVRCVYILDPWFAGSSNVGINRWRFLLQCLEDLDANLRKLNSRLFVIRGQPADVFPRLFKEWSIAKLSIEYDSEPFGKERDAAIKKLASEAGVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLISRMEPLEMPVETITPEVMQKCTTPVSDDHDEKYGVPSLEELGFDTDGLPSAVWPGGETEALTRLERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSVNAGSWMWLSCSSFFQQFFHCYCPVGFGRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPESVQKAAKCVIGVNYPKPMVNHAEASRLNIERMKQIYQQLSRYRGLGLLATVPSNPNGNGNGGLMSFSPGESISGCSSAGGAQLGTGDGQTVGVQTCALGDSHTGGSGVQQQGYCQASSILRYAHGDNQQSHLMQPGRASLGTGISAGKRPNPEEETQSVGPKVQRQSTN", "text": "FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post- translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus (By similarity). Interacts with CLOCK- BMAL1 independently of PER proteins and is found at CLOCK-BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-BMAL1 in a poised and repressed state until the proper time for transcriptional activation (By similarity). Represses CLOCK- BMAL1-mediated transcriptional activation (PubMed:11684328). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocated to the nucleus through interaction with other Clock proteins such as PER2 or BMAL1. SIMILARITY: Belongs to the DNA photolyase class-1 family."}
{"protein": "MNHAITMGIFWHLIGAASAACFYAPFKKVKHWSWETMWSVGGIVSWLILPWAISATLLPDFWAYYRSFNASTLLPVFLFGAMWGIGNINYGLTMRYLGMSMGIGIAIGITLIVGTLMTPIINGQFSVLMHTQGGQMTLLGVLVAVIGVGIVTRAGQLKERKMGIKAEEFNLKKGLLLAVMCGIFSAGMSFAMNAAKPMHDAAAALGVDPLYAALPSYVVIMGGGALVNLGFCFIRLAKVKNLSVKADFSLAKPLIISNLLLSALGGLMWYLQFFFYAWGHASIPAQYDYMSWMLHMSFYVLCGGLVGLVLKEWNNAGRRPVSVLSLGCVVIIIAANIVGLGMAS", "text": "FUNCTION: Uptake of L-rhamnose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the L-rhamnose transporter (TC 2.A.7.6) family."}
{"protein": "MKISSFISTSLPLPASVSGSSSVGEMSGRSVSQQKSDQYANNLAGRTESPQGSSLASRIIERLSSMAHSVIGFIQRMFSEGSHKPVVTPALTPAQMPSPTSFSDSIKQLAAETLPKYMQQLSSLDAETLQKNHDQFATGSGPLRGSITQCQGLMQFCGGELQAEASAILNTPVCGIPFSQWGTVGGAASAYVASGVDLTQAANEIKGLGQQMQQLLSLM", "text": "FUNCTION: Essential virulence determinant; cytotoxic effector, involved in resistance to phagocytosis. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the YopE family."}
{"protein": "MARGPARTSLGPGSQQLPLLSLLLLLLLRDADGSHTAAARPPPPAAADGLAGDKNPQRSPGDVAAAQSPGAQDMVAVHMLRLYEKYSRRGARPGGGNTVRSFRARLEVVNQKAVYFFNLTSMQDSEMILTATFHFYSEPQWPPAREVPCKQRAKNASCRLLPPGPPARQHLLFRSLSQNTATQGLLRGAMALPPPPRGLWQAKDISLIVKAARRDGELLLSAQLDSGEKDTGVPRLGPHAPYILIYANDLAISEPNSVAVTLQRYDPFQAGDPEPGAAPNSSADPRVRRATQATGPLQNNELPGLDERPAQAPHAQHYHKHELWPNPLRALKPRPGRKDRRKKGQDVFMASSQVLDFDEKTMQKARKKQWDEPRVCSRRYLKVDFADIGWNEWIISPKSFDAYYCSGACEFPMPKMVRPSNHATIQSIVRAVGIVPGIPEPCCVPDKMSSLGVLFLDENRNVVLKVYPNMSVETCACR", "text": "FUNCTION: Growth factor involved in osteogenesis and adipogenesis. Plays an inhibitory role in the process of osteoblast differentiation via SMAD2/3 pathway. Plays an inhibitory role in the process of adipogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MPTQRWAPGTQCMTKCENSRPKPGELAFRKGDMVTILEACEDKSWYRAKHHSSGQEGLLAAAALRQREALSTDPKLSLMPWFHGKISGQEAIQQLQPPEDGLFLVRESARHPGDYVLCVSFGRDVIHYRVLHRDGHLTIDEAVCFCNLMDMVEHYTRDKGAICTKLVKPKRKQGAKSAEEELAKAGWLLDLQHLTLGAQIGEGEFGAVLQGEYLGQKVAVKNIKCDVTAQAFLDETAVMTKLQHRNLVRLLGVILHHGLYIVMEHVSKGNLVNFLRTRGRALVSTSQLLQFALHVAEGMEYLESKKLVHRDLAARNILVSEDLVAKVSDFGLAKAELRKGLDSSRLPVKWTAPEALKNGRFSSKSDVWSFGVLLWEVFSYGRAPYPKMSLKEVSEAVEKGYRMEPPDSCPGPVHTLMGSCWEAEPSRRPPFRKIVEKLGRELRSVGVAAPAGGQEAEGSAPTRSQDP", "text": "FUNCTION: Could play a significant role in the signal transduction of hematopoietic cells. May regulate tyrosine kinase activity of SRC- family members in brain. SUBCELLULAR LOCATION: Cytoplasm Membrane Note=In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily."}
{"protein": "MTSGSGPRSDAMHREKNFPVASWIIHPRHRALILAFYRFVRMADDIADHATLAPDEKLLYLDLLEAELLGKGETRAEAVHLRTALDRRGMPPRHALDLLTAFRMDVTKQRYENWDEVIDYCRYSAMPVGRFVLDVHGESAATWPASDVLCAGLQVCNHLQDCGKDFLNLNRVYIPRDALSASGASIEELGAAKSSLQMLQCLRSLAAKAEVLLNGGGALVSQVKDFRLRFEVSVILSFADKIVSMLKMRDPLRERVHLSPLELLLHGVGAMANEAARRAFGRGTRFKTTVDV", "text": "FUNCTION: Involved in the biosynthesis of the hopanoid precursor squalene (SQ) from farnesyl diphosphate (FPP). Catalyzes the second step, the conversion of presqualene diphosphate (PSPP) to hydroxysqualene (HSQ). SIMILARITY: Belongs to the phytoene/squalene synthase family. HpnC subfamily."}
{"protein": "MKIATIKTGLASLAMLPGLVMAAPAVADKADNAFMMICTALVLFMTIPGIALFYGGLIRGKNVLSMLTQVTVTFALVCILWVVYGYSLAFGEGNNFFGNINWLMLKNIELTAVMGSIYQYIHVAFQGSFACITVGLIVGALAERIRFSAVLIFVVVWLTLSYIPIAHMVWGGGLLASHGALDFAGGTVVHINAAIAGLVGAYLIGKRVGFGKEAFKPHNLPMVFTGTAILYIGWFGFNAGSAGTANEIAALAFVNTVVATAAAILGWIFGEWALRGKPSLLGACSGAIAGLVGVTPACGYIGVGGALIIGVVAGLAGLWGVTMLKRLLRVDDPCDVFGVHGVCGIVGCIMTGIFAASSLGGVGFAEGVTMGHQLLVQLESIAITIVWSGVVAFIGYKLADLTVGLRVPEEQEREGLDVNSHGENAYNA", "text": "FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (PubMed:14668330, PubMed:15876187, PubMed:15563598, PubMed:15361618, PubMed:16910683, PubMed:30211659, PubMed:32662768). Transport is electrogenic (PubMed:30211659, PubMed:32662768). Following sequestration of NH(4)(+) at the periplasmic face, NH(4)(+) is deprotonated and neutral NH(3) is transported into the cytoplasm (PubMed:15876187, PubMed:16910683, PubMed:18362341, PubMed:19278252, PubMed:32662768). Neutral NH(3) and charged H(+) are carried separately across the membrane on a unique two-lane pathway, before recombining to NH(4)(+) inside the cell (PubMed:32662768). In vitro can also transport the larger analogs methylamine and methylammonium (PubMed:11847102, PubMed:14668330, PubMed:12023896, PubMed:15876187, PubMed:17998534, PubMed:18362341). Also acts as a sensor of the extracellular ammonium concentration (PubMed:14668330). FUNCTION: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)). Transport is electrogenic. Following sequestration of NH(4)(+) at the periplasmic face, NH(4)(+) is deprotonated and neutral NH(3) is transported into the cytoplasm. Neutral NH(3) and charged H(+) are carried separately across the membrane on a unique two-lane pathway, before recombining to NH(4)(+) inside the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family."}
{"protein": "MTWRHHVRLLFTVSLALQIINLGNSYQREKHNGGREEVTKVATQKHRQSPLNWTSSHFGEVTGSAEGWGPEEPLPYSRAFGEGASARPRCCRNGGTCVLGSFCVCPAHFTGRYCEHDQRRSECGALEHGAWTLRACHLCRCIFGALHCLPLQTPDRCDPKDFLASHAHGPSAGGAPSLLLLLPCALLHRLLRPDAPAHPRSLVPSVLQRERRPCGRPGLGHRL", "text": "FUNCTION: NODAL coreceptor involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Secreted Note=Does not exhibit a typical GPI- signal sequence. The C-ter hydrophilic extension of the GPI-signal sequence reduces the efficiency of processing and could lead to the production of an secreted unprocessed form. This extension is found only in primates. SIMILARITY: Belongs to the EGF-CFC (Cripto-1/FRL1/Cryptic) family."}
{"protein": "MTVDKVKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKDDTVSDFFGIDGIGDKPEEFPKVERSDFEGEGKHASLALIDILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYYAVGNVDGGSSAEYNFHGDPEAASIVLRRMKCPITIVPWEAFYFESKTHDASVDFSAHLKYGTPLANYLSLATSIGRVKCEANGRQYSYCDEIAVATAIDEDKIAKKSQYLYVDVELNGTKTRGQVVVDWTEQLWSNEEAPNQHTHRRVKFVTSYDVHTVDKWLHAATSGSGKFD", "text": "FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine. SIMILARITY: Belongs to the IUNH family."}
{"protein": "MPLPLFASEGGFGLNLNLFETNLINLVIVIGVLYWFLKGFLGGILERRRQAILKDLEDSEGRLRQATTDLARAQEDLAAAQQKAEKIRSDGKARAEAIRKDGEMRTINAMAAVKQDALADLNAEGARLTEQLRREAALAAIDKVMTELPGRLDQAGQSRLIDASISNLEDA", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MSASSITGDFQDFLKHGLPAIAPAPGSETPHSPKLEEKHREKRAGLPDRHRRPIPARSRLVMLPKVETEASGLVRSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNQKRYTCIENQNCQIDKTQRKRCPYCRFKKCIDVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTSAIQNIHSASKGLPLSHVALPPTDYDRSPFVTSPISMTMPPHGSLHGYQPYGHFPNRAIKSEYPDPYSSSPESMMGYSYMDGYQTSSPASIPHLILELLKCEPDEPQVQAKIMAYLQQEQNNRNRQEKLSAFGLLCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLILDHIYRQVAHGKEGTIFLVTGEHVDYSSIISNTEVAFNNLLSLAQELVVRLRSLQFDQREFVCLKFLVLFSSDVKNLENFQLVEGVQEQVNAALLDYTLCNYPQQTEKFGQLLLRLPEIRAISKQAEDYLYYKHVNGDVPYNNLLIEMLHAKRA", "text": "FUNCTION: Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid metabolism. Plays an anti- inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development (By similarity). Activates the transcription of CYP2C38 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR5 subfamily."}
{"protein": "MTTVLFVGLGLIGGSLASNIKYHNPNTNIIAYDADISQLDKAKSIGIINEKCLNYSEAIKKADVIIYATPVAITNKYLSELIDMPTKPGVIVSDTGSTKAMIQQHECNLLKHNIHLVSGHPMAGSHKSGVLNAKKHLFENAYYILVYNEPRNEQAANTLKELLSPTLAKFIVTTAEEHDYVTSVVSHLPHIVASSLVHVSQKNGQEHHLVNKLAAGGFRDITRIASSNAQMWKDITLSNKTYILEMIRQLKSQFQDLERLIESNDSEKLLSFFAQAKSYRDALPAKQLGGLNTAYDLYVDIPDESGMISKVTYILSLHNISISNLRILEVREDIYGALKISFKNPTDRERGMQALSDFDCYIQ", "text": "SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family."}
{"protein": "MVNSTHRGMHASLHLWNRSSHRLHSNASESLGKGYSDGGCYEQLFVSPEVFVTLGVISLLENILVIVAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETIVITLLNSTDTDTQSFTVNIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVKRVRIIISCIWAACTVSGILFIIYSDSSAVIICLITMFFTMLALMASLYVHMFLMARLHIKRIAVLPGTGAIRQGANMKGAITLTILIGVFVVCWAPFFLHLIFYISCPQNPYCVCFMSHFNLYLILIMCNSVIDPLIYALRSQELRKTFKEIICCYPLGGLCDLSSRY", "text": "FUNCTION: Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a central role in energy homeostasis and somatic growth. This receptor is mediated by G proteins that stimulate adenylate cyclase (cAMP). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MDGNDNVTLLFAPLLRDNYTLAPNASSLGPGTDLALAPASSAGPGPGLSLGPGPSFGFSPGPTPTPEPTTSGLAGGAASHGPSPFPRPWAPHALPFWDTPLNHGLNVFVGAALCITMLGLGCTVDVNHFGAHVRRPVGALLAALCQFGLLPLLAFLLALAFKLDEVAAVAVLLCGCCPGGNLSNLMSLLVDGDMNLSIIMTISSTLLALVLMPLCLWIYSWAWINTPIVQLLPLGTVTLTLCSTLIPIGLGVFIRYKYSRVADYIVKVSLWSLLVTLVVLFIMTGTMLGPELLASIPAAVYVIAIFMPLAGYASGYGLATLFHLPPNCKRTVCLETGSQNVQLCTAILKLAFPPQFIGSMYMFPLLYALFQSAEAGIFVLIYKMYGSEMLHKRDPLDEDEDTDISYKKLKEEEMADTSYGTVKAENIIMMETAQTSL", "text": "FUNCTION: Transporter for bile acids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family."}
{"protein": "MGLQKSHLTVCLPPSVPFLILVSTLATAKSVTNSTLNGTDVVLGSVPVIIARTDHIIVKEGSSALINCSAYGFPDLEFKWYNSVGKLLKEMDDEKEKGGGKWQMLDGGLLNITKVSFSDRGKYTCVASNIYGTINNTVTLRVIFTSGDMGVYYMVVCLVAFTIVMILNITRLCMMSSHLKKTEKAINEFFRTEGAEKLQKAFEIAKRIPIITSAKTLELAKVTQFKTMEFARYIEELARSVPLPPLIMNCRTIMEEIMEVVGLEEQGQNFVRHTPEGQEAPDRDEVYTIPNSLKRSESPTADSDASSLHEQPQQIAIKVSVHPQSKRDHVDDQEGGHFEVKDEEETEPSEEHSPETAEPSTDITTTELTSEETSPVEAPERGLPPAHLETTEPAVTCDRNTCIIYESHV", "text": "FUNCTION: May participate in the nuclear signaling of EGFR and MAPK1/ERK2. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Nucleus Cytoplasm Note=Mainly localized in the nucleus."}
{"protein": "MLRIPVKRALIGLSKSPKGYVRSTGTAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGSDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFEGKAVAAIAGGLVDAEALVALKDLLNKVDSDTLCTEEIFPNEGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYRYDHLGDSPKILQDIASGNHEFSKVLNAAKKPMVVLGSSALQRDDGAAILAAVSSIAQKIRVASGAAAEWKVMNILHRIASQVAALDLGYKPGVEAIRKNPPKLLFLLGADGGCITRQDLPKDCFIVYQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGITLPYDTLDQVRNRLGEVSPNLVRYDDVEEANYFQQASELAKLVDQEFLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQAVEEPSIC", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (By similarity). Essential for catalysing the entry and efficient transfer of electrons within complex I (By similarity). Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
{"protein": "MFFFEKYRPKKPSDFLFNTDVLRQLKYLASNEDVPHIIISGPSGSGKKTLVKFLLEFLYDEDVNILRKRKYNINGSSTKKEIEILQSNYHIIIEPTSTNHDKYILQEIIKQYAMHKSFDIFKTKRKFKTIVIHNIENLANNSQAALRRTMERYAKTCRFIMVCNNLSKIMDPLRSRCRTFCVPLPTIENINTVVDYIAFMENIKLNKNDTKFILDNCNNNLKTAIWFLNCKGLNCSPFIALDEAFDLVVESILECRTGKNIFKIHNDIRTNIYNILITNIKGSEIINILVDKLIRKIDDDVINMNIIQYASKAEYNLTHGRRDITDIEYFISGVMQELVLNRNKEPEKSEKTKSKTGKLSRTNSKKTIKN", "text": "FUNCTION: Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. SIMILARITY: Belongs to the activator 1 small subunits family. RfcS subfamily."}
{"protein": "MESWPWPSGGAWLLVPARALLQLLRADLRLGRPLLAALALLAALDWLCQRLLPPLAALAVLAATGWIVLSRLARPQRLPVATRAVLITGCDSGFGNATAKKLDTMGFTVLATVLDLNSPGALELRACCSSRLKLLQMDLTKPGDISRVLEFTKVHTPSTGLWGLVNNAGQNIFVADAELCPVATFRTCMEVNFFGALEMTKGLLPLLRRSSGRIVTVSSPAGDMPFPCLAAYGTSKAALALLMGNFSCELLPWGVKVSIIQPACFKTESVKDVHQWEERKQQLLATLPQELLQAYGEDYIEHLNGQFLHSLSQALPDLSPVVDAITDALLAAQPLRRYYPGHGLGLIYFIHYYLPEGLRQRFLQSFFISPYVPRALQAGQPGLTSARDIAQDQGPRPDPSPTAQ", "text": "FUNCTION: Catalyzes the conversion of biologically active 11beta- hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) (PubMed:10822012, PubMed:17470521, PubMed:26519454). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids (PubMed:10822012). Affinity towards corticosterone is higher than cortisol or dexamethasone (PubMed:10822012). Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen. Catalyzes the conversion of 11beta- hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11- ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone. Converts 7-beta-25- dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro. 7-beta- 25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus- induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity). May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol (PubMed:17470521, PubMed:26519454). SUBCELLULAR LOCATION: Microsome Endoplasmic reticulum. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "SGPGFMGVR", "text": "FUNCTION: Myoactive peptide. Increases the amplitude and frequency of spontaneous contractions and tonus of hindgut muscle. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTSDQDAKVVAEPQAQRVQEGKDSSHLMNGPISQTTSQTRSLPALTQVPTTKVSELNPNAKVWGTHMLHLEASSAAVGVNAAWEEAPGHPTDCDQQVLGLDANGDGDKSRENAALPDAQEAEQTDMSTLALDHSEYEPLPENNDTGGNESQPESQEDPREVLKKTLEFCLSRENLASDMYLISQMDSDQYVPITTVANLDHIKKLSTDVDLIVEVLRSLPLVQVDEKGEKVRPNQNRCIVILREISESTPVEEVEALFKGDNLPKFINCEFAYNDNWFITFETEADAQQAYKYLREEVRTFQGKPIKARIKAKAIAINTFLPKNGFRPLDMNLYTQQRYATSFYLPPVYSPQQQFPLYSLITPQTWSTTHSYLDPPLVTPFPSTGFINGFTSPTFKPATSPLTSLRQYPPRSRNPSKSHLRHAIPSTERGPGLLESPSIFNFTADRLINGVRSPQTRQAGQTRTRIQNPSAYAKREIGTGRVEPSSLESSPGLGRGRKNSFGYRKKREEKFTSSQTQSPTPPKPPSPSFELGLSNFPPLPGAAGNLKTEDLFENRLSSLIIGSSKERNLSTDASTNTVPVVGPREPSVPAPCAVSAAFERSPSPVHLPEDPKVAEKQRETQSVDRLPSTPTTTACKSVQVNGAATELRKPSYAEICQRTSKDPSSSSPLQPPKEQKPSTVACGKEEKQLSEPVERHREPPALKSTPGVPKDQRRQPGRRASPPAAGKRLSKEQNTPPKSPQ", "text": "FUNCTION: Stimulates mRNA translation. SUBCELLULAR LOCATION: Cytoplasm, cytosol Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs in response to arsenite treatment."}
{"protein": "MRKNNTAIIFGSLFFSCSVMAANGTLAPTVVPMVNGGQASIAISNTSPNLFTVPGDRIIAVNSLDGALTNNEQTASGGVVVATVNKKPFTFILETERGLNLSIQAVPREGAGRTIQLVSDLRGTGEEAGAWETSTPYESLLVTISQAVRGGKLPAGWYQVPVTKETLQAPAGLSSVADAVWTGNHLKMVRFAVENKTLSALNIRESDFWQPGTRAVMFSQPASQLLAGARMDVYVIRDGEGN", "text": "FUNCTION: Involved in pilus assembly. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
{"protein": "MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL", "text": "FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (By similarity). Important for normal progress through mitosis and normal cytokinesis (By similarity). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (By similarity). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration (By similarity). SUBCELLULAR LOCATION: Nucleus matrix Cytoplasm, cytoskeleton Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium Cell projection, growth cone Cell projection, axon Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
{"protein": "MPVIKGPQVFPRAEFLRRLNAVKLEMGRLEIDALIVGSSADITYLTGYTAKSGYVPQALVISSNDEEPTFILRRQDAPAAIHQTFMDRDKVIGYSEALIGNPDKDGYDAVVDFLNERDGANKRGVGVQLGYLSVRSAEKFKTRLPSARIVDCTHSVAWIRMIKSDLEISMMRDAAAIADAGVQKAFEVIRPGVREADVMADVAAQLARGTNGKAGTDLASMYFCSSPRTGTCHIRWSEDVIRDGSQINLEIAGVRHGYVSAIMRTFSVGAPSDRLRRIHDAEVLGLEAALSTVKPGATCSDVANAFYRTIEKSGFQKDSRCGYAIGIDWSEPTASLKDGDMTKLKPNMTFHLMLGNWIEEDFGYVLSETFRVTEAGCEVLTKSPRQLCVI", "text": "SIMILARITY: Belongs to the peptidase M24 family."}
{"protein": "MSSGLKTQTTIDILHDHSVESSSDHLYILKQQQQHQHEDTDSPKKKKLRHQCEETSQYIVPSLNDEVDDLGHHHLHHHHVNNINNSLLKQGLSALSSLSASSTSSISPSSSQSSSPLKQSERSIATSIDSMNDSTSSSSSSNNNNNFSSVPSHNIYTPSCLLSNLNNDTDSIIPNMNGSTDGDGGDIRREKVDENDEEVLCNDNHLSKDNEQEDNMVSFLNESNEEVIQTNNNNNNDNNNSSNICINNFCNINNNQQQQQQQQQQQQNNVNSSIILEDSNKENKTESNNSNSNSNSSPSFFHNLQQHPTSAATTTTTTTTTITTTSATTSIIIKEDNSDDEIDDECDDESEEEEEDEEEFNPFLFIKQLANATTMPPPVALPPKEHSSPKISLVLDLDETLVHCSTEPLEQPHLTFPVFFNNTEYQVFAKKRPFFEEFLHKVSDIFEVIIFTASQEVYANKLLNMIDPNNKIKYRLYRDSCVYVDGNYLKDLSVLGRDLKQVVIIDNSPQSFGFQVDNGIPIESWFEDENDKELLQLVPFLESLTNVEDVRPHIRDKFKLYQLISQA", "text": "FUNCTION: Probable phosphatase. SIMILARITY: Belongs to the CTDSPL2 family."}
{"protein": "MASGKHHQPGGTRSLTMQKVSLRVTPRLVLEVNRHNAICVATNVPEFYNARGDLNVRDLRAHVKARMISSQFCGYILVSLLDSEDQVDHLNIFPHVFSERMILYKPNNVNLMEMCALLSMIENAKSPSIGLCREVLGRLTLLHSKCNNLDSLFLYNGARTLLSTLVKYHDLEEGAATPGPWNEGLSLFKLHKELKRAPSEARDLMQSLFLTSGKMGCLARSPKDYCADLNKEEDANSGFTFNLFYQDSLLTKHFQCQTVLQTLRRKCLGSDTVSKIIP", "text": "FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm. SUBCELLULAR LOCATION: Virion Virion tegument Host cytoplasm Host Golgi apparatus Note=Probably associates with the Golgi apparatus through its interaction with BSRF1. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 1 family."}
{"protein": "MGNVLAASSPPAGPPPPPAPPLVGLPPPPPSPPGFTLPPLGGGLGAGAGTGRGSERTPGTAAASAGGTADDGACGCLPNPGTFEECHRKCKELFPIQMEGVKLTVNKGLSNHFQVNHTVALSTIGESNYHFGVTYVGTKQLSPTEAFPVLVGDMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGELVYHRRPGEEGAVMSLAGKYTLNNWLATVTLGQAGMHATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDLPKANLLFKGSVDSNWIVGATLEKKLPPLPLTLALGAFLNHRKNKFQCGFGLTIG", "text": "FUNCTION: Channel-forming protein essential for import of protein precursors into mitochondria. Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by forming a complex with BCAP31 and mediating the translocation of Complex I components from the cytosol to the mitochondria. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Note=Associates with the mitochondria-associated ER membrane via interaction with BCAP31. SIMILARITY: Belongs to the Tom40 family."}
{"protein": "MEVCCCSTSSAVPGRRFAAAGAAAAAVAARWGAVGVGRAVVLAHPLRPAPRGGHAHAQQAGARRARRAVVRAVFERFTERAVKAVVLSQREAKGLGEGAVAPRHLLLGLIAEDRSAGGFLSSGINIERAREECRGIGARDLTPGAPSPSGSGLEMDIPFSGSCKRVFEVAVEFSRNMGCSFISPEHLALALFTLDDPTTNSLLRSLGADPSQLASVALTRLQAELAKDCREPAGASSFKVPKKSPAGAGRSAFSKSLNSKKEKGALDQFCLDLTTQASGGFIDPIIGREEEIERVVQIICRRTKNNPILLGEAGVGKTAIAEGLALRIANGDVPIYLVAKRIMSLDVGLLIAGAKERGELESRVTSLIREVREAGDVILFIDEVHNLIGSGTVGKGKGAGLDIGNLLKPPLARGELQCIAATTLDEHRMHFEKDKALARRFQPVLVEEPSQDDAVKILLGLREKYETYHKCKFTLEAINAAVYLSARYIPDRQLPDKAIDLIDEAGSRARMESFNRKKEGQSSILLKSPDEYWQEIRAAQNMHEVVSSNQMKYSPRQENGSAAIKAPSEDMNELTSELQVEEPIVVGTEEIARVASLWSGIPVQQLTADDRKLLVGLDGELRKRVIGQDDAVMAISRAVKRSRVGLNDPDRPIATLLFCGPTGVGKTELTKALAASYFGSESAMLRLDMSEYMERHTVSKLIGSPPGYIGYGETGTLTEAVRRKPFTVVLLDEIEKAHPDIFNILLQIFEDGHLSDSQGRRVSFKNTLIVMTSNIGSTSISKGRRSMGFMTEDTESSSYVAMKSLVMEELKAFFRPELLNRIDEMVVFRPLEKTQMLAILDIILQEVKGRLLALGIGLEVSDAMKDLICEEGYDKSYGARPLRRAVTHLIEDVISEAILFGEYKPGDTILMDIDAGGKLCMSHLNEKVVQLSDPTRTF", "text": "FUNCTION: Molecular chaperone that may function in heat stress response. May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast (PubMed:20141629). Chaperone involved in response to abiotic stresses. Plays a positive role during dehydration and salt stress (PubMed:27457985). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ClpA/ClpB family. ClpD subfamily."}
{"protein": "MDADKIVFKVNNQVVSLKPEIIVDQHEYKYPAIKDLKKPCITLGKAPDLNKAYKSVLSGMSAAKLDPDDVCSYLAAAMQFFEGTCPEDWTSYGIVIARKGDKITPGSLVEIKRTDVEGNWALTGGMELTRDPTVPEHASLVGLLLSLYRLSKISGQNTGNYKTNIADRIEQIFETAPFVKIVEHHTLMTTHKMCANWSTIPNFRFLAGTYDMFFSRIEHLYSAIRVGTVVTAYEDCSGLVSFTGFIKQINLTAREAILYFFHKNFEEEIRRMFEPGQETAVPHSYFIHFRSLGLSGKSPYSSNAVGHVFNLIHFVGCYMGQVRSLNATVIAACAPHEMSVLGGYLGEEFFGKGTFERRFFRDEKELQEYEAAELTKTDVALADDGTVNSDDEDYFSGETRSPEAVYTRIMMNGGRLKRSHIRRYVSVSSNHQARPNSFAEFLNKTYSSDS", "text": "FUNCTION: Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the lyssavirus nucleocapsid protein family."}
{"protein": "MGMRMMFTVFLSVVLATTVVSTPSDRASDGRNAAVHERQKELVPSVITTCCGYDPGTMCPPCRCTNSCPTKPKKPGRRND", "text": "FUNCTION: Neurotoxin with probable activity on sodium channel (Probable). Induces intense repetitive firing of the frog neuromuscular junction, leading to a tetanic contracture in muscle fiber (spastic paralysis) (PubMed:17115716). In vivo, shows the same effect as the whole venom when injected on fish prey (PubMed:17115716). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
{"protein": "METRESEDLEKTRRKSASDQWNTDNEPAKVKPELLPEKEETSQADQDIQDKEPHCHIPIKRNSIFNRSIRRKSKAKARDNPERNASCLADSQDNGKSVNEPLTLNIPWSRMPPCRTAMQTDPGAQEMSESSSTPGNGATPEEWPALADSPTTLTEALRMIHPIPADSWRNLIEQIGLLYQEYRDKSTLQEIETRRQQDAEIEDNTNGSPASEDTPEEEEEEEEEEEPASPPERKTLPQICLLSNPHSRFNLWQDLPEIRSSGVLEILQPEEIKLQEAMFELVTSEASYYKSLNLLVSHFMENERIRKILHPSEAHILFSNVLDVLAVSERFLLELEHRMEENIVISDVCDIVYRYAADHFSVYITYVSNQTYQERTYKQLLQEKAAFRELIAQLELDPKCRGLPFSSFLILPFQRITRLKLLVQNILKRVEERSERECTALDAHKELEMVVKACNEGVRKMSRTEQMISIQKKMEFKIKSVPIISHSRWLLKQGELQQMSGPKTSRTLRTKKLFHEIYLFLFNDLLVICRQIPGDKYQVFDSAPRGLLRVEELEDQGQTLANVFILRLLENADDREATYMLKASSQSEMKRWMTSLAPNRRTKFVSFTSRLLDCPQVQCVHPYVAQQPDELTLELADILNILDKTDDGWIFGERLHDQERGWFPSSMTEEILNPKIRSQNLKECFRVHKMDDPQRSQNKDRRKLGSRNRQ", "text": "FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) which differentially activates the GTPases RHOA, RAC1 and CDC42. Plays a role in axon guidance regulating ephrin-induced growth cone collapse and dendritic spine morphogenesis. Upon activation by ephrin through EPHA4, the GEF activity switches toward RHOA resulting in its activation. Activated RHOA promotes cone retraction at the expense of RAC1- and CDC42-stimulated growth cone extension (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane Cell projection, growth cone Note=Associated with membranes. Localizes to axonal growth cones (By similarity)."}
{"protein": "MGPAPESSEFVHRTWVQCENESCLKWRLLSPAAAAAVNPSEPWYCFMNTDPSYSSCSVSEEDFPEESQFLENGYKFVYSQLPLGSLVLVKLRNWPSWPGILCPDPFKGKYVTYDQDGNVEKYYVEFLGDPHSTAWMSAAFVGHFSLTLEAADCTKKKRWYRSALEEAYQLYRCSAEQRLEVCCLSKPNRAKTDTKAAVVTKKGMQVSKINTEKKRPRVRKRKRDAALKCSVEIFCSDEALSKENMVVSETEGLLKELEKMLQQIQEPTAREDESQGEQLSQCSPESPTGSPFQSYHEEDYIVPDGAGLKAGEYIEIITNNLKKIDALISEF", "text": "FUNCTION: Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (By similarity). The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 (By similarity)."}
{"protein": "MPHTITTTDELAAYCARAATQPYVTVDTEFLRERTYFAQLCLVQVAMPGTDDTDAVLIDPLAEGLSLEPLYELFRNVNVVKVFHAARQDLEIFFVEGGLVPTPLFDTQVAAMVCGFGDQVGYETLVRRIAKANLDKSSRFTDWSRRPLSDAQKVYALADVTYLREIYEYLSAELARTDRTHWLEEELAQLTNADAYVVDPENAWKRLKLRSNSGRVVAIAQQLAAFRETYAQEKNVPRNRVLKDDALLELAGTKPKTVADLGKSRLLLRDARKGAIAEGLVAAVARGMSVPNSEIPKVQAGRDRSNLNPALADLLRVLLKAKAENAGVATKLIASSSDLDDIASGFTDGVWASGWRSEVFGADALRLLNGEVALAAKGQKVKIVEV", "text": "FUNCTION: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase D family."}
{"protein": "MLWITRFAGLFSAAMAVIVLSPSLQSFPPAAAIRSSPSPIFRKAPAVFNNGDECLSSGGVCNPSLVHVAITLDVEYLRGSIAAVNSILQHSVCPESVFFHFIAVSEETNLLESLVRSVFPRLKFNIYDFAPETVRGLISSSVRQALEQPLNYARSYLADLLEPCVNRVIYLDSDLVVVDDIAKLWKTSLGSRIIGAPEYCHANFTKYFTGGFWSEERFSGTFRGRKPCYFNTGVMVIDLKKWRRGGYTKRIEKWMEIQRRERIYELGSLPPFLLVFSGHVAPISHRWNQHGLGGDNVRGSCRDLHPGPVSLLHWSGSGKPWIRLDSKRPCPLDALWTPYDLYRHSH", "text": "FUNCTION: May be involved in pectin and/or xylans biosynthesis in cell walls. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 8 family."}
{"protein": "MLRKLPINFAKWTVKKVPVQQKRFNSQQKEISPHIMFYKNYARPLGKVTLFALATYYGLEIVWWKLDASEQEAIKNSKLLICESSFSLLTFRRITEFRECEIKTRDLYDPEI", "text": "FUNCTION: Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the INA17 family."}
{"protein": "MKSKKQARAACPCGGGELAACCGRYLGPDASPAPTAQALMRSRYSAYALGLEDYLLATWHPSTRPEALHLDEDAGVVKWIGLEVKRCEAGSERDAEGVVEFVARCKVGGKAERMHETSRFLREDGRWYYVSGLVA", "text": "SIMILARITY: Belongs to the UPF0225 family."}
{"protein": "MSSSEVKANGWTAVPVSAKAIVDSLGKLGDVSSYSVEDIAFPAADKLVAEAQAFVKARLSPETYNHSMRVFYWGTVIARRLLPEQAKDLSPSTWALTCLLHDVGTAEAYFTSTRMSFDIYGGIKAMEVLKVLGSSTDQAEAVAEAIIRHEDVGVDGNITFLGQLIQLATLYDNVGAYDGIDDFGSWVDDTTRNSINTAFPRHGWCSWFACTVRKEESNKPWCHTTHIPQFDKQMEANTLMKPWE", "text": "FUNCTION: Cyanamide hydratase involved in the detoxification and/or utilization of cyanamide, a toxic nitrile compound distributed widely in the environment. SIMILARITY: Belongs to the cyanamide dehydrase family."}
{"protein": "MLHPRARTMLLLSLPAVAIGIASSLILIMVMKIASVLQNLLWQRLPGTLGIAQDSPLWIIGVLTLTGIAVGLVIRFSQGHAGPDPACEPLIGAPVPPSALPGLIVALILGLAGGVSLGPEHPIITVNIALAVAIGARLLPRVNRMEWTILASAGTIGALFGTPVAAALIFSQTLNGSNEVPLWDRLFAPLMAAAAGALTTGLFFHPHFSLPIAHYGQMEMTDILSGAIVAAIAIAAGMVAVWCLPRLHAMMHQMKNPVFVLGIGGLILGILGVIGGPVSLFKGLDEMQQMVANQAFSTSGYFLLAVIKLAALVVAAASGFRGGRIFPAVFVGVALGLMLHEHVPAVPAAITVSCAILGIVLVVTRDGWLSLFMAAVVVPNTTLLPLLCIVMLPAWLLLAGKPMMMVNRQKQQPPHDNV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family."}
{"protein": "MVKLHIGIDDTDSPKGMCTTYLGALLYREISKIAEPLDLPKLIRLNPNVPYKTRGNGAVAMSFDAREEDILKIKNLVLEMVKKLSEFSHQNTNPGVVFIEGDIPEKLERFAYKAIWEHLNITDAENIAEELNAEIHKFRLGRGIIGALAAIGHPLKVFTYELLAYRTREFWGTARKVNKESVFAVDHLTYPFTYDNVDLSKGSVLITPHGKDPVLVGIRGIDKNKVIWAFENITFEEPIDFFQIYKTNQNTDDHLRFKKIAELKPLDSAIVRGKVIKKYWEKGRHVFFEISDDTGKLRVAAFEPTKGFRKYVRMLIEGDEIIAAGGVKEFNGVLTLNLEKFYPIKLTEKITYEKPKCPKCKGTMKSKGEYLKCKKCGYKMKKVLIPKRIPRDLKRKIYEVPPDARKHLSRPLVLPMAENKILDVLKLKR", "text": "FUNCTION: ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TiaS family."}
{"protein": "MIQKFTNLYVTDNSGAIAVRVFQTYPGNRKIVPVGSIVRHSVKKIHRILPWGKQLRGRRKRIICRSQCGRSWIVQTSYQIPYIDGATLRFSKNRVLLVKRKRGIRIYRGRRIYGLTTRAVNNERTINLFRICI", "text": "SUBCELLULAR LOCATION: Hydrogenosome. SIMILARITY: Belongs to the universal ribosomal protein uL14 family."}
{"protein": "MMQRNSNNTSITSNISNNSSSHQACASCKHQRKKCNNECILSPYFPARKTKEFQAVHKVFGVSNVQKMVRTVREEDRTKLSDSLTWEALWRQKDPVLGSYGEYRRICEELKLYKSLVHNQPLIGWDNNQRVFNNNSNNKNGLAMTNSSGSGGFSVNNNGVGVNREIVNGGYASRNVQGGWENLKHDQRQQCYAVINNGFKQHYLPL", "text": "SIMILARITY: Belongs to the LOB domain-containing protein family."}
{"protein": "MNLASVLLLLAACHLSVSVNGQEHKEAIELSMANHDHVLGSAQVVFVAFCADWCPFSRRLKPIFEESARVFHQENPQASAVWAIVDSQRQADIGDKYFVNKYPTMKVFVNGELITKEYRSTRSVEALTNFVKFQLSTAINEFSSQDQLNQEMDKSKRNVVAWLKKDGPEFANLKKVASILREDCSFWVPTDHFGTQTNDNKLSFFDPDSNEEAKFTGNFNDYDFVKQWVTDKCIPLVREVTFENVEELTEEGMPFLIYFRDPDNKTTDKVFGEAVARELYDQRSAINPLLADGHKFAHPLKHLGKTKEDLPVLAIDSFQHMYLFPDMTQMNIPGKLREFVMDLHSGKLHKDFHENLDQRMIELAKAKAARGITDDHEAQAPSTRPIDTTPPPSVFKELKPSDKRYSILQKSEL", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "MSWTRVVVLSLLTTLLFLTFSSVVDSAAVRDDSKAGHPKGPARQVFVPESEASNFFKRRSRRSPRSYAELQAEQRVKIAANERWREYNEEQRNEHENYAEEARDESDERSRETHEQIREYHYDGLYPRYHWFH", "text": "FUNCTION: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the UCMA family."}
{"protein": "MDFLVLFLFYLAFLLICVVLICIFTKSQRLKAVVLGGAQVCSRVIPQCLQRAVQTLLHQLFHTRHPTFIVLHLLLQGLVYAEYTCEVFGYCRELEFSLPYLLLPYVLLSVNLVFFTLTCAANPGTITKANESFLLQVYKFDDVMFPKNSRCPTCDLRKPARSKHCRLCDRCVHRFDHHCVWVNNCIGAWNTRYFLIYLLTLTASAATIATVTAAFLLRLVTVSDLYQETYLDDVGHFQAVDTVFLIQHLFLAFPRIVFLLGFVIVLSMLLAGYLCFALYLAATNQTTNEWYKGDWAWCQRWPLVAWSPSAEPRIHQNIHSHGFRSNLREIFLPATPSYKKKEK", "text": "FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto protein substrates including the D(2) dopamine receptor DRD2. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MDISAAVFNAARDGKLKLMQKLLINKSPEERAALAEERTEGGTPLLIAARYGHLPVVHFLLERCGANVALGGSVNFDGETIEGAPPLWAASAAGHLPVVKALLEHGAPVNNTTLTNSTPLRAACFDGHLEIVRYLVEHQADLEVANRHGHTCLMISCYKGHREIAQFLLEKGADVNRKSVKGNTALHDCAESGSLEIMKMLLKCDARMERDGYGMTPLLAASVTGHTNIVEFLVHQPRASREQRIHALELLGATFVDKKRDLLGAMRYWRRAMELRWAGGQAGALEKPTAGPLVPAYDCSREVSTAEELEALITDPDDMRMQALLVRERILGPAHPDTSYYIRYRGAVYADSGNFERCIRLWKYALDMQQSNLEPLSPMTASSFLSFAELFSFVLQDRAKGTLAARVSFQDLMGVLSKSVREVERAVAQRERPPEPPQFSKALSIILHLLFLLQKLRCGPEQEHLKRQTVYRLLKLNPRARGGHTPLHMAVDRDTTSVGRYPVGRFPSLAVASLLLECGADVDSRDYDNNTPLHIAAANGCPDIMAALIRAGAHFDATNAAQQTAYQLLEAQSSGRHALHPLNHTTLQCLAARAVTAHRLPYKGLISEQMEAFIELH", "text": "FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1A) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg- Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, leading to their ubiquitination and degradation. SUBCELLULAR LOCATION: Mitochondrion Cytoplasm. SIMILARITY: Belongs to the fem-1 family."}
{"protein": "MAPSSNKVGKAIQAKKAVVKGSKTNVRKNVRTSVHFRRPKTLVTARAPRYARKSAPARDKLDSFAVIKAPHTTESSMKKIEDHNTLVFIVDEKANKHHIKRAVHALYNVKAVKVNTLITPLQQKKAYVRLASDYDALDVANKIGFI", "text": "FUNCTION: This protein binds to a specific region on the 26S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
{"protein": "MPGWRLLTQVGAQVLGRLGDGLGAALGPGNRTHIWLFVRGLHGKSGTWWDEHLSEENVPFIKQLVSDEDKAQLASKLCPLKDEPWPIHPWEPGSFRVGLIALKLGMMPLWTKDGQKHVVTLLQVQDCHVLKYTSKENCNGKMATLSVGGKTVSRFRKATSILEFYRELGLPPKQTVKIFNITDNAAIKPGTPLYAAHFRPGQYVDVTAKTIGKGFQGVMKRWGFKGQPATHGQTKTHRRPGAVATGDIGRVWPGTKMPGKMGNIYRTEYGLKVWRINTKHNIIYVNGSVPGHKNCLVKVKDSKLPAYKDLGKNLPFPTYFPDGDEEELPEDLYDENVCQPGAPSITFA", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL3 family."}
{"protein": "MSWSFLTRLLEEIHNHSTFVGKIWLSVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIARMVEHSDVDRRFRSKSFSTRWKQHRGLEEAEDDHEEDPMMYPEIELESERENKEQQPPAKAKHDGRRRIREDGLMRIYVLQLLVRATFEVGFLIGQYLLYGFEVSPVFVCSRKPCPHKIDCFISRPTEKTIFLLIMYGVSCMCLLLNVWEMLHLGFGTIRDTLNNKRKELEDSGTYNYPFTWNTPSAPPGYNIAVKPDQMQYTELSNAKMAYKQNKANIAQEQQYGSNEENIPADLENLQREIKVAQERLDMAIQAYNNQNNPGSSSREKKSKAGSNKSSASSKSGDGKNSVWI", "text": "FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SIMILARITY: Belongs to the connexin family. Gamma-type subfamily."}
{"protein": "MKIAKVINNNVISVVNEQGKELVVMGRGLAFQKKSGDDVDEARIEKVFTLDNKDVSEKFKTLLYDIPIECMEVSEEIISYAKLQLGKKLNDSIYVSLTDHINFAIQRNQKGLDIKNALLWETKRLYKDEFAIGKEALVMVKNKTGVSLPEDEAGFIALHIVNAELNEEMPNIINITKVMQEILSIVKYHFKIEFNEESLHYYRFVTHLKFFAQRLFNGTHMESQDDFLLDTVKEKYHRAYECTKKIQTYIEREYEHKLTSDELLYLTIHIERVVKQA", "text": "FUNCTION: Mediates positive regulation of the glucanase operon (licST) by functioning as an antiterminator factor of transcription. Prevents termination at terminator lic-t. SIMILARITY: Belongs to the transcriptional antiterminator BglG family."}
{"protein": "MSASTNRRRLKDINTGAGENPSSGKKPLRSVTPLPISSKNSNPALQKSLSSKENPNPKLSHRSFGSTQKPVLRPVPRIDKSAVSGEGRVTRSTSSGLRGRSSSPSDLIRVFSDLRKRNESRVIGEKGESGQDKKSGLKSSGFKQGTSEIKVEPSSVCEKADEGSSCPVNSSKFEGSSVARNSISDPKAHALVGSGEKSTVALKSDSKIEKTGKGTSVALRRKSLDNVGKAMEMSKDIRGNEGSSNSTAKYPSKLHEKLAFLEGKVKKIASDIKKTKDMLDLNNPDSSKVIISDIHQKITGIEKSMSHVIDGPEKNKTTKAKSSVKGLNKEELEDRLLPHQRLLRSRTQSKTSSHVSKGHDSVESNKAVNAEEKPSAPVEENAIALEFLASLDKEKVTFMSDQNALENLEVQEMDTEEPSKENDVSKDVNLTSNLTEILRANEALEEIDDEENREEMELEEIDDGCMYQLNDIGSKTSTGGWFVSEGEAVILAHDDGSCSYYDVANSEFMVNECNSLSIWVRLYEVTGVFGFVHYVKSVYSPPDGISPNTWRDCWVVRAPGADGCSGRYVVAASAGNTLESGFCSWDFYTKDIKALHIEDGSSRVSRTALAPLPNNTSHGRNTPACAVVPETQQWWYRPCGPLIASTGSFQSIVKVFDIRDGEQIMKWGVQNPVSALDYSSPLQWRNRGKLVIAETEAISVWDVNSLHPEAQHTISSSGRKISAFHINNTDAEVGGGVRQRVSSLDAEGNDGVFCTSDSINILDFRNPSGIGAKIPKLGVNAQCVSSRGDSVFLGCTNQKSTVKKQMASSSQVQQFSIRKQRLVSTYSLPDSNSHPHHSAITQVWGNSNFVMATSGMGLFVFDTAKEETLQQQPLTSDYGSVQTVREIIGPNDMYCPSFDYSGCRVLLISRDRPALWRYLL", "text": "FUNCTION: Might be involved in division plane determination. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at the pre-prophase band."}
{"protein": "MSVIRPTTVEVETSLRLVAPDATALPVRASLRYDPADPYAVHVLFHAESAGGEAVSWSFARELLVTGLDEPAGIGDVRVWPWATPRGDFVALALSSPDGNALFEVPRSVLVRFLRRTYVVVARGREAEHLDVDTAVNRLLAGR", "text": "FUNCTION: Involved in sporulation-specific cell division (PubMed:19567872). Required for early stages of sporulation. Important in the process of growth cessation prior to sporulation-specific cell division. Recruits cell division protein FtsZ to the future septum sites and tethers the contractile ring structure (Z ring) to the cytoplasmic membrane during sporulation. Stimulates polymerization and filament length of FtsZ in vitro (By similarity). SUBCELLULAR LOCATION: Cell septum Note=Localizes to the divisome in sporogenic aerial hyphae in a ladder- like manner. Temporospatial localization is controlled by SsgA and it colocalizes with SsgA in presporulation foci. Localizes to the septum sites prior to FtsZ and after that colocalizes with FtsZ at the divisome throughout cell division. SIMILARITY: Belongs to the SsgA family."}
{"protein": "MKAKTLTATLALILLAFAQADYDVASYCQLVQSGTKLPSLDSCQNYYTCVSNGLPTLSSCSSGYVFNKDSQQCVPTGSFNCFFGVANPCQNQDKKFVPSAKQCNEWHYCLAGAIAGTGTCKEGQIFNFAKQSCVYGECSNTGNNILDSPNLSVCQIMPNGIYFGDNKNCSTWHKCSGMEEKKGTCPNGDNFDPTYASCVPSNMPACSRIQNPPSTGVVSGPPSTSPCSLGTVVGDLTSCSVYYKCENATRSNSTIWNTYTCSGQFFDVISKQCTSTNQARTLKGCNRCQFTTGSMYWVNAVDPQCSEYFTCSNGLETKSTASTCGAGNFFNEDLQYCMIGNSTVGQYAQTHGACENYTCNPNTRLCNLVTATNTTSSHR", "text": "FUNCTION: Binds chitin and may bind related oligosaccharide structures."}
{"protein": "MHIHLINPNSTASMTAQALESALLVKHAHTHVSASNPTDTPASIEGGADEAMSVPGMLAEIRQGEAQGVDAYVIACFDDPGLHAAREVAKGPVIGICQAAVQVAMTISRRFSVITTLPRSVPIIEDLVSDYGAERHCRKVRAIDLPVLALEEDPQRAERLLLKEIEIAKAEDGAEAIVLGCAGMSSLCDRLQKATGVPVIDGVTAAVKMAEALLGAGYATSKVNTYAYPRIKAAAGHKVCA", "text": "FUNCTION: May be involved in the asymmetric conversion of racemic 5- substituted hydantoins to the corresponding L-amino acids. Catalyzes the racemization via enolization of D- and L-5-monosubstituted hydantoins. It shows a slight preference for hydantoins with short rather than long aliphatic side chains or those with aromatic rings. SIMILARITY: Belongs to the HyuE racemase family."}
{"protein": "MNAARTGYRVFSANSTAACTELAKRITERLGAELGKSVVYQETNGETRVEIKESVRGQDIFIIQTIPRDVNTAVMELLIMAYALKTACARNIIGVIPYFPYSKQSKMRKRGSIVCKLLASMLAKAGLTHIITMDLHQKEIQGFFSFPVDNLRASPFLLQYIQEEIPNYRNAVIVAKSPDAAKRAQSYAERLRLGLAVIHGEAQCTELDMDDGRHSPPMVKNATVHPGLELPLMMAKEKPPITVVGDVGGRIAIIVDDIIDDVESFVAAAEILKERGAYKIYVMATHGILSAEAPRLIEESPIDEVVVTNTVPHELQKLQCPKIKTVDISLILSEAIRRIHNGESMAYLFRNITVDD", "text": "FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis. SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family."}
{"protein": "MKQRLIVKTALSAAILATLAGCATQPTQEWAADTTYKLTVLHTNDHHGRFWQNKYGEYGMAARKTLIDELRAEIQAEGGSVLLLSGGDINTGVPESDLQDAEPDFKGMSKIGYDAMALGNHEFDNPLDVLMKQKEWANFPMLSANIYDKKTGERMFQAYEMFDKQGIKIAVIGLTTEDTAKLGNPEFIGAIDFRDPKEEAKKLIAELKETEKPDLIFAVTHMGHYEDGKRGINAPGDVALARYLNEGDLDMIVGGHSQEPVCMEAPNVVKKNFKPADECKPDQQNGTYIVQAHEWGKYVGRADYEFRNGELRMVSYDLIPVNLKKKVEVDGKSQRVFIESEIKEDTALLEFLRPYQEKGQEQLNVKIADTNGKLEGDRNVVRFQQTNLGRLIAVSHMERAKADFAVMNSGGVRDSIEAGEVTYKDVLTVQPFANILTYTDMTGKEVLDYLNVVATKPVDSGAYAQFAGISMTVANGKVSNVFIGGKQLRLDETYRFTVPSYNAAGGDGYPKLTGHPGYVNTGFVDAEVLKEFLEKNSPIDVNKFAPNGEIVYK", "text": "FUNCTION: Degradation of extracellular 5'-nucleotides for nutritional needs. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the 5'-nucleotidase family."}
{"protein": "MNPEERLVTWLISLGVLESPKKTVCDPEEFLKSSLKNGVVLCKLINRLLPGSVEKYCLEPQTEADCIDNINDFLKGCATLQVEVFEPDDLYSGANFSKVLNTLLAVNKATEDQLSERPCGRSSSLSAATSSQTNPQVAVPSTAPEQHSEEKAEMTENGSHQLIVKARFNFKQTNEDELSVCKGDIIYVTRVEEGGWWEGTLNGRTGWFPSNYVREIKPSERPLSPKAIKGFDTAPLTKNYYTVVLQNILDTEKEYAKELQSLLVTYLRPLQSNNNLSTVEFTCLLGNFEEVCTFQQTLCQALEECSKFPENQHKVGGCLLNLMPHFKSMYLAYCANHPSAVNVLTQHSDDLERFMENQGASSPGILILTTSLSKPFMRLEKYVTLLQELERHMEDTHPDHQDILKAIIAFKTLMGQCQDLRKRKQLELQILSEPIQAWEGDDIKTLGNVIFMSQVVMQHGACEEKEERYFLLFSSVLIMLSASPRMSGFMYQGKIPIAGMVVNRLDEIEGSDCMFEITGSTVERIVVHCNNNQDFQEWMEQLNRLTKGPTSCGSLSKTSSSSCSTHSSFSSTGQPRGPLEPPQIIKPWSLSCLRPAPPLRPSAALGYKERMSYILKESSKSPKTMKKFLHKRKTERKASEEEYVIRKSTAALEEDAQILKVIEAYCTSASFQQGTRKDSVPQVLLPEEEKLIIEETRSNGQTIIEEKSLVDTVYALKDEVKELKQENKKMKQCLEEELKSRKDLEKLVRKLLKQTDECIRSESSSKTSILQ", "text": "FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF). SUBCELLULAR LOCATION: Cell projection, lamellipodium."}
{"protein": "SLEIDELARFAVDEHNKKQNALLEFGKVVNTKEQVVAGKMYYITLEATNGGVKKTYEAKVWVKPWENFKELQEFKPVDAATS", "text": "FUNCTION: Strong inhibitor of papain and ficin but poor inhibitor of cathepsin H, B and L. SIMILARITY: Belongs to the cystatin family."}
{"protein": "MASKPGPLTQWPWNNLGNYKYALVAPSAAYSTYRFVTASSAAERDLLNFMVFPMLLLRLLYGQLWITVSRHQTARSKHKIVNKSLDFEQIDRERNWDDQIILTALVFYLVSATMPQAQVAPWWSTKGMVVTAVLHAGPVEFLYYWLHRALHHHWLYARYHSHHHASIVTEPITSVIHPFAEEVVYFVLLAIPILSTVATGTVSVVTANGYLVYIDFMNYLGHCNFELVPKCLFHVFPPLKYLLYTPSFHSLHHTQFRTNYSLFMPVYDYIYGTTDKSSDELYERTLQGRDEAAWRPDVVHLTHLTAPESVFHNRLGFAAVASNPLGAAASGHLLRAASAVASPLLSLFASTFRSEANRLDKLNIETWVIPRFTSHYTSKSDGYKVSRLIEKAVSDAEASGARVLTLGLLNQGYDLNRNGELYVVRKPSLKTKIVDGTSLAVAAVLNMIPQGTKDVLLLGNANKISLVLTLSLCKREIQVRMVNKELYECLKQQLQPEMQEHLVLSRSYSSKVWLVGDGVTDEEQMKAQKGSHFVPYSQFPPNKARNDCVYHCTPALLVPESFENLHVCENWLPRRVMSAWRAAGIVHALEKWDGHECGGRVTGVQKAWSAALARGFRPYDDHHHPGITHDGRGGL", "text": "FUNCTION: Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MADSRDPASDQMKQWKEQRAPQKPDVLTTGGGNPIGDKLNIMTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDAMLFPSFIHSQKRNPQTHLKDPDMVWDFWSLCPESLHQVTFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLPVEEAGRLAQEDPDYGLRDLFNAIASGNYPSWTFYIQVMTFKEAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPANYFAEVEQMAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMHDNQGGAPNYYPNSFSAPEQQGSALEHHSQCSADVKRFNSANEDNVTQVRTFYTKVLNEEERKRLCENIANHLKDAQLFIQRKAVKNFTDVHPDYGARVQALLDQYNSQKPKNAIHTYVQAGSHIAAKGKANL", "text": "FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the catalase family."}
{"protein": "MTLVVLATGLLASGTAVSNADQASELNVDVHSSNVLATEDTRFLRSHQITDDKVEINEHGEEERMSGSNLFSALKLEKMGRDTSYRDKEFQRWKNYGNSVGDVTPHVPVSLKEAYATYLRIREMVLVND", "text": "FUNCTION: Effector that suppresses flg22-induced post-translational MAP kinase activation in tomato but not in Arabidopsis. The perception of highly conserved pathogen- or microbe-associated molecular patterns (PAMPs/MAMPs), such as flg22, triggers converging signaling pathways recruiting MAP kinase cascades and inducing transcriptional re- programming, yielding a generic antimicrobial response. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host cell membrane. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MSYTTATADSDDGMHSSIHNESPAPDSISNGCRSRGKRSVLKKGPWTSTEDGILIDYVKKHGEGNWNAVQKHTSLARCGKSCRLRWANHLRPNLKKGAFSQEEEQLIVEMHAKMGNKWAQMAEHLPGRTDNEIKNYWNTRIKRRQRAGLPLYPPEIYVDDLHWSEEYTKSNIIRVDRRRRHQDFLQLGNSKDNVLFDDLNFAASLLPAASDLSDLVACNMLGTGASSSRYESYMPPILPSPKQIWESGSRFPMCSSNIKHEFQSPEHFQNTAVQKNPRSCSISPCDVDHHPYENQHSSHMMMVPDSHTVTYGMHPTSKPLFGAVKLELPSFQYSETSAFDQWKTTPSPPHSDLLDSVDAYIQSPPPSQVEESDCFSSCDTGLLDMLLHEAKIKTSAKHSLLMSSPQKSFSSTTCTTNVTQNVPRGSENLIKSGEYEDSQKYLGRSEITSPSQLSAGGFSSAFAGNVVKTEELDQVWEPKRVDITRPDVLLASSWLDQGCYGIVSDTSSMSDALALLGGDDIGNSYVTVGSSSGQAPRGVGSYGWTNMPPVWSL", "text": "FUNCTION: Transcriptional activator of alpha-amylase expression that binds to 5'-CAACTGTC-3' motif in target gene promoter (PubMed:11743113). In vegetative tissues, inhibits growth by reducing cell proliferation. Promotes the expression of aleurone-related genes (e.g. CP1, CP, GASA1, BXL1 and BXL2) in seeds. Together with MYB33 and MYB101, promotes the programmed cell death (PCD) the vacuolation of protein storage vacuoles (PSVs) in the aleurone layers during seed germination (PubMed:20699403). Together with MYB33, facilitates anther and tapetum development (PubMed:15722475). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSLPDKAFPVSWDQFHRDARALAWRLAGLDQTFKAIVCITRGGLVPAAIISRELNIRLIETVCIASYHDYVNQGDMVLLKGIAPELAENGGEGVLVVDDLTDTGKTAAQVRTMLPKAHFACVYAKPKGVPTVDTFITEVSQDTWIYFPWDMGFTYQEPIAKGAR", "text": "FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'- monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily."}
{"protein": "EAVAPYERPALSKNIFYLREIADADQLVEAIKLKDGRTLDADIVVVGVGGRPLVSLFKTSIPDVYAVGDVATYPLKLYNELRRVEHVDHARLSIEEYDYLPYFYSRTFNLAWQFYGDNVGETVLFPDNFGTYWIKVVGVFLEGGTPDEYKVARVQPPVESLDQLAK", "text": "FUNCTION: Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process. SIMILARITY: Belongs to the FAD-dependent oxidoreductase family."}
{"protein": "MAVNVNTNVSAMTAQRYLTSATNAQQSSMERLSSGYKINSAKDDAAGLQISNRLNVQSRGLGVAVRNANDGISMAQTAEGAMKETTNILQRMRDLSLQSANGSNSKADRVAIQEEITALNDELNRVAETTSFGGNKLLNGTFATKSFQIGADNGEAVMLNIKDMRSDNALMGGKTYQAANGKDKNWGVEAGKTDLTITLKDKREGDVTISINAKEGDDIEELATYINGQTDMIKASVDEEGKLQLFTDNNRIDGAATFGGALAGELGIGAAQDVTVDTLDVTTVGGAQESVAIVDAALKYVDSHRAELGAFQNRFNHAINNLDNINENVNASKSRIKDTDFAKETTALTKAQILSQASSSVLAQAKQAPNSALALLG", "text": "FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaC is not essential for flagellar synthesis and motility (By similarity). FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaC is not essential for flagellar synthesis and motility. SUBCELLULAR LOCATION: Secreted Bacterial flagellum. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the bacterial flagellin family."}
{"protein": "MTDANHLLDPSGALPQTRPPWTSRDSLRITRVRAIVTAPEGQPLVVVRVDTSDDGLYGLGCATFTQRYAAVAAAVDEHVGPLAVGRHPADIEDITRLIHYSSYWRSGPVLNNALSGLDQALWDIAGKRAGMPVYELLGGRSRSAVEVYSHAAGGTIEATLDQAEELLAEGYRNVRLQLGGPGLGTYGAPGTLGGYPRSPHPDGWAVEQYLRDAPRLFAAARERLGDSVNLMHDVHSRLTPKQAVVLARALEPYRLSFLEDVIAPELYDRLPEVRAASPVPIAVGEQIGSVPDAVRLVRDGGVDLLRLHTSAVGGLTPTRKIVALCELLGVRTAFHSPADVSPVGVAANLAVDISTPAFGYQESHTYNDATHEVFPGTRVVREGHLYPAEEPGWGIEIDERAAAKFPPVKFLHERWSSGVRRPDGGLEAP", "text": "FUNCTION: Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. GalD subfamily."}
{"protein": "MESVKQRILTPGKEGLKNFAGKSLGQIYRVLEKKQDAGETIELTEDGKPLEVPEKKAPLCDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVDMVNNSTIHRGGKVIKEKAKFNWDPETVGMIHGSFFWGYIITQIPGGYIASRLAANRVFGAAILLTSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTSFCGSYAGAVIAMPLAGILVQYTGWSSVFYVYGSFGMIWYMFWLLVSYESPAKHPTITDEERRYIEESIGESANLLGAMEKFKTPWRKFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGMLSAVPHLVMTIIVPIGGQIADFLRSKQILSTTTVRKIMNCGGFGMEATLLLVVGYSHTRGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKNKSREEWQYVFLIAALVHYGGVIFYAIFASGEKQPWADPEETSEEKCGFIHEDELDEETGDITQNYINYGTTKSYGATTQANGGWPNGWEKKEEFVQEEVQNSYNYKDRDDYS", "text": "FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as a uniporter which transports preferentially L-glutamate but also, phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane therefore affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, functions as a vesicular K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular L-glutamate uptake. The vesicular H(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Also involved in the regulation of retinal hyaloid vessel regression during postnatal development (By similarity). May also play a role in the endocrine L-glutamatergic system of other tissues such as pineal gland and pancreas (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Synapse, synaptosome Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily."}
{"protein": "MAADGERSPLLSEPIDGGAGGNGLVGPGGSGAGPGGGLTPSAPPYGAAFPPFPEGHPAVLPGEDPPPYSPLTSPDSGSAPMITCRVCQSLINVEGKMHQHVVKCGVCNEATPIKNAPPGKKYVRCPCNCLLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGVRVICGHCKNTFLWTEFTDRTLARCPHCRKVSSIGRRYPRKRCICCFLLGLLLAVTATGLAFGTWKHARRYGGIYAAWAFVILLAVLCLGRALYWACMKVSHPVQNFS", "text": "FUNCTION: Catalyzes the hydrolysis of phosphatidylinositol-4,5- bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (PubMed:16365287). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5- monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (PubMed:16365287). Regulates lysosomal positioning by recruiting JIP4 to lysosomal membranes, thus inducing retrograde transport of lysosomes along microtubules (PubMed:29146937). Contributes to assembly of the V-ATPase complex in lipid rafts of the lysosomal membrane and to subsequent amino acid- dependent activation of mTORC1 (PubMed:29644770). May play a role in the regulation of cellular cholesterol metabolism (PubMed:25035345). SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein."}
{"protein": "MKTSMFLTLTGLVLLFVVCYASESEEKEFPKELLSSIFAADSDFKVEERGCLGDKCDYNNGCCSGYVCSRTWKWCVLAGPWCR", "text": "FUNCTION: Agglutinates erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 51 (Hntx-8) subfamily. Hntx-8 sub-subfamily."}
{"protein": "MLDAFSRVVTGADSKAAYVGGADLQALKKFVSEGNKRLDAVNAIVSNASCIVSDAVSGMICENPSLISPSGECYTNRRMAACLRDAEIILRYVSYSLLSGDSSVLEDRCLSGLKETYASLGVPAAGNARAVGIMKATVVAFINNTSNQKKLLTPSGDCSALASEAAGYFDKVTSALA", "text": "FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore- protein from the phycobiliprotein complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the phycobiliprotein family."}
{"protein": "MSTEFNQVNKLKKTPRRNDNLNEAKFVERLIKISRVTKVTKGGKKLSFRAVVVIGDENGKVGVGVGKAEDVVNAFKKAKTDGRKNLIDVPITKSLSIPHAVIGDLGACKIIMRPSIEGSGVIAGGAVRTVLEVAGIKNVIAKQLGSDNLLNNARTAIVALESLTTLDEVKRKRYHKSVL", "text": "FUNCTION: With S4 and S12 plays an important role in translational accuracy. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
{"protein": "MKVLLIGSGGREHALAWKIAQSPRLTKLYAAPGNPGIAEEAAIVDLHTENHEDVVDFCRTHAIDFVVVGPEAPLVAGLGDVLRAADIPTFGPSAAAAQLEGSKGFTKDLCARYGIPTGAYRRFTDAEPAKAYIREEGAPIVIKADGLAAGKGVTVAMSLDEAFAAVDECFAGAFGAAGAEVVVEAYLDGEEASFFCLCDGKSVLPLASAQDHKRVGDGDTGPNTGGMGAYSPAPVMTAEMVERTMKEIIEPTVRGMAESGYPFTGVFFAGLMITEKGPELIEYNVRFGDPECQVLMMRLESDLLPLLYAAATGTLEGMKAEWRDEAALTVVMASRGYPGAYEKDTPIAALPDASAATKVFHAGTAMKGGGLVAAGGRVLNVTATGKTVGEAKDAAYAAVRDVSWENGFYRNDIGWRAVARETA", "text": "SIMILARITY: Belongs to the GARS family."}
{"protein": "MELHIWPSDFGLPTIDVSSLQFLACSKMCASPVRVVQSARPWRSPNGELPMVAQIDGNAKPVTDFEKFVDILKKCGQDVVIDADLTTIERAQLDAFSCYLHHNLYPAVLHTFWADDLNYNTVTQYWYASHLHFPYNLYYLEKRKKKALRMLGGKNDTEILKDAFMALNTLSTKLGDNKFFCGNKPTSLDALVFGYLAPLLRVPLPNDRLQVQLSACPNLVRFVETVSSIYLPLSEDELKRQQSNRKMWQSRISKAKADKEAAKTTEEAAEAIPDEPPMRDAILFTIGALVLSVAFAIHTGLIQVSVEEEIAE", "text": "FUNCTION: Involved in transport of proteins into the mitochondrion. Essential for embryonic development (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane. SIMILARITY: Belongs to the metaxin family."}
{"protein": "MTKAASGDTKSTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREEHKIAFVKSKDGVPTPREICEVLDDYVIGQGHAKKVLAVAVHNHYKRLNHASKNNDVELAKSNILLVGPTGTGKTLLAQTLARIIDVPFTMADATTLTEAGYVGEDVENIVLKLLQAADYNVERAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTTNILFICGGAFAGLEKIISARGAAKSIGFGAKVTDPEERRTGEILRNVEPDDLQRFGLIPEFIGRLPVVATLEDLDEAALVKILTEPKNAFVKQYQRLFEMENIGLTFTEDALHQVAKKAIARKTGARGLRSIMEGILLETMFELPTYEGVEEVVVNAEVVEGRAQPLLIYAEKKGGAASA", "text": "FUNCTION: ATP-dependent specificity component of the Clp protease (By similarity). It directs the protease to specific substrates (By similarity). Required for degradation of response regulator CtrA, thus contributing to the G1-to-S transition (PubMed:9755166). Required to degrade DNA replication inhibitor toxin SocB, this function is probably the reason why the protease is essential in this organism (PubMed:24239291). Can perform chaperone functions in the absence of ClpP (By similarity). FUNCTION: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. SIMILARITY: Belongs to the ClpX chaperone family."}
{"protein": "MNIMIEIPEFIIPLIPWIRGVVGLVLVGAIFLGAMGAVWLERKLSADIQFRYGPSRVGKFGLLQLVADAIKLFTKEDMRPRNADRLLFDNAPIFMMSSVFLMLVAIPVGAVFINGVEYPLAVTEMDISVLYIEAMSAITIFGIFMIAYGSNNKYSLLGAFRNFARMVGYEVPLGITVVSVAIMTGSLNIVEIASAQGLLWNIFLQPIGFIVFFIALMADMGRLPFDQNESEEELVAGWITEYTGMRFGLGFFAEYIHMILGSFLVALLFLGGWNVPAFVANNPVLGLIAPTGFFLLKTVLVLMTIIGMRWAVPRFRIDQVVDLSWKRLLPLSLLNLVWAVGLGLYLGA", "text": "FUNCTION: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family."}
{"protein": "METQRASLCLGRWSLWLLLLGLVVPSASAQALSYREAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDPGTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVKQCVGTVTLKEIRGNFDITCNQLQSVRIIDLLWRVRRPQKPKFVTVWVR", "text": "FUNCTION: Exerts antimicrobial activity against both Gram-positive and negative bacteria at concentrations of 2-16 micro molar. Its activity appears to be mediated by its ability to damage bacterial membranes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cathelicidin family."}
{"protein": "MEEGMNILHDFGIQSTRYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLKETVGINLLWVAVVGDWFNLVFKWILFGQRPYWWVLDTDYYSNSSVPIIKQFPVTCETGPGSPSGHAMGAAGVYYVMVTSTLAIFRGKKKPTYGFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIRGIYNASLRKYCLITIFLFGFALGFYLLLKGLGVDLLWTLEKAKRWCERPEWVHLDTTPFASLFKNLGTLLGLGLALNSSMYRKSCKGELSKLLPFRFACIVASLVLLHLFDSLKPPSQVELIFYILSFCKSATVPFASVSLIPYCLARILGQTHKKSL", "text": "FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glucose-6-phosphatase family."}
{"protein": "MNTTLTDSQLDRWNQTGYIKLPEFLSEAETQNLREWVEEISAWPADDEKWMHHFEQTPSGVRPARTEYILAFHAGIRQLLTQGKIPDCAGALMGEPAILYKEKINYKYPGGGGYAAHQDAPAYEFIRNHITCSIAVDAATPENGCLFFTPELHQRGLLHLDKNGCIDREYADTLDWEPVPMQPGDALFFSSYAPHKSPPNETQQPRRTLYLTYNALAEGDLREEYYADKRRSFAQVDTTGGEKLKISKIGHFDGKPAQQT", "text": "FUNCTION: Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source (PubMed:30810303). Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid (PubMed:30810303). Is specific for the hydroxylation of methylphosphonate (PubMed:30810303). SIMILARITY: Belongs to the PhyH family."}
{"protein": "GKPICGETCFKGKCYTPGCTCSYPVCKKN", "text": "FUNCTION: Probably participates in a plant defense mechanism. SIMILARITY: Belongs to the cyclotide family."}
{"protein": "MSEFQKVVVIDAKGHLLGRLASVVAKQLLGGQKVVVVRCEELNISGHFFRNKLKYLAYLRKACRYNPSRGAFHFRAPSRIFQKAVRGMLPHKTARGQAALEHLQAVEGIPPPFDKQKRVVVPAALRVLRLKPGRKYCTVGRLSSEVGWKYNDIVAKLEERRKVKSAAFYQAKLAKQKKIASAKEASPVNQKLSQFGY", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL13 family."}
{"protein": "MDTKKIFKHIPWVILGIIGAFCLAVVALRRGEHISALWIVVASVSVYLVAYRYYSLYIAQKVMKLDPTRATPAVINNDGLNYVPTNRYVLFGHHFAAIAGAGPLVGPVLAAQMGYLPGTLWLLAGVVLAGAVQDFMVLFISSRRNGASLGEMIKEEMGPVPGTIALFGCFLIMIIILAVLALIVVKALAESPWGVFTVCSTVPIALFMGIYMRFIRPGRVGEVSVIGIVLLVASIYFGGVIAHDPYWGPALTFKDTTITFALIGYAFVSALLPVWLILAPRDYLATFLKIGVIVGLALGIVVLNPELKMPAMTQYIDGTGPLWKGALFPFLFITIACGAVSGFHALISSGTTPKLLANETDARFIGYGAMLMESFVAIMALVAASIIEPGLYFAMNTPPAGLGITMPNLHEMGGENAPIIMAQLKDVTAHAAATVSSWGFVISPEQILQTAKDIGEPSVLNRAGGAPTLAVGIAHVFHKVLPMADMGFWYHFGILFEALFILTALDAGTRSGRFMLQDLLGNFIPFLKKTDSLVAGIIGTAGCVGLWGYLLYQGVVDPLGGVKSLWPLFGISNQMLAAVALVLGTVVLIKMKRTQYIWVTVVPAVWLLICTTWALGLKLFSTNPQMEGFFYMASQYKEKIANGTDLTAQQIANMNHIVVNNYTNAGLSILFLIVVYSIIFYGFKTWLAVRNSDKRTDKETPYVPIPEGGVKISSHH", "text": "FUNCTION: Transports pyruvate with a high affinity and specificity. The process is driven by the proton motive force (PubMed:29061664). Under nutrient limiting conditions, mediates the uptake of pyruvate, thus enabling it to be used as a carbon source for the growth and survival (PubMed:29061664). Part of a nutrient-sensing regulatory network composed of the two-component regulatory systems BtsS/BtsR and YpdA/YpdB, and their respective target proteins, BtsT and YhjX (PubMed:24659770). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptide transporter carbon starvation (CstA) (TC 2.A.114) family."}
{"protein": "MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIVAYQRAFPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEQQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQQDASLPHCRFYEEFDAHGRQVPLPAGIYNLDDLKALGQRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQSNLDTLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEIADLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARADKRGKLPRWIQEHLTDSNLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLQSEETLRRVEQIAQQL", "text": "FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre- initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily."}
{"protein": "ISCTGSKQCYDPCKKKTGCPNAKCMNKSCXCYGC", "text": "FUNCTION: Binds to voltage-gated potassium channels Kv1.3/KCNA3 (IC(50)=0.48 uM) and Kv1.1/KCNA1 (IC(50)=6.7 uM) and inhibits channel activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 06 subfamily."}
{"protein": "MASIDPYQHIIVEHQYSHRFTVTVIKATNVTKGTFGDMLDTPDPYVELYISSAPDSRKRTKHFNNNINPVWNETFEFILDPNQDNVLEITLMDANYVMDESLGTTTFPISSVKPGEKKQVPFTFNKVTEMILEFLLEVCSSTDLRFSMALCDQEKFFRQKRKNQVINGLRKLLGPEKTKDLNPTSRDVPVIAVLGSGGGFRAMIGFSGVMKALFESGVLDCVTYIAGLSGSTWYMSALYSHADFPNKGPKEINKELMNNVSHNPLLLLTPQKVKRYIEALWKKKSSGQPVTFTDIFAMLIGETLIKDRMNRKLSHMQEKISHGQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMPPDHFGSKFFMGTVIKKYEENPLHFLMGVWGSAFSILINRVLGVSTNNQGSTMEEEIENLKPKHILGNDSSDSDDEMQEPKGTENSKAEEEYQRNNQASWVQRMLMALLGDSALFNTREGRAGKVHNFMLGLNLNTSYPYSPLSGLCTQQSMEEDEFDAAVADPDEFEQIYEPLDVKSKKIHIVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNKLPFPKIDPHVFDREGLKECYIFKPKNPSVEKDCPTVIHFVLANLQFRNFKAPGVPRETAEEKEFADFDIFDDPETPFSTFNFQYPNEAFKRLHDLMEFNTLNNINVIKQAMVESIEYRKQHPSRCSVSLNDVEARKLLHKDSQSKFQM", "text": "FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle Note=Translocates to membrane vesicles in a calcium- dependent fashion."}
{"protein": "MERLMRLTILLFLGAVLAGCASVPSTSAPQAIGTVERPVPSNLPKPSPGMDPDVLLREFLKATADPANRHLAARQFLTESASNAWDDAGSALLIDHVVFVETRSAEKVSVTMRADILGSLSDVGVFETAEGQLPDPGPIELVKTSDGWRIDRLPNGVFLDWQQFQETYKRNTLYFADPTGKTVVPDPRYVAVSDRDQLATELVSKLLAGPRPEMARTVRNLLAPPLRLRGPVTRADGGKSGIGRGYGGARVDMEKLSTTDPHSRQLLAAQIIWTLARADIRGPYVINADGAPLEDRFAEGWTTSDVAATDPGVADGAAAGLHALVNGSLVAMDAQRVTPVPGAFGRMPEQTAAAVSRSGRQVASVVTLGRGAPDEAASLWVGDLGGEAVQSADGHSLSRPSWSLDDAVWVVVDTNVVLRAIQDPASGQPARIPVDSTAVASRFPGAINDLQLSRDGTRAAMVIGGQVILAGVEQTQAGQFALTYPRRLGFGLGSSVVSLSWRTGDDIVVTRTDAAHPVSYVNLDGVNSDAPSRGLQTPLTAIAANPSTVYVAGPQGVLMYSASVESRPGWADVPGLMVPGAAPVLPG", "text": "FUNCTION: May modulate activity of the MtrAB system in controlling homeostasis of the cell wall and cell division (By similarity). Partially restores antibiotic resistance to M.smegmatis in which this gene has been disrupted. FUNCTION: May modulate activity of the MtrAB system in controlling homeostasis of the cell wall and cell division. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Secreted, cell wall. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Secreted, cell wall. SIMILARITY: Belongs to the LpqB lipoprotein family."}
{"protein": "MKGKEEKEGGARLGAGGGSPEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLSRLIAAERERELEECQRNHEGDEDDSHVRAQQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY", "text": "FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 (PubMed:15466472). Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 (PubMed:10330192, PubMed:11146632, PubMed:15466472). Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation (PubMed:11557750, PubMed:23990462). Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome (PubMed:19713937). Mediates polyubiquitination of CYP3A4 (PubMed:19103148). Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation (PubMed:19567782). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome (PubMed:24043303). Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD- L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity (PubMed:28813410). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed:29883609). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg)."}
{"protein": "MELQLTGKESGWWIVSHENKLWLPKGELPQGNAANWSLQGATARQIGEWQGQAVWLIRQMMSTDMGSVRQLLDVDRGLFQLAGRGVQLAEFYRSHRYCGYCGHQMHASRTEWACLCNHCRERYYPQIAPCVIVAIRRGDEILLAQHVRHRGGINTVLAGFVEVGETLEQAVSREVLEESNIHIKNLRYVTSQPWPFPHSLMMAFMAEYDSGELRHDPKELLNAGWYRYDQLPLLPPPGTVARRLIEDTVVLCREEQFDDGE", "text": "FUNCTION: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates. SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily."}
{"protein": "MFSWLPFSCALLLLQPLPARSLENAYTAEVGKNAYLPCSYTVPAPGTLVPICWGKGSCPLLQCASVVLRTDETNVTYRKSRRYQLKGNFYKGDMSLTIKNVTLADSGTYCCRIQFPGPMNDEKLELKLSITEPAKVIPAGTAHGDSTTASPRTLTTEGSGSETQTLVTLHDNNGTKISTWADEIKDSGETIRTAVHIGVGVSAGLALALILGVLILKWYSSKKKKLQDLSLITLANSPPGGLVNAGAGRIRSEENIYTIEENIYEMENSNEYYCYVSSQQPS", "text": "FUNCTION: Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand. Regulates macrophage activation. Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF-kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits. In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN. Expressed on Treg cells can inhibit Th17 cell responses. Receptor for LGALS9. Binding to LGALS9 is believed to result in suppression of T-cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6. Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis-infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth. However, the function as receptor for LGALS9 has been challenged (By similarity). Also reported to enhance CD8+ T cell responses to an acute infection such as by Listeria monocytogenes. Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent. May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells. Expressed on T-cells, promotes conjugation but not engulfment of apoptotic cells. Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha. In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid- sensing and trafficking of nucleid acids to endosomes. Can enhance mast cell production of Th2 cytokines Il-4, IL-6 and IL-13. Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9. In contrast, shown to suppress NK cell-mediated cytotoxicity. Negatively regulates NK cell function in LPS-induced endotoxic shock. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Cell junction Note=Localizes to the immunological synapse between CD8+ T-cells and target cells. SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family."}
{"protein": "MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the alkaline phosphatase family."}
{"protein": "MPFPLNRTDTALVISPSEFRIIGIFISICCIIGVLGNLLIIIVFAKRRSVRRPINFFVLNLAVSDLIVALLGYPMTAASAFSNRWIFDNIGCKIYAFLCFNSGVISIMTHAALSFCRYIIICQYGYRKKITQTTVLRTLFSIWSFAMFWTLSPLFGWSSYVIEVVPVSCSVNWYGHGLGDVSYTISVIVAVYVFPLSIIVFSYGMILQEKVCKDSRKNGIRAQQRYTPRFIQDIEQRVTFISFLMMAAFMVAWTPYAIMSALAIGSFNVENSFAALPTLFAKASCAYNPFIYAFTNANFRDTVVEIMAPWTTRRVGVSTLPWPQVTYYPRRRTSAVNTTDIEFPDDNIFIVNSSVNGPTVKREKIVQRNPINVRLGIKIEPRDSRAATENTFTADFSVI", "text": "FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MLRPQLNPSSSHHHTTTTSSSSSTQLYFASSSCIASLRRPSPPSLIAGAGCRTTRRRQQGRQRVVVRCASSSAASSASEAARRGTGSSDMAPAAVVKVKAVATIKVTVEGLLNSLRPSKAIDNIRDLIGRSLFLELVSSELEAKTGKKKATVHSYAHKVDDDDHGVVTYEADFDVPTGFGPIGAVVVTNELGQEMFLEDLNLTAGDGAGNSTVLPIRCNSWVQPKSSIDEGTPGKRIFFAKAYLPGQTPAGLRSYREEDLKQKRGNGAGQREADDRVYDYDVYNDLGNPDSNGDLARPVLGGSKQFPYPRRCRTGRPPSKKDPKSETRKGNVYVPRDEEFSEVKNAQFLLKTLQSVLHAAVPAAQSALIDNLSLNLPFPSFFVIDKLFEDGVELPGVEKLGFLHSIVPRLLELLRDSPGDKILLFDTPANVQKDKFAWLRDEEFARETLAGINPYAIELVREFPLKSKLDPAVYGPAESAITADLLEEQMRRVMTVEEAISQKRLFMLDFHDLFLPYVHKIRSLKHTTMYGSRTIFFLTDDGTLRLLAIELTRPASPSQPQWRQVFTPSTDTTKSWLWRMAKAHVRAHDAGHHELITHWLRTHCAVEPYIIAANRQLSEMHPIYQLLHPHFRYTMRINALARSRLISAAGIIELSFSPQKYSMELSSVAYDKLWRFDMEALPADLVRRGMAEEDPTAEHGLRLAIEDYPFANDGLLIWDAIKTWVQAYVARFYPDADSVAGDEELQAFWTEVRTKGHGDKKDAPWWPKLDSPESLAHTLTTIVWVAAAHHAAVNFGQYDFGGYFPNRPSIARTVMPVEEPVDGAAMERFLDNPDQALRECFPSQVQATVVMAVLDVLSTHSTDEEYLGGEQTRPWNSDAAVQAAYAGFTARLKEIEGVIDGRNKDRKLKNRCGAGILPYQLMKPFSDAGVTGMGIPNSTSI", "text": "FUNCTION: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the lipoxygenase family."}
{"protein": "MLQTTLLALQGLSCMNCAQRVKAALESREDVHHAEVNVHYAKVTGEADTHALIETIKQTGYQATEAQTPDVELHLSGLSCGHCTETVRKALEAVSGVISADVTLESANVYGKADIQTLIAAVEQAGYHATQQGIDSPKTEPLTHSAQSQPESLAAAPNTVPATNVALATSTVSDTNTVLPTNTALPTNTTSTTSTADTASATSTAPVINPLPVTESVAQPAASEGESVQLLLTGMSCASCVSKVQNALQRVDGVQVARVNLAERSALVTGTQNNEALIAAVKNAGYGAEIIEDEGERRERQQQMSQASMKRFQWQAALGLLLGIPLMAWGLFGGSMTLTPETQTPWLIIGIITLLVMIFAGGHFYRNAWVSLKNGRATMDTLVALGTGAAWIYSITVNIWPDVFPMEARHLYYEASAMIIGLINLGHAMEQRARQRSSNALERLLDLAPPTAKLVTDDGEKVIPLADVQLGMILRLTTGDRVPVDGEIVQGEVWMDEAMLTGEPIPQQKSVGDIVHAGTQVQDGTVQFRASAIGSQTTLARIIKLVRQAQSSKPEIGKLADRISAVFVPTVVVIAIVAGLIWYFFGPQPQLVYTLVVATTVLIIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQQASNLDTLVFDKTGTLTEGHPQVVAIHTFNGVSEQQALGWAAALETGSNHPLARAILQRAEGLTLATASQFRTLRGLGVSGEVDGIPLLLGNNRLLEEQQIDTRELQSLIQQQAESGATPVILTANGKPAALLSIRDPLREDSIGALQRLHQLGYSLVMLTGDNPITANAIAKEAGIDRVIAGVLPDGKADAIKQLQAAGHKVAMIGDGINDAPALAQADVGIAMGGGSDIAIETAAITLMRHSLYGVVDAVELSKATLRNMKQNLLGAFFYNALGIPIAAGILYPFTGTLLSPVVAGAAMALSSITVVSNANRLLRFKPKQ", "text": "FUNCTION: Involved in copper export. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily."}
{"protein": "MADAPTRATTSRVDSDLDAQSPAADLVRVYLNGIGKTALLNAAGEVELAKRIEAGLYAEHLLETRKRLGENRKRDLAAVVRDGEAARRHLLEANLRLVVSLAKRYTGRGMPLLDLIQEGNLGLIRAMEKFDYTKGFKFSTYATWWIRQAITRGMADQSRTIRLPVHLVEQVNKLARIKREMHQHLGREATDEELAAESGIPIDKINDLLEHSRDPVSLDMPVGSEEEAPLGDFIEDAEAMSAENAVIAELLHTDIRSVLATLDEREHQVIRLRFGLDDGQPRTLDQIGKLFGLSRERVRQIERDVMSKLRHGERADRLRSYAS", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. A non-essential principal sigma factor that responds to cell envelope stress and hypoxia. Controls a regulon of about 40 genes, with another 100 genes expression being altered during SDS stress and about 50 gene being altered during diamide (oxidative) stress. FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. A non-essential principal sigma factor that responds to cell envelope stress and hypoxia (By similarity). SIMILARITY: Belongs to the sigma-70 factor family."}
{"protein": "MREESWEDHDTIQLTAQRKYLAEVQALETLLTRELSAFLTEPGSKKTNIINRITGKTYALPSTELLRLYEHLEQCRKQGALMYFLERQGTYSGLMLDYDLKLNTNAVPPLEPPALSRLCHRIFVHIKNSSVLPEGSHKIHFFFTLKPEVVQGKYGFHVLIPGLKLAASTKKSIIGSLQHDATVQKILHEQGVANPESCLDPHSASVPSLLYGSSKLNHKPYQLKTGFELVFDSSDPDYIPIHQIKNIESYNLVSELSLTNEQGSLVRPVYCAADIAAEKEEEIPTDDHSLSILMLHDPEARYLHKILNLLPPEYYVEYPLWSNVVFALANTSANYRPLAEWFSQKCPEKWNTGGKEKLEKLWNDASRHTEKKITKRSIMYWAHKHAPQQYKEIVEQGYFSILAEYVYSYNGMLEHYMIAKVIYAMMGNKFVVDVDSNGKYVWFEFVLPGQPMNQGEIWKWRKEVNPDELHIYISENFSRVMDRITEHIKYHLSQPHETNILNYYKKLLKAFERSKSKIFNDSFKKGVIRQAEFLFRQRSFIQTLDTNPHLLGVGNGVLSIETIPAKLINHFHEHPIHQYTHICYVPFNPENPWTKLLLNALQDIIPELDARLWIMFYLSTAIFRGLKEALMLLWLGGGCNGKTFLMRLVAMVLGDHYASKLNISLLTSCRETAEKPNSAFMRLKGRGYGYFEETNKSEVLNTSRLKEMVNPGDVTARELNQKQESFQMTATMVAASNYNFIIDTTDHGTWRRLRHYRSKVKFCHNPDPGNPYEKKEDPRFIHEYIMDPDCQNAFFSILVYFWEKLQKEYNGQIKKVFCPTIESETEAYRKSQDTLHRFITERVVESPSAETVYNLSEVVTAYAEWYNANINVKRHIALELSQELENSVLEKYLQWSPNKTRILKGCRILHKFETLQPGESYIGVSTAGTLLNTPICEPKNKWWEWSPNLSAPPEKEASAPTP", "text": "SIMILARITY: Belongs to the asfivirus helicase C962R family."}
{"protein": "MTKETIRVVICGDEGVGKSSLIVSLTKAEFIPTIQDVLPPISIPRDFSSSPTYSPKNTVLIDTSDSDLIALDHELKSADVIWLVYCDHESYDHVSLFWLPHFRSLGLNIPVILCKNKCDSISNVNANAMVVSENSDDDIDTKVEDEEFIPILMEFKEIDTCIKTSAKTQFDLNQAFYLCQRAITHPISPLFDAMVGELKPLAVMALKRIFLLSDLNQDSYLDDNEILGLQKKCFNKSIDVNELNFIKDLLLDISKHDQEYINRKLYVPGKGITKDGFLVLNKIYAERGRHETTWAILRTFHYTDSLCINDKILHPRLVVPDTSSVELSPKGYRFLVDIFLKFDIDNDGGLNNQELHRLFKCTPGLPKLWTSTNFPFSTVVNNKGCITLQGWLAQWSMTTFLNYSTTTAYLVYFGFQEDARLALQVTKPRKMRRRSGKLYRSNINDRKVFNCFVIGKPCCGKSSLLEAFLGRSFSEEYSPTIKPRIAVNSLELKGGKQYYLILQELGEQEYAILENKDKLKECDVICLTYDSSDPESFSYLVSLLDKFTHLQDLPLVFVASKADLDKQQQRCQIQPDELADELFVNHPLHISSRWLSSLNELFIKITEAALDPGKNTPGLPEETAAKDVDYRQTALIFGSTVGFVALCSFTLMKLFKSSKFSK", "text": "FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (Probable). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the mitochondrial Rho GTPase family."}
{"protein": "MYLVKSAGSPIYRTLRTLTTSNLMAATIASAKDPLTGPRYEREPNVLRKKLASVVPGTVNLQVLGSGANGAPAAVYLFTDQARYLFNCGEGTQRLAHEHKTRLSRLEQIFLTQNTWASCGGLPGLTLTIQDAGVRDIGLHGPPHLGSMLQSMRRFVVLKNLQVRPNDCSEGACFEDSILKVDSLPLINSEDPTKSVINYICQLKPRAGALNLVKCVEQGVPPGPLLGQLKNGNDITLPDGKVVRSVDVTEASETALSFVFLDVPSENYLPALLTHGKRLKKLGEEKLTEVALVVHFTPYHISSRQVYKDFVVESFSSEAQHIYLSSPLNQFSGYAAAHRIQHQLHQLAPQVFPLLGEQLSCQSQTLSLNLKKTKLDEADSEDKANAKANETEEQGVVAMTNYHLRPRKGLDRTLESKLTPEEYVKETHAVPGFLELLAKFKEEYSFPDNSADSYPKIIFLGTGSCIPNKTRNVSSILIRTAIDAYVLLDCGEGTYGQIVRLYGHEKGQLILRQLQAIYVSHLHADHHIGLIGLLRERRQLKPRADPLILLAPRQIEPWLEFYNRQIETVEDAYTLVGNGELLASPLSGEQVERLGITSISTCLVRHCPNSFGISLTLAAKHNSEPVKITYSGDTMPCQDLIDLGRDSTVLIHEATMEDDLEEEARLKTHSTVSQAIQQGRNMNARHTILTHFSQRYAKCPRLPSDEDMQRVAIAFDNMEVTIEDLQHYHKLYPALFAMYAEYTEELEQRAVKRELKQERKRKLAET", "text": "FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity of nuclear and mitochondrial pre-tRNA. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. May participate in tRNA processing in the developing embryo. SUBCELLULAR LOCATION: Nucleus Mitochondrion. SIMILARITY: Belongs to the RNase Z family."}
{"protein": "MFTMKKSLLFFFFLGTIALSLCEEERGADEEENGAEITDEEVKRGILLNTLKGAAKNVAGVLLDKLKCKITGGC", "text": "FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MSVRNIFADESHDIYTVRTHADGPDGELPLTAEMLINRPSGDLFGMTMNAGMGWSPDELDRDGILLLSTLGGLRGADGKPVALALHQGHYELDIQMKAAAEVIKANHALPYAVYVSDPCDGRTQGTTGMFDSLPYRNDASMVMRRLIRSLPDAKAVIGVASCDKGLPATMMALAAQHNIATVLVPGGATLPAKDGEDNGKVQTIGARFANGELSLQDARRAGCKACASSGGGCQFLGTAGTSQVVAEGLGLAIPHSALAPSGEPVWREIARASARAALNLSQKGITTREILTDKAIENAMTVHAAFGGSTNLLLHIPAIAHQAGCHIPTVDDWIRINKRVPRLVSVLPNGPVYHPTVNAFMAGGVPEVMLHLRSLGLLHEDVMTVTGSTLKENLDWWEHSERRQRFKQLLLDQEQINADEVIMSPQQAKARGLTSTITFPVGNIAPEGSVIKSTAIDPSMIDEQGIYYHKGVAKVYLSEKSAIYDIKHDKIKAGDILVIIGVGPSGTGMEETYQVTSALKHLSYGKHVSLITDARFSGVSTGACIGHVGPEALAGGPIGKLRTGDLIEIKIDCRELHGEVNFLGTRSDEQLPSQEEATAILNARPSHQDLLPDPELPDDTRLWAMLQAVSGGTWTGCIYDVNKIGAALRDFMNKN", "text": "FUNCTION: Catalyzes the dehydration of D-xylonic acid to form 2- dehydro-3-deoxy-D-pentonate. SIMILARITY: Belongs to the IlvD/Edd family."}
{"protein": "MVSSFTSAPRSGFYYFAQGWKLVSQPGIRRFVILPLLVNILLMGGAFWWLFTQLDVWIPTFMSYVPDWLQWLSYLLWPLAVISVLLVFGYFFSTIANWIAAPFNGLLAEQLEARLTGATPPDTGIFGIMKDVPRIMKREWQKFVWYLPRAIVLLILYFIPGIGQTVAPVLWFLFSAWMLAIQYCDYPFDTHKVPFKEMRTALRTRKITNMQFGALTSLFTMIPLLNLFIMPVAVCGATAMWVDCYRDKHAMWR", "text": "FUNCTION: High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CysZ family."}
{"protein": "MNPAVFLSLADLRCSLLLLVTSIFTPITAEIASLDSENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEYPDKNQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKSNPVHEIQSLDEVTNLDRSKRNIIGYFEQKDSENYRVFERVASILHDDCAFLSAFGDLSKPERYNGDNVIYKPPGRSAPDMVYLGSMTNFDVTYNWIQDKCVPLVREITFENGEELTEEGLPFLILFHMKDDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIPGKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQDQDVASSPPESSFQKLAPSEYRYTLLRDRDEL", "text": "FUNCTION: Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "MATPGALAKFRLPPLPTIGEIVKLFNLRAEKQLSQNFLLDLKLTDKIVRRAGNLQNAYVCEVGPGPGGITRSILNAGVEELLVVEKDTRFIPGLKMLNEASGGKVRTVHGDILTYRMDRAFPKHLIKSWDDEPPNVHIIGNLPFSVSTPLIIKWLEQVADRTGPFTYGRTQMTLTFQQEVAERLTASTKNKQRSRLSIMSQYLCNVKNCFTIPGRAFIPKPKVDVGVVHLTPFVQPKIEQPFKLVEKVVRCIFQFRRKYCHHGVSILFPEEIRIQLTEQMLRLADVDPTLRPTELTMTHFKKLCNVYREMCDQNPHLFSYNYREELRMKKLQGKSTEEEDDLLQ", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA. Stimulates transcription independently of the methyltransferase activity (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. KsgA subfamily."}
{"protein": "MSVHPTLRFLATALVALGAGAALAQDAPRLTGADRPMSEVAAPPLPETITDDRRVGRNYPEQPPVIPHSIEGYQLSVNANRCLECHRRQYSGLVAAPMISITHFQDREGQMLADVSPRRYFCTACHVPQTNAQPLVTNEFRDMLTLMPASNEAE", "text": "FUNCTION: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the NapB family."}
{"protein": "MGERKGVNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGAQRKEERWDMEDNEQVLTTEHEKKQKLEMDAMFRLEHGEADRSTLKKALPTLSHIQEAQSAWKDDFALNSMLRKRFREKKKAMQEEEERDQALQAKASLAIPLVPETEDDRRLAALLKFHTLDSYEDKQKLKRTEIISRSWFPSTPGASASSSSSSKTNSVLKKLAQNRRATPTSSPVTMGHLGIVRRRSREVPESPQHVAETFKSGEPQLPEGTNQNRPVSPQDCSLETAETPKNSSALGQEESCQDRPQPPPDTSPEAPNPQDTPQPCSLGSSLVADYSGSESE", "text": "FUNCTION: May be involved in mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC16 family."}
{"protein": "MKLLEQMVYVECFMIIMATLLVSMSYGHRAMINDVAEAPVIDNVGSPTNGLDSSWYDARATFYGDIHGGETQQGACGYGDLFKQGYGLETAALSTALFNEGYTCGACYQIMCVHDPQWCLPGTIKITATNFCPPDYSKTEGVWCNPPQKHFDLSLPMFLKIAQYKAGVVPVKYRRISCARTGGVKFETKGNPYFLMILPYNVGGAGDIKLMQVKGDKTGWITMQKNWGQNWTTGVNLTGQGISFRVTTSDGVTKDFNNVMPNNWGFGQTFDGKINF", "text": "FUNCTION: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily."}
{"protein": "MAQLPPRAPSAAAAAGQEWSAMAAAGEFLGFAAARRGAHRRSASDSAAFLMEAAVPMDDVIVGVGGGGEFDRLDDEQLMSMFSDVEAPAVSDGGGERGPAGEAHLMDMGDGDDGMGATSPAGAGAMAAAAAAAAADGIADPKRVKRILANRQSAQRSRVRKLQYISELERSVTTLQMEVSALSPRVAFLDHQRSLLTVGNSHLKQRIAALAQDKIFKDAHQEALKKEIERLRQVYHQQQIKATGGADIATAASMQAKHELLACEGAAMR", "text": "FUNCTION: Transcription regulator. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MITGYSTPSAHVLMSSRAFKSSSYRAAAGQTQHYLARSSLPVVKNSWGSPPSPFNELPRVSRGVPLSYLSASSSLLLNGEQGSLSGTLPVLPVRRKTLLTPRASKDVPSSFRFPPMTKKPQWWWRTLACLPYLMPLHETWMYAETAYHLHPFLEDFEFLTYPFLGAIGRLPSWFLMAYFFVAYLGIVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSKWMPLGVYWGKFGMHFWTAVAFAYLFTVLESIRCALAGMYADIPFVCDAAYIQIPYD", "text": "FUNCTION: Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein- conducting channel at the inner envelope. Seems to be specific for photosynthesis-related pre-proteins. Partially redundant with TIC20-IV, but not with TIC20-II or TIC20-V. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tic20 family."}
{"protein": "MRAIFLILCSVLLNGCLGMPESVKPVSDFELNNYLGKWYEVARLDHSFERGLSQVTAEYRVRNDGGISVLNRGYSEEKGEWKEAEGKAYFVNGSTDGYLKVSFFGPFYGSYVVFELDRENYSYAFVSGPNTEYLWLLSRTPTVERGILDKFIEMSKERGFDTNRLIYVQQQ", "text": "FUNCTION: Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MAGYKPVVIQTYPVLGEKITQDTLYWNNYKTPVQIKEFGAVSKVDFSPQPPYNYAVTASSRIHIYGRYSQEPVKTFSRFKDTAYCATFRQDGQLLVAGSEDGVVQLFDISGRAPLRQFEGHTKAVHTVDFTADKYHVVSGADDYTVKLWDIPNSKEILTFKEHSDYVRCGCASKLNPDLFVTGSYDHTVKMFDARTNKNVLCVEHGQPVESVLLFPSGGLLVSAGGRYVKVWDMLKGGQLLVSLKNHHKTVTCLCLSSSGQRLLSGSLDRKVKIYSTTSYKVVHSFDYAASILSLALSHQDETVVVGMTNGILSVKHRKSEAKKESLPRRRRPAYRTFIKGKIYTKQRDDIVVTRPAKKHLEWYDRDLKSFRISKALDRVLEPNCVIKTPEVTVSIIKELNRRGVLANALAGRDEKEITRVLNFLIRNLSQPRFAPVLINAAEIIIDIYLPVIGQSSVVDKKFIVLQGLVEKEIDYQRELLETLGMMDMLFATMTRNGSAPVWEHVPAELPEEKTESPRQPSDTDKNS", "text": "FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Note=Found predominantly at the fibrillar center."}
{"protein": "MKQDSQSENESIVCDLSVSEDQRNVKFFSDLQTPIPKHLPFFMDVTLRDGNQALRRPWNLEQKETIFKQLLKLGVQGIEVGFASSNNQEFEACKYLSSIAPDNVVISSLSRAVEKEIEVSWKAIRFAPKPRIHIVYPVSAFTIQNVLKISPEKVLDRISQSVAYAKSLVGSKGEVQFSGEHFGDSLENLDFAAEAFQIALNNGADVVNLPNTVERYRPWLFVSMVKAVANLLPEDTRISIHTHNDLGMATATTVESYFAGAVQLETALNGLGERAGNTNTYEVAIALHNCGVEVPLNFSTIYETSRLVSYLSEIPIYEKAPLIGEDVISHRSGIHQDGVAKTRHLQKGAYRAFDAALIGRPEGDRIEFTNQSGKSAVYCILKDAGENITLEEAGRLQPILKKISEDLGRRELTLEEIRIEWNRLLRAI", "text": "FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). Has high alpha- isopropylmalate synthase activity and low citramalate synthase activity (PubMed:15292141). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily."}
{"protein": "MNDSCSWDQLWDQQGTLNEYTGKGIDLLERIMAYSKERASIELEYSSKLKALSKKTAMKMKSESELWNSVSYVKGFHDVIAGIVPVATQHELIAENLKSAVIPFTTQKIAEYRVAKKQLESDNSNLGKQLRMVIDEMAKSHKEYVKCYKETEAAMLKYAKAEKNMDISRLELEKTKNNYQQKCGMLEESKQTYAVMTTKANEEQSAHYDRKLPQLLDNYKKLHTNRILDTVEILSKCVEAESCVNQIIASCHNDMRRDIGLIDPSRDANLVVENMKSGHPVPQPFVFEDLGHPQDRSSFMGGGASGPAGSMDGMDATMKKGGTLMSKNGKGVARKQSMHQKFFGGGTADKKTDSGDYGTLPPQQRARKIAGKISDLEKEKDRATQSREGVSKMQAAYRENPKLGNPSDCDAQLAQYGHEIDALSNQIQKFKILLDDVNAQLGAGGLSATSVGGSDTPPSIRSVSSASSGVTSRVNTINDAHRTNGGVGGGRRESFSGSNGGSDTDPTINGNGHGRDELYEECSNPNPVLGEAIAQFAFDGAQDGTIRMEANEKLWLIEKDEGDGWTRVRKENNSADGFVPSSYLKVTWFGKV", "text": "FUNCTION: Plays a role in protein trafficking, actin organization and embryonic morphogenesis (PubMed:19798448). Potentially acts as cdc-42 effector (PubMed:25775511). May play a role in hypodermal P-cell nuclear positioning (PubMed:23150597). Together with toca-2, is required for protein trafficking regulating yolk protein clathrin- mediated endocytosis by oocytes during oogenesis and retrograde recycling and the sorting of recycling endosome cargo proteins such as mig-14 (PubMed:19798448, PubMed:25775511). Also, together with toca-2, controls the distribution of actin at cell junctions (PubMed:19798448, PubMed:26578656). SUBCELLULAR LOCATION: Cell junction Apical cell membrane; Peripheral membrane protein; Cytoplasmic side Basolateral cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle Cytoplasm Cytoplasm, perinuclear region Recycling endosome Note=Co-localizes with ajm-1 at cell junctions (PubMed:19798448). Co-localizes with toca-2, rme-1, cdc-42 and wve-1 on recycling endosomes (PubMed:25775511). SIMILARITY: Belongs to the FNBP1 family."}
{"protein": "MEYPWDDLTLAFSRTSMFPFFDIAHYLVSVMALKQRPGAVAAAWNNPLASWLSAMLHCFGGGILSCMLLAESPLKFLTNHTNILLASSIWYIVFFCPRDLVSQGYSYQPIQFLAAGMKEVTRTWKIVGGVSDANSYYRNAWIVMIVVGWARGAGGAVVTACEQLLKGDWKPEGDEWLKMSFPCKITLLGSIMFTFQHTRHLAISKHDLMFLYTIFLVTIKVTMMMTKDTAVTLTPFEDTLTRMLFGRRQQQQFSSSEKKTEVKPSSNGSASSASKRGAEPSGGAKRHAKKED", "text": "FUNCTION: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM38 family."}
{"protein": "MAERGELDLTGAKQNTGVWLVKVPKYLSQQWAKAPGRGEVGKLRIAKNQGRTEVSFTLNEDLANIHDIGGKPASVSAPREHPFVLQSVGGQTLTVFTESSSDKLSLEGIVVQRAECRPAANENYMRLKRLQIEESSKPVRLSQQLDKVVTTNYKPVANHQYNIEYERKKKEDGKRARADKQHVLDMLFSAFEKHQYYNLKDLVDITKQPVSYLKDILKEIGVQNVKGIHKNTWELKPEYRHYQVEEKSD", "text": "FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIF beta subunit family."}
{"protein": "MLTLLSYFGFLFAILTLTSVLFIGLNKIQLI", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetL family."}
{"protein": "MFTSQDARDSRPDRELRMMNDVLMTYPYTVIHLPAQNMLSTAKGMVNIAENYRDYPILAIFYVKYLMKKLPYGVIPVNLEWPEPYVVLNTILKRLKEHKFFANKDKEDFAERLHKLIAPDVSIPESRKDEILGQQKKERVVTKTINENFLDPVNARPRLQRFFEKLHNGTLVENLEVGLCKVEILVSSKAMLGQSFKLQIMAANVRELWVGEMVCNMITNETDYGFDEGGGDDDEGSSVEVQNSQSASPGQDQEAQRAPEAPETSSQLFDKIVSALQDDPDSAKAQLGQCRKLASYLLSHKREQEDFFMQTKDTRARLYLDLKGCLGSSWKFSIYRGVRCKQNGQLKVSLKPSNSGHLSGFWVNIKMTSQGNTLDDIRLQVRCDILGKDTNRRGGSEKDPEDQSETESSG", "text": "FUNCTION: Plasmid partition require REP1, REP2, and a cis-acting DNA sequence (known as STB). REP1 may act by intercalating in the yeast nuclear matrix and binding STB either directly or via REP2."}
{"protein": "MGSETTAAGDALDALDWNKGDGLLPVIVQDADNLRVLMLGYMNAEALAVTRARGEVTFFSRSKQRLWTKGESSGNVLRVVAIETDCDADTLLVQARPHGPTCHLGRTSCFPTAPSQFLGSLDALIAEREHERPHGSYTTKLFEQGIRRIAQKVGEEGVETALAGVVQGDAELLGESADLLYHLIVLLRARGLGLGDAVALLESRHK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family."}
{"protein": "MPGKWIFALLLLQISFCLRSAKCGKVLVWPMEFSHWMNIKTILDELVQRGHEVTVLKPSAYYVLDPKKSPDLKFETFPTSVSKDELEKYFIKLADAWTYELQRDTCLSFSPLLQNMMDEFSDYYLSVCKDAVSNKQLMAKLQESKFDVLLSDPVAACGELIAEVLHIPFLYSLRASPGHKIEKSSGRFILPPSYVPVILSGLGGQMTFIDRVKNMICMLYFDFWFHMFNAKNWDPFYTEILGRPTTLAETMGKAEMWLIRSYWDLEFPHPTLPNVDYIGGLQCKPAKPLPKDIEDFVQSSGEHGVVVFSLGSMVSSMTEEKANAIAWALAQIPQKVLWKFDGKIPATLGPNTRVYKWLPQNDLLGHPKTKAFVTHGGANGVYEAIYHGIPMIGIPMFGEQHDNIAHMVAKGAAVTLNIRTMSKSDLFNALKEVINNPFYKKNAMWLSTIHHDQPMKPLDKAIFWIEYVMRHKRAKHLRPLGHNLPWYQYHSLDVIGFLLACLAVIAALAVKCFLFIYRFFAKKQKKMKNE", "text": "FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. About 30-fold less active than Ugt2b17 toward testosterone and dihydrotestosterone. SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MKKRGAFLGLLLVSACASVFAANNETSKSVTFPKCEDLDAAGIAASVKRDYQQNRVARWADDQKIVGQADPVAWVSLQDIQGKDDKWSVPLTVRGKSADIHYQVSVDCKAGMAEYQRR", "text": "SUBCELLULAR LOCATION: Secreted Note=The outer membrane proteins OmpF, OmpC and OmpX are involved in YebF export. OmpX may help target and load YebF onto the OmpF/OmpC porins. SIMILARITY: Belongs to the YebF family."}
{"protein": "MNVTVRFLRPFARCLVPYTFHRKRSHLYSGVLQRYMSSKAPSLSCHNKDSASPPEQLELDGWKATMKSSIQEDGVSEVSDKDEDSLASTRELIEMWRLLGKEVPEHITEEDLKTLMECASKSAKKKYLRYLYGKEKAKKAKQVKKEMKAEAREEAKRARLLETTAEEQQQDFMFLRLWDRQINIALGWKGVQAMQFGQPLVFDMAYDNYMKPSELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDSAYHRELVKRYREKWDKLLLTATEKSPVDLFPKDSIIYLTADSPNVMTTFKHDKIYIIGSFVDKNTQTGTSLAKAKRLNIATECLPLDKYLQWEIGNKNLTLDQMIRILLCLKNTGNWEEALKFVPRRKHTGYLEVSEQSQELVRKLKKTKTLNSFRKGSLNVRTWKR", "text": "FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. TRM10 family."}
{"protein": "MEKFGMNFGGGPSKKDLLETIETQKKQLLQYQARLKDVVRAYKSLLKEKEALEASIKVLSVSHEADVGLAGVQLPGLTFPDSVDDRCSTHSEDSTGTATSLDTAASLTSTKGEFGVEDDRPARGPPPPKSEEASWSESGVSSSSGDGPFAGGEVDKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSHIEKNIRDQSREGANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVIMRLPTSASWWPSGKR", "text": "FUNCTION: Probably involved in maintaining Golgi structure. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein."}
{"protein": "MESTNRFMIGVFGPTGVGKTKLGVSIAKSVHGQVISVDSLQCYSPGGIVTAKPTPEEMDGIEHHMIGYLEAEEEPTNFVAEAVERLEKLCDHGAIPVVVGGSTSLTLPLLRGALNRGWRMAAITLLPHQSTYLGNIESRVDDMLEAGLLEELSGLKSLEDRNLNGKPNFHKGIWKTIGYQELYPYLEAQRSDGHCDELLKSGLASMKENTFQYGNTQLEWIRQALSPFLHAEKIANMSLTVVDKTSWTRGVEKPAIRMASDFCYASTSISFHPINEPKPRVICIFGGSSSGNDPAHMEAAKSLGRVCHENSIKLVYGGGTTGVMGAIASTLVELSGPNAVHGIIPEALLKYEAKESGRHAQDSAFARYGRRTVVKDMHTRKRLMIQEVIDGGDGSGFVGLSGGYGTLEELFEVITWHQLGIHDRGVCLLNMDGFFDGLVNWLGNVVKKGFIGLQDAAILSIASTAEGVVKCLDQKPGFSRKGELEWV", "text": "FUNCTION: Bifunctional cytokinine synthesis protein; part of the gene cluster that mediates the biosynthesis of cytokinins such as fusatin, fusatinic acids or 8-oxofusatin, known for their growth promoting and anti-senescence activities toward host plants (PubMed:28802024). FCK1 is a bifunctional enzyme that performs the first steps in the biosynthesis of Fusarium cytokinins (PubMed:28802024). It first condenses adenosine monophosphate (AMP) with dimethylallyl diphosphate (DMAPP) to yield isoprenyl adenosine monophosphate (PubMed:28802024). It then catalyzes the removal of the phosphoribose to produce isopentenylaldehyde (PubMed:28802024). The cytochrome P450 monooxygenase then converts isopentenylaldehyde to trans-zeatin (PubMed:28802024). A condensation step converts trans-zeatin to fusatin which is further modified to produce fusatinic acid (PubMed:28802024). The mechanism for oxidation of fusatin to fusatinic acid remains unknown (PubMed:28802024). 8-oxofusatin could be produced through several pathways, via direct oxygenation of fusatin, or via the 8-oxo- pentenyladenine intermediate which itself must arise from either the prenylation of 8-oxo-AMP by FCK1 and/or oxygenation of isopentenylaldehyde (PubMed:28802024). Both the FCK3 and FCK4 enzymes act downstream of the identified cytokinins to produce yet unidentified compounds (PubMed:28802024). SIMILARITY: In the N-terminal section; belongs to the IPP transferase family. SIMILARITY: In the C-terminal section; belongs to the LOG family."}
{"protein": "FLKIAEVGAGGNKLTLSMSVAVEFRDYLGDFIEHYAQLGPSQPPDLAQAQDEPRYYMDLKENQRGPGLGSTQGQTIALPAQGLIEFRLIDDYGVEEEPAELPEGTSLTVDNKRFFFDVGSNKVSEVKPTYRFGHTFCK", "text": "FUNCTION: This is a probable transcription activator that specifically binds the purine-rich single strand of the PUR element located upstream of the c-Myc gene. May play a role in the initiation of DNA replication and in recombination (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PUR DNA-binding protein family."}
{"protein": "MGETKIIYHLDGQETPYLVKLPLPAERVTLADFKGVLQRPSYKFFFKSMDDDFGVVKEEISDDNAKLPCFNGRVVSWLVSAEGSHPEPAPFCADNPSELPPSMERTGGIGDSRPPSFHPHASGGSQENLDNDTETDSLVSAQRERPRRRDGPEHAARLNGTTKGERRREPGGYDSSSTLMSSELETTSFFDSDEDDSTSRFSSSTEQSSASRLMRRHKRRRRKQKVSRIERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNEINFENMSNDDAVRVLREIVHKPGPITLTVAKCWDPSPRGCFTLPRSEPIRPIDPAAWVSHTAAMTGTFPAYGMSPSLSTITSTSSSITSSIPDTERLDDFHLSIHSDMAAIVKAMASPESGLEVRDRMWLKITIPNAFIGSDVVDWLYHNVEGFTDRREARKYASNLLKAGFIRHTVNKITFSEQCYYIFGDLCGNMANLSLHDHDGSSGASDQDTLAPLPHPGAAPWPMAFPYQYPPPPHPYNPHPGFPELGYSYGGGSASSQHSEGSRSSGSNRSGSDRRKEKDPKAGDSKSGGSGSESDHTTRSSLRGPRERAPSERSGPAASEHSHRSHHSLTSSLRSHHTHPSYGPPGVPPLYGPPMLMMTPPPAAMGPPGAPPGRDLASVPPELTASRQSFRMAMGNPSEFFVDVM", "text": "FUNCTION: Involved in the signal transduction pathway mediated by multiple Wnt genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DSH family."}
{"protein": "MSQSLRIVFAGTPDFAARHLAALLSSEHEIIAVYTQPERPAGRGKKLTASPVKTLALEHNVPVYQPENFKSDESKQQLAALNADLMVVVAYGLLLPKVVLDTPKLGCINVHGSILPRWRGAAPIQRSIWAGDSETGVTIMQMDVGLDTGDMLKIATLPIEASDTSASMYDKLAELGPQALLECLQDIAQGTAVAVKQDDGLANYAHKLSKEEARINWSDAATHIERCIRAFNPWPMSHFEVAENSIKVWQARVETRAVTQTPGTIIQADKSGIYVATGQDVLVLESLQIPGKKALPVQDILNARADWFSVGSQLS", "text": "FUNCTION: Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. SIMILARITY: Belongs to the Fmt family. SIMILARITY: Belongs to the Fmt family."}
{"protein": "MSVKQKSALQDLVDFAKWHVWTRVRPSSRARLAYELFADDHEATTEGAYINLGYWKPGCAGLEEANQELANQLAEAAGISEGDEVLDVGFGLGAQDFFWLETRKPARIVGVDLTPSHVRIASERAERENVQDRLQFKEGSATDLPFGAETFDRVTSLESALHYEPRTDFFKGAFEVLKPGGVLAIGDIIPLDLREPGSDGPPKLAPQRSGSLSGGIPVENWVPRETYAKQLREAGFVDVEVKSVRDNVMEPWLDYWLRKLQDESFKKSVSRLFYSQVKRSLTSDSGMKGELPALDFVIASARKPGA", "text": "FUNCTION: S-adenosyl-L-methionine-dependent O-methyltransferase that catalyzes the last step in the erythromycin biosynthesis pathway. Methylates the position 3 of the mycarosyl moiety of erythromycin C, forming the most active form of the antibiotic, erythromycin A. Can also methylate the precursor erythromycin D, forming erythromycin B. SIMILARITY: Belongs to the methyltransferase superfamily."}
{"protein": "MGINLSNGDWNRYKKEGFLITKFGDLIDYIMNWARSGSLWPMTFGLACCAVEMMHTASSRYDLDRYGIIFRASPRQADVMIVAGTLTNKMAAALRKVYDQMADPKYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALLYGMLCLQNKIKRTKNI", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MASGRRAPRTGLLELRAGAGSGAGGERWQRVLLSLAEDVLTVSPADGDPGPEPGAPREQEPAQLNGAAEPGAGPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQVLKKTGKEVVLEVKYMKDVSPYFKNSTGGTSVGWDSPPASPLQRQPSSPGPTPRNFSEAKHMSLKMAYVSKRCTPNDPEPRYLEICSADGQDTLFLRAKDEASARSWATAIQAQVNTLTPRVKDELQALLAATSTAGSQDIKQIGWLTEQLPSGGTAPTLALLTEKELLLYLSLPETREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCHRAAEGVQEVSTACTWNGRPCSLSVHIDKGFTLWAAEPGAARAVLLRQPFEKLQMSSDDGASLLFLDFGGAEGEIQLDLHSCPKTIVFIIHSFLSAKVTRLGLLA", "text": "FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate (By similarity). SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side Cell junction Cytoplasm, cytoskeleton Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. SIMILARITY: Belongs to the syntrophin family."}
{"protein": "MLKRRLEFFFLYMMLIGAYVIWFFPVSRLEFYGGLLCYISIILFSIYSLILENRTSQHTLLWIHILVFFPIVGYVFYLFSGQLYVKGKLFKTKRMYNREKLRKLFDKEETPEVTGLKDNQERFFTYSIRAAHMNINTKSNIKVLKNGEETFPDIFKAMRKAESYIHIEYYMFKSDMLGRGMMDIMMEKARQGVEVRFLYDAAGSMKLARRDIMRMKQAGVDIVPFSPLKYGFFNQKLNFRNHRKIVIIDGKTGFVGGLNVGKEYISRDPYIGFWRDTHLRLEGEIVQTLHAIFMLDWEYVSNEVLIDQEEYNTPVPVEGGGIYQIVATGPDMKESMSDLYYEMISSAQKSIWIATPYFVPNESIRTALKAAATKGVEVRVMVPEKNDSFLTQYASRSYFPELLLEGIEVYSYQKGFMHQKVMIIDGDLASVGTANMDMRSFQLNFEVNVFFTDAEAIRTLEAHFEEDMQESEKLSPVGFYKRGVADRTKESFARLFSGVL", "text": "FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol (By similarity). May have a role in the heat shock response since the level of the transcript of ywiE increases after a heat shock. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase subfamily."}
{"protein": "MSRSESRKNRGGREEILEQWVAGRKKLEELERDLRKTKKKLKKIEDENPWLGNIKGILGKKDKDGEGAPPAKRARTDQMEVDSGPRKRPLRGGFTDKERQDHRRRKALENKKKQLSAGGKNLSKEEEEELRRLTEEDERRERRVAGPPVGGVIPLEGGSRGAPGGGFVPSLQGVPESPFSRTGEGLDIRGNRGFP", "text": "FUNCTION: Promotes both transcription and replication of genomic RNA. Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. May interact with host RNA polymerase II thereby changing its template requirement from DNA to RNA. RNA pol II complex would then acts as an RNA-directed RNA polymerase, and transcribe and replicate HDV genome (By similarity). SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the hepatitis delta antigen family."}
{"protein": "MLSQSLLSGMRVLRTEARRNFGIVAPALNKASDPIQQLFLDKVREYKQKSAGGKLVDSNPDIERELKTELDRVAKQFGSDGKTDMLKFPEFQFPDVKVDPITQAPQ", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family."}
{"protein": "MNLISRTLTRAVSSSLYHSKAAKLPTQKWIISQQIRVFSATVISGGGKKPLAKVSVKPPLNVATEKESTPPKKIEYKPEISNWINLIGFVEQPVQFGPCSDGKFWAGTVISQRSGSKSSNFWIPIIFEGDLAKIAVQHVKKEDRIHVSGKLFIDSPPPNVTYSQSNVQVMVQNLNFVQAATSTTKTISPPEKEVTSIKKKPARSKKVKVIDEETSNSWKHLIENPKEWLDHRGNKANGLVKPGHPDFKMKVGGLSLWLSTAPDWALLKLEELKFDVLVPKGNIKLNQLKGEESWKDLVQNPDKWLDNRSDKTNVKYPDFKHKETGEALWMTNSPIWVLSKLPPLKKNQERPFMSNKVSQLELDVEVPKGNLKQLKREEIWKNLVENPSKWWDNRLDKRNPKGPDFKHKETGEALWIGDSPTWALSKLPPLKKNQERPVMA", "text": "FUNCTION: Binds single-stranded DNA. SUBCELLULAR LOCATION: Mitochondrion Plastid, chloroplast."}
{"protein": "MSRRNKRSRRRRKKPLNTIQPGPSKPSAQDEPIKSVSHHSSKIGTNPMLAFILGGNEDLSDDSDWDEDFSLENTLMPLNEVSLKGKHDSKHFNKGFDNNTALHEVNTKWEAFYSSVKIRQRDVKVYFATDDILIKVREADDIDRKGPWEQAAVDRLRFQRRIADTEKILSAVLLRKKLNPMEHE", "text": "FUNCTION: Interacts with the host phosphatase PP1 catalytic subunit (PPP1CB) and recruits it to dephosphorylate EIF2S1/eIF2alpha and therefore restores the host translation that has been shut-down by the host. Also inhibits the EIF2S1/eIF2alpha-ATF4-DDIT3/CHOP pathway. SIMILARITY: Belongs to the asfivirus DP71L family."}
{"protein": "MASFKGFSVNTVPVSKAKRDISSLAATPGIRSQPFTPSVDMSQSREFLTKAIEQGSMSIPYQHVNVPKVDRKVVSLVVRPFSSGAFSISGVISPAHAYLLDCLPQLEQAMAFVASPESFQASDVAKRFAIKPGMSLQDAITAFINFVSAMLKMTVTRQNFDVIVAEIERLASTSVSVRTEEAKVADEELMLFGLDHRGPQQLDISNAKGIMKAADIQATHDVHLAPGVGNIDPEIYNEGRFMFMQHKPLAADQSYFTLETADYFKIYPTYDEHDSRMADQKQSGLILCTKDEVLAEQTIFKLDAPDDKTVHLLDRDDDHVVARFTKVFIEDVAPGHHAAQRSGQRSVLDDLYANTQVVSITSAALKWVVKHGVSDGIVNRKNVKVCVGFDPLYTLSTHNGVSLCALLMDEKLSVLNSACRMTLRSLMKTGRDADAHRAFQRVLSQGYASLMCYYHPSRKLAYGEVLFLERSSDMVDGIKLQLDASRQCHECPVLQQKVVELEKQIIMQKSIQSDPTPMALQPLLSQLRELSSEVTRLQMELSRTQSLNAQLEADAKSAQACSLDMYLRHHTCINGHTKEDELLDAVRVAPDVRKEIMEKRGEVRRGWCERISKEAAAKCQTVIDDLTQMNGKQAREITELRESAENYEKQIAELVGTITQNQMTYQQELQALVAKNVELDTMNQRQAKSLRITPSLLSATPIDSVDGAADLIDFSVPTDEL", "text": "FUNCTION: Non-structural protein with ssRNA-binding activity. Is probably involved in the formation of viral inclusions, where the assembly of cores and the replication of viral RNA are thought to occur. Together with mu-2, recruits the other core proteins to these inclusions. SIMILARITY: Belongs to the orthoreovirus mu-NS protein family."}
{"protein": "MIIEKKIKNYTVFVKKDGEKYIEIFKDFLSYNHQVIKVFRNIEDTKVVLINTDYGKYILKVFSPKVKNTERFFKSLVKGDYYEKLFHQTDRVRREGFAALNDFYLLAEIKTLRYVKTYVMIIEYIEGIELVDMPEISDEVRGKIKQSIYSLHQHGMVSGDPHKGNFILQGNEIRIIDLSGKRPSRQRKAKDRIDLERHYGIKNNVRDIGFYLLIYKKKLRNFLRRIKGKEKR", "text": "FUNCTION: Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. SIMILARITY: Belongs to the protein kinase superfamily. RfaY/WaaY family."}
{"protein": "MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKTYTTPKKIKHKHKKVELAVLKYYKVEDDGSVKRLRRECPNCGASTFMANHKDRLYCGRCHLTLKLEA", "text": "FUNCTION: [Small ribosomal subunit protein eS31B]: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored- polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm Nucleus. SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31B]: Cytoplasm Nucleus, nucleolus. SIMILARITY: In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family. SIMILARITY: In the N-terminal section; belongs to the ubiquitin family."}
{"protein": "MPTISTAECFTHGKVANELHAFARGYPHEYLFSIDRKKVDISVVAGMFIPTLTGVRTLLHFEPLEPRLVIDTVKVYEQDQDCIMACRMAEAVMRVTGADIGIGTTAGIGKGAVAIASQDKIYSKVTRIDADFRTSDAKKLMQREKSGVFTALRLFEEFLLEGEFPDSYNKYI", "text": "SIMILARITY: Belongs to the UPF0254 family."}
{"protein": "MSLISAVEDRDIHNIGKTSGGGSRTSSITSSKKSLKHGSKSLRKPKVYQTTGEPLSREALYKAKLKYGVYQSPAQSYSIGVSDAHAASDKAANLAHDNQTTVEAYKRMFIDPNATKAASKMGPKVVRNNSITSATSKTSKESQTKRKSKESPGAAASKAYSMTMETTSLSSQTNSRSYSITSASSVLSGASGSFNSTVNPKPKTLNLEKVLVGAEKKAESRIKERWEPEKTNFQYGVKTDEHGNLNQFSFSNEMMNNIMAKVDAPKAQDLQKVKKVSAEKEAKSMKFALGAANAVKDMHPGEDIDKSIALKAQKRETYLSQLTSQQVLTLARANVDRQLDIIEKSDMHRKLFTNMEYNKAAVAVAQSNHQKKTEFHNKINMGGGLFLSPEDITKIASGLISPVLGEVSERAEAQRAMDEEIAERTEAYNKSSNEWETMERSIISNDAKVLTTTANRHQTEKKTSQEKIKASFDALVARMDTKVAERETLLEDTKSKEIEFKKQMQQELKDEKARLDQDLEEWGKKCEQDITEARKEQEELLKPYHDDLANAEAEHKTLVEERDEINAEISRLQDAIVDHKRKISGYGNDLDAQKNRNIREDDKLLELGQTKESLESHLNDDVIILANKAKEQAELSTKEARLKQLEVDSLINERKSELNATEIELKKEKLNLLEAMKDVASARGDDKIDEEKVKKLIGMTSEEYLTQNKSVEKNVEDLPTQLEKIEEGDELKKEEIVGAETKNSGGDGVPVSTAAKEATETSSAVQTKEPEEKISIGNKSSGKEDANDCKSAEHSKEISVSQKAGNNKSLGVSPDSLEHTFSGFSQGSSIEDDQDAISNQEKK", "text": "FUNCTION: Required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis. SUBCELLULAR LOCATION: Cytoplasmic granule. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes at the eisosomes. SIMILARITY: Belongs to the EIS1 family."}
{"protein": "MKRPGGAGGGGGSPSLVTMANSSDDGYGGVGMEAEGDVEEEMMACGGGGEKKRRLSVEQVRALERSFEVENKLEPERKARLARDLGLQPRQVAVWFQNRRARWKTKQLERDYAALRHSYDSLRLDHDALRRDKDALLAEIKELKAKLGDEEAAASFTSVKEEPAASDGPPAAGFGSSDSDSSAVLNDVDAAGAAPAATDALAPEACTFLGAPPAAGAGAGAAAAASHEEVFFHGNFLKVEEDETGFLDDDEPCGGFFADDQPPPLSSWWAEPTEHWN", "text": "FUNCTION: Probable transcription activator that binds to the DNA sequence 5'-CAAT[AT]ATTG-3'. May be involved in the regulation of gibberellin signaling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class I subfamily."}
{"protein": "MSNVPPPSGLSYQVKKKLEGKRDKDQENEALEWIEALTGLKLDRSKLYEDILKDGTVLCKLMNSIKPGCIKKINENATMPFKIMENISAFLEAMKGYGVPVADLFQTVDLFEKKDIAQVTRTLFALGRTCQTHPEYSGPVLGPKLATENKREFTEQQLREGQNVVSLQYGSNKGASQAGINMGKQRMIMD", "text": "SIMILARITY: Belongs to the calponin family."}
{"protein": "MGHKKNGHRRQIKERENQNKFERSTYTNNAKNNHTQTKDKKLRAGLKKIDEQYKKAVSSAAATDYLLPESNGYLEPENELEKTFKVQQSEIKSSVDVSTANKALDLSLKEFGPYHIKYAKNGTHLLITGRKGHVASMDWRKGQLRAELFLNETCHSATYLQNEQYFAVAQKKYTFIYDHEGTELHRLKQHIEARHLDFLPYHYLLVTAGETGWLKYHDVSTGQLVSELRTKAGPTMAMAQNPWNAVMHLGHSNGTVSLWSPSMPEPLVKLLSARGPVNSIAIDRSGYYMATTGADRSMKIWDIRNFKQLHSVESLPTPGTNVSISDTGLLALSRGPHVTLWKDALKLSGDSKPCFGSMGGNPHRNTPYMSHLFAGNKVENLGFVPFEDLLGVGHQTGITNLIVPGAGEANYDALELNPFETKKQRQEQEVRTLLNKLPADTITLDPNSIGSVDKRSSTIRLNAKDLAQTTMDANNKAKTNSDIPDVKPDVKGKNSGLRSFLRKKTQNVIDERKLRVQKQLDKEKNIRKRNHQIKQGLISEDHKDVIEEALSRFG", "text": "FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. SUBCELLULAR LOCATION: Nucleus, nucleolus."}
{"protein": "MQYVREMSSDLATFASGLLALFERSAGVPLRELALVGLTAAIITYFATGLVGVLANRLEAVAYPRERDVHVTPTPRMGGLAMYLGVLAAVFLASQLPALTRGFVYSSGMPAVLVAGAVITGIGLIDDRWGLDALTKFAGQITAASVLVTMGVAWSVLYIPLGGVGTIVLDQTSSILLTLALTVSIVNAINFVDGLDGLAAGLGLITAMAICIFSVGLLRDHDGDVLFYPPAVISVVLAGSCLGFLPHNFHRAKIFMGDSGSMLVGLMLAAASTTAAGPISQNAYGTRDVFALLSPFLLVVAVMFVPMLDLLLAIVRRIRAGRSAFSPDKMHLHHRLLQIGHSHRRVVLLIYLWVGIVAFGAASTIFFNPRNTGAVMLGAIVITGMATVIPLLRRRDNY", "text": "FUNCTION: Involved in the biosynthesis of the disaccharide D-N- acetylglucosamine-L-rhamnose which plays an important role in the mycobacterial cell wall as a linker connecting arabinogalactan and peptidoglycan via a phosphodiester linkage. Catalyzes the transfer of the N-acetylglucosamine-1-phosphate (GlcNAc-1P) moiety from UDP-GlcNAc onto the carrier lipid decaprenyl phosphate (C50-P), yielding GlcNAc- pyrophosphoryl-decaprenyl (GlcNAc-PP-C50) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA subfamily."}
{"protein": "MELAMDFALRLRDAANHHLSRYEPLVLLAAPLLALLAARTLHAAAAAVADRGLRTVLLALAMTAIKLLPGVSAYINAEKRKVVDQLQSGGTSTKSTLRTELPTVGLSNQVINDLETLKARDVNWQGKCSGTVYIAGSESEGHFALINKAYSMFSHTNPLHQDVFKSVAQLEAEVVAMTAALLGIKEKSSGGQICGNMTSGGTESILLAVKTSRDYMRTKKGITKPEMIIAESAHSAYDKAAQYFNIKVRRVPVNKEFLADVKGFKRCINGNTIMMVGSAPGFPHGLIDPIEELGELASRYDICLHVDLCLGGFVLPFARKLGYPIPPFDFCVKGVTSISTDVHKYGLAPKGTSIVLYKNHEIRKHQFVAVTEWTGGLYVSPTIAGSRPGGLIAGAWAAMTSLGLNGYMENTGHIMEVSKKIQRGIEDIPGLFVIGKPDMTVVAFGSDSVDIFEVNDIMSSKGWHLNALQRPNSLHICVTLQHTVIYEEFLKDLKDSVDTVKANPGPISGGRAPIYGAAGKMPDRGMVRELLVEFMDASC", "text": "FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine- 1-phosphate lyase subfamily."}
{"protein": "MKEVIDTNTTGTNFKFENRNYKLQNQSFSFVRYKNFNLDKLLIPKTNANLNSTRNGVLTQAPTLDFVLNPVFVNAITNVYNLSEQVKDLEQRLESKSNESEKAGINSVLTQIKNKQVDYLKVKEYISSLDKDTNKVSTPINSTGWVKWYQEANKELGLNLNQEPKDWDQFLKLVASYFSMAIYANVTLGQKVTKEVKVWDGQNFQFLAIENNEDQAQCFSKRKQSWNYC", "text": "SIMILARITY: To M.pneumoniae MPN_376 central region."}
{"protein": "MINEDPSSLTDMDNNIDSWKNNSENSSYSHADSLADVSNIDNLLSDKIFSIRDSNSNIYDIYYAYDTNDTNITKYKWTNNINRCIESYLRSQICEDIDFNSDICDKVQRTIIILIRSTNDTNDISDTNDISDTNDTNDTNAIYDPFDISDTNDTNEIYDPFFILDINDTNDTNDIYGIYDPDDIYETNIKDICERYSEIYPRNREKSTFVPIDYSDPNCMEKLARLWVQCETCYGLNFKQFFRPKMNICEHCGEHLKMSSSDRIDLLIDRDTWNPMDEDMVSVDPIKFDSIKELGSEEESSKDRLDEDMLSPDPIELDSEEESSKDRVDSEEEKDQSYIDRLDSYQEKTGLPETVQTGTDQREEIHPLFEDIMNQLDLYLQTAKNRVDSEEEKDQSYIDRLDSYQEKTGLPEAVQTGTGQLNGIPLALAVMDSEFIAGSMGCVVGEKITRLIEYATNLLLPLIIVCASGGARMQEGSLSLMQMAKISSALYNYQINQKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNATIAFAGKRVIEQLLNKEVPEGSQSADLLFDRGLLDAVVPRHLLKEFLTELFQFHGFVPLT", "text": "FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the AccD/PCCB family."}
{"protein": "MSHASRRRWRRATTSAATAALLCGALLTFPSAPAAAQVRLGSGSYTTVLPPGASGPSDHTGAPVAPKVTADFTQPVVTNDWWSSLIFQRYPGNPYGENLYAHPLSFKAQAHGLEVGYPDTPELVADGLKYQYTHSPDFVLGIHGLNAPAAKVAGYSDWTVTADLSDGTRQLRTTIGQGLPFVYADVSGGPIRVEFTAPPTVWRRSGNAVGVTVNGHHYALFAPSGTTWSESDTVFTADVGGSGYASVALLPSPDDFDRYAPYAYSFVTSTTLTYDYDPASATLTSTYRVTTEAREGTAQGTLLALYPHQWKETTTALTDLSYASPRGPMRVVEGDRFTTELTTHGILPSLPTVDSADHQRLRALIDAELHASDPWKGASDTYWTGKALGRLAQLVPIADSIGYTAGRDALLDLLKNKMEDWLTADGPGDNAQFYYDDQWDTLIGFPASFGSNTELNDHDFHYGYFITAAATIARYDRSWISEERWGPMVTTVLRDANNPDRDDERFPWLRSFSPYAGHGWASGHAGFASGNNQESSSEAMHFAASAALLGSLIGDEELRDLGVYLHTTQASAMRRYWQNADGDAFPAGYSHDVVGMVWSDGGDHRIWWDGTPEELYGINYLPITAGSLYLGHDPEHAAAMHQSLVTRLGRQPQVWRDIHWAHQALSDPDAALAAFEAQWQSYEPESGSSKAHTYQWLSTLAEFGTVDTSVTADTPHYAVFRDGDRRTYVAFNPTGQPLTVTFSDGTTLTVPPGQLATG", "text": "FUNCTION: Cleaves internal linkages in 1,3-beta-glucan (PubMed:17115704, PubMed:19435780). May contribute to biomass degradation by hydrolyzing the 1,3-beta-linked plant polymer callose that is present in decomposing plant tissue (PubMed:17115704). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 81 family."}
{"protein": "MDRSRTSSQGRDVLPPRGDEGRISPSLDKEKSPGPEDQPDAPPDGGLTAWLVVVGAWCTSFCSFGWVNSVGIFQNYYESHLLKHLSSSTISWIPSLQIFFMFAMGPIVGKLYDTFGARYLIIGGTFFHVFGLMMASISTQYYQLLLSQGICSAIGAAAIFQPALSAVSAWFNRKRGIAFATLSTGSSVGGVIFPIMVDRLIAKVGFGWSMRISAFMILFLLGIAIVTVKARRPPPQGPKPSGVQLLQPFKEPVFIVTLLGYMLLTYGVFIPINYVIVQAVASGMNADLASYLVPMLNGASLFGRLGAGFMSDRYGRYNIFIVMCIVAGVLVLALWIPATSNAPIIVFATLFGFASGAYVSLSPALIAQISPLKEVGYRTGLLFLFASVGGLTTSPIAGAILQNAGGDYTHMKIFSGVMLLGGTAFIITARIVGTGLKLVVKY", "text": "FUNCTION: MFS transporter; part of the gene cluster that mediates the biosynthesis of aspergillic acid (PubMed:29674152). Probably involved in aspergillic acid metabolism and transport (PubMed:29674152). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family."}
{"protein": "MNNLIKYSTFLISDLFDVVIGKTIDGNKAQRNENGTPYITRKATRNGFEFMIDGEKEKLYSGKLPVITIGNETSKPFVQEFHFFTGTKVNICIPKLDLNRNHLLYITTMIENATKMFSYSYTINSTRLKSLKILLPIKGEEPDWDYMNTYISKILSNMEKNFDVQQNDGVSDLRSLKDLSWSQFKMDEIFSINSGVRLTKADMKPGNIPFIGATDSNNGITEFTSSTNASFDGNVLGVNYNGSVVENFYHPYKAVFSDDVKRLKLKNYPNNKHVLLFMKVVILQQKVKYAYGYKFNATRMKEQIILLPTKADGTPDYEFMEQYMMRMENKVVGRTTEKEAD", "text": "FUNCTION: The specificity subunit (PubMed:12654995). A B, G, H and S subtype restriction enzyme that recognizes the double-stranded sequence 5'-CGAN(6)TGC-3' and cleaves bilaterally and symmetrically 10 base pairs upstream and 12 base pairs downstream of the sequence to release a 34-base pair fragment. Methylation of the recognition sequence occurs on the adenine in either one or both strands; seems to methylate restricted DNA (PubMed:8451198, PubMed:8276869, PubMed:12654995). This subunit degrades DNA in a non-specific manner (PubMed:8276869). SIMILARITY: Belongs to the type-I restriction system S methylase family."}
{"protein": "MTKANHHIFADGELSRKEGTLRIDTLEGETKYLPVESIDALYLHGQISFNTRALGLLNKHGVPVHIFGWKDYYRGSYLPKRSQLSGNTVVEQVRAYDNTERRLRIGHRIIEASIHNMRANLQYYSGRRGDFDSVVETLRELKTAVSDTQRIDELRAVEGDARKRYYDCFDSILEAPFRLAKREYNPPSNETNALISFLNGMVYTSCVSAIRKTALDPTVGFVHEPGERRFTLSLDIADIFKPILADRLVFRLVNRKQITTDDFETELAGCLLTEQGRLTVLEEFERSLDQTVQHPRLKRKVSFKTLIQTDVYSLKKHLLTGEPYHATEKWW", "text": "FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family."}
{"protein": "MTLLLELAHGLPWLYFSLVFLFSLMIGSFLNVVIHRLPIMLEREWQAEYRSYFSSDTPQPEDDERYNLMVPRSCCPRCNHPITALENIPLLSWLWLKGRCRGCQAAISARYPLVELLTALLSVVVAMTLTPGWGTLAALLLTWVLVALTFIDLDKMLLPDQLTLPLLWGGLLFNLLGGYVPLGDAVIGAMAGYLVLWSLYWAFKLLTGKEGMGYGDFKLLAALGAWLGWQALPIVLLLSSLVGAIFGIGLILLRNHHQSKPIPFGPYLAIAGWIALLWGDSITRWYLSTIL", "text": "FUNCTION: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha- amino group of the newly exposed N-terminal phenylalanine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A24 family."}
{"protein": "MFTMKKSMLLLFFLGTISLSLCEQERNADEEERRDEEVAKMEEIKRGLLSGILGAGKNIVCGLSGLC", "text": "FUNCTION: Antimicrobial peptide active at least against the Gram- positive bacterium S.aureus but with otherwise unclear activity spectrum (PubMed:16487561, PubMed:16621155). Lacks hemolytic activity against rabbit or human erythrocytes (PubMed:16487561, PubMed:16621155). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MANEEDDPVVQEIDVYLAKSLAEKLYLFQYPVRPASMTYDDIPHLSAKIKPKQQKVELEMAIDTLNPNYCRSKGEQIALNVDGACADETSTYSSKLMDKQTFCSSQTTSNTSRYAAALYRQGELHLTPLHGILQLRPSFSYLDKADAKHREREAANEAGDSSQDEAEDDVKQITVRFSRPESEQARQRRVQSYEFLQKKHAEEPWVHLHYYGLRDSRSEHERQYLLCPGSSGVENTELVKSPSEYLMMLMPPSQEEEKDKPVAPSNVLSMAQLRTLPLADQIKILMKNVKVMPFANLMSLLGPSIDSVAVLRGIQKVAMLVQGNWVVKSDILYPKDSSSPHSGVPAEVLCRGRDFVMWKFTQSRWVVRKEVATVTKLCAEDVKDFLEHMAVVRINKGWEFILPYDGEFIKKHPDVVQRQHMLWTGIQAKLEKVYNLVKETMPKKPDAQSGPAGLVCGDQRIQVAKTKAQQNHALLERELQRRKEQLRVPAVPPGVRIKEEPVSEEGEEDEEQEAEEEPMDTSPSGLHSKLANGLPLGRAAGTDSFNGHPPQGCASTPVARELKAFVEATFQRQFVLTLSELKRLFNLHLASLPPGHTLFSGISDRMLQDTVLAAGCKQILVPFPPQTAASPDEQKVFALWESGDMSDQHRQVLLEIFSKNYRVRRNMIQSRLTQECGEDLSKQEVDKVLKDCCVSYGGMWYLKGTVQS", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for efficient transcription from both the type 2 VAI and type 3 U6 RNA polymerase III promoters. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNAIANLAATLRADLGECLADLAVDALIDEAELSPKPALVDRRGNGAHADLHLGLMQASALSLWPCFKEMADAAQRHGRIDARLRGVLGQLGRDGEAAMLRTTEGVNTHRGAIWALGLLVAAAALEPRRTQAGEVAARAGRIALLDDPAAAIGDSHGERVRRRYGVGGAREEARLGFPRAVRHGLPQLWRSREGGAGEQNARLDALLAIMSVLDDTCVLHRAGRVGLAAMQDGARAVLAAGGSASLAGRRRLCELDRRLLALNASPGGAADLLAACLFLDRLPAVSGGWAGSL", "text": "FUNCTION: Involved in the formation of 2-(5''-phosphoribosyl)-3'- dephosphocoenzyme-A, the prosthetic group of the acyl-carrier protein of the malonate decarboxylase. SIMILARITY: Belongs to the CitG/MdcB family."}
{"protein": "MGTSARRALWLLLALCWALRESGATATGRKTKCEASQFQCTNGRCITQLWKCDGDEDCVDGSDEKNCVKKTCAESDFVCNNGQCIPNRWQCDGDPDCEDGSDESPEQCHMRTCRINEISCGARSTQCIPVSWRCDGESDCDSGEDEENCGNVTCSSDEFTCSSGRCISRNFVCNGQDDCSDGSDELDCAPPTCGAHEFQCSTSSCIPISWVCDDDADCSDQSDESLEQCGRQPVIHTKCPASEIQCGSGECIHKKWRCDGDPDCKDGSDEVNCPSRTCRPDQFECEDGSCIHGSRQCNGIRDCVDGSDEVNCKNVNQCLGPGKFKCRSGECIDISKVCNQEQDCRDWSDEPLKECHVNECLVNNGGCSHICKDSVIGYECDCAAGFELIDRKTCGDIDECQNPGICSQICINLKGGYKCECSRGYQMDLATGVCKAVGKEPSLIFTNRRDIRKIGLERKEYIQLVEQLRNTVALDADIAAQKLFWADVSQKAIFSASIDDKVGRHVKMIDNVYNPAAIAVDWVYKTIYWTDAASRTISVATLDGAKRKFLFNSDLREPASIAVDPLSGFVYWSDWGEPAKIEKAGMNGFDRRPLVTVDIQWPNGITLDLIKSRLYWLDSKLHMLSSVDLNGQDRRIVLKSLEFLAHPLALTIFEDRVYWIDGENEAVYGANKFTGSELATLVNNLNDAQDIIVYHELVQPSGKNWCEEDMENGGCEYLCLPAPQINEHSPKYTCSCPNGYHLEENGRECQSTATTVTYSETKDTNTTEISPTSGLVPGEINVTTAVSEVSVPPKGTSAAWAILPLLLLAMAAVGGYLMWRNWQHKNMKSMNFDNPVYLKTTEEDLSIDIGRHSASVGHTYPAISVVSTDDDLA", "text": "FUNCTION: Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism. Binds also to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE- containing ligands as well as clusterin/CLU. In the off-state of the pathway, forms homooligomers or heterooligomers with LRP8. Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 (By similarity). This interaction results in phosphorylation of DAB1 leading to the ultimate cell responses required for the correct positioning of newly generated neurons. Later, mediates a stop signal for migrating neurons, preventing them from entering the marginal zone (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit; Single-pass type I membrane protein."}
{"protein": "MNFKIPQFPDFEISITAFENVTNSESIRSKVATLPYAFLDARMIYSQEQLYAALYRVLVEQNYNKLRTKTIHSEIMLCLSPTSNIGDAFKKFGIKEDSSTVICLHIKDRSDEPELPSLSSIVEGQEISLSKEFINQHRDIGMVGHVYKINGEMIENSTEDQVSSMIVNMIQLRGL", "text": "FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CGI121 acts as an allosteric effector that regulates the t(6)A activity of the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. CGI121 is not required for tRNA modification (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the CGI121/TPRKB family."}
{"protein": "MLGPAVLGLSLWALLHPGTGAPLCLSQQLRMKGDYVLGGLFPLGEAEEAGLRSRTRPSSPVCTRFSSNGLLWALAMKMAVEEINNKSDLLPGLRLGYDLFDTCSEPVVAMKPSLVFLAKAGSRDIAAYCNYTQYQPRVLAVIGPHSSELAMVTGKFFSFFLMPQVSYGASMELLSARETFPSFFRTVPSDRVQLTAAAELLQEFGWNWVAALGSDDEYGRQGLSIFSALAAARGICIAHEGLVPLPRADDSRLGKVQDVLHQVNQSSVQVVLLFASVHAAHALFNYSISSRLSPKVWVASEAWLTSDLVMGLPGMAQMGTVLGFLQRGAQLHEFPQYVKTHLALAADPAFCSALGEREQGLEEDVVGQRCPQCDCITLQNVSAGLNHHQTFSVYAAVYSVAQALHNTLQCNASGCPAQDPVKPWQLLENMYNLTFHAGGLMLRFDSSGNVDMEYDLKLWVWQGSVPRLHDVGRFNGSLRTERLKIRWHTSDNQKPVSRCSRQCQEGQVRRVKGFHSCCYDCVDCEAGSYRQNPDDIACTFCGQDEWSPERSTRCFRRRSRFLAWGEPAVLLLLLLLSLALGLVLAALGLFIHHRDSPLVQASGGPLACFGLVCLGLVCLSVLLFPGQPSPARCLAQQPLSHLPLTGCLSTLFLQAAEIFVESELPLSWADRLSGCLRGPWAWLVVLLAMLVEVALCTWYLVAFPPEVVTDWHMLPTEALVHCRTRSWVSFGLAHATNATLAFLCFLGTFLVRSQPGRYNRARGLTFAMLAYFITWVSFVPLLANVQVVLRPAVQMGALLLCVLGILAAFHLPRCYLLMWQPGLNTPEFFLGGGPGDAQGRNDGDTGNQGKHE", "text": "FUNCTION: Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose (By similarity). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family. TAS1R subfamily."}
{"protein": "MKVLALSALLSLASAASISRRSDFCGQWDTATAGDFILYNDLWGEDNASSGSQCTGVDSASGNEIAWHTSWSWEGGSSDVKSYANAALQFTGTQLSSISSIPSTWKWTYSGSDIVADVAYDMFLGSTADASSDEYEIMVWLAALGGAGPISSTGSTIATPTINGVTWDLYTGPNGDTTVYSFVAQSTTEDFSGDLNDFFTYLVDNEGVSDSLYLTTLEAGTEPFTGSDAELKVSEYSVSIE", "text": "FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family."}
{"protein": "MAEKNRLVTVAALQFACTDDVSTNVATAERLVRAAHQKGANIILIQELFEGYYFCQAQKEEFFHRAKPYLGHPTIVRMQNLAKELGVVIPVSFFEEANNAHYNSVAIIDADGTDLGLYRKSHIPDGPGYQEKFYFNPGDTGFKVFQTKYAKIGVAICWDQWFPEAARAMALQGAEVLFYPTAIGSEPQDDGLDSRDHWRRVMQGHAGANVVPLVASNRIGKEIIETEHGNSEITFYGYSFIAGPTGELVAAAGDKEEAVLVAQFDLDKIKSKRHGWGVYRDRRPDLYKVLLTLDGSNPVK", "text": "FUNCTION: Involved in polyamine biosynthesis. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily."}
{"protein": "MTTLATLIFLVTLLFVLWQPKGLDIGITALTGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGNGLKMFVYIILLGAIVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFHIGFIRYFSRMIIPNLFSLLASIIVLWLYFRKAIPKTFDDNNIKHPKDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLMLARKSNALNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFITLIGLYLTLIIF", "text": "FUNCTION: Involved in arsenical resistance. Thought to form the channel of an arsenite pump. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ArsB family."}
{"protein": "MMKVLVVAALLVTLISYSSSEGIDDLEADELLSLMANEQTRAKACTPRYYDCSHDRHSCCRSSMFKDVCTCFYPEGGDNKEVCTCQQPKHLKYMEKATDKIKNLFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 02 (D7) subfamily."}
{"protein": "MPVQHRTIVVGNTSTLKSPVGIVRILEVIFACVTFSLVVHTGRWGGRIGDLCMFCWCFCFAVTLVILIVEFAGVQNRMPVSWKNFPITFAMYGVLMCLSATVIYPLQYLEDKAYNSEARNYQIVAIVFSCLTTLAYIIEVSLTRAKPGEVTGYMATTPGLLKVLETFIACIIFVFISDPAQYERHDAMKWCLAVYCICFILSIVVIILCVGECTGWLPCAFNKFLSGYALLAVLMYASAMIVWPIFAFDRKHGGTPSRPSYCRSGQGNLYRVCDWDKLVAVAVLTAVNLIAYIMDLVHSARLIFITV", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MAL family."}
{"protein": "MGNVQTSTNVYNIDGNGNTFAPSSQMASTASPAIDLKPGVLNPTGKLWQTMGTGAPSADSLVLVVDNKGEYTYLSENMRETLNKAVTDVNMWQPLFQATKSGCGPVVLANFTTISTGYVGATADDAFSNGLVSNGPFLATMHIMELQKTIAARMRDVAIWQKHLDTAMTLMTPDVSAGDVTCKWRSLLEFAQDILPLDNLCRSYPNEFYTVAAQRYPAIRPGQPDTQVALPQPHPLGEVAGSFNAPTSEVGSLVGAGAALSDAISTLASKDLDLVEADTPLPVSVFTPSLAPRTYRPAFIDPQDAAWIAQWNGDANIRIITTYQSTDYTVQLGPGPTRVIDMNAMIDAKLTLDVSGTILPFQENNDLSSAIPAFVLIQTKVPLHSVTQASDVEGITVVSAAESSAINLSVNVRGDPRFDMLHLHAMFERETIAGIPYIYGIGTFLIPSITSSSSFCNPTLMDGELTVTPLLLRETTYKGAVVDTVTPSEVMANQTSEEVASALANDAVLLVSGQLERLATVVGDVIPIASGEDDAATSAIVGRLAIEATMRARHGGDTRALPNFGQLWKRAKRAASMFASNPALALQVGVPVLADSGILSALTSGVSTAIRTGSLGKGVSDASSKLNARQSLTLARKTFFKKVEELWPSQ", "text": "FUNCTION: Interacts with VP7 to form the outer icosahedral capsid with an incomplete T=13 symmetry, about 80 nm in diameter, and consisting of 200 VP4-VP7 trimers. Myristoylated N-terminal peptide may be released in the endosome and involved in permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm (Potential). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the aquareoviridae outer capsid VP4 protein family."}
{"protein": "MNQEDNTGGGGIFGLFKWTKDALFGTDISPSMKYKDQEERRDRSRYAQDDTNFSMKFGNDSNRRSTNLSRSNSWSGLDSTLHRKYELLPEYNENGFNSIVNGDHHSKERIRSLRSPAPIVPREPLRNEPTDTFGHRLHTKRRTINELSNSQIPFIPPQEDDPLLSKLFNKDGVNEVRRSPYKLSVKDIPGKFPSPLTKRDEIDNYYVRDEDACHNNREYKKAYFDLFAQMDLNSRDLEDLCEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYYSLGQKYKSLKKVLDQTISHEAELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNYESEIHDLLLQLSLRNNERKDTSAGSNIFSTGQYDRTPFHNGNNSYDSNSHSWDTDYLKNIDGFIER", "text": "FUNCTION: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. Connects the central plaque of the SPB with the half-bridge. Required for proper localization of CDC5 at the SPB and for proper M-phase progression (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body Note=Associates with the periphary of the central plaque. SIMILARITY: Belongs to the BBP1 family."}
{"protein": "EVDMRCKSSKECLVKCKQATGRPNGKCMNRKCKCYPR", "text": "FUNCTION: Reversibly blocks voltage-gated potassium channels (Kv1.1/KCNA1 (Kd=79 uM), Kv1.2/KCNA2 (Kd=547 nM) and Kv1.3/KCNA3 (Kd=492 nM)). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 01 subfamily."}
{"protein": "MADGYWNRQQSLLPHSGLHKRPRPDYEMPASGLPSGNEMHYLSREEDRSGHPMVKDSKTIGSAYDRYLQGQVPSFTSGEASTVGALGLQRGIGGLPNHSLSDPSAMIGRHGGGGPDLAPNGRGMNYGFQPPMDPVSRHGPEPALLPPDASPTLYIEGLPSDCTRREVAHIFRPFVGYREVRLVSKEAKHRGDPLILCFVDFANPACAATALSALQGYKVDEINPESSHLRLQFSRYPGPRSGGGPRSSGPPRGGHGSRGRR", "text": "FUNCTION: RNA-binding protein interacting with the enod40 RNA. SUBCELLULAR LOCATION: Nucleus speckle Cytoplasmic granule Note=Exported into cytoplasmic granules during nodule development (PubMed:15037734). Relocalizes to cytoplasmic granules when associated with enod40 RNA (PubMed:15037734)."}
{"protein": "MAATTAPNPLTAYRFLLRATRIAFQGDFTTLHAARAEARKQFDQHRKQGVDTPMRIQHAMETAEILRTNVVQGVKISGAGEEAERYASILVMRRFRGEYEGEDERREKEEAMRELRIHEHIERGDNDSIKTAGKNERVKVAVGKACSNTQSSE", "text": "FUNCTION: Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family. MZM1 subfamily."}
{"protein": "MVGAAILESPGEGIGSNSILSQKRQLSSSDAAKRDAKKRSTMLMDLEILDCPICYEAFTIPIFQCDNGHLACSSCCPKLNNKCPACTSPVGHNRCRAMESVLESILIPCPNAKLGCKKNVSYGKELTHEKECMFSHCACPALDCNYTSSYKDLYTHYRITHMEINQINTFICDIPLSVRMNISKKILIRTEHLTNHLFAVQCFREPYGVYVTVSCIAPSSPELSQYSYALSYTVDGHTVIYQSPEVKRVLKLSFQTPQENFMLIPNSLLRGDVLEMRISVKKLNKE", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. SIMILARITY: Belongs to the SINA (Seven in absentia) family."}
{"protein": "MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRVFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGLNQEEFTDGEEEEEEEDTAAGEPSRDTRGAAGPLDKGGSWCDS", "text": "FUNCTION: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Membrane; Peripheral membrane protein Membrane; Lipid-anchor Postsynaptic density Synapse, synaptosome Cytoplasm, cytoskeleton Note=Also membrane-associated, present at excitatory synapses."}
{"protein": "MVAGLRDFTLRTEDGSGKPVLDESNGEELMHVQTSVAVALGNRPIESPGTLYITSRKLIWLSDVDMAKGYAVDFLSISLHAVSRDPEAYSSPCIYTQIEVEEDEDDESDSESTEVLDLSKIREMRLVPSDSTQLETLFDVFCECAELNPEPVQEEEEESGHNWVFSADQMDVRGGDDDAEWQISQSPTSVIGHSNGDEGLNQPMLELQINDQRFEDAEEMVHESETKDH", "text": "FUNCTION: May participate in cellular volume control by activation of a swelling-induced chloride conductance pathway. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pICln (TC 1.A.47) family."}
{"protein": "MATVPEPINEMMAYYSDENELLFEADDPKQMKSCIQHLDLGSMGDGNIQLQISHQFYNKSFRQVVSVIVAMEKLRNSAYAHVFHDDDLRSILSFIFEEEPVIFETSSDEFLCDAPVQSIKCKLQDREQKSLVLASPCVLKALHLLSQEMNREVVFCMSFVQGEERDNKIPVALGIKDKNLYLSCVKKGDTPTLQLEEVDPKVYPKRNMEKRFVFYKTEIKNTVEFESVLYPNWYISTSQIEERPVFLGHFRGGQDITDFRMETLSP", "text": "FUNCTION: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B- cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T- helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. SUBCELLULAR LOCATION: Cytoplasm, cytosol Secreted Lysosome Secreted, extracellular exosome Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. SIMILARITY: Belongs to the IL-1 family."}
{"protein": "MVHSNGAITSTILKARHADVVRKTSLHHANDLTLIDLVLNVQRLLALPSDANFVLKYKDEEGDLVTLAEDSDLLLALHTSGATLDVTVVVDSRAREAVHDVQKQVEQIKLDVGKLLGALSALDVAQIAEQSNTSVANLSAPKQSHHDNIVFQKSFEAAPPSPVPSEKAELPATIQPSVHEQFNHRPAHVEEEIPLENHYAPPPHQQIPDDLNTSFSSQPPPPIEQFGAIPPPNATIPSFPTSNAASPPVQEFAPPPPQQQQQQFQAPPPPMASHSSISSTPVQQQGFAPPQQFGGPPPSGPPSEYGGYAPPQQQQQQFGAPPPQGAPQQGFGAPPQGPPQGGPPQGSFGAPPPQQFHAPSPQSFGGPPPPVSSAPGNFAPPPQSGPPGAFAPPPSAFGAPQGPGGPGGYGPPPPGGPGAPGSYGPPQGGPGGFGPPPPGGPGAYGPPPTGFPPVGAPPPGAAGAPGGNPFARGPSATGYRQSPYQQ", "text": "FUNCTION: In its hexameric form, promotes the accumulation of sec-16A.1 and the COPII subunit npp-20 at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER), to positively regulate secretory cargo trafficking from the endoplasmic reticulum to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) and Golgi apparatus (PubMed:21478858). Required for the assembly of proteins, such as the GTPase rab-6, at the Golgi apparatus (PubMed:21478858). Plays a role in negatively regulating cell death and promoting cell and body growth (PubMed:18635357). SUBCELLULAR LOCATION: Endoplasmic reticulum Endoplasmic reticulum-Golgi intermediate compartment Mitochondrion Note=In oocytes, co-localizes with sec- 16A.1 at endoplasmic reticulum exit sites (ERES) (PubMed:21478858). In proximal oocytes, localizes to a cloud-like region at endoplasmic reticulum exit sites that spreads to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (PubMed:21478858)."}
{"protein": "MKLLLLLLSFSLAPKTEAGEIIGGHEAKPHSRPYMAYLQIMDEYSGSKKCGGFLIREDFVLTAAHCSGSKINVTLGAHNIKEQEKMQQIIPVVKIIPHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKCESYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKKVAAGIVSYGQNDGSTPRAFTKVSTFLSWIKKTMKKS", "text": "FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T- cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (By similarity). It cleaves after Asp (PubMed:9765264). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (By similarity). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution (By similarity). Cleaves caspase-3 and -9 (CASP3 and CASP9, respectively) to give rise to active enzymes mediating apoptosis (PubMed:9765264). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity). SUBCELLULAR LOCATION: Secreted Cytolytic granule Note=Delivered into the target cell by perforin. SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily."}
{"protein": "MNKVFIIGVCLFIVSQAVLAVPWDSDESSDERLSDRSDESREEPRKLVVSDDDSREDSNESAEVRRRDDSRESEEEPRKLSADTSDEDSDDSQESPLDLFFKTLRDSKISRAQRAALLKALLSRYAGY", "text": "FUNCTION: Plays a role in cuticle calcification. May induce precipitation of the calcium stored in the posterior caeca as calcium carbonate. SUBCELLULAR LOCATION: Secreted Note=During the premolt period, localizes to microvilli-rich apical regions and to the subnuclear region. During the postmolt period, localizes to the intercellular space, basal region of cells and calcium reabsorption spherules."}
{"protein": "MAAAAPAAAAASSEAPAASATAEPEAGDQDSREVRVLQSLRGKICEAKNLLPYLGPHKMRDCFCTINLDQEEVYRTQVVEKSLSPFFSEEFYFEIPRTFQYLSFYVYDKNVLQRDLRIGKVAIKKEDLCNHSGKETWFSLQPVDSNSEVQGKVHLELKLNELITENGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEIFYFEVTRSSSYTRKSQFQVEEEDIEKLEIRIDLWNNGNLVQDVFLGEIKVPVNVLRTDSSHQAWYLLQPRDNGNKSSKTDDLGSLRLNICYTEDYVLPSEYYGPLKTLLLKSPDVQPISASAAYILSEICRDKNDAVLPLVRLLLHHDKLVPFATAVAELDLKDTQDANTIFRGNSLATRCLDEMMKIVGGHYLKVTLKPILDEICDSSKSCEIDPIKLKEGDNVENNKENLRYYVDKLFNTIVKSSMSCPTVMCDIFYSLRQMATQRFPNDPHVQYSAVSSFVFLRFFAVAVVSPHTFHLRPHHPDAQTIRTLTLISKTIQTLGSWGSLSKSKSSFKETFMCEFFKMFQEEGYIIAVKKFLDEISSTETKESSGTSEPVHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSRELTYHKQPGSKDAIYTIPVKNILAVEKLEESSFNKKNMFQVIHTEKPLYVQANNCVEANEWIDVLCRVSRCNQNRLSFYHPSVYLNGNWLCCQETGENTLGCKPCTAGVPADIQIDIDEDRETERIYSLFTLSLLKLQKMEEACGTIAVYQGPQKEPDDYSNFVIEDSVTTFKTIQQIKSIIEKLDEPHEKYRKKRSSSAKYGSKENPIVGKAS", "text": "FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4). SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region."}
{"protein": "MSTATIQDEDIKFQRENWEMIRSHVSPIISNLTMDNLQESHRDLFQVNILIGRNIICKNVVDFTLNKQNGRLIPALSALIALLNSDIPDIGETLAKELMLMFVQQFNRKDYVSCGNILQCLSILFLYDVIHEIVILQILLLLLEKNSLRLVIAVMKICGWKLALVSKKTHDMIWEKLRYILQTQELSSTLRESLETLFEIRQKDYKSGSQGLFILDPTSYTVHTHSYIVSDEDEANKELGNFEKCENFNELTMAFDTLRQKLLINNTSDTNEGSNSQLQIYDMTSTNDVEFKKKIYLVLKSSLSGDEAAHKLLKLKIANNLKKSVVDIIIKSSLQESTFSKFYSILSERMITFHRSWQTAYNETFEQNYTQDIEDYETDQLRILGKFWGHLISYEFLPMDCLKIIKLTEEESCPQGRIFIKFLFQELVNELGLDELQLRLNSSKLDGMFPLEGDAEHIRYSINFFTAIGLGLLTEDMRSRLTIIQEVEDAEEEEKKLREEEELEKLRKKARESQPTQGPKIHESRLFLQKDTRENSRSRSPFTVETRKRARSRTPPRGSRNHRNRSRTPPARRQRHR", "text": "FUNCTION: May be involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CWC22 family."}
{"protein": "MSQTDILYACVSYKGVCLVEHKIANGNFIDLARRLITKIPPTSKKIYTSENHNFHYISENDLAFLCLCHEKLGVQIPSEFLSDIRQQFIRSYGQSFSQNSPTATYDPFIRVLEERMKYYSNPKSNKMNLVMDQVSEAKGALTDAIEKTIHRGEKIEIIVDKTERLQSESFVFKSNSVALKRKLWWQNKKLAIAIGLVVCILIAVITLALLKYFKVI", "text": "FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein Late endosome membrane; Single-pass type IV membrane protein Lysosome membrane; Single-pass type IV membrane protein Endoplasmic reticulum membrane; Single-pass type IV membrane protein Cytoplasmic vesicle, phagosome membrane; Single-pass type IV membrane protein Note=During macropinocytosis highest levels are found in endosomes with lower levels observed in the lysosomes. SIMILARITY: Belongs to the synaptobrevin family."}
{"protein": "MSLAEAIRLWNEGVLAADKKDWKGALEAFSEVQDPHSRICFNIGCVNTILENLQAAEQAFTKSINRDKHSAVAYFQRGMLYYRMEKYDLAIKDLKEALTQLRGNQLIDYKILGLQFKLFACEVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKQKLFEPVVIPVGRLFRPNERQVAQLAKKDYLGKATVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSPESDIPPPPNSSPPGRLQLSPGHKQKEPKELKLSVPMPYMLKVHYKYTVVMETRLGLPYSQLRNMVSKKLALSPEHTKLSYRRRDSHELLLLSEESMKDAWGQVKNYCLTLWCEHTVGDQGLIDEPIQRENSDASKQTTEPQPKEGTQVVAIFSYEAAQPEDLEFVEGDVILVLSHVNEEWLEGECKGKVGIFPKAFVEGCAAKNLEGIPREV", "text": "FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NCF2/NOXA1 family."}
{"protein": "MLDLYPVQNLTVDQLEYEKNTRFLQPAWDWIKNGNEHILSSPLFPPFYALSIDYTWVAVFTFIDVFLCNVPFFKDAKIQKDRKVTWDLIKKSLKLQGWNQLLWIYPMALVQLIWVPDTELPILAPTVFEMLSQLAIFFLAFDFTYFWFHYINHKVKWLYRWCHSVHHMYSSPFAASAQHLHPFELFFVGTFITTIPWIFPTHCLTYWIWFFIAQSVSYEVHIGYDFPFALHRIFWFYSGAPAHDMHHLRPLTCFQPWFNYLDRLMGYHITYADLKKMTEAKFKKFGLYSAEDEKGLIKIN", "text": "FUNCTION: Probable sterol desaturase. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MARPQQRYRGFRQRHWGSWVSEIRHSILKTRIWQGTFESAEDAARAYDEAARLMCGTRARTNFPYNPNASQSSSSKLLSATLIAKLHRCYMASLQMTRPSSLPEAPRIIASPNNAVKGIGADAMLLPKKREQEEQETGGNLDFKKVKVECSQQFKPLEEDHIAQ", "text": "FUNCTION: Essential for all lupin cells independent of the respective tissue. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MINIDPHFIHNLTNKLKTFDNFSLYVHVNPDFDAFGAAFAFKAFLAVYFPHKKAYVMGSHNIKADGKDLFPFEAAPIDDAFVKNSLAIIFDTSNQERVLTQKHKLAKETVRIDHHPKTESFADLEWIDPAFSAAAEMVGYLILQMGYELNAEMAAYIYAGIITDTQRFSSSATTPQTFALTAKLLETGFNRNKVHDAVYLKPLLEHKYFSYVLNKAKITPNGLAYALLKKGTYKQFGVVSPLPMVHALNNIKGVKIWTTCYFNEDIKKWIGSIRSRSIPINNFAQMFGGGGHKYAAAFVLDDKRQFMKLVEIMDDFLAKQKHVNS", "text": "SIMILARITY: Belongs to the mgp1/MG371 family."}
{"protein": "MGGLDVVRAAHLHPSYELVDWKRVGQNKLVALVRSALVRVKFQDTTSSDSNNQDTSQNALSFDTQESQKALNGSQSGSSDTSGSNSQDFASYILIFQAAPRATWVFERKIKLALPYVKQESQGSDDQGSNGKGSLYTTLQDLLVEQPVTPYTPNAGLARVNGVAQDTVHFGSGQESSWNSQRSQKGLKTTPLPMPSPALSSIRAARTGSWMKVDRCMNPWIRPRRGRGRMRALGKIRKKQRRKMMPRWWGWLEVVRLEVLLVYKAMARTVRG", "text": "SIMILARITY: Belongs to the MgpC family."}
{"protein": "MEESQQLKDAGLKITLPRIKVLQILEQSRNHHLSAEAVYKALLESGEDVGLATVYRVLTQFEAAGLVSRHNFEGGHSVFELSQGEHHDHLVCVKCGRVEEFVDEIIEQRQKAIAERAHFKMTDHALNIYGICPQCQ", "text": "FUNCTION: Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Fur family."}
{"protein": "CSKGGVGRGYGIG", "text": "FUNCTION: Inulin-specific lectin. Has hemagglutinating activity towards rabbit erythrocytes. Has mitogenic activity towards murine splenocytes."}
{"protein": "MNAPRPHDLLWGMPVSGLPTDAPQWALEVLASGQPVVVRRATCEAGWVAVGLRGHGRAQRLGALMRLTDIQRQQGPEALRVHGQSPWPALQALASVTPVLQARGLAWGPTGGVGYQLATGMEVVHAGSDLDLLLRTPRPLARAQARELLDILDCAPCRIDVQLETPSGAVALREWASFALRVLLKSPHGPRLVSDPWAVMERAP", "text": "FUNCTION: Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-A to the apo-[acyl-carrier-protein] of the malonate decarboxylase to yield holo-[acyl-carrier-protein]. SIMILARITY: Belongs to the MdcG family."}
{"protein": "MNTSSRSSEPSKVADDVYVQTRWNNEFKHADYLPESLQKCLDQEKTVLERYSELVEVSKTVANESSQALVKHTTKPGDQLVRRVFQQPHQQISLMERYEKTRSYKPQWHAPWKLSKVINGHTGWVRCVCVDPVDNEWFATGSNDTTIKIWDLAAGKLKITLIGHVMSVRDIAISKRHPYMFSASEDKLVKCWDLERNTAIRDFHGHLSGVHTVDVHPSLDIIATAGRDAVVRLWDIRSRSEIMVLPGHKSPINKVKCLPVDPQIISCSGDATVRLWDIIAGKASKVLTHHSRNIRDLTLHPAEFSFASVSTNDVRSWKLPEGQLLTNFQSQNTGILNTVSINHDNVLLAGGDDGTLCFYDYKTGHKYQSMMTTEVAGSLESERSILCSTFDVTGTRLITGEGDKSIKIWKQVPDATEDTFPGLPWNPTLISQRF", "text": "FUNCTION: Involved in pre-mRNA splicing and required for cell cycle progression at G2/M. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the WD repeat PRL1/PRL2 family."}
{"protein": "MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVALAEHHDLDLPYCFNRKEAKDHGEGGNLVGSALQGRVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV", "text": "FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily."}
{"protein": "MGFVLVPKSDFQIPLEADTIRPDLFEGLDLDEIRSLQVYEGNIKRPLGEFFEIAETSHEDQLIRIDGDVSRVKYIGSGMKSGKIIINGDVGLQLGCEMKGGEIEVNGNVSSWIGMEMHGGTIKINGNAGDYVGCAYRGEWRGMKGGKIIIQGNAGNNIGGGMMAGEIYIGGDAGNFCGIRMNGGEITVRGDAGRAPGAEMVSGIIKIHGRISSLLPGFKEISTFKEDGSLMILFKGDLSEKNPEGNLYINYNKNLHILENETDEGRVITKKGIKVIYNSGSTIREGQIIKGGNKLTDDYIDECARCCISPEDYKLLGEPENVVVSSHGNEVVLRAVEDPGIQMGTIFIPRGIWANVLTPPYTESTGSPMYKGVPVYLRKASQGERILSAEELVEEYGVGK", "text": "FUNCTION: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize formylmethanofuran. This enzyme is oxygen-labile. SIMILARITY: In the C-terminal section; belongs to the molybdenum dinucleotide binding protein family. SIMILARITY: In the N-terminal section; belongs to the FwdC/FmdC family."}
{"protein": "MDARHQPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINQGLGLDLFEGDIKLEANGKNSIIGDHKRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEANYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYVIIVWDRIQPGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIVTRISEFEDVIGQRMDFSDYDLLKLNQLYNCTSSLSFMDSCDFELENICGMIQSSGDSADWQRVSQVLSGPESDHSKMGQCKDSGFFMHFNTSILNEGATAMLESRLLYPKRGFQCLEFYLYNSGSGNDQLNIYTREYTTGQQGGVLTLQRQIKEVPIGSWQLHYVTLQVTKKFRVVFEGLRGPGTSSGGLSIDDINLSETRCPHHIWHIQNFTQILGGQDTSVYSPPFYSSKGYAFQIYMDLRSSTNVGIYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMFNQRSITTDPTMTSDNGSYFWDRPSKVGVTDVFPNGTQFSRGIGYGTTVFITRERLKSREFIKGDDIYILLTVEDISHLNSTSAVPDPVPTLAVHNACSEVVCQNGGICVVQDGRAECKCPAGEDWWYMGKRCEKRGSTRDTVIIAVSSTVTVFAVMLIITLVSVYCTRRKYRKKARANTAAMTLENQHAF", "text": "FUNCTION: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position (PubMed:11278902). Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Secreted Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17."}
{"protein": "MGCLFSVNSKKVRIFDTTLRDGEQAPGIDLTVDQKIRVAKRLAELGVDVIEAGFPASSDGEFEATKKILSEIGDQVEVTGLSRSVKQDIDRTIDTGLSSIHIFIATSDIHLKYKLKMTREEVLNRIYESVRYAKDHGLIVEYSPEDATRSDEEFLLKAVKTAIDAGADRINIPDTVGVMHPFKFYDLISKIVKVTGDKIVSVHCHNDFGLATANSIAGVMAGARQVHVTVNGIGERAGNASLEEVVMSLKKLLGYDVGVRTYLLYEVSRYVAELTGVPVPYFKAIVGENAFGHEAGIHVHGVIENPMTYEPISPEEVGNFRRIALGKHSGIHGLKRLLEEQGIFLDDTQLREVLKEIKSLAEAGNKVTSADAKAIAIKVINKKITA", "text": "FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). Carries out the first step of the leucine biosynthesis pathway. Also displays a low citramalate synthase activity, using pyruvate as substrate, but is unable to use 2-oxoglutarate. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family."}
{"protein": "MAELGEADEAELQRLVAAEQQKAQFTAQVHHFMELCWDKCVEKPGSRLDSRTENCLSSCVDRFIDTTLAITGRFAQIVQKGGQ", "text": "FUNCTION: Probable mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the small Tim family."}
{"protein": "MQVQQPQQIQQQHLQQQQAQQHQQQQVQQHQQQQQQQQQQQQIYQQIVNQPVNNVHQLPSLQQQQLLEQYDELLKQVSLIRSNVSDFFNSFIEDAKQQQTIVNKEEMKQKLKKSMDLVLGSISSIDKVSKRISSYSFQIASSNFSTQEASWAYSTGIYDNRNIKVQLEIRNENYWRSQTSYKSSLASSNLENKLKDLFPIIFQEDEESSSLSKKRKQISSLTSNSLSTTTITTTTTPSPLFKLPSTPPTLLLSGTISPFYDYFAQIERVIHSIRQESALEIFEIQKQSSGAPKGLFVECPDVFKCLICFGIPNDRKDCFTIDRISFFGVKENFDSLWASSKYNIFKKISENSFEAISYYSANPNGGSILKCILSWIWSFRGLFLEECKGCQDILHLDSPQYMYLPPSFRTFDNYTPYHPSCYQNHLLSCNSFSSSTSSSIQQSPFSPLNK", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 27 family."}
{"protein": "MTTLSCKVTSVEAITDTVYRVRLVPDAAFSFRAGQYLMVVMDERDKRPFSMASTPDEKGFIELHIGASELNLYAMAVMDRILKDREIVVDIPHGDAWLRDDEERPLILIAGGTGFSYVRSILLTALARNPARDVTIYWGGREEKHLYDLSELEALSVNHPNLRIEPVVEQPEEGWRGRTGTVLTAVLQDYGTLAGHDIYIAGRFEMAKIARDLFCHERNAREDRLFGDAFAFI", "text": "FUNCTION: Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family."}
{"protein": "MKLWLFACLVACFVGAWMPVVHAQGAFEDCCLGYQHRIKWNVLRHARNYHQQEVSGSCNLRAVRFYFRQKVVCGNPEDMNVKRAMRILTARKRLVHWKSASDSQTERKKSNHMKSKVENPNSTSVRSATLGHPRMVMMPRKTNN", "text": "FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MNLRLSCLLFILVTSLPAGRCSIGNKGISFETCTAIEGLCFFGCKLGWVWIAYCNNIMSCCRKDTDFVLPQTKGI", "text": "FUNCTION: Has bactericidal activity (By similarity). May play a role in the antimicrobial protection of sperm and urogenital tract epithelia (PubMed:16023745). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family."}
{"protein": "MATKASNLVVFLLSLLLLFLLISFQVGVADATRNKRQGQEQRVDYDYPRPPTAPIYLPPSKSRKGKGP", "text": "FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (PubMed:33514716, PubMed:34535661, PubMed:31001913). Promotes the expression of immune-related marker genes (e.g. WRKY30, WRKY33 and CYP81F2) in a MIK2-dependent manner (PubMed:34535661). Inhibits root growth and regulates root meristems (PubMed:34535661, PubMed:31001913). Prevents general growth and development (PubMed:31001913). Exhibits antibacterial effects against Pseudomonas syringae pv. tomato DC3000, Ralstonia solanacearum, Bacillus subtilis and Agrobacterium tumefaciens, thus being an antimicrobial peptide (AMP) (PubMed:31001913). SUBCELLULAR LOCATION: Cell membrane Secreted, extracellular space, apoplast Note=The precursor of SCOOP13, PROSCOOP13, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP13 in the apoplasm. SIMILARITY: Belongs to the serine rich endogenous peptide (SCOOP) phytocytokine family."}
{"protein": "MAKLNQVTLSKIGKNGDQTLTLTPRGVNPTNGVASLSEAGAVPALEKRVTVSVAQPSRNRKNFKVQIKLQNPTACTRDACDPSVTRSAFADVTLSFTSYSTDEERALIRTELAALLADPLIVDAIDNLNPAY", "text": "FUNCTION: Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation. The capsid contains also 1 copy of the A2 maturation protein. SUBCELLULAR LOCATION: Virion Note=The shell is composed of 89 dimers of the capsid protein and 1 copy of the maturation protein. SIMILARITY: Belongs to the Leviviricetes capsid protein family."}
{"protein": "MGSTATETEELENTTFKYLIGEQTEKMWQRLKGILRCLVKQLEKGDVNVIDLKKNIEYAASVLEAVYIDETRRLLDTDDELSDIQSDSVPSEVRDWLASTFTRKMGMMKKKSEEKPRFRSIVHVVQAGIFVERMYRKSYHMVGLAYPEAVIVTLKDVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNVLINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGLDKAKTMSLILHAADISHPAKSWKLHHRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIIIPLIEEDSKTKTPSYGASRRSNMKGTTNDGTYSPDYSLASVDLKSFKNSLVDIIQQNKERWKELAAQGEPDPHKNSDLVNAEEKHAETHS", "text": "FUNCTION: Calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cGMP and cAMP, which are key regulators of many important physiological processes. Has a higher efficiency with cGMP compared to cAMP. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily."}
{"protein": "MSAAALEEIGIAPLQENTSLRPPPLPATCVDVSSDDYIKLTTLERQLAHLQVMEDYIKLETRNLEKELLHAQEEVKRIQSVPLVIGQFLEAVDQNHAIVGSTTGSNYYVRVLSILDRELLKPGCSVALHKYSNALVDVLPPEADSSIQMLRPDEKPDISYGDIGGLDMQKQEVREAVELPLTHGELYQQIGIDPPRGVLMYGPPGCGKTMLAKAVAANTAASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENSPSIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQSTNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTVCSRMNLSDDVDLEDWVARPDKISGADINSICQEAGMQAVRENRYVVLTKDLEKAYKNVVKKDTNDFEFYK", "text": "FUNCTION: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MTTIQPFEPVDLFKTNNVNLDILTENFPLEFYFEYMIIWPDLFFKSSEMTVDPTFKHNISGYMMAKTEGKTTEWHTHITAVTVAPRFRRISLASKLCNTLETMTDVMPHEVNFIDLFVKCNNQLAIKLYEKLGYSVYRRVVGYYNSAEDGYPDTLKKVDDNKDAFDMRKAMARDRNRSVRPDGRSHKCYPHDVRF", "text": "FUNCTION: Catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn, Met-Gln or Met-Met. NatB acetylates TPM1 protein and regulates tropomyocin-actin interactions, it is presumed to N-acetylate 15% of all yeast proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily."}
{"protein": "MNTVRVTFLLVFVLAVSLGQADEDGNRMEMRQEIEKTEADSSYFAENLLLQKLEELEAKLWEETSEESRNSRQKRCAAEGIPCDPNPVKDLPCCSGLACLKPTLHGIWYKHHYCYTQ", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 01 (HNTX-16) subfamily."}
{"protein": "MATANSIIVLDDDDEDEAAAQPGPSHPPPNPASPQAEAPGSSQPHGAGGSSSSGGKKCYKLENEKLFEEFLELCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRAQSRPAKLYVYINELCTVLKAHSAKKKLNLAPAATSSEPSGNNPPTDPSSDPTNAETTASEAPRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSTYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGIDPALSDPALARRLRENRSLAMSRLDEVISKYAMMQDKSEEGERQKRRARLPQATSSHSTDPLKASLDSGEGPSGMASQECPTTSKPETDDEEDEESEEEEEEEEEEEEEEATDSEEEEDLEQMQEGQGDDEEEEEEEEEAGQDGDKSPMSPPRISTEKNLEPSKGISRSMGEQQNKEFTVSPSSEEPLAPSSIDAESNGENLEELLLEEESPISQLFELEIEALPLDTTPSPEERDISSSRKQSEEPLTTVLENGAAMVTSTSFNGGVSPHTWGDSCPPCKKSRKEKETGAEPLGNSYVERQRSVHEKNGRKIPTLPSPPSPLTSMAPVADSSTRVDSPSHGLVTSSLCSASQARLSQTPHSQPSRPGTYKMSVATQCDPEEIIVLSDSD", "text": "FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX (By similarity). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Nucleus, PML body Nucleus, nucleolus Chromosome, centromere Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. SIMILARITY: Belongs to the DAXX family."}
{"protein": "MSLEFGFILINIFTAIVSFSTLSHALLHPSSVSHNVSRSRYYMTTNELWFNQTLDHESPNDHRKFRQRYYEFMDYFRSPDGPMFMIICGEGPCSGIANDYINVLAKKFQAGVVSLEHRYYGKSSPFNSLATENLKYLSSKQALYDLASFRQYYQESLNKKLNISSGGSDNPWFFFGISYSGALSAWFRLKFPHLTCGSLASSAVVRAIYEFSEFDQQIGESAGQECKLALQETNKLLELGLKVKNKAVKSLFNATELDVDADFLYLTADAAVMAFQYGNPDKLCVPLVEAKKNGSDLVVTYSTYVREYCMRIWGLRVRTYNRKHLRNTVVTADSAYRLWWFQACTELGYFQVAPKYDSVRSHQINTTFHLDLCKSLFGKDVYPKVDATNLYYGGDRLAATKIIFTNGSEDPWRHASKQNSTHEMPSYIIKCRNCGHGSDIRGCPQSPMVIEGKSNNCSLPDYVNKVRQQMVEHIDLWLSECRQSIRSSI", "text": "FUNCTION: May be involved in a proteolytic pathway controlling the nuclear division phase of megagametogenesis. SUBCELLULAR LOCATION: Secreted Note=Prediction of a peroxisomal location. SIMILARITY: Belongs to the peptidase S28 family."}
{"protein": "MKNPHLNSPCKILNTVSGDKKMKRKAREPIKHVSEDHYPYFKLYKNPHLMAETLGDGSPQETHRSEIITSRDDSVRNDVLNTAVDMRINTITAAEVPDSKLRSVSEKTVNSKIVQASPQVSVLSAPQVFPLERVVLSQRAASQAPAGGSERAESPRKRAGEPSGVVTEIKAIQQTRRLLANARERTRVHTISAAFEALRKQVPCYSYGQKLSKLAILRIACNYILSLAQLADLDYTPDHRNMSFRECVEQCTRTLQAEGRSKKRKE", "text": "FUNCTION: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (By similarity). During development, is required for heart looping and swim bladder formation by acting in concert with GATA4 and ZFPM1 (PubMed:23836893). During the development of both the retina and skeletal muscles is required for neural retinal cell through modulating PAX6 and NEUROG3 expression and myogenic differentiation (PubMed:20532172). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm."}
{"protein": "MPLDDDLEDNPSLVPPPSTTTTSSNATGDAATMMDEVEEAEDAPTADFRLFASTYSKTKNISAQTIRKGEKDFESHGTRAQASALDASRDAMRDVLSYTRVHNTKSASGWCRGWYFPDWWKDWPEDWEQQKLTKRGKEGAGEDDEEEKDRKLPPLHVRDRVVLLEHTNVASQSLGRAVTGLPKDRPARGREWLLPEEALYLVERGSLDLWWPTKGIEEVFPADGSVPAAAAATTSAKGEGEQRTEEDEEDDDEYKYGLPLSLQAAYALLIGEDGERGKVSLQKFQVFSHLKRAGYNVIRAPTNPLPVQEDTQLTTTTQPASKPISVTEWLISCLPQSKSSPTDPPPYGPLVPPGFYRSYNTIYNYLSLRPSSTSSSASPTADNQPQKPQSPESDESDSGSDSPYKIHYHVYKASTKFTRTRPPPPDFYISVISAKDTSIPTLSEISSLLASAPADLPKAEWLAGGPARLYARLKHGYRNVLLAVNDHGVINYMRFAEGGFAKEELFRNYDMRVSGGPRRGGGGGGKKSGNNNGRGSRGRGGGRGGGRGGRGGRGRGN", "text": "FUNCTION: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. May be required to embody the molecular ruler of the complex (By similarity). SIMILARITY: Belongs to the SEN54 family."}
{"protein": "MLTRSVLRKAPRAFSPFLQKRNLALHEYISHDILRKFGVDVPRGAPARSGEEAEKVARDLKVTDLVVKAQVLAGGRGKGQFDSGLRGGVRPVYDATEARMFAEQMIGHKLITRQTGPAGKICNVVYVCERKFIRKEYYFAILMDRENQCPMIVASDQGGVDIETVAAENPSAIIKRSLPNSPNLDPHIAEELVDKLGFSSSSKPKAVDAIVKLYKVFNDCDATQVEINPLAETTDHKVLCMDAKLNFDDNAEFRHSNIFVLRDISQEDPDEARAAKVGLNFIKLDGNIGCLVNGAGLAMATMDIIKLHGGEPANFLDVGGNANAEAIREAFSLITNDPKTTAIFVNIFGGIVRCDVIAKGLISVVSALNLNIPIICRLQGTNQGAAKEVINNSGLRIFSFDDLDEAAKKACRFSRVVEMAREADVNVSFELPL", "text": "FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family."}
{"protein": "MRFQSIMMLTITCAGTCLAEGLAPSDQAYRPTMTGLKSRLNDPRPLSTATIATSSERFLRFDTVARDTAGNDEERVGPSWLAKVDGLMHKMVTSSLSAEEAQLKVWIQSQIHPRELFGVLSLGKRAAKLDDNPDFVQWLRLVKDFRANNGNQAFSDLDIYYLLLKTNSPEQLKLLFETLRHTPGMTKIGASMEKSLSGNWIRKALEQDTYPTIVYNTLRLKDAGTKLDDTPMFRQWLEYVEKYWNKNAGAFFGDTQMLTLFQKTMTEEEDIIKLVHMLRNNPGMKSHADKLERYLLLTSESSHKTMADVWLKARETPEEVFRILRLAEKQTAAADDNRMLNLWLRYTQTYRDKIDKNAFSDAEALQFFRKAKPLDFDWEIV", "text": "FUNCTION: Effector that specifically binds host autophagy protein ATG8CL of the ATG8 family to stimulate autophagosome formation and subsequent autophagy rather than blocking autophagic flux (PubMed:26765567, PubMed:29932422). The pathogen remodels host-microbe interface by co-opting the host autophagy machinery which plays a key role in plant immunity (PubMed:29932422). PexRD54 competes with the autophagy cargo receptor Joka2 to deplete it out of ATG8CL complexes and interferes with Joka2's positive effect on pathogen defense (PubMed:26765567, PubMed:29932422). SUBCELLULAR LOCATION: Secreted Host nucleus Host cytoplasm Note=Localizes to host autophagosomes across the perimicrobial membrane. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MGGIYTALLVVITLFIGNDNILAAHIELQTIQPDHTTYSPFLRKTDPRPQRAFENTAELSATSEERQWYEISMRRAKENLTFYIWYKKGKTPQDIYLKFFTNSMDTITVSKSPNFGTFSRYTEYYNKNKKNDSWFRS", "text": "FUNCTION: Effector that is involved in host plant infection. Contributes to virulence during the early infection stage, by inhibiting plant defense responses induced by both PAMP-triggered immunity (PTI) and effector-triggered immunity (ETI). SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MTDVTLKALAAERQVSVDRLVQQFADAGIRKSADDSVSAQEKQTLLAHLNREAVSGPDKLTLQRKTRSTLNIPGTGGKSKSVQIEVRKKRTFVKRDPQEAERLAAEEQAQREAEEQARREAEEQAKREAQQKAEREAAEQAKREAAEKAKREAAEKDKVSNQQTDDMTKTAQAEKARRENEAAELKRKAEEEARRKLEEEARRVAEEARRMAEENKWTATPEPVEDTSDYHVTTSQHARQAEDENDREVEGGRGRGRNAKAARPAKKGKHAESKADREEARAAVRGGKGGKRKGSSLQQGFQKPAQAVNRDVVIGETITVGELANKMAVKGSQVIKAMMKLGAMATINQVIDQETAQLVAEEMGHKVILRRENELEEAVMSDRDTGAAAEPRAPVVTIMGHVDHGKTSLLDYIRSTKVASGEAGGITQHIGAYHVETDNGMITFLDTPGHAAFTSMRARGAQATDIVVLVVAADDGVMPQTIEAIQHAKAAGVPVVVAVNKIDKPEADPDRVKNELSQYGILPEEWGGESQFVHVSAKAGTGIDELLDAILLQAEVLELKAVRKGMASGAVIESFLDKGRGPVATVLVREGTLHKGDIVLCGFEYGRVRAMRNELGQEVLEAGPSIPVEILGLSGVPAAGDEVTVVRDEKKAREVALYRQGKFREVKLARQQKSKLENMFANMTEGEVHEVNIVLKADVQGSVEAISDSLLKLSTDEVKVKIIGSGVGGITETDATLAAASNAILVGFNVRADASARKVIESESLDLRYYSVIYNLIDEVKAAMSGMLSPELKQQIIGLAEVRDVFKSPKFGAIAGCMVTEGTIKRHNPIRVLRDNVVIYEGELESLRRFKDDVNEVRNGMECGIGVKNYNDVRVGDMIEVFEIIEIQRTIA", "text": "FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily."}
{"protein": "MQKFLTTAPVVAAIWFTLTAGILIEWNRFFPDLLFHPM", "text": "FUNCTION: May help in the organization of the PsaE and PsaF subunits. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaJ family."}
{"protein": "MLPDSSVRLNKYISESGICSRREADRYIEQGNVFLNGKRATIGDQVKPGDIVKVNGQLIEPREAEDLVLIALNKPVGIVSTTEDGERDNIVDFVNHSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITDEFIRGMGAGVPILGTVTKKCKVKKEAPFVFRITLVQGLNRQIRRMCEHFGYEVKKLERTRIMNVSLSGIPLGEWRDLTDDELIDLFKLIENSSSEAKPKAKAKPKTAGIKRPVVKMEKTAEKGGRPASNGKRFTSPGRKKKGR", "text": "FUNCTION: Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35 in the anticodon of tRNA(Tyr). SIMILARITY: Belongs to the pseudouridine synthase RsuA family."}
{"protein": "MTSQVPCYTIINSPDLEVTNEMQLKRDLEKGDTNVKIETLKRVIKLLLNGERYPGLIMTIIRFVLPVQNHTIKKLLLIFWEIVPKTSADGKLLQEMILVCDAYRKDLQHPNEFLRGSTLRFLCKLKEPELLEPLMPAIRACLDHRHSYVRRNAVLAIFTIYKNFDWLVPDGPELIASFLDTQQDMSCKRNAFLMLLHADQERALNYLASCIDQVHTFGDILQLVIVELIYKVCHANPAERSRFIRCIYNLLNSSSNAVRYESAGTLITLSLAPTAIKAAASCYIELVVKESDNNVKLIVLDRLVAMKEHEGMEKVMQDLVMDVLRVLAAPDIEVRRKTLALALDLVYSRNIGEMVLVLKKEVAKTHNVEHEDTGKYRQLLVRTLHTCSIKFPDVAANVIPVLVEFLSDTNELAAADVLIFIREAIQKFPALRALIIEHLIEAFPQIKSSKIHRAAVWILGEYVEGSQILEVIAVIQQTLGEVPMVEAEQRRLAGDQTEEQKQQQGSAGGNAAGSAAEGSGSGNASNKVTSDGTYATQSAYSLAPVAKAEKRPPLRQYLMDGDFFIGAALSATLTKLALRYAELETEARAQNRLTTQVMLIMSSILHLGKSGFPSKPITNDDTDRIFVCLRTLSERTPEAISVFTLYCREALGKMLDAQHDEDQRMLKEKQKATAKVQPDDPVLFAQLSNGRDNQLGENVFESSLNQALAGSKNAQLSDVASPNSKLNKVTQLTGFSDPVYAEAYVNVNQYDIVLDVLIVNQTNDTLQNCTLELATLGDLKLVERPHPVVLAPHDFCNIKANVKVSSTENGIIFGNIVYETALNTNVVVLNTIHIDIMDYIIPASCTDTEFRQMWQDFEWENKVTVNTSFTDLHEYLKHLLKSTNMKCLTPEKALSGQCGFMAANMYAKSIFGENALANLSIEKPVDDPDSKVTGHIRIRAKSQGMALSLGDKISSSQKQSVQAA", "text": "FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Required for limiting lipid storage in lipid droplets. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity). Present within the clusters of tubulo-vesicular structures of Golgi membrane and cis-Golgi membranes."}
{"protein": "MSSFHKNSSYMEDPDYPGYSGSQNHTQNYLRTQDDLEFPGCLDNPGFHHPRRNPYSSDSRTNPDYHHSLAEPDYPGSPSDADYQNTRCHPRSAHPRTRPDYEPDYEPDYNDFQSESYHPDLSMEPDYPGSHGHPGFAGVRSSVNSTGPRTNLGYLDLEEPDYPGAQGNSYHSGPRSHSNLPGSRRNAGYAGSRINSYPDSLGEPDYPGAENQPNSPDFYGKPDYPGAEEGDVYSPSKTLGVIGRSRGSFGILGREDGDYPEGIEMASLGMAGDPRNGYVNPAYMRGSSPVCPDRNLLLCARDWNTSPQGQKLIASLVPMTSRDRIKTIRNQPRTMQEKRELRKIVDKEKNKQSHGTFEANCCAQCLSSLSLAYRRTKSSLSELLNYISLWQKRFKVIGGKFGTSVLSYFSFLRWLLKFNIFSFVMNFSFIIIPQFTVGEKNTLQFTGLEFFTGAGYFRETVMYYGFYTNSTIRHRMGGASYNMQLAYIFTIGACLVICFFSLLFSMAKYFRNNFINPHIYSRGIAKLIFCWDFTVTHEKAVKLKQKNLSTEIRENLSEIRQENDRLTLNQKLTRFSVHVAAWLVSTGITAACCVAVYYLAEYNSEFLKTHKNPGAVLLLPFVVSCINLAVPRFYSMFRLVERYEIPRQEVYVLLIRNIFLKISIVGILCYYWLNIVALSGEECWETLIGQDIYRLLLMDFVFSLADSLLGEFLRRLIGMKFITSLSLQEFDIARNVLELIYAQTLAWLGIFFCPLLPFIQMITLFIMFYVKNVSLMMNFQPPSKAWRASQMITFFIFLLFFPSFTGVLCTLAITIWRLKPSADCGPFRGLPSFIQSIYSWIDTLSHRPGYLWVVWIYQNLIGSVHFFFILTLIVLIITYLYWQITEGRKVMIRLLHEQIINEGKDKMFLIEKLTKLQDIERRANPSTLVLERREVEQQSPLHLEELDAAPDLRLRRSMQEENAIA", "text": "FUNCTION: Probable ion channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMC family."}
{"protein": "MEPSPAKGKAQGRLLVSTSLDAKDELEERLERCMSITTSITNGLSEREANDALTAHVCKGPQQHEEVCLGLFTLLLTEPPQAQRCYRDLTLVNRDGMNVVLMKINQILMEKFLKLQDVCRTQLVWLVRELVKSGVIGADGVLMTLMKQIAGGDISSKNLWLAENVLDILVDQREWVLKSGMLVAMSLYTYLRLIVDHGTTSLLPLRQREVDFCIGLLRERFMECFIIGRDLVRLLQNVARIPEMELVWRDLLHSPQTLSPQFTGILQLLTSRTSRKFLACRLTPDMETKLLFMTSRVRFGQQKRYQDWFQRQYLSTAESQSLRCDLIRYICGVVHPSNEVLSSDILPRWAIIGWLLTTCTSNVAASNAKLALFYDWLFFNPEKDSIMNIEPAILVMHHSMKPHPAITATLLDFMCRIIPHFFPPLEGQVRQGVFNSLNFIMEKRVLAHLAPLFDNPKLDRELRSMLRERFPEFCSSPSPPTEVKMEESVPLEMDNHVLDKEDGCYDNTDATFSDDEEELNNKGKKREFRFHQLKETYIDEPSDITPFVDQLDEALKERVLQLQKGSDTETHCEVMQEIVDLILEEDFDSEQMSTLASCLAELFKSHFRGDVLPEEITEESLEESVCKPVCLIFRNLCQMQEDNSGFSVLLDLLAELYQKQPKIGYHLLYYLKASKAASGKMSLYESFAQATALGDLHTCLMMDMKACQEDDVRLLCYLTPSIYSEFPDETLRSGELLNMIVAVIDSAQLQELMCHVMMGNLVMFRKDSVLNILIQSLDWETFEQYSTWQLFLAHSIPLETIIPILQHLKYKEHPEALSCLLLQLRREKPSEEMVKMVLSRPYHQEDQFTTSILRHWTAKHDDLLGEHIKALLIKNNNMPRKRQSLRSSSSKLAQLTLEQMLEHLDSLRLSLSNTKNNFFSQTPILQALQHVQASCDEAHKMRFSDLFSLAEEYEDSSKPPKSRRKAPASSPRSRKGAAPQPCNEEESVSSSASEEEDSKPKASKRKRKGSAVGSDSD", "text": "FUNCTION: Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing (By similarity). FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs). In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Localizes to nuclear foci following DNA damage. SIMILARITY: Belongs to the Integrator subunit 3 family."}
{"protein": "MRSQVIEYPMSLVRLAHELPIEAPRTAWLDSIIKGDCVSALERLPDHSVDVIFADPPYNLQLGGDLHRPDQSMVSAVDDHWDQFESFQAYDAFTRAWLLACRRVLKPNGTIWVIGSYHNIFRVGTQLQDLGFWLLNDIVWRKTNPMPNFRGRRFQNAHETLIWASREQKGKGYTFNYEAMKAANDDVQMRSDWLFPICTGSERLKDENGDKVHPTQKPEALLARIMMASSKPGDVILDPFFGSGTTGAVAKRLGRHFVGIEREQPYIDAATARINAVEPLGKAELTVMTGKRAEPRVAFTSVMEAGLLRPGTVLCDERRRFAAIVRADGTLTANGEAGSIHRIGARVQGFDACNGWTFWHFEENGVLKPIDALRKIIREQMAAAGA", "text": "FUNCTION: A beta subtype methylase that recognizes the double-stranded sequence 5'-GANTC-3' and methylates A-2 on both strands (PubMed:12654995) (By similarity). CcrM-mediated methylation has important cellular functions. Contributes to the accurate cell-cycle control of DNA replication and cellular morphology (By similarity). SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MEVCIVKPDRIFFKEEADELLLPTNTGYIGILKDHAPLVTGLDNGVLGVRQGTTWRFLALLGGFGVIKEGRVNILCRDIQDASEINLEEAEQLAATAKESMTKSDSKKGYIENQLKFDRETARVAAAKMYKESAGGSPVFGN", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family."}
{"protein": "MQNLNVGLIGGGFMGKAHSLAYAAMPMFFWPAPALPVRKVIAEANPELAAEAARRFGFENSTSDWRSIIDDPDIHVVDIATPNHLHAEIAIAAAEAGKHIICEKPLARTGEESKAMYDAVKDKNIVHMVAFNYRRTPAVALAKKYIEEGAIGRILSFRGTYLQDWSADPNSPLSWRFQKSIAGSGALGDIATHVIDMARYLVGEFSAVNAVLSTWIPERPLQSGGADALGTVRGGEGPKGPVDVDDEVMTMIRFANGAVGSVEATRNAHGRNNYITFEIHGTEGSIVFNYERRDELQVAFASDQADRRGFRTVYTGPAHPYGEGLWPIPALGIGYGETKIIEAHDFFKAIAEGGSVSPSFADGYQVALIDDAIVESAAKESWVDVPQISA", "text": "FUNCTION: Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG) (PubMed:30224354). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction (PubMed:30224354). Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%) (PubMed:30224354). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG (PubMed:30224354). SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MASSSLCHRYFNKITVTPFFNTKKLHHYSPRRISLRVNRRSFSISATMSSSTKKVLIPVAHGTEPFEAVVMIDVLRRGGADVTVASVENQVGVDACHGIKMVADTLLSDITDSVFDLIMLPGGLPGGETLKNCKPLEKMVKKQDTDGRLNAAICCAPALAFGTWGLLEGKKATCYPVFMEKLAACATAVESRVEIDGKIVTSRGPGTTMEFSVTLVEQLLGKEKAVEVSGPLVMRPNPGDEYTITELNQVSWSFEGTPQILVPIADGSEEMEAVAIIDVLKRAKANVVVAALGNSLEVVASRKVKLVADVLLDEAEKNSYDLIVLPGGLGGAEAFASSEKLVNMLKKQAESNKPYGAICASPALVFEPHGLLKGKKATAFPAMCSKLTDQSHIEHRVLVDGNLITSRGPGTSLEFALAIVEKFYGREKGLQLSKATLV", "text": "FUNCTION: May be involved in oxidative stress response. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the peptidase C56 family."}
{"protein": "MKFSSIILLTLLICSMSKFGNCQVETNVKCQGGSCASVCRKAIGVAAGKCINGRCVCYP", "text": "FUNCTION: Blocks both human ERG1/Kv11.1/KCNH2 potassium channels (in a reversible manner) (PubMed:14599291) and A-type voltage-gated potassium channels Kv4/KCND (in an irreversible manner) (PubMed:11457451, PubMed:12473099, PubMed:12637022). The presence of the Kv4-associated proteins DPP6 or DPP10 is mandatory to have high-affinity blockade of Kv4.2/KCND2 and Kv4.3/KCND3 channels (By similarity). In contrast, the presence of the Kv4-associated protein KChIP1/KCNIP1 does not enhance the affinity blockade (By similarity). May dispose of two functional faces (A and B); the two basic residues (Arg-40 and Lys-41) on the alpha-helix side of the peptide that blocks the hERG current (face A) and the typical dyad through which it blocks A-type currents on the beta-sheet side (face B) (PubMed:14599291). In adult rat brain, it binds to sites in the striatum, hippocampus, superior colliculus, and cerebellum. It shares the same target in rat brain than AaTX1 (AC Q867F4) and AmmTX3 (AC P60208). In DPP6 knockout mice, A-type currents are much less affected by the toxin than in wild-type mice (PubMed:23440961). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 15 subfamily."}
{"protein": "MSLSKETEVIFDEHRGVDYDSANPPLYDSSTFHQKVLGGNAKFDYARSGNPNRQLLEEKLAKLEGGQYAFAYASGIAAISAVLLTLKANDHVILPDDVYGGTFRLTEQILNRFDIQFTTVNATQPKEIERAIQPNTKLIYVETPSNPCFKITDIRAVAAIAKRHHLLLAVDNTFMTPLGQSPLALGADIVVHSATKFLGGHSDIIAGAAITNRKDVADALYLLQNGTGTALSAHDSWTLAKHLKTLPVRFKQSTSNAEKLVAFLKEREEIAEVYYPGNSSLHLSQANSGGAVIGFRLKDETKTQDFVDALTLPLVSVSLGGVETILSHPATMSHAAVPEDVRNERGITFGLFRLSVGLEQPQELIADLNYALKEAFNESIIESITEQRFSS", "text": "FUNCTION: Catalyzes the transformation of cystathionine into homocysteine (PubMed:19035565). Can also catalyze, at low levels, the conversion of cystathionine into methionine and the conversion of methionine into methanethiol (PubMed:19035565). SIMILARITY: Belongs to the trans-sulfuration enzymes family."}
{"protein": "MSVSRLAASGLLLVSLLALALDGKPVEKWSPWLWPPRPRPPIPPLQQQKWLDPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWQRPLQPEVPSLMELHQERQKQGRMMHHDEDPGDAAEGPRRQKKEPGKPEGNGCFGKKIDRINAGFGCPKLPPSGGH", "text": "FUNCTION: pEKW peptides may serve as metalloproteinase inhibitors during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the victim. FUNCTION: [C-type natriuretic peptide]: Exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: In the C-terminal section; belongs to the natriuretic peptide family."}
{"protein": "MSGIDFKQKISFQRPFSKPIEAEEEYDIVRQFESDRGRIVNSAAIRRLQQKTQVFPLERNAAVRSRLTHSMEVQQVGRHIAKEILNRFKQDGRVDALGLTKLLDPFESIVEMACLMHDIGNPPFGHFGESAINNWFSQRLDPASCGSEPASNDRCQVSALRLHEGESDLNRLRSRIRHDLSHFEGNAQAIRLVHTLLKLNLTYAQVGCILKYTRPAYWASDIPASHNYLMKKPGFYLAEEAFVDRLRRELNMGEFDRFPLTYIMEAADDISYCVADLEDAVEKNIFTVEQLYQHLTQEWGEVTPGDLFDKTVASAFRKIAHGGARRSSEDQFFMYLRVFTVARLVPHAAQRFIDNLEAVYQGNFNQALLEDSSPAYQLLKIFKNVAFKHVFNHPEVEQLELQGYRVISGLLDIYSPLLAMPLADFTLLVQEDSHRAYPIETRLFHKLSTKHRLAYIEAIEGLQHLSPEQLAIREYYFRARLLQDYISGMTDLYAYDEYRRLMAAE", "text": "FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs. SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily."}
{"protein": "MVKETHRFETFTEEPIRLIGEEGEWLGDFPLDLEGEKLRRLYRDMLAARMLDERYTILIRTGKTSFIAPAAGHEAAQVAIAHAIRPGFDWVFPYYRDHGLALALGIPLKELLGQMLATKADPNKGRQMPEHPGSKALNFFTVASPIASHVPPAAGAAISMKLLRTGQVAVCTFGDGATSEGDWYAGINFAAVQGAPAVFIAENNFYAISVDYRHQTHSPTIADKAHAFGIPGYLVDGMDVLASYYVVKEAVERARRGEGPSLVELRVYRYGPHSSADDDSRYRPKEEVAFWRKKDPIPRFRRFLEARGLWNEEWEEDVREEIRAELERGLKEAEEAGPVPPEWMFEDVFAEKPWHLLRQEALLKEEL", "text": "FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). SIMILARITY: Belongs to the BCKDHA family."}
{"protein": "MSTTKRSVTTRPSTSSRNVPRGIWELARLHTRESWLCWYPSIWGACVAAGVSDTVLEPLAFARFLFGIWASVTATHCAFCTFKSVPFCFFVVPRYSSDYWHLDKHVQRCKVRPLPSGMISTPEALLAFVCWVPFTFAITWATLGPAVTVSFIPVWVLSVIYPFMKRLMPFPQVVLGAIIGGAVFPGWVGVTGDLDHLDQALPLFFATAAWVVYFDVFYATQDLPDDKKAGVKSLAVWMGPNVKILLAGLGILQIAFFAMTALRADLSLIFWILGIGVWAVSVPWHVLSLNLKDRHSGGSVFKANIKLGLYMTGVSLLELVLLRVHHAPMKVY", "text": "FUNCTION: Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria (PubMed:24684908). The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA (PubMed:24684908). 6-MSA is then converted to m-cresol by the decarboxylase yanB (PubMed:24684908). The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol (PubMed:24684908). Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation by yanG leads to 7-deacetoxyyanuthone A (PubMed:24684908). The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A (PubMed:24684908). O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E (PubMed:24684908). Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D (PubMed:24684908). Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E (PubMed:24684908). YanG is also involved in the synthesis of yanuthone X1 which does not have 6-methylsalicylic acid (6-MSA) as precursor (PubMed:24684908). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family."}
{"protein": "SQIKFKPSYIELAVVADHGMFTKYNSNINTIRIVHEMVNTVDGFFRTITSFGEWRERDIIPRSCIMASTISKHNPQCIINQPI", "text": "FUNCTION: This protein is a zinc protease from snake venom that is devoid of significant myotoxic and hemorrhagic activities. It hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen, without affecting the gamma-chains. It induces cell detachment and a apoptosis (anoikis) in endothelial cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I subfamily."}
{"protein": "MSQKQPQSPNQTLISITNDTESSSSVVSNDTTNKGWTGDNSPGIEALCAIYITYAVIISVGILGNAILIKVFFKTKSMQTVPNIFITSLALGDLLLLLTCVPVDATHYLAEGWLFGRIGCKVLSFIRLTSVGVSVFTLTILSADRYKAVVKPLERQPSNAILKTCAKAGCIWIMSMIFALPEAIFSNVHTLRDPNKNMTSEWCAFYPVSEKLLQEIHALLSFLVFYIIPLSIISVYYSLIARTLYKSTLNIPTEEQSHARKQVESRKRIAKTVLVLVALFALCWLPNHLLNLYHSFTHKAYEDSSAIHFIVTIFSRVLAFSNSCVNPFALYWLSKTFQKQFKAQLFCCKGELPEPPLAATPLNSLAVMGRVSGTENTHISEIGVASFIGRPMKKEENRV", "text": "FUNCTION: Role in sperm cell division, maturation, or function. The relative order of ligand affinity is GRP = neuromedin-C >> neuromedin- B. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MYEVIQKRKTKIINVLQSPELMRLIEDPSNLGISLHFPVSSLLKSNKCTPMPKLSTYSLASGGFKDWCADIPLDVPPEIDIIDFYWDVILCMESQFILDYNVPSKNKGNNQKSVAKLLKNKLVNDMKTTLKRLIYNENTKQYKNNNSHDGYNWRKLGSQYFILYLPLFTQELIWCKLNENYFHVVLPSLLNSRNVHDNHSTYINKDWLLALLELTSNLNQNFKFEYMKLRLYILRDDLINNGLDLLKNLNWVGGKLIKNEDREVLLNSTDLATDSISHLLGDENFVILEFEC", "text": "FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels (PubMed:15538383). Binds to ODC/SPE1 monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:18089576). SIMILARITY: Belongs to the ODC antizyme family."}
{"protein": "MFRWLNINKCMSKIIHPYVLKPNNCIHTNWLFKFATLKNENKIFPKKNLNNNILMQNIKVADDGNAICEQLLFSKYDLPYLLKIPVSDLRLIDTGNNNHNPTILIRKDVILLRTGFISCIIRYNETWLFEGSNSVVINAKDLISKNLKKQNNNKFKNCNNDEIVESLCRKRNCTDNGKENMKQINNDEKEELNYLNIINNFYRYNKGKAYFEFLCLDICMQLSIKEYENDLEGINYKIRDIILLQRKEENNELNMLTNKLLRDMMKIKNNLQKLSNLLNALRTNIEKILNNENDMKNMYLTYLNKNPYNNLKDCSDLEILLETHLQLTDELYGQLENVEEKITHYEELMRLNLDYNRNKFILLNAKISFSTLLFSISSVVTSLFGMNLKNFVEDSNYAFIIVSIFVSVWSIIGIYVTKNINTLLKFFDRYNFR", "text": "FUNCTION: Mitochondrial inner membrane magnesium transporter required for mitochondrial magnesium homeostasis (By similarity). Involved in the development of the sporozoite in the mosquito vector midgut (PubMed:26796412). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family."}
{"protein": "MSTQYSILFKQEHAHEDAIWSVGWGKNSNDGSELVISGSLDDLVKVWKWSDERLELQSTLEGHQLGVVSVDVSPSGNIMASSSLDAHIRLWDLESGKQIRAIDAGPVDAWSVAFSPDSQHLATGSHVGKVNIFGVETGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYEVQHASLAATLSGHGSWVLNVAFSPDDTHFVSSSSDKSVKVWDVSARTCVHTFLDHQDQVWGVKYNKNGSKIVSVADDQEIHVYDCPI", "text": "FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser- 5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. Also acts as a component of the SKI complex, a multiprotein complex that assists the RNA- degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the SKI8 family."}
{"protein": "MSSPGNSGVAIDSTVLKAIELGTRLFKSGEYLQAKRIFTNALRVCDSYSQEQIMRIRNAYQLDTARPDNKRLYHPRYIKILDNICACYEKLNDLKSCLDVSQRLLKLEPGNIKCYIRCTRTLIKLKDWKRAYKTCSRGLQLCNNDSNHLRQQKQFIKNNMVQKQDGKRSYIDPLEETKIAKKKKNNNVLESLPKKKIKGSTKKTDLVGNLPIEILPIIFQRFTTKELVTLSLVCNKWRDKILYHLDCFQEFNLAPINFKNFVKFMDFLQQNFTRTYRKYILSQVKVSSRITSEELRITQLLFSKMPKCINIERLILSMPTLTTTQIFKLMVRGGTDFFTRLLELSLMITYRPDKQHELEILQTCPLLKKIELIFVNSLVPIFDGNNSVGRDGSFNVMARHTNMQISTADNDEQGIVEEKVIYSELEKITLICDKKKIKNFPLCRALLRGQFPLLQKLTITGVTFPMNNQDIMNFQWLLNFPDLKELWIEDNDNCELSKFLQLLKFSNVWKNLEKLTFRENKLYPIVNLDEDQPVTNDDEVPSMLFYKENLQNLEKLDLMGTSISGSALTRLCEQEYLDGRKLRSLNIGNCPNIQFPNNHAHTARMILDVNAVLKRLSKLEEINLSHLSSLNDSTMKSFIINVPFLENLKRLDISHNFEITGISIYEFLKKFQMDHDNEAGGQPLAYLNIDGCSQVSHITVNMIRAQNLVTQVDCVYERDVWRKFGINSYSYS", "text": "FUNCTION: F-box protein component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). The SCF(DIA2) complex is specifically involved in the pheromone induced degradation of phosphorylated TEC1. The SCF(DIA2) complex binds to DNA replication origins. Involved in DNA replication, genome stability, and the control of cell cycle, probably through its association to replication origins to facilitate the ubiquitination of another origin- binding protein. Required for invasive growth and growth under alkaline conditions. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DIA2 family."}
{"protein": "MWGETFDDFENDEGEMAMAKQNLIAEPARADFTFAKLPLGIQPVDFMKTHFAETAGKSMQFRKGTTTLAFVYEPATPADKGGIIVAVDSRASSGEYISSKSVMKILDIGDRMVATMAGGAADCQFWTRIVAKYCTLYELREKTSITVSAASKYFANTLYGYRGQGLSVGSMVAGYDKKGPQIFKVDSEGDRCQLKVCSVGSGSLNAYGILDNHYKPKMTDDEARKLGLRAIMHATYRDSGSGGVCNLCHITPTEKIRLPPMDVSKLWYEFADELGRDITYNPVE", "text": "FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins (PubMed:27528192). This complex plays numerous essential roles within the cell by associating with different regulatory particles (By similarity). Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins (By similarity). The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MSTETDEILERLKKITLLEAYELVKQIENTFGVDATIALSASNTNPSILPSKADETVVEEKTEFDVIIQEVPSAKRINVIKTVRSLTTLGLKEAKDLIESVPKVVCEAVSKEVAEETKKLLEEAGASIIIK", "text": "FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family."}
{"protein": "MDSQRGIVEQAKSQSLNRQSSLYSLTLDEVQNHLGSSGKALGSMNLDELLKSVCSVEANQPSSMAVNGGAAAQEGLSRQGSLTLPRDLSKKTVDEVWKDIQQNKNGGSAHERRDKQPTLGEMTLEDLLLKAGVVTETIPGSNHDGPVGGGSAGSGAGLGQNITQVGPWIQYHQLPSMPQPQAFMPYPVSDMQAMVSQSSLMGGLSDTQTPGRKRVASGEVVEKTVERRQKRMIKNRESAARSRARKQAYTHELEIKVSRLEEENERLRKQKEVEKILPSVPPPDPKRQLRRTSSAPF", "text": "FUNCTION: Binds to the embryo specification element and the ABA- responsive element (ABRE) of the Dc3 gene promoter. Could participate in abscisic acid-regulated gene expression during seed development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. ABI5 subfamily."}
{"protein": "MSDIPSGALEADESRAVSLLSRVILPRPGEPLDVRKLYIEESTTNSRRAHAPTRTSLEIGPESEVSFATYFNAFPASYWRRWSTLDTVVLRVELTGTARVDVYRSKATGARITVGGAPVAGEGDGPAAVEFEIDLTPFEDGGWIWFDITTNTAVRVHSAGWYAPVPAPGRANVAVGIPTFNRPADCVNALAALTSDPLVDEVISAVIVSDQGTSKAKDHPGFADAAARLGDRLSIHNQPNLGGSGGYSRVMYEALKNTDCEQILFMDDDIRIEPDSILRALAMNRFAKSPILVGGQMLNLQEPSHLHVMGEVVDRANFMWTAAPNAEYDHDFAKFKLSDAEEPRTKLLHRRVDVDFNGWWMCMIPRQIAEELGQPLPLFIKWDDAEYGLRAGEHGYGTVTLPGAAIWHMAWSDKDDAIDWQAYFHLRNRLVVAALHWDGPVSGLIASHLKATIKHLLCLEYSTVAIQNKAMEDFLAGPENLFSILESAMPDVRKLRSQYPDAVVLPGATSLPPASDMRRKKIAIPVSKPAIAVNLARGVVHQLRSHDPETHVRPQINVATQDARWFSLCRVDGVTVTTADGRGVVYRQRDRAKMFALLRASLRQQARLARKFDRMRKVYRDALPMLTSTQKWESVLLTETPEKVGR", "text": "FUNCTION: Involved in the galactan polymerization of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacteria cell wall. Thus, successively transfers approximately 28 galactofuranosyl (Galf) residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl- galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha- GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and 1->6 links, forming a galactan domain with approximately 30 galactofuranosyl residues. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MVMPTVVSDRMGTIDFIDYTNNHVFSKCQTDSLNTVNNGSLKHDDYLHGLANGKLVAKQMIGDALRQRVESIDSEFCEPGDEDTFFVADLGEVYRQHLRWKLNLPRVKPFYAVKCHPDERLLQLLAALGTGFDCASKAEIEQVLRMGVDPSRIIYAQPCKTNSYLRYVAQQGVRQMTFDNADELRKIARLYPDAELFLRILTDDSSSLCRFSMKFGASLDSTDGLLGLARQLGLNVVGVSFHVGSGASDPTAFLKAVQDAHVVFQQAAAYGYSLKTLDVGGGFCSDDSFEQMANVLRAALDEYFPAHTGVNLIAEPGRYYASSAFTLACNIIARRTIQDGSAVSVSDSSSMSDDGSVNNGDARYMVYVNDGLYGNFSSIMFDHQHPVAKILRAGGRTMYNSVAAHESSAEDAIEYSIWGPTCDGIDRITESIRFREILDVGDWLYFEDMGAYTKCSATTFNGFSNEHDVIYVCSEPGAMALLGL", "text": "FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family."}
{"protein": "MKLLLVGIIPIALYAIFNYLFYTWLPTNYLFDKQVLQELVQETLKDHLDGNATAIMIDLTPKIQKKYPKIINDLNFDDWVYNNAGGAMGTMFILHASISEYLIFFGTAIGTEGHTGVHFADDYFTILTGEQRAAYPGALIPEVYLPGDQHHLPKGHVKQYAMPGESFALELAQGWIPAMLPFGFLDTLTSTMDFYTFYLTAYYTGKDMIKNLLIGKF", "text": "FUNCTION: C-8 sterol isomerase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4- dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3- beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron- containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C- methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl- methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen- 3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ERG2 family."}
{"protein": "MWLPALVLATLAASAAWAGHLSSPPLVDTLHGKVLGKFVSLEGFAQPVAVFLGIPFAKPPLGPLRFTLPQPAEPWNFVKNATSYPPMFTQDPKAGQLISELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSPGNWGHLDQLAALHWVQDNIASFGGNPGSVTIFGGSVGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEVGLRLVRLRLDTPTSLALCS", "text": "FUNCTION: Has no esterase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "MEEGKMDENEWGYHGEGNKSLVVAHAQRCVVLRFLKFPPNRKKTSEEIFQHLQNIVDFGKNVMKEFLGENYVHYGEVVQLPLEFVKQLCLKIQSERPESRCDKDLDTLSGYAMCLPNLTRLQTYRFAEHRPILCVEIKPKCGFIPFSSDVTHEMKHKVCRYCMHQHLKVATGKWKQISKYCPLDLYSGNKQRMHFALKSLLQEAQNNLKIFKNGELIYGCKDARSPVADWSELAHHLKPFFFPSNGLASGPHCTRAVIRELVHVITRVLLSGSDKGRAGTLSPGLGPQGPRVCEASPFSRSLRCQGKNTPERSGLPKGCLLYKTLQVQMLDLLDIEGLYPLYNRVERYLEEFPEERKTLQIDGPYDEAFYQKLLDLSTEDDGTVAFALTKVQQYRVAMTAKDCSIMIALSPCLQDASSDQRPVVPSSRSRFAFSVSVLDLDLKPYESIPHQYKLDGKIVNYYSKTVRAKDNAVMSTRFKESEDCTLVLHKV", "text": "FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many processes such as mRNA export, non-homologous end-joining, endocytosis, ion channel regulation. It also protects cells from TNF-alpha-induced apoptosis. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the IPK1 type 2 family."}
{"protein": "MSDSGHSQPNVFIPGRNRRRRWMDQGPPGHLNLSEPGREKDPMLRDRDQDRWEGNEEGYGYTIQKTPIILAKPTSDRTKAATPAAPPPMEKPIVLMKAREDGKPAAPAEGATAPPPTAVAKVEKEGQRPTQPVYQIQNRGMGAAASASGNVDPVVGQAKLLPPQKMKHSIKLVDEYMNWCDSAIEFLLDQTDVLVVGILGLQGTGKSTLMSLLSANSPDDDQRSYVFRMQSQEVRERAGNQTSGIDFFISQERIIFLDTQPILSPAILDHLINNDRKLPPEYNLPHTYVEMQSLQIAAFLFTVCHVVIVVQDWFTDFNLYRFLQTAEMLKPSTPSPSHESSGSSGSDEGIEYYPHVVFVQNKAKREDYCPRTLKQMHTVIDKLMLHSHLRYKGTLSMLDCNIFPGLPYDFIESEVNLFLIPTMESDVDETISRAGTSGIPLFSLLPAYKGHPSFHSLISRLRSQIMSMSRPQLSHTILTEKNWFHYAARIWDGVKKSSALSEYSRLLG", "text": "FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with smg1 and smg8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between smg1 and smg8 (By similarity). SIMILARITY: Belongs to the SMG9 family."}
{"protein": "MGVEIQSPQEQSSYTVEQLVALNPFNPEILPDLENYVNVTSQTYSLEVNLCLLRLYQFEPERMNTHIVARILVKALMAMPTPDFSLCLFLIPERVQMEEQFKSLIVLSHYLETGRFQQFWDEAAKNRHILEAVPGFEQAIQAYASHLLSLSYQKVPRSVLAEAVNMDGASLDKFIEQQVTNSGWIVEKEGGSIVLPQNEFNHPELKKNTGENVPLEHIARIFPILG", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit K family."}
{"protein": "MSSSKKIVILYGSETGNAHDFATILSHRLHRWHFSHTFCSIGDYDPQDILKCRYLFIICSTTGQGELPRNVNALKGERPVTFWSFLKRKNLPSNLLNHIQTAMLGLGDSSYPKFNYGIRKLHQRIVTQLGANELFDRLEADDQAMAGSNKGTGLGIESVYFEYEKKVLSFLLSKYPNRKVNGQIIKREELDPEVYLEPASYLQLSDEHANEKFTSTKVIFEGDESLKVGRVNINKRITSEGHFQDVRQFKFSNVDKIQENYEPGDTVTIYPCNTDEDVSRFLANQSHWLEIADKPLNFTSGVPNDLKDGGLVRPMTLRNLLKYHCDFMSIPRTSFFLKIWTFATDVTKMERGQEQLNDQREKLRQFATDQDMQDLYDYCNRPRRSILEVLEDFISVKLPWKYVLDYLPIIKPRYYSISSGPGDPNIELTVAIVKYKTILRKIRRGICTNYIARLQEGEQIRYKLQNNHIIKKEFLNKPMILVGPGVGLAPLLSVVKAEISKDIKLLFGCRYKDKDYIYKDMLEDWFRKGKIALHSSFSRDEENSPGVKYVQDYLWRLGEEITNLVVNKDAVFFLCGSSGKMPIQVRLTFIEMLKKWGNFSDEETAKKYLKEMEKSDRYIQETW", "text": "FUNCTION: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery (PubMed:20802492). Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery (PubMed:20802492, PubMed:21902732). In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins (PubMed:20802492). Positively controls H(2)O(2)-induced cell death (PubMed:19194512). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Note=Relocalizes to mitochondria after H(2)O(2) exposure. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family. SIMILARITY: In the N-terminal section; belongs to the flavodoxin family."}
{"protein": "MAALLRAVRRFRGKAVWERPLHGLWCCSGQEDPKRWVGSSSPISKEKLPNAETEKFWMFYRFDAIRTFGFLSRLKLAQTALTVVALPPGYYLYSQGLLTLNTVCLMSGISGFALTMLCWMSYFLRRLVGILYLNESGTMLRVAHLNFWGWRQDTYCPMADVIPLTETKDRPQEMFVRIQRYSGKQTFYVTLRYGRILDRERFTQVFGVHQMLK", "text": "FUNCTION: As part of the MCIA complex, required for efficient assembly of the mitochondrial complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM186 family."}
{"protein": "MANTKKSAINQVVTRDYTIHMHKRLYGVSFKKRAPRAIKEIVAFAQKHMQTKEVRVDPSLNKEVWKRGIRNVPHRLRLRLSRKRSDEDDKALYTYVQAVDVANPKMETTVVEE", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family."}
{"protein": "MAPITFRKSYTIVPAEPTWSGRFPLAEWDQVGTITHIPTLYFYDKPSESFQGNVVEILKTSLSRVLVHFYPMAGRLRWLPRGRFELNCNAEGVEFIEAESEGKLSDFKDFSPTPEFENLMPQVNYKNPIETIPLFLAQVTKFKCGGISLSVNVSHAIVDGQSALHLISEWGRLARGEPLETVPFLDRKILWAGEPLPPFVSPPKFDHKEFDQPPFLIGETDNVEERKKKTIVVMLPLSTSQLQKLRSKANGSKHSDPAKGFTRYETVTGHVWRCACKARGHSPEQPTALGICIDTRSRMEPPLPRGYFGNATLDVVAASTSGELISNELGFAASLISKAIKNVTNEYVMIGIEYLKNQKDLKKFQDLHALGSTEGPFYGNPNLGVVSWLTLPMYGLDFGWGKEFYTGPGTHDFDGDSLILPDQNEDGSVILATCLQVAHMEAFKKHFYEDI", "text": "FUNCTION: Hydroxycinnamoyl transferase involved in the conjugation of feruloyl CoA to spermidine (PubMed:19077165, PubMed:19762055, PubMed:33519864). Catalyzes the three conjugating steps required for the biosynthesis of N(1),N(4),N(8)-triferuloyl-spermidine (PubMed:19077165, PubMed:33519864). Spermidine is the only acceptor substrate while feruloyl CoA > caffeoyl CoA > coumaroyl CoA > cinnamoyl CoA >> sinapoyl CoA are efficient acyl donors. No activity with hydroxyferuloyl CoA (PubMed:19077165). Required for the biosynthesis of these conjugated spermidine derivatives, specifically in anther tapetum (PubMed:22912643). SIMILARITY: Belongs to the plant acyltransferase family."}
{"protein": "MDRRRFIKGSMAMAAVCGTSGIASLFSQAAFAADSDIADGQTQRFDFSILQSMAHDLAQTAWRGAPRPLPDTLATMTPQAYNSIQYDAEKSLWHNVENRQLDAQFFHMGMGFRRRVRMFSVDPATHLAREIHFRPELFKYNDAGVDTKQLEGQSDLGFAGFRVFKAPELARRDVVSFLGASYFRAVDDTYQYGLSARGLAIDTYTDSKEEFPDFTAFWFDTVKPGATTFTVYALLDSASITGAYKFTIHCEKSQVIMDVENHLYARKDIKQLGIAPMTSMFSCGTNERRMCDTIHPQIHDSDRLSMWRGNGEWICRPLNNPQKLQFNAYTDNNPKGFGLLQLDRDFSHYQDIMGWYNKRPSLWVEPRNKWGKGTIGLMEIPTTGETLDNIVCFWQPEKAVKAGDEFAFQYRLYWSAQPPVHCPLARVMATRTGMGGFSEGWAPGEHYPEKWARRFAVDFVGGDLKAAAPKGIEPVITLSSGEAKQIEILYIEPIDGYRIQFDWYPTSDSTDPVDMRMYLRCQGDAISETWLYQYFPPAPDKRQYVDDRVMS", "text": "FUNCTION: Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs). FUNCTION: Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs). SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the OpgD/OpgG family. SIMILARITY: Belongs to the OpgD/OpgG family."}
{"protein": "MSESPMFAANGMPKVNQGAEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDDRVLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLEKPRTTVGWKGLINDPDVNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADLVSFGAIGARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHSHHFMGVTKHGVAAITTTKGNEHCFVILRGGKKGTNYDAKSVAEAKAQLPAGSNGLMIDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEGNQGIPAEGKAGLKYGVSITDACIGWETTEDVLRKLAAAVRQRREVNKK", "text": "FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). SIMILARITY: Belongs to the class-I DAHP synthase family."}
{"protein": "MIETDILVVGAGPSGSLAAKEAALHGADVILIDRKSEIGSPKRCAEGVSKDGLAQLGIKPDPRWIARDLYGVRLVSPNNTSVWMDNNTIKIPEAGYILERKVFDKHMAMDAARAGAKIMIKTNATSLKRVDDGIIVSTNHMGKDIDIHAKIVIAADGPESRIGRWAGLECNTEFKYMESCIQFEMAGVNMENNRDIALFFGSVAPGGYVWIFPKGDDIANVGIGVLKNKTNKTAYEHLMEFIKTCPETKDAQPVEINVGGDPVGGIIKDRIGDNILVVGDAAGFVNSLTGGGINSALESGVYAGIVAAQAIKDGDYSKNNLKEYVSLTDEHIGKHYKKYNKAKEYLLSLEDEELDEIAEEFAKADFEEVNPRTLIKMLIKVSPKALVKLGKLF", "text": "FUNCTION: Is involved in the reduction of 2,3- digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3- diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di- O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains. SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL reductase subfamily."}
{"protein": "QTFQYSRGWTN", "text": "FUNCTION: Cardioactive peptide. Corazonin is probably involved in the physiological regulation of the heart beat. FUNCTION: Cardioactive peptide. Corazonin is probably involved in the physiological regulation of the heart beat (By similarity). FUNCTION: Cardioactive peptide. Corazonin is probably involved in the physiological regulation of the heart beat (By similarity). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the corazonin family. SIMILARITY: Belongs to the corazonin family."}
{"protein": "MNGQRYRETPLDIERLRRLNRATVERYMAMKGAERLQRHSLFVEDGCAGNWTTESGEPLVFRGHESLRRLAEWLERCFPDWEWHNVRIFETEDPNHFWVECDGRGKALVPGYPQGYCENHYIHSFELENGRIKRNREFMNPIQKLRALGIAVPQIKRDGIPT", "text": "FUNCTION: Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule. PhzA1 (operon phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during planktonic growth. SIMILARITY: Belongs to the PhzA/PhzB family."}
{"protein": "MAGVPVGALLPLLVGVCGAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWIPREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESNNDKERFIRESQFAKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGYEERNGECQACKIGYYKALSTDVACAKCPPHSYSIWEGSTSCTCDRGFFRAENDAASMPCTRPPSAPQNLISNVNETSVNLEWSAPQNKGGRDDISYNVVCKRCGAGEPSHCRSCGSGVHFSPQQNGLKTTKVSITDLLAHTNYTFEVWAVNGVSKHNPSQDQAVSVTVTTNQAAPSPIALIQAKEITRHSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVKTASRNTDIKGLNPLTSYVFHVRARTAAGYGDFSGPFEFTTNTVPSPIIGDGTNPTVLLVSVAGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGSESSRPSTALLDPSSPEFSAVVSVSDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGITAITHQNKILSSVQAMRSQMQQMHGRMVPV", "text": "FUNCTION: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI- anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Early endosome Note=Clustered upon activation and targeted to early endosome. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily."}
{"protein": "MNIYVWLFAIIALSFSALVGLRLSFKKGTANVLVGESIITVVAGTLIVVISQKYNLAFADTIALAIFICGVVGAFAFCKVIGGDNEKAKQPN", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.thermoautotrophicum MTH1250."}
{"protein": "MPTNLFFNAHHSPVGAFASFTLGFPGKSGGLDLELARPPRQNVLIGVESLHESGLYHVLPFLETAEEDESKRYDIENPDPNPQKPNILIPFAKEEIQREFHVATDTWKAGDLTFTIYSPVKAVPNPETADEEELKLALVPAVIVEMTIDNTNGTRARRAFFGFEGTDPYTSMRRIDDTCPQLRGVGQGRILSIVSKDEGVRSALHFSMEDILTAQLEENWTFGLGKVGALIVDVPAGEKKTYQFAVCFYRGGYVTAGMDASYFYTRFFQNIEEVGLYALEQAEVLKEQSFRSNKLIEKEWLSDDQTFMMAHAIRSYYGNTQLLEHEGKPIWVVNEGEYRMMNTFDLTVDQLFFELKLNPWTVKNVLDLYVERYSYEDRVRFPGEETEYPSGISFTHDMGVANTFSRPHYSSYELYGISGCFSHMTHEQLVNWVLCAAVYIEQTKDWAWRDKRLAILEQCLESMVRRDHPDPEQRNGVMGLDSTRTMGGAEITTYDSLDVSLGQARNNLYLAGKCWAAYVALEKLFRDVGKEELAALAGEQAEKCAATIVSHVTDDGYIPAIMGEGNDSKIIPAIEGLVFPYFTNCHEALDENGRFGAYIQALRNHLQYVLREGICLFPDGGWKISSTSNNSWLSKIYLCQFIARHILGWEWDEQGKRADAAHVAWLTHPTLSIWSWSDQIIAGEITGSKYYPRGVTSILWLEEGE", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 52 family."}
{"protein": "MLQFSFQNCKTHTCYMNTSVNEHLDQDESFLRILIDTRKKIRSSYFKPQTFDEFVHCLARVRAMKRLVSICSNFDEEDNWNGVWNTLVVDGDSHASAMIDYEGLLDKCSLSRNLLELINDYAEYTTQVLPFRKIPSSDNLDSSLNLTVASPKSNLYYRYSSESPKYAKILDCPDEILQLIFSYCYDASYIEKLPFAFSYRKQRHTLIHDLPNTCLRFKKILSPRNVSFWKRLLKVHKKNPNSAVTCSESINTSAVAKFTDIPTIIPIFLDPSYQSYAAKTIHSDTSSLASSIIQTGDGTQSCDESTYIELACNLVGRCVLCNRIPKLTKFKDCITSFYRPSVATNICDQCLEAIIDFYEPVSRYKFDVMKDRLGVGYISRPGQKFPSWLSEHVQLARDEEKAFKSIYHSQGEFARSLFRLFRAQLAELCEQ", "text": "FUNCTION: Expression is induced during oxidative stress. Plays an essential, SCF-independent, role in the stress response to hydrogen peroxide for survival, by negatively regulating ergosterol synthesis via direct binding to the squalene synthase erg9. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum. Note=Associated with vesicle-like and endoplasmic reticulum (excluding a nuclear rim) structures."}
{"protein": "MELPLLALLSLGLVCQGGQGLVPPNELKQLSAAGSKYIDAEVENAINGVKQMKTLMDKTSKEHQAMLHTLEETKKKKEEAVKLALEKEKQLAEKQEVCNETMLSLWEECKPCLKHTCMRVYSKMCHSGSGLVGRQLEEFLNRSSPFSIWVNGERIDDLLDREQRQERRFEDLEERFGLMEDGVEDIFQDSTQLYGPAFPFFRTPPFGGFREAFVPPVQRVHLVPRRRLSRELHPFFQHPMHGFHRLFQPLFEMTQHMLDGGHGAWEHPLGGFATESRNFSTDRMVCREIRRNSAGCLRMRDECEKCREILAVDCSQTDPVQSQLREQFEDALRLAERFTRRYDDLLSAFQAEMLNTSSLLDQLNRQFGWVSRLGNLTQGNDGFLQVTTVFSKTPNLEDPSAPADTQVTVQLFDSEPLSLTVPGDISWDDPRFMEIVAEQALQHYKQNNTIE", "text": "FUNCTION: Functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Modulates NF-kappa-B transcriptional activity. Promotes apoptosis when in the nucleus. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation (By similarity). SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle, chromaffin granule Nucleus Cytoplasm Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytosol Endoplasmic reticulum Note=Present in chromaffin granules. Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis (By similarity). SIMILARITY: Belongs to the clusterin family."}
{"protein": "MLRLVSWNINGIRSPLQGVRCEEPSSCSAMAMGRILDKLDADIVCLQETKVTRDVLTEPLAIIEGYNSYFSFSRNRSGYSGVATFCKDSATPVAAEEGLSGLLSTQNGDVGCYGNMDDFTQEELRALDSEGRALLTQHKICTWEGKEKTLTLINVYCPHADPGKPERLTFKMRFYRLLQIRAEALLAAGSHVIILGDLNTAHRPIDHWDAVNMECFEEDPGRKWMDGLLSNLGCESGSHMGPFIDSYRCFQPKQKGAFTCWSTVSGARHLNYGSRLDYVLGDRTLVIDTFQSSFLLPEVMGSDHCPVGAVLSVSSVPAKQCPPLCTCFLPEFAGTQLKILRFLVHFKQDPVFKQSALQPSNQTQVHMRKNKARVRSTRSRPSKTGSSRGQKNLMSYFQPSSSGPQTSNLDLPSLGTLITPKTSEEDVMANVVEGQTKASEAKDEKEIRTSFWKSLLGGPSPMPLCGGHREPCVMRTVKKPGPNLGRHFYMCARPQGPPTDPSSRCNFFLWSRPS", "text": "FUNCTION: Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents (By similarity). Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'- hydroxyl ends (By similarity). Also displays double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially (By similarity). Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway (By similarity). Plays a role in reversing blocked 3' DNA ends, problematic lesions that preclude DNA synthesis (By similarity). Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes (By similarity). Required for proper cell cycle progression during proliferation of peripheral lymphocytes (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Mitochondrion Note=Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family."}
{"protein": "MSSNFRHQLLSLSLLVGIAAPWAAFAQAPISSVGSGSVEDRVTQLERISNAHSQLLTQLQQQLSDNQSDIDSLRGQIQENQYQLNQVVERQKQILLQIDSLSSGGAAAQSTSGDQSGAAASTTPTADAGTANAGAPVKSGNANTDYNAAIALVQDKSRQDDAMVAFQNFIKNYPDSTYLPNANYWLGQLNYNKGKKDDAAYYFASVVKNYPKSPKAADAMFKVGVIMQDKGDTAKAKAVYQQVISKYPGTDGAKQAQKRLNAM", "text": "FUNCTION: Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division. Promotes physical and functional coordination of the PBP1B-LpoB and Tol machines, and regulates PBP1B activity in response to Tol energy state. SUBCELLULAR LOCATION: Periplasm Note=Targeting to the Sec-translocase for transport across the inner membrane is SecB-dependent (PubMed:16352602). Localizes to the septum concurrent with PBP1B-LpoB and Tol at the onset of constriction (PubMed:25951518). Localization is dependent on divisome assembly and requires ongoing septal peptidoglycan synthesis (PubMed:25951518). SIMILARITY: Belongs to the CpoB family."}
{"protein": "MEVTNLIEKCTKHSKDFATEVKKLWNDELSSESGLSRKTRNVIRNILRDITKSLTTDKKSKCFRILERSTINGEQIKDVYKTIFNNGVDVESRINTTGKYVLFTVMTYVAAELRLIKSDEIFALLSRFFNMICDIHRKYGCGNMFVGIPAALIILLEIDHINKLFSVFSTRYDAKAYLYTEYFLFLNINHYLLSGSDLFINVAYGAVSFSSPISVPDYIMEALTFKACDHIMKSGDLKYTYAFTKKVKDLFNTKSDSIYQYVRLHEMSYDGVSEDTDDDDEVFAILNLSIDSSVDRYRNRVLLLTPEVASLRKEYSDVEPDYKYLMDEEVPAYDKHLPKPITNTGIEEPHATGGDEDQPIKVVHPPNNDKDDAIKPYNPLEDPNYVPTITRTAIGIADYQLVINKLIEWLDKCEEECGNSGEFKTELEEAKRKLTELNAELSDKLSKIRTLERDSVYKTERIDRLTKEIKEHRDIQNGTDDGSDLLEIDKKTIRELRESLDREREMRSELEKELDTIRNGKVDGSCQRELELSRMWLKQRDDDLRAEIDKRRNVEWELSRLRRDIKECDKYKEDLDKAKTTISNYVSKISTLESEIAKYQQDRDTLSVVRRELEEERRRVRDLESRLDECTRNQEDTQEVDALRSRIRELENKLTDCIESGGGNLTEISRLQSKISDLERQLSECRENATEISRLQSRISDLERQLNDCRRNNETNAETERDATS", "text": "FUNCTION: Structural protein that forms a matrix surrounding the mature virion (MV) through interaction with protein A26. Presence of protein A25 in the virion structurally prevents direct virus-cell fusion mechanism. SUBCELLULAR LOCATION: Virion. Note=Present above the membrane of mature virions (MV). SIMILARITY: Belongs to the poxviridae A25 protein family."}
{"protein": "MELSYQALRVASQNREAEELRTEARRKNLLILIMHYLLQEGYMDSANSLEQETKISLRRFDVCDNVDLETILMEYESYYYIKFQKYPKITKKALDHDSRVQSKPRSAGKLRRAGSNSTQGLPRIAQQTVLHRPVSGSYFRTHAHQKALSRENSKQENGGNSPREASEIGLNVSAISKTSGEGGQTRRRQVIDFRSMIQDTIKGASQEIALNSLNCNPDPSERLIKPVGAFIGGNSEMRELAAVISRDIYLQNPNVRWDDIIGLDAAKRLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECNTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTGPGGEHEGSRRMKTELLVQMDGLARSDDLVFVLAASNLPWELDYAMLRRLEKRILVDLPSKEARQAMIQHWLPPVSNSSGVELRTDLDYSTLGAETDGYSGSDIRLVCKEAAMRPVRKIFDALENHHSEHKNLPVISLDTVTTSDFLEVLAHTKPSAKSLAEKYAAWQKEFESV", "text": "FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=Localizes within the cytoplasm, partially overlapping with microtubules in interphase and to the mitotic spindle and spindle poles during mitosis. SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily. A-like 2 sub-subfamily."}
{"protein": "MASPVTVLENPIPKSGQHLLFFLTSKQQLALEQRPIESSLGYSAYVDHGVSQGVIVNPSSIAAAMRSSLITVYGITKPGTDKQYISVISPTYNLIANRQNQPIETTQKALAACSDNDRNNWVYYLNLPQGTAQYAIYELNIQDSTSAPTVYSGPTPSGNSNLAAVYFSPNKDRFIIFSNTDTRHYLYWVNSTLQSANRIAGTGSVMSASPLAATTITNVQTRSMTIFLYYMDVNTLLNRIVGKVTDNEIHWYANQVVEGAPPMKVDTLLTGVVVEEKWNCLYYIPDGDTEFRAFNDTIRDSFFDEPREG", "text": "FUNCTION: May participate in wall plasticization and/or intussusception or in cell wall turnover. SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral membrane protein."}
{"protein": "MRAPGAGTASVASLALLWFLGLPWTWSAAAAFCVYVGGGGWRFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGDTIPCIFQAVARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGRYVPLDERVHARICAGDFSL", "text": "FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane (PubMed:7954810, PubMed:9786857, PubMed:9671728, PubMed:10471110, PubMed:12235169, PubMed:11970897, PubMed:15699031, PubMed:28178239, PubMed:24858472, PubMed:19527715) (Probable). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl- CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake (PubMed:10593920, PubMed:12235169, PubMed:12937175). May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation (PubMed:14991074, PubMed:15897321). Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis (PubMed:12235169). May be involved in regulation of cholesterol metabolism (PubMed:12235169). Probably involved in fatty acid transport across the blood barrier (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Mitochondrion outer membrane Endomembrane system; Single-pass membrane protein Cytoplasm Note=Plasma membrane and intracellular membranes, at least in adipocytes (PubMed:10593920, PubMed:11970897, PubMed:28178239). In adipocytes, but not myocytes, insulin via the mTORC1 signaling pathway induces a rapid translocation of SLC27A1 from intracellular compartments to the plasma membrane, paralleled by increased LCFA uptake (PubMed:11970897, PubMed:28178239). Insulin-dependent translocation from the cytoplasm to the cell membrane is regulated by EPRS1 (PubMed:11970897, PubMed:28178239). Predominantly cytoplasmic in myocytes (PubMed:15897321). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MDPPGYLLFLLLLPVAASQTSAGSCSGCGTLSLPLLAGLVAADAVMSLLIVGVVFVCMRPHGRPAQEDGRVYINMPGRG", "text": "FUNCTION: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain- related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilization and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR- induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein. SIMILARITY: Belongs to the DAP10 family."}
{"protein": "MTITDLVLILFIAALLAYALYDQFIMPRRNGPTLLSIALLHRGRVDSVIFVGLVAILIYNNVTSHGAQMTTWLLSALALMGFYIFWIRTPRIIFKQRGFFFANVWIEYNRIKEMNLSEDGVLVMQLEQRRLLIRVRNIDDLEKIYKLLIENQ", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0266 family."}
{"protein": "MLLLHYFNLSHFQVNDHFYPHMRNFLYGETAFYVADTINMMFYIWVLFSAQQFHFNFTLVSGTQYVIHFFDNLAIIVMRLHSLLGFTDDFDIGSNVVFNGAMTFSVYCIVAAMCSLPFSILERCFATRYLKDYEANSRAYISYALVFLLNFIGIIGAILLQNKNNTIFVVAFLMILNLFALLTNQFLRTWNLKKYEECHSNVSIRFQRGGKYSLAKRFQISENIKSLHMLNFIILYMGFMNVCLVISVLFSSFDISPERQAICSLALDASIFFYSFAIPQIMTCFCHKWKVQTNTFRIRIGCLRTGKVNLEPLRDTFGGDMRGSVSMNRYFDQLQDSWENA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein sre family."}
{"protein": "MKKTLLAAGAVVALSTTFAAGAAENDKPQYLSDWWHQSVNVVGSYHTRFGPQIRNDTYLEYEAFAKKDWFDFYGYIDAPVFFGGNSTAKGIWNKGSPLFMEIEPRFSIDKLTNTDLSFGPFKEWYFANNYIYDMGRNDSQEQSTWYMGLGTDIDTGLPMSLSLNVYAKYQWQNYGASNENEWDGYRFKVKYFVPLTDLWGGSLSYIGFTNFDWGSDLGDDNFYDLNGKHARTSNSIASSHILALNYAHWHYSIVARYFHNGGQWADDAKLNFGDGPFSVRSTGWGGYFVVGYNF", "text": "FUNCTION: Functions as substrate-specific channel for nucleosides and deoxynucleosides. Functions also in albicidin uptake and as receptor for colicin K. Is also a receptor for several Tsx-specific bacteriophages. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family."}
{"protein": "MAVLRTMKLKERLVISLGATLVLLTLLLIVDVQMDFGVANRHLLQQQHQKIRLGNDYDGGTGGGGMLHEFKRKFLQKSNASGSKEASTQAGASQSGGATSGQDAAAGASGGAAGPGTSRSTSTRKPTPHDRYADLQKHLLSDEYSHVIVDNAPDVSRDNPTLAEMLHRKASANASNLERFQLRITKKELYGEQDTLVDAVLRDMIKLPIQHVVQKEGGTQLKLIIEYPNDIKALMKPMRFPREQQTLPNHFYFTDYERHNAEIAAFHLDRILGFRRAMPVAGRTLNITTEIYQLAEENLLKTFFVSPSLNLCFHGKCSYYCDTSHAICGNPDMLEGSFAAFLPNFESGNRKLWRHPWRRSYHKRKKAQWETDANYCALVRDIPPYDDGRRLYDLMDMAVFDFLTGNMDRHHYETFKVYGNETFPLHLDHGRGFGRPFHDELSILAPVLQCCLIRKSTLVKLLDFHNGPKPLSQLMSESLSQDPVSPVLWQPHLEALDRRTGIILQSIRDCIKRNPPGDVDGSETDVSS", "text": "FUNCTION: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Secreted Note=Resides in the Golgi apparatus membrane and is secreted following propeptide cleavage. SIMILARITY: Belongs to the FAM20 family."}
{"protein": "MEMRGKITKINENGLGVLGNILVPFAYPGDEVEVTETRERFGKIIARDFKLMTPSPLRIPGKCSHFGKCGGCLWQGLRYREQLKLKEEIFKRITGIEAEIKGSPRIWYFRNISNFIITVNGIGFKEFGMPKTVVNIRECPIFSERTPKYLKALKDFLRESNLKPWNWREGDVHYLQVREGKFTGEVMVNIIAHVPLNYREALMEAFNFADSIYWSLKADKKDDPRGFPTLVLGNEVIREKVEGITYLIHPSVFFQTNSYALPLLLKSVEKFCEGSKVLDLYSGIGTLSLYLAKRGFEVTGVEVNGTSVEMAKRSAEINSINATFIQGKAEDAELEGYETLIVDPPRKGLKEFSRRIVKKGPNTLIYVSCNPLRFILDYRNYLSEAYKVDDALLIDMFPHTPHIEAVIKLVRR", "text": "FUNCTION: Catalyzes the formation of 5-methyl-uridine at position equivalent to 747 (m5U747) in 23S rRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family."}
{"protein": "MGDLPGSGSTAQPRDAAVTGTGGNSTAGGGSSVGSTAVDRPPSPARLSHTSEKHPKVTLTELNMLRRHRELCDVVLNVGGRKIFAHRVILSACSSYFCAMFTGELEESRQTEVTIRDIDENAMELLIDFCYTAHIMVEESNVQTLLPAACLLQLVEIQDICCEFLKRQLDPTNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFLLLPVGQLVDIICSDELNVRSEEQVFNAVMSWLKYNVAERRQHLAQVLQHVRLPLLSPKFLVGTVGSDLLVRSDEACRDLVDEAKNYLLLPQERPLMQGPRTRPRKPTRRGEVLFAVGGWCSGDAIASVERFDPQTNDWKMVAPMSKRRCGVGVAVLNDLLYAVGGHDGQSYLNSIERYDPQTNQWSCDVAPTTSCRTSVGVAVLDGFLYAVGGQDGVQCLNHVERYDPKENKWSKVAPMTTRRLGVAVAVLGGFLYAIGGSDGQCPLNTVERYDPRHNKWVAVSPMSTRRKHLGCAVFNNYIYAVGGRDDCMELSSAERYNPLTNTWSPIVAMTSRRSGVGLAVVNGQLYAVGGFDGSAYLKTIEVYDPETNQWRLCGCMNYRRLGGGVGVMRAPQTENYMWCENSFKQPNS", "text": "FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin- protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May have a role in synapse differentiation and growth (By similarity)."}
{"protein": "MQITIKKLQDLLSSVQRKKIQTLKLKQGKFELLLNKTYKKVNQEIIPSQKSAVLQNSPSTIIKSINNTKKIFCVNEDRTEYATIVSPMVGTFYHSPAPGEKIFVQVGDEVKFNQTVCIIEAMKLMNEIEAEIEGKIIEILVKDGDIVDCGQALMKVET", "text": "FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MEQIRRYLQLERFQQHDFLYPXFFQEYIYVFAHGRGFSRSIWSENENTGYDNKSSLRVMKRLITRMYQQNNFIILPNDFNKKNPFLAKKKFFYSQIIAEGFAFIVEIPFSLRFISYLEGKKKIVKSQNLRSIHSIFPFLEDNFSHLNFVLDILILHPVHVEILVQILRYWVKDASSLHLLRFFLNKYWNSLITPNKASSSLSKKNKRLFVFLYNSHVGGYESSFVFIRNQSSHLGSTPFGVLLERIYFYGKIERLVNVFVKVKDFRTNLWFVKEPYIHYIRYQRKWILASKGTFLFVKKWKCYLIIFWQWHFSLWFYPRRIYINQLSNHYFEFLGYLSNLRMTPSVVRSQSLENTFIINNAIKKIDNFVPIISMIASLAKAKFCNVFGHPISKPVRADLSDSNIIDQFGCICRKFFHYYSGSSKKKSLYRIKYILRLACARTLARKHKSTVRTFLKRLGSELLEEFLLSEEDVLFLTFPKASSSLQGVYRSRIWYLDIIYINDLVDHKYKL", "text": "FUNCTION: Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the intron maturase 2 family. MatK subfamily."}
{"protein": "MARLPGHPEVPGAEPGSAVRGGRGGRGARARHVIINVGGCRVRLAWAALARCPLARLERLRACRGHDELLRVCDDYDVSRDEFFFDRSPCAFRAIVALLRAGKLRLLRGPCALAFRDELAYWGIDEARLERCCLRRLRRREEEAAEARATPPARGPQTSPGRALGSGRLERGRRRLRDVVENPHSGLAGKLFAYVSVAFVAVTAVGLCLSTMPDVRAEEERGECSTKCRNLFVLETVCVAWFSFEFLLRSLQAESKCAFLRTPLAIIDILAILPFYVSLLAGLAAGPTGSKMLERAGLVLRLLRALRVLYVMRLARHSLGLRSLGLTVRRCAREFGLLLLFLCVAMALFAPLVHLAERELGAHRDFSSVPASYWWAVISMTTVGYGDMVPRSLPGQVVALSSILSGILLMAFPVTSIFHTFSRSYSELKEQQQRAASPEPVLREDSTRDDSTRSASATEDSSQDPETAGAAGSLPGPVGP", "text": "FUNCTION: Potassium channel subunit. Modulates channel activity by shifting the threshold and the half-maximal activation to more negative values (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. G (TC 1.A.1.2) subfamily. Kv6.2/KCNG2 sub-subfamily."}
{"protein": "MLKLLRNNGINKLKSNLIRNYSTKQSIFQALDTFPKRHIGPNENEINEMLKSINTSKLSKKNPNSLEQLIEYTIPKDIRLNRELNIEENKVIGENQLLKDLKKIAEKNKVYRSFIGMGYYGTITPHVIQRNILENPGWYTPYTPYQAEISQGRLESLLNFQTMVSEFTGLPMSNASLLDEATAAAEAMQMCVNISKSKGPFAFLVDKYCHPQTIDTIKTRAEPKGIRIEVVDSKDFKFTEDVVGCIVQYPSSNGVITDYKEMADRAHQANALVVAATDLLSLALLKPPGEWGADIALGNSQRFGVPLGFGGPHAAFFSTKDKYARLLPGRIIGVSKDKQGNSAFRMALQTREQHIRREKATSNICTSQALLANMSAMYAVYHGQQGIKDIANAVHRKAIILAEGIKRLGYTVLDRPFFDTVLIITGDKTDMMIKELESRQINVRQYCSKSISISLDETVTSADISALLNGFSAHASKPLGLSSPEQLEKETSTISVISEEFARQTPFLTHPIFNRYHSEHELLRYIHKLQKKDLGLTTAMIPLGSCTMKLNATTEMYPVSWPEFNSIHPFVPANQSLGYKEMFESISNMLCEVTGFDGCSLQPNAGSQGEYAGLMVIRSYLTSIGQSQRNVCLIPVSAHGTNPASAAMVGMKVVVVDCDTNGNIDVADLKAKAEKHKDTLAALMITYPSTHGVFEEGANDICDIIHANGGQVYMDGANMNAQVGLCRPGDIGADVCHLNLHKTFCIPHGGGGPGMGPICVKSHLAPFLPGHSVVKGVGGERAMSAVSAGPWGSSSILPITYVYLKLMGGQGLKKATQVAILNANYMASRLKDHYKILYTGSHGLVAHEFIIDLRMFKESAGIEAEDVAKRLQDMNFHGPTMSWPVPNTLMIEPTESESKYELDRLCDALILIREEIREIETGKADRKNNVLVNSPHTEKVIVADNWNYPYSRSKAAFPTPATVASKFWPTVGRIDNVHGDKNLVCSCPPLSDYQ", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvP family."}
{"protein": "MANSNTYLTTPTKTPSSRRNQQSQSKMQSHSKDPINAESRSRFEAYNRLQAAAVAFGEKLPIPEIVAIGGQSDGKSSLLEALLGFRFNVREVEMGTRRPLILQMVHDLSALEPRCRFQDEDSEEYGSPIVSATAVADVIRSRTEALLKKTKTAVSPKPIVMRAEYAHCPNLTIIDTPGFVLKAKKGEPETTPDEILSMVKSLASPPHRILLFLQQSSVEWCSSLWLDAVREIDSSFRRTIVVVSKFDNRLKEFSDRGEVDRYLSASGYLGENTRPYFVALPKDRSTISNDEFRRQISQVDTEVIRHLREGVKGGFDEEKFRSCIGFGSLRDFLESELQKRYKEAAPATLALLEERCSEVTDDMLRMDMKIQATSDVAHLRKAAMLYTASISNHVGALIDGAANPAPEQWGKTTEEERGESGIGSWPGVSVDIKPPNAVLKLYGGAAFERVIHEFRCAAYSIECPPVSREKVANILLAHAGRGGGRGVTEASAEIARTAARSWLAPLLDTACDRLAFVLGSLFEIALERNLNQNSEYEKKTENMDGYVGFHAAVRNCYSRFVKNLAKQCKQLVRHHLDSVTSPYSMACYENNYHQGGAFGAYNKFNQASPNSFCFELSDTSRDEPMKDQENIPPEKNNGQETTPGKGGESHITVPETPSPDQPCEIVYGLVKKEIGNGPDGVGARKRMARMVGNRNIEPFRVQNGGLMFANADNGMKSSSAYSEICSSAAQHFARIREVLVERSVTSTLNSGFLTPCRDRLVVALGLDLFAVNDDKFMDMFVAPGAIVVLQNERQQLQKRQKILQSCLTEFKTVARSL", "text": "FUNCTION: Probable microtubule-associated force-producing protein that is targeted to the forming cell plate during cytokinesis. May play a role in cell division. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, phragmoplast Note=Localizes in the forming cell plate during cytokinesis. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MERSQSQQHGGEQSWWGTAPQYQYMPFEHCTSYGLPSENGGLQHRPRKDLGPRHNAHPTQIYGHHKEQYSYQAQDRGIPKKTDSSSTVDSLDEDHYSKCQDCVHRLGRVLRRKLGEDWIFLVLLGLLMALVSWCMDYVSAKSLQAYKWTYAQMQPSLPLQYLAWVTFPLILILFSALFCQLISPQAVGSGIPEMKTILRGVVLKEYLTLKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSMFSGVYEQPYYYTDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASLTFPPGMGQFMAGELMPREAISTLFDNNTWVKHIGDPKSLGQSAVWIHPQVNVVIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPEGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKFTIFVEDIMVRDVKFVSASCTYGELRNLLQTTTVKTLPLVDSKDSMILLGSVERSELQSLLQRHLCAERRLKAAQDMARKLSELPYNGQAQLAGEWHPGGRPESFAFVDEDEDEDVSRKTELPQTPTPPPPPPPPLPPQFPIAPSYPEEPNGPLPSHKQPPEASDSADQRSSIFQRLLHCLLGKAHSTKKKITQDSTDLVDNMSPEEIEAWEREQLSQPVCFDFCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIKGHTKSGVQLRPPLASFRNTTSIRKTPGGPPPPAESWNVPEGEDGAPEREVMVPTMPETPVPPPSPEVPSCLAPARVEGELEELEMVGNLGPEEDLADILHGPSLRSTDEEDEDELIL", "text": "FUNCTION: Voltage-gated chloride channel (PubMed:1659664). Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC- 1/CLCN1 subfamily."}
{"protein": "MVKILVLALVFSLAHAQDFAELQGKWYTIVIAADNLEKIEEGGPLRFYFRHIDCYKNCSEMEITFYVITNNQCSKTTVIGYLKGNGTYQTQFEGNNIFQPLYITSDKIFFTNKNMDRAGQETNMIVVAGKGNALTPEENEILVQFAHEKKIPVENILNILATDTCPE", "text": "FUNCTION: Acts as an aphrodisiac pheromone, reliably eliciting copulatory behavior from male hamster. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MAAPVGAQARKLLRDLVLRPPLLAARSQVVQLTSRRWLNLQEYQSKKLMSDNGVKVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFSSGLKGGVHLTKDPKVVGQLAKQMIGYNLATKQTPKEGVKVKKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIIEGIKDSQAQRMAENLGFLGPLKNQAADQIKKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVHEAQNILSNSGLPITSAVDLEDAAKKAVASVAKK", "text": "FUNCTION: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family. GTP-specific subunit beta subfamily."}
{"protein": "MSQAFNLVLFTEIKQAQNVKTGNDKEPNSKLRAIVRISERSSKKTPRATPRDDFVYTWNSTISLKLRSQLKLPLIQISVWDKQAHRSVYVGEVRFFLIGLLKSLAYNEHTSSWESTPQWYQLYSSEDKKSFSSGTILVQFRVQQHLSKKNLFFNAKSDVTLSDQTGSSDLLNQYIQAIETSTPRSLQKKAFDLSNPNEQRFYPDIETNALASSILDCEIDSMLEDFTYRKPNITESSLHDDTLTDTDFESIHSDPTIPSSALVPKRILFIEILSVTDLPPYKSFTRATFDMDPFVVISFGKRTYRTSWRKHTLTPVFNERLAFEVCDYEKNYDLQFSVLDKDKFSFHDQVATGFVSVSELLEEKTTDKPCTDFKPTSSNLILLDKPMNANESADNLLDTKKKKYKRNVNTDATLQGGLLRKYELVMSLDGKKNWSRKTKDEYIPILKFNTRFERYEILRRQLWMHLLQGNDTQMKGTLDLIELNYFVDCLGSNLSDKTLASFFEYYDKNPWVGETLTIEQVIDSLERLVFKRQCANTHENYIINIDTCPLCGQGRLSLRQDLDILKHLSICASRDWSTVNKVLKPSFVSSKAATRRWYSRLLIKLTFGQYTLGGNSANILIQDRDTGYILEEKMNIHVRLGIKLLYKSFDKANSRKIKTLLRKLSIRQGIKFDSPSSVSQIPSFIKFHKLDVDDCLLQLDEYKTFNEFFYRKLKPGSRPQEDENNSNIATSPADCRCTVFESITFAKTFWIKGRNFTTKKLFGSFYSREMADLYDECSIGIFRLAPQDYHRFHSPVTGTVGKVQSISGEYFTVNPMAIRSDLDVFGENVRCLLPIQTKEFGRVLVVPVGAMMVGSIILSVKENQEVKKGDELGYFKFGGSTLLVLFPNKRFKFDSDLLANSNNKIETLIKVGMSIGHTPEEPQFERHYRSFEEEPVDQQLRIIRCITGGSTFEESKQATQRRNELLGNEGSPQEKDLQVENLSWEAKNMNLEELEENESLLLYDLVNDGT", "text": "FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily."}
{"protein": "MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK", "text": "FUNCTION: Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA. SUBCELLULAR LOCATION: Cytoplasm. Note=After completion of the hook- basal body structure, it is exported out of the cell through the completely assembled hook-basal body structures. SIMILARITY: Belongs to the FlgM family."}
{"protein": "MGNAPQRPILITGGGRRIGLALAHHFLTLRQPVIVSYRNEYPSIEGLRQAGATCIQADFSTDEGILRFAETVKSNTRGLRAIIHNASAWQAEKPGTPLSETLACMMQIHVHAPYLLNHALEELLRGHGHAAGDIIHFTDYVVERGSDKHIAYAASKAALDNMTRSFARKLAPEVKVNAIAPSLILFNEEDDAEYRQKALNKSLMKIVPGEKEVIDLIDYLLTSCYVTGRSFGVDGGRPLN", "text": "FUNCTION: Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. FolM subfamily."}
{"protein": "MEKLRKVVNEIAYTRVHTNSPALHRSLVPFLTIASSLYGVALQIRRSLYRYSLLQKHRLPVPVISVGNLSWGGNGKTPMVEYISQFLVDSGLTPLILTRGYAGGDEVKMLERHLRGGPVKIGVGANRAATAALFLDKYGCVDSSSLRSFFDLHERAQVWTISEKIGCIILDDGMQHWSLSRDLEIVMLNGLNPWGNGHLMPHGPLREPLLALERADVAVVHHVDLITKQSLRDIENMIQGFKKSIPIFYSKMVPKYLFDVKNARSHVALEALRCASVLCVSAIGSADAFVKSIEMTGAHYVDRLDFSDHHLFEAEDVETMSRRAKGLEHKSNCKPIIVVTEKDYDRDPEILKCLDSYTVLVLCSELQITPILETDVDSFNYTLMKALAAKFYVSS", "text": "FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Transfers the gamma-phosphate of ATP to the 4'- position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the LpxK family."}
{"protein": "MTSTFNPRECKLSKQEGQNYGFFLRIEKDTEGHLVRVVEKCSPAEKAGLQDGDRVLRINGVFVDKEEHMQVVDLVRKSGNSVTLLVLDGDSYEKAVKTRVDLKELGQSQKEQGLSDNILSPVMNGGVQTWTQPRLCYLVKEGGSYGFSLKTVQGKKGVYMTDITPQGVAMRAGVLADDHLIEVNGENVEDASHEEVVEKVKKSGSRVMFLLVDKETDKRHVEQKIQFKRETASLKLLPHQPRIVEMKKGSNGYGFYLRAGSEQKGQIIKDIDSGSPAEEAGLKNNDLVVAVNGESVETLDHDSVVEMIRKGGDQTSLLVVDKETDNMYRLAHFSPFLYYQSQELPNGSVKEAPAPTPTSLEVSSPPDTTEEVDHKPKLCRLAKGENGYGFHLNAIRGLPGSFIKEVQKGGPADLAGLEDEDVIIEVNGVNVLDEPYEKVVDRIQSSGKNVTLLVCGKKAYDYFQAKKIPIVSSLADPLDTPPDSKEGIVVESNHDSHMAKERAHSTASHSSSNSEDTEM", "text": "FUNCTION: A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with NHERF1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function (By similarity). SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Cell membrane Note=Associated with peripheral membranes. Localizes to the apical compartment of proximal tubular cells and to sinusoidal liver membranes. SIMILARITY: Belongs to the NHER family."}
{"protein": "MFKSKTSTLSYDETPNSNEGDRNATPVNPKEKSQTKHLNIPGDRSRHSSIADSKRSSSRYDGGYSADIIPAQLRFIDNIDYGTRLRKTLHRNSVVSNGYNKLSENDRWYFDLFDRKYFENYLEEPTYIKIFKKKEGLEQFDRMFLAQELKIPDVYKSTTYQGEPAVANSELFKNSICCCTFSHDGKYMVIGCKDGSLHLWKVINSPVKRSEMGRSEKSVSASRANSLKIQRHLASISSHNGSISSNDLKPSDQFEGPSKQLHLYAPVFYSDVFRVFMEHALDILDANWSKNGFLITASMDKTAKLWHPERKYSLKTFVHPDFVTSAIFFPNDDRFIITGCLDHRCRLWSILDNEVSYAFDCKDLITSLTLSPPGGEYTIIGTFNGYIYVLLTHGLKFVSSFHVSDKSTQGTTKNSFHPSSEYGKVQHGPRITGLQCFFSKVDKNLRLIVTTNDSKIQIFDLNEKKPLELFKGFQSGSSRHRGQFLMMKNEPVVFTGSDDHWFYTWKMQSFNLSAEMNCTAPHRKKRLSGSMSLKGLLRIVSNKSTNDECLTETSNQSSSHTFTNSSKNVLQTQTVGSQAIKNNHYISFHAHNSPVTCASIAPDVAIKNLSLSNDLIFELTSQYFKEMGQNYSESKETCDNKPNHPVTETGGFSSNLSNVVNNVGTILITTDSQGLIRVFRTDILPEIRKKIIEKFHEYNLFHLEAAGKINNHNNDSILENRMDERSSTEDNEFSTTPPSNTHNSRPSHDFCELHPNNSPVISGMPSRASAIFKNSIFNKSNGSFISLKSRSESTSSTVFGPHDIPRVSTTYPKLKCDVCNGSNFECASKNPIAGGDSGFTCADCGTILNNFR", "text": "SIMILARITY: Belongs to the WD repeat DGR2 family."}
{"protein": "MSSKLFCLRSFPSVQRTAWQRLVLPSTRKFSLTPTTFDKTPSGRIPPDQKAANIISSVPSTSLLTKSGVLTVTAAALATAISKGIYVVNDESIVVASFLGLVGVFGTLGRKAYNEWSDKTIAKIGGIMQAARNDHTSAIRERIDQVASLQEVESVTQALFHTSKETARMEAEIFELEQRVALAKEAKSVLDSWVHHEANVRAEQQERLVEDVLARVNSKVSTQKFQQDALNESLGEIEKVLASA", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase B chain family."}
{"protein": "MSSPTSTPSRRKSKRGRGSNPPTPRGEEVQSPPSQKRRTEDSTSIGELLPMPTSPSGDIQSPLFSSPAPSRHSAHQSELDLSSPLTYGTPSSRVEGTPRSGIRGTPARQRADLGSARKVKQVDLHSDQPAAEELVTSEQSLGQKLVIWGTDVNVAICKEKFQRFVQRFIDPLAKEEENVGLDLNEPIYMQRLEEINVVGEPFLNIDCDHLRSFDQDLYRQLVCYPQEVIPTFDMAANEIFFERYPDSILEHQIQVRPYNALKTRNMRSLNPEDIDQLITISGMVIRTSQIIPEMQESFFKCQVCAFTTRVEIDRGRIAEPSVCKHCNTTHSMALIHNRSMFSDKQMIKLQESPEDMPAGQTPHTTILYAHNDLVDKVQPGDRVNVTGIYRAVPIRVNPRVRNVKSVYKTHIDVIHYRKTDSKRLHGIDEDTEQKMFTEERVAVLKELAAKPDIYERLAAALAPSIYEHEDIKKGILLQLFGGTRKDFSHTGRGKFRAEVNILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMNESTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPVESQWNPKKTTIENIQLPHTLLSRFDLIFLMLDPQDETYDRRLAHHLVALYYQSEEQLKEEHLDMAVLKDYIAYARTYVNPRLGEEASQALIEAYVDMRKIGSGRGMVSAYPRQLESLIRLSEAHAKVRFSSKVETIDVEEAKRLHREALKQSATDPRTGIVDISILTTGMSATARKRKEELAQVLKKLIQSKGKTPAFKYQQLFEDLRGQSDAAITKDMFDEALHALADEDYLTVTGKTVRLL", "text": "FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. SIMILARITY: Belongs to the MCM family."}
{"protein": "MNPCVLPTPLPDLDGDKRWHSIHRRFISDCREKDPDVIFLGDCIFETVQDTEAWNKYFAPLHCLNFSIRDDCTEHVLWRIENGALDNVNPKIVVLHVGTNNVRNSAEEVAEGVLANVTKIRQKLPNAYIVLPSLLPRGQQPNKLREKNAKINEVVNGLTKGLYRVQTVAIDKGLVQTDGSISHHDMFDYKNLTNAGAKKILEPLYDLLSQILNENEPENDLTPSE", "text": "SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. Platelet- activating factor acetylhydrolase IB beta/gamma subunits subfamily."}
{"protein": "MMVQVPIFDLLKLLDVLGIDSISFRVLNEYDEGFIRVDYLEEALQKDGWSKVYNESEDPNYCCGNFDVEYANNGYKIILRCDEDGYVFQITINKVT", "text": "FUNCTION: Essential for virus function."}
{"protein": "MAGAIIENMSTKKLCIVGGILLVFQIVAFLVGGLIAPAPTTAVPYTAIKCVDVRKNHHKTRWLAPWGPNKCDKIRDIEEAIPREIEANDIVFSVHIPLPSMEMSPWFQFMLFILQLDIAFKLNNQIRENAEISMDVSLGYRDDMFSEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYNCDVLPFMEIGSVAHKYYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQVGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDVGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKVRRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVSEGHWKWGGVTVQVSSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE", "text": "FUNCTION: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Also plays an important role in establishment of the anterior-posterior body axis formation during development. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the wntless family."}
{"protein": "MNLNRFERYPLTFGPSPITPLKRLSEHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLIPEAIEQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQENWVNYSDAVYDRVGNIEMSRIMGADVRLDAAGFDIGIRPSWEKAMSDVVERGGKPFPIPAGCSEHPYGGLGFVGFAEEVRQQEKELGFKFDYIVVCSVTGSTQAGMVVGFAADGRSKNVIGVDASAKPEQTKAQILRIARHTAELVELGREITEEDVVLDTRFAYPEYGLPNEGTLEAIRLCGSLEGVLTDPVYEGKSMHGMIEMVRRGEFPDGSKVLYAHLGGAPALNAYSFLFRNG", "text": "FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source. SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase family."}
{"protein": "MTTSAQRPERVIVVGGQDWDQVVTAARQMSNSSSRAGDAAEHAGERIVVNMGPQHPSTHGVLRLILEIEGETIVEARCGIGYLHTGIEKNLEFRTWTQGVTFVTRMDYLSPFFNETAYCLGVEKLLGVTDDIPERASVIRVMMMELNRISSHLVALATGGMELGAMTAMFLGFRERELILSVFETITGLRMNSAYIRPGGVAADLPEEGLPQIRELLTLLPTRLRDMENLLNENYIWKARTLGVGYLDLTGCMALGITGPVLRSTGLPHDLRKSQPYCGYQTYDFDVITDDRCDSYGRYLIRVKEMRESLRIVEQCVERLERSTGEPVMITDRKLAWPADLKVGPDGLGNSPEHIAKIMGHSMEGLIHHFKLVTEGIRVPPGQVYVAVESPRGELGVHMVSDGGTRPYRVHYRDPSFTNLQAVAAMCEGGMVADAITAVASIDPVMGGVDR", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 49 kDa subunit family."}
{"protein": "MKSAMTSSPLRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGNASVWDDPQAMLLAVKPDVVSVCSPNRFHYEHTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLGEIYVTTARALRRCGVPGWGVFTNKELQGGGPLIDIGIHMLDAAMYVLGFPAVKSVNAHSFQKIGTQKSCGQFGEWDPATYSVEDSLFGTIEFHNGGILWLETSFALNIREQSIMNVSFCGDKAGATLFPAHIYTDNNGELMTLMQREIADDNRHLRSMEAFINHVQGKPVMIADAEQGYIIQQLVAALYQSAETGTRVEL", "text": "FUNCTION: Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-glucosides leading to 3-dehydro-D-glucosides. Cannot act on UDP-glucose, UDP-N-acetyl-D-glucosamine, D-glucosamine, N-acetyl-D- glucosamine, or UDP-D-galactose. SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MATREQQPEGRRLKVARIYLRASTDEQNLERQESLVAATRAAGYYVAGIYREKASGARADRPELLRMIADLQPGEVVVAEKIDRISRLPLAEAERLVASIRAKGAKLAVPGVVDLSELAAEANGVAKIVLESVQDMLLKLALQMARDDYEDRRERQRQGVQLAKAAGRYTGRKRDAGMHDRIITLRSGGSSIAKTAKLVGCSPSQVKRVWAAWNAQQQK", "text": "FUNCTION: Involved in plasmid partition. SIMILARITY: Belongs to the site-specific recombinase resolvase family."}
{"protein": "TDIGGGLDVGGGLRGGLDIDAKGPDVDIKGPKVGGDISGPDLDVSGPDLDIDGGGKKGKGGFGFGLKMPKFGFGGHGKGDIDVDADVDIERPDLDVSGDADLPSGGVGLDVGGGIGGGLGGGLDIDANGPDVDIKGPKVGGDISGPDLDVSGPDLDIDVDGKKKGKGGFGFGMKMPKFGFGGHGKGDIDVDADVDIERPDLDVSGDADLPSGGVGLDVGGGIGGGLGGGLDIDANGPDVDIKGPKVGGDISGPDLDVSGPDLDIDVDGKKKGKGGFGFGLKIPKFMDPTFGFGGHGKGDIDVDADGGVVIPEGDIKVKTGKPDIGGDVDLPSGGVDLDVGGGIGGGLGGGLDIDAKGPDVDIKGPRVGGDISGPDLDVSGPDLDIDGDGKKKGKGGFGFGLKMPKFGFGGHGKGDIDVDADVDIERPDLNVSG", "text": "FUNCTION: May function as a multidomain RNA-binding protein. May play a role in nuclear RNA processing and in early development. SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. Nucleus Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Initially a peripheral membrane protein associated with the microsomal membrane fractions. May be targeted to the nucleus later in development."}
{"protein": "MASTFAIGLGVATAAFLGRAGYVALRRYQGGINAMGKAFYKGGFEPRMTRREAALILELPERTLNKEKVRKKHRQLMLLNHPDRGGSPYLATKINEAKEFLDKHI", "text": "FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1/sscA) (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM14 family."}
{"protein": "MADSDNTPTSRKDFETAIIAKAWKDPEYLRRLRSNPREVLQEELEALHPGAQLPDDLGISIHEEDENHVHLVMPRHPQNVSDQTLTDDDLDQAAGGTGIGVVVAVVAGAVANTGAGVNQVAGGNINVVGNINVNANVSVNMNQTT", "text": "FUNCTION: Antimicrobial peptide active against Gram-positive bacteria (MIC=4->125 ug/ml) (PubMed:22983711). May act by forming transmembrane ion channels, since the peptide rapidly depolarizes the bacterial cytoplasmic membrane, simultaneously decreasing the membrane potential and intracellular potassium contents (PubMed:22983711)."}
{"protein": "MMSDYTWFEGIPFPAFWFSKEILENSCKKFVVKEDDLIILTYPKSGTNWLIEIVCLIQTKGDPKWIQSMPIWDRSPWIETGSGYDKLTKMEGPRLMTSHLPMHLFSKSLFSSKAKVIYLIRNPRDVLVSAYFFWSKIALEKKPDSLGTYVEWFLKGNVAYGSWFEHIRGWLSMREWDNFLVLYYEDMKKDTMGSIKKICDFLGKKLEPDELNLVLKYSSFQVVKENNMSNYSLMEKELILTGFTFMRKGTTNDWKNHFTVAQAEAFDKVFQEKMAGFPPGMFPWE", "text": "FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze sulfonation of hydroxysteroids and xenobiotics. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfotransferase 1 family."}
{"protein": "MRILFIIIQLTLILSACAYQQGKQGQNVEKESTRQQETKPIHVKDTTQETKDNGTRTDIAKHLVSVAEKNPDVKDATAVVLGGYAVVGIDVDDTLDRSKVETIKYSVAQALKNDRYGANAVVIADPDTVSRLREMSREISEGHPVTGILDELAAIVGRVLPEVPNDVIDNEDEPQTKQQNDQLNRKQQQEMEKEQNDQSDHHMKKNNND", "text": "FUNCTION: Probably contributes, directly or indirectly, to early events in germination. SUBCELLULAR LOCATION: Forespore inner membrane; Lipid-anchor."}
{"protein": "MFDALAERLEQAWTKLRGQDKISESNVQEALKEVRRALLEADVNLGVVKEFIAQVQEKAVGTQVISGIRPDQQFIKVVYDELVQVMGETHVPLAQAAKAPTVILMAGLQGAGKTTATAKLALHLRKEGRSTLLVATDVYRPAAIDQLITLGKQIDVPVFELGSDANPVEIARQGVEKARQEGIDTVIVDTAGRLQIDTEMMEELAQVKEAIAPHEVLLVVDSMIGQEAASLTRSFHERIGITGAILTKLDGDSRGGAALSIRRVSGQPIKFVGLGEKVEALQPFHPERMASRILGMGDVLTLVEKAQEEIDLADVEKMQEKILAAKFDFTDFLKQMRLLKNMGSLAGFIKLIPGLGGKINDEQLRQGERQLKRVEAMINSMTPQERRDPDLLSNSPSRRHRIAKGCGQTEAEIRQIIQQFQQMRTMMQQMSQGGFPGMGGMGMPGFGGGMPGFGGGAPAPQPGFRGYGPPKKQKKGSKKKKGFGL", "text": "FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. SUBCELLULAR LOCATION: Cytoplasm Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily."}
{"protein": "MTEFKRIPPEQAQALRAQGAVLVDVRDAQAFQSNHIPDSQHLDNHSIADFIANADLDKPLVVVCYHGNSSQSAAAYLVGQGFSDVYSVDGGFERWRSTFPEETAQG", "text": "FUNCTION: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GlpE family."}
{"protein": "MSKFSFFNYRINMRNSHATSLRFIKFNYSEFKNIRNFSSEKKRDPKLSLFLNNVSKILSEHKKDLHKAQEIIEREWLKLATPSTDVKSDITSTMYTKHRLIHDRAFDLLKLYKSNGNLNKISKSLKDYIVNEKFIFIAWSYLLASYSKSSLTNLDYRIGYSITRHIYTEYYKDEFMSFDDFSNYNKFDVGFFVKLGDIFINTFTSPLNPIFERVFENEIYSLKINKEYENEIMESLVISPKALPMVCPPLPWGHGIRGGNLINLTDTQDESLVVGSFHHRHKIAITDKLYNVINKLNAFKFKINGDLLSYLQNEGSFILDFYKNTKKDTYINNMITIDIARTYLNTPFYLNVNIDWRGRIYTQSFYLDYQGSELSLALINLFEGKKLDEKGLFFFYVYGANIYNDGGKFSKKSFQDRFNWVVENLDNIIAMDKEFILKAESPTLFAAFCLTMRKLKENPDYPVFNPIFLDATCSGVQHFAAMLLDLELGKYVNLINSGESVNDFYSQLIPAINKAINESAEKKFKNLKFSDISLNRSLLKKVIMTKSYNVTTYGITEQLKSKLEKVEKIVISKGKEIKVYDYLVPTKNGDFVVLDTFEVETLASIINDNIFNQFPKLHSIYDYLTRLAKIYLKLDIPLSWSTPDGLELTQRYNLSKVKKLTINFLGKNRTAVLRSWVNEKDSRREVQAIIPNIIHSLDASHLTMIIDSWDSYILPIHECFGTHPNDMYKLAEQVRECFILLYSKNDFLNKIDYKFRENLKDYKIEIVNKNGEDFVKIKGNKRYEYLPLPVLPQMGELNVEDIRDMGKYMIS", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase family."}
{"protein": "MKKRNKGLVEQTTTEKNNFSRKTAWKVFWWVIILAVVIGVLAYIFSPRAATAVVESWKLNGGSNSTLTAKVSGFSNELTFKQINGSTYVTDTILQVSITFDGLNSPLTVTAHKTVNSNGNVIFNIANLSINQSNGQITVNSNGTMMNGGSSNNTKSIAGFETLGTFIAPDTRARDVLNGLFGLLPIIIFVVFFLLFWRSARGISAGGREEDNIFSIGKTQAKLAKSTVKFTNIAGLQEEKHELLEIVDYLKNPLKYAQMGARSPRGVILYGPPGTGKTLLAKAVAGEAGVPFFQSTGSGFEDMLVGVGAKRVRDLFNKAKKAAPCIIFIDEIDSVGSKRGRVELSSYSVVEQTLNQLLAEMDGFTSRTGVVVMAATNRLDVLDDALLRPGRFDRHIQINLPDIKEREGILKVHAENKNLSSKISLLDVAKRTPGFSGAQLENVINEATLLAVRDNRTTININDIDEAIDRVIAGPAKKSRVISDEDRKLVAYHEAGHALVGLHVHSNDEVQKITIIPRGQAGGYTLSTPKSGDLNLKRKSDLLAMIATAMGGRAAEEEIYGNLEITTGASSDFYKATNIARAMVTQLGMSKLGQVQYVPSQGTLPSNVKLYSEQTAKDIDNEINFIIEEQYKKAKTIIKSNRKELELLVEALLIAETILKSDIDFIHKNTKLPPEILLQKQEQQAKQKLNKSEVKPESETNS", "text": "FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein; Cytoplasmic side. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family. SIMILARITY: In the central section; belongs to the AAA ATPase family."}
{"protein": "ADNRRPIWNLGHMVNALKQIPTFLXDGANA", "text": "FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). In vivo, intradermal injection induces dermonecrosis (PubMed:8819009). Induces hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod phospholipase D family. Class I subfamily."}
{"protein": "MASAPSDIPENAFRLAKASGRCQSMMSQMKDETKCMGAVFSGYPTALWLEYEVSPQPMSGTLKERLKKARASSQPFCSVVKRIKVENEENDQTLSEPGESSKEENCSKAQESLENKDNEPEKESSEDKNTSESKSLDTGSSSVLQKDSTEKTIKQTLKEEKAKLTRQVQEKEDLLRRLKLVKMYRIKNDVTELEDLIKKWRRCGQRLLCELQSIMSEDEDEKLTLTELIDYYGIDDKLLHYNRTEEEFTGV", "text": "FUNCTION: Component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination. Acts as a transcriptional modulator for ESR1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SFR1/MEI5 family."}
{"protein": "MTTSMQPSKYTGLVADLMPNIRAMKYSGLFMHNFTGGSAFMKKVYSSVHLVFLLMQFTFILVNMALNAEEVNELSGNTITTLFFTHCITKFIYLAVNQKNFYRTLNIWNQVNTHPLFAESDARYHSIALAKMRKLFFLVMLTTVASATAWTTITFFGDSVKMVVDHETNSSIPVEIPRLPIKSFYPWNASHGMFYMISFAFQIYYVLFSMIHSNLCDVMFCSWLIFACEQLQHLKGIMKPLMELSASLDTYRPNSAALFRSLSANSKSELIHNEEKDPGTDMDMSGIYSSKADWGAQFRAPSTLQSFGGNGGGGNGLVNGANPNGLTKKQEMMVRSAIKYWVERHKHVVRLVAAIGDTYGAALLLHMLTSTIKLTLLAYQATKINGVNVYAFTVVGYLGYALAQVFHFCIFGNRLIEESSSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK", "text": "FUNCTION: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Expression of Orco alone leads to formation of rapid and transient ion channels not directly responding to odorants, but directly activated by intracellular cAMP or cGMP. Snmp, Or67d and lush act in concert to capture fatty-acid-derived male pheromone 11-cis vaccenyl acetate (cVA) molecules on the surface of Or67d expressing olfactory dendrites and facilitate their transfer to the odorant-receptor Orco complex. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Heteromeric odorant receptor channel (TC 1.A.69) family. Orco subfamily."}
{"protein": "MWASFMWHGALSPGRRAHSALAQLRCILDSELEGIRGAGTWKSERVITSRQGPSIRVDGISGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP", "text": "FUNCTION: Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA. Catalyzes the second reaction step on the main metabolic degradation pathway for L-threonine. SUBCELLULAR LOCATION: Mitochondrion Nucleus Note=Translocates to the nucleus upon cold and osmotic stress. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MDTQMCALFAQPLTLLPDLNICSWQTVNGSQRTFFVWTWTMTSSGLRTRAINLKQWNGLTYRSYAILSWNPRETPLHLTRVTPSPQVTKGSLSTTSIPINTKIQLICLPAVAMLATPPKTTDNCRTSWAALQMLLLLWHLSSWIKTQRRWRISLTE", "text": "FUNCTION: May be required for viral persistance in the host."}
{"protein": "MKHLTEMVRQHKAGKTNGIYAVCSAHPLVLEAAIRYASANQTPLLIEATSNQVDQFGGYTGMTPADFRGFVCQLAESLNFPQDALILGGDHLGPNRWQNLPAAQAMANADDLIKSYVAAGFKKIHLDCSMSCQDDPIPLTDDIVAERAARLAKVAEETCLEHFGEADLEYVIGTEVPVPGGAHETLSELAVTTPDAARATLEAHRHAFEKQGLNAIWPRIIALVVQPGVEFDHTNVIDYQPAKASALSQMVENYETLIFEAHSTDYQTPQSLRQLVIDHFAILKVGPALTFALREALFSLAAIEEELVPAKACSGLRQVLEDVMLDRPEYWQSHYHGDGNARRLARGYSYSDRVRYYWPDSQIDDAFAHLVRNLADSPIPLPLISQYLPLQYVKVRSGELQPTPRELIINHIQDILAQYHTACEGQ", "text": "FUNCTION: Component of the tagatose-1,6-bisphosphate aldolase KbaYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of KbaY. When expressed alone, KbaZ does not show any aldolase activity. SIMILARITY: Belongs to the GatZ/KbaZ family. KbaZ subfamily."}
{"protein": "MKGNSTLATTSKNITSGLHFGLVNISGNNESTLNCSQKPSDKHLDAIPILYYIIFVIGFLVNIVVVTLFCCQKGPKKVSSIYIFNLAVADLLLLATLPLWATYYSYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYIVPLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPLIFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALAWMGVINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRVPITWLQGKRESMSCRKSSSLREMETFVS", "text": "FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide (PubMed:8185599, PubMed:28379944, PubMed:29967536, PubMed:31899086). Signals primarily via a non-canonical G-protein- and beta-arrestin independent pathways (PubMed:28379944). Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation (PubMed:15123706). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MTAQSLLQTTLFLLSLLFLVQGAHGRGHREDFRFCSQRNQTHISSLHYKFTPDLRISIENSEEALTVHAPFPEAHPASRSFPHPRGLYHFCLYWDRHAGRLHLLYGKHDFLLSDQASSLLCFQHQEESLAQGPPLFATSVTSWWSPQNISLPSASNFTFSFHSPPHTAAHNASVDMCELKRDLQLLSQFLKHPQKASRRPSATPASQQLQSLESKLTSVRFMGDTVSFEEDRVNATVWKLQPTAGLQDLHIHSRQEQEQSEILEYSVLLPRTLFQRTKGRRGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQPQPKNVTLQCVFWVEDPTLSNPGRWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEVDAVHKHYLSLLSYVGCVVSALACVVTIAAYLCSRRKPRDYTIKVHMNLLLAVFLLDVSFLLSEPVALTGSQSGCRASAIFLHFSLLACLSWMGLEGYNLYRLVVEVFGTYIPGYLLKLSAMGWGFPIFLVTLVALVDVDNYGPIILAVHRTPESVIYPSMCWIRDSLVSYITNLGLFSLVFLFNMAMLGTMVVQILRLRPHTQKWSHVLTLLGLSLVLGLPWALIFFSFASGTFQLVVLYLFSIITSFQGFLIFLWYWSMRLQARGGPSPLKSNSDSARLPISTGSTSSSRI", "text": "FUNCTION: Receptor involved in cell adhesion and probably in cell-cell interactions. Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells. Receptor for collagen III/COL3A1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination. Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12. Plays a role in the maintenance of hematopoietic stem cells and/or leukemia stem cells in bone marrow niche (By similarity). Plays an essential role in testis development (By similarity). Plays a critical role in tumourigenesis. SUBCELLULAR LOCATION: [ADGRG1 N-terminal fragment]: Secreted Note=Interaction with its ligand COL3A1 leads to the release of ADGRG1 NT from the membrane and triggers the association of ADGRG1 CT with lipid rafts. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [ADGRG1 C-terminal fragment]: Membrane raft. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily."}
{"protein": "MSNMYCGIGKVPKGKERGTPEHCFQSNQIRYYGIKKIDKSLLEKPKKKRLSLIKEQTKLNNLLEKGKRMVKEANKLKSIINDPESSKTEIRNAKKKLEKIVAKKNKFVLELKQQRQVVDELLEEEREKEKAERKAEKAKKNKKKSSTKTKKK", "text": "SIMILARITY: Belongs to the mimivirus R546 family."}
{"protein": "MSIKKLILAASILTTLALTGCGGKGAVQPSGVSTGDVNAKIVFDNDKVNADNVDGLSVSEREVKITKPGMYTFSGTWNDGQILVDIGKEFEAVLVLDGVNITNTKSAPIYIKSAEKVKIELADGKDNVLTDAEFYEFEDPQDNKPNACIYSRDDITIKGNGNLTVNANFNNGIGTSNDLKITGGNITVKAFNNGLKGNDSVTISGGNIDITAEADGIKVENTEEPHKGYVNITGGTIKIRAKDDAIDSVRSVSINNADVKVSVGGKDVKCEGVLNIAEGCLGKLEE", "text": "FUNCTION: Binds cellulosic and pectic substrates. Displays no enzyme activity (in vitro). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
{"protein": "MAAAEMERTTSFDAAEKLKAADAGGGEVDDELEEGEIVEESNDAASYLGKEITVKHPLEHSWTFWFDNPTARSRQIDWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVMGADFHCFKHKIEPKWEDPICSNGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVNVRVKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV", "text": "FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection (e.g. Potato virus Y (PVY)) by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg) (PubMed:22146867). Displayed sequence is the allele Eva1 that confers resistance to potato virus Y (PVY) by failing to interact with the viral VPg protein (PubMed:22146867). FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (PubMed:22146867). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the eukaryotic initiation factor 4E family."}
{"protein": "MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE", "text": "FUNCTION: Chaperone that confers thermal protection to other proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
{"protein": "MTATPANSGSNPRKFSEKIALHNQKQAEETRAFDELMSDLTVSRVQFQKLQQLRLAQTRAQYYGGSLPNVNQISSSPNDFQPSFHPMDNIRGMRHHGLVERVSRNRLHSSHHRPVEKHGRQCDSSPYGSVYLSPPPDNNWRRTNSDSALHTSASSSKLQDAFMGGNQAMLRAPKPPQRNPSLQDGEMNNFGEAFSYPTSMTEENMLNVTKPLPKQIWEAQKVQCITSRPRSCEVPGIKVFPSSDSNASLSHYQGSLNTGGSLPDLTNLHFPSPLPTPLDPDDTVYANINAENSSGLPAAMTHLGISNSQGIQNTCSNPSIQATMNNNVNNHTPPGRNNPTLHPSLRLSSLSNPSLPTSALGSSPRRRHTPVSPLTLTPGSESNRSISNQFSPTSPMDMLPNSQGVSMDRCPLSLPPLEPPPPYPLYTDQPQPQLHHTQQQMHESPESQNFQPPSPVPCPPLDLNLANSSLSGFFGDSFFDQQQPTKQGKYLWQQQEQYDMFGSPSSSLPNTNAFFDPNMNLQYSQASLMGLGGSHGSLQDSFHLRPNYLYSNYGGSVPNIILTDDSSNSLSKDISNAVAGVSELGFDADNTFQFDDELKLGPLSLDGLSMLSDPDMVLPDPSIEDSFRSDKL", "text": "FUNCTION: Transcriptional coactivator for creb1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of creb1 'Ser-119' phosphorylation. Enhances the interaction of creb1 with taf4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of ppargc1a and inducer of mitochondrial biogenesis in muscle cells (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Appears to be mainly nuclear. SIMILARITY: Belongs to the TORC family."}
{"protein": "MTGRGKGSKGKLGRDNATDDPVDLVYAAEKIIQKRVKKGVVEYRVKWKGWNQRYNTWEPEVNILDRRLIDIYEQTNKSSGTPSKRGIKKKEKEPDPEPESEEDEYTFTENDVDTHQATTSSATHDKESKKEKKHHHHHHHHHHIKSERNSGRRSESPLTHHHHHHHHESKRQRIDHSSSSNSSFTHNSFVPEPDSNSSSSEDQPLIGTKRKAEVLKESGKIGVTIKTSPDGPTIKPQPTQQVTPSQQQPFQDQQQAEKIASEAATQLKSEQQATPLATEAINTTPAESGAEEEEVANEEGNQQAPQVPSENNNIPKPCNNLAINQKQPLTPLSPRALPPRFWLPAKCNISNRVVITDVTVNLETVTIRECKTERGFFRERDMKGDSSPVA", "text": "FUNCTION: Polycomb group (PcG) protein (PubMed:1898775). PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (PubMed:1898775, PubMed:11493925, PubMed:11583617). PcG proteins are not required to initiate repression, but to maintain it during later stages of development (PubMed:1898775). Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility (PubMed:11493925, PubMed:11583617). Promotes locus- specific chromatin compaction (PubMed:11493925, PubMed:11583617). Binds to (N(6)-methyladenosine) DNA and thereby might implement repression of specific loci (PubMed:30078725). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MADIKNNPEYSSFFGVMGASSAMVFSAMGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDGITLYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK", "text": "FUNCTION: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). FUNCTION: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:32165585). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32165585). SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family."}
{"protein": "MNINVANLLNGNYILLLFVVLALGLCLGKLRLGSIQLGNAIGVLVVSLLLGQQHFAINTEALNLGFMLFIFCVGVEAGPNFFSIFFRDGKNYLMLALVMVGSAMILALGLGKLFGWDIGLTAGMLAGSMTSTPVLVGAGDTLRHTMANGSSLQQAQDNLSLGYALTYLIGLVSLILGARYLPKLQHQDLPTSAQQIARERGLDTDSQRKVYLPVIRAYRVGPELVAWADGKNLRELGIYRQTGCYIERIRRNGILANPDGDAVLQVGDEISLVGYPDAHSRLDPSFRNGKEVFDRDLLDMRIVTEEIVVKNSNAVGKRLSHLKLTDHGCFLNRVIRSQIEMPIDDNVVLNKGDVLQVSGDARRVKSVAEKIGFISIHSQVTDLLAFCSFFILGLMIGLITFQFSNFSFGIGNAAGLLLAGIMLGFLRANHPTFGYIPQGALNMVKEFGLMVFMAGVGLSAGGGINSSLGAVGGQMLISGLIVSLVPVVICFVFGAYVLRMNRALLFGAIMGARTCAPAMDIISDTARSNIPALGYAGTYAIANVLLTLAGSLIVILWPGILG", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family. YbjL subfamily."}
{"protein": "MIQRFITCLAALTLVFAVVAPAHSVQSNPFQQDNQFLSVDQAFDFDSEVNDSKVTVSWVVAPEYYLYQHRFKVVPENALAAEPELPQGESHNDEFFGESIVYRNYVEWSFTLNPEFSGDTITVQYQGCADAGLCYPPTEKQIKLSSTSETAPATAPPNTDSSLFGIGEQHLIITLLLFFALGIGLAFTPCVFPMYPILSGVVLGNRERNWKNTLWLSFIYVQGMAITYSLLGLVVASAGMQYQAYFQHPVVLIVLAVLFALFALSMFGAYTLQLPISWQSKLQSFSGQQSGGNIVGVFIIGAISGLVASPCTTAPLSGALLFIAQSGDMVSGVAILYALSLGMGVPLILFGLSGGKLLPKAGAWMNVVKQFFGWLLLAVTLFLIERLIPTSISMWLWIFYFILAAVSLAVSISQPLRITTKVITIVLLAAAATTGSYWQVNKAQLEQKSHGLFTVVSNVSDIQQQVAESDRWVMLDLYADWCVACKEFEQYTFSDEQVQAQFQEFKLIQADVTRNNAQDVEILSRYKVLGLPTILFFDPEGNERPEYRVTGYMNAEDFKKHLEKIVSE", "text": "FUNCTION: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily."}
{"protein": "MASESDTEEFYDAPEDVHLGTGYPVGSPGKVGLLSFKEAENTANQAGNESPVQELRQDVSKKIIESIIEESQKVLQLEDDSLDSKGKGLSDEATAGPSVAGTEFSNIPGLLAIEHELQQDSEKAESQNVAEESELETQKCFPSDETCEKSEKTVDETDNLTEVSSGEQLDASGLEAETLNKEALEVKEGDVLDPASLDTLSTTDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPPPTNFPPPRPPPPSRPAPPPRKKKSELEFEALKTPDLDVPKENITSDSLLTTNMASENTVRDSLPSLDLASATSGDKIVTAQENGKAPDVQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSNDATQSDDEEKLQSQQTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMPYTRPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNIVRIWALKNAFDYFNNMRMKYNTEGRVSPSPSQESLSSSKSDTDMGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYDTEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFTYLVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKLEGIDKYEDAEVLDSTSTGIVKTDNTEVLLSADFTGAIKVFINKRKTVS", "text": "FUNCTION: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia."}
{"protein": "MAAATPTETPAPEGSGLGMDARLDQETAQWLRWDQNPLTSESVKQLIAGGNKEELRKCFGARMEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFSDLKQRGVVISFDARAHPASGGSSRRFARLAATAFITQGVPVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLVDSSPLLHNPSASIGNDYFEDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDQSNLKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFLATKNLSLSQQLNAIYVEYGYHITTASYFICHDQGTIQNLFGNLRNYDGKNNYPKMCGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEHLKKELDELVGAIEEHFFQPQKYNLQPKAE", "text": "FUNCTION: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5- phosphopentoses. Catalyzes the interconversion of glucose-1-phosphate into glucose-6-phosphate but with a lower catalytic efficiency. In vitro, has also a low glucose 1,6-bisphosphate synthase activity which is most probably not physiologically relevant. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the phosphohexose mutase family."}
{"protein": "MCAARQILLLLLAFLAYALDSAAAYGTAETLCGGELVDTLQFVCGDRGFYFSRPVGRNNRRINRGIVEECCFRSCDLALLETYCAKSVKSERDLSATSLAGLPALNKESFQKPSHAKYSKYNVWQKKSSQRLQREVPGILRARRYRWQAEGLQAAEEARAMHRPLISLPSQRPPAPRASPEATGPQE", "text": "FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Acts as a ligand for integrin which is required for IGF2 signaling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
{"protein": "MFKKFSALFTLLFTLCLVNPMLVYSIDLDENTRSVPLDDAGNTVILTPEQVKRGKRLFNASCGQCHVGGITKTNPNLGLEPDALSLATPARDNINALVDYMKNPTSYDGLESIAEVHPSIKSADIFPKMRSLSDEDLFAIGGHILLQPKLSSEKWGGGKIYY", "text": "FUNCTION: Low-potential cytochrome c that plays a role in the oxygen- evolving complex of photosystem II. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Associated with photosystem II at the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily."}
{"protein": "MSALFLAIPLTIFVLFVLPIWLWLHYSNRSGRSELSQSEQQRLAQLADEAKRMRERIQALESILDAEHPNWRDR", "text": "FUNCTION: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspB is involved in transcription regulation (By similarity). FUNCTION: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspB is involved in transcription regulation. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PspB family."}
{"protein": "MKPVFCGNFEYDAREGDLERLFRKYGKVERVDMKAGFAFVYMEDERDAEDAIRALDRFEFGRKGRRLRVEWTKSERGGDKRSGGGSRRSSSSMRPSKTLFVINFDADNTRTRDLEKHFEPYGKIVNVRIRRNFAFIQYEAQEDATRALDASNNSKLMDKVISVEYAVKDDDARGNGHSPERRRDRSPERRRRSPSPYKRERGSPDYGRGASPVAAYRKERTSPDYGRRRSPSPYKKSRRGSPEYGRDRRGNDSPRRRERVASPTKYSRSPNNKRERMSPNHSPFKKESPRNGVGEVESPIERRERSRSSPENGQVESPGSIGRRDSDGGYDGAESPMQKSRSPRSPPADE", "text": "FUNCTION: Required for constitutive and alternative pre-mRNA splicing (Probable). Involved in primary miRNA processing and pri-miRNA biogenesis. Binds both intronless and intron-containing pri-miRNAs (PubMed:26227967). SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the splicing factor SR family. RS subfamily."}
{"protein": "MKKRVVTAGTFDILHPGHYEILKFAKSLGDELIVIVARDETVKKLKGRKPIIPEEQRREMVEALKPVDKAILGSLKNKLEPILELKPDIIVLGPDQTTFDEETLKKELAKYNLYPEIVRFRGYKKCPFHSSFDIVKEIIRRFCNKEIKI", "text": "FUNCTION: Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. To a lesser extent, is also able to utilize other nucleotides such as CTP and GTP as substrates, producing the modified coenzymes, flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide (FGD), respectively. Does not catalyze the reverse reaction to produce FMN and ATP from FAD and PPi. Does not function as a glycerol-3- phosphate cytidylyltransferase, as previously annotated in the complete genome. SIMILARITY: Belongs to the archaeal FAD synthase family."}
{"protein": "MAESPAFLSAQDVGSFAYLTIKDRTPQILTKVIDTLHRHKSEFFEKHGEEGVEAEKKAISLLSKLRNELQTDKPIIPLVDKCVDTDIWNQYLEYQRSLLNEGDGEPRWFFSPWLFVECYMYRRIHEAIMQSPPIHDFDVFKESKDENFFESQDSINALCTHLLQLKPITDLGEKQIQDEFFKLLQISLWGNKCDLSLSGGESSSQKADIINSLKDLKPFILVNETESLWALLSKLKKTAEPPAVRVDIVLDNSGFELVTDLVFADFLLSSELATEIHFHGKIIPWFVSDVTVRDFEWIVEHMKGSHLESMSACGAAWEAYVGMKKWVYHDHAFWTLPHPFCAMPQVAPDLYAELQKAGVVLFKGDLNYRKLMGDRKWKFTVPFHQALSGFHPAPLCSIRTLKCELQVGLQPGQAEHLTASDPHWLTTGKYGIFQFDGPL", "text": "FUNCTION: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1- phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (By similarity). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (By similarity). SIMILARITY: Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily."}
{"protein": "MKTFLTEQQIKVLVLRAKGLKQSEIAKILKTTRANVSILEKRALEKIEKAKNTLLLWEQINSKVNVNVKAGEDIFSVPEKLFKKADEAGVKVPYSTAEIIAFLVEHAPIENRLAKRDFVIFLDSKNRLRISDCLINLDEIEKK", "text": "FUNCTION: Putative transcriptional regulator. SIMILARITY: Belongs to the Tfx family."}
{"protein": "MPKYKYNKINILFSCCLLVSFVVAPLVVQAQEDPLVTQAREAAKEAKPLVQELLHLKNQQQFEKVEQNFEKAQRFLEDNRPNQEQIVEQLKSAKDVQTITKITIDFGGEEIFLDFDEVTKHYLNQPLSAKTVFALTKELTQVLYNAGYVTSAIGLKSSKIKNGEVEFVVLWGKVNDILVEEQQASLFKDKAMLFVLPNLKGKVLRIYDVDQLIEILNTGNKTAKVNVIAANEKSMSNLSIERHRTSYPQVSLSLNNSGEGSNAEGRNQATLSISWSDLLGTNDRWSFSTGYRIYKDRQANRQQNYSLSYTQPFSFSTLDIKLSYSGYKKQLRGIHTHGSSGETKQASFKLSHTLLRNKDMILSLYGELEFKRRLSYFGDIRIGKYHNNKLNIGLSYVTNLGHGKLYSDLSYSNGLRWFNANHSAYNSHRDKTLRLVSGSINWQRPFVFFNRGMSYQFRLGAQYGFDSLYGENQFSIGDEYTVRGFKGGAGSGDRGFYISQTVTIPFYPQKSYLSYINPFLGIDIGKVHAKRPHHVVDTFAGFAFGVKAQIKSLALSLTYAKPINGVGTFEESNKKSVFYFTGSVSF", "text": "FUNCTION: Possible member (with IbpA) of a two partner secretion pathway (TPS) in which it would mediate the secretion of protein IbpA (high molecular weight immunoglobulin-binding protein). SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the TPS (TC 1.B.20) family."}
{"protein": "MSNYSVSLVGPAPWGFRLQGGKDFNMPLTISSLKDGGKASQAHVRIGDVVLSIDGISAQGMTHLEAQNKIKACTGSLNMTLQRASAAAKSEPVSVQKGEPKEVVKPVPITSPAVSKVTSTTNMAYNKAPRPFGSVSSPKVTSIPSPSSAFTPAHAATSSHASPTPVAAATPLHLSASGLHVSANLSADQCSSPPNTGKPAVNVPRQPTVTSVCSESAQELAEGQRRGSQGDIKQQNGPPRKHIVERNTEFYHIPTHSDASKKRLIEDTEDWRPRTGTTQSRSFRILAQITGTEHLTESENDNTKKANSTQEPSQQPASSGASPLSASEGPESPGSSRPSVAGLRSAAAFKPVGSTSVKSPSWQRPNQAAPSTGRISNNARSSGTGASVGPPQPSDQDTLVQRAEHIPAGKRTPMCAHCNQVIRGPFLVALGKSWHPEEFNCAHCKNTMAYIGFVEEKGALYCELCYEKFFAPECGRCQRKILGEVINALKQTWHVSCFVCVACGKPIRNNVFHLEDGEPYCETDYYALFGTICRGCEFPIEAGDMFLEALGYTWHDTCFVCSVCCESLEGQTFFSKKDKPLCKKHAHSVNF", "text": "FUNCTION: May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May be required to restrain postsynaptic growth of excitatory synapses. Isoform 1, but not isoform 2, expression favors spine thinning and elongation. SUBCELLULAR LOCATION: Postsynaptic density Presynapse Postsynapse Cytoplasm, cytosol Note=Detected both at presynaptic and postsynaptic sites, exclusively at excitatory synapses, but not inhibitory synapses, in hippocampal neurons."}
{"protein": "MEAIKGSEVNVPDAVFAWLLDGRGGVKPLEDDDVIDSQHPCWLHLNYTHPDSARWLASTPLLPNNVRDALAGESSRPRVSRMGEGTLITLRCINGSTDERPDQLVAMRLYMDERLIVSTRQRKVLALDDVVSDLQEGAGPTDCGGWLVDVCDALTDHASEFIEQLHDKIIDLEDNLLDQQIPPRGFLALLRKQLIVMRRYMAPQRDVYARLASERLPWMSDDHRRRMQDIADRLGRGLDEIDACIARTGIMADEIALVMQESLTRRTYTMSLMAMVFLPSTFLTGLFGVNLGGIPGGGWRFGFSLFCILLVVLIAGVTLWLHRSKWL", "text": "FUNCTION: Zinc transporter. Acts as a Zn(2+):proton symporter, which likely mediates zinc ion uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family."}
{"protein": "MAQVSINRDLGEWGLSTDSGERARLLQSPSVDIAPKSEGEAPPGGVGGGTTSTLGAIFIVVNACLGAGLLNFPAAFSTAGGVAAGITLQMAMLVFIISGLVILAYCSQASNERTYQEVVWAVCGKLTGVLCEVAIATYTFGTCIAFLIIIGDQQDKIIAVMAKEPEGPGGSPWYTDRKFTISLTAFLFILPLSIPREIGFQKYASFLSVVGTWYVTAIIIIKYIWPDKEMTPADILNRPASWIAVFNAMPTICFGFQCHVSSVPVFNSMRQPEVKTWGGVVTAAMVIALAVYMGTGICGFLTFGDAVDPDVLLSYPSEDMAVAVARAFIILSVLTSYPILHFCGRAVIEGLWLRYQGMPVEEDVGRERRRRVLQTLVWFLLTLLLALFIPDIGKVISVIGGLAACFIFVFPGLCLIQAKLSEMEEVKPASWWAMVSYGVLLVTLGAFIFGQTTANAIFVDLLA", "text": "FUNCTION: Symporter that selectively cotransports sodium ions and amino acids, such as L-glutamine and L-asparagine from the lysosome into the cytoplasm and may participates in mTORC1 activation. The transport activity requires an acidic lysosomal lumen. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Cell projection, axon Note=In neurons, located in soma. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
{"protein": "MKHIALLTTLLLSASLQAVEKPYDYVFFENSLMKGDYFYSQAKYTSPSWIKNARHHLPVAGSVAFTPGNSLELTYVSAPGGDWYSEIQYCPVRGNDFFREPSTLSMQVRLRESMNAAALPNIAIRYADSTYTQYLNLRNYLKDTRPGVWHPVSIPLEDFGLNAVNDTNIKKLAAVALRPGTADGNEYTIYLDDIELLPASLPSVSALNAPVLQEAKAYERHIDIKWIPQSKEDIKYYRIYRSFDGITYQPVAVRRPWMNRYTDFLGEVGKKAYYKVTAVDYALNESNDSQTVSATTYPMTDEQLLDMVQEANFRYYWEGAEPNSGLARENIPGRNDMIATGASGFGIMAIVAGIERGFITREEGVQRFLKITSFLEKADKFHGAVSHFIDGTTGKTVAFFGPKDNGGDLVETSFLFQGLLTARQYFNQENDKEKQIRKSIDNLWKNVEWSWYKQFKDSPYLYWHWSPDQAWVINHKLIGWNETMITYMLAIMGPKYGISPEMYYSGWASQEEYAQEYRADWGRVEDGKMYTNGNTYYGENLKVGVSNGGPLFFIHYSYLGLDPHKFTDKYTNYFENNQKMAKINQRYCIENQGGYVGYGEDCWGLTASDFAWNYQAQEPMPHRDNGTMAPTGALASFPYTPDASMKALRNYYRNHGSFLWGEYGFRDAFNLTVNWVSPLFMGLNQAPVTVMIENYRTNLLWNLFMSHPDVQKGIQKIQSIK", "text": "FUNCTION: Catalyzes the hydrolysis of linear beta-1,2-glucan and beta- 1,2-glucooligosaccharides with degrees of polymerization (DPs) greater than or equal to 4, to produce sophorose. The best substrates are tetra- and pentasaccharides. Acts as an exo-type enzyme that releases sophorose from the non-reducing end of the substrate. It cannot hydrolyze cyclic beta-1,2-glucans. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MAASFVIVIVISFFISLAFMCYVHYTSRQRRKLHGYGHEKAVRLPPGSMGWPYIGETLQLYSQDPNVFFASKQKRYGEIFKTHILGCPCVMLASPEAARFVLVTQAHLFKPTYPRSKERMIGPSALFFHQGDYHLRLRKLVQGPLGPDALRALVPDVEAAVRSTLASWDGNVSSTFHAMKRLSFDVGIVTIFGGRLDERRKAELRQNYAIVEKGYNSFPNSFPGTLYYKAIQARRRLHGVLSDIMRERRARGEPGSDLLGCLMQSRAGDDGALLTDEQVADNIIGVLFAAQDTTASVLTWIVKYLHDHPKLLEAVRAEQAAIRAANDGGRLPLTWAQTRSMALTHKVILESLRMASIISFTFREAVADVEYKGFLIPKGWKVMPLFRNIHHNPDYFQDPQKFDPSRFKVSPRPNTFMPFGNGVHACPGNELAKLEMLVLIHHLVTGYRWEIVGSSDEVEYSPFPVPKHGLLAKLWRDDSVSVETDGCQNGDNDDNGVAMV", "text": "FUNCTION: Involved in the oxidative degradation of abscisic acid. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MEEKYSSNVMSSGRLGPVDAPESRLTRYIVLLCFTKFLKALGIFESYDLLKVVHIVQFIFILKLGSTCFMVLFQKPFSSGKSITKRQWVSIVKHAFVSCIISLLWFFGLTLCGPLRTLLLFEHSDIVVISLLTVLFTGSGGGPSKTRGAAFFIIAVICLLLFDNDDLMAKIAEHPEGHHDSALTHFLYRAFFLLGVADHKGGVLLLVLALCFNVGFHTASRKLSLDIGGAKRLQALSHLVSVIILSPWVIILSATTESKIESWSALIMPFMTVIFSVMIMDFYVESVCSVKMEPSKCARYGSFLIFASALLLGNFWTHPITDQLRAMNKPAHQLHTEHVLSGGVVVSAIFFILSAQILASSSRKGQRGTLVGYSPEGTPLYNFMGDALHNTSPSMPRFLKDSLKQILEEYDSRQIFYFLCLNLAFTFVEIFYGVWTNSLGLLSDGFHMLFDCSALVMGLIAALMTRWKATRIFSYGYGRVEILSGFINGLFLVVIAFFVFIEAVARIYDPPDINTDMLTPVSVGGLIVNLVGICAFSHAHSHGAARGGCPSHDHGHSHHGHGHSHGHNHGHSHSDHGHNHGHTHNHGHSHGSAGVGMNANMRGVFSHVLADTLGSVGVIVSTILIRQFGWLIADPLCSLFIAVLIFGSVLPLLKDACQVILLRIPQETEKGINIALEKISNLDGLISYRDPHFWRHSASLVAGTIHVQVMSDVVEQRIIQQVTSLLKDAGVNNLTVQVEKEAYFQHMSGLSTGFQDVLIMTKQMDTIKYYKDGTYIM", "text": "FUNCTION: Together with SLC30A6 forms a functional proton-coupled zinc ion antiporter mediating zinc entry into the lumen of organelles along the secretory pathway. By contributing to zinc ion homeostasis within the early secretory pathway, regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosynthesis. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Note=Enriched in early compartments of the secretory pathway including COPII-coated vesicles and the Golgi cis cisterna. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
{"protein": "MNGSGSQGAENTSQEGGSGGWQPEAVLVPLFFALIFLVGTVGNALVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDDWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLALLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDLCTFVFSYLLPVLVLSLTYARTLRYLWRTVDPVTAGSGSQRAKRKVTRMIIIVAVLFCLCWMPHHALILCVWFGRFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRKICAGLLRPAPRRASGRVSILAPGNHSGSMLEQESTDLTQVSEAAGPLVPPPALPNCTASSRTLDPAC", "text": "FUNCTION: Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MDKVLHATSLPILPGAIMSKNDAPEVEQLFKENGRLYQVWPRDRYLLPADQTEQDRLDIFSQLFKIILKEKLHTDASRVEENSHVLDLGCGTGLWVILMAHELHPKPSLFIGADVQMTQPDLIPATVRFTPADIEAPWTDEMVQHAPYDLINCRLMKGAIRSWPALYEKIAAHLKPETGVFEQFEIDWQFRCDDGPIPPALKQWSDEVMQAMDQHGMSIRCNREETRSMLLNHGFDDVQEQAIVLPISNWAEDERGREIGRWFNLALNHSTLPMSLAPLFRVMKKTPQYIDELNKAASREVCSQAHTDGVYCMLYIWTARTRPSRRR", "text": "FUNCTION: Secondary metabolism regulator that controls the expression of the tenuazonic acid biosynthesis cluster (PubMed:28820236). Methyltransferase that performs automethylation (By similarity). No other methyl-accepting substrate has been identified yet (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the methyltransferase superfamily. LaeA methyltransferase family."}
{"protein": "MLAVALLVLLCASASANSIQSRTSSYSGEYGGKGGKRFSHSGNQLDGPITAFRIRVNRYYIVGLQVRYGTVWSDYVGGTQGDLEEIFLHPGESVIQVSGKYKSYVKQMIFVTDKGRYLPFGKASGTSFNAVPLHPNTVLRFISGRSGSAIDSISLHWDTYPSHCNTC", "text": "FUNCTION: May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Zymogen granule lumen Golgi apparatus lumen. SIMILARITY: Belongs to the jacalin lectin family."}
{"protein": "MAALWLLLLVLSLHCMGAGGFVAHVESTCVLDDAGTPQDFTYCVSFNKDLLACWDPIVGKIVPCEFGVLYPLAENFSRILNKEESLLQRLQNGLPDCASHTQPFWNALTHRTRPPSVRVAQTTPFNTREPVMLACYVWGFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDWTPGLSPIQTVKVSVSAATLGLGFIIFCVGFFRWRKSHSSSYTPLSGSTYPEGRH", "text": "FUNCTION: Plays a critical role in catalyzing the release of class II- associated invariant chain peptide (CLIP) from newly synthesized MHC class II molecules and freeing the peptide binding site for acquisition of antigenic peptides. SUBCELLULAR LOCATION: Late endosome membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Note=Localizes to late endocytic compartment. Associates with lysosome membranes. SIMILARITY: Belongs to the MHC class II family."}
{"protein": "MEASKESPSAFKTPCKPAKVKSPVNACGTPVTIPASPFMKKLGCGTGVNVYLMNRMGKQTHSPWAIKKINSKCAQGQVSVYQKRLCEEAKILKDLKHPNIVGFRAFTTAKDGSKCLAMEFGGEQSLNDLIEKRREEGLQAFPVDTIEKVALHVARGLLYLHNEKKLLHGDMKSCNVVIKGDFESIKICDVGVSLPLDENMQVSDPKAHYIGTEPWKPKEALEDGVITDKADIFAYGLTLWEMMTLSVPHLEMLDTEGDEDDDDESFEEDFDEDAYYERLGSRPALDAVTLGGSYQRMVELFCLCTEEDPQKRPSAAHIVQVLESNSQLSKQNTEVIVID", "text": "SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily."}
{"protein": "MNVMRRLKSIASGRTSISSDPGGDYALKRAKLDQENDNLCVDPMQVDQNSSCFEMKADVLSQESVAGTSNVPAVSEKPVDDQLPDVMIEMKIRDERNANREDKDMETTVVNGSGTETGQVITTTVGGRDGKPKQTISYMAQRVVGTGSFGVVFQAKCLETGEQVAIKKVLQDKRYKNRELQIMRLQDHPNVVRLRHSFFSTTDKDELYLNLVLEYVPETVYRASKHYTKMNQHMPIIFVQLYTYQICRALNYLHRVVGVCHRDIKPQNLLVNPQTHQLKICDFGSAKMLVPGEPNISYICSRYYRAPELIFGATEYTNAIDMWSGGCVMAELLLGQPLFPGESGIDQLVEIIKILGTPTREEIRCMNPNYTEFKFPQIKAHPWHKIFHKRMPPEAVDLVSRLLQYSPNLRCTALEACAHPFFDDLRDPNVSLPNGRALPPLFNFTAQELAGASTELRQRLIPAHCQGTGSSS", "text": "FUNCTION: May mediate extracellular signals to regulate transcription in differentiating cells. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily."}
{"protein": "MAAQRRSLLQSEQQPSWTDDLPLCHLSGVGSASNRSYSADGKGTESHPPEDNWLKFRSENNCFLYGVFNGYDGNRVTNFVAQRLSAELLLGQLNTEHTEADVRRVLLQAFDVVERSFLESIDDALAEKASLQSQLPEGVPQHQLPPQYQKILERLKALEREISGGAMAVVAVLLNSKLYVANVGTNRALLCKSTVDGLQVTQLNMDHTTENEDELFRLSQLGLDAGKIKQMGVICGQESTRRIGDYKVKYGYTDIDLLSAAKSKPIIAEPEIHGAQPLDGVTGFLVLMSEGLYKALEAAHGPGQANQEIAAMIDTEFAKQTSLDAVAQAVVDRVKRIHSDTFASGGERAKFCPRHEDMTLLVRNFGYPLGEMSQPTPTPAPGGRVYPVSVPYSSAQSTSKTSVTLSLVMPSQGQMVNGSHSASTLDEATPTLTNQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEFYRLWSVDHGEQSVMTAP", "text": "FUNCTION: Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines (PubMed:12464436, PubMed:28073917). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation. Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:24037507). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism. Plays also a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits (By similarity)."}
{"protein": "MINSPRVCIQVQSVYIEAQSSPDDERYVFAYTVTIRNLGRAPVQLLGRYWLITNGHGRETEVQGEGVVGVQPRIAPGEEYQYTSGAVIETPLGTMQGHYEMIDENGDAFTIDIPVFRLAVPTLIH", "text": "FUNCTION: Not known; mutations in apaG/corD give a phenotype of low- level Co(2+) resistance. They also decrease Mg(2+) efflux but not influx via the CorA Mg(2+) transport system."}
{"protein": "MKPVERAKLVRSLRQESRRLRLLVLVIGFFLVTLTFVVISKPDALLFNLNGRLSVDHAPRSLLIRQRIHADSRRSADTFPAAEDPKVVDEDEGAEDATAKGTSEEEKRLLSSEPEQGKNEEAATASEVLGGGGEEDNKNGEEEGHTQHSKVTLPTVSNYTIRDAEDTDNGKQEDGKPNEKYEFEMDADKGDNVEPETDNEEWNKKPLCDFSNFRANVCEMRGNIRIHPNASSVMYMEPASSKREEIWKVKPYPRKGDELCLGHITEITVKSSKVAPECSKYHNVPAVVFALTGYTGNLFHDFTDVLVPLFTTASEFNGEVQFLITDMAIWWTRKYKVVFDKLSKYPLIDFNNDDQVHCFKHAIVGLHAYMEFTIDSSKAPHNYSMVDFNRFMRRTYSLPRDFVTALGEIPKAKPRLLIISRQRTRMFLNLNEIVAMAEEIGYEVVVEEANVSSDLSHFGKVVNSVDVMMGVHGAGLTNCVFLPQNATLIQIVPWGGLDWISRIDFGNPAEQMGLRYKQYSIGVHESSLTDQYPLDHEIFTNPLSFHKHGFEFIRQTFMDKQNVKLDCNRFKPVLLEVLDQLNQ", "text": "FUNCTION: Glycosyltransferase involved in the arabinosylation of xylan, the major hemicellulose (non-cellulosic component) of primary and secondary walls of angiosperms (PubMed:22215597). Possesses alpha-1,3- arabinosyltransferase activity, transferring an arabinofuranose residue to the xylan backbone (PubMed:22215597). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 61 family."}
{"protein": "MSFRGGGRGGFNRGGGGGGFNRGGGSNNHFRGGGGGGGGSFRGGGGGGGGSFRGGGRGGFGRGGGRGGFNKFQDQGPPERVVLLGEFMHPCEDDIVCKCTTEENKVPYFNAPVYLENKEQVGKVDEIFGQLRDFYFSVKLSENMKASSFKKLQKFYIDPYKLLPLQRFLPRPPGEKGPPRGGGGGGRGGRGGGRGGGGRGGGRGGGFRGGRGGGGGFRGGRGGGGFRGRGH", "text": "FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, Cajal body Note=Also localized to Cajal bodies (coiled bodies). SIMILARITY: Belongs to the GAR1 family."}
{"protein": "MESNRGQGSIQQLLAAEVEAQHIVNAARTAKMARLKQAKEEAEKEIAEYKAQTEQDFQRKLEETSGDSGANVKRLEQETDTKIEQLKNEASRISKDVVEMLLKHVTTVKN", "text": "FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Cell membrane Vacuole membrane; Peripheral membrane protein. SIMILARITY: Belongs to the V-ATPase G subunit family."}
{"protein": "MSWWWAGAIGAARKKFEEDDAPRDCQSVALIIGVTGIVGNSLAEILPISDTPGGPWKVYGVARRPRPAWNADHPVEYIQCDISDASDTHTKLSPLTDVTHIFWVTWANRPTESECCELNGTMLRNVLNALIPKAANLHHICLQTGHKHYIGPFEAFGKIKPHEPPFTEDMPRLNAPNFYYTLEDMLVEASEKKAGLNWSVHRPAVIFGFSPFSMMNIIGTLCVYAAICKHENTPLKFPGTKAAWNCYSVASDADLIAEHQIWAAVDPYAKNEAFNCSNGDLFKWKHLWKVLAEQFGVEYAEFDESEKPTSLVERMKDKGPVWEEIVRENGLHTTKLEGVATWWFADVILGGECLLDSMNKSKEHGYLGFRNTKNSLISVIDKMKAHKIVP", "text": "FUNCTION: Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8- oxogeranial as substrate. Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-inflammatory, antifungal and antibacterial activities. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. Highly divergent."}
{"protein": "MNMSVLTLQEYEFEKQFNENEAIQWMQENWKKSFLFSALYAAFIFGGRHLMNKRAKFELRKPLVLWSLTLAVFSIFGALRTGAYMLYILMTKGLKQSVCDQSFYNGPVSKFWAYAFVLSKAPELGDTIFIILRKQKLIFLHWYHHITVLLYSWYSYKDMVAGGGWFMTMNYGVHAVMYSYYALRAAGFRVSRKFAMFITLSQITQMLMGCVINYLVFNWMQHDNDQCYSHFQNIFWSSLMYLSYLVLFCHFFFEAYIGKVKKATKAE", "text": "FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ELO family. ELOVL6 subfamily."}
{"protein": "MTAELPPQIQNQIAQLQQIQQQIQALAMQKSQVEAMQKESKMALDELGRLADDAVVYRNVGELVIKTSKEESITKLKDREETLSLRLQSISRQEERLTSRFKQLQEQIQQALGPRAQ", "text": "FUNCTION: Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin subunit beta family."}
{"protein": "MSAEKTENLSWIDKRFPLSETWRNHLSEYYAPKNLNFWSFFGSLAILTLVIQIVTGVWLAMSYKPDAGLAFASVEYIMRDVDWGWLIRYMHSTGASMFFIVIYLHMFRGLLWGSYRKPRELLWMIGVVIYLVMMATAFFGYLLPWGQMSYWGAQVIVNLFAAVPVVGEDLSVWVRGDFVISDATLNRFFAFHFLLPFLLAGLVFLHIVALHHVGSNNPDGIEIKEGPKGNRWSDKAPADGIPFHPYYTVKDLMGVVVFLAIFGYVMFFNPTMGGLFLEAPNFQPANPMQTPAHIAPVWYFTPFYAMLRAVPPMYGSQFPGVVVMFAAILILFVLPWLDRSPVKSMRYKGPIFKWATGIFVVSFVALAWLGIQPASDFYTLLSQIFTVLYFAYFLLMPIYSSLDKTKPVPERVTS", "text": "FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family."}
{"protein": "MASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGSKSENAGAQGWLAALKPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGSHPTAFVVSYAAALPAAALWHKLGSLWVPGGQGGSGNPVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQAPADAPE", "text": "FUNCTION: ABC transporter associated with antigen processing. In complex with TAP2 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules (PubMed:25656091, PubMed:25377891). Uses the chemical energy of ATP to export peptides against the concentration gradient (PubMed:25377891). During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle (PubMed:25377891, PubMed:25656091, PubMed:11274390). Typically transports intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome. Binds peptides with free N- and C-termini, the first three and the C-terminal residues being critical. Preferentially selects peptides having a highly hydrophobic residue at position 3 and hydrophobic or charged residues at the C-terminal anchor. Proline at position 2 has the most destabilizing effect (PubMed:7500034, PubMed:9256420, PubMed:11274390). As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation (PubMed:26611325, PubMed:1538751, PubMed:25377891). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=The transmembrane segments seem to form a pore in the membrane. SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. MHC peptide exporter (TC 3.A.1.209) subfamily."}
{"protein": "MTAAEAPLPPLAPRERTATTAAERRTGSPLAVSLSGVRKSFGDKTVLSGIDLEITRGEFVVLLGPSGTGKTTLLRLLSGLEPPDGGDVLVPRQRTVVYQEPRLIPSKRVLANVSVGQKRAQLTRDNARRALAEVNLADKERAWPATLSGGEAQRVALARALVREPELLLLDEPFAALDALTRLQMQDLVGDLVARHRPAVLLVTHDVDEAVRLADRVLILDNGGFAVDVDIDLPRPRDRNDPEALRYRATFLAQLGVGRPSSTRQDIS", "text": "FUNCTION: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Aliphatic sulfonates importer (TC 3.A.1.17.2) family."}
{"protein": "MQNYKYDKAIVAESKNGGSPALNNNPRKGGSKRVLLICLDLFCLFMAGLPFIIIETSTIKPYHRGFYCNDESIKYPQKTGETINDAVLTAVGIVIAILAIITGEFYRIYYLKEKSRSTIQNPYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLNVCNPDFSQINCSVGYIQNYRCRGEDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPPSAIRKDMLSPVDIDRSNHHNMV", "text": "FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1- phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z- octadecenoyl)-ethanolamine phosphate, a potential physiological compound. Has both an extracellular and an intracellular phosphatase activity, allowing the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes. Through the dephosphorylation of extracellular sphingosine-1-phosphate and the regulation of its extra- and intracellular availability, plays a role in vascular homeostasis, regulating endothelial cell migration, adhesion, survival, proliferation and the production of pro- inflammatory cytokines (By similarity). By maintaining the appropriate levels of this lipid in the cerebellum, also ensure its proper development and function (By similarity). Through its intracellular lipid phosphatase activity may act in early compartments of the secretory pathway, regulating the formation of Golgi to endoplasmic reticulum retrograde transport carriers (By similarity). FUNCTION: Independently of this phosphatase activity may also function in the Wnt signaling pathway and the stabilization of beta- catenin/CTNNB1, thereby regulating cell proliferation, migration and differentiation in angiogenesis or yet in tumor growth. Also plays a role in integrin-mediated cell-cell adhesion in angiogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Membrane raft; Multi-pass membrane protein Note=Cycles between the endoplasmic reticulum and the Golgi. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family."}
{"protein": "MAKEINNDTIAKFENDLNNHPVFNVASHAAQENGIYKASQNLQTKIDLDPIFSIEIDTGKPADQKQSGRCWMFSALNTMRHPLQKKFKLQDFELSQNYTNFWDKFEKSNWFFENVIATADKDLGDRKVSFLFATPQQDGGQWDMLCGIIEKYGIVPKSVYPETANATNSSALNDTLNTLLRKDGLELRRLVNAGKSEDEVQARKEEMLNDVFRVLAISTCVPPKKFNFEYRDDNHNYHIDKDITPKEFFDKYVGMDLANHISTINAPTSDKPFHKVFSVEYLGNVEGGRQVRHLNLKVDEMKDLIIKQLNNGEVVWFGSNVVKDSERRAGLLATNLYRRDQLFDVDFSMSKADKLDSGESMMDHAMVITGVDIVDGKPTKWKIENSWGEKPGFKGYFVMSDSWFDSFVYQAVINKDILPEDLKKAYDEGKDNPIQLLPWDPMGALAFKY", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MNKYIIFDNTKLLEYIGKNSLITPCYIYDLELLEDTFLNAKKSLDKNFKNAEIHYAIKANHNPKIVGIAKKYGMGIDCVSGGEIKRALEQKVDSQHIVFARFEIELAIDNDIFAFNSESLEEIQVINQIAQRKNKQVNICLRVNPNIDAQTHHYISTGQFDDKFGIAFVDILNWLKDEYRNFANINIIGLHYHVGSQILNYQVFQSLAITTNEHIKLLRQNDINIKHINFGGGLGIDYQNPQQNPIVDFDGYFARFREFFKYSDELVLHFELGRSLVGQSGVLVSQVLFNKVTQGTHFVIIDAGMTELIRPALYQAQHKIAALIDENINQKQHYHIVGPICESSDVFAKYYQLPKLKRGDLLAIYSAGAYGKVLASEYNLRPSVQEYFI", "text": "FUNCTION: Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily."}
{"protein": "MAKSQIALCCMSHSPLLNLPGPAQELLDEIDKAIAAARDFVAEFDPELVVTFSPDHYNGFFYRAMPPFCIGTAAEGVGDYGTHEGPLDVPSDLATDCARAVLDHDVDVALSAAMDVDHGTVQPLQKLFGDATAKPVIPVFINSVATPLGPIRRVRALGAAVGAHLATLGKRVLVIGSGGLSHDPPVPTLATAPPAALDRIVRGVPMTTDQRQARQTAVIEAAREFASGRGTLAPLNPDWDRAFLDIVDSGRLAEVDGWDNGWIAEQAGNSAHEVRTWIAAFAALAAQGEYVTENRFYRAAPELIAGFAIRTAVTT", "text": "FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6- ketononatrienedioate, respectively. SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family."}
{"protein": "MKVFILALLALTATTAIAQLETTCSQGFGQYQQQQQPGQRQLLEQMKPCVAFLQQQCRPLRMPFLQTQVEQLSSCQIVQHQCCQQLAQIPERIRCHAIHSVVEAIMQQQSQQQWQERQQQAQHKSMRMLLENLSLMCNIYVPVQCQQQQQMGQQQQQQQLQEQLTPCATFLQHQCSPVTVPFPQIPVDQPTSCQNVQHQCCRQLSQIPEQFRCQAIHNVAEAIRQQQPQQQWQGMYQPQQPAQHESIRMSLQALRSMCNIYIPVQCPAPTAYNIPMVATCTSGAC", "text": "FUNCTION: Seed storage protein. Might be integrated via inter-chain disulfide bonds within the glutenin polymer. SIMILARITY: Belongs to the prolamin family."}
{"protein": "MKNERHVLIVFPHPDDESYCVAGTILAYTQRNVPLTYVCLTLGEMGRAMGNPPFATRESLYAIREKELKRATNILGIKDLRMMGYRDKTLEFETPGELRRVIQKCVEELNPSLVISFYPGYAVHPDHDATGEAVAEALATIPENKRPTFYAVAFANNHEAEIGPPHVKNEVKEYVPKKLEALQAHASQFATKVTELKREYEDGVTETVEWLEREPFWIYPFKDKNK", "text": "FUNCTION: Involved in bacillithiol (BSH) biosynthesis. Catalyzes the second step of the pathway, the deacetylation of N- acetylglucosaminylmalate (GlcNAc-Mal) to glucosamine malate (GlcN-Mal). Could also be involved in bacillithiol-detoxifying pathways through formation of S-mercapturic adducts. SIMILARITY: Belongs to the PIGL family."}
{"protein": "MDVHDLTRAPPEYLEVVWVTDVCKLVMAVGWLSNYIGMIAKSIKEQTYSMALMPLCCNFAWEFTYFFIYPYKVPMERNIHTLAFLLNCGVMYTAVRYGAREWGHAPLVQRNLPVIFVVCIACWVSAHVAFAEQYGPSLAQAVSGFACQILLSAGGTCQLLCRGHSRGASYKLWLARFMGSFALILPNMLRYKYWRDDHQYIGSPLYIWFLGMFLFLDGSYGFVLWYVRRHEREQVLVAKPKVQ", "text": "FUNCTION: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones subglutinols A and B (PubMed:32286350). The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpasA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (PubMed:32286350). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpasD through the action of the prenyltransferase dpasC to yield a linear alpha-pyrone diterpenoid (PubMed:32286350). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpasE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpasB (PubMed:32286350). The FAD-linked oxidoreductase dpasF is then involved in tetrahydrofuran (THF) ring formation at the C5 unit to complete the formation of subglutinols A and B (PubMed:32286350). DpasF possesses also an additional catalytic ability of multi-step oxidations to generate a new DDP analog with an enone system at the C5 named FDDP A (PubMed:32286350). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the paxB family."}
{"protein": "MASSCELCCEIFIAILLPPVGVCLRHGCCTVEFFICLILTCLGYLPGIIYAIYAICFLHRDEYFDEYRRPIYYVA", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0057 (PMP3) family."}
{"protein": "MVKDLLQNHMHPLGLCNNNDEEDLYEYGWVGVVKLEQPEMDLKPCLTVLGKAKRAVQRGATAVIFDISDNPDAVEQLNQGLDDPLKRPVVYMKGMDAIKLMNIVNKQKGARARIQHRPPRQPTEYFDMGIFLAFFVVVSLVCLILLIKIKLKQRRSQNSMNRMAVQALEKMETRKFKAKGKVSREGSCGGLDTLSSSSISDCAICLEKYIDGEELRVIPCTHRFHKRCVDPWLLQNHTCPHCRHNIIEQKKGGHGPGCVENSLSHGRQQQQQRVILPVHYPGRVQRTGPIAAYPTRTSMGPHGNPITVLTVERPVEPDLYPARTPTFLAGYRPVSLDHASSGHHCDLEHPPYPAPPAGHAFRRAKYNGRGFNNGTCYSQYETMYQHYYFQGLSFPHQQEVGGSQASRVVENGHNHSFHSGNMLYQPAPTMMHMAPPSSVESCYLHSQHQHRSVCSGYLADVPCSDSSSSSSASSAQGHASSSDSMLDCTEASNQGVYGSCSTFRSSLSSDFDPYVYRSCSPAKTGGGDAPASGGEGGTGRGRVECRSHQTFPNSPSRDRLSSCSMEMNYSSNSSLERRGAVLSSGTVPDASVSIAQSGGKDRRGPEKGCACCFQRQAGDPSSDCTTLYLGPEPHQTLGPSSSGGLYSVTSNILHRTDPGTVLGHPSRSCCLYEENHGSCYNEDYAVSIQYALAEAAAAAAAAAVAGCEAGQPIPIIPEDPGYEGGLEYVGHVSWEMEGDEEEVLYCQEGPCCMLEEETRALCRSTAKDRAGSTTGQDCHQTDTD", "text": "FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components (PubMed:22575959). Along with RSPO2 and RNF43, constitutes a master switch that governs limb specification (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ZNRF3 family."}
{"protein": "MLLLLLGILFLHIAVLVLLFVSTIVSQWLVGNGHRTDLWQNCTTSALGAVQHCYSSSVSEWLQSVQATMILSVIFSVLSLFLFFCQLFTLTKGGRFYITGVFQILAGLCVMSAAAIYTVRHSEWHVNNDYSYGFAYILAWVAFPLALLSGIIYVILRKRE", "text": "FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family."}
{"protein": "MSKARVYADVNVLRPKEYWDYEALTVQWGEQDDYEVVRKVGRGKYSEVFEGINVNNNEKCIIKILKPVKKKKIKREIKILQNLCGGPNIV", "text": "FUNCTION: The Nipponbare allele of HD6 contains a premature stop codon, resulting in a truncated non-functional product. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily."}
{"protein": "MGNGERGRPNKKMKYGGKDDQKMKNIQNAEDYYDDADEDSRDGEGEEKKRDFTKLELKPDHGNRPLWACADGRIFLETFSPLYKQAYDFLIAIAEPVCRPESMHEYNLTPHSLYAAVSVGLETETIISVLNKLSKTKLPKEMIEFIHASTANYGKVKLVLKKNRYFIESPFPEVLKRLLSDDVINRARFSSEPYYGGDGFSVGRTCGELEAGPGELLNEAEFAAAAEEKETHSFEIDPAQVENVKQRCLPNALNYPMLEEYDFRNDNVNPDLDMELKPHAQPRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVSAAARIKKSCLCLATNAVSVDQWAFQFKLWSTIRDDQICRFTSDSKERFRGNAGVVVTTYNMVAFGGKRSEESEKIIEEMRNREWGLLLMDEVHVVPAHMFRKVISITKSHCKLGLTATLVREDERITDLNFLIGPKLYEANWLDLVKGGFIANVQCAEVWCPMTKEFFAEYLKKENSKKKQALYVMNPNKFRACEFLIRFHEQQRGDKIIVFADNLFALTEYAMKLRKPMIYGATSHIERTKILEAFKTSKDVNTVFLSKVGDNSIDIPEANVIIQISSHAGSRRQEAQRLGRILRAKGKLEDRMAGGKEEYNAFFYSLVSTDTQEMYYSTKRQQFLIDQGYSFKVITSLPPPDAGSSLSYHSQEEQLSLLGKVMNAGDDLVGLEQLEEDTDGMALQKARRSMGSMSVMSGSKGMVYMEYNSGRHKSGQQFKKPKDPTKRHNLFKKRYV", "text": "FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription (By similarity). Required during the early stages of development, including seed germination (PubMed:11737776). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily."}
{"protein": "MKDFNDIETIDFAETGCSFTREAIASGGYYQALKTPTCKEISGRRYKGTNTPDAVRDLWSTPREVIAYLEGRYGKYDLDAAASEENKVCEKFYSQETNCLKRWWGKNKHVWLNPPYSRPDIFVKKAIEQMEHNNQIDMLLPADNSTAWFTEARQNAAEIIWIEADLTEDIDGNEYARSGRLAFISGETGKAVDGNNKGSVIFIMRELKEGEVQQTHYIPITSICPSVKNKRAKVRKVD", "text": "FUNCTION: Methyltransferase that methylates adenine residues in the dsDNA sequence 5'-GATC-3' (PubMed:2180941, PubMed:3312202). May prevent degradation of viral DNA by the host restriction-modification antiviral defense system (PubMed:376871). SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MKEENEYIVKRRKKRRRKRITIFLFLLICILVTLCLKLPYFNIKYINVEGNKIIKSDNIIENSKLKKGNNIFYLNLNKYKDNIMQDPYIKNVSIRQKLPNTIDIIVKERQAVFYINSGENYFIIDKNGVLLEIRKNISGMNLIKLDGVTLKNGKIGTEIPCDSRRLELINQITSVSIKDNNLKITDVDMSHILSLKVYFKNMCVVIGTPDDIYNKLNEAVNVIISQKLIDKKGYVDVSFKGNPVYSLQQ", "text": "FUNCTION: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the FtsQ/DivIB family. DivIB subfamily."}
{"protein": "MFSITTLRDWTPDPGSIICWHASPTAKAKARQAPISEVPPSYQQAQHLRRYRDHVARGLDMSRLMIFTWDLPGRCNIRAMNYAINAHLRRHDTYHSWFEFDNAEHIVRHTIADPADIEVVQAEHQNMTSAELRHHIATPQPLQWDCFLFGIIQSDDHFTFYASIAHLCVDPMIVGVLFIEIHMMYSALVGGDPPIELPPAGRYDDHCVRQYADTAALTLDSARVRRWVEFAANNDGTLPHFPLPLGDLSVPHTGKLLTETLMDEQQGERFEAACVAAGARFSGGVFACAALAERELTNCETFDVVTTTDTRRTPTELRTTGWFTGLVPITVPVASGLFDSAARVAQISFDSGKDLATVPFDRVLELARPETGLRPPRPGNFVMSFLDASIAPLSTVANSDLNFRIYDEGRVSHQVSMWVNRYQHQTTVTVLFPDNPIASESVANYIAAMKSIYIRTADGTLATLKPGT", "text": "FUNCTION: Required for the biosynthesis of sulfolipid-1 (SL-1), a major mycobacterial cell wall lipid (PubMed:17259623, PubMed:17592143, PubMed:22194604). Catalyzes the acylation of trehalose-2-sulfate by adding the palmitoyl group at the 2'-position to yield the intermediate trehalose-2-sulfate-2'-palmitate (SL659) (PubMed:17592143, PubMed:22194604). FUNCTION: Catalyzes the acylation of trehalose-2-sulfate by adding the palmitoyl group at the 2'-position to yield the intermediate trehalose- 2-sulfate-2'-palmitate (SL659). FUNCTION: Required for the biosynthesis of sulfolipid-1 (SL-1), a major mycobacterial cell wall lipid. Catalyzes the acylation of trehalose-2- sulfate by adding the palmitoyl group at the 2'-position to yield the intermediate trehalose-2-sulfate-2'-palmitate (SL659). SIMILARITY: Belongs to the PapA acyltransferase family."}
{"protein": "MEPIHNPPPQTCSYSRSSTTYTSFKDASCDTKVIRIIIALFLIVISCGLILCAYTFRDLLDADYLAQEGPQQATKLLQQLDDVLTGPPLPIWDNEHLFQFSCLMQNKHKRVLPIDICNPLTKFNFLECICNCLMTKQSVNVNETDMCELFCPPTCTPENYRRLLCTSSVFPFVMWHDPSADTQEAMLTKMDQTMSSGRVGNSHWVLVIVDIEYRCVTFFDSLCDYVASPQQMREQLEGLAVSLGAIYPKEGGADSDQEELLSPFQVRIGSTVKVQSPGEFTCGAWCCQFLAWYLENPDFDLEEKVPKNPSERRALLADFISTTEQAMSRYSSLSWPTTD", "text": "FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease possesses deubiquitinating and deneddylating activities (By similarity). SUBCELLULAR LOCATION: Secreted Host cell Membrane; Single-pass membrane protein Note=Secreted, and delivered into the host cell. SIMILARITY: Belongs to the peptidase C48 family."}
{"protein": "MEGECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLKSQELHELYEGLKVNDVNKYDYVLTGYTRDKSFLAMVVDIVRELKQQNSRLVYVCDPVMGDKWNGEGSMYVPQDLLPVYRDKVVPVADIITPNQFEAELLSGRKIHSQEEAFEVMDMLHCMGPDTVVITSSDLPSSQGSDYLIALGSQRMRKPDGSTVTQRIRMEMRKVEAVFVGTGDLFAAMLLAWTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAGEGQKPSPAQLELRMVQSKRDIEDPEIVVQATVL", "text": "FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (By similarity). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the pyridoxine kinase family."}
{"protein": "MNIKPASEASLKDWLELRNKLWSDSEASHLQEMHQLLAEKYALQLLAYSDHQAIAMLEASIRFEYVNGTETSPVGFLEGIYVLPAHRRSGVATMLIRQAEVWAKQFSCTEFASDAALDNVISHAMHRSLGFQETEKVVYFSKKID", "text": "FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, kanamycin, tobramycin and netilmicin."}
{"protein": "MLDFGALPPEINSGRMYAGPGSGPLLAAAAAWDALAAELYSAAASYGSTIEGLTVAPWMGPSSITMAAAVAPYVAWISVTAGQAEQAGAQAKIAAGVYETAFAATVPPPVIEANRALLMSLVATNIFGQNTPAIAATEAHYAEMWAQDAAAMYGYAGSSATASQLAPFSEPPQTTNPSATAAQSAVVAQAAGAAASSDITAQLSQLISLLPSTLQSLATTATATSASAGWDTVLQSITTILANLTGPYSIIGLGAIPGGWWLTFGQILGLAQNAPGVAALLGPKAAAGALSPLAPLRGGYIGDITPLGGGATGGIARAIYVGSLSVPQGWAEAAPVMRAVASVLPGTGAAPALAAEAPGALFGEMALSSLAGRALAGTAVRSGAGAARVAGGSVTEDVASTTTIIVIPAD", "text": "SIMILARITY: Belongs to the mycobacterial PPE family."}
{"protein": "MAEDQLTAQAVAPPTEASAALEPALETPESPVETLKTSISASRRVRARLARRMTAQRSTTNPVLEPLVAVHREIYPKADLSILQRAYEVADQRHASQLRQSGDPYITHPLAVANILAELGMDTTTLVAALLHDTVEDTGYTLEALTEEFGEEVGHLVDGVTKLDRVVLGSAAEGETIRKMITAMARDPRVLVIKVADRLHNMRTMRFLPPEKQARKARETLEVIAPLAHRLGMASVKWELEDLSFAILHPKKYEEIVRLVAGRAPSRDTYLAKVRAEIVNTLTASKIKATVEGRPKHYWSIYQKMIVKGRDFDDIHDLVGVRILCDEIRDCYAAVGVVHSLWQPMAGRFKDYIAQPRYGVYQSLHTTVVGPEGKPLEVQIRTRDMHRTAEYGIAAHWRYKEAKGRNGVLHPHAAAEIDDMAWMRQLLDWQREAADPGEFLESLRYDLAVQEIFVFTPKGDVITLPTGSTPVDFAYAVHTEVGHRCIGARVNGRLVALERKLENGEVVEVFTSKAPNAGPSRDWQQFVVSPRAKTKIRQWFAKERREEALETGKDAMAREVRRGGLPLQRLVNGESMAAVARELHYADVSALYTAIGEGHVSAKHVVQRLLAELGGIDQAEEELAERSTPATMPRRPRSTDDVGVSVPGAPGVLTKLAKCCTPVPGDVIMGFVTRGGGVSVHRTDCTNAASLQQQAERIIEVLWAPSPSSVFLVAIQVEALDRHRLLSDVTRALADEKVNILSASVTTSGDRVAISRFTFEMGDPKHLGHLLNAVRNVEGVYDVYRVTSAA", "text": "FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp (By similarity). SIMILARITY: Belongs to the RelA/SpoT family."}
{"protein": "MLLSDLSSDQEATGSNSHGGGGGGDRMVVGSHGAAHVVLSNLFLPPAAAAAATMLLPAAPVMVRPAAMAAAQEPRAKKKRSLPGNPDPEAEVIALSPRALVATNRFVCEVCNKGFQRDQNLQLHRRGHNLPWKLRHRAAAVSAVTTAAPAPRKRVYVCPEPTCVHHDPARALGDLTGIKKHFSRKHGEKRWRCERCGKRYAVHSDWKAHVKNCGTREYRCDCGILFSRKDSLLTHRAFCDALAEESARLLAAANNSSSITTTTCNNSNISSNNNNNNINSISNSNNLLITSSSSSPPLFLPFSTTPAENPNPNQLLFLQQHQAAHHQLLLPQFQQPPSSPPAYFDHLAFGGGGGVITSSSCNDDNSSIAGDVMVAAGGDSVSFGLTSEGSVTMHAGDVGRRRLTRDFLGVDHDAGEVDELELDELPADLSTTAAACQGCNFAAATTVACCATDFTTGSRQYLGRLPPVNETWSHNF", "text": "FUNCTION: Transcription activator that acts as a flowering master switch in both long and short days, independently of the circadian clock (By similarity). Promotes flowering upstream of HD1 by up- regulating FTL1, FTL4, FTL5, FTL6, EHD1, HD3A and RFT1 (By similarity). Seems to repress FTL11 expression (By similarity). May recognize the consensus motif 5'-TTTGTCGTAAT-3' in target gene promoters (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MARKMLNDGEPDLKKGEEQGKVYDFDLFIIGAGSGGVRAARFSSNFGAKVGICELPFHPISSETIGGVGGTCVIRGCVPKKILVYGASYGGELQDARNFGWELNENVDFNWKKLLQKKTDEINRLNGIYKRLLSNAGVKLFEGEGKIASPNEVEVTQLDGTKLSYSAKHILIATGSRAQRPNIPGQELGITSDEALSLEEFPKRAVILGGGYIAVEFASIWRGMGSSVNLVFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLAQLIKTEDGIKVITDHGEELIADVVLFATGRSPNSKRLNLEKVGVEFDKAGAIVVDEYSRTNIPSIWAVGDVTNRLNLTPVALMEASLFAKTVFGGQASKPDYNDIPYAVFCIPPLSVVGLSEEQAVEQTKGDVLIFTSTFNPMKNTISGRQEKTVMKLVVDAQTDKVLGASMCGPDAPEIVQGIAIAIKCGATKAQFDSTVGIHPSSAEEFVTMRSETRRVTGGVKPKTNL", "text": "FUNCTION: Maintains high levels of reduced glutathione in the cytosol. May play a role in the restoration of the post-stress redox state of the cytosolic glutathione pool. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MRRRLRLRREALLTLLLGATLGLLLYAQQEGAAPTTSAPRAQGRAAPGPTPGLRVFQAPDTGAAPPAYEGDTPEPPTPTGPFDFGRYLRAKDQRRFPLLINQPHKCQGNGAFPRGPDLLIAVKSVAADFERRQAVRQTWGAEGRVQGALVRRVFLLGVPRGTGTVAGEAEAGTQTHWSALLRAESRAYADILLWAFDDTFFNLTLKEIHFLAWASDYCPDVRFVFKGDADVFVHVGNLLEFLAPRDPAQDLLAGDVIVQARPIRVRASKYYIPEAVYGLPAYPAYAGGGGFVLSGATLRRLAGACAQVELFPIDDVFLGMCLQRLRLTPEPHPAFRTFGIPRPSAAPHLHTFDPCFYRELVVVHGLSAADIWLMWHLLHGPNGPACARPWPVPAGPFQWGP", "text": "SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family."}
{"protein": "MERSLKNVLVVSCGFLLLFTAYGGLQNLQSSLYSEQGLGVATLSTLYASVLLSSMFLPPILIKKCGCKWTIVGSMCCYVVFSLGNFHANWYTLIPTSILLGLGAAPLWSAQGTYLTTMGNLQAEKVGKLGKDVVNQYFGIFFLVFQSSGVWGNLISSLVFGKMSMQEAIPEEQLMSCGAKDCLMGPAATNSTHHPSQQLIYTLLGIYTGCGVLAILLVAVFLESLEDKLENEGERRPRPPPLWSTLLSTFMLFRDKRLCLLMFLPLYSGFQQEFLSGEYTKSYVTCALGIHFVGYVMICFSAMTALCSLLYGKISKYTGRAALYALGAAIHFSCIVVFLLWHPNTNQLPVFFVLSGLWGMSDAVWQTQNNALFGVLFEENKEPAFANYRLGEAIGFVIAFGYSSFLCVSTKLYILLGVLSLAMVGYGTVEYLEVKAASKVLGAEKKNQAEEEEMKTKI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the unc-93 family."}
{"protein": "EVKYDPCFGHKIDRINHVSNLGCPSLRDPRPNAPSTSA", "text": "FUNCTION: Exhibits vasodilator, natriuretic and diuretic properties in animal models and human tissues. Acts by stimulating cGMP via the natriuretic peptide receptor A (NPR1). Is a poor agonist of the atrial natriuretic peptide receptor B (NPR2). Is not degraded by neutral endopeptidase (NEP/MME). Binds to atrial natriuretic peptide clearance receptor (NPR-C/NPR3), which may be responsible of the removal of DNP from the circulation. Increases calcium uptake and induces histamine release from rat peritoneal mast cells. Increases calcium-activated potassium (KCa) current in gastric antral circular smooth muscle cells by increasing cGMP production and activating inositol trisphosphate receptors (IP3Rs). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family."}
{"protein": "MASNLPVRSFSEVCCAEARAAIIQMENNPDETVCNRIWKIHRDLQSSDLTTTVQVMMVYRFISKRVPEGCFAILSGVNTGMYNPRELKRSYVQSLSSGTSCEFLRSLDKLAKNLLAVHVCSDVKMSLNKRQVIDFISGEEDPTLHTAEHLTSLALDDSPSAVVYSGWQQEAIKLHNTIRKIATMRPADCKAGKFYSDILSACDQTKELLDAFDQGKLAYDRDVVLIGWMDEIIKIFSKPDYLEAKGVSYQVLKNVSNKVALLRESI", "text": "FUNCTION: plays a role in virion budding and release by presumably binding the ribonucleocapsid and the host membrane. SUBCELLULAR LOCATION: Virion."}
{"protein": "MSDDIFLVTGGAGYIGSHTVIELINHGIKVVIADNLSNSSYDAVARIEFIVKQHVSHFIKVDIRNEKELNQVFSNHKISGVIHFAALKAVGESTKIPLEYYDNNVSGTIALLNVCKSNNVKTIVFSSSATVYGDVTRFGDNSMIPIPEHCPME", "text": "FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity). SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. SIMILARITY: In the C-terminal section; belongs to the aldose epimerase family."}
{"protein": "MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAADEADEADEE", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
{"protein": "MSALLGLPPEVQDTCISLGLMLLVVLFMGLARVIARQQLHRPMVHAFVLEFLATFQLCYCTHELQLLSEQDSGHPTWTLTLIYFFSLVHGLTLVGTASNPCGVMMQMILGGMSPEMGAVRLMAQLVSALCSRYCISALWSLSLTKYHFDERILACRNPINTDISKAIIIEAICSFIFHSALLHFQEVRTKLRIHVLAALITFLAYAGGSLTGALFNPALALSLHFPCFDESFYKFFVVYWVAPSLGVLLMILMFSFFLPWLHNNQLSNKKE", "text": "FUNCTION: Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway (By similarity). Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating in the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER. Plays a role in the proximal tubule function by regulating its endosomal acidification. May play a role in postnatal kidney development (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Cytoplasm Cytoplasm, perinuclear region Note=Localizes mainly to the periphery of lipid droplets. it accumulates partly in mitochondrial-associated endoplasmic reticulum membranes. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12 subfamily."}
{"protein": "MLSRFMSNTWCTPLRQAQRLFSSTTTMQATLNQIKRGSGPPRRKKISTAPQLDQCPQRKGVVLRVMVLKPKKPNSAQRKACRVRLTNGNVVSAYIPGEGHDAQEHSIVYVRGGRCQDLPGVKYHVIRGAGDLSGVVNRISSRSKYGAKKPSKS", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (PubMed:25609543, PubMed:28154081). uS12m is required for respiratory growth (PubMed:11780787). SUBCELLULAR LOCATION: Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
{"protein": "MNTSVPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPESPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPKSSPNTVKRPTKKGRDRGGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTVNPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC", "text": "FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM1 sub-subfamily."}
{"protein": "MMVYNGSQLESVEEGEAVAVPGPPPEPRAPEPGAPVPEPGLDLSLSPRSESPGRGRPNCSPGRRKGRADRRGGARKGRQVRFLLAPPSPVRSGPPPAAASSSEKPEAPQDLGTPVQQSSLALSLELQAARAAAGGQFDAAKAVEEQLRKSFQTRCGLEESVTEGLNVPRSKRLFRDLVSLQVPEEQVLNAALREKLALLPPQARAPPPKEPPGPGPDMTILCDPETLFYESPHLTLEGLPPLRLQLRPRPSEDTFLMHRTLRRWEA", "text": "FUNCTION: During centriole duplication, plays a role in the centriole elongation by promoting the recruitment of the microtubule-binding elongation machinery through its interaction with RTTN, leading to the centriole to centrosome conversion (By similarity). In addition may play a role in the primary cilia assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Recruited to the nascent daughter centriole early in the duplication cycle and localizes to the proximal centriolar lumen just above the cartwheel. Co-localizes with RTTN at the centriole. SIMILARITY: Belongs to the PPP1R35 family."}
{"protein": "MEGGAYGAGKAGGAFDPYALVRQPHTILRVVSWLFSIVVFGSIVNEGYLNSASEGEEFCIYNRNPNACSYGVAVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFLWFVGFCYLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPSTGPDPAGMGGTYQQPANTFDTEPQGYQSQGY", "text": "FUNCTION: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short- term and long-term synaptic plasticity (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Melanosome. SIMILARITY: Belongs to the synaptogyrin family."}
{"protein": "MAAAGGGGGGAAGRAYSFKVVLLGEGCVGKTSLVLRYCENKFNDKHITTLQASFLTKKLNIGGKRVNLAIWDTAGQERFHALGPIYYRDSNGAILVYDITDEDSFQKVKNWVKELRKMLGNEICLCIVGNKIDLEKERHVSIQEAESYAESVGAKHYHTSAKQNKGIEELFLDLCKRMIETAQVDERAKGNGSSQPGAARRGVQIIDDEPQAQSSGGGCCSSG", "text": "FUNCTION: Small GTPase involved in membrane trafficking control (By similarity). Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general. As a result, may regulate cell adhesion and migration. During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis (By similarity). Involved in neurite growth (By similarity). Modulates protein levels of the cargo receptors TMED2 and TMED10, and required for appropriate Golgi localization of TMED10 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Lipid-anchor Golgi apparatus, trans-Golgi network Golgi apparatus membrane Early endosome membrane Cytoplasmic vesicle membrane Cleavage furrow Cell projection, neuron projection Note=Colocalizes with ANKRD27 and VAMP7 in neurites (By similarity). In nonpolarized epithelial Caco-2 cells, found in the endoplasmic reticulum; in polarized cells, observed in vesicles in the apical cytoplasm. During mitosis, in mid-telophase, localized in the ingressing cleavage furrow. In late telophase, detected at the opposite poles of the daughter cells, in vesicles at the base of lamellipodia formed by the separating daughter cells (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MHEVVTISVSQRANHLTTQFFNIQEGYLQLSKEQQVNDSKIFLNSVVDKVSKTISYAPRALLWDARTGNGSLGTYQYSESQDYHFGNEDKFKEQTVIKTHPRIPKSEYQSSLDAGAPLPCLNRENTMYWSDYSKLIYGPSSFNILRNWYHDTENPNQPDFQNLGERKFDRYSIGYDEFTENYLQEFFDGNLHRELEKCDTLQGFNLVSDMESGWGGFSSALLVELRNELPKKAVFSWGHNEDDPFTDDFPMKRLSKKWLPIISNKLRSTINMMQESDLYFPLYAAPGLTNWETAGKSCRIFDSINATISQSNLEQRKTMDYLTTAITLGYSSRNMVTGMVIGDTDYSFCSRVLPFKNSHKPNSTHIFSKSFIDRGNQTHKHHSEPDSRSKMIEMYTHRYFPSDTIPTEFSNDREFVLELESSEKNRDIFKHWNEFVVRYFKNDSDREELKNELSDYASAYESGWYEDEDSGDDDM", "text": "FUNCTION: Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the misato family."}
{"protein": "MVPVGPERGANSLFSLRFTTFAVGTVSLPLFAFLFCIVWSLLFNFSETTATHCHVPNYLPSVSAAIGGETPQRYIWRLCIGLHSAPRFLVGVAYLHYYQGTPCSSPAYPRLCHLNFLLNCCEIFFLILLTYVSSSENYEVHKLGFMAFMLFSVGYMFVTCSLWRVARKGSGSLEERTSYAWKKRLFGFYLLMFLSSILVYIWHNMYCEAGVYTVFALLEYLVVLSNMGFHMTAWWDFGNKELMICSPGDKRI", "text": "FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Required for stable expression of GPI-anchored proteins at the cell surface (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PGAP2 family."}
{"protein": "MRGKTFRFEMQRDLVSFPLSPAVRVKLVSAGFQTAEELLEVKPSELSKEVGISKAEALETLQIIRRECLTNKPRYAGTSESHKKCTALELLEQEHTQGFIITFCSALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRVVDLATACIQHLQLIAEKHKGEEHRKALEDFTLDNILSHIYYFRCRDYTELLAQVYLLPDFLSEHSKVRLVIVDGIAFPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDRNQALLVPALGESWGHAATIRLIFHWDRKQRLATLYKSPSQKECTVLFQIKPQGFRDTVVTSACSLQTEGSLSTRKRSRDPEEEL", "text": "FUNCTION: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD51 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1- BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single- stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA- dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross- link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region Mitochondrion Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA. SIMILARITY: Belongs to the RecA family. RAD51 subfamily."}
{"protein": "MNTSVTSIKLVLLGEAAVGKSSIVLRFVSNDFAENKEPTIGAAFLTQRVTINEHTVKFEIWDTAGQERFASLAPMYYRNAQAALVVYDVTKPQSFIKARHWVKELHEQASKDIIIALVGNKIDMLQEGGERKVAREEGEKLAEEKGLLFFETSAKTGENVNDVFLGIGEKIPLKTAEEQNSASNERESNNQRVDLNAANDGTSANSACSC", "text": "FUNCTION: Required for protein transport to the vacuole. Involved in two vesicle trafficking steps to the prevacuolar compartment (PVC), regulating the docking of endosomes and Golgi vesicles to the PVC by interacting with PEP7/VAC1 on the PVC membrane and promoting SNARE complex formation. SUBCELLULAR LOCATION: Endosome membrane; Lipid-anchor Mitochondrion membrane; Lipid-anchor. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MVLESIARVIKVQLPAYLKRLPIPDSIAGFIRLTVSEWLRLLPFLGVLALLGYLAIRPFLLKKKQQKDSLINLKIQKENPKVVNEINIEDLHLAKAAYCRCWRSKTFPVCDGSHNKHNELTGDNVGPLILKKKEV", "text": "FUNCTION: Regulator of autophagy that contributes to antagonize becn1- mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of bcl2 with becn1 and is required for bcl2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CISD protein family. CISD2 subfamily."}
{"protein": "MSMKIKICIPTERIQNPIISETIVETGILLNIMVANIDSTYGELIADVKDSRFARIKKALESRGAIVAILDRPIHRDEEECVECGACISVCPMNVYSFDETWSLCVDEKKCIQCGMCIKMCPHGALKLGE", "text": "FUNCTION: Required for O-acetylhomoserine sulfhydrylase (OAHS)- independent homocysteine (Hcy) biosynthesis (PubMed:25315403, PubMed:25938369). Together with MA_1821, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. May be involved in the reduction of the disulfide formed in MA_1821 (Probable)."}
{"protein": "MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDRSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYKTGFGGKFGVQSERQDSSAVGFDYKERLAKHESQQDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKKQTPPASPSPQPIEDRPPSSPIYEDAAPFKAEPSYRGSEPEPEYSIEAAGIPEAGSQQGLTYTSEPVYETTEAPGHYQAEDDTYDGYESDLGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ", "text": "FUNCTION: Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:17403031). Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (PubMed:22262902). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)- mediated endothelial cell (EC) barrier enhancement (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell projection, ruffle. Cell projection, dendrite. Cell projection Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, podosome Cell junction Cell junction, focal adhesion Membrane, clathrin-coated pit Cell projection, dendritic spine. Cytoplasm, cell cortex Endoplasmic reticulum Note=Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2, localizes at the cell cortex. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft. Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones (By similarity)."}
{"protein": "MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKENKGCESPDPDSSYALTPRTEEKYKKINEEFDNMIKSHKIPAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNFLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT", "text": "FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, sarcoplasm."}
{"protein": "MTEPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYLLWNSELPNDSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAVSVLGANHARAQDSSPEANLEKAMSLLATFPSVVAYDQRRRRGEELIEPREDLDYSANFLWMTFGEEAAPEVVEAFNVSMILYAEHSFNASTFTARVITSTLADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRKDESLDEAATRSKAWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEMLGLYNGLEAAMEEAKQIKPNLDYPAGPTYNLMGFDTEMFTPLFIAARITGWTAHIMEQVADNALIRPLSEYNGPEQRQVP", "text": "FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity. SIMILARITY: Belongs to the citrate synthase family."}
{"protein": "MNNPSETSKPSMESGDSNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLGHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPIQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSALCSPSALNSPGLGVEGLNRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVGTTPSLVTSSAATTLTVNPVLPLTSAAVTNLSVTGTTDTTSNNTATVISTAPPASSAVTSPSLSPSPSASGSTSEVSSASETSTTQTTSTPLSSPLGTSQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPGLMAPSQFAAGGALLSLNPGTLGGALSPALMSNSTLATIQALASGGSLPITSLDATGNLVFGNAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASAGNSGPVASLHATSTSAESIQNSLFTVASASGAASTTTTASKAQ", "text": "FUNCTION: Transcription factor that binds to the octamer motif (5'- ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-2 subfamily."}
{"protein": "MGPGQPASTCVHLAPRTQLDGRSDPKVLQTQNQLQFNRNVPTHSSNLAIRYSCPHAIRIEKLKHSYNESYHCKDADCRVGPDLGSSVSFSVISQERLSYAVHLARRDVKRRQFEKHIKEHHLRSQPQSSQKCGHTKYKIPDHRVERKESKSQAACQCSHQPSKVEISSSGAKVYLYSSHPGQSDLTVPNSPPTHDPGLQPHPRIGDHKNISEQKSLLEVQRLQKELSSCIHKIEEVTKKDRLEEALDPDEERRIRIRRQEQAARSARMLYVLQQQVKEIQEELDKLSPHKIKHTKKSWAMSKLAAAHRGAIRALQMFVTQFTDRGEHPLPARCKELGSLIRQLSLCSVKLDADPSVPDVVIDILQQIEALESLLEKKLSPKKVKKCFSEIRSRFPIGSQKALERWPSTSPKGERRPLTAKDTFPQETSRPSVAKQLLADKYQPDTELPETQRLQSELDVLDADIVLEEGPFILDQSASFKDEVLAVAKTKAGKKKPVTENVPFRKKDTLAPARQQGLRKAERGRQSQPHSKSRVQQTTVSSRLKMNRQPVKDRKAPWIPPNPTSPPASPKCAAWLKVKTSPRDATKEPLQQEDPQEESHLTGAVEHEAARLAWLDAETSKRLKELEELKAKEIDSMQKQRLDWLDAETSRRTKELNELKAEEMYRLQQLSVSATHLADKVEEAVLDRLKPLLVKAQRVNSTTEANIHLKDGSSVNTAKAQPAQEVAAVDFESNNIRQLDDFLEDCASELWAVTHAKILGSETLATVEDSKDSPDLEIMMRRMEEMEKYQESVRQRYNKIAYADPRLWMQEENNDQKISAISEKPLSPHPIRITKTVDRKDPAVNIMLERPCNGNSLDESVGTEEGSEKREAPLLSLAEDSQQKEGRAPLFVPPGMQHSIGDYCSRFEQYLRIISHEAVGSFNPWLIAESFSEELVDEALGAVAAELQDMCEDYAEAVFTSEFLEAAT", "text": "FUNCTION: Involved in centriole duplication (PubMed:24613305, PubMed:26297806). Positively regulates CEP63 centrosomal localization (PubMed:24613305, PubMed:26297806). Required for WDR62 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:24613305, PubMed:26297806). May play a role in cilium assembly. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localization to centrioles and pericentriolar satellites may be mediated by interaction with PCM1."}
{"protein": "MKKWFPALLFSLCVSGESSAWNNIVFYSLGNVNSYQGGNVVITQRPQFITSWRPGIATVTWNQCNGPEFADGSWAYYREYIAWVVFPKKVMTKNGYPLFIEVHNKGSWSEENTGDNDSYFFLKGYKWDERAFDAGNLCQKPGETTRLTEKFNDIIFKVALPADLPLGDYSVTIPYTSGIQRHFASYLGARFKIPYNVAKTLPRENEMLFLFKNIGGCRPSAQSLEIKHGDLSINSANNHYAAQTLSVSCDVPANIRFMLLRNTTPTYSHGKKFSVGLGHGWDSIVSVNGVDTGETTMRWYKAGTQNLTIGSRLYGESSKIQPGVLSGSATLLMILP", "text": "FUNCTION: Tip adhesin component of type P pili that plays a critical role in kidney infection through targeted interaction with the globoseries glycolipids containing the Gal-alpha(1-4)-Gal disaccharide present on uroepithelial cells. In turn, transcriptionally regulates host gene expression in kidney cells, leading to inflammatory pathway activation and renal tissue damage (PubMed:31181116). Acts thereby as key determinant of invasive uropathogenic E.coli (UPEC), which cause pyelonephritis and urinary-source bacteremia (PubMed:33235212). SUBCELLULAR LOCATION: Secreted Fimbrium Note=At the tip of P pili. SIMILARITY: Belongs to the adhesin PapG family."}
{"protein": "MTFPRALTVIDDNGLVISIIFWFLLIIILILFSIALLNIIKLCMVCCNLGRTVIVPVQHAYDAYKNFMRIKAYNHDGALLV", "text": "FUNCTION: Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis. SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass type III membrane protein Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. SIMILARITY: Belongs to the alphacoronaviruses E protein family."}
{"protein": "MFVDYSGLERYTDINASFGKLVNTYCCFQRCEAISEQLEILKSLVPKCHDIVALTDEDFASGRTAGLTQKLFAMAMTLHQITDCIDLLQKCNTIIPIEIANPASFESGAATAPLRQSYARLLDDWSHYMGPSTVKHTGCTNRPKWRFPWQQSRTIIIPMLFIGETAMSTRDLRSVLHDCEIRHASEMPLQLLWTSSPELVYATPHVDDYDIWSRYGSDYNMQIEDEDEASKGRQRKCVVQLEALLGALPTTDPLFQW", "text": "SIMILARITY: To yeast YKR015c."}
{"protein": "MSCPIDKRRPLIAFLRRLRDLGQPPRSVTSKAHVKRAPKEVPLCPLMTDGETRNVTSLPGPTNWPLLGSLLEIFWKGGLKKQHDTLAEYHKKYGQIFRMKLGSFDSVHLGSPSLLEALYRTESAHPQRLEIKPWKAYRDHRNEAYGLMILEGQEWQRVRSAFQKKLMKPVEIMKLDKKINEVLADFMGQIDELRDERGRIQDLYSELNKWSFESICLVLYEKRFGLLQKDTEEEALTFIAAIKTMMSTFGKMMVTPVELHKRLNTKVWQAHTLAWDTIFKSVKPCIDHRLERYSQQPGADFLCDIYQQDHLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQRLLREIQSVLPDNQTPRAEDVRNMPYLKACLKESMRLTPSVPFTTRTLDKPTVLGEYTLPKGTVLTLNTQVLGSSEDNFEDADKFRPERWLEKEKKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIIQKYNIVATDSEPVEMLHLGILVPSRELPIAFCPR", "text": "FUNCTION: A cytochrome P450 monooxygenase with a key role in vitamin D catabolism and calcium homeostasis. Via C24-oxidation pathway, catalyzes the inactivation of both the vitamin D precursor calcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25- dihydroxyvitamin D(3)). With initial hydroxylation at C-24 (via C24- oxidation pathway), performs a sequential 6-step oxidation of calcitriol leading to the formation of the biliary metabolite calcitroic acid. Hydroxylates at C-24 or C-25 other vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S- hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSDEINETCKPQACAIQNCLMKNGYNESKCSYYIDELYKCCKKFYESNGSSASSVCCPKFNLLQLKLKQRELGQIDANLIDTKHG", "text": "SUBCELLULAR LOCATION: Mitochondrion intermembrane space Note=Imported into the mitochondria via the mitochondrial disulfide relay system. SIMILARITY: Belongs to the CMC4 family."}
{"protein": "MMSRIEAYQSDIAVLMDPETVLLPDFISALSYAHELGRDWLLVSSSVEIPRFPFHWDETRHFWRQDNGKRVRFRELQKMISLRSLQSNSSASKMIMAWNNIDMPLHCGVLPPFLYQRGTHNQWIINEAMSCKRRFVFDATSTISSFFLGNAENIYNRSDNVSEPKTRNWEYVGNSHLGQLYGSLYSRSYTLPKLLKCNRRYIFVSASERSTDLSIPKGKSLGFRTREKISACITRTKSRSLKLDFVQKDETVPPLKFPFDLESLLPLVADKNRTVVLSVAGYSYKDMLMSWVCRLRRLKVPNFLVCALDDETYQFSILQGLPVFFDPYAPKNISFNDCHFGSKCFQRVTKVKSRTVLKILKLGYNVLLSDVDVYWFRNPLPLLQSFGPSVLAAQSDEYNTTAPINRPRRLNSGFYFARSDSPTIAAMEKVVKHAATSGLSEQPSFYDTLCGEGGAYRLGDDRCVEPETNLTVQFLDRELFPNGAYGDLWLKEDVRAECEKKHCFVLHNNWISGRLKKLERQMMKGLWEYDASMRMCV", "text": "FUNCTION: Beta-arabinofuranosyltransferase that transfers specifically an arabinosyl residue from UDP-arabinofuranose to the monosaccharide galactose or beta-methyl-galactoside in vitro. Catalyzes the addition of a beta-arabinofuranose residue onto a beta-galactosyl residue of an Yariv-precipitable wall polymer in vivo. SIMILARITY: Belongs to the glycosyltransferase 77 family."}
{"protein": "MPSVALKSPRLRRVFVVGVGMTKFMKPGGENSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVEIVAQEMMTDLPSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLYRMGFPEAASSFRTHQVSAAPTSSAGDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLAMKLQNLQLQPGKAKL", "text": "FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids (PubMed:10706581). Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA) (PubMed:10706581). Also active with medium and long straight chain 3-oxoacyl-CoAs (By similarity). Stimulates the microsomal conversion of 7- dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro (By similarity). Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (PubMed:9553048). FUNCTION: [Isoform SCP2]: Mediates the transfer of all common phospholipids, cholesterol and gangliosides from the endoplasmic reticulum to the plasma membrane. May play a role in regulating steroidogenesis (By similarity). Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol (By similarity). Also binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA (PubMed:9553048). Involved in the regulation phospholipid synthesis in endoplasmic reticulum enhancing the incorporation of exogenous fatty acid into glycerides (PubMed:11003606). Seems to stimulate the rate- limiting step in phosphatidic acid formation mediated by GPAT3 (PubMed:11003606). Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (PubMed:9553048). SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome. SUBCELLULAR LOCATION: [Isoform SCP2]: Cytoplasm Peroxisome Endoplasmic reticulum Mitochondrion. SIMILARITY: In the N-terminal section; belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MESLIFIAPLAGVISLVFAAFFAKSILKEDAGNKRMKEIAGAIQEGAMAYLNRQYKTIAVVSIILSFLILFLLDDGLKIAIGFLAGAISSAAAGYIGMSVSVRANIRTAHAASSGLEKAMSVAFRGGAVTGLAVVGLALLGTSSFYILYGDVDLVVGFGFGASLISLFARVGGGIFTKAADVGADLVGKVEAGIPEDDPRNAGVIADNVGDNVGDCAGMGADLFETYVVTSLAAMLLGSLIIGTYENAILYPLVLGSVAIFASIISVFFVKIGKEGKIMQALYKGVGGSAIISLIAFYFVTNSLMGDIRLFYATVVGIIITVLMVIITEYYTSTDYRPVKTIAASSETGAATNIISGLSIGFESTLVPTVVIVIGILISYFIVGGAADAGIGLYGIAIAAVAMLSTTGMIVALDSYGPITDNAGGIAQMANLPAQVRKVTDALDAVGNTTKAVTKGYAIGSAALGALALFADYRSKVNLGGQSLNLDDPVVLAGLLLGALLPFVFSAVTMSAVGKAAFEVVNEVRRQFREIPGIMEGTAKPEYGRCVDIVTKAALHEMAMPGFLAVLVPLLVGLILGPKALAGLLIGLIVVGFMLALMMDNGGGAWDNAKKLIEDGNHGGRGSEAHKAAVVGDTVGDPFKDTAGPALNALIKVVNMVAILFSSLIIHSGLF", "text": "FUNCTION: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-insensitive subfamily."}
{"protein": "MMRVIILLLTLHVLGVSSVMSLKKKIDGPWQTIYLAASTMEKINEGSPLRTYFRHILCGRRCNQVYLYFFIKKGTKCQLYKVIGRKKQEVYYAQYEGSIAFMLKMVNEKILLFHYFNKNRRNDVTRVAGVLAKGKQLNKEEMTEFMNLVEEMGIEEENVQRIMDTDNCPSKIKP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MSSKIPLLFIISFGLYVSTTNSSPIERRSLWNFFFMTFIGGKRAPWKYDGYGNHCGIGGKGSPVDSIDRCCQVHDRCYHEVNENECGSYKRNVKFIDYDWYMQDKQIVCDTTDTVCAQAICKCDKDIVECLNQNDKDYNPKYNKAIG", "text": "FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MEFQGERGTGPGVSSSSVACSQVTVSRELLTAGSEGSGGIWDQLLISSKPHPRKTSTLQTVRMQRSPLLDQVQAFLPQMAQANEKLRREMAAAPAGHFNIENIDETSGNIIQMDVALFEMSRSDSKEEDSPEESSRDSSGDSSESEEDVCVPSEVTIENIKLPNAEGGKGKIEILDSPASKKKKQ", "text": "FUNCTION: Client-loading PAQosome/R2TP complex cofactor that selects NOP58 to promote box C/D small nucleolar ribonucleoprotein (snoRNP) assembly. Acts as a bridge between NOP58 and the R2TP complex via RUVBL1:RUVBL2. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MQSVDPQVVGVGKQFVEHYYGIFDSNRAGLTQIYQQQTTLTWEGKFLSGADAIVKHIVELPFQQTNRKINSIDCQQTYQPGIMITVTGTLIIDGEAKNQLKFVQVFNLASNNGSFLLINDFFRLVLD", "text": "FUNCTION: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus outer membrane Nucleus, nuclear pore complex Nucleus inner membrane Nucleus, nucleoplasm Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci."}
{"protein": "MKASISIDEKKDFIRWFLNKHQMKTREAMWVLNYIAGHDQIVKYVHFVDNLEGCARGLSLSAHGVESEPFLFFKGNIMTTDPEKAFHDIRLNWDEELYVELHFEEAITSPEYALVREDNPFTAVKLADEEKEMADALIYQSVHQFSREKVLQQIDEALDARDEVTFHKLVRILQQMDTVKE", "text": "SIMILARITY: Belongs to the UPF0302 family."}
{"protein": "MAAVGAGGSTAAPGPGAVSAGALEPGTASAAHRRLKYISLAVLVVQNASLILSIRYARTLPGDRFFATTAVVMAEVLKGLTCLLLLFAQKRGNVKHLVLFLHEAVLVQYVDTLKLAVPSLIYTLQNNLQYVAISNLPAATFQVTYQLKILTTALFSVLMLNRSLSRLQWASLLLLFTGVAIVQAQQAGGGGPRPLDQNPGAGLAAVVASCLSSGFAGVYFEKILKGSSGSVWLRNLQLGLFGTALGLVGLWWAEGTAVATRGFFFGYTPAVWGVVLNQAFGGLLVAVVVKYADNILKGFATSLSIVLSTVASIRLFGFHVDPLFALGAGLVIGAVYLYSLPRGAAKAIASASASASGPCVHQQPPGQPPPPQLSSHRGDLITEPFLPKLLTKVKGS", "text": "FUNCTION: Transports uridine diphosphate galactose (UDP-galactose) from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges UDP-galactose for UMP (PubMed:9010752, PubMed:12682060). It is also able to exchange UDP-galactose for AMP and CMP, and to transport UDP-N-acetylgalactosamine (UDP-GalNAc) and other nucleotide sugars (PubMed:12682060, PubMed:11784306). As a provider of UDP- galactose to galactosyltransferases present in the Golgi apparatus, it is necessary for globotriaosylceramide/globoside (Gb3Cer) synthesis from lactosylceramide (PubMed:30817854). SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane. SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A subfamily."}
{"protein": "YSKSLPLSVLNP", "text": "FUNCTION: Has bactericidal activity against E.coli ATCC 29522 and S.aureus. Inhibits growth of S.marcescens and B.cereus ATCC 14579. A synthetic peptide has antibacterial activity against E.coli ATCC 29522 (MIC=8 ug/ml), S.aureus (MIC=64 ug/ml), S.marcescens (MIC=32 ug/ml), B.cereus ATCC 14579 (MIC=64 ug/ml), B.subtilis (MIC=32 ug/ml), L.plantarum ATCC 8014 (MIC=32 ug/ml), B.flexus (MIC=32 ug/ml), S.enteritidis ATCC 13076 (MIC=4 ug/ml), Enterobacter spp (MIC=32 ug/ml), B.anthracis (MIC=128 ug/ml), B.licheniformis (MIC>128 ug/ml) and L.lactis ATCC 11454 (MIC>128 ug/ml)."}
{"protein": "MIPGNRMLMVILLCQVLLGGTNHASLIPETGRKKVAELQGQAGSGRRSAQSHELLRGFETTLLQMFGLRRRPQPSKSAVIPSYMLDLYRLQSGEEEERSLQEISLQYPERSASRANTVRSFHHEEHLESVPGPSEAPRIRFVFNLSSVPDNEVISSEELRLYREQVEEPSAAWERGFHRINIYEVMKPLSERSQAITRLLDTRLVHHNVTRWETFDVSPAVIRWTKDKQPNHGLVIEVTHLHQAQTHQGKHVRISRSLPQGHGGDWAQLRPLLVTFGHDGRGHALTRRARRSPKHHGSRKNKKNCRRHALYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHLNSTNHAIVQTLVNSVNSSIPKACCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR", "text": "FUNCTION: Negatively regulates the structure and function of the limb apical ectodermal ridge. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MEWDADDLLIEPTTEVENDYEDLCTQWVNERMAPDLLPFAEEIVSRVLDRIEAQRETLQLAIGTSSATSYRSVLMQTELERVKFVLRSYMRTRINKIDKYAQYIQSHPNLLLYLSSPERQYLLRHQQIVHRHYMDSFLREVPAKMNKLDDKVGNLSMVASPDMDTAVFCVVNESVEENFRVSENEYITLDKGDVLILRYSVISDYLRLGVVSLI", "text": "FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation and is required for bir1 localization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GINS4/SLD5 family."}
{"protein": "MNTTSYIRGCIPLVFNISSFGFWENLKSPDVIFGYSLPLMEFQILLIFVFIIIIHSFLKSFGISPIPSYMLAGLILGPQLFNLREVSSRKLSWDPALDGNGPLRGLSVCGNIMLAFFMTVKISRRLAFNNGWLPIVIGTLSFIVPFLGGFCVRNLHTDNIDPYYMSPNKVLAERIVVISSQSSILLPTVVHFLSELKILNSELGRLVLSASLINDIFASTVSIFAYLVGTYKNISPMTAYRDLIAVIILILVAFCVLRPVVEWIVERTPEGKPVADVYVHAVVLSVIASAAYSSFFNMKYLLGPFLLGIIIPEGPPIGSALEAKYEALTMNVLIPISITFSTMRCDVMKIVYQYDDIWYNIFLMTFTGFLKMATGMVPCLYCKIPFKEAIAASLLLCSKSFSEIFLYESTYDDSYISQATYTFLITCALINSGIIPTALAGLYDPKRKYVGYQKKNIMNLKPDSDLRILTCIHRPENISAAISFLQFLPSTIVVTVLHLVKLVGKTVPVLISHNKQINRVVTNSYIHTANLAFSQLESVTMTMFTAITHENLMHDEICKVALEQATSIIIVPSGRKWTVDGAFESEDEAIRRLNESLLKSASCSIGILVDRGQLSLKGTRKFNIDVGVIFIGGKDDREALSLVKKMKQNPRVKITVIRLISDRETESTNWDYILDHEVLEDLKDTEATNSIAYTERIVTGGPEVATTVRSLSEDYDLMVVGRDHGMASPDFDGLMEWVELPELGVIGDLLASRELDSRVSVLVVQQQQQT", "text": "FUNCTION: May operate as a cation/H(+) antiporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family. CHX (TC 2.A.37.4) subfamily."}
{"protein": "MQEALALFFGSESLLVGTIIPFLFVLTVVVFVHEMGHYLVARWCGIGAQAFSIGFGPELLGFTDRHGTRWKLSAIPLGGYVKFIGDESETSSPVGVNESALSEEDRKRAFHTQPVWKRAATVFAGPAFNIILTIAIFSVFFALYGRQIADPLIAGVQPGSPAAEAGFEPGDRFVSVEGEKITTFADVQRIVSGRAGDKLNFTVERDGKMVDLQAVPKIVERTDPLGNKVKLGAIGVETTEAVGNFRRIEYGPLESVGQAVIETGHIIGRTGEFFKRFAVGREDKCQLGGPVKIATMASKAASQGFDWLIQLMAMLSIGIGLLNLFPLPPLDGGHLVFYAVEAIKGSPVSGAAQEIFYRIGFLLVMGFMGFVLFNDLFAC", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
{"protein": "MARTVCGCSWALIFIIMSLLVKAKIDVCKRGDVTVQPSHVISLGSAVNISCSLKPRQGCLQVSSLNKLILYRFHRRIHFQRGHSLSSQVTGLPLGTTLFVCKLACSSKEEIRICGAEISVGVVPEQPQNVSCMQKGERGTVACSWDRGRDTHLYTAYTLQLNGPKNLTWQKQCSDYYCDSLDLGINLPPESPESSYTAQVTAINSLGTASSLPSTFTFLDVVRPLPPWDIRIKCVNASVSTCTLQWRDEGLVLLNRLRYRPVYSRSWNMVNATNAKGRHDLVDLKPFTEYEFQISSKPHLQKGRWSDWSESLRTQTPEKEPTGMLDVWYMKQHIDYKRQQISLFWKNLSLSEARGKILHYQVTLQEVAEGNATLQNITERNSWTWTIPRTGIWAAAVSAANSKGSSLPTRINIADLCGAGLLAPQQVSANPEGSDNLLVKWTSPGEGATAVQEYVVEWRELHLRGGMQPPLSWLRSPPYNTSTLISDNIKPYICYEIRVHALSGDQGGCSSIRGDLKHKAPLSGPHINAISEEKGSILISWDEIPAQEQMGCILHYRIYWKERDSDSQPQLCEIPYRVSPKSHPINSLQPRVTYVLWMTALTAAGESPQGNEREFCLQGKANWSTFVAPSICIAVITVGVFSMRCFRQKVFVLLLALRPQWCSREIPDPANSTWAKKYPIVEEKKQLSLDRLLADWPTPEEPEPLVINEVLPQVTPVFRRPHHPNWPGKGQRLQGRHASEEDTGSSASSPPPPRALTAETGPAVDLYKVLGSRRPDSKPGNPVSHLTVLPVDYLPTHEGYLPSNMDYLPSHEAPITDSLEELPQHISLSVFPSNSLHPLTFSCGEKLALDQLKMGCGSLML", "text": "FUNCTION: Receptor for interleukin-12. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily."}
{"protein": "MRLLYVIKKENPMDQMPNCPKCQSEYVYHDSINFVCPDCGNEWDNNEIQESDDDQLIVKDSNGNLLAEGDNVLLIKDLKLKGSSEVLKKGTKFKNIRLVNGDHNVDCGKIMLKSEFLKKA", "text": "SIMILARITY: Belongs to the YjdM family."}
{"protein": "MQRVLELLLLSSTALAVIGDGFIALPVHKLQAGEGSAHFPNRLPIFDVVNGVAKSVEDDVNQIIQPIFGNGIFSGGSIQGTHSGNGHSVKYEVSLPSSSSQKGSNGPSSTDNKDTDPSKTGFSLDDLMNSIPTDFWNLIGLNKAPTSSDNGSKDADFTPSAVSQVEQPTSKSVESTAPGPASSASSSSSSEAASSSQPSEDSQPSSSANKKTGAFFLSLDNTQTLYTATLKVGSPAQEVQVMIDTGSSDLWFISSGNSQCKVNGGSIDCDKYGVFDKSKSSTWHDNKTDYSISYYDGDKASGTMGQDNITFADGFSIENANFAVIDNTTSSIGVFGVGYPELEAVKSKYTNLPFAMKEQNLIAKVAYSLYLDSRDAVQGYILFGGIDHAKYTGDLKAFDIVQSNDKYVYSQIPLTSVASSLNNYTNAYGLPAGSNHPKVGAVIYNGTDSFNGGVDLKDTPTLLDTGTTYSYLSKDQVESIVGLYGNVTYNDAGKAYEVPCWVGNPGNYLEFNFKNEQYIKVPTSEFVISVGTYASGAELCVFGILPGTHSILGDNFMRSVYAVFDLEDHVISIAQAAYNDNHAVVPIE", "text": "FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MDLFRVWSGMDFLAWRGMAYTLLLLNFVFACQLLLLQPLVSALDGQSVDAAELFERASQSIKVKRYSDALDDLNAAIEADPALSEAYFKRASVLRHFCRYEDSENSYQKYLEFKSGDSNAEKELSQLHQAKSALETASTLYESKDIAKALEFVDKVVLVFSPACSKAKLLKVKLLMVSKDYSGAISETGYILKEDENNLEALLLRGRAYYYLADHDIAQRHYQKGLRLDPEHSELKKAYFGLKKLLKKTKSAEDNANKGKLRVSAEEYKEAIALDPEHTANNVHLYLGLCKVSVRLGRGKDGLNSCNEALNIDAELIEALHQRGEAKLLLEDWEGAVEDLKQAAQNSQDMEIHESLGKAEKALKMSKRKDWYKILGISRTASISEIKKAYKKLALQWHPDKNVGNREEAENKFREIAAAYEILGDDDKRARFDRGEDLEDMGGGGGGGYNPFHGGGGGGQQYTFHFEGGFPGGGGGFGGFGF", "text": "FUNCTION: Plays an important positive role in viral symptom development and is required for viral multiplication and pathogenesis. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "MKLFMVLVASFAFAVALPSKKREETAAENELTGDLQEAAQPMIYAVAFPEIRASCVIGWKQQGATCQRDCECCGVAATCITGDSSTGFCGYHQTPNALGQGILYTADTIKNGFSAIFCAG", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 03 subfamily."}
{"protein": "MSKHELSLVEVTHYTDPEVLAIVKDFHVRGNFASLPEFAERTFVSAVPLAHLEKFENKEVLFRPGFSSVINISSSHNFSRERLPSGINFCDKNKLSIRTIEKLLVNAFSSPDPGSVRRPYPSGGALYPIEVFLCRLSENTENWQAGTNVYHYLPLSQALEPVATCNTQSLYRSLSGGDSERLGKPHFALVYCIIFEKALFKYRYRGYRMALMETGSMYQNAVLVADQIGLKNRVWAGYTDSYVAKTMNLDQRTVAPLIVQFFGDVNDDKCLQ", "text": "FUNCTION: Necessary to process the inactive microcin B17 (McbA) precursor into the active peptide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: To R.leguminosarum TfxB which is involved in the processing of trifolitoxin."}
{"protein": "MSCTPCRPQKRLTRPRSQVPRVQTLATEVKKGGVEVLAAVPLSEETEFKVELFVKPVIGNTTAAQDGREPTPHYWSISSAIHDKESGSSIKVEETPDADTTVCYSLAEIAPPDIPNQVSECDMKVWELYRMETELLVVPLVNALGNTNGVVHGLAGTQLYFWAVGGQPLDVVGVTPTDKYKGPTTYTINPPGDPRTLHVYNSNTPKAKVTSERYSVESWAPDPSRNDNCRYFGRVVGGAATPPVVSYGNNSTIPLLDENGIGILCLQGRLYITCADMLGTANSRIHTPMARFFRLHFRQRRVKNPFTMNVLYKQVFNRPTETVDAQVGVTEVTMVEEIGPLPPSIQTTLPTSVNLTQLPRTVTLQSQTPLLNTQQNSK", "text": "FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA. The viral progenies exit the cells by lytic release. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family."}
{"protein": "MGKIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTEYMTYMFKYDTVHGQWKHHEVKVKDSKTLIFGTKEVAVFGCRNPEEIPWAAAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEKEYKSDVNIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHAITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMAFRVPTVDVSVVDLTVRLEKPASYDQIKAAIKEEAEGKLKGILGYVEEDLVSTDFQGDSRSSIFDAKAGIALSDTFVKLVSWYDNEWGYSTRVIDLIRHMHSTN", "text": "FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3- phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family."}
{"protein": "MTPTLETKYVFTITARIGDVTSAGEIGTGVRRIIPILGGEVKGEGISGKVLPFGADFQIIRPNELIELEAKYAFETDDGAVVYVENAGIRFGPVELLQKLKCGEPVDPKLIYFRTRPRFETGHPNYQWLMQHLFIGSAARHADRVVIDVHQVL", "text": "SIMILARITY: Belongs to the UPF0311 family."}
{"protein": "MAMQMNSVVHVSTSPSPSPATSPPPEGKQEHGEVAAVHVVGVGDDEAVMVVKDEEAFGGGGVDYSGRAQWLRAAVLGANDGLVSVASLMIGVGAVSESGRAMLVSGVAGLVAGACSMAIGEFVSVYAQYDIEVAAARRRRRQRRRRCDGDGEEEGSGRLPSPFKAAAASALAFTVGALLPLLAGGFVRPWAPRVAAVCAATSAALAGFGALGAALGGASPARSAARVLLGGWAAMAACYGVLRLFANLY", "text": "FUNCTION: Probable vacuolar iron transporter that may be involved in the regulation of iron distribution throughout the plant. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CCC1 family."}
{"protein": "MTALTAQVALVTGASRGIGKATALALAATGMKVVVNYAQSSTAADAVVAEIIANGGEAIAVQANVANADEVDQLIKTTLDKFSRIDVLVNNAGITRDTLLLRMKLEDWQAVIDLNLTGVFLCTKAVSKLMLKQKSGRIINITSVAGMMGNPGQANYSAAKAGVIGFTKTVAKELASRGVTVNAVAPGFIATDMTENLNAEPILQFIPLARYGQPEEVAGTIRFLATDPAAAYITGQTFNVDGGMVMF", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis (Probable). Is capable of reducing acetoacetyl-CoA, but less well than its paralog PhaB (PubMed:26358291). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MAFKYLLPLLLLSLLVANCASRPLYRLPSEAKHATKKPLQTSRPYNLAHRGSNGELPEETAPAYMRAIEEGADFIETDILSSKDGVLICHHDVNLDDTTDVADHKEFADRKRTYEVQGMNMTGFFTVDFTLKELKTLGAKQRYPFRDQQYNGKFPIITFDEYISIALDAPRVVGIYPEIKNPVFMNQQVKWADGKKFEDKFVETLKKYGYKGSYLSEDWLKQPIFIQSFAATSLVYISNMTDSPKLFLIDDVTILTEDTNKTYAEITSDAYLDYIKPYVIGIGPWKDTIVPVNNNRLMTPTDLVARAHSRNLQVHPYTYRNENQFLHLEFNQDPYLEYDYWLNKIGVDGLFTDFTGSLHNYQELKSPLPQQQ", "text": "SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family."}
{"protein": "MTSEPSTSSEAGSSSLLDADKTNLLQEALVRAGVIRSQRQGISPTATNIKSPKKSALFEKIASHPLMPIVELLLEKCETAATTFDRKAFETDDIKRLFQSLEQRGVQLSSNRDEVDELMETAILALRTCMVELERVYSLMESFKAKYLATLRRTVCHEALVGNNGDSDDELSDNPLMPVLEMSEAAFQAQNKAMESALATLQSVSGSLSLPLQFTHQSITAAQIERNLEFLKQCGFPTQLPPNFLKPSNEKSPEKSEEEKSQKPSSSPKSPSLSD", "text": "FUNCTION: Probable transcription coregulator (PubMed:16824957). Required for asymmetric cell divisions of the T hypodermal cells, and cell fate determination, in concert with homeobox proteins nob-1 and ceh-20 (PubMed:16824957). Acts downstream of the Wnt signaling pathway, and of ceh-20 and nob-1 (PubMed:16824957). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLTMDKEFDSKLTLQGNSSSNGETISRSKSFAFKAPQENFTYHDFELGKIYGVGSYSKVVRAKKKDNGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIVKLFFTFQDTQSLYMALESCEGGELFDQITRKGRLSEDEARFYSAEVVDALEYIHNMGLIHRDIKPENLLLTLDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTDPSRRPGAGSEGYDSLKRHPFFKGVDWKNLRSQTPPKLAPDPASQSASPERDGSPWNPTHVGDTSVLQNDGHNGLSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPRLIYVDPSKLVVKGNIIWSDNSNDLNVQVSSPSHFKICTPKKVLSFEDAKQRALQWKKAIETLQNR", "text": "SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Note=Membrane-associated after cell stimulation leading to its translocation. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily."}
{"protein": "MLTPLFAIAPATVTWSPKVALVMIVCNVIAIAVGKATIKHPSEGAKLPNAAFFGGMGHAALLGTTSLGHIIGIGAIQGLAARGVL", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaG/PsaK family."}
{"protein": "MTSNLYYVLISPYSLAYMVQYRSVTTAAGECRGDMWAVCARISSDVTCARHANLQRSIRRCFYIRSTMCEIMLLRDHGDYPVASRMKVIVWDEELAALAKRHTQGCVPEAYKCRHTLRFWTPGQLNFEFYADKMPFTMSLISTAIKRGHMQKHNITRDIVEKYQPVGPKGNVKELALAIFDRVTAVGCGLTTWKLGGKARAFFTCNFFSENDYNRPVYKTGNSPGEKCIKKDETFKNLCFAQEPINPNEHNL", "text": "FUNCTION: Inhibits platelet aggregation induced by all agonists tested (ADP, arachidonic acid, the thromboxane A2 analog U46619, thrombin, and snake venom snaclecs (TMVA that activates platelet through GPIB, and stejnulxin that specifically acts through GPVI (GP6))) (By similarity). May act by competing with fibrinogen for binding to glycoprotein IIb/IIIa (ITGA2B/ITGB3) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MSKFHKTISRRDFMKGLGLAGAGIGAVAASAPVFHDIDELVSSEANSTKDQPWYVKHREHFDPTITVDWDIFDRYDGYQHKGVYEGPPDAPFTSWGNRLQVRMSGEEQKKRILAAKKERFPGWDGGLHGRGDQRADALFYAVTQPFPGSGEEGHGLFQPYPDQPGKFYARWGLYGPPHDSAPPDGSVPKWEGTPEDNFLMLRAAAKYFGAGGVGALNLADPKCKKLIYKKAQPMTLGKGTYSEIGGPGMIDAKIYPKVPDHAVPINFKEADYSYYNDAEWVIPTKCESIFTFTLPQPQELNKRTGGIAGAGSYTVYKDFARVGTLVQMFIKYLGYHALYWPIGWGPGGCFTTFDGQGEQGRTGAAIHWKFGSSQRGSERVITDLPIAPTPPIDAGMFEFCKTCYICRDVCVSGGVHQEDEPTWDSGNWWNVQGYLGYRTDWSGCHNQCGMCQSSCPFTYLGLENASLVHKIVKGVVANTTVFNSFFTNMEKALGYGDLTMENSNWWKEEGPIYGFDPGT", "text": "FUNCTION: Catalyzes the reductive dechlorination of chloroethene (or vinyl chloride, VC) to ethene (PubMed:15294827). Can also reduce all dichloroethene (DCE) isomers, but not tetrachloroethene (PCE) or trichloroethene (TCE), at high rates (PubMed:15294827). Reduced methyl viologen can act as the artificial electron donor (PubMed:15294827). SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the PceA family."}
{"protein": "MHQIYSCSDENIEVFTTVIPSKVTSPARRRVKSSQHLLTKNVVIESDLYAPRPVELLPHRTDRRDGEGRWSGRFQNPRLQGPHPAKTPARPVGTSEPKSANLCGNRTYGKALMPPVARISVKAPTVLEAAAPGSENVAVLTRGSRHLKKMTEEFPTLPQGAEASLPLTGSAPCGMPSILRKMWTRHKKKSEYVGATNSAFEAD", "text": "FUNCTION: Required for neurogenesis in the neural plate and retina. Strongly cooperates with neural bHLH factors to promote neurogenesis. SUBCELLULAR LOCATION: Cell membrane Nucleus Note=Nuclear localization is essential for its function in neurogenesis. SIMILARITY: Belongs to the vexin family."}
{"protein": "MDLWRVFLTLALAVSSDMFPGSGATPATLGKASPVLQRINPSLRESSSGKPRFTKCRSPELETFSCYWTEGDDHNLKVPGSIQLYYARRIAHEWTPEWKECPDYVSAGANSCYFNSSYTSIWIPYCIKLTTNGDLLDEKCFTVDEIVQPDPPIGLNWTLLNISLPGIRGDIQVSWQPPPSADVLKGWIILEYEIQYKEVNETKWKTMSPIWSTSVPLYSLRLDKEHEVRVRSRQRSFEKYSEFSEVLRVTFPQMDTLAACEEDFRFPWFLIIIFGIFGVAVMLFVVIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILGIHDNYKPDFYNDDSWVEFIELDIDDADEKTEESDTDRLLSDDQEKSAGILGAKDDDSGRTSCYDPDILDTDFHTSDMCDGTSEFAQPQKLKAEADLLCLDQKNLKNSPYDASLGSLHPSITLTMEDKPQPLLGSETESTHQLPSTPMSSPVSLANIDFYAQVSDITPAGGVVLSPGQKIKAGLAQGNTQLEVAAPCQENYSMNSAYFCESDAKKCIAAAPHMEATTCVKPSFNQEDIYITTESLTTTARMSETADTAPDAEPVPDYTTVHTVKSPRGLILNATALPLPDKKKFLSSCGYVSTDQLNKIMQ", "text": "FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling. FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway. SUBCELLULAR LOCATION: [Isoform 2]: Secreted. Membrane. Note=Mainly secreted. In adipose tissue, isoform 2 is mostly membrane associated. SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted Note=Complexed to a substantial fraction of circulating GH. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non- degradative pathway. SIMILARITY: Belongs to the type I cytokine receptor family. Type 1 subfamily."}
{"protein": "MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALVVLAGAGWIALSRLARPPRLPVATRAVLITGCDTGFGKETAKKLDAMGFTVLATVLDLNGPGALELRARCSPRLKLLQMDLTKPEDISRVLEITKAHTASTGLWGLVNNAGLNMVVADVELSPVVTFRECMEVNFFGALELTKGLLPLLRHSRGRIVTVGSPAGDMPYPCLAAYGTSKAAIALLMDTFSCELLPWGIKVSIIQPGCFKTEAVTNVNLWEKRKQLLLANLPRELLQAYGEDYIEHLHGQFLNSLRMALPDLSPVVDAIIDALLAAQPRSRYYTGRGLGLMYFIHHYLPGGLRRRFLQNFFISHLLPRALRPGQPGPVHDTTQDPNPSPTVSAL", "text": "FUNCTION: Catalyzes the conversion of biologically active 11beta- hydroxyglucocorticoids (11beta-hydroxysteroid) such as corticosterone, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as 11- dehydrocorticosterone, in the presence of NAD(+) (PubMed:7649078). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids (PubMed:7649078, PubMed:34028587). Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (PubMed:34028587). Catalyzes the oxidation of 11beta- hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11- ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen (By similarity). Catalyzes the conversion of 11beta- hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11- ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone (By similarity). Converts 7- beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro (By similarity). 7-beta-25-dihydroxycholesterol (not 7-oxo-25- hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity). SUBCELLULAR LOCATION: Microsome Endoplasmic reticulum. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "YRTIDRIYPALTREHKLLIPDIKGEAHIVYEEGRLYPHHNLYYITSEIWDLRALQAVLLSGIARLFVSVYSTKMHGGFLRFQAQYLRRIRVPNWSQVPAAVRQELITAGAKPDLAACNRAVFALYAMTAEERAALGGNGD", "text": "FUNCTION: A methylase, recognizes the double-stranded sequence 5'- CTCGAG-3', methylates A-5 on both strands, and protects the DNA from cleavage by the AbrI endonuclease. SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MIKAMALSSAGVVSHLHPPSFSSSSGLSVNRVLFRNRNASPCGLSLPILNPSRSVLVFARGKNRKGFVSSSSSSPKKNKKKSLDGADNGGGEEEEDPFEALFNLLEEDLKNDNSDDEEISEEELEALADELARALGVGDDVDDIDLFGSVTGDVDVDVDNDDDDNDDDDNDDDDDDSEEDERPTKLKNWQLKRLAYALKAGRRKTSIKNLAAEVCLDRAYVLELLRDPPPKLLMLSATLPDEKPPVAAPENSSPDPSPVESLSAEDVVVEPKEKVKDEAVHVMQQRWSAQKRVKKAHIETLEKVYRRSKRPTNAVVSSIVQVTNLPRKRVLKWFEDKRAEDGVPDKRAPYQAPV", "text": "FUNCTION: May modulate chromatin structure by regulation of nucleosome assembly/disassembly (By similarity). Homeodomain transcription factor that mediates jasmonic acid (JA)-mediated COI1-dependent and abscisic acid (ABA)-mediated PMR4-dependent resistance to infection by necrotrophic fungal pathogens (e.g. B.cinerea and P.cucumerina) and bacterial pathogens (e.g. P.syringae DC3000); this resistance involves at least callose deposition (PubMed:15923348, PubMed:20836879, PubMed:21564353). Required for the P.fluorescens WCS417r-triggered JA- dependent induced systemic resistance (ISR) against both P.syringae DC3000 and H.arabidopsidis (PubMed:20836879). Negative regulator of the ABA-dependent drought resistance (PubMed:19175769). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MCSYYHMKKRSVSGCNITIFAVMFSHLSAGKSPCGNQANVLCISRLEFVQYQS", "text": "FUNCTION: Enhances IgA secretion from B-cells stimulated via CD40. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MAALVVSGAAEQGGRDGPGRGRAPRGRVANQIPPEILKNPQLQAAIRVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGADFLVHYGHSCLIPMDTSAQDFRVLYVFVDIRIDTTHLLDSLRLTFPPATALALVSTIQFVSTLQAAAQELKAEYRVSVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQAARQEAIATARSAKSWGLILGTLGRQGSPKILEHLESRLRALGLSFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGTAFPKPLLTPYEAAVALRDISWQQPYPMDFYAGSSLGPWTVNHGQDRRPHAPGRPARGKVQEGSARPPSAVACEDCSCRDEKVAPLAP", "text": "FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post- translational modification of histidine which occurs in elongation factor 2 (PubMed:30877278). DPH1 and DPH2 transfer a 3-amino-3- carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Acts as a tumor suppressor (PubMed:10519411). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Punctate, primarily perinuclear localization. SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily."}
{"protein": "MATEPEAAEPVVPSLVDRYFTRWYKPDVKGKFCEDHCILQHSNRICVITLAESHPVLQSGKTIKSISYQISTNCSRLQNKVSGKFKRGAQFLTELAPLCKIYCSDGEEYTVSSCVRGRLMEVNENILHKPSILQEKPSTEGYIAVVLPKFEESKSITEGLLTQKQYEEVMVKRINATTATS", "text": "FUNCTION: Actin-binding protein that regulates actin polymerization, filopodia dynamics and increases the branching of proximal dendrites of developing neurons. SUBCELLULAR LOCATION: Nucleus speckle Cell projection, lamellipodium Nucleus Cell projection, growth cone Cell projection, dendrite Note=Localizes to somata and dendrites in cortical neurons (By similarity). Colocalizes with G- and F-actin in lamellipodia (By similarity). Colocalizes in the nucleus with PTK2 (By similarity). SUBCELLULAR LOCATION: Nucleus speckle Cell projection, lamellipodium Nucleus Cell projection, growth cone Cell projection, dendrite Note=Localizes to somata and dendrites in cortical neurons (By similarity). Colocalizes with F- and G-actin in lamellipodia (By similarity). Colocalizes in the nucleus with PTK2 (By similarity). SIMILARITY: Belongs to the ABITRAM family."}
{"protein": "MRLSTATLLLLLASCLSPGHGILEAHYTNLKCRCSGVISTVVGLNIIDRIQVTPPGNGCPKTEVVIWTKMKKVICVNPRAKWLQRLLRHVQSKSLSSTPQAPVSKRRAA", "text": "FUNCTION: Strongly chemotactic for B-lymphocytes, weakly for spleen monocytes and macrophages but no chemotactic activity for granulocytes. Binds to BLR1/CXCR5. May play a role in directing the migration of B- lymphocytes to follicles in secondary lymphoid organs. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family."}
{"protein": "MAGTLDLDKGCTVEELLRGCIEAFDDSGKVRDPQLVRMFLMMHPWYIPSSQLAAKLLHIYQQSRKDNSNSLQVKTCHLVRYWISAFPAEFDLNPELAEQIKELKALLDQEGNRRHSSLIDIDSVPTYKWKRQVTQRNPVGQKKRKMSLLFDHLEPMELAEHLTYLEYRSFCKILFQDYHSFVTHGCTVDNPVLERFISLFNSVSQWVQLMILSKPTAPQRALVITHFVHVAEKLLQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPETIKLWEGLTELVTATGNYGNYRRRLAACVGFRFPILGVHLKDLVALQLALPDWLDPARTRLNGAKMKQLFSILEELAMVTSLRPPVQANPDLLSLLTVSLDQYQTEDELYQLSLQREPRSKSSPTSPTSCTPPPRPPVLEEWTSAAKPKLDQALVVEHIEKMVESVFRNFDVDGDGHISQEEFQIIRGNFPYLSAFGDLDQNQDGCISREEMVSYFLRSSSVLGGRMGFVHNFQESNSLRPVACRHCKALILGIYKQGLKCRACGVNCHKQCKDRLSVECRRRAQSVSLEGSAPSPSPMHSHHHRAFSFSLPRPGRRGSRPPEIREEEVQTVEDGVFDIHL", "text": "FUNCTION: Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Synapse, synaptosome Cell projection, ruffle membrane; Peripheral membrane protein Note=Found both in the cytosol and associated with membranes. Isoform 2 mainly localizes to the cell membrane. Enriched at juxtamembrane areas and membrane ruffles through association with F- actin. Localizes to the cell bodies and axons of striatal neurons (By similarity). SIMILARITY: Belongs to the RASGRP family."}
{"protein": "MATPVVTKTAWKLQEIVAHASNVSSLVLGKASGRLLATGGDDCRVNLWSINKPNCIMSLTGHTSPVESVRLNTPEELIVAGSQSGSIRVWDLEAAKILRTLMGHKANICSLDFHPYGEFVASGSQDTNIKLWDIRRKGCVFRYRGHSQAVRCLRFSPDGKWLASAADDHTVKLWDLTAGKMMSEFPGHTGPVNVVEFHPNEYLLASGSSDRTIRFWDLEKFQVVSCIEGEPGPVRSVLFNPDGCCLYSGCQDSLRVYGWEPERCFDVVLVNWGKVADLAICNDQLIGVAFSQSNVSSYVVDLTRVTRTGTVTQDPVQANQPLTQQTPNPGVSLRRIYERPSTTCSKPQRVKHNSESERRSPSSEDDRDERESRAEIQNAEDYNEIFQPKNSISRTPPRRSEPFPAPPEDDAATVKEVSKPSPAMDVQLPQLPVPNLEVPARPSVMTSTPAPKGEPDIIPATRNEPIGLKASDFLPAVKVPQQAELVDEDAMSQIRKGHDTMFVVLTSRHKNLDTVRAVWTTGDIKTSVDSAVAINDLSVVVDLLNIVNQKASLWKLDLCTTVLPQIEKLLQSKYESYVQTGCTSLKLILQRFLPLITDILAAPPSVGVDISREERLHKCRLCFKQLKSISGLVKSKSGLSGRHGSAFRELHLLMASLD", "text": "FUNCTION: Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). SIMILARITY: Belongs to the WD repeat KATNB1 family."}
{"protein": "MTSGEAERLRLTHLDHCRRHKCFARGSGEFCYFELPEEHIEGPAHGVRLTTQVELTRSLIREFTKRPLLVERERGPCVLTVVCNCPNPGLHQDLCCHLCAEYNKYRN", "text": "SIMILARITY: Belongs to the adenoviridae E3A-2 family."}
{"protein": "MTYYGVLFVEKCTPSTITQLQDVLSTDLISMGDKWSFELKTFRTSAKNTDPNDTKVMHTVQLSHKNNETVTIKNQSAIITPTYVTKALYDNGCVFGTPEPFDYMLSNKLSNIWTQRQSIKGEFGVSYQTADLSIRVNNAFSYSGFQGLILELESKSSDNLEAFEKNVERVRTMLSGMGLSDVRVSSDKSQGSKQEDSSLFDLAAHYLKVLG", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 20 family."}
{"protein": "MKLQTLQALICIEEVGSLRAAAQLLHLSQPALSAAIQQLEDELKAPLLVRTKRGVSLTSFGQAFMKHARLIVTESRRAQEEIGQLRGRWEGHITFAASPAIALAALPLALASFAREFPDVTVNVRDGMYPAVSPQLRDGTLDFALTAAHKHDIDTDLEAQPLYVSDVVIVGQRQHPMANATRLAELQECRWAFSSAPRGPGAIIRNAFARYGLPEPKLGLVCESFLALPGVVAHSDLLTTMPRTLYERNAFKDQLCSIPLQDALPNPTIYVLRRHDLPVTPAAAGLIRWIQHHALQTG", "text": "FUNCTION: Regulates expression of the tsaMBCD1 operon and of tsaT in response to p-toluenesulfonate (TSA). Acts by binding directly to the promoter region. Binding to the tsa promoter depends on TSA concentration. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MSQQHTLPVTLPPALSQELLDTVPPPVNTQQEQRKQPAALPPPCQEVPVELPVEGPSKHEEKHMTIVKGAPEQECEQQQQPQEQKLQQQHWEQDEEHQKAENPEQQLKQEKAQREKQQLQGQLEEEKKLLDQQPDHELAKSDEQLGTKKEQLLEFPEQQEGQLKCLEQQEGHLELPEQQEGQLKCLEQQEGHQELPEQQEGQLKHLEQQEGQLKHLEQQEGQVKHLEQQEKQSELPEQQRGQPKYLEQQEGQLKHLEEQKGQLKHLEHQEGQLELPEQVGQPKHLEQLEKQLEHPEQQEGQLKQLEEQEGQVKHLEQQEEQLKHLEQQEGQPKHPEQLEKQLEHPEQQEGQLKQLEEQEGQVKHLEQQEEQLKHLEQQEGQPKHLEQLEKQLEHLEQQEGQLKHLEQREEQLELPEQQVGQSKHLEQEEKQLEHPEQQEGQLKHLGKQEAQLELPEQVGQPKHLEQQEKQLEHPEQQEGQLKPQEQQEGQLKGLEQQERQLEQPVFAPAPGQVQGIQQALPPKGEVLLPVEQQQQKQEVQWQHK", "text": "FUNCTION: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope. SIMILARITY: Belongs to the involucrin family."}
{"protein": "MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYLEDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCLSSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINPGLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVSQAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSSFVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKILYELSMKLTPSYDLAPFRISRFPSLGKAHL", "text": "FUNCTION: Metabolizes sarcosine and L-pipecolic acid. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the MSOX/MTOX family."}
{"protein": "PPPNPEGTRQARRNRRRRWRERQRQIRSIGAWILSTYLGRSAEPVPLQLPPLERLTLDCEEDCGTSGTQGVGSPQVLVESPAVLEQGTKE", "text": "FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre- mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) binds directly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran- GDP) and targets Rev to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm (By similarity). SUBCELLULAR LOCATION: Host nucleus, host nucleolus. Host cytoplasm. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm."}
{"protein": "MIPAVVLLLLLLVEQAAALGEPQLCYILDAILFLYGIVLTLLYCRLKIQVRKAAIASYEKSDGVYTGLSTRNQETYETLKHEKPPQ", "text": "FUNCTION: Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of interleukin-3 receptor complex, selectively mediates interleukin 4/IL4 production by basophils priming T-cells toward effector T-helper 2 subset. Associates with pattern recognition receptors CLEC4D and CLEC4E to form a functional signaling complex in myeloid cells. Binding of mycobacterial trehalose 6,6'- dimycolate (TDM) to this receptor complex leads to phosphorylation of ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen- specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. May function cooperatively with other activating receptors. Functionally linked to integrin beta-2/ITGB2-mediated neutrophil activation. Also involved in integrin alpha-2/ITGA2-mediated platelet activation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the CD3Z/FCER1G family."}
{"protein": "MAKSHLLQWLLLLPTLCCPGAAITSASSLECAQGPQFWCQSLEHAVQCRALGHCLQEVWGHAGANDLCQECEDIVHLLTKMTKEDAFQEAIRKFLEQECDILPLKLLVPRCRQVLDVYLPLVIDYFQSQINPKAICNHVGLCPRGQAKPEQNPGMPDAVPNPLLDKLVLPVLPGALLARPGPHTQDFSEQQLPIPLPFCWLCRTLIKRVQAVIPKGVLAVAVSQVCHVVPLVVGGICQCLAERYTVLLLDALLGRVVPQLVCGLVLRCSTEDAMGPALPAVEPLIEEWPLQDTECHFCKSVINQAWNTSEQAMPQAMHQACLRFWLDRQKCEQFVEQHMPQLLALVPRSQDAHITCQALGVCEAPASPLQCFQTPHL", "text": "FUNCTION: Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter. SUBCELLULAR LOCATION: Secreted, extracellular space, surface film."}
{"protein": "MASLSTSVVASASSRLWNPAASNGKICVPSASLSLRTGCRRSSSSLTSSASSQLLHCSFLSSPVSLASPFSGLSIAFDLSSQTSGLNGQRRRGLVVRAGKAALCQTKRSRSRKSLARTHGFRRRMRTTSGRATIKRRRAKGRWNLCPKSNPSSGKRA", "text": "FUNCTION: This protein binds directly to 23S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family."}
{"protein": "MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATTGKVAAFFVADAVVRKHFCFLKYLPRVRPFYAVRCNSSLGVLKVLAELGLGFSCASKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKSWGEVLTLDALGLHHTHRRVGCSLMFQASVIASVAQGYLELVCQPFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLEGAKVRFEEVTSVIGKNIPFYTPPPCHVPLRTHATKKMTSSDFCCRVHVTAKEKPLFSPFLTEQTGAAPKSIVYHLDEGVYGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVDGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGTQACRVTYAMSRLAWEALQGQLLPAEEDQDAEGVCKPLSCGWEITDSLCVGPVFTPASIM", "text": "FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region Membrane Cytoplasmic vesicle Endoplasmic reticulum-Golgi intermediate compartment Golgi apparatus, cis-Golgi network Golgi apparatus, trans- Golgi network Cytoplasmic granule Cell projection, axon Cell projection, dendrite Perikaryon Note=Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in a antizyme-dependent manner. Localizes with vesicle- associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN) (By similarity). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. ODC antizyme inhibitor subfamily."}
{"protein": "MGLETEKADVQLFMDDDAYSRHSGVDYADPEKFGGSGPDRDPHRLNSHLQLGFEDVVAEPVSTHSFDKVWICSHALFEISKYVVYKFLTVFLAIPLAFAAGILFATLSCLHIWIIMPFVKTCLMVLPSVQTVWKTVTDVVIAPLCASVGRSFSSVSLQLSHD", "text": "FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27- phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments. SIMILARITY: Belongs to the caveolin family."}
{"protein": "MPLRRFSPGLKAQFAFGMVFLFVQPDASAADISAQQIGGVIIPQAFSQALQDGMSVPLYIHLAGSQGRQDDQRIGSAFIWLDDGQLRIRKIQLEESEDNASVSEQTRQQLMTLANAPFNEALTIPLTDNAQLDLSLRQLLLQLVVKREALGTVLRSRSEDIGQSSVNTLSSNLSYNFGVYNNQLRNGGSNTSSYLSLNNVTALREHHVVLDGSLYGIGSGQQDSELYKAMYERDFAGHRFAGGMLDTWNLQSLGPMTAISAGKIYGLSWGNQASSTIFDSSQSATPVIAFLPAAGEVHLTRDGRLLSVQNFTMGNHEVDTRGLPYGIYDVEVEVIVNGRVISKRTQRVNKLFSRGRGVGAPLAWQIWGGSFHMDRWSENGKKTRPAKESWLAGASTSGSLSTFSWAATGYGYDNQAVGETRLTLPLGGAINVNLQNMLASDSSWSNIASISATLPGGFSSLWVNQEKTRIGNQLRRSDADNRAIGGTLNLNSLWSKLGTFSISYNDDRRYNSHYYTADYYQSVYSGTFGSLGLRAGIQRYNNGDSSANTGKYIALDLSLPLGNWFSAGMTHQNGYTMANLSARKQFDEGTIRTVGANLSRAISGDTGDDKTLSGGAYAQFDARYASGTLNVNSAADGYINTNLTANGSVGWQGKNIAASGRTDGNAGVIFDTGLENDGQISAKINGRIFPLNGKRNYLPLSPYGRYEVELQNSKNSLDSYDIVSGRKSHLTLYPGNVAVIEPEVKQMVTVSGRIRAEDGTLLANARINNHIGRTRTDENGEFVMDVDKKYPTIDFRYSGNKTCEVALELNQARGAVWVGDVVCSGLSSWAAVTQTGEENES", "text": "FUNCTION: Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP is found in both commensal and pathogenic strains and plays a dual role in early-stage biofilm development and host cell recognition. SIMILARITY: Belongs to the EcpC/MatD family."}
{"protein": "MYRVLIVFFLFVFLYIVYQPFYQAYLHIGHAQQDYNDTLDDRMDYIESVMRRRHYVPIEALPAIRFDTNLGTLAGDTIKCMSVPLFVSDIDLPMFDCSQICDNPSAAYFFVNETDVFVVNGHRLTVGGYCSTNSLPRNCNRETSVILMSLNQWTCIAEDPRYYAGTDNMTQLAGRQHFDRIMPGQSDRNVLFDRLLGREVNVTTNTFRRSWDELLEDGTRRFEMRCNARDNNNNLMFVNPLNPLECLPNVCTNVSNVHTSVRPVFETGECDCGDEAVTRVTHIVPGDRTSMCASIIDGLDKSTASYRYRVECVNLYTSILNYSNNKLLCPSDTFDSNTDAAFAFEVPGSYPLSRNGINEPTYRFYLDTRSRVNYNDVRGQLS", "text": "FUNCTION: Per os infectivity factor that mediates the specific binding of occluded virions (ODV) to the host midgut target cells."}
{"protein": "MVVGDFPIETDTIVIGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGVCLNVGCIPSKALLHASHRFVEAQHSENLGVIAESVSLNFQKVQEFKSSVVNKLTGGVEGLLKGNKVNIVKGEAYFVDNNSLRVMDEKSAQTYNFKNAIIATGSRPIEIPNFKFGKRVIDSTGALNLQEVPGKLVVVGGGYIGSELGTAFANFGSEVTILEGAKDILGGFEKQMTQPVKKGMKEKGVEIVTEAMAKSAEETDNGVKVTYEAKGEEKTIEADYVLVTVGRRPNTDELGLEELGVKFADRGLLEVDKQSRTSISNIYAIGDIVPGLPLAHKASYEAKVAAEAIDGQAAEVDYIGMPAVCFTEPELATVGYSEAQAKEEGLAIKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGMNAEDIALTIHAHPTLGEMTMEAAEKAIGYPIHTM", "text": "FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family."}
{"protein": "MILSKRPHLMIRKLSEMLVPRSRSAAIKPEEYTASPRSPLDLNFPSPVHSKRFGSGGVGLGIVAALEETSNGINRHDPVRYSGRFRCPEIDLSDEEYTYVTSPNGPTKVYYNDDGFELSENDYRRVHKPMVTVDEPPVIERQSVRGPTEFLSSCCLCKKKLQGKDIYMYKGEMGFCSAECRSVQIMNDERQEQCKTQVSRNADVLSSPYAAGQRLSAGVFVF", "text": "FUNCTION: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles from the cytoplasm to the nucleus when associated with KIN10. SIMILARITY: Belongs to the FLZ family."}
{"protein": "MSEQTIYGANTPGGSGPRTKIRTHHLQRWKADGHKWAMLTAYDYSTARIFDEAGIPVLLVGDSAANVVYGYDTTVPISIDELIPLVRGVVRGAPHALVVADLPFGSYEAGPTAALAAATRFLKDGGAHAVKLEGGERVAEQIACLTAAGIPVMAHIGFTPQSVNTLGGFRVQGRGDAAEQTIADAIAVAEAGAFAVVMEMVPAELATQITGKLTIPTVGIGAGPNCDGQVLVWQDMAGFSGAKTARFVKRYADVGGELRRAAMQYAQEVAGGVFPADEHSF", "text": "FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanB family. SIMILARITY: Belongs to the PanB family."}
{"protein": "MRVLGGRTGTLLACLALVLPVLEANFLSRQHASQVLIRRRRANTLLEETKKGNLERECIEELCNKEEAREIFENNPETEYFYPKYLGCLGSFRAGLFTAARLSTNAYPDLRSCVNAISDQCNPLPCNEDGFMTCKDGQATFTCICKSGWQGEKCESDINECKDPVNINGGCSQICENTPGSYHCSCKNGFVMLSNKKDCKDVDECVLKPSICGTAVCKNIPGDFECECAEGYKYNPVSKSCDDVDECAENLCAQLCVNYPGGYSCYCDGKKGFKLAQDQKSCEAVPVCLPLDLDKNYELLYLAEQFVGVVLYLKFRLPETTRFSAEFDFRTYDSEGVILYAESSDHSAWFLIALREGKIEIQFKNEKTTKMTTGGKVINDGLWHMVSVEELEQSISVKIAKEAVMNINKPGSLFKPTNGFLETKVYFAGVPRKMENALIRPINPRLDGCIRGWNLMNQGTSGVKEIIQEKQNKHCLVNVEKGSYYPGTGVAQFSINYKNESNPEAWQINVSLNIRPSAGTGVMLALVSDNTVPFALSLVDSATEKLQDILVSVESMVIGRIEAISLCSDQQTFLEIRVNRNNLELSTQLRKDSFHSEDFQRQFAILDEAMKGTVVTYLGGLPDVPFSATPVNAFYQGCMEVNINGVQVDLDEAISKHNDIRAHSCPSVWQKTKHT", "text": "FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MNYRIDFAVLSEHPQFCRFGLTLHNLSDQDLKAWSLHFTIDRYIQPDSISHSQIHQVGSFCSLTPEQDVINSNSHFYCEFSIKTAPFPFHYYTDGIKAAFVQINDVEPRVRHDVIVTPIALASPYRERSEIPATDAATLSLLPKPNHIERLDGEFALTAGSQISLQSSCAETAATWLKQELTHLYQWQPHDIGSADIVLRTNPTLDEGAYLLSVDRKPIRLEASSHIGFVHASATLLQLVRPDGDNLLVPHIVIKDAPRFKYRGMMLDCARHFHPLERVKRLINQLAHYKFNTFHWHLTDDEGWRIEIKSLPQLTDIGAWRGVDEVLEPQYSLLTEKHGGFYTQEEIREVIAYAAERGITVIPEIDIPGHSRAAIKALPEWLFDEDDQSQYRSIQYYNDNVLSPALPGTYRFLDCVLEEVAALFPSHFIHIGADEVPDGVWVNSPKCQALMAEEGYTDAKELQGHLLRYAEKKLKSLGKRMVGWEEAQHGDKVSKDTVIYSWLSEQAALNCARQGFDVILQPGQFTYLDIAQDYAPEEPGVDWAGVTPLERAYRYEPLVEVPEHDPLRKRILGIQCALWCELVNNQDRMDYMIYPRLTALAGSGLDTKIPA", "text": "FUNCTION: Hydrolyzes aryl-N-acetyl-beta-D-glucosaminide (aryl-beta- GlcNAc), aryl-beta-GalNAc and chitin oligosaccharides. Can hydrolyze rapidly the artificial substrates p-nitrophenyl-N-acetyl-beta-D- glucosaminide (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, and is slightly active on p-nitrophenyl-beta-GalNAc. This enzyme is not processive, i.e. when it hydrolyzes (GlcNAc)n, both products, (Glc- NAc)n-1 and the terminal GlcNAc, are released before the enzyme attacks a second molecule of (GlcNAc)n or (GlcNAc)n-1. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the glycosyl hydrolase 20 family."}
{"protein": "MTDRNELIGVAIRVVAAAAVSFLSVRYLVKYLDPNYSVNEESKKKVAQLFHELGIDRQIELSEHEIRIATQFVGGEDVGADWDEIGGCEELVAELKDRIILPLRFASQSGSHLLSPPRGILLYGPPGCGKTLLAKAVARAAGCRFINLQVSNLTDKWYGESQKLAAAVFSVAQKFQPTIIFIDEIDSFLRDRQSHDHESTAMMKAQFMTLWDGFSSSGDQIIVMGATNRPRDVDAAILRRMTARFQVPVPNAKQRSQILNVILRNEKINNTVNLGEIAQAAEGLSGSDLKEVCRLALLARAKATVASGGSVNQLLPLEQSDFESAVHKYMRAAHLLVEETLD", "text": "FUNCTION: Involved in intramitochondrial sorting of proteins. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MERLMRLTILLFLGAVLAGCASVPSTSAPQAIGTVERPVPSNLPKPSPGMDPDVLLREFLKATADPANRHLAARQFLTESASNAWDDAGSALLIDHVVFVETRSAEKVSVTMRADILGSLSDVGVFETAEGQLPDPGPIELVKTSGGWRIDRLPNGVFLDWQQFQETYKRNTLYFADPTGKTVVPDPRYVAVSDRDQLATELVSKLLAGPRPEMARTVRNLLAPPLRLRGPVTRADGGKSGIGRGYGGARVDMEKLSTTDPHSRQLLAAQIIWTLARADIRGPYVINADGAPLEDRFAEGWTTSDVAATDPGVADGAAAGLHALVNGSLVAMDAQRVTPVPGAFGRMPEQTAAAVSRSGRQVASVVTLGRGAPDEAASLWVGDLGGEAVQSADGHSLLRPSWSLDDAVWVVVDTNVVLRAIQDPASGQPARIPVDSTAVASRFPGAINDLQLSRDGTRAAMVIGGQVILAGVEQTQAGQFALTYPRRLGFGLGSSVVSLSWRTGDDIVVTRTDAAHPVSYVNLDGVNSDAPSRGLQTPLTAIAANPSTVYVAGPQGVLMYSASVESRPGWADVPGLMVPGAAPVLPG", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the LpqB lipoprotein family."}
{"protein": "MAKKDQEFVKDITNMDEDFPQWYTDVITKTDLVDYSPVKGFMVIKPYGYAIWENIQAFLDRRFKETGHQNCYFPLLIPESLLNKEKEHVEGFAPEVAWVTHGGSEKLAERLCVRPTSETIICSMYSKWLTSYRELPYLYNQWCSVVRWEKSTRPFLRTSEFLWQEGHTLHETAEEAQAETLQMLAIYKEMAEDLLAIPVVDGRKSDRERFAGAAATYTIEALMHDGKALQSGTSHNLAQHFTKAFDITFQGRTGELEYPHHTSWGASTRLIGGIIMVHGDNRGLVLPPRVAPTQVVIIPIAQNKEGVLDKAYEIKKELEAKGIRVTLDDDTNYSPGWKFNQYEMKGVPLRLEIGPRDIENNVAMIARRDTLSKDSYSLDNIGDTVKNLLDTVHTDMLERARAHRDSKTFTFKDYEEFKRKMIETPGFAKGMWCGEEECEAKIKEDTGVTIRCIPFVQENLGETCQFCGKPAKHMVYLAKAY", "text": "FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine. Misacylated Cys-tRNA(Pro) is not edited by ProRS; this function may be provided by ProX. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily."}
{"protein": "MRGKLITLEGIDGSGKSTVAKKLQENSELRVFEPVFTREPTRGTLTGNAVENAIQSDTDQLAELFLFTADHAEHLAKLVKPALEDGKTVISDRYSDSRYAYQGITLKNRLDNPLEWVRDLHRGWTVIPDLTFLFDIEPEIAVKRCGKRGEQTKFEKIEFLRGVRELFLGLAAEEPERFVIVDASGSPEDVEKAVVQKILDFVQRIE", "text": "SIMILARITY: Belongs to the thymidylate kinase family."}
{"protein": "MNIIVVGLSHKTAPVDFREKLSIPKVRIGEAIRELCNYPHIEEVAILSTCNRLEIYLLTSDTYQGIREATQFLADSSDLSLPELRQHLFILLHQDAVMHLMRVTAGLDSLIIGEGQILSQVKQCYQLGQQYQGIGPVLNNIFKQAISAGKRVRTETQISTGAVSISSAAVELAQIKKQDLRTANITILGAGKMSRLLVQHLLSKRVKDINIVNRSVERAKLLVDQFKEANINIYNLSELKTILQNSDIVFTGTSSQEPIITPELINDCDNLPSELMLFDIAVPRNVDPNVSQFDNIKVFNVDDLKVVVSQNQQTRRKMAKAAEILLEEELSAFNIWWGSLEAIPTINKLREKAEIIRVKELEKAISRLGNEFVSDHQEIVESLTRGIVNKILHDPMVQLRAQQDIEIRGRALKILQTLFNLDTIKNGMSPTL", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the glutamyl-tRNA reductase family."}
{"protein": "SCFEGGKDCKNDCQCCGKWSYCKCPIWGLFGCSCVIGDSMVEVRKCQ", "text": "FUNCTION: Neurotoxin. Causes spastic paralysis and death in mice by intracerebroventricular injection at dose levels of 3 ug per mouse. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 37 family."}
{"protein": "MSEEAAYQEDTAVQNTPADALSPVESDSNSALSTPSNKAERDDMKDFDENHEESNNYVEIPKKPASAYVTVSICCLMVAFGGFVFGWDTGTISGFVAQTDFIRRFGMKHHDGTYYLSKVRTGLMVSIINIGCAIGGIILAKLGDMYGRKMGLIVVVVIYIIGIIIQIASINKWYQYFIGRIISGLGVGGIAVLSPMLISEVSPKHIRGTLVSCYQLMITLGIFLGYCTNYGTKTYTNSVQWRVPLGLGFAWALFMIGGMTFVPESPRYLVEVGKIEEAKRSIALSNKVSADDPAVMAEVEVVQATVEAEKLAGNASWGEIFSTKTKVFQRLIMGAMIQSLQQLTGDNYFFYYGTTVFTAVGLSDSFETSIVLGIVNFASTFVGIFLVERYGRRRCLLWGAASMTACMVVFASVGVTRLWPNGKKNGSSKGAGNCMIVFTCFYLFCFATTWAPIPFVVNSETFPLRVKSKCMAIAQACNWIWGFLIGFFTPFISNAIDFYYGYVFMGCLVFSYFYVFFFVPETKGLTLEEVNTLWEEGVLPWKSPSWVPPNKRGTDYNADDLMHDDQPFYKKMFGKK", "text": "FUNCTION: Low-affinity glucose transporter. Can also transport xylose (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "AREETLIIIPGLPLSLGATDTMNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWATAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA", "text": "SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily."}
{"protein": "MSGTRASNDRPPGTGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIVSRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSARFKNLAHQHQSMFPTLEIDVEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKVLVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGDLLQNRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLSEIKVGISYKLNGKRIPYFPANQEILQKVEVEYETLPGWKADTTGARKWEDLPPQAQSYVRFVENHMGVAVKWVGVGKSRESMIQLF", "text": "FUNCTION: Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Partially associated with particulate fractions. SIMILARITY: Belongs to the adenylosuccinate synthetase family."}
{"protein": "MNQANVKNTTFHSMTSVSYNLSPYCSTGTTFRKQPLYRIWETESSTSADLSQKLNYMFPKLGLSESQTSLKDKDVTKDVVCQDIHWSVDATSLFTINSDYGIRQYLIPDPKSDQTLLNPYSRIFAHESVLSSDISPRYSLYEGSSEPLANSILIGAKNVPIKLVDLNDTNNLSTIRSYDISNLENEKFETPYVLKYHRESLFLSGTVRNKVNVYDVNRREPVNTLTYSRRSKCGTQSYKSIISCLDDSFSDNQVRYCGSYKNQVFIIDLRGKTLQLLNNLQGNGARGCYQIINSDNGSYLYVLQRYSSRIEILDHRRPDRPVNHLELPGRSDFQKLKACYNGSFQVGSPLGKGQILSWDKSTIESGGITRENQVVQCQPDILYNVPQCKSMRINIIKTSSDATAISYSGDTAGIALLQR", "text": "FUNCTION: Involved in mRNA splicing. Helps to stabilize the U1 snRNP-5' splice site interaction (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SWT21 family."}
{"protein": "MGRQGNLEELWCLRMPEIITPIITPFTKDNRIDKEKLKIHAENLIRKGIDKLFVNGTTGLGPSLSPEEKLENLKAVYDVTNKIIFQVGGLNLDDAIRLAKLSKDFDIVGIASYAPYYYPRMSEKHLVKYFKTLCEVSPHPVYLYNYPTATGKDIDAKVAKEIGCFTGVKDTIENIIHTLDYKRLNPNMLVYSGSDMLIATVASTGLDGNVAAGSNYLPEVTVTIKKLAMERKIDEALKLQFLHDEVIEASRIFGSLSSNYVLTKYFQGYDLGYPRPPIFPLDDEEERQLIKKVEGIRAKLVELKILKE", "text": "FUNCTION: Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto- 3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2- keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3- deoxygalactonate (KDGal). SIMILARITY: Belongs to the DapA family. KDPG aldolase subfamily."}
{"protein": "MSRNVDKANSVLARYQELVAENTSGYKDYSRFKRPTAVHRISNLEEAQRWRAEVVKDIGNKVTQIHDPSLNEMQIEDINNELNRLFQEKMRWESHIRRNLRGPDYRRMKQGLNTTGGTVINGTRYFGRALELPHVQELLQQQQQQRVKQQNQKQREQELRAKVRQWEEELGPDYYGEDVPPGMQEYEAQRSRELQDILRSAAGRAPQVQIPLFERLPTQEEVEGWLVERRRKRLQERLDL", "text": "FUNCTION: Involved in nuclear pre-mRNA splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ISY1 family."}
{"protein": "MSKENVVADSWDDADADPVKELMDKVEKVKLLQRKEEKKEAFFEKVKAEESSGVVSKLQTEEGLGPSAEEPKRVFLRRPKDGFAASENVIEASPPTSADTEEQPVTNVRSRSHHKLNQKEKQPAPTYEERQAAYQAARNRILGTEYKPDNQEIKEIKFIDRSKSPETLKMTQQNMVEHYGEELSRELMEQPAEIVPPERQYTPDFTQPPPSVSESGGVYNGPPGFQQKQPNFQPTLQQQSLHQQQYLDNQYMMQMNVQIPIQYHNQTQHQFVPHEASAISTTSQNSNGDGQNDQAIYYYQAPTQQPMNYIPYNLPNMAYPPPNFQPQGQLHHQMNAGQLHQIQQQQQQCQQIQHQPPQQHQQVINGQVMNQQNQRNQVNSYPQQNGAGRGQNRQPMMYQMPCNSGPTAKPPPLMNQMQNRCMTNNGQNYQNRNMQQQGQQRSYSSQPQNGQFYQNGNSNQNNPNNGRKQQHQPQQQQNKSGKFGQNRNDMQKNNYQPNLQQPPMSQNPIPFGCPPRNVNAIREQHANNGSPNTGAGILGPHPMMSASQWPALQQNRPQ", "text": "FUNCTION: RNA binding protein that is required for normal cell division and cytokinesis during embryonic development (PubMed:19081077, PubMed:27689799). Functions with RNA-binding protein atx-2 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, and in astral microtubule outgrowth and nucleation (PubMed:19081077, PubMed:27689799). Furthermore, negatively regulates the levels of the protein kinase zyg-1 at the centrosome (PubMed:19081077, PubMed:27689799). Also involved in ensuring centrosome attachment to the nuclear envelope (PubMed:19081077). SUBCELLULAR LOCATION: [Isoform f]: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Nucleus, nucleolus Chromosome Note=Co-localizes with sas-4 at centrioles. Localizes to nucleoli during interphase and to the surface of chromosomes during meiosis and mitosis. Localizes in puncta adjacent to the male pronucleus at the centrosome during meiosis. Localization at the centrosome peaks at prometaphase and metaphase, but then decreases and expression is at its most minimal during interphase. SUBCELLULAR LOCATION: Cytoplasm Note=Co- localizes with atx-2 in the cytoplasm."}
{"protein": "MAAWAGFSEEELRKLQHNGEVANQAVSVTLGRGRKPAQTNRSRQQLQRERALQLAAKQKEISQSLLPDQQLTRPPEPPASSHPAPPAETPDEQSVPVKHEAEPVKPDPASPVQSIPPADFKELDKQEVELREKNRLQQLQWEQRIMEEKNKKRKALLTKTIAEKSKQTQAEAIKLKKIQRELQVLDDSVSSDIGVLRKLIEQSSMDYSLAWKRFEKAEAEYVAAKMDLHRKTEVKEQLTEHLCAIIQQNELRKARKLEELMLQLELNAEEVPSPDQTQLQDKQKEPVTENGPAAELERCTEANGSSMSKDSSITETKISQDNQESEAADVSADGLR", "text": "SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus. SIMILARITY: Belongs to the GORAB family."}
{"protein": "MSAQAQMRAMLDQLMGTSRDGDTTRQRIKFSDDRVCKSHLLNCCPHDVLSGTRMDLGECLKVHDLALRADYEIASKEQDFFFELDAMDHLQSFIADCDRRTEVAKKRLAETQEEISAEVAAKAERVHELNEEIGKLLAKVEQLGAEGNVEESQKVMDEVEKARAKKREAEEVYRNSMPASSFQQQKLRVCEVCSAYLGLHDNDRRLADHFGGKLHLGFIEIREKLEELKRVVAEKQEKRNQERLKRREEREREEREKLRRSRSHSKNPKRSRSREHRRHRSRSMSRERKRRTRSKSREKRHRHRSRSSSRSRSRSHQRSRHSSRDRSRERSKRRSSKERFRDQDLASCDRDRSSRDRSPRDRDRKDKKRSYESANGRSEDRRSSEEREAGEI", "text": "FUNCTION: May bind to RNA via its Arg/Ser-rich domain. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleoplasm Note=Colocalizes with SCNM1 and SNRNP70 in nuclear speckles. SIMILARITY: Belongs to the Luc7 family."}
{"protein": "MTSMMAMGEPRLNWDVSPKNGLKTFFSRENYKDQSMAPSLKELCILSSRRIGENLNASAGSVENEPTVNSAAQAKEKVKTTVGMVLLPKPRVPYPRFSRFSQREQRNYVDLLVKYAKVPPNSKTVGINKNDYLQYLEMKKHVNEEVTEFLKFLQNSAKKCAQDYNMLSDDACLVTEQILKACIEQVKKYPEFYTLHEVTSLMGFFPFRIEMGFKLEKTLLALGSVKYVKTVFPSMPAKLQLSKDTIPAIETPEQIAAAMHYDISEDPNAEKLVARYHPQIALTSQSLFTLLNNHGPSYKEQWEIPVCIQVIPVAGSKPIKVIYINSPLPQKKMTMRERNQIFHEVPLKFMMSKNTSVPVSAVFMDKPEEYISEMDISYEVNECRKIETLENLDLEFDDDVTELETFGATTTKPSKSPSPASTSTVAPMTDTLTAPSIADTSEAPTSPDISAHSRSLSQILMEQLQKEKQLVTGMIDSGPEESKNKDDQRFIPCGEKVSNSDKPLVQDSDLKTSDPLQLESSMEIETSSKNDMATEMESVDERVNVLENTDTNSKEKTVTSEAANTEDVVLDSSDTDEDCLIIDMECQSNSHGKTAEVGSNLSSKPASLNSSSGQTSTGNQTNSTCPEESCVLKKPIKRVYKKFDPVGEILKMQDELLKPISRKIPELPLMNSENSKQPPISEQPSAPSDACSWPKSIWPSAFQKPKGRLPYELQDYVEDTSEYVAPQEGNFVYKLFSLQDLLLLVRCSVQRIETRPRSKKRKKIRRQFPVYVLPKVEYQACYGVEALTESELCRLWTESLLHSNSSFYVGHIDAFTSKLFLLEEITSEELKEKLSALKISSLFNILQHILRKLSSLQEGSYLLSHAAEDSSLLIYKTSDGKVTRTAYNLHKTHCGLPGVPSSLSVPWVPLDPSLLLPNHIHHGRIPCTFPPKSLGPTAQQKIGGTRMPTRSHRNSVSVETKSLPAQQVENEGVASSKRKIT", "text": "FUNCTION: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with COIL in subnuclear Cajal and histone locus bodies. Translocates in the LEC complex to Cajal and histone locus bodies at snRNA genes in a ICE1- dependent manner. Associates to transcriptionally active chromatin at snRNA genes (By similarity). SIMILARITY: Belongs to the ICE2 family."}
{"protein": "MRLTAKQVTWLKVSLHLAGLLPFLWLVWAINHGGLGADPVKDIQHFTGRTALKFLLATLLITPLARYAKQPLLIRTRRLLGLWCFAWATLHLTSYALLELGVNNLALLGKELITRPYLTLGIISWVILLALAFTSTQAMQRKLGKHWQQLHNFVYLVAILAPIHYLWSVKIISPQPLIYAGLAVLLLALRYKKLRSLFKRLRKQVHNKLSV", "text": "FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MsrQ family."}
{"protein": "MVYEATPFDPITVKPSDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKDLPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRDAEDLGDVEEDSAEAKDTKGGSQYARDLHVEHDNEFY", "text": "FUNCTION: Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily."}
{"protein": "MFTSAHANRSPLTSASVRRPSHSVVEHSATGLISEIVYREDQPMMTQLLLLPLLQQLGQQSRWQLWLTPQQKLSKEWVQSSGLPLSKVMQINQMSPCNTLESMIRALRTGNYNVVIGWLTDELTEQEHERLALAAEEGHPMGFIMRPVRNTSQPGRQLSGLKIHSNLYH", "text": "FUNCTION: Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. SIMILARITY: Belongs to the SulA family."}
{"protein": "MSEKNKLPKGIIVLKTLSMPENINANGDIFGGWIMSQMDLGGAILAKEISGGKVATVRVDSINFLKSVSVGDIVNCYANCIKIGKSSIKINVEIWIKKIYSKPLGQYYCAAEAIFIYVAINKTGQPRELLPMSII", "text": "SIMILARITY: Belongs to the acyl coenzyme A hydrolase family."}
{"protein": "MIWLRNRRCLEPLQGTPKWVPVLGELQKTLQKGEYLPLRPLPMFESNFVQVTHQGGPVFVNHRTNRLAMGVAASLPGLVLPDILLIGQPAEDRDCSGLVLTRMIPLDLVHLCVHDLSAWRLKLRLVSGRQYYLALDAPDNEVGFLFHCWVRLINLLQEPAPTWTPRTTRTAPLDMPLAEAPASTWHLQDQPISRHAVRVAERNFPHKTVAAQRQRKAKALKRSFKSQAVGDSVPLIWSQLEHADVRKKPAEKKSHSDPRPDRTHTQIRLPEKTSITTWTIFSIISSTANQTQSSPKACTSASDEATGQGHVVESPSHCVSADSPDGFFLGSCSSLDPCLWHQDTEDLMDSGGSTLSSAASGLAPYPPAACLSTPYSSIPRGREKAGPMGSHQGPGPPPCQKAPSGLVTSCKAPFLVDQSQKLPAVPASSWKPPPGLAPPQKAPAASAPPRKAPAVPAPSQKAPAVPAPSQKAPAIPAPSRKASAASASPRKASAVPAPPQKTPPPSQKAPSVPTIPQKAVSPTAPKKKSLLLPAPSQKALPTSPTEYQMALSPPASRGKLPGDFDVLPTGIPGRAVLERSQSGGKPEPVVTVRTQETDVVEMTTQAKSPESPFTVTKKESKDILISQTKEVTLEAFRGQGKLEDWAHWAKLEERSPDLPGVRSKELEQRKRWVKAKELAVEGPSQEHSRPFSVEALTLTKLMITANSKEQPSKSALVSLPSWLLATPQASATSMMASVPSRPGQLSLLEGKPVVVREQPESHTWVKEGKRPWGEMKEQPWGEMKEPPWDPKGPPKVPFRSKPTSASLKREGISQAPIPLTASPWEDLRPSPLSETLISKMEATARASQQPKRVSQEPMRMPAQHPLATVGSSSEILLPMLLELETVRNTATKAEEIQEESGVLNLLPSLQHSQHSEWPDAGA", "text": "SIMILARITY: Belongs to the GARIN family."}
{"protein": "MNLLPSNPHGNGLLYAGFNQDHGCFACGMENGFRVYNTDPLKEKEKHEFLEGGVGHVEMLFRCNYLALVGGGKKPKYPPNKVMIWDDLKKKTVIEIEFSTEVKAVKLRRDRIVVVLDSMIKVFTFTHNPHQLHVFETCYNPKGLCVLCPNSNNSLLAFPATHSGHVQIVDLANTEKPPVDIPAHEGVLCCITLNLQGTRIATASEKGTLIRIFDTSAGQLIQELRRGSQTANIYCINFNQDASLICVSSDHGTVHIFAAEDPKRNKQSSLASASFLPKYFSSKWSFSKFQVPSGSPCVCAFGTEPNAVIAICADGSYYKFLFNPKGECSRDVYAQFLEMTDEKI", "text": "FUNCTION: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. Binds phosphatidylinositol 3-phosphate (PtdIns3P), and other phosphoinositides including PtdIns(3,5)P2, forming on membranes of the endoplasmic reticulum upon activation of the upstream ULK1 and PI3 kinases and is recruited at phagophore assembly sites where it regulates the elongation of nascent phagophores downstream of WIPI2. SUBCELLULAR LOCATION: Preautophagosomal structure Lysosome. SIMILARITY: Belongs to the WD repeat PROPPIN family."}
{"protein": "MWFEILPGLAVMGVCLVIPGVATAYIHKYTNGGKEKRVGRLRYQWYLMERDRRVSGVNRYYVSRGLENID", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFA1 subunit family."}
{"protein": "MFRSQFTTLLGLFSGAWLPTGSGRPGAPATPVQSGTAINQSWTLDPLVPISALGSWEAFLGLQNKQQGTGELQGGGQRVAAGVPLPLAPQEVLQETCKALSFVQVISRPGCTSARVLNHLCFGRCSSFYIPSSDPTPVVFCNSCVPARKRWTSVTLWCGAGQLASPRRVRISTVLVQKCQCRPKL", "text": "FUNCTION: Seems to play a role in the correct specification of the left-right axis. May antagonize NODAL and BMP4 signaling. Cystine knot- containing proteins play important roles during development, organogenesis, and tissue growth and differentiation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DAN family."}
{"protein": "MENWTNEIWVAIGIAFIVGLFIGYIIVRLTKGSVKHQAKTEAELKTVKTQLDTQKAQIEKHFAESAELFKTLINDYQKLYRHYATSSNNLLGEKDQKGLFTQQLITATDKSQNEQPRDYSEGASGLFKENKEEN", "text": "SIMILARITY: To E.coli YhcB."}
{"protein": "MSVTELKERHMAATQTVNDLREKLKQKRLQLLDTDVSGYARSQGKTPVTFGPTDLVCCRILQGHTGKVYSLDWTPEKNRIVSASQDGRLIVWNALTSQKTHAIKLPCAWVMTCAFSPSGHSVACGGLDSVCSIFNLNSPIDKDGNHPVSRMLSGHKGYVSSCQYVPDEDTHLITSSGDQTCVLWDITTGLRTSVFGGEFQFGHTADVQSVSISSSNPRLFVSGSCDTTARLWDTRVASRAQRTFYCHEGDVNTVKFFPDGNRFGTGSEDGTCRLFDIRTGHQLQVYYQPHGDGDIPHVTSMAFSISGRLLFVRYSNGDCYVWDTLLAKVVLNLGAVQNSHEGXISCLGLSADGXXLCTGSWDTNLKIWAFGGHRSVI", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. SUBCELLULAR LOCATION: Cell membrane. Endoplasmic reticulum membrane. SIMILARITY: Belongs to the WD repeat G protein beta family."}
{"protein": "MARNNLEKMASIDAQMRLLVPGKVSEDDKLIEYDALLLDRFLDILQDLHGEDIRAMVQECYERSGEYEGKNDPHKLEELGNVLTSLDPGDSIVVASSFSHMLNLANLAEEVQIAYRRRNKIKRGGFADESNATTESDIEETFKRLVNQLGKSPAEVFDALKNQTVDLVLTAHPTQSVRRSLLQKHARIRNCLSQLYGKDITPDEKQELDEALLREIQAAFRTDEIRRTPPTPQDEMRAGMSYFHETIWKGVPKFLRRIDTALKSIGINERVPYNAPLIQFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAANLYYSQIEDLMFELSMWRCSDELRARALQLHSASKKDAKHYIEFWKQIPPNEPFRVILGDVRDKLYNTRERTRQLLSNGISDIPEEVTFTNIDEFLEPLELCYRSLCSTGDQPIADGSLLDFMRQVSTFGLSFVKLDIRQESDRHSDVADAITRHLGIGSYKEWSEEQRQAWLLSELQGKRPLFGPDLPKTDEVRDVLDTFHVISELPADNFGAYIISMATAASDVLVVELLQRECHVKKPLRVVPLFEKLADLEAAPAALARLFSINWYRNRIDGKQEVMIGYSDSGKDAGRLSAGWALYKAQEDLIKVAKEFGIKLTMFHGRGGTVGRGGGPTHLAILSQPPDTIHGSFRVTVQGEVIEQSFGEEHLCFRTLQRFTAATLEHGMRPPVAPKPEWRELMDEMAVVATKEYRSIVFQDPRFVEYFRSATPELEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGAAFKHVMEKDIRNLHMLQQMYNEWPFFRVTIDLIEMVFAKGDPGIAALYDKLLVSDDLWAIGEKLRANYGETKDLLLQVAGHKDLLEGDPYLKQRLRLRDSYITTLNVCQAYTLKRIRDPNYHVNLRPHLSKESSTKPAAELVKLNPTSEYAPGLEDTLILTMKGIAAGMQNTG", "text": "FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PEPCase type 1 family."}
{"protein": "MKNEMNIQFTALSQNESFARVTVAAFIAQLDPTMDELTEIKTVVSEAVTNAIIHGYENSGQGNVYISVTLEDHIVYLTIRDEGVGIPNLEEARQPLFTTKPELERSGMGFTIMENFMDDISIDSSPEMGTTIHLTKHLSKSKALCN", "text": "FUNCTION: Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition. SIMILARITY: Belongs to the anti-sigma-factor family."}
{"protein": "MVRWQTWPLLLLFQLVTCQQLQQRIVEAPKDTLAAVGETAILTCRVEHQQGPVQWMKDDFGLGTDRDKPLPGNKRYRMVGSAANGEYNLEISNVTLFDDDDFACQISESDHAKAVVSSKAKLTVLVRPTPPKIVKSHHSLKAIAGDPITQSCLSRKGKPPPTIGWAIASDEHGKHIVSWLGESRSKFGGIHAKPEISQETVIAHVNETTQVEEGGNNSREDSSIYSIMSNLSFIPRPEDDHKYLICISQHMTFPNKIEVDSVKLSLRYAPQINLTVASKLPLRENGSALLACNVNAKPLDNVKISWYKGNQKLRETGDTLTFETLKMEDHNRDIFCEATNEIGTTRGSIKLNVAFGARIMSTSQDKEVNEGDNAFFHCATLANPAPAIFWTRGDSDEIIGHGENLTLENVRTWQQGNYNCTATVEGFRKQILSHYLHIRGPPTVSMKDEVSASLDEATEIICEISGRPKTNNVRWTVNGKEINFNNGRITVHQYPKPYGKESILKIKDLKEEDFGVYNCSANNGLGFDNRGTLLKKRNILDWIVITAKFDRMVALAIISAGVLLVSLLCCLCMCRSNCRSRKSKFIDDQSDVTVKCEALDGQYFPEMYSSSPVDNVHLSTKDYISIPQNNPDLDFLGATGSFGPPGGLYPKCFNNSANEYIYNRYEHSYGSFGSGLSTPGGVSDMYGVAMSDKLPVMETLQEVETPKTSNYNFLSSPEVVRPISRTSTHV", "text": "FUNCTION: Cell adhesion protein (PubMed:15035988). Involved in synapse formation in the HSNL egg-laying motor neuron (PubMed:12628183, PubMed:15035988, PubMed:21858180, PubMed:24485456). Inhibits assembly of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and protects them from elimination (PubMed:17626846). Also required for F- actin assembly at the synaptic region and for axon branch formation (PubMed:24439377). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon Synapse. SIMILARITY: Belongs to the immunoglobulin superfamily."}
{"protein": "MDTLATSINQFALELSKKLAESAQGKNIFFSSWSISTSLAMVYLGTKGTTAAQMGQVLQFNRDQGVKSSPESEKKRKMEFNSSNSEEIHSDFHTLISEILKPNDDYLLKTANAIYGEKTYPFHNKYLEDMKTYFGAEPQSVNFVEASDQIRKEINSWVERQTEGKIQNLLPDDSVDSTTRMILVNALYFKGIWEHQFLVQNTTEKPFRINETTSKPVQMMFMKKKLQIFHIEKPQAVGLQLYYKSRDLSLLILLPEDINGLVQLEKDITYEKLNEWTSADMMELYEVQLHLPKFKLEDSYDLKSTLSSMGMSDAFSQSKADFSGMSSARNLFLSNVFHKAFVEINEQGTEAAAGTGSEIESRIRVPSIEFNANHPFLFFIRHNKTNSILFYGRLCSP", "text": "FUNCTION: Protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. May regulate protease activities in the cytoplasm and in the nucleus (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily."}
{"protein": "MGGPYIGIVADDLTGSGDTAVQFVRAGWATQLSVGGAEQALADPAVRQAEVLAVTTHSRPLAAADAAAVVRGEVERLRAAGVQRLYKKVDSTLRGAFKAEIDAARLAWGEDAIAVVCPAFPVTGRTVRQGVLYVGDRPVTETSAATDPVTPVTESHIPTLLGCAQLAAQAGETPAELARRIAAAAPVVVVDALDDADVQRLARAIGVLGQRAVPVGSGGLAAPLARVWAGGQAAGPVLVVVTSQHSAARQQAAALQQAGARTWAPTLAQLADDRNWAAWTAEVEAAEHGMPAVDALMLLAPEGRLAGLDADSVARRLGELAARLVLAHGAAGVVATGGDGASAVLAALQASGIALVDEVTGGVPLGTLTGGQAAGLPVVTKAGGFGEQDVLIRAAQAIRERRFTK", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-threonate to D-threonate 4-phosphate. Can also phosphorylate 4-hydroxy-L-threonine, with lower efficiency. SIMILARITY: Belongs to the four-carbon acid sugar kinase family."}
{"protein": "MEESQAELGVEPPLSQETFSDLWKLLPENNLLSSELSPAVDDLLLSPEDVANWLDERPDEAPQMPEPPAPAAPTPAAPAPATSWPLSSFVPSQKTYPGSYGFHLGFLHSGTAKSVTCTYSPALNKLFCQLAKTCPVQLWVSSPPPPGTRVRAMAIYKKSEYMTEVVRRCPHHERCSDYSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNFMCNSSCMGGMNRRPILTIITLEDSNGNLLGRNSFEVRVCACPGRDRRTEEENFHKKGQSCPELPTGSAKRALPTGTSSSPPQKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGESRAHSSHLKSKKGQSPSRHKKLMFKREGPDSD", "text": "FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non- coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, PML body Endoplasmic reticulum Mitochondrion matrix Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). SIMILARITY: Belongs to the p53 family."}
{"protein": "MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNETSSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKTVLPVTIMSGLVFHSQPINDRPKQAWCWFGGKWKDAIKEVKQTIVKHPRYTGTNNTDKINLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRDVTTQRPKERHRRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANIDWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTDVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASLTLTAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVTAIEKYLKDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNDTWQEWERKVDFLEENITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLASWIKYIQYGIYVVVGVILLRIVIYIVQMLAKLRQGYRPVFSSPPSYFQXTHTQQDPALPTREGKEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPILQRLSATLRRVREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGAWRDLWETLRRGGRWILAIPRRIRQGLELTLL", "text": "FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. FUNCTION: Surface protein gp120 (SU) may target the virus to gut- associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha- 4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS (By similarity). FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. SIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of SIV-specific CD4+ cells (By similarity). FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl- ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes. The virus undergoes clathrin- dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Host endosome membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag."}
{"protein": "MHSSVFILILFSLAVINPIFFDMKVEAGCMKEYCAGQCRGKVSQDYCLKHCKCIPRFI", "text": "FUNCTION: Blocks potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 20 subfamily."}
{"protein": "MAAAEEGCDAGVEADRELEELLESALDDFDKAKPSPAPPPTTSAPDASGPQKKSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDANSQQEFTSCLKETLSGLAKNATDLQNSGMSEEELTKAMEGLGMDDGDGDGNILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHQESIPPEQFEKYQEQHSVMGKICEQFEAETPTDSEATHRARFEAVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDTLNLSGPPGANGEQCLIM", "text": "FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53. SUBCELLULAR LOCATION: Cytoplasm Peroxisome membrane; Lipid-anchor; Cytoplasmic side Note=Mainly cytoplasmic. Some fraction is membrane-associated to the outer surface of peroxisomes. SIMILARITY: Belongs to the peroxin-19 family."}
{"protein": "MRTLWIVAVWLIGVEGSVIEFGTMIIEETGRSPFPFYTSYGCYCGLGGKGKPKDDTDRCCFVHDCCYGSMPDCSPKTDIYRYHRENGEIICESGTSCEKRICECDKAAAVCFRENLKTYKNKYMVYPDSLCKEESEKC", "text": "FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
{"protein": "MSVTVKMLVDKVKLDVIYGDDDLLSKEITTSDISRPGLEMTGYFDYYSPERLQLLGMKEWSYLTKMTSHNRRHVLREMIKPETPAIIVARNLAIPEEMISAAKEKGIAILQSHVPTSRLSGEMSWYLDSCLAERTSVHGVLMDIYGMGVLIQGDSGIGKSETGLELVKRGHRLVADDRVDVFAKDEETLWGEPAEILRHLLEIRGVGIIDVMSLYGASAVKDSSQVQLAIYLENYESGKVFDRLGNGNEELELSGVKIPRLRIPVQTGRNMSVVIEAAAMNYRAKQMGFDATKTFEERLTQLITKNEGNQ", "text": "FUNCTION: Catalyzes the ATP- as well as probably the pyrophosphate- dependent phosphorylation of 'Ser-46' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl- phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, the HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it probably mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion. SIMILARITY: Belongs to the HPrK/P family."}
{"protein": "MDLIHTFLNLVAPPFTFFFLCLFLPPYWGLKFMVSILSWLLSENVAGKVVHITGASSGIGEYLAYEYAKRGACLALSARRETALHQVADTARHLGSPDVIVMRADVSKPEDCMRLIDQTVNHFGRLDHLVNNAAISIATLFEETPDISNLRPIMETNFWGSVYTTRYALQHLRKSRGKIVVMSSVDSWLPAPRRHIYSASKAALVSLYETLRVEVGSEIGITIVTPGYIESEITKGKFLSAQGEVDVDQDLRDVEVSAVPVGSVSGCAESIIKSTLRGDRCLTVPSWFRMTYLIKLLCPELLEWTFRLLYLTAPGTPTSDALSKKILDATGAKNLFYPPSIQSPDVKTD", "text": "FUNCTION: Has dehydrogenase activity against 11 beta-hydroxysteroid and 17 beta-hydroxysteroid. May be involved in signal transduction regulated by various sterols. SUBCELLULAR LOCATION: Lipid droplet Membrane; Single-pass type II membrane protein Note=Surface of oil bodies. Exists at a monolayer lipid/water interface. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MKTPRRFPLIALTVAAVLTAAALYWWYSHSTASTVQNRQGTEQQRASNSQGSAKRAGNAPPVQAAEALRQNVPQYLSGLGTVTAANTVTLRSRVDGDLVALHFNEGQEVAAGQLLAEIDPRPYEVALMQAEGQLAKDRATLTNARRDLARYEKLAQTQLVSAQELDTQRARVSETLGTIKADEGSVASARLNLTYSRVTAPIAGRVGLKQVDVGNYVSSGDANGIVVIAQTHPIDLVFSLPESDIASVLSAQKNGKLPVEAWDRNNKNLLTRGTLLSMDNQIDSTTGTVKLKARFDNQDDRLFPNQFVNARLKIGTLEDAIVIPAAALQMGNESHFVWVINGDSTVSKKIVASGLQGSGQVVISAGLQAGEKVVTDGIDRLTDGAQTEIVPAQASTPLPASGASS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family."}
{"protein": "MTRKSRRLWLVGACLLGLGTATALVLNAFSSNIVFFMAPSQVRAHPPAADRTIRLGGMVVAGSVRRQTQGDTPIALFDVTDGQAAVTVRYAGILPDLFREGQSVVAVGTVAPDGAFRASEVLAKHDETYMPKEVAEALRRSGKWDPRYGKAPDAASWNTMTVGDARHGEANRS", "text": "FUNCTION: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH (By similarity). Also required for indole-3-acetic acid (IAA) biosynthesis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the CcmE/CycJ family."}
{"protein": "MNNGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASLHAQMRWLPPSEATSQGWKSRQFC", "text": "FUNCTION: Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins (PubMed:26347403). Binds to poly(A) RNA (PubMed:17099224, PubMed:26347403). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, P-body Note=Translocates into cytoplasmic stress granules that probably correspond to P-bodies in response to oxidative stress."}
{"protein": "MKKTEMGRFNISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETDFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGHKAYGLAGKLAASGSITMQNIGAMSSYLFIVKYELPLVIKALMNIEDTNGLWYLNGDYLVLLVSLVLILPLSLLRNLGYLGYTSGLSLLCMIFFLIVVICKKFQIPCPVEAALVANETVNGTFTQAALALAFNSTADDACRPRYFIFNSQTVYAVPILTFSFVCHPAVLPIYEELKSRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYGHVESELLHTYSEIVGTDILLLVVRLAVLVAVTLTVPVVIFPIRSSVTHLLCPTKEFSWLRHSIITVTILSFTNLLVIFVPTIRDIFGFIGASAAAMLIFILPSAFYIKLVKKEPMRSVQKIGALCFLLSGIVVMIGSMGLIVLDWVHDASAAGGH", "text": "FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane (PubMed:34406367). The trasnport is pH-sensitive, Li(+)- intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (By similarity). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (PubMed:16365304). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (PubMed:34406367). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes (PubMed:17050538). Enriched in the somatodendritic compartment of neurons, it is also detected at the axonal shaft but excluded from the nerve terminal (By similarity). SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
{"protein": "MLNLCHALRGVRQFSCSVIVKVKCASCSIKLQDQDPSKPGYYTKPKSLPDSKLNPDLQDLKYLLFSQDIQLSKQAIQNDPDLKTKRDLLLRVICKRCSNALHHNNYNPEEFPESTLNDILNYVPRGSNVMHIVPFVEFPLHLDPNVLKRNDLDTTLVLTKSDQVFKDKNAVSKKVPIFMKQFLKNTLRIDSNKTFAISALKNWNISMFYNYFKNYTYLLGNPNVGKSTLINTLLQKYLGYKVKIDSTGKINSPSEEVMQEAFTNPKNFFKIQAAGVSHIPNLTRSGQAYQVGGKILFDLPGYSTSTSRLRLEEPIDERWLQRLRKTDLFNRKHIKQKTYESMKGTSQGGCYTVGGIFYLVPPKGSINQIVKYIPGPSKTFKNIEKGIDVFNSCNSSSGTHPLSRYCGIKSVICEKSQYKRYAIPPFIGSIEIVLKDIGYILLRTTGRYEFKGLHEIWIPRGIQVGIREPLENLIESGYQRYIETNGKESSCPRDRPIISSLYEMAPDEADTLNAVKKSYLEKTEKDLSARRFVDDDPYDLVQHLEKKKNPYWYYQW", "text": "FUNCTION: Interacts genetically with prohibitins and thus may be involved in the mitochondrial lipid metabolism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. GEP3 subfamily."}
{"protein": "MAFMEKPPAGKVLLDDTVPLTAAVEASQSLQSHTEYIIRVQRGISAENSWQIVRRYSDFDLLNNSLQITGLSLPLPPKKLIGNMDREFIAERQRGLQNYLNVIMANHVLSNCELLKKFLDPNNYSANYTEIALQQVSMFFRSEPKWEVVEPLKDIGWRIRKKYFLMKIKNQPKERLVLSWADLGPDKYLSDKDFQCLIKLLPSCVHPYIYRVTFATASESSALLIRAFNEKGTLKDLIYKAKPKDPFLKKYCNPKKTQGLELQQIKTYGRQILEALKFLHDKGFPYGHLHAANVMLDGNTCRLLDLENSLLGLPSFYRSYFTQFRKINTLESVDVHCFGHLLYEMTYGRPPDSVPVDSFPPASSLAVVAVLESTLSCEACKNGMPTVSRLLQMPLFSDVLLTTSEKPQFKIPTKLKEALRIAKECIEKRLTEEQKQIHQHRRLTRAQSHHGSEEERKRRKILARKKSKRSAVENSEEQPVKHSNSNNSAGSGASSPLTSPSSPTPPSTAGLSSALPPPPPPPPPPPPPAGPSPTSATEMPAPFLPQPVNGVNRGALLSSIQNFQKGTLRKAQTCDHSAPKIG", "text": "FUNCTION: Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and ATP1B3 and may thereby participate in the regulation of electrical excitability and synaptic transmission. May not display kinase activity. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Note=Also associates with the plasma membrane. SIMILARITY: Belongs to the protein kinase superfamily."}
{"protein": "MEDLNEANFSHLLINLSNNKDIDMQYTSTLSVVHELLSAINFKIFNINKKSKKNSKSIEQQHPVVHHAASTGREFNRR", "text": "FUNCTION: Required for the association between the dense viroplasm and the viral membranes to form the mature virion (MV). SIMILARITY: Belongs to the orthopoxvirus OPG157 family."}
{"protein": "MADRLAIFIKQCGLQRCVILTGAGCSTESGVPDYRGPNGLYRRPNFVPLTRQVFLSGSEHRKRYWARSMFGYNTVSGASCNDTHMGLYELYRAGVVNRLLTQNVDGLHHLAAHGGTGSKTVEAYAKYTSSNSGVLELHGNIHQVCCMQCGDVSPRRRLQQRLCEANYQLCRDYEAEFSEVRPDGDYEVPDRVVQAMQLVCCEHCGGLLKPHVVLFGENVPKECVREAYTAVRAASCLICLGTSLQVFSALRFVLAARESGVPIAIVTAGRTRADGLEELKVDTNSTAATMRGVVKQLLGFELGGTK", "text": "FUNCTION: NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the sirtuin family. Class II subfamily."}
{"protein": "MTYDFRAEIVKAKNTGSAKSGSHHWLLQRITAIILVLCSLWLLYFTLANKNSDVNIIIWELKRPINLIPLLIAVITSLYHAMLGMQVVIEDYISCNKLRNTLIIAVKLFSILTIVAFIVAVFYRG", "text": "FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MRLTSKGRYAVTAMLDVALHSQQNPVPLADISERQGISLSYLEQLFSKLRKAGLVASVRGPGGGYRLGMDSYAISIGTVIAAVDESVDATKCNGKGDCQGGTRCLTHTLWRDLSSRITDFLNNITLGELMMDNEVLEVSDRQDLHLAVSQRVSQNNSNTVTIGAAPFGINVRS", "text": "FUNCTION: Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins."}
{"protein": "MATNLSVIMILTFALWVTNPLHELQSTAAFSQTTEKINSNWESGINVDVAVTMQRHHLQQLFYRYGENDSLSVEGFRKLLQNIGIDKIKRVHIHHDHERHSDHERHSDHERHSHRGHAAAGKNSRKAFCPDLDSDNSGKNPNTSQGKGSRPAEHVNGRRNGKESASSSEVTSAVYNTVSEGTHFLETIETPKPGRRTKDINPSTPPSITEKSRVGRLSRLARRKGNDSVSEPRKSFMYSRTSNDNIQECFNATKLLTSHGMSVQALLNATEFNYLCPAIINQIDARSCLIHTASEKKAEIPPKTYSLQIAWLGGFIAISIISFLSLLGVILVPLMNRVFFKFLLSFLVALAVGTLSGDALLHLLPHSHASHHHSHSHEEPAMEMKRGPLFSHLSAQNLEESSYFDSTWKGLTALGGLYFMFLVEHVLTLIKQFKDKKKKNQKKPENDEDVESKKQLSKYESQLSTNEEKVDTGERPESYLQADSQEPSPFDSQQPTLLEEEEVMIAHAHPQEVYNEYVPRGCKNKCHSHFHDTLGQSDDLIHHHHDYHHILHHHHHQNHHPHSHSQRYSREELKDAGIATLAWMVIMGDGLHNFSDGLAIGAAFTEGLSSGLSTSVAVFCHELPHELGDFAVLLKAGMTVKQAVLYNALSAMLAYLGMATGIFIGHYAENVSMWIFALTAGLFMYVALVDMVPEMLHNDASDHGCSRWGYFFLQNAGILLGFGIMLLISIFEHKIVFRINF", "text": "FUNCTION: Acts as a zinc-influx transporter. When associated with SLC39A10, the heterodimer formed by SLC39A10 and SLC39A6 mediates cellular zinc uptake to trigger cells to undergo epithelial-to- mesenchymal transition (EMT). SLC39A10-SLC39A6 heterodimers play also an essentiel role in initiating mitosis by importing zinc into cells to initiate a pathway resulting in the onset of mitosis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MTTPTTLSGAILDPMLRADPVGPRITYYDDATGERIELSAVTLANWAAKTGNLLRDELAAGPASRVAILLPAHWQTAAVLFGVWWIGAQAILDDSPADVALCTADRLAEADAVVNSAAVAGEVAVLSLDPFGRPATGLPVGVTDYATAVRVHGDQIVPEHNPGPVLAGRSVEQILRDCAASAAARGLTAADRVLSTASWAGPDELVDGLLAILAAGASLVQVANPDPAMLQRRIATEKVTRVL", "text": "SIMILARITY: Belongs to the TIGR03089 family."}
{"protein": "MSDFNAIAQQFTEFYYKTFDTDRAQLAPLYRENSMLTFEQSPFLGTANIVGKLQELPFQRIEHQVATVDAQPSNESGGILVVVSGALLVEEERRPMSYTQTFQLLPADGAYYVFNDVFRLVYPAA", "text": "FUNCTION: Facilitates protein transport into the nucleus. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MKKKQQHPGGGADPWPHGAPMGGAPPGLGSWKRRVPLLPFLRFSLRDYGFCMATLLVFCLGSLLYQLSGGPPRFLLDLRQYLGNSTYLDDHGPPPSKVLPFPSQVVYNRVGKCGSRTVVLLLRILSEKHGFNLVTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSRFGGDQPVYINIIRDPVNRFLSNYFFRRFGDWRGEQNHMIRTPSMRQEERYLDINECILENYPECSNPRLFYIIPYFCGQHPRCREPGEWALERAKLNVNENFLLVGILEELEDVLLLLERFLPHYFKGVLSIYKDPEHRKLGNMTVTVKKTVPSPEAVQILYQRMRYEYEFYHYVKEQFHLLKRKFGLKSHVSKPPLRPHFFIPTPLETEEPIDDEEQDDEKWLEDIYKR", "text": "FUNCTION: Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N- resulfated heparin. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 3 family."}
{"protein": "MSLLIKNGTIVNDDAIFKSDVLVLDGRIVEIAPSIQPTPGLEVVDATDRLVIPGGIDPHTHMQLPFMGEIAKDDFHRGTEAAVAGGTTMIIDFVIPTKGESLLVAYDRWRGWADPKVVCDYGLSMAITSWGPEIAKEMEIVTGAEYGINSFKFFLAYAGVFMVRDEEFYQGMIQCAKLRALARVHAENGSVIAERCEHLLSSGITGPEGHTQSRPEELEAEATFRACTMASQANCPLYVVHVMSKGAAAAIAHHRKKGAVVFGEPIAAGLATDGSHYYNEDWLHAARYVMSPPLSRDPSTPSALMKLLAAGELHLTATDNCTFDCQQKSLGKDDFTKIPNGVNGVEDRMSVVWDKGVHAGIIDPMRFVAVTSTMAAKIFNCYPQKGRIAVGSDADIVIWNANATRTISKDTHHHAIDFNIFEGMQVHGVPEITISRGRTVWANGQLKTVQGSGQFIPLAPDSQIVFSAVDNRKKAMEPVKIDRIPYEPSALQTPDANANIVVKAPVRAAIPPGGASSIQF", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family."}
{"protein": "MRRTGPEEEACGVWLDAAALKRRKVQTHLIKPGTKMLTLLPGERKANIYFTQRRAPSTGIHQRSIASFFTLQPGKTNGSDQKSVSSHTESQINKESKKNATQLDHLIPGLAHDCMASPLATSTTADIQEAGLSPQSLQTSGHHRMKTPFSTELSLLQPDTPDCAGDSHTPLAFSFTEDLESSCLLDRKEEKGDSARKWEWLHESKKNYQSMEKHTKLPGDKCCQPLGKTKLERKVSAKENRQAPVLLQTYRESWNGENIESVKQSRSPVSVFSWDNEKNDKDSWSQLFTEDSQGQRVIAHNTRAPFQDVTNNWNWDLGPFPNSPWAQCQEDGPTQNLKPDLLFTQDSEGNQVIRHQF", "text": "FUNCTION: DNA-binding protein that accumulates at DNA double-strand breaks (DSBs) following DNA damage and promotes DNA resection and homologous recombination (PubMed:29042561). Serves as a sensor of DNA damage: binds DNA with a strong preference for DNA substrates that mimic structures generated at stalled replication forks, and anchors RBBP8/CtIP to DSB sites to promote DNA end resection and ensuing homologous recombination repair (PubMed:29042561). Inhibits non- homologous end joining (NHEJ) (PubMed:29042561). Required for the dynamic movement of AURKA at the centrosomes and spindle apparatus during the cell cycle (PubMed:20596670). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Note=Accumulates at sites of DNA damage by binding to DNA substrates that mimick structures generated at stalled replication forks (PubMed:29042561). Localizes to the centrosome in interphase and to the spindle pole in metaphase (PubMed:20596670). SIMILARITY: Belongs to the AUNIP family."}
{"protein": "MFALRAASKADKNLLPFLGQLSRSHAAKAAKAAAAANGKIVAVIGAVVDVQFDDNLPPILNALEVDNRSPRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFQVAEVFTGHAGKLVPLEQTIKGFSAILAGDYDHLPEVAFYMVGPIEEVVEKADRLAKEAA", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MSFKNRGDYNFTPRNVVSRNSVFFMCLASFCLGMFFTNRMWNIVPEARGISRLSKLSLSSSDCDKKNVLDYGNNTIGILDKSISNLEMKLVAARAERESLSGKFNISNEAKKRKYFMVIGINTAFSSRKRRDSVRSTWMPQGENLKKLEEEKGIIVRFVIGHSVLSHGILDKAIEAEEKTHGDFLRLEHTEGYMKLSAKTKTFFATAVSLWDAEFYIKVDDDVHVNLASLKKALSAHQNKPRVYVGCMKSGPVLARKSVKYHEPEYWKFGEVGNKYFRHATGQFYAISKDLATYILINQDLLHKYANEDVSLGSWFIGLNVEHVDEKRLCCSTSQDCELKAMMGHVCAASFDWKCSGICRSAERMADVHERCGEPQNALWTSNS", "text": "FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family."}
{"protein": "MSLSVLSRKEKEKVIHRLLVQAPPGEFVNAFDDLCLLIRDEKLMHHQGECAGHQHCQKYCVPLCIDGNPVLLSHHNVMGDFRFFDYQSKLSFRFDLLQNQLRDIQSHGIIRNETEYLRSVVMCALKLYVNDHYPNGNCNVLRKTVKSKEFLIACIEDHSYDNGECWNGLWKSKWIFQVNPFLTQVTGRIFVQAHFFRCVNLHIEVSKDLKESLEVVNQAQLALSFARLVEEQENKFQAAVIEELQELSNEALRKILRRDLPVTRTLIDWQRILSDLNLVMYPKLGYVIYSRSVLCNWII", "text": "FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the morphogenesis of spermatid. SIMILARITY: Belongs to the F-actin-capping protein alpha subunit family."}
{"protein": "MAFLSLFLCLVFSSPLMAMPPALQGRKAISPASILKGPSTDNGARDFHGRKFPHFMMQLYQNIISRRDKDLSNLEHPTLQESDTVQSFIAKSYTTVGNHWTLFFDMSSISTNNELKLAELRICLPSFGKSHSVTVEIYHTKDTKEKLFMGSFKTKISSALDADCKVFNLTMVLHNYLIRGKRLIKDEYIQAKGLLLRDLEKSAAEKGAENVDTLKQDKHHVSDFAAERIILVVFAKERSQAKPDPPSLGKQLFPLKYGMADNANKVNGFRRLRRNKKEKTRMDVGTTPPKPVEEIKPKCRKVDMFVDFQKIGWGSWIVYPKAYNAYRCESACAVPLNETDDATNYSYIKSLLPLSDTERRECPSCVPVKMRSMSMLYYENEEFILRHHEEMIVEECGFKDI", "text": "FUNCTION: Exhibits mesoderm-dorsalizing activity and neural-inducing activity, but lacks mesoderm-inducing activity. Regulates the expression of specific mesodermal and neural genes. Induces convergent extension movements at the embryonic midline by activating the fgf signaling pathway to induce t/bra expression in the organizer region. Acts with wnt11 to induce Spemann organizer cells and induce axis formation (By similarity). The unprocessed protein antagonizes bmp- signaling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MALFAVFQTTFFLTLLSLRTYQSEVLAERLPLTPVSLKVSTNSTRQSLHLQWTVHNLPYHQELKMVFQIQISRIETSNVIWVGNYSTTVKWNQVLHWSWESELPLECATHFVRIKSLVDDAKFPEPNFWSNWSSWEEVSVQDSTGQDILFVFPKDKLVEEGTNVTICYVSRNIQNNVSCYLEGKQIHGEQLDPHVTAFNLNSVPFIRNKGTNIYCEASQGNVSEGMKGIVLFVSKVLEEPKDFSCETEDFKTLHCTWDPGTDTALGWSKQPSQSYTLFESFSGEKKLCTHKNWCNWQITQDSQETYNFTLIAENYLRKRSVNILFNLTHRVYLMNPFSVNFENVNATNAIMTWKVHSIRNNFTYLCQIELHGEGKMMQYNVSIKVNGEYFLSELEPATEYMARVRCADASHFWKWSEWSGQNFTTLEAAPSEAPDVWRIVSLEPGNHTVTLFWKPLSKLHANGKILFYNVVVENLDKPSSSELHSIPAPANSTKLILDRCSYQICVIANNSVGASPASVIVISADPENKEVEEERIAGTEGGFSLSWKPQPGDVIGYVVDWCDHTQDVLGDFQWKNVGPNTTSTVISTDAFRPGVRYDFRIYGLSTKRIACLLEKKTGYSQELAPSDNPHVLVDTLTSHSFTLSWKDYSTESQPGFIQGYHVYLKSKARQCHPRFEKAVLSDGSECCKYKIDNPEEKALIVDNLKPESFYEFFITPFTSAGEGPSATFTKVTTPDEHSSMLIHILLPMVFCVLLIMVMCYLKSQWIKETCYPDIPDPYKSSILSLIKFKENPHLIIMNVSDCIPDAIEVVSKPEGTKIQFLGTRKSLTETELTKPNYLYLLPTEKNHSGPGPCICFENLTYNQAASDSGSCGHVPVSPKAPSMLGLMTSPENVLKALEKNYMNSLGEIPAGETSLNYVSQLASPMFGDKDSLPTNPVEAPHCSEYKMQMAVSLRLALPPPTENSSLSSITLLDPGEHYC", "text": "FUNCTION: Associates with IL31RA to form the IL31 receptor. Binds IL31 to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing OSM-specific signaling events. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily."}
{"protein": "MMQQRSGSLSLLSNAVQAGQSSDPMQDDPAKTEPGTPKGYDGSKNSSPASVPSWIHEKTKAGKDRKRLPLACQSCRKKKVKCSGERPSCDQCLKHNIPCIYKSNSTKRSHSRHEEIHHQQQLHLNHQYQHQHKNVAANSIDNLSRQYSQPNHINTHDSVNSPPSYGIMASATNQPLSHPTIVPSSNSSSLLNSTNNISHNPQVSLMSASLSKNLVLDPASPKSVSPDLVYVSSDNPPVSTAASAYSSSLPISDVTRALPLAPASNSQHPSLSSQPVSVPSNTINIPTDSLSIVSNPSQTPAKFDSNRISQVPNSDYSIYSNFNNFPIANHAPSFPQSSVKKLDSSFSPTSLPTFTTNSASSGLSTSYTNNNDTTSDNNSLQAVPRLDPVPSLTLSSTPVAELPPLELRIHLAEVFFHCCHGQSYNLFHRPTFFESLNNNTVPLVVVYAVCAVSARFSSRMHDRFSPPYMAGEQYAREARRLALDNFDRPDLSLVAALLLLSLHDSGTCETGKSWMYGGMALRMAAALQLNCEQGSNPLDLDNIDSGPRISFLERELRRRTFWSCFLMDRYASSHEHLQFLDENDIGIQLPVHELLFTKQIAGVTQTLDGRILEGVPSIVIPADTTENMGVAAYTVKIIALWGRAVKYLKQDGKRRDPYPYWHRNSDFSHISEALYAWADGLPQRLKYSAVGLENHLSIQQGAQYAFLHLAYHHTLMWLFRSIGETENNQLSKISSSVSLAGNTVSFSPVSHTPINVTNGESQNNSNNDPSANGAARRLHKAAREICLRCANAISMIVDDCRKHNVILTSPFIASGVYTAFCVQAEAAFGSNVLAASTARHNLEIDLRLMLEMKNYWGSISALCDKMSEIWADWVQRTSSGIQEEDTIPNEMIDEERMLDLEKHFMYITESPIVPNQAAQKSYSPDLMSYFGFAKNSDLQQWNGLWPSDDLRNYQESTIDSLVAYATGNPGWNISFAG", "text": "SUBCELLULAR LOCATION: Cytoplasm. Nucleus."}
{"protein": "MNMQKLRIELGEETNDELYDLLLLADPSKDIVDEYLERGECYTAWAGDELAGVYVLLKTRPQTVEIVNIAVKESLQKKGFGKQLVLDAIEKAKKLGADTIEIGTGNSSIHQLSLYQKCGFRIQAIDHDFFLRHYDEDIFENGIQCRDMVRLYLDL", "text": "FUNCTION: Probable N-acetyltransferase."}
{"protein": "MKHQYFAKKSFLFISMLAAFKTSAFELPSVPFPAPGSDEILFVVRDTTFNTQAPVNVKVSDFWTNRNVKRKPYEDVYGQSVFTTSGTKWLTSYMTVNINDKDYTMAAVSGYKSGHSAVFVKSGQVQLQHSYNSVANFVGEDEGSIPSKMYLDETPEYFVNVEAYESGSGNILVMCISNKESFFECKHQQ", "text": "FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined. SIMILARITY: Belongs to the TDH hemolysin family."}
{"protein": "MKKIEAIIKPFKLDEVKEALQAAGVQGLSVTEVKGFGRQKGHTELYRGAAYVVDFLPKVKIEVVLADDMVEAAVEAIVSASRTDKIGDGKIFISPVEQAIRIRTGETGEDAV", "text": "FUNCTION: P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme. SIMILARITY: Belongs to the P(II) protein family."}
{"protein": "MDFKEILYNVDNGVATLTLNRPEVSNGFNIPICEEILKAIDIAKKDDTVQILLINANGKVFSVGGDLVEMQRAVDADDVQSLVRIAELVNKISFALKRLPKPVVMSTDGAVAGAAANIAVAADFCIASDKTRFIQAFVNVGLAPDAGGLFLLTRAIGITRATQLAMTGEALNAEKALEYGIVYKVCEPEKLEKITDRVITRLKRGSVNSYKAIKEMVWQSSFAGWQEYEDLELELQKSLAFTNDFKEGVRAYTEKRRPKFTGK", "text": "FUNCTION: Catalyzes the isomerization of trans-2-decenoyl-ACP to cis-3- decenoyl-ACP (By similarity). Required for survival at low pH. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MNMAERAEATKSWSCEPLSGKTLEEIVQNAENAADLVAYIRKPEVDLDFRLKFIAEHEEFFNVQLSDRNSRIRTCHNLSDKGIRGDTVFVFVPGLAGNLEQFEPLLELVDSDQKAFLTLDLPGFGHSSEWSDYPMLKVVELIFVLVCDVLRKWSTAVPNNDNVNPFNGHKIVLVGHSMGCFLACHLYEQHMADTKAVQTLVLLTPPKAHIEQLSKDKHIIQWALYGVFKLPWLFDVYRNKFDQVKGLQSSGIKQYFYQQGDDVKLKYRKFWQFKNNISNKSRTIIGYLLGWETVDWVKFNGVLTQTDMKQKIIIFGAEKDPIAPIENLEFYKQTINKECLRKVIILPDCSHNLCFDRPELVCENFQREVIDNSKL", "text": "FUNCTION: Serine hydrolase required for the maintenance of steady state level of non-polar and polar lipids of lipid droplets and thus plays a role in maintaining the lipids homeostasis (PubMed:21478434). Exhibits both esterase and triacylglycerol lipase activity (PubMed:21478434). SUBCELLULAR LOCATION: Lipid droplet. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MAWPRIFQRGALLSRFSHHHMVVFLLTFFSYSLLHASRKTFSNVKVSISKQWTPSAFNKSTELLPVEIWSSNHLFPSAEEATLFLGMLDTIFLFSYAVGLFISGIVGDRLNLRWVLSFGMCSSALVVFVFGTLTEWLHFYNKGLYCSLWIVNGLLQSTGWPCVVAVMGNWFGKAGRGVVFGLWSACASVGNILGACLASSVLQYGYEYAFLVTAAVQFAGGIIIFFGLLVSPEEIGIPGIETEDNFEEDSHRPLINGAENEDEAEPNYSIQEGNTVTQVKAISFYQACCLPGVIAYSLAYACLKLVNYSFFFWLPFYLSNNFGWKEAEADQLSIWYDVGGIIGGTLQGFISDMLQKRAPVLALSLLLAIGSLVGYSRSPNDKSINALLMAVTGFFIGGPSNMISSAISADLGRQELIQGSSEALATVTGIVDGTGSIGAAVGQYLVSLIQDNLGWMWVFYFFILMTSCTVLFISPLIVRETCSLMQRRQTRVLNE", "text": "FUNCTION: Unlike the other SLC37 members, lacks glucose-6-phosphate antiporter activity. In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containg-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family."}
{"protein": "MENGIKESPVGLNKNGALAILPTPLVSEGHKNHKSVLNSLTSGALAGAVAKTAVAPLDRTKIIFQVSSNRFSAKEAYRLIYRTYMNDGFLSLWRGNSATMVRVIPYAAIQFCAHEQYKKLLGSYYGFQGSALTPIPRLLAGALAGTTATLLTYPLDLVRARMAVTQKEMYSNIIHVFMRMSREEGLKSLYRGFTPTVLGVIPYAGISFFTYETLKKLHAEHSGRTQPYTFERLLFGACAGLFGQSSSYPLDVVRRRMQTAGVTGHTYGSIIGTMQEIVAEEGFIRGLYKGLSMNWVKGPVAVGISFTTFDLTQILLKKLQQISHIQR", "text": "FUNCTION: Mitochondrial carrier mediating the transport of coenzyme A (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine nucleotides and adenosine 3',5'-diphosphate. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MGSSSLLLVCLAGMVYLTEAAPLVSHGSIDSKCPLMVKVLDAVRGRPATSIAVKVSKMSEEGDWKEFANGKTNEFGEIHELTTDEQFVQGLYKVEFDTSSYWKALGVSPFHEYADVVFSANDSGHRHYTIAALLSPFSYSTTAVVSDPKE", "text": "FUNCTION: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the transthyretin family."}
{"protein": "MNDVKLTVLGGEGTGKSALIVRFLTKRFIGEYASNFESIYNKHLCLEGKQLNLEIYDPCSQPQKAKFSLTSELHWADGFVIVYDISDRSSFAFAKALIYRIREPQTSHCKRPVESAVLLVGNKQDLCHVREVGWEEGHKLALDNRCQFCELSAAEQSLEVEMMFIRIIRDILTNFKLKEKRRYSGSKSMAKLINNVFGKRRKSV", "text": "FUNCTION: Binds GDP/GTP and may possess intrinsic GTPase activity. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
{"protein": "MGFSLSNFTSDPFAISTVSFGIMAWVVAIAGAASSKQENFPHFSWWGISYQIVIILIIFVLYANNNIELYKFTLVGLVSIAFIYTTNSTNNLIYNSNSAGNLCCAAGCILLSILNLIWILYFGGHPESPTNQFIDSFSLRGQGHEQLGSGSHNHNANNANNNIPIGAGNAIIGKGEMSPYDDRFAASGVNQPTSESLRLASGPQMGNGPFTTTGAIINPNLQQPLSGSIGGSAHHTPTNINNNNNNNNNTGYMTSSHLTGLENFSSPHVPGSGAGAGLGVGAGRDLTHNSNGGGGGSGGGPASANNSNNTNKRNTIYTDSETGTGITFRYKAKALYSYDANPDDINEISFVKDEILEVDDIDGKWWQARRANGQVGICPSNYVKLLDT", "text": "FUNCTION: Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Mediates resistance to oxidative stress. Controls the activation of the CEK1 MAP kinase. Influences the molecular weight and polymer distribution of cell wall mannan. Involved in invasive filamentation into semi-solid medium and plays a role in morphological dimorphic transition which is a differentiation program characteristic of C.albicans and which is known to play a major role in pathogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SHO1 family."}
{"protein": "MAGLPVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGESISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLISGNPQPVHVAGPGSGPNVSMNQQNPQAPQAQSLGGMHVNGAPPMMQASMPGGVPAPVQMAAAVGGPGPGSLAPAGVMQAQVGMQGAGPVPMERGQVPMQDPRAAMQRGALPTNVPTPRGLLGDAPNDPRGGTLMTVTGDVEPRAYLGPPPPPHQGPPMHHVPGHEGRGPPPHDMRGGPLAEPRPLMAEPRGPMLDQRGPPLDARGGRDPRGLDARGMEARAMEARGLDARGLEARAMEARAMEARAMEARAMEARAMEARAMEARGMDTRGPVPGPRGPMPSGIQGPNPMNMGAVVPQGSRQVPVMQGAGMQGASMQGGSQPGGFSPGQSQVTPQDHEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAP", "text": "FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Localized with DDX1 in cleavage bodies."}
{"protein": "MATSHFILKLFLVISFCNVCFASRKLTALVQEPENQLLQYHKGALLFGKISVNLIWYGKFKPSQRAIVSDFITSLSSSTPSKTDPSVAKWWKTTEKYYHLANSKKSLSLYLGKQVLVENYSLGKSLTQKQIVQLASKGEQKDAINIVLTASDVAVDGFCVNRCGTHGSSKGAIIRGKTYKFAYIWVGNSETQCAGYCAWPFHQPIYGPQSPPLVAPNNDVGVDGMVINLASLLAGTATNPFGNGYYQGEADAPLEAASACPGVYAKGAYPGYAGDLLVDKTTGASYNAHGTNGRKYLLPALYDPSTSTCSTLV", "text": "FUNCTION: May be involved in the regulation of cell division. SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the EXORDIUM family."}
{"protein": "MTAAVFFGCAFIAFGPALALYVFTIATDPLRVIFLIAGAFFWLVSLLLSSVFWFLVRVITDNRDGPVQNYLLIFGVLLSVCIQELFRLAYYKLLKKASEGLKSINPEETAPSMRLLAYVSGLGFGIMSGVFSFVNTLSNSLGPGTVGIHGDSPQFFLNSAFMTLVVIMLHVFWGVVFFDGCEKNKWYTLLTVLLTHLVVSTQTFLSPYYEVNLVTAYIIMVLMGIWAFYVAGGSCRSLKLCLLCQDKDFLLYNQRSR", "text": "FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (amyloid-beta precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Probably present in a minority of gamma-secretase complexes compared to APH1A (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the APH-1 family."}
{"protein": "MFRTLLSSTVRSIQLKPVTSTLSTTIPSITSIPTVSYFSTSPINYKTNTSTRTKENVHDLTTFLTLIGRNSIEYKDLFEDDLNKFLSTTSAQMKNMGIDTRARRYLLRWRHKFLNDLEPLREHKLGKKRNGGERKAKTVIAKRQALERLEEKEKWAQEELEAEKRGERLF", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mS41 is involved in telomere length regulation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS41 family."}
{"protein": "MAAGPISERNQDATVYVGGLDEKVSEPLLWELFLQAGPVVNTHMPKDRVTGQHQGYGFVEFLSEEDADYAIKIMNMIKLYGKPIRVNKASAHNKNLDVGANIFIGNLDPEIDEKLLYDTFSAFGVILQTPKIMRDPDTGNSKGYAFINFASFDASDAAIEAMNGQYLCNRPITVSYAFKKDSKGERHGSAAERLLAAQNPLSQADRPHQLFADAPPPPSAPNPVVSSLGSGLPPPGMPPPGSFPPPVPPPGALPPGIPPAMPPPPMPPGAAGHGPPSAGTPGAGHPGHGHSHPHPFPPGGMPHPGMSQMQLAHHGPHGLGHPHAGPPGSGGQPPPRPPPGMPHPGPPPMGMPPRGPPFGSPMGHPGPMPPHGMRGPPPLMPPHGYTGPPRPPPYGYQRGPLPPPRPTPRPPVPPRGPLRGPLPQ", "text": "FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex (PubMed:27720643). SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well (PubMed:10882114). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SF3B4 family."}
{"protein": "MESLSELQNPLLPRSPAHLHGPYPYPETPPSWSCQEKLYSYLLGGAGPAGAHQLLDPGSLQLAVEAWYRPSCLLGRDKVKEPRAGSCETSFTEDREPQEGPPEQPTGPGQAAENVTIQTVSYGVQEELRDQEDDQEEEESDATSTESESEDNFLTLPPRDHLGLTLFSMLCCFWPLGIAAFYFSQGTSKAISKGDFRLASTTSRRALFLATLAIAVGAGLYVAVVVALAAYMSQNGHG", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Golgi apparatus, cis-Golgi network. SIMILARITY: Belongs to the CD225/Dispanin family."}
{"protein": "MFSLISAGVAPGVALLSYFYLKDEYEAEPLSFVLRMFLFGVLLVFPIMFIQYVLAAEGIVASPAAEAFLSAALLEEFVKWFVVYFFVYDHDEFDEPYDGIVYSASVSLGFATLENILYLLANGVETAIARALLPVSSHALFSVIMGFYFGKAKFAVKKRRYYLWASFLLPFFLHGVYDWLLLAKERWGYYMGLFMLALWWAALRKVKQAKGYARPQAVPPVKSQA", "text": "FUNCTION: Involved in the degradation of specific anti-sigma factors. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the protease PrsW family."}
{"protein": "MTLRQALGEAVRRLAAGGVERPRLEAEVLLGWACSLTRPRLLARLEEELAPAAAGRFWQAIDRRAAGYPLQYLTGHQEFMSLDFKVTPAVLIPRQDTEVVVEAVLERLDPCESYTIADCGTGSGAIALSLAHYLPRARVYATDISPAALTVAQENARKLGLAARVTLLQGDFLAPLRGLKLDALVANPPYIPTAALPGLPADVRSEPRLALDGGPDGLDAYRFLLPGAAGLLRPGGLLALEIGSDQGQAVKDLARAVGAYRNEQVLPDYAGRDRCFLAYRREE", "text": "FUNCTION: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif. SIMILARITY: Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily."}
{"protein": "MAEEVWVGTWRPHRPRGPIMALYSSPGPKYLIPPTTGFVKQTPTKLRAPAYSFRGAPMLLAENCSPGPRYSVNPKILRTGKDLGPAYSILGRYHTKTTLTPGPGDYFPEKSTKHVFDSAPSHSISARTKTFRVDSTPGPAAYMLPMVMGPHTIGKVSQPSFSIKGRSKLGSFSDDLHKTPGPAAYRQTDVQVTKFKAPQYTMAARVEPPGDKTLKPGPGAHSPEKVTMTRPCAPVVSFGIKHSDYMTPLVVDVD", "text": "FUNCTION: Outer dense fibers are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail. May help to maintain the passive elastic structures and elastic recoil of the sperm tail. SUBCELLULAR LOCATION: Cytoplasm Note=Expressed in the cytoplasmic lobe of spermatids. SIMILARITY: Belongs to the ODF3 family."}
{"protein": "MGRLLGFLLALGPWALVAGVVIRGPTISLVSDSLLAAGAVGANGSFLEDLEVPGELHFLGPQVPHVTYYDGSVELLHYPPDARCPRAVLVEEMTACPRRNAVAFTLCRS", "text": "FUNCTION: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells. In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Host cell membrane; Single-pass type I membrane protein Host cell junction Host Golgi apparatus membrane; Single-pass type I membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). The heterodimer gE/gI then redistribute to cell junctions to promote cell-cell spread later in the infection (By similarity). SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein I family."}
{"protein": "QAKVTWSLKAAEEAEAVANINCSGHGRAFLDGILSDGSPKCECNTCYTGADCSQKITGCSADVASGDGLFLEEYWQQHKENSAVLVSGWHRTSYFFNPVSNFISFELEKTIKELHEIVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTATPCAPQSKVVAHAPYYPVFREQTKYFDKKGYEWKGNAADYVNTSTPEQFIEMVTSPNNPEGLLRHEVIKGCKSIYDMVYYWPHYTPIKYKADEDIMLFTMSKYTGHSGSRFGWALIKDETVYNKLLNYMTKNTEGTSRETQLRSLKILKEVTAMIKTQKGTMRDLNTFGFQKLRERWVNITALLDKSDRFSYQKLPQSEYCNYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQSGEGFEAGSRYVRLSLIKTKDDFDQLMYYLKIMVEAKRKTPLIKQLSNDQISRRPFI", "text": "SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the alliinase family."}
{"protein": "MRKRISAIIMTLFMVLASCSNQLEAEKLAAESKNTFFDSLVKIGQGFQDIFGIFGNAIGDALGFNAVKSDDKRSKVGEHFEGVGEGLKDTKIKLDELLKEVTAAPHADTTEVKSVINNAGAVLTKLIDSVAKLAGATKSEAPIGDAGTAQAAAATPADIADVNTVIEGVKKIIEVAEKSGVKIEKGTAGAQVANANGPKVLTNNAQADANSGPALAAEVDKADPWAMIDKIKMLKLLLHLLHLRLMMTPGQLATGSANAANNGTAATNADLAAAVALKAITKGGKFTQPAANEDGAVKVAAASAVNKVLGILDAIIRKAVNLELGKIKEAVKGIKYSEITGEATESGIDQPITNKSSN", "text": "FUNCTION: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the variable large protein (Vlp) family. Beta subfamily."}
{"protein": "MADTDCKWDPGADKYPLLGFGQAVIGPPGSGKSTYVRAMQALLAQMGRKSAIINLDPAGEDEPGAAVSLRELLGLEEVMSELRLGPNGALLYCMEYLQENLDWLRGRLQGLRGTYFLLDCPGQVELYTHHPALPDVLRRLGAWGLRLCAVHLVDSHYCTDPAKFISVLCTSLSTMLHVELPHINVLSKMDLIEQYGRLAFNLDYYTEVMDLSYLVEQLTSDPFFRRHKRLHEKLAEVIQDYGLVTFMPLSIKDEKSLRLVLSAVDKASGFCFGETKQSLGNLMSVAVGADFQFTSYPSHDCRG", "text": "FUNCTION: Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import. SIMILARITY: Belongs to the GPN-loop GTPase family."}
{"protein": "MNKSILLLVTLLSLYSCTDTEKTPLEEKDVFNEDYIKTSMIKALEWQEAHPIFAIHPTDWTNGAYYTGVARAHHTTKNMMYMAALKNQAVANNWQPYTRLYHADDVAISYSYLYVAENEKRRNFSDLEPTKKFLDTHLYEDNAWKAGTNRSKEDKTILWWWCDALFMAPPVINLYAKQSEQPEYLDEMHKYYMETYNRLYDKEEKLFARDSRFVWDGDDEDKKEPNGEKVFWSRGNGWVIGGLALLLEDMPEDYKHRDFYVNLYKEMASRILEIQPEDGLWRTSLLSPESYDHGEVSGSAFHTFALAWGINKGLIDKKYTPAVKKAWKAMANCQHDDGRVGWVQNIGAFPEPASKDSYQNFGTGAFLLAGSEILKMR", "text": "FUNCTION: Glucuronyl hydrolase involved in ulvan degradation. Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3- sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L- iduronic acid (IduA), or D-xylose (Xyl). Unsaturated 3S- rhamnoglycuronyl hydrolase works together with ulvan lyases to fully degrade the ulvan polymer, catalyzing specifically the cleavage of the unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) of deltaUA-Rha3S disaccharides and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides, the end products of the ulvan lyase reaction. Also hydrolases deltaUA-Rha3S-IduA-Rha3S and deltaUA-Rha3S-GlcA-Rha3S tetrasaccharidestetrasaccharides. Prefers tetrasaccharides over disaccharides and prefers an uronic residue at subsite +2. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 105 family."}
{"protein": "MLVGADDKSLLARFYHADRALTAVASELDSFDGRAEPVRCTRLVGRLRQGQDRVLAITNQIMDELLGEDRAARAFRAKFPEEVLQESLAGQLWFGAECLAAGSSIMNREVESATMRPLAKAVTKSLDNVRNLLREQCLRNNTPNSLTLRLDVNDAATEQLYESLKIFDRLFAEFELLYVSAMVQVKSKQEYEMQELICVLFSETLQRALKVGLLEQEQVDSYDPALMFSIPRLAIVAGLVIFKEGPLNMDQPADDISEMFRPFRKLLIKMRDLLRTLTKHELYQLEKLLCTNEEISLKEQQIICDGNEIVGGGQSPSAAPNPARDDTVVIVTTSATVNSSDNLRGQEPQEDISSFYTSNNRRTVDSEPNEDDDVSESNDEDEDEGEEVDEDDPANILKDALVTSDCASGYLIPNTNFGNLLQTNEAPLTDSFIATDEELKLASGAASSHARIEQILSESNQKLTDSGLGTANPSLDHSPELETERPVTSSHPIAQSSSSSSEEEGEVDEYDEDDSESTLCEPKPHHTKHQRRHRHHHHHHRKHYSKHRSSAAGSAGTSGTTCSAAERQISSCDTSPSSGGLPSECGSSTSGGSSGNSSGGSGDADAAQEVAMAIRAAGRIKFKTTENLLHRLFVCIAGVADQLQTNFAADLRQMLKSVFVINSSPPEPEDPPEPAANSTDKPKEPDPADLFEFRASEQDVITNSGGSSQSIYSAEEVNAEDPHDSVFGSPPGGASPVRASSAPRTMMTTAASSENGSVTVNVSVSVVTAGSGGSGSGSSRSSQERSVSLSETSIVVDGSGGNTEGTALLVPRESTPKSVQSEQSGQRGMMEERRMPEAPPRWIPDGDAPRCMACASSFTPFRRRHHCRNCGGVFCGGCSSASAPLPKYGLTKAVRVCRECFVREVGV", "text": "FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR) signaling. SIMILARITY: Belongs to the lst-2 family."}
{"protein": "MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRKFTEIYEFHKMLKEMFPIEAGEIHTENRVIPHLPAPRWYDGQRAAESRQGTLTEYFNSLMGLPMKISRCPHLLNFFKVRPDDLKLPNDSQVKKPETYLTAKDGKNNVADITGPIILQTYRAIADYEKGSKTEMTVATGDVVDVVEKSESGWWFCQMKTKRGWVPASYLEPLDSPDEAEDPDPNYAGEPYVTIKAYAAVEEDEVSLSEGEAIEVIHKLLDGWWVVRKGDITGYFPSMYLQKAGEEITQAQRQIRSRGAPPRRSTIRNAQSIHQRSRKRLSQDTYRRNSVRFLQQRRRPARPGPQSPDSKDNPSTPRAKPQPAVPPRPSSDLILHRCTESTKRKLTSAV", "text": "FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MPVTDPELVAIVQKRVLKKYVCRKCGALNPWGATKCRRCKSTNLRPKHYELGGKR", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL40 family."}
{"protein": "MKFLYGIVFIALFLTVMFATQTDGCGPCFTTDANMARKCRECCGGIGKCFGPQCLCNRI", "text": "FUNCTION: Toxin with unknown function in healthy organisms. On glioma cells, inhibits chloride currents in a voltage-dependent manner (when tested on gliomas cells) (PubMed:17166663). Also interacts with MMP2 and significantly inhibits its catalytic activity (PubMed:21424168). May be internalized with chloride channels (probably ClC-3/CLCN3) and MMP2, thus inhibiting the chloride channels necessary for cell shrinkage and tumor propagation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family."}
{"protein": "MGRDVLNFNVDWLYIPEDLNDAYKFDFDESNFEVVSLPHANKTFPHHYFKEEDYRFVSWYRKHFKVDERYKGKKVYIHFEGVITVAKVYVNGEFVGEHKGGYTPFEFDITEYIKYGNFENLIAVQVDSREHKDIPPEGHLVDYMLFGGIYRNVWLKILNDTHIKDVYFVVDKLQDSVAEISITTTIAGKEISNGKILTEVINKEGVVCSSVVTDIKEMQKEIVQQIKMDNPLTWHPDHPYLYNVSVKLIAENEILDNYTFKTGIRTVEFRDDGKFYINGEPLKLRGLNRHQTFPYVGGAMPDRVQRKDADILKYELGLNYVRTSHYPQAVSFLDRCDEIGLLVFEEIPGWQHIGDENWKNIAKENLKEMILRDRNHPCIFMWGVRINESLDDHDFYKEMNEIAHKLDRSRPTGGVRYLRDSEKLEDVFTYNDFIYNLEGKIQLPNHKKYMVTEYMGHMYPTKSYDNLNRLITHARLHALIQDKQYGIPNMAGASGWCAFDYNTTSAFGSGDNICYHGVCDIFRLPKFAAHFYRSQADPHLYGPYVFIASYLIPSFEEENGDKLLVFSNCEEVELYINDKFVKRQMPNRVDFPSLPHPPFEFSMKECGINYMEVRVNNASITAIGLIDGKEVARHTLRPYGKPHKLILSCDDNEIMADGADCTRVVVSVVDENGSILPYANIPVSFEIEGEGKLIGENPLTLEAGRGAVYVKSTRKPGEIILKAKSHYVAEESNVSIKTKSIGY", "text": "FUNCTION: Beta-galactosidase. SIMILARITY: Belongs to the glycosyl hydrolase 2 family."}
{"protein": "MEHHSHQEHENHTSHGNHEHHHHGNFKSKFFISLIFAIPIIILSPMMGVKLPFQISFTGSDWIVLILATILFFYGGKPFLSGAKDEISTKKPGMMTLVALGISVAYIYSLYAFYMNNFSGSSTHTMDFFWELATLILIMLLGHWIEMNAVGNAGNALKKMAELLPNTAVKLIDNNQREEVKISDIHIDDIVEVRAGESIPTDGIIVRGETSIDESLVTGESKKVHKTHNDDVIGGSINGSGTVQVKVTATGENGYLSQVMGLVNQAQNDKSKAELLSDKVAGYLFYFAVSIGLISFIVWMLIQNNVDFALERLVTVLVIACPHALGLAIPLVTARSTSIGAHNGLIIKNRESVEIAQHIDYIMMDKTGTLTEGNFSVNHYESFTDELNNEEILSLFASLESNSNHPLATGIVDFAKGKNISYATPQEVNNIPGVGLEGTVDNKKLKIVNVSYLDKSNFDYNKEQFTNLAQQGNSISYLIHDRQVIGIIAQGDKIKESSKQMVSDLLSRNITPVMLTGDNKEVAQTVAEELGISDVHAQLMPEDKESIIQDYQSNGSKIMMVGDGINDAPSLIRADIGMAIGAGTDVAIESGDVILVKSNPSDIINFLSLSKNTMKKMVQNLWWGAGYNVIAVPLAAGILASIGLILSPAVGAILMSLSTIIVAINAFTLKLK", "text": "FUNCTION: Involved in copper transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily."}
{"protein": "MSVVSNHHSNGNGNSTVYDTNGNDEIKKEVKDEPMASDSEVPFGELMKRDKKEKKQKKRKAESGSDEDDYKPEKRKSSAKNGKKKDVGSDSEDDYKPEKKKSKKNNKKKAQESSEDDDEESEGDVSEEDVKPQIHSDDELEEEDEAPTTDDEEEQKRKEKERRKKEKREKKERKEKKRLEKENRKIKEEDDEDSDDEDDEKAKKKKRKSKGAEKSKPSTSKKDAGGKKEPPKKKVKKEEDIEDIWEWWKEEKKPAGVKWNSLQHCGPLFAPPYIPLPSHVHFKYGGEKMKLTLETEEIAQFYAGVLDHEYSTKEAFNKNFMKDWRKVMTVEERERIHDLKKCDFRAIDAYQKEQREIRKAMTKEEKLKIKEEKEAEVKIYGIAIIDGHRQKVANFRIEPPGVFRGRGGHPKMGLIKKRIMPEDVIINCGKDTEIPKPPPGHKWKEVRHDNTVTWLCSWTESVLGQNKYIMLNPSSKIKGEKDFEKYETARRLKKKIGGIRERYTDDFKSKEMRVRQRATALYFIDKLALRAGNEKDVDEAADTVGCCSLRVEHIKLFDSAKLNEDDKKEKEFVVEFDFLGKDSIRYFNRVSVEKRVYKNLKIFMEGKAPSDDLFDRLDTATLNDHLRSLMDGLTVKVFRTYNASITLQEQLIKLTNPKDNVAAKILSYNRANRQVAILCNHQRAVSKGFDESMQKLEQKIKDKKKEVKEAEAALKSARGAEKEKAQKKYDRLKEQLKKLKISRTDKDENKQIALGTSKLNYIDPRITVAWCKKFEVPLEKVFTKTHREKFRWAIDMTNSSDEEYVF", "text": "FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)- enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Required for normal spermatogenesis and oogenesis (PubMed:16943775). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Chromosome Note=Localizes around sperm chromatids. SIMILARITY: Belongs to the type IB topoisomerase family."}
{"protein": "MSSSSSPPAASAAARLDLDGNPIAPLTICMIGAGGFIGSHLCEKLMAETAHVVYAVDVYCDKIRHLVDPAPPHLHGRISFHRLNIKNDSRLEGLIKMADLTINLAAICTPADYNTRPLDTIYSNFIDALPVVKYCSENNKRLIHFSTCEVYGKTIGSFLPTDHPLRKEPEFYVLKEDESPCIFGPIVKQRWSYACAKQLIERLIFAEGAENGLEFTIVRPFNWIGPRMDFIPGVDGPSEGVPRVLACFSNNLLRREPLKLVDGGQSQRTFVYIKDAIEAVHLMIENPARANGQIFNVGNPNNEVTVRQLAEMMTEVYANVSGEPPLDEPMIDVSSKQFYGEGYDDSDKRIPDMTIINKQLGWNPKTPLKDLLETTLTYQHKTYKEAIKRQMSQASASS", "text": "FUNCTION: Catalyzes the conversion of UDP-D-glucuronate to a mixture of UDP-D-apiose and UDP-D-xylose. D-Apiose (3-C-hydroxymethyl-d-erythrose) is the only plant cell wall monosaccharide with a branched carbon skeleton and found in rhamnogalacturonan II (RG-II), apiogalacturonan, and several apioglycosides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MWVALGMLWLLALGGPHQAWSFCPSQCSCSLHILSDGSKARTVVCSDPDLTLPPASIPPDTCKLRLERTAIRRVPGETFRPLSRLEQLWLPYNALSELSTLMLRGLRRLRELRLPGNHLVTFPWAALKDTPQLQLLDLQANRLSTLPPEAVHFLENLTFLDLSNNQLMRLPEELLDTWAHLKTGPYLSSRRTRLVLGLQDNPWVCDCRLYDLVHLLDGWASNLIFIEARLRCGSPRSLAGVAFSQLELRKCQSPELRPGVTSIISPLGSTVLLRCGATGIPGPEMSWRRANGRPLNGTVHQEVSSDGSSWTLLDLPVVSLFDSGDYICQAKNFLGASETLISLIVTEPQTSTEYTGIPGALWARTGEGAEAAAYNNKLVARHVPHVPEPVALATKPSVPSIKEELPLQNFQMDVPGEFSREPSEHQETQMVRSLKVVGDTYHSVSLVWKAPQAGNTTAFSVLYAVFGQRDMRRMTVEAGKTSVTIEGLAPKTKYVACVCVRGLVPTKEQCVIFSTDEVVDAEGTQRLINMVVISVAAIIALPPTLLVCCGALRRRCHKCRAGGSAEASGAYVNLERLGHSEDGSEELSRSSLSEADRLLSARSSLDSQVLGVRGGRRINEYFC", "text": "FUNCTION: Possible role in phototransduction. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein."}
{"protein": "MFHFARCSRLTRGTVTSDRLLSSHKTRDFLFQHLNRRGNHSAPWSSSQIPSTQLTVGVPVLRVWRQAQKLLRLTSRQQPRPPSIALKFILGPAALTVTARLLGPSAHCEADVNNNKVPLEVQVKEKIPEFSWAVLWEFVRPQLFALMGAILLAFGAAALNIQIPLMLGDLVNVVARHMREQAGHYMRDIQAPAVKLLGLYALQGLLTSGYIILLSRVGERVAADMRTTLFTSLLRQDIAFFDANKTGQLVNRLTSDIQEFKSSFKLVISQGLRSATQTVGCFVSLYFISPKLTGLTVVVLPCLVGAGALIGSFLRKLSRKAQEQVAKATGVADEALGNVRTVRAFAMEDRELEMYAAEVQKSAAMNETLGTGIAVFQGLSNIVLNCIVLGTIFAGGSLMARDDLSPGDLMSFLVASQTVQRSLASISILFGQMVRGMSAGARVFEYLALDPSVPLTGGGRIPLDSLMGRVDFMNISFSYPTRPGNQILKHFSLTLPPCKTVAIVGESGGGKSTVAALLERFYDPSSGVVMLDGLDIRTLDPSWLRGHVIGFISQEPVLFGTSVMENIRFGKPSATDAEVVSAAKQANAHNFITGFADGYNTVVGERGVTLSGGQKQRIAIARALVKNPSILILDEATSALDAESERVVQEALDRATTGRTVLIIAHRLSTIQAADLICVMSNGRIVEAGTHLELLSKGGLYAELIKRQRSNGHK", "text": "FUNCTION: ATP-binding subunit of the mitochondrial potassium channel located in the mitochondrial inner membrane. Together with CCDC51/MITOK, forms a protein complex localized in the mitochondria that mediates ATP-dependent potassium currents across the inner membrane (that is, mitoK(ATP) channel) (By similarity). Plays a role in mitochondrial iron transport. Required for maintenance of normal cardiac function, possibly by influencing mitochondrial iron export and regulating the maturation of cytosolic iron sulfur cluster-containing enzymes (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily."}
{"protein": "MRLIQALSLCLALSLSLAAPPQHKEDHSHKGKPGGEGHKHELHHGAQLDRCKGIEFDAVAVNEEGVPYFFKGDHLFKGFHGKAELSNKTFPELDDHHHLGHVDAAFRMHSEDSPDHHDHQFFFLDNMVFSYFKHKLEKDYPKLISAVFPGIPDHLDAAVECPKPDCPNDTVIFFKGDEIYHFNMHTKKVDEKEFKSMPNCTGAFRYMGHYYCFHGHQFSKFDPMTGEVHGKYPKEARDYFMRCPHFGSKTTDDHIEREQCSRVHLDAITSDDAGNIYAFRGHHFLSITGDKFHSDTIESEFKELHSEVDSVFSYDGHFYMIKDNDVFVYKVGKPHTHLEGYPKPLKDVLGIEGPVDAAFVCEDHHVVHIIKGQSIYDVDLKATPRKLVKEGTITQFKRIDAAMCGPKGVTVVIGNHFYNYDSVQVMLMAKIMPEQQKVSQQLFGCDH", "text": "FUNCTION: Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the hemopexin family."}
{"protein": "MKNSYQQLTTNLEYLKLKQMAQHLGDVVDFSINNELSFVETLVKLTNYEIDVREQNMIHSMVKMGAFPHRKEVDEFDFEFQPSINKQQILDFISLRFLEQQENIVFLGPSGVGKTHLATSIGIAAAKKRTSTYFIKCHDLLQNLKRAKIENRLESRLKHYTKYKLLIIDEIGYLPIDPEDAKLFFQLIDMRYEKRSTILTTNINFKSWDEVFQDPKLANAILDRVLHHATVVSIVGQSYRIKDHFSKEND", "text": "SIMILARITY: Belongs to the IS21/IS1162 putative ATP-binding protein family."}
{"protein": "MTLESPSTRLMTCQSSLLPEKPRFLSQKMWAPHLVVAYLIFVTLALALPGTQTRFSQEPADQTVVAGQRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLTVLIPPEETRIDGGPVILLQAGTPYNLTCRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIEPTDLDIGRVFTCRSMNEAIPNGKETSIELDVHHPPTVTLSIEPQTVLEGERVIFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVYNKVGSTNVSTLVNVHFAPRIVVYPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPLYVNGPPIISSEAVQFAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLEEREVLPVGIIAGATIGAGILVVFSFAALVFFLYRRRKGSRKDVTLRKLDIKVETVNREPLTMHSDREDDTASISTATRVMKAIYSSFKDDVDLKQDLRCDTIDTREEYEMKDPTNGYYNVRAHEDRPSSRAVLYADYRAPGPTRFDGRPSSRLSHSSGYAQLNTYSRAPASDYGTEPTPSGPSAPGGTDTTSQLSYENYEKFNSHPFPGAAGYPTYRLGYPQAPPSGLERTPYEAYDPIGKYATATRFSYTSQHSDYGQRFQQRMQTHV", "text": "FUNCTION: Required for proper function of the glomerular filtration barrier. It is involved in the maintenance of a stable podocyte architecture with interdigitating foot processes connected by specialized cell-cell junctions, known as the slit diaphragm (PubMed:11416156). Is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Predominantly located at podocyte slit diaphragm. SIMILARITY: Belongs to the immunoglobulin superfamily."}
{"protein": "MWTGGRRPGRLRRAASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQQRVSLHMEKHGCSLPSPLCHPSYADSVPTCVIAKVLEKPDPGSLSSRMSDASARDLAYRDGVENPGPRPPYKGDIYCSDTALYCPDERDHDRRPSVDTPVTDVGFLRAQNSTDSLAEEEEAEAAAFPEAYRREAFQGYAASLPTSSSYSSFSATSEEKEHAQASTLTASQQAIYLNSREELFSRKPPSATYGSSPRYAKAAATLGSPLEAQVAPGFARTVSPYPAEPYRYPASQQALMPPNLWSLRAKPSGNRLAAREDIRGQWRPLSVEDVGAYSYQAGAAGRAASPCNFSERFYGGGGGGGSPGKNAEGRASPLYASYKADSFSEGDDLSQGHLAEPCFLRAGGDLSLSPSRSADPLPGYATSDGDGDRLGVQLCGPGSSPEPEHGSRDSLEPSSMEASPEMHPPTRLSPQQAFPRTGGSGLSRKDSLTKAQLYGTLLN", "text": "FUNCTION: May sustain the structure of the postsynaptic density (PSD). SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein."}
{"protein": "MKFYTYSGETAAEALKIAQSHHGVDTLVFKTQEIRKKTLTSSGLYEIVVAVEEEENKKAPLIPESLYDEELNEEDVVMQLSSTVEEMRKLAGVSSNQRNYTFSKNKTLLEKDAPLEDTPLEANKQDALLQALKDEANHKKEREKREVKQEEEIKDINAQLSKIRDSLKLIQNMFWDEKNPNSVNIPQEFAEIYKLAKQSGMKSSHLDEIMQLSLELMPLRMRENSVTIKRYFREVLRKIILCRPEDLNLRQKRILMLVGPTGVGKTTTLAKLAARYSRMLAKKYKVGIITLDNYRIGALEQLSWYANKMKMSIEAVIDAKDFAKEIEALEYCDFILVDTTGHSQYDKEKIAGLKEFIDGGYNIDVSLVLSVTTKYEDMKDIYDSFGVLGIDTLIFTKLDESRGLGNLFSLVHESQKPISYLSVGQEVPMDLKVATNEYLVDCMLDGFSNPNKEQA", "text": "FUNCTION: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GTP-binding SRP family."}
{"protein": "MENNKKLTLCEIPNAFIQFFNNKDYENKSKLFNNTETDQWWVSGDKNVYPFAGSDSIQKRLDGFQTLQNGYDKYSMTLIDQIIDHERRIMLVVGKTVSMGFGMTKEYSNEYAFIISVNEDGKICAIKEYFDPSAYLKMAQSTPSLQGIFKNFFPDSFAPTSRD", "text": "SIMILARITY: Belongs to the UPF0523 family."}
{"protein": "MRNLDFIDSFIPTEGKYIRVMDFYNSEYPFCIHAPSAPNGDIMTEICSRENNQYFIFFPTDDGRVIIANRHNGSVFTGEATSVVSDIYTGSPLQFFREFKRTMSTYYLAIQNPESATDVRALEPNSHELPSRLYFTNNIENNSNILISNKEQIYLTLPSLPENEQYPKTPVLSGIDDIGPNQSEKSIIGSTLIPCIMVSDFISLGERMKTTPYYYVKHTQYWQSMWSALFPPGSKETKTEKSGITDTSQISMTDGINVSIGADFGLKFGNKTFGIKGGFTYDTKTQITNTSQLLIETTYTREYTNTENFPVRYTGYVLASEFTLHRSDGTQVNTIPWVALNDNYTTIARYPHFASEPLLGNTKIITDDQN", "text": "FUNCTION: Component of a binary toxin active against Culex and some Aedes mosquito larvae (PubMed:1512580, PubMed:8419297). The individual subunits are not toxic. BinAB binds to the gastric caecum and posterior midgut of C.quinquefasciatus larvae; this subunit alone binds the entire larval gut. Binary toxin internalization into host gut cells requires both proteins (PubMed:1512580). Toxic to Aedes atropalpus mosquito larvae; mortality towards both C.quinquefasciatus and A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible to this toxin (PubMed:8419297). SUBCELLULAR LOCATION: Spore, perispore. SIMILARITY: Belongs to the toxin_10 family."}
{"protein": "MDVRERNVFGNASVATPGEHQKFVRELILSGHNNVVLQTYTGKWSDCRKHGKSVMYNTGEARHPTCKAHQR", "text": "SIMILARITY: Belongs to the varicellovirus ORF57 protein family."}
{"protein": "MSRSRHLGKIRKRLEDVKSQWVRPARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSSLQSGTYFPVASEGSEPALLHSWASAEKPYLKEKSSATVYFQTVKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAANKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWLCGHVHRNILSKFTGQAVELFDEEFRHLYASSKPVMGLKSPRLVAPVPPGAAPANGRLSSSSGSASDRTSSNPFSGRSAGSHPGTRSVSASSGPCSPAAPHPPPPPRFQPHQGPWGAPSPQAHLSPRPHDGPPAAVYSNLGAYRPTRLQLEQLGLVPRLTPTWRPFLQASPHF", "text": "FUNCTION: Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both RAS/MAPK and PI3K/AKT/TOR signaling cascades downstream of EGFR. Required for the RAS/MAPK signaling cascade activation upon EGFR stimulation, it also activates both signaling cascades independently of EGFR activation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAM83 family."}
{"protein": "MIVRPVTSADLPALIELARSTGTGLTTLPANEQRLQHRVSWAEKAFRGEAERGDADYLFVLEDDAGKVVGISAIAGAVGLREPWYNYRVGLTVSASQELNIHREIPTLFLANDLTGNSELCSLFLHADHRSGLNGKLLSRARFLFIAEFRHLFGDKLIAEMRGMSDEEGRSPFWESLGRHFFKMEFSQADYLTGVGNKAFIAELMPKFPLYTCFLSEEARGVIGRVHPNTEPALAMLKAEGFSYQGYVDIFDAGPAIEAETDKIRAIAESQNLVLAVGTPGDDAEPYLIHNRKREDCRITAAPARAAAGTLVVDPLTAKRLRLSAGASVRAVPLSAQKRG", "text": "SIMILARITY: Belongs to the succinylarginine dihydrolase family."}
{"protein": "MITKEEAQKIAKLARLKFEKDIVEKFSTQLSTIMNMINILNEIDCKDIEPLTSVSNMNARMREDTVTSSDLSNKLFDNVSGNSAKLAKEVKYFITPKVVE", "text": "FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity). SIMILARITY: Belongs to the GatC family."}
{"protein": "MKVELCSFSGYKIYPGHGPVYARIDGKVFQFLNAKCESAFLTKRNPRQINWTVLYRRKHKKGQSEEVTKKRTRRAVKFQRAITGASLAEILAKRNQKPEVRKAQREQAIRAAKEAKKAKQATKKVSTQSTKAPAKAAPKQKIAKPMKVSAPRVGGKR", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family."}
{"protein": "MEKMNITNQQHDAFVKSHPNGDLLQLSKWADTKKLTGWYSRRIAVGENGQIKGVGQLLFKKIPKLPYTLCYVSRGFVADYNNKEVLEALLSYAKEVAKDEKSYAIKIDPDVEVDKGAEALKNLRELGFKHKGFKEGLSKDYIQPRMTMITPIDKTDDELVQSFERRNRSKVRLALKRGTKVERSNREGLKIFANLMKITGERDGFLTRDISYFENIYDALHEDGDAELFLVKLEPKPVLDTVNQDLEAQLAEKEKLQSKKQDKKTLNKLNDIDNKIKKTNELKSDLTELEKSEPEGIYLSGALLMFAGNKSYYLYGASSNDYRDFLPNHHMQFEMMKYAREHGATTYDFGGTDNDPDKDSEHYGLWAFKRVWGTYLSEKIGEFDYVLNQPLYHLVEKVKPRLTKAKIKISRKLKGK", "text": "FUNCTION: Catalyzes the incorporation of amino acid(s) into the interchain peptide bridge of peptidoglycan, using aminoacyl-tRNA as amino acid donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FemABX family."}
{"protein": "MLSRVVLSAAATAAPCLKNAAVLGPGVLQATRVFHTGQPRLAPLPPLPEYGGKVRLGLIPEEFFQFLYPKTGVTGPYVLGTGLSLYFLSKEIYVITPETFSTISVVGLIVYVIKKYGASIGEFIDKLNEEKIAQLEEIKQSSMKQIQDAINREKAQQALVQKRHYLFDVQRNNIALALEVTYRERLHKAYKEVKNRLDYHISVQDMMRRKEGEHMINWVEKHVIQSISAQQEKETIAKCIGDLKMLAKKAQAQPIM", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase B chain family."}
{"protein": "MAAFAVDPQAPTLGSEPMMLGSPTSPKPGANAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVPAHKDKSGAPPVRSIYDDISSPGLGSTPLPSRRQANISVLQSPLVGVTTPVTGQSMFSPANIGQPRKTTLSPAQLDPFYTQGDSLTSEDHLDDTWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVKPCIDKNVMENSDRGVLSSPSLAFTPPIRTLGTPTQPGSTPRVSTMRPLATAYKASTSDYQVISDRQTPKKDESLVSRAMEYMFGW", "text": "FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity). SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein Note=Tightly associated with the nuclear membrane and lamina. SIMILARITY: Belongs to the Nup35 family."}
{"protein": "MPITKATPLFLRYRLKGFVFLTLLLVQGVFTACAPAVPVNNKSVSAVQPEDKQALKPDPALGEYTSDLKFNTNFIPKKDDPFRPFYDLSFTLQFQDPYTATYGTGWLIDWKDNNQPNKFTAYIATNLHVADNLRNVNDYEFFNQFDYFDDPTESFTLGKFVDGNEIKQIVPDAMHEPSLVRIETSKLPKTAYTTTLFINDLGEYRLPAADFAVLESI", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the MG067/MG068/MG395 family."}
{"protein": "MWSNCIFLTLFTFYLFLGQSCCQTDTLLQGQYLKDGQELVSAFNIFKLKFFNFENSSNWYLGIWYNNFYLSGAVWIANRNNPVLGRSGSLTVDSLGRLRILRGASSLLELSSTETTGNTTLKLLDSGNLQLQEMDSDGSMKRTLWQSFDYPTDTLLPGMKLGFNVKTGKRWELTSWLGDTLPASGSFVFGMDDNITNRLTILWLGNVYWASGLWFKGGFSLEKLNTNGFIFSFVSTESEHYFMYSGDENYGGPLFPRIRIDQQGSLQKINLDGVKKHVHCSPSVFGEELEYGCYQQNFRNCVPARYKEVTGSWDCSPFGFGYTYTRKTYDLSYCSRFGYTFRETVSPSAENGFVFNEIGRRLSSYDCYVKCLQNCSCVAYASTNGDGTGCEIWNTDPTNENSASHHPRTIYIRIKGSKLAATWLVVVASLFLIIPVTWLIIYLVLRKFKIKGTNFVSESLKMISSQSCSLTNKRLSTLRVGSTIDQEMLLLELGIERRRRGKRSARNNNNELQIFSFESVAFATDYFSDANKLGEGGFGPVYKGRLIDGEEVAIKRLSLASGQGLVEFKNEAMLIAKLQHTNLVKLLGCCVEKDEKMLIYEYMPNKSLDYFLFDPLRKIVLDWKLRFRIMEGIIQGLLYLHKYSRLKVIHRDIKAGNILLDEDMNPKISDFGMARIFGAQESKANTKRVAGTFGYMSPEYFREGLFSAKSDVFSFGVLMLEIICGRKNNSFHHDSEGPLNLIVHVWNLFKENRVREVIDPSLGDSAVENPQVLRCVQVALLCVQQNADDRPSMLDVVSMIYGDGNNALSLPKEPAFYDGPPRSSPEMEVEPPEMENVSANRVTITVMEAR", "text": "FUNCTION: Promotes the expression of genes involved in photosynthesis at least in dedifferentiated calli. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MSIMDDLMEGRIKLYEIERHVPVDEAVRIRREFIERTCGVKLEHVSNYSIDMERASRRNIENPIGVVQIPLGVAGPLRVRGEHADGEYYVPLATSEGALVASVNRGCSVITRAGGATVRVTGDSMTRAPVIRTGSVVEALQLREWIYENMDALREEAESTTRHGKLVKIDPIIVAGSYVYPRFVYTTGDSMGMNMVTIATERALELLTRETGAHVIALSGNLCTDKKPAAVNLIEGRGKSITAEITVPGEMVESVLKTTPEAVVEVNTAKNLIGSAAAGSMGFNAHYANIIGAIFLATGQDEAHIVEGSLGVTIAEERKGDLYFAVNLPDVPLATVGGGTGLETASECLDIMGVRGGGRVHAFAEIVGGAVLAGELSLMGALAAGHLARAHSELGRG", "text": "FUNCTION: Converts HMG-CoA to mevalonate. SIMILARITY: Belongs to the HMG-CoA reductase family."}
{"protein": "MKYFKRLSDRERAIFEAGITLGAIYHQFCGTPVSPGTAEEVAKCIERAALLQPCVIDARVEVDVSSEDTDNYGGYTEVSGRNLRVTIVTRCGEWEAVGKLEFIEELNYPLMWVEEIRRVEQ", "text": "FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD). SIMILARITY: Belongs to the archaeal dihydroneopterin aldolase family."}
{"protein": "MEEDLFQLRQLPVVKFRRTGESARSEDDTASGEHEVQIEGVRAGLEAVELDDGAAVPKEFANPTDDTFMVEDAVEAIGFGKFQWKLSVLTGLAWMADAMEMMILSILAPQLHCEWRLPSWQVALLTSVVFVGMMSSSTLWGNISDQYGRKTGLKISVLWTLYYGILSAFAPVYSWILVLRGLVGFGIGGVPQSVTLYAEFLPMKARAKCILLIEVFWAIGTVFEVVLAVFVMPSLGWRWLLILSAVPLLLFAVLCFWLPESARYDVLSGNQEKAIATLKRIATENGAPMPLGKLIISRQEDRGKMRDLFTPHFRWTTLLLWFIWFSNAFSYYGLVLLTTELFQAGDVCSISSRKKAVEAKCSLACEYLSEEDYMDLLWTTLSEFPGVLVTLWIIDRLGRKKTMALCFVVFSFCSLLLFICVGRNMLTLLLFIARAFISGGFQAAYVYTPEVYPTATRALGLGTCSGMARVGALITPFIAQVMLESSVYLTLAVYSGCCLLAALASCFLPIETKGRGLQESSHREWGQEMVGRGAHGTGVARSNSGSQE", "text": "SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MALNGPGVYHRTREHEQEDASDITKNILAESWKSWPNEAAFDRLEEHRGPLRLTLKGTIPSWAAGSLYRTGPGQSRVEDTARGTHFTTHWFDGFAQTHRFDIIPSEDGETQVWYSSRRQADEWIADVKKKGWRSGMTFGQKADPCVGIFAKVMTVFEPKLGNHNVALLANVPGVPKDEETEVSNGVPGPLGHRVNTSNLFVSTDYTGIRRIDPSTLQPLAETTQYDLHPSLSGPCSCSHAQRDPDSGDLFNFNLAFGRVPTYRIFRVDTASGETEVLATISDLNVPPAYMHSFFLTENHVVICIPASHYAWRGLKTQWEGNIIDSMKPFDKERKCKWLVVDRRHGKGLVATFSTPAAFFFHSINAFEKNIEDEDGTEQTDLFFDLAKYNNMDIIKGFYYDVLMDRDDATKKYWFKNDRYKNCAPTLTRYRFRLPSAPTPDTTFSASAEQVLAIPSPHAGELPTIHPLRNGKPYRYVYSASLRGLTTSVDALVKTDLDTSEAFIWTGPEGHTPGEPVFVPRPGAEAEDDGIVFSLVVDGVNEKAYILCLNGKTMEELGRAEADFAIGQGFHGIHLPAA", "text": "FUNCTION: Torulene dioxygenase; part of pathway that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation (PubMed:17493127). CarT mediates the cleavage of torulene into beta- apo-4'-carotenal, the aldehyde corresponding to the acidic neurosporaxanthin (PubMed:17493127). Is also active on other monocyclic synthetic substrates such as beta-apo-8'-carotenal and beta-apo-10'- carotenal to produce beta-apo-14'-carotenal and retinal(beta-apo-15'- carotenal), respectively (PubMed:17493127). Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma- carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the carotenoid oxygenase family."}
{"protein": "MRRNILTALACSWLTAHAASVDLKSLLLESDIQWASDTVISFSDTPEFEDATVRWNSYNAPTYAGAISPADEEDVVKVVKLAKEHNVPFLATGGRHGCTDMVGLQEGLAIDLSQINSYEVDSDDATVTVGAGSTFGQFQNAIHDAGFMIQSGSVTCPGFIGITLGGGIGRYTGIFGLEIDALISARIVTADGEVLTISETENAELFWGVRGAGFNFGIVTSATYKLHKLADNNNGEILTADFIIPANKTLFYFDWLESLGETMPPNAAGVSRFQFDSIAKEGQIGANWVFIGPEDEGREFLSPILDLQPSVAMLSYVPWNKLIETAGGGQGAMLCEARAPRSLFTGQMRKYTALTLQETFDKITTLWETHPGLAYTSLNFEAFPNHAAVAVPDDATAYPWRDAIGWFQFEIISLEGVGSDSFNAGEHAGQVLRDSWVRTSGYDNHTIYVNYARGDETLEQKYGASKLPRLAALKKKYDPDNVFGWNNALPTEYPGSG", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds (PubMed:32134669). FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners (PubMed:32134669). The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols (PubMed:32134669). In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products (PubMed:32134669). The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring (PubMed:32134669). The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners (PubMed:32134669). The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives (PubMed:32134669). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MNSRLQEIRERQKLRRQLLAQQLGAESPDSIGAVLNSKDEQKEIEETRETCRASFDISVPGAKRKCLNEGEDPEEDVEEQKEDVEPQHQEESGPYEEVYKDSSTFLKGTQSLNPHNDYCQHFVDTGHRPQNFIRDGGLADRFEEYPKQRELIRLKDELISATNTPPMYLQADPDTFDLRELKCKFDVILIEPPLEEYYRESGIIANERFWNWDDIMKLNIEEISSIRSFVFLWCGSGEGLDLGRMCLRKWGFRRCEDICWIKTNKNNPGKTKTLDPKAVFQRTKEHCLMGIKGTVRRSTDGDFIHANVDIDLIITEEPEMGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPGWLTVGPTLTNSNFNIEVYSTHFSEPNSYLSGCTEEIERLRPKSPPPKSMAERGGGAPRGGRGGPAAGRGDRGRERNRPNFRGDRGGFRGRGGPHRGFPPR", "text": "FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis. In the heterodimer formed with mettl3, mettl14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MT-A70-like family."}
{"protein": "MAAPSGVPPLRVLEELGIGLSPTGEVTEAVTSEGAYYLEQVTITETSEDECEYEEIPDDNFSIPEGEEDLEKAIHIIGEQARDIHILEQQTILPARNVMQEAIEDFLCNFLIKMGMTRTLDCFQAEWYELIQKKGSDFKGLGNVPDVYSQVMLLETENKNLKKELKHFKQAAEKAKEDLLRTQKERDFHRMHHKRIVQEKNKLIADLKGLKLHYASYEPTIRVLHEKHHALLKEKMLTSLERDRAVGKISGLQATLKNIDMGHIQVPVIKGSYESASITRESGDRAGHSCEKENSSEGPTQKSLREAREEVGYKSKLKNEKKDSEFPVDMQPDPNVTSCTENVSAAKFDYKLNNIFRLHELPVSCIVMHPCRDYLISCSEDRLWKMVGLPQGNVLLTGSGHTDWLSGCCFHPSGSKLATSSGDSTIKLWDLNKGECTLTLEGHNHAVWSCTWHSCGDFVASASLDMTSKIWDVNSERCRYTLYGHTDSVNSIEFFPFSNILLTASADKTLSVWDARTGKCEQSLYGHMHSVNDATFTPRGHIIASCDARGVTKLWDFRKLIPIVSIDVGPSSGNEVNFDQSGRVLAQASANGIIHLLDLKSGQIHKLVGHESEVHSVVFSHLGENLYSGGSDGTIRLWI", "text": "FUNCTION: Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, flagellum axoneme Cell projection, cilium, flagellum Note=Detected on the sperm flagellum. Detected in the central apparatus of the axoneme. Colocalizes with SPAG6 on microtubules."}
{"protein": "MKVTLIAILTCAAVLVLHTTAAEELEAESQLMEVGMPDTELAAVDEERLVECSVSCEIEKEGNKDCKKKKCKGGWKCKFNMCVKV", "text": "FUNCTION: Postsynaptic neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 02 (Hwtx-2) subfamily."}
{"protein": "MEQKNKKNTIPWIWGFNVYAENWNGRLAMISFLLIICVEFITNKNVLDLVKLN", "text": "FUNCTION: Possible role in chlorophyll and/or carotenoid binding. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ELIP/psbS family."}
{"protein": "MFRRSPGGKANMSGRAQPARAVLFAAMASCLLSPAAALAEPPTAVIPKQTIYPGEKLDASMLEVVDVTNPDLRDGYVRSIDEVDGMVTKRTLLPGRVILASALREQYAVERGSTVRLVFNNGGLTITAAGSPLQDAAVGDLIRVRNVDTGVIVSGTVMADSTIHVVAK", "text": "SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the FlgA family."}
{"protein": "MQLEVNNMWISFSVRYLVNVEDLNNVESAGNYVRHRRAPLVFKDKDSYTVTYVPAVSGEMIAHGYQMNLVELALQRNLPVDSLAKQGILIKRGSDDKVHEGTKCTDEKGSDYELCVINEDIVEDVAGFMNPNKLVKRTSNVAFSYMVPAIDAVKASTISSQFHVRYANKELMDKYKNENIQSLYNIETASASYVLTGYLNVNSVGKTQNYPVKEVDKKKDREKAALDALMLTLTQFLFGAKLTRFKPIVEIEALFVSASEKPFNLPPVTGDIKKYIDLVNSTTDSFAKILNIKRPVVKYYLKEEKGNVNTPIDAFTVM", "text": "FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). SIMILARITY: Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily."}
{"protein": "MQLKTSIGLITCRMNTQNNQIETILVQKRYSLAFSEFIHCHYSINANQGHLIKMFNNMTINERLLVKTLDFDRMWYHIWIETPVYELYHKKYQKFRKNWLLPDNGKKLISLINQAKGSGTLLWEIPKGKPKEDESDLTCAIREFEEETGITREYYQILPEFKKSMSYFDGKTEYKHIYFLAMLCKSLEEPNMNLSLQYENRIAEISKISWQNMEAVRFISKRQSLNLEPIIGPAFNFIKNYLRYKH", "text": "FUNCTION: Decapping enzyme required for the removal of the 5'-end m7GpppN cap tethered to viral and host mRNAs to allow their decay in cells. May therefore accelerate viral and cellular mRNA turnover to eliminate competing host mRNAs and allow stage-specific synthesis of viral proteins. Acceleration of the turnover of cellular transcripts may even promote the shutoff of host protein synthesis. In addition to the mRNA cap, g5R also efficiently hydrolyzes diphosphoinositol polyphosphates. Down-regulation of the level of PP-InsP5 (diphosphoinositol pentakisphosphate) may play a role in viral manipulation of the cellular secretory pathway, a step necessary for the formation of virions. Binds viral and cellular poly(A) mRNAs, thereby decreasing both types of mRNAs. SUBCELLULAR LOCATION: Host rough endoplasmic reticulum Note=Accumulates at the periphery of the viral factories. SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily."}
{"protein": "MQKKSDDPYERLLLLHLQHYGFLSDNSSGIPIKREWEGIQDSTASDMINSSSPSESSDSNLEEEQEESKPCSNFFSLNKALRTRQLVFDFDGERPIPRLRDPLDLFTIPSTSCPFQGVRWPIECDVICDKIQHIEWDPSEPETFYQPTGNEQTPMPVGEVRGNTVYCIDPATKASSFTYSRVGGSRGPIKSATSCANNQKEPTLAFESRFECGNLQKAVQVGQYDYGLTLRTDLYTTKHTQWFYFRVRNMREGVTYRFTIINLMKSSSLYGAGMCPLLYSEKTAWLKGEGWKRTGSSIRYYRNNIEQDGKALYSLTWTLEFPYDGDTCYLAHCYPYTYSKLQHYLREVISDPVRAAYCKLRVLCRSLAGNAVYVLTITAPSSSLAERKAKRAVVVTARVHPGETNGSWMMQGFLEFLLSDLPDAHLLRETFIFKVIPMLNPDGVVVGNYRCSLAGRDLNRNYRSMLRDSFPCIWYTRNMVKRLLAEREVVVYCDFHGHSRKNNVFMYGCNERKDASQCLQERVFPLMMSKNAKDKFSFRSCKFKMHKSKEGTGRIVMWRLGIRNSYTMESTFGGSTLGDRKGTHFSTLDLKSMGYCFCDTLLDFCDPDPAKMTRCLEELGVLLKQEIRRKLGREVDSLENLSDIDIESSTSGSNSTESDGLPVHLLNVTNQGKKKLLRSRKERNRLRQGRVQSAGKTDASKPYSCQTLNATTQHGDTEDQS", "text": "FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body Note=Colocalizes with gamma- tubulin in the centrioles and with glutamylated tubulin in the basal bodies of ciliated cells. SIMILARITY: Belongs to the peptidase M14 family."}
{"protein": "MDAATPGNGIISDVVFVIEGTANLGPYFESLRKHYLLPAIEYFNGGPPAETDFGGDYGGTQYSLVVFNTVDCAPESYVQCHAPTSSAYEFVQWLDSIKFMGGGGESCSLIAEGLSTALQLFDDFKKMREQIGQTHKVCILICNSPPYLLPAVESTTYSGYTTENLVQKIGERGIHFSIISPRKLPALRTLFEKAMPVGLIEPQPKDYSQDPRHMILVRGMVLPVGGATSVPGVMPPKQHISQPPLPVVPPQIASAPSHQLPPVQPPYMQVPQQSTLTPAHAAAHSAVEAAKNQKNSPSNRFLLPNLNPMPNAPAVGTPFNQPPAPTLPPNASVPKMVPSPSSLMTPASQSSLITTVTTGPGPAPVQLQQQGAPQQPVPPSMPITGAVGGVQAPQPSQPQIGTVQLPCTQTPVNGNKLLAWSGVLEWQEKPRSVSVDNNAKLTRSLPCQVYINPGENLKTDQWPQKLIMQLIPQQLLTTLGPLFRNSRMVQFHFTNKDLESLKGLYRIMGSGFAGCVHFPHTTPCEVRVLMLLYSSKKKIFMGLIPNDQSGFVNGIRQVITNHKQVQMQKIDQQRNMGAVQGVGAGSVPANSQGFLQKQPGTLPVGQAVSQQMQGQQVAPGMPSISQVAMMDEQQRSQNLLHIRVQQPQQLASQAPPQATQSSVQAPGQPQNPQPGAMLRPQNPGANPQLRNLLLSQQPPQSSVPQTQQPLHHMQQAAQSMLPHQAMGQQMQHQAPGQLQLPGQSLMHQTPAQQWGNQMQQRAPIPGTLMMSAGPRGPVPQSGLQQVQAQSVMEDDILMDLI", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 25 family."}
{"protein": "MASSTPSPATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEKSRLVSAFRERQSSKNLLSCENSDQGARFRRTETDFSNLFAQDLLPAKNGEEQTAQFLLEVVDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWSNKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADLEAKILDAKQKGYVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELADYLYAKIKNREEFEMVFDGEPEHTNVCFWYIPQSLRGVPDSPERREKLHRVAPKIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL", "text": "FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor. SIMILARITY: Belongs to the group II decarboxylase family."}
{"protein": "MLFHLRTLLNNAALRNGHNFVVRNFRCGQPLQDKVQLKGRDLLTLKNFTGEEIKYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPCFLTTDDIHLGVNESLTDTARVLSSMTDAVLARVYKQSDLDLLAKEASIPIVNGLSDLYHPIQILADYLTLQEHYGSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQVATPKGYEPDPSITKMAEQYAKENGTKLSLTNDPLEAACGGNVLITDTWISMGQEEEKKKRLQAFQGYQVTMKTAKVAAPDWTFLHCLPRKPEEVDDEVFYSPRSLVSPEAENRKWTIMAVMVSLLTDYSPQLQKPKF", "text": "FUNCTION: Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
{"protein": "MNLSQFEQFDLSPELLKALEKKGYSRPTAIQMEAIPAAMEESDVLGSAPTGTGKTAAFLLPALQHLLDYPRRKPGPPRILVLTPTRELAMQVAEQAEELAQFTHLNIATITGGVAYQNHGDVFNTNQDLVVATPGRLLQYIKEENFDCRSVEMLIFDEADRMLQMGFGQDAEKIAAETRWRKQTLLFSATLEGELLVDFAERLLNDPVKVDAEPSRRERKKINQWYYHADSNEHKIKLLARFIETEEVTRGIVFIRRREDARELSETLRKRGIRSAYLEGEMAQTQRNNAIDKLKSGIVTVLVATDVAARGIDIDDVSHVMNFDLPYSADTYLHRIGRTARAGKKGTAVSFVEAHDYKLLGKIKRYTEEILKARILAGLEPRTKPPKDGEVKSVSKKQKARIKEKREEKKKTEAKKKVKLRHKDTKNIGKRRKPSNSNV", "text": "FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. SrmB subfamily."}
{"protein": "MKFLCILLLASLAATSLAILNEPEDETHLEAQPTDASAQFIISNLQISTEDLSKEPSISREDLISKEPNVIRSPRQPQNQNPKLPLSILKEKQLRNATLGSEETTEHAPSDASTTEGKLMELGHKIMKNLENTVKEIIKYLKSLFPPASEVVKP", "text": "SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the PP3/GlyCAM-1 family."}
{"protein": "MADSERLTAPGCWAACTSFSRTRKGFLLFAEIILCLVILICFSTSTSGYSFLSVIEMIFAAIFFVVYMCDLHTKIQIINWPWSDFFRTLVAAILYLITSIVVLVERGNGSKIAAGALGLCAAGLFGYDAYITFPLRQQRHTAAPTDPADGPV", "text": "FUNCTION: May play a role in cell differentiation in the intestinal epithelium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MEALVLVGHGSRLPHSKNVVMEVAEKIKARNIYDIVEVGMMEFNEPTIPQTIKKVIDAGAKKVIVTPVFLAPGNHTERDIPKILGIYEGDDEGGHHHHHDHEHHHHHHDTTAVEIPEGVELVYRKPMGADDRIIDIVLDRANGL", "text": "FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin. SIMILARITY: Belongs to the CbiX family. CbiXS subfamily."}
{"protein": "MKPIFLVLLVATSAYAAPSVTINQYSDNEIPRDIDDGKASSVISRAWDYVDDTDKSIAILNVQEILKDMASQGDYASQASAVAQTAGIIAHLSAGIPGDACAAANVINSYTDGVRSGNFAGFRQSLGPFFGHVGQNLNLINQLVINPGQLRYSVGPALGCAGGGRIYDFEAAWDAILASSDSSFLNEEYCIVKRLYNSRNSQSNNIAAYITAHLLPPVAQVFHQSAGSITDLLRGVGNGNDATGLVANAQRYIAQAASQVHV", "text": "FUNCTION: It is likely that the major role of L-chain is to prevent the retention of H-chain in ER by forming the disulfide linkage. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MQNEEGQMVDLYVPRKCSATNRIITAKDHASVQINIGHVDENGLYDGRFTTFALSGFIRAQGDADSALDRLWQKRKAEVKQQ", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family."}
{"protein": "MARKVVVVDDEKPIADILEFNLKKEGYDVYCAYDGNDAVDLIYEEEPDIVLLDIMLPGRDGMEVCREVRKKYEMPIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRELIARVKANLRRHYSQPAQEVSGATNEITIKDIVIYPDAYSIKKRGEDIELTHREFELFHYLSKHMGQVMTREHLLQTVWGYDYFGDVRTVDVTIRRLREKIEDDPSHPEYIVTRRGVGYFLQQHD", "text": "FUNCTION: Member of the two-component regulatory system WalK/WalR. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN", "text": "FUNCTION: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA. Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)- octadecadienoate or CLA), which provides all energy and carbon precursors required for the growth of E.coli. Thus, supports growth on oleate or conjugated linoleate as the sole source of carbon by hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate beta-oxidation via the alternative thioesterase-dependent pathway, and 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation, respectively. Seems to be involved in 3-hydroxyalkanoate production in E.coli. FUNCTION: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA (PubMed:1645722, PubMed:24271180, PubMed:20547355). Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)- octadecadienoate or CLA), which provides all energy and carbon precursors required for the growth of E.coli. Thus, supports growth on oleate or conjugated linoleate as the sole source of carbon by hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate beta-oxidation via the alternative thioesterase-dependent pathway, and 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation, respectively (PubMed:18702504, PubMed:14707139). Seems to be involved in 3-hydroxyalkanoate production in E.coli (PubMed:20547355). SIMILARITY: Belongs to the C/M/P thioester hydrolase family."}
{"protein": "MSTTQRKDDSHLFTSSCTRQLQVQEDRQQQEKYVIAQPIFVFEKGEHNFKRPAEDSLEETAEPEFTGFLRKRVRSSSVTLHTTDPQSQGVATLSQTRLRSSSFTDVPTFPPCRPVRKNNVFMTSRLLQRSDDMNNVEQGPPMRSSEQVLRPAVLQPSQTQSCQKAGTTFGPGALKSYKTKEKAEHEISEVGSSSSLLSENLPNARSSIQLSTDPCISEAPSGCQPKEDKCSFTSCSSDFVFGENMVERVLGTQKLTQPPLQNLSYAKEKTFKSVLKFPNAVSNSDSIENISLVESAAAFSSKPSQKCLLEKIDVITGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNDTAGRECGTLQSRLIMRNQGSLRLVLNSRLWAQMKIQRASQKNLRITATDLEDDGIKIFLIQASAKDTGFLYAAIHHRLVALRSLAKQGDGGPAESQSDTALPQLNGESCDEDEDEIAQVTKNGSDPSRWSHRQSIVCS", "text": "FUNCTION: Nuclear export factor for BMP-specific SMAD1/5/8 that plays a critical role in terminating BMP signaling and regulating mesenchymal stem cell differentiation by blocking osteoblast differentiation to promote myogenic differention. Directly recognizes dephosphorylated SMAD1/5/8 and mediates their nuclear export in a Ran-dependent manner. SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MRQMKRTAYIILLVCVLALWMDSVQAGSSFLSPSQRPQGKDKKPPRVGRRDSDGILDLFMRPPLQDEDIRHITFNTPFEIGITMTEELFQQYGEVMQKIMQDLLMDTPAKE", "text": "FUNCTION: Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the motilin family."}
{"protein": "MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERANPNSFWQPYIQTLPSEYDTPLYFEEDEVRYLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNQDLSVRAKMAIKLRLGEKEILEKAVKSAAVNREFYRQQMEEKAPLPKYEEGNLGLLESSVGDSRLPLVLRNLEEEAGVQDALNIREAISKAQATENGLVNGENSVPNGTRSENENLNQEESKRAVEDAKGSSSDNTAEVKE", "text": "FUNCTION: Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes mainly in the cytoplasm. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. SETD3 actin-histidine methyltransferase family."}
{"protein": "MEVKPPPGRPQPDSGRRRRRRGEEGHDPKEPEQLRKLFIGGLSFETTDDSLREHFEKWGTLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDAAMCARPHKVDGRVVEPKRAVSREDSVKPGAHLTVKKIFVGGIKEDTEEYNLRDYFEKYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHNCEVKKALSKQEMQSAGSQRGRGGGSGNFMGRGGNFGGGGGNFGRGGNFGGRGGYGGGGGGSRGSYGGGDGGYNGFGGDGGNYGGGPGYSSRGGYGGGGPGYGNQGGGYGGGGGYDGYNEGGNFGGGNYGGGGNYNDFGNYSGQQQSNYGPMKGGSFGGRSSGSPYGGGYGSGGGSGGYGSRRF", "text": "FUNCTION: Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus Note=Component of ribonucleosomes."}
{"protein": "MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVATPKPPVEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA", "text": "FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (PubMed:27474409). Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (PubMed:27474409). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids. SIMILARITY: Belongs to the dynein intermediate chain family."}
{"protein": "MSLLLLQLLVLSCLGDTEPQPDSQQRKRRPLQHLFYLDRNLLESQSFHELVGENPVGVKETQEEPSFFIAFPQTAGESQKQGEKKMSRFILPNAELYAHQDLRTWAAPKEISPVENFSPSYYSNKRDVEPPYRKDAKKFWDHFMLRKNSASEEVVLPIKTNEMHQETCRTLPFSQSVAHESCEKVIVQNNLCFGKCSSFHVPGPDDRLYTFCSKCLPTKFSMKHLDLNCTSSVPVVKKVMIVEECNCETQKIEDPLLGSRQSDFLGNLPEHN", "text": "FUNCTION: Cytokine that acts as a regulator of the activity of Nodal/BMP pathways during the establishment of bilateral asymmetry in the head and trunk of the embryo. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DAN family."}
{"protein": "MFKFVMILAVVGVATALAPVSRSDDVHADVLSRSDDVRADGFDSSLHTSNGIEQAASGDAHGNIHGNFGWISPEGEHVEVKYVANENGYQPSGAWIPTPPPIPEAIARAVAWLESHPPAPEHPRHH", "text": "FUNCTION: Component of the larval cuticle."}
{"protein": "MSLKEKTQSLFANAFGYPATHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAPRDDRKVRVMAADYENQLDEFSLDAPIVAHENYQWANYVRGVVKHLQLRNNSFGGVDMVISGNVPQGAGLSSSASLEVAVGTVLQQLYHLPLDGAQIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLGTKAVSMPKGVAVVIINSNFKRTLVGSEYNTRREQCETGARFFQQPALRDVTIEEFNAVAHELDPIVAKRVRHILTENARTVEAASALEQGDLKRMGELMAESHASMRDDFEITVPQIDTLVEIVKAVIGDKGGVRMTGGGFGGCIVALIPEELVPAVQQAVAEQYEAKTGIKETFYVCKPSQGAGQC", "text": "FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily."}
{"protein": "MNLKKFFNTPTHEPFRDKKAERNLFARRTLVAFLGILLLTGVLFTNIYQLQIVNFDTYQTRSNGNRIKLLPLPPTRGLIYDRYGKLLAENLTFFGLYIVPEKTENLDRTLDELRYIVGLTDNDIENFKKERRRGTRYTPILLKPNLTEEQISRFAVNGYQYPSLEVRPYFKRHYLYGETMAHILGYVGKMNDKDVERLKREDKFANYAGTNDIGKLGIERYYEDILQGTTGFEEVEINNRGKVIRTLRSRPAVAGKSIHLTIDLALQRYITELLSGLKGAVVVLDPKDSSVLAMVSTPSYDNNLFVDGISSEDYKRLLNDLARPLYSRATQGAYPPASTVKPFIAVAAQTENVITPNTTIFDPGYWVLPNSTKRFRDWKKTGHGDTDLNKAITESSDTYFYQVAYNMGIDRLSNWMKDFGFGMPTGIEIQEETAANIPTREWKQKRYKRPWVQGDTISVGIGQGYWTATPLQVAKATTILVNNGKVNTPHLMKAIEGAVLEPYEDPLLYPDINTPKVAAWEAAKRGMYNVVNAANGTGRKAFADANYRVAGKSGTAQVFSLKENEKYNTAGLKKELHDHAWFTAYAPYDNPKLVVTVILENAGGGSSNAAPLARKVMDYYLNQRLPQVEKYNVPIQQKKDLSQESEQINGR", "text": "FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the transpeptidase family. MrdA subfamily."}
{"protein": "MSFLKNLFKKKSPTHELFHPLSRSPLTALRRRSEHIKQVYRCPISGKSVEYECPESGFPTHCNRTHWEQDKIHQSLIPKLRQINEDYHDLARPNPLPELLKLPGPMEEDEVVSLLSWDSFFYTRDFPKFQSSRTARHITSLLTYPMSIGAILHKNSPYNLKNGLTPQGLQSLTALRYMLHRPLSAQSTDPRPTRIFVLGATKECSLPPSIWLQGLNFLFPGRLFQLHFIGPEVVVPSKQPNLPSPLSLHFHQDYYHNLHRVGAFEPFDPYYDTFFLPMPLISHPLYSSSWIPTLHDLVSTRCSVWLTSPSSQRTTKDLEVLNNVLKDSIEPLLLPTVNKFASLGWSVDDSNLHEVYHANQEVFGFRALYYNVQNVSKE", "text": "FUNCTION: Has a dual role in the assembly of cytochrome oxidase subunit 1 (cox1). It has a regulative function on cox1 synthesis, acting as a translational activator specific for the cox1 mRNA, and it also binds to newly synthesized cox1 protein (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the MSS51 family."}
{"protein": "MDFESQLCIKVVLLLLPFFIIGIRLLWVLPAVNSPAMGSEKEKGLSQIPSELRGSNIMIFLGSGGHTGEMMRILANVDLNNFNRTWVTSSGDSTSILKCKKYEDERLTSGQNKSDYLVLHRARTVGESIISSVFSTVRSLISTIKHLYELPQFPSILLLNGPGTSVPLAYIIFLLKFLGLCKTRIIYIESLARVKQLSVSGLLILPITDRFIVQWKQLAVKYKRAEYYGILI", "text": "FUNCTION: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus membrane; Single- pass membrane protein. SIMILARITY: Belongs to the ALG14 family."}
{"protein": "MAKGGKGPKGKKITLNVAKNCIKITFDGRKRLDLSKMGITTFPKCILRLSDIDELDLSRNMIRKIPDSIAKFQNLRWLDLHSNYIDKLPESIGQMTSLLFLNVSNNRLTTNGLPVELNQLKNIRTVNLGLNHLDSVPTTLGALKELHEVGLHDNLLTTIPASIAKLPKLKKLNIKRNPFPNADESEMFVDSIKRLENLYLVEEKDMCSSCLQRCQQARDKLNKIKSMAPSAPRKALFSNLVSPNSTAKDAQEEWRLRSPSTF", "text": "FUNCTION: May be involved in the regulation of spermatogenesis and sperm maturation. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MNSIVNFSQQLIQNFQEVSQKTAADSSNLKAFAYLGAGLAMIGVIGVGAGQGYAAGKACDAIARNPEAQKQVFRVLVIGTAISETSSIYALLVALILIFVG", "text": "FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family."}
{"protein": "MWMAWCVAALSVVAVCGTSHETNTVLRVTKDVLSNAISGMLQQSDALHSALREVPLGVGDIPYNDFHVRGPPPVYTNGKKLDGIYQYGHIETNDNTAQLGGKYRYGEILESEGSIRDLRNSGYRSAENAYGGHRGLGRYRAAPVGRLHRRELQPGEIPPGVATGAVGPGGLLGTGGMLAADGILAGQGGLLGGGGLLGDGGLLGGGGVLGVLGEGGILSTVQGITGLRIVELTLPRVSVRLLPGVGVYLSLYTRVAINGKSLIGFLDIAVEVNITAKVRLTMDRTGYPRLVIERCDTLLGGIKVKLLRGLLPNLVDNLVNRVLADVLPDLLCPIVDVVLGLVNDQLGLVDSLIPLGILGSVQYTFSSLPLVTGEFLELDLNTLVGEAGGGLIDYPLGWPAVSPKPMPELPPMGDNTKSQLAMSANFLGSVLTLLQKQHALDLDITNGMFEELPPLTTATLGALIPKVFQQYPESCPLIIRIQVLNPPSVMLQKDKALVKVLATAEVMVSQPKDLETTICLIDVDTEFLASFSTEGDKLMIDAKLEKTSLNLRTSNVGNFDIGLMEVLVEKIFDLAFMPAMNAVLGSGVPLPKILNIDFSNADIDVLEDLLVLSA", "text": "FUNCTION: May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm. SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family."}
{"protein": "MTIEFSHTTGLLLLAMPALLLMAAVIKPKQGAAYARAYRQRVQWTSFAAFGLALLAVVSFLFARQQNLMLGAGSLPAGLGLLALSIQVNGLTLVLASLVSFVLSVIARYSVQYLDGDPQQARFFRLLAVTGGFFLLVVISGNLGLFTLAIIATGFGLHRLLSFYADRPRAIMATHKKSIFSRTADALLLAATVLIGHQIGSLEFSQISAYVHAQDHLSIALHVAAWLIVLAAILKSAQFPFHGWLIQVMEAPTPVSALMHAGVVYSGAIIVLRTSELLAADGTALLLLALIGLMTLAIGSLVMLTQSAIKSSLAWSTAAQLGFMMLELGLGLFGLALLHLVGHSLYKAHAFLSSGSMTDHLRQAKVLKNRPISVVAWFTTVIVSGLFTLGIAAAMGLSIDQEPMLPAVLTIIALATAQLMLKALSHGTWREILVAAGAAIAMTGVYVFLHEVFITGFADTLAATPQRAPLLDLLLMAITIITFLFVAWLQGPGKTLMSPERQFALFVHLNNGLYLDRWVERLAFRFWPEKVGRAPKKSCAVIPPNPSGIEP", "text": "FUNCTION: Part of an energy-coupled inorganic carbon pump; its substrate may be carbon dioxide. Expression of both dabA2 and dabB2 (DAB2) restores growth in ambient air to E.coli deleted of its carbonic anhydrase genes (called CAfree, deletion of 'can' and 'cynT'); neither dabA2 or dabB2 alone is sufficient. Rescue is pH-independent, suggesting it transports CO(2) and not carbonate ions. Together the genes allow greater than normal uptake of inorganic carbon by E.coli (PubMed:31406332). Uptake of carbon dioxide rather than bicarbonate has been suggested based on kinetic calculations (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabB family."}
{"protein": "MENTLGEGSTVNASVDVDQHGNDNNSDSNANAAVAGVANTDTAGEESQQQDESLKDEATVPNTRDAESEAITVTAKQQPTMQANKLDSQETPSTEESRAQNVFGQDNEDSDNLFGETESSVSNNEANTPSIPTNPVDNENNKPAIKEDSTIQDSNGDVKNMEDVKIQKEEEPENNTVIEGVKEESQPDENTKEMDEVEEDDEDDDQPMISPDNSIFGDTKSESKQLGNTSSVANTPSEIPDAHKAEQEDIIEKTESVDKKVDSGEERNEQEREIMNDHSKSANPKKTTITRVEPETFEIPQAHEIVIPSYSKWFNLEKIHSIEVQSLPEFFTNRIPSKTPEVYMRYRNFMVNSYRLNPNEYFSVTTARRNVSGDAAALFRLHKFLTKWGLINYQVDSKLLPKNIEPPLTSQYSTRHDAPRGLFPFESYKPSVQLPDMAKLKKMMNTSDSESTLYKYLKESKRKYDEITHPPSTTDDENGDKNDNGGKMNNEVSTSTSMTGDANLLEEGETSRPLKKVKILEQIDENWSKEDLQKLLKGIQEFGADWYKVAKNVGNKSPEQCILRFLQLPIEDKFLYGDGNGKGDNDNGLGPLKYAPHLPFSKSENPVLSTIAFLVGLVNPKTVQSMTQRAIQSAESIKSQKEEISDQKPIEHIKEGSEIAISSLGYRSHIFATNEERQMNFLTNELIRLQMEKLDAKLNHLKKLEKFMELERKTLERQQENLLIQRLNFNQNSSKIVNVLSKCLNLISDSNINNSSVAEKEEIRSQIDHFKSMLSKPETLSIGKNPFNKPNIETGENHNGQSISNENDVKPISIEAPQFYRYWSA", "text": "FUNCTION: Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MVTILSTPLSPRLTFLCETKLSLSRSNRSVCCSLSEEPKDQCLSRRSLVYVLVASPCLLLPALSSSAKTKSKSPYDERRLLEQNKRIQRENNAPDEFPNFVREGFEVKVLASDNYIKADSGLIYRDFNVGQGDFPKDGQQVTFHYIGYNESGRRIDSTYIQGSPARIRMGTNALVPGFEMGIRDMKPGGRRRIIIPPELGPPVGPSTFFSSKQFEVFDVELLSIQNCERRTIIGFYSDVTCS", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Involved in the accumulation of the PSII complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the FKBP-type PPIase family."}
{"protein": "MAVIESVGANTTVEAGGLISPSPPSSVTSQESGASSNNDHGGNGIHDEIGVHVARSDGGESFKRDMRELHELLSKLNPMAKEFIPPSLTKPVVNGFNGGFFAVNNGFVAAGNFPVNEDGSFRRKKSFGQQGKRRMNPRTSLAQREEIIRRTVYVSDIDQQVTEEQLAGLFIGFGQVVDCRICGDPNSVLRFAFIEFTDEVGARTALNLSGTMLGFYPVKVMPSKTAIAPVNPTFLPRTEDEREMCARTIYCTNIDKKLTQTDIKLFFESVCGEVYRLRLLGDYHHPTRIGFVEFVMAESAIAALNCSGVLLGSLPIRVSPSKTPVRSRAIPRHQMH", "text": "FUNCTION: Binds nucleotic acids in vitro. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLFRSLVTYLSLVSSVLSIASIKVEGNAFWDSESGDRFYIRGVDYQPGGSSELEDPLADTNVCERDVKYFQELGINTIRVYSIDNTKNHTECMDTLAKAGIYVILDVNTPHSSITRSDAACSYNTDYLQEVFASIVEFAQFDNTLGFFAGNEVINDGPSLEAAPYVKAVVRDMKTFIKNRGFRTIPVGYSAASVDEYRLPSGLYFNCGDDDMARIDMYGINDYSWCGDASMTTSQYSQQMKDFANYTVPLFFSEFGCNAKRPRPFSEIEAIYSTEMSSVFSGGLVYEYSEEASNYGLVELKGDSVTTNDDFDNLKSQFEKTKNPSGDGGYLKSTGGNKCPPKSNIWNVTEEIPDTPKGALKYLKGLAEPTGHGFDAYVQGNCNAKGNNVDDTGNYTSSITASSRASPSQTSQVSSSSATSANSTSSKKNDAAVEGAGFLSVIALAAGIALL", "text": "FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis. Plays a key role in virulence. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Lipid-anchor, GPI-anchor Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). SIMILARITY: Belongs to the glycosyl hydrolase 72 family."}
{"protein": "MLNFVRIFLPFLKYQVFTDKTNDLLKYNIYVFDVDKKLNKLQIKNIIEYIFNIKIYSINTYIKNNKYCCFNKIKGLKTNYKRAFIRLKSVNIIPYFSC", "text": "FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uL23 family."}
{"protein": "MAKKSMIERDKKRENLMNKYLVKRQQLKTRLNETDSVEEKLLLNQELQKLPRNSAPSRVRIRCWLTGRPRGNYRDFGVSRHVLREMAHQGLLPGVTKSSW", "text": "FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the universal ribosomal protein uS14 family."}
{"protein": "MAAGSRTSLLLAFALLCLPWLQEAGAVQTVPLSRLFKEAMLQAHRAHQLAIDTYQEFISSWGMEAYITKEQKYSFLHDSQTSFCFSDSIPTSSNMEETQQKSNLELLHISLLLIESRLEPVRFLRSTFTNNLVYDTSDSDDYHLLKDLEEGIQMLMGRLEDGSHLTGQTLKQTYSKFDTNSHNHDALLKNYGLLHCFRKDMDKVETFLRMVQCRSVEGSCGF", "text": "FUNCTION: May be a novel gestational hormone required to compensate for absence of other members of the GH/CS cluster during gestation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family."}
{"protein": "MKASGTLREYKVVGRLLPSVKNPAPPLYRMRIFAPNHVVAKSRFWYFVSQLRKMKKASGEIVYCGLVFEKSPLKVKNFGIWLRYDSRSGTHNMYREYRDLTTSGAVTQCYRDMGARHRARAHAIQIMKVQVIAANKCRRPAIKQFHDSKIKFPLPHRVLRRQHKPRFTTKRPNTFF", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL20 family."}
{"protein": "MAAATTSRRGPGAMDDENLTFETSPGVEVISSFDQMGIRDDLLRGIYAYGFEKPSAIQQRAVLPIISGRDVIAQAQSGTGKTSMISLSVCQIVDTAVREVQALILSPTRELAAQTERVMLAIGDFINIQVHACIGGKSIGEDIRKLEHGVHVVSGTPGRVCDMIKRRTLRTRAIKLLILDEADEMLGRGFKDQIYDVYRYLPPELQVCLISATLPHEILEMTSKFMTDPVRILVKRDELTLEGIKQFFVAVEKEEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTERMRSNNFTVSAMHGDMPQKERDAIMGEFRSGATRVLITTDVWARGLDVQQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKKEDIRILRDIEQYYSTQIDEMPMNVADLI", "text": "FUNCTION: ATP-dependent RNA helicase. Core component of the splicing- dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by MLN51/CASC3, but abolished in presence of the MAGO-Y14 heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGO-Y14 heterodimer increases the RNA-binding affinity of the EJC (By similarity). EJC core proteins play essential roles in rice development, growth and reproduction. Regulates the splicing of UDT1 (UNDEVELOPED TAPETUM 1) pre-mRNA transcript. UDT1 is a key regulator in stamen development (PubMed:27071313). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. SIMILARITY: Belongs to the DEAD box helicase family. DDX48/FAL1 subfamily."}
{"protein": "MYQSPRRLCSALLLRDAPGLRRTLVPGPRRTLAPPVLGSRPASPQLQAAASGAARSRPRTVSPMGNGTSRLYSALAKTINSSAAAQHPEYLVSADPEHLEPIDPKELLEECRAVLHTRPPRYQRDFVDLRTDCSSSHPPIRVMQWNILAQALGEGKDNFVQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFFLQSRFKLINSTNIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITEGAKIPLIVCGDFNAEPTEEVYKHFASSSLNLNSAYKLLSPDGQSEPPYTTWKIRTSGECRHTLDYIWYSRHALSVTSALDLLTEEQIGPNRLPSFHYPSDHLSLVCDFSFNEEPDELL", "text": "FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control (By similarity). Exerts a rhythmic post- transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis (By similarity). Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance (By similarity). Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity (By similarity). Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone (By similarity). Critical for proper development of early embryos (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, perinuclear region Mitochondrion. SIMILARITY: Belongs to the CCR4/nocturin family."}
{"protein": "MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGEAKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRNDKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIISWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD", "text": "FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J- domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Substrate recognition component in chaperone- mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co- chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21. SUBCELLULAR LOCATION: Cytoplasm Melanosome Nucleus, nucleolus Cell membrane Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEVSGARFWGFFRNLCGQPEVFFHHCFVHNLCPLLFLAPSGRNLTPAELPAKQREQLLGICDAALCRQVQLLGVRLVVGVGRLAEQRARRALAGLMPEVQVEGLLHPSPRNPQANKGWEAVAKERLNELGLLPLLLK", "text": "FUNCTION: Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5- formylcytosine), nor other oxidized bases. The activity is damage- specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. SMUG1 family."}
{"protein": "MNLVNKAEKTFALTTPLYYVNDVPHIGSAYTTMAADAVARFQKLLGRDVLLITGTDEHGQKIQRSAESLGKAPQEFCDEIVPSFMSLWRLLNIQYDRFSRTTAVRHKAIVDEFFARVWEAGDIYQGQQKGWYCVSCEEFKEERELLEGNRCPIHVNKEVEWRDEQNYFFRLSKYQTQLEEFYQSHPDFIQPESRRNEVLNFVSQGLQDFSISRVNLDWGFPVPNDPKHTLYVWFDALLAYVTALLDPEDEPTLENALGKWWPINLHLIGKDILRFHAVYWPAMLLSAGLPLPDRVFGHGFLTKDGQKMGKSLGNTVDPVGLVQQYGSDAVRYYFLKEIEFGKDGDFNEVRFIHVLNADLANDLGNLLNRTLNMVKKYCANYALSITNEDIPAENTLKALGVDLGAKVKQAYEVLAFNQACGVVLSLVQASNKFIDDQAPWSLYKQERQQEVETVLYTVLESVRLAAYLLSPVIPNISSNIYQQLGFGINFNEQTDITPFAIHAQWGLLSNKQQLGQPQPIFKRIEQTKNV", "text": "FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2A subfamily."}
{"protein": "MKNIVFCGLSSRAFSMFIKPLMERFSTHYEITGLLDADPKRFAVCKKKFPELAHVPEFSEDAFDEMMRVSKPDIVIVAGRDDTHVAYIVKSLQWNTDVITEKPMVTTVQDANRVLEAEAKSEGKVTVAFNYRYSPFHRKIKEMILDGKIGRVTSVDLNWYIDTYHGASYFKRWNRSRQFSGGLSVHKSTHHFDLVNWWLGQNPEEVFAYGALNYYGPDSEWNPLPEEDGRFCGTCRVKEKCHYYSRWHPRSSKASIKDDHLEAGDQSSLYTAYRPDACIFDEEIDIEDTYVAAVKYDGGALLSYSIIFSAPYEGYRLTINGTKGRIESNEFHEPSRIPFAFPEQTIEYYPLFESKQTIQVVKNEGGHGGGDPLLLEDLFLGKDPLRRYDILAGAEAGAYSIAVGEGMWRSVAEKKPIGMKELFQMQNV", "text": "FUNCTION: May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. SIMILARITY: Belongs to the Gfo/Idh/MocA family."}
{"protein": "MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFIDNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKAHNNVTGESEKNHDTGVSPVFAGGVEWAITPEIATRLEYQWTNNIGDANTIGTRPDNGLLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA", "text": "FUNCTION: Required for conjugation with F-type plasmids; probably serves as the mating receptor on recipient cells. FUNCTION: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpA family."}
{"protein": "MKTTIKDIKTRLFKIPLKEILSDAKHGDHDHFELITTTVTLEDGSQGTGYTYTGGKGGYSIKAMLEYDIQPALIGKDATQIEEIYDFMEWHIHYVGRGGISTFAMSAVDIALWDLKGKREGLPLWKMAGGKNNTCKAYCGGIDLQFPLEKLLNNICGYLESGFNAVKIKIGRENMQEDIDRIKAVRELIGPDITFMIDANYSLTVEQAIKLSKAVEQYDITWFEEPTLPDDYKGFAEIADNTAIPLAMGENLHTIHEFGYAMDQAKLGYCQPDASNCGGITGWLKAADLITEHNIPVCTHGMQELHVSLVSAFDTGWLEVHSFPIDEYTKRPLVVENFRAVASNEPGIGVEFDWDKIAQYEV", "text": "FUNCTION: Involved in the degradation of 3,6-anhydro-L-galactose, which is the major monomeric sugar of red macroalgae. Catalyzes the isomerization of 3,6-anhydrogalactonate (AHGA) to 2-keto-3-deoxy- galactonate (KDGal). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family."}
{"protein": "MGQKFSIKCKKQSKNKNTSKCQKIPKKAYEGPPGSYMVKAKYKYAASGDTDISFEEKEIMYVLEQFDEFWLKVVKQKDNKEGLVPSNYVSKQDGSPQSVEAWREIQRWEAEKSLMKIGLQKGTYIIRPSRKENSYALSVRDFDEKKKICIVKHFQIKTLQDEKGISYSVNIRNFPNILTLIQFYEKNGIGNTHIPLTDPMPDNYQPPVHFQDIEINRENIEILNEIGRGFFGSVHRAKWGRSYEVAAKMLQSSKAEREKFVLEAKIMHKLRHRKIVELLGVCTEPQDMPMLIIVEYMKNGSLKEYLKTPDGKKTNLNQMVHMMAEISEGMAYLESEKVVHRDLRADNILVANDLTRKVADFGLTELTDGSLGDQEKKTLRFPYKWTAPEAAKSKVFTSKSDVWSYGIVMFEILTWASSPYPDIPAKEVIEKVSKGYRMPNPEKFITGVCCPDEIYKIMIWCWDANPEKRPTFLVLQEKMDLLIVDTLTNNAYYSHSK", "text": "SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family."}
{"protein": "MSSETGPVAVDPTLRRRIEPHEFEVFFDPRELRKETCLLYEINWGGRHSVWRHTSQNTSNHVEVNFLEKFTTERYFRPNTRCSITWFLSWSPCGECSRAITEFLSRHPYVTLFIYIARLYHHTDQRNRQGLRDLISSGVTIQIMTEQEYCYCWRNFVNYPPSNEAYWPRYPHLWVKLYVLELYCIILGLPPCLKILRRKQPQLTFFTITLQTCHYQRIPPHLLWATGLK", "text": "FUNCTION: Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs. Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the apolipoprotein B mRNA. Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA (By similarity). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (PubMed:21496894). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MVGTALLLLALLPGTSSKHGTPRAPLLPGAPGPWLRRPLFSLELSDAEDAFPRRAGPLEVPADSHVFVQAALARPSPRWGLALHRCSVTPSSRPTLGPALVLLRGGCPADDSVSFSPPPRPDAASVSRFSFRLRPVFNASVQFLHCQISRCRRRSSHHRRAVRLTPVPLTPPAPLRCLPQDEACAGSSLSLGTDSPHLHMLTQPIVVTIPRPSPRPSKSLPGRSVHPEPPAPAPAALEPAPVVALVLAAFVLGAALAAGLGLVCAHSAPPPPGPPPRASLSGPQLQRPPVGRDGTTQ", "text": "FUNCTION: Expressed in gonadotrope cells, acts as an inhibin B coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein."}
{"protein": "MEILRIEPTPSPNTMKVVLSYTREDKLSNTYKKVEENQPRFINQLLSIDGITSIFHVMNFLAVDKAPKADWEDILPDIKAAFSGESQVLESGKDPQIDNHFGEIKAELLTFKGIPYQIKLTSADQELREQLPQTYVDHMTQAQTKHDNIVFMRKWLDLGNRYGNIEEVMDGVLEEVLATYPESQLPVLVKHALEENHATNNYHFYRHVSLDEYHATDNWKTRLRMLNHFPKPTFEDIPLLDLALSDEKVPVRRQAIVLLGMIESKEILPYLYKGLRDKSPAVRRTAGDCISDLGYPEALPEMVLLLDDPQKIVRWRAAMFIFDEGNAEQLPALKAHINDNAFEVKLQIEMAISRIENGDEALGSVWKQMTNRTI", "text": "FUNCTION: Required for hemolysin production. SIMILARITY: Belongs to the CvfC family."}
{"protein": "MKKKQTKVKQTVKLVLRNPLSISWPIVDANTQEKLAQTLVQWLPASHKDILDSKLTVGLNSVNELLERCCQNAKDVTQPAVVFILHDQDSMLVTHMPQLVANANFYGSSKCRLVPLGFSAQALIAKKLGLSRAGAIAVQDDSPLWKYLKDLVMNIEEPQARWLSENPEYEVTKVEKIITSQKENQGTKKEGKNEKGNEFKK", "text": "FUNCTION: Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the POP3 family."}
{"protein": "MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLGISFSKPELITQLEQGKETWREEKKCSPATCPADPEPELYLDPFCPPGFSSQKFPMQHVLCNHPPWIFTCLCAEGNIQPGDPGPGDQEKQQQASEGRPWSDQAEGPEGEGAMPLFGRTKKRTLGAFSRPPQRQPVSSRNGLRGVELEASPAQSGNPEETDKLLKRIEVLGFGTVNCGECGLSFSKMTNLLSHQRIHSGEKPYVCGVCEKGFSLKKSLARHQKAHSGEKPIVCRECGRGFNRKSTLIIHERTHSGEKPYMCSECGRGFSQKSNLIIHQRTHSGEKPYVCRECGKGFSQKSAVVRHQRTHLEEKTIVCSDCGLGFSDRSNLISHQRTHSGEKPYACKECGRCFRQRTTLVNHQRTHSKEKPYVCGVCGHSFSQNSTLISHRRTHTGEKPYVCGVCGRGFSLKSHLNRHQNIHSGEKPIVCKDCGRGFSQQSNLIRHQRTHSGEKPMVCGECGRGFSQKSNLVAHQRTHSGERPYVCRECGRGFSHQAGLIRHKRKHSREKPYMCRQCGLGFGNKSALITHKRAHSEEKPCVCRECGQGFLQKSHLTLHQMTHTGEKPYVCKTCGRGFSLKSHLSRHRKTTSVHHRLPVQPDPEPCAGQPSDSLYSL", "text": "FUNCTION: May be involved in transcriptional regulation as a repressor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."}
{"protein": "MNATEQAANGDRGTTRSAGGRLRYLLHAPGACQLMGVHDGLSARIAVAEGFEALWASGLCMSTARGVRDSDEASWTELLTLVGTMTDAVPGVPVLVDGDTGYGNFNTARRFAGRAERVGAAGVCFEDKVFPKMNSFFGDGHQLAPVAEFCGKIRACKDAQRDPDFVVVARTEALISKLPMEEALDRAAAYAEAGADALFIHSRMNTPQQIATFMERWEGSTPVLIAPTTYHTPSVDDFAALGIAGCIWANHSMRAAFAAMRDVCQRIRTDRGIYGIEDQVAPLKEIFGLFDYEGLEKDENCYTQAPDLAAVQG", "text": "FUNCTION: Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP mutase family."}
{"protein": "MQNSTCQAVGECRVPEHAVLPQPLYREVVQFIESLPQKEGHLVTVLHKAQSVFGYLPIEVQQFVADHMEVPLAQVYGVVSFYTFFTMVPKGKYPISVCMGTACFVKGADKVVHAFKEQLKIDIGDVTPDGRFSIDTLRCVGGCALAPIVMVGEKVYGNVTPGQVKKILAEY", "text": "FUNCTION: Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH. SIMILARITY: Belongs to the complex I 24 kDa subunit family."}
{"protein": "MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKSGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI", "text": "FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly- ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'- linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1- UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'- linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UB2V1, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (By similarity). UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MAQFEWVHAAWLALAIVLEIVANVFLKFSDGFRRKIFGLLSLAAVLAAFSALSQAVKGIDLSVAYALWGGFGIAATLAAGWILFGQRLNRKGWIGLVLLLAGMIMVKLA", "text": "FUNCTION: Catalyzes the excretion of spermidine. FUNCTION: Catalyzes the excretion of spermidine. Can also confer resistance to deoxycholate and SDS. FUNCTION: Catalyzes the excretion of spermidine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtI subfamily. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtI subfamily."}
{"protein": "MDLLLLEKTLLGSFVAILVAILVSKLRGKRFKLPPGPLPVPVFGNWLQVGDDLNHRNLTDLAKKFGDILLLRMGQRNLVVVSSPELSKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKVVQQYRYGWEEEAAQVVEDVKKNPGAATHGIVLRRRLQLMMYNNMYRIMFDRRFESEEDPLFNKLKALNGERSRLAQSFDYNYGDFIPILRPFLRGYLKICQEVKERRLQLFKDYFVDERKKLASTKNMCNEGLKCAIDHILDAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRHELDTLLGPGHQITEPDTYKLPYLNAVVKETLRLRMAIPLLVPHMNLHDAKLGGFDIPAESKILVNAWWLANNPAHWKNPEEFRPERFLEEEAKVEANGNDFRYLPFGVGRRSCPGIILALPILGITLGRLVQNFELLPPPGQSKIDTSEKGGQFSLHILKHSTIVAKPRSF", "text": "FUNCTION: Catalyzes the first oxidative step of the phenylpropanoid pathway in higher plants by transforming trans-cinnamate into p- coumarate (By similarity). The compounds formed by this pathway are essential components for lignification, pollination, and defense against ultraviolet light, predators and pathogens (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MYNMRRLSLSPTFSMGFHLLVTVSLLFSHVDHVIAETEMEGEGNETGECTGSYYCKKGVILPIWEPQDPSFGDKIARATVYFVAMVYMFLGVSIIADRFMSSIEVITSQEKEITIKKPNGETTKTTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFTAGDLGPSTIVGSAAFNMFIIIALCVYVVPDGETRKIKHLRVFFVTAAWSIFAYTWLYIILSVISPGVVEVWEGLLTFFFFPICVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIEHEGDRPSSKTEIEMDGKVVNSHVENFLDGALVLEVDERDQDDEEARREMARILKELKQKHPDKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNTEVTENDPVSKIFFEQGTYQCLENCGTVALTIIRRGGDLTNTVFVDFRTEDGTANAGSDYEFTEGTVVFKPGDTQKEIRVGIIDDDIFEEDENFLVHLSNVKVSSEASEDGILEANHVSTLACLGSPSTATVTIFDDDHAGIFTFEEPVTHVSESIGIMEVKVLRTSGARGNVIVPYKTIEGTARGGGEDFEDTCGELEFQNDEIVKTISVKVIDDEEYEKNKTFFLEIGEPRLVEMSEKKALLLNELGGFTITGKYLFGQPVFRKVHAREHPILSTVITIADEYDDKQPLTSKEEEERRIAEMGRPILGEHTKLEVIIEESYEFKSTVDKLIKKTNLALVVGTNSWREQFIEAITVSAGEDDDDDECGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWNGWACFIVSILMIGLLTAFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIYHAANGEQFKVSPGTLAFSVTLFTIFAFINVGVLLYRRRPEIGGELGGPRTAKLLTSCLFVLLWLLYIFFSSLEAYCHIKGF", "text": "FUNCTION: Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes (PubMed:1374913, PubMed:11241183, PubMed:1476165). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle (PubMed:1374913, PubMed:11241183, PubMed:1476165). In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum (PubMed:1374913, PubMed:11241183, PubMed:1476165). SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline (PubMed:1374913, PubMed:11241183, PubMed:1476165). Required for normal embryonic heart development and the onset of heart contractions (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC8 subfamily."}
{"protein": "MPESQIIELGTLGQIPLYSLERALQDPLRAVKLRRQIVSQHQATGNIDFTTDGSALPYEGYDYKAVLGACCENVIGYMPIPVGVAGPIKINGKMVFLPMSTTEGALVASTNRGCMAINAGGGVTALVLGDGMTRAPIVRFPSLEEAGAAKQWLGSDAGFLIIEDAFNASSRFARLQNIKATAVGSDLYIRFTASTGDAMGMNMISKGVEQALEAMQKHGFESMDVVSLSGNFCADKKPAAVNWIEGRGKTVTAQATIPEHAVRETLKTSVEALVELNVSKNLVGSAVAGALGGFNAHAANVVTAIYLATGQDPAQNVQSSNTLTVMKNVNGDLQISVFMPSIEVGTVGGGTVLGPQKAMLHMMGVQGADPEQPGRNAQELALLVAAGVLAGELSLCSALSAGSLVKSHLTHNRKKG", "text": "FUNCTION: 3-hydroxy-3-methylglutaryl coenzyme A reductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent- pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara- 8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HMG-CoA reductase family."}
{"protein": "MAATFFGEVVRTPCRAGTEEEEEEEDGNRETPEDREVRRQLARKREVRLFRRQTKTTLEVSLLEKHPCSKFIIAIGNNAVAFLSSFVMNSGAWEEVGCAKLWNEWCRTTDTAHLSPTEAFCVFYHLKSNPSVMLCQCSCYVAEDQQYQWLEKVFGSCPRKNMQVTILTCRHVTDYKTSESTSSLHTPFLKALKTQNFKEPPFCSLLEQPNIVHDLPAAVLSYCQVWRIPAVLYLCYTDVMKLDLITIEAFKPVLSSKSLKCLVKNIPQSTEILKKLMTTNEIQSNIYT", "text": "FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the PSMG1 family."}
{"protein": "MLRTLLRRRLFSYPTKYYFMVLVLSLITFSVLRIHQKPEFVSVRHLELAGENPSSDINCTKVLQGDVNEIQKVKLEILTVKFKKRPRWTPDDYINMTSDCSSFIKRRKYIVEPLSKEEAEFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDTKSEDSYLAAVMGIASCFSNVFVASRLESVVYASWSRVQADLNCMKDLYAMSANWKYLINLCGMDFPIKTNLEIVRKLKLLMGENNLETERMPSHKEERWKKRYEVVNGKLTNTGTVKMLPPLETPLFSGSAYFVVSREYVGYVLQNEKIQKLMEWAQDTYSPDEYLWATIQRIPEVPGSLPASHKYDLSDMQAVARFVKWQYFEGDVSKGAPYPPCDGVHVRSVCIFGAGDLNWMLRKHHLFANKFDVDVDLFAIQCLDEHLRHKALETLKH", "text": "FUNCTION: Glycosyltransferase that catalyzes the transfer of an N- acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan (PubMed:1329093, PubMed:23027862). The catalysis is metal ion- independent and occurs with inversion of the anomeric configuration of sugar donor (By similarity). Selectively involved in synthesis of mucin-type core 2 O-glycans that serve as scaffolds for the display of selectin ligand sialyl Lewis X epitope by myeloid cells, with an impact on homeostasis and recruitment to inflammatory sites (By similarity). Can also act on glycolipid substrates. Transfers GlcNAc moiety to GalGb4Cer globosides in a reaction step to the synthesis of stage- specific embryonic antigen 1 (SSEA-1) determinant (By similarity). Can use Galbeta1-3GalNAcalpha1- and Galbeta1-3GalNAcbeta1- oligosaccharide derivatives as acceptor substrates (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Note=Also detected in the trans-Golgi network. SIMILARITY: Belongs to the glycosyltransferase 14 family."}
{"protein": "MARLGNCSLTWAALIILLLPGSLEECGHISVSAPIVHLGDPITASCIIKQNCSHLDPEPQILWRLGAELQPGGRQQRLSDGTQESIITLPHLNHTQAFLSCCLNWGNSLQILDQVELRAGYPPAIPHNLSCLMNLTTSSLICQWEPGPETHLPTSFTLKSFKSRGNCQTQGDSILDCVPKDGQSHCCIPRKHLLLYQNMGIWVQAENALGTSMSPQLCLDPMDVVKLEPPMLRTMDPSPEAAPPQAGCLQLCWEPWQPGLHINQKCELRHKPQRGEASWALVGPLPLEALQYELCGLLPATAYTLQIRCIRWPLPGHWSDWSPSLELRTTERAPTVRLDTWWRQRQLDPRTVQLFWKPVPLEEDSGRIQGYVVSWRPSGQAGAILPLCNTTELSCTFHLPSEAQEVALVAYNSAGTSRPTPVVFSESRGPALTRLHAMARDPHSLWVGWEPPNPWPQGYVIEWGLGPPSASNSNKTWRMEQNGRATGFLLKENIRPFQLYEIIVTPLYQDTMGPSQHVYAYSQEMAPSHAPELHLKHIGKTWAQLEWVPEPPELGKSPLTHYTIFWTNAQNQSFSAILNASSRGFVLHGLEPASLYHIHLMAASQAGATNSTVLTLMTLTPEGSELHIILGLFGLLLLLTCLCGTAWLCCSPNRKNPLWPSVPDPAHSSLGSWVPTIMEEDAFQLPGLGTPPITKLTVLEEDEKKPVPWESHNSSETCGLPTLVQTYVLQGDPRAVSTQPQSQSGTSDQVLYGQLLGSPTSPGPGHYLRCDSTQPLLAGLTPSPKSYENLWFQASPLGTLVTPAPSQEDDCVFGPLLNFPLLQGIRVHGMEALGSF", "text": "FUNCTION: Receptor for granulocyte colony-stimulating factor (CSF3), essential for granulocytic maturation. Plays a crucial role in the proliferation, differientation and survival of cells along the neutrophilic lineage. In addition it may function in some adhesion or recognition events at the cell surface. SUBCELLULAR LOCATION: [Isoform 2]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily."}
{"protein": "MKFPLLLALLVGGASALHLSSETSDSKSPLMDENLPRDAEISGPEGEECPPGEELMPLEGEKEEGSGSEGVPGDEGAVSGQDVTDVDLQCPKEEDTTSLMGDSGCKTCRYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIKGWGRCKRFRWVDGSSWNFAYWAAGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFICSY", "text": "FUNCTION: Cytotoxin and helminthotoxin. MBP also induces non-cytolytic histamine release from basophils. It is involved in antiparasitic defense mechanisms and immune hypersensitivity reactions (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MSMNNITSKMNQDSYGYFQLHMSDFTRVSLSIVFTLVFLVGIIGNAVIIWFIGFKWTKTISTLLFINLALADSLFLIFIPVYTVYVLSNFHWYLGEFLCRVSSFFFTTNMYASMFLLTFISIDKYLTLTSHRLVYKYRKYRNYYVCIGAIWCISIALGVPTLYYKRVILSSSRNETRCISYYGDDKHTAITIYRIIVCIRFIIGYVFPMTVILLSYALIVYKVKFINKPPNRSFMITTASIFVFLACWTPHHVLNIISLYGLKSTSMYNYIKESIPFVNAIAFVYSAINPIIYIFVIRLTSTYDSDTMDELRSALLDEETTSTEDCSDIEISDISR", "text": "SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MMNPRRLPPLPSSTSSASAADDMDPRVWRRLPQPLVDRVLACLPTPSFLRLRAACRRFYHLLFSSPFLHSHLLLSPHLPFFAFVVPAAGHLLLLDPTATASWSRLPLPLPPVAGGPAAFSPAAASAGLLAFLSDASGHKTLLLANPITRLLAALPISPTPRLSPTVGLAAGPTSIIAVVAGDDLVSPFAVKNISADTFVADAASVPPSGFWAPSSLLPRLSSLDPGAGMAFASGRFYCMSSSPFAVLVFDVAENVWSKVQPPMRRFLRSPALVELGGGREGAARVALVSAVEKSRLSVPRSVRLWTLRGGGGGGGGGAWTEVARMPPEVHAQFAAAEGGRGFECAAHGDYVVLAPRGPVAQAPTSALVFDSRRDEWRWAPPCPYVVVAHHGGAGAAGFRVFAYEPRLATPAIGLLDATAPVALHGMHDG", "text": "FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Together with FL/APO2, involved in the temporal regulation of meristem identity during both vegetative and reproductive developments in an APO2- dependent manner (By similarity). Promotes spikelet formation by suppressing the precocious conversion of inflorescence meristems to spikelet meristems, probably via a positive regulation of class-C floral homeotic genes, but not of class-B genes, and through the control of cell proliferation in meristems (PubMed:21119645). Mediates culm development and strength/diameter enhancement at internodes (PubMed:21119645). Required for the regulation of the plastochron, floral organ identity, and floral determinacy (By similarity). Controls the number of primary rachis branches (PRBs) (PubMed:20151298). May trigger the formation of vascular bundle systems which, consequently, promote carbohydrate translocation to panicles (PubMed:20151298). Involved in ozone-induced grain yield regulation (PubMed:25923431). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MGRVIFVSFGLLVVFLSLSGTAADCPSEWSSYEGHCYKAFKQSKTWADAEKFCTQQHKGSHLASFHSSEEADFVVTLTTPSLKTDLVWIGLKNIWNGCYWKWSDGTKLDYKDWREQFECLVSRTVNNEWLSMDCGTTYSFVCKFQA", "text": "FUNCTION: Agglucetin specifically causes platelet aggregation and surface exposure of integrin alpha-IIb/beta-3 with a GPIb-(GP1BA-) dependent manner in washed platelets. It binds to human platelets in a saturable manner, and its binding is specifically blocked by anti-GP Ib mAb. It regulates endothelial cell survival and promotes angiogenesis by activating integrin alpha-v/beta-3 signaling through FAK/phosphatidylinositol 3-kinase (PI3K)/Akt pathway. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
{"protein": "MALDFLAGCAGGVAGVIVGHPFDIVKVRLQVQSTEKPQYRGTLHCFQSIIKQESVLGLYKGLGSPLMGLTFINALVFGVQGNTLRALGQDSPLNQFLAGAAAGAIQCVICCPMELAKTRLQLQAVGPARTYKGSLDCLVQIYRHEGLRGINRGMVSTLLRETPSFGVYFLTYDVMTRAMGCEPGDRLLVPKLLLAGGTSGITSWLSTYPMDVVKSRLQADGLQGTPRYRGIVDCMRQSYQAEGWQVFTRGLASTLLRAFPVNAATFATVTVVLTYTRGEEAQVDSEAALGTSPTPAGSALAQPSSL", "text": "FUNCTION: Mitochondrial transporter of arginine, lysine, homoarginine, methylarginine (By similarity). Transports with a much lesser extent, ornithine and histidine (PubMed:19287344). Does not transport carnitine nor acylcarnitines. Functions by both counter-exchange and uniport mechanisms. Plays a physiolocical role in the import of basic amino acids into mitochondria for mitochondrial protein synthesis and amino acid degradation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MTWLLLCLLAQYENGGKVLALSSSAKPYKTSVRFDPKTAHPNLVVSQDKKTVTWVQEAQSVPDNPERFNSTPCLLGSPGFTSGKHYWEVEYGNQRELAAGVARKSVKRKDHLRLT", "text": "FUNCTION: Neurotoxin that produces dose-dependent hypolocomotion and hyperalgesia in mice. May directly act on the central nervous system, as it is 6500-fold more potent when administered intracerebroventricularly than intraperitoneal. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ohanin/vespryn family."}
{"protein": "MFGCLVAGRLVQTDAQQVASDKFVFNLPDYEHVNHVVVFLLGTVPFPEGLGGAVYLCVPGGAAGQVWQLLGFITNEKPSAIFRISGLKAGEGSSHPFGMMDAPAAPSMAQVGVSVEGLHLLAQQTPVSSSAVSTLDSFTQFTQKMLDSLFNFTSSFALSQSQMSPNPSEMFIPASSIRRWYENFQRRLMQNPNFWKT", "text": "FUNCTION: Acts as a specific nuclear import carrier for hsp70 proteins following heat-shock stress: acts by mediating the nucleoporin- dependent translocation of ATP-bound hsp70 proteins into the nucleus. hsp70 proteins import is required to protect cells from heat shock damages (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the OPI10 family."}
{"protein": "MKIITCYKCVPDEQDIAVNNADGSLDFSKADAKISQYDLNAIEAACQLKQQAAEAQVTALSVGGKALTNAKGRKDVLSRGPDELIVVIDDQFERALPQQTATALAAAAQKAGFDLILCGDGSSDLYAQQVGLLVGEILNIPAVNGVSKIISLTADTLTVERELEDETETLSIPLPAVVAVSTDINSPQIPSMKAILGAAKKPVQVWSAADIGFNAEAAWSEQQVAAPKQRERQRIVIEGDGEEQIAAFAENLRKVI", "text": "FUNCTION: Required for anaerobic carnitine reduction. May bring reductant to CaiA. SIMILARITY: Belongs to the ETF beta-subunit/FixA family."}
{"protein": "MGSPSLTKTINASLSLHSITQPITLLKTMHYVLQLTILPSAMQHYATLRNFTHPACSVNKQAEQGKEQQQYAMKSQFQFRSGICSKVRSDELGFKGNSLQLNDLPKNPY", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MSTENGKSADAPVAAPAAKELTSKDYYFDSYAHFGIHEEMLKDEVRTTTYRNSIYHNSHLFKDKVVMDVGSGTGILSMFAAKAGAKKVFAMEFSNMALTSRKIIADNNLDHIVEVIQAKVEDVHELPGGIEKVDIIISEWMGYCLFYESMLNTVLVARDRWLAPNGMLFPDKARLYVCAIEDRQYKEDKIHWWDSVYGFNMSAIKNVAIKEPLVDIVDNAQVNTNNCLLKDVDLYTVKIEDLTFKSDFKLRCTRSDYIQAFVTFFTVEFSKCHKKTGFSTGPDVQYTHWKQTVFYLKDALTVKKGEEITGSFEMAPNKNNERDLDINISFDFKGEVCDLNEQNTYTMH", "text": "FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins (PubMed:21531333, PubMed:24140420, PubMed:27994012, PubMed:28158808). Catalyzes the formation of monomethylarginine and asymmetric dimethylarginine on histones H2A and H4, a specific tag for epigenetic transcriptional activation (PubMed:21531333). Catalyzes asymmetric arginine dimethylation of mitochondrial proteins necessary for mitochondrial oxidative phosphorylation activity and thus aerobic respiration and ATP synthesis, and the mitochondrial stress response (PubMed:27994012). Methylates arginine residues in P-granule components pgl-1 and pgl-3 to promote P-granule degradation by autophagy in somatic cells to ensure exclusive localization of the P-granules in germ cells (PubMed:24140420). Modulates the interaction of P-granule proteins epg- 2 and sepa-1 (PubMed:24140420). Methylates arginine residues in daf-16, which blocks ftt-2 binding to daf-16, prevents akt-mediated phosphorylation and allows for daf-16 to translocate to the nucleus (PubMed:21531333). In turn, association with daf-16 therefore allows for the transcriptional activation of daf-16 and regulation of longevity-related genes (PubMed:21531333). Maintains lifespan by modulating daf-16 activity downstream of the daf-2 signaling pathway (PubMed:21531333, PubMed:28158808). Plays a role in heat and oxidative stress resistance (PubMed:21531333, PubMed:28158808). Role in stress resistance and also fat storage may be in association with the daf-2 signaling pathway (PubMed:21531333). Required for normal feeding behavior (PubMed:27994012). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Diffuse cytoplasmic localization during embryogenesis. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family."}
{"protein": "MVDQNPKRSGEPPVWLMFGAGGTVSAIFLPVVILIIGLLLPFGLVDAHNLITFAYSWIGKLVILVLTIFPMWCGLHRIHHGMHDLKVHVPAGGFIFYGLATIYTVWVLFAVINL", "text": "FUNCTION: Anchors the catalytic components of the fumarate reductase complex to the cell membrane, binds quinones. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FrdD family."}
{"protein": "MCGLAGIINLAAPRSQECTFHILKGMADAISYRGPDDEQYHIDSKVGFAFRRLSILDLVNGQQPFLNEDGSIVVMVNGEIYNYKELKASLHNHMFKTTSDCEVIVHLYEEKGIGFVDDIIGMFSIAIWDKNKNKVFLVRDRFGIKPLFYTELKHELIFASEIKSLFSHPHCPRQFNWKEALSDIWLSGEAASNHKETTSFFVNIQNLDAGHYLEINLTTNERKTASYWSLQDILLRQGYRENLHPDDLIEGYRELLADSVHRCLQSDVEVGLFLSGGIDSAAVAHFAAEKQDLHTFTVLSQSTFTNEDAKYAHWLAKDLHLPNHQVLYQLGNDELLQPESYKHLLWICETPFCGPEQLYKFHLHKYAKAIRPNLKVMLTGQGSDEFNGGYSTTLSPAENPSWEGFIESVNTMEMNRLHRLQGNIFRVWEEHFGLSPINLSYLKSNDSSQADPWQSYVLTKYRDLQMYNCWHEDRIAAANHIENRVPFLDHRLVEWVCGIPDGLRKDLLWDKSVLRKSLTNELHTSYTHRPKVPFFYGKDVRYTHKMMFHLLKKNNYQLIEEAFSHSDASSIIQVEHIHAIMTYLEDDPEFTNFEFLLRLVNMGLLSKMTKETPSVQLDITSHLESITIKDWHSQEGDIASRLNISANKCEGQDILALNPGVTLLRPESDSEHCIYIAEEGFIQFIVSEEDVGAWLHILCDINGKDTLHTILDRHGVSLEEVAKYIQEAIEHNIILIKQKNLPEGAYR", "text": "SIMILARITY: Belongs to the asparagine synthetase family."}
{"protein": "MDPTLISLGALALAGAAATVSGCAEDLESDVGSQSNPNSQVQLGPQMGNIHRYFNKAISGEPVSYGLYVAVAGTIAWALINAGLNAVLAIIVGSGVAAVVHGAYSVSAFLGRTVGQSKKFGQPVYMDVLTSHIGPIVGHGFIAVFTMTLAAYLATTALGNPFPLPLVALIFGITVGAIGSSTGDVHYGAEREYQKYPFGGGIPVANQGDIDIYAEYGVRNGLDSSYFCSRFGGPLTGLCFGLIIFLDGWRSILGNIIGGDLVTKTSIALLVGLLVVAVAAGINRKLEVYARNKYGPYRN", "text": "FUNCTION: Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MtrE family."}
{"protein": "MSLTYKPKMQHEDMQDLSSQIRFVAAEGKIWLGEQRMLVMQLSTLASFRREIISLIGVERAKGFFLRLGYQSGLMDAELARKLRPAMREEEVFLAGPQLYALKGMVKVRLLTMDIAIRDGRFNVEAEWIDSFEVDICRTELGLMNEPVCWTVLGYASGYGSAFMGRRIIFQETSCRGCGDDKCLIVGKTAEEWGDVSSFEAYFKSDPIVDERYELQTQVANLRNRLKQYDGQYYGIGHSPAYKRICETIDKAARGRVSVLLLGETGVGKEVIARSVHLRSERAEQPFVAVNCAAIPPDLIESELFGVDKGAYTGAVNARAGRFERANGGTIFLDEVIELTPRAQATLLRVLQEGELERVGGDRTRKVDVRLITATNENLEEAVKMGRFRADLFFRLNVFPVHIPPLRERVEDIPLLVEHFLRRHHKEYGKKTLGLSDRAMEACLHYQWPGNIRELENALERGVILTESNESINVESLFPGLATATEGDRLSSEGRLEEESGDSWFRQIIDQGVSLEDLEAGLMRTAMDRCGQNISQAARLLGLTRPAMAYRLKKLDPSLSVKAMGR", "text": "FUNCTION: Regulatory protein of the TOL plasmid xyl operons. In the presence of m-xylene or m-methylbenzyl alcohol XylR activates both the xylCMABN operon and the regulatory gene xylS; xylS itself activates the xylXYZLTEGFJQKIH operon. XylR interacts with sigma-54."}
{"protein": "MATSSSDRWPIPLKQHIPTLIFITVTVLTSNLVSRTQPTAYLDEIFHIPQAQQFCSALSSTSLFSAQQVWRQLTSVRYDAQLTTPPGMYAISVGMAKVLPGWECKDVVWLRSTNLVLLLTLPVLVARILGQIEEQARIASAAEDYSPSKTITQNLGKEITRHEIEMLQAKAKLQLPPTPSASHDDLAHIEPPTISIAQAALPAPTGSAAPLLRALKQREASAYTMALACTICFLPPLWFFGFLYYTDLASTWLVLAMLSLYNDLNTSNAHVAPTITGLLIALTSILAVAVRQTNIVWIGFAAAQATLSRVGKHVSHTQQGSDPVTQAIGMVKGAFGDNKKGWWTAVAINAAPMVPVLAVCVLFLRWNGSIVLGEKAAHQVALHLPQMGYFVAFALGFGLFPLLFSLQSMSHKAQDQGPSSSTLATFTHSVRSAVSALIDSTIASPGCILALAAALAGFYIAVDRFTIEHAYMLADNRHYTFYIWRKYRSSYAIPALDGMTIEPKLAVVPLFALALIAWSRALTHHAVNKRTGALFSLLFWMATAAVLVPTPLIEPRYFLMAYLLLRIYSHPYAPCEKQEKSAQLKWIYLALEAATYAAVNVITVGLFVNRPFQWPSHAVDVSRNEHTTMRFLW", "text": "FUNCTION: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ALG10 glucosyltransferase family."}
{"protein": "MIHFKGLIFYHYSAGDDVAIHTQDMAWLEESDVVVAEVTQPSLGVGYEIGRAVAWKKRILCLYRPDDGKGLSAMVRGAHDGKNFIVKDYQEPEVPGILKEFLSSS", "text": "FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family."}
{"protein": "MKLKKKFLEKSKKIAEERIDVLMNLAEKESKAGKIDRSKNYVLLGKKIAMRMRMPYPKEWKRRICKNCGSFLIYGKNARVRTKAKNYPHVVITCLECNSITRIPIKSEKK", "text": "FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 4 family."}
{"protein": "MPGGPGAPSSPAASSGSSRAAPSGIAACPLSPPPLARGSPQASGPRRGASVPQKLAETLSSQYGLNVFVAGLLFLLAWAVHATGVGKSDLLCVLTALMLLQLLWMLWYVGRSYMQRRLIRPKDTHAGARWLRGSITLFAFITVVLGCLKVAYFIGFSECLSATEGVFPVTHAVHTLLQVYFLWGHAKDIIMSFKTLERFGVIHSVFTNLLLWANSVLNESKHQLNEHKERLITLGFGNITIVLDDHTPQCNCTPPALCSALSHGIYYLYPFNIEYQILASTMLYVLWKNIGRRVDSSQHQKMQCRFDGVLVGSVLGLTVLAATIAVVVVYMIHIGRSKSKSESALIMFYLYAITVLLLMGAAGLVGSWIYRVDEKSLDESKNPARKLDVDLLVATGSGSWLLSWGSILAIACAETRPPYTWYNLPYSVLVIVEKYVQNIFIIESVHLEPEGVPEDVRTLRVVTVCSSEAAALAASTLGSQGMAQDGSPAVNGNLCLQQRCGKEDQESGWEGATGTTRCLDFLQGGMKRRLLRNITAFLFLCNISLWIPPAFGCRPEYDNGLEEIVFGFEPWIIVVNLAMPFSIFYRMHAAAALFEVYCKI", "text": "FUNCTION: Proton-selective channel that specifically transports protons into cells (PubMed:29371428). Proton channel activity is only weakly- sensitive to voltage (PubMed:29371428). Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes (PubMed:29371428). In the vestibular system of the inner ear, required for the formation and function of otoconia, which are calcium carbonate crystals that sense gravity and acceleration (PubMed:12651873). Probably acts by maintaining the pH appropriate for formation of otoconia (PubMed:29371428). Regulates purinergic control of intracellular calcium in vestibular supporting cells (PubMed:17606897, PubMed:20554841). May be involved in sour taste perception in sour taste cells by mediating entry of protons within the cytosol (PubMed:29371428). Also involved in energy metabolism, by reducing adipose tissue inflammation and protecting from obesity- induced metabolic dysfunction (PubMed:24379350). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Detected in the gelatinous membrane overlying the inner ear macular epithelium. SIMILARITY: Belongs to the otopetrin family."}
{"protein": "MESKEELAANNLNGENAQQENEGGEQAPTQNEEESRHLGGGEGQKPGGNIRRGRVRRLVPNFRWAIPNRHIEHNEARDDVERFVGQMMEIKRKTREQQMRHYMRFQTPEPDNHYDFCLIP", "text": "FUNCTION: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole Nucleus Cytoplasm Note=Also localizes to microtubules. SIMILARITY: Belongs to the BEX family."}
{"protein": "MKQALRVAFGFLILWASVLHAEVRIVIDSGVDSGRPIGVVPFQWVGPGAAPEDIGGIVAADLRNSGKFNPLDRARLPQQPGSAQEVQPAAWSALGIDAVVVGQVTPNPDGSYNVAYQLVDTGGAPGTVLAQNSYKVNKQWLRYAGHTASDEVFEKLTGIKGAFRTRIAYVVQTNGGQFPYELRVSDYDGYNQFVVHRSPQPLMSPAWSPDGSKLAYVTFESGRSALVIQTLANGAVRQVASFPRHNGAPAFSPDGSKLAFALSKTGSLNLYVMDLASGQIRQVTDGRSNNTEPTWFPDSQNLAFTSDQAGRPQVYKVNINGGAPQRITWEGSQNQDADVSSDGKFMVMVSSNGGQQHIAKQDLATGGVQVLSSTFLDETPSLAPNGTMVIYSSSQGMGSVLNLVSTDGRFKARLPATDGQVKFPAWSPYL", "text": "FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the TolB family."}
{"protein": "MKYGYFDNDNREYVITRPDVPAPWTNYLGTEKFCTVISHNAGGYSFYHSPEYNRVTKFRPNFTQDRPGHYIYLRDDETGDFWSVSWQPVAKNLDDAHYEVRHGLSYSKFRCDYNGIVATKTLFVPKGEDAQVWDVEIENTSDQPRTISAFGYVEFSFSHIASDNQNHQMSLYSAGTEYNNGVLEYDLYYNTDDFLGFYYLTATFDADSYDGQRDAFLGMYRDEANPIAVANGRCSNSAQTCYNHCGALHKQFVLQPGEKVRFAVILGVGKGNGEKLRAKYQDLSQVDAAFAGIKQHWDERCAKFQVRSPNQGLDTMINAWTLYQAETCVVWSRFASFIEVGGRTGLGYRDTAQDAISVPHTNPAMTRKRLVDLLRGQVKAGYGLHLFDPDWFDPEKADVKPSKSPTVVPTPSDEDKIHGIKDTCSDDHLWIVPTILNFVKETGDLSFIDEVIPYADGGDATVYQHMMAALDFSAEYVGQTGICKGLRADWNDCLNLGGGESAMVSFLHFWALEAFLELARHRQDAAAIDKYQAMANGVREACETHLWDDNGGWYIRGLTKDGDKIGTFEQQEGKVHLESNTLAVLSGAVSQQRGEKAMDAVYEYLFSPYGLHLNAPSFATPNDDIGFVTRVYQGVKENGAIFSHPNPWAWVAEAKLGRGDRAMEFYDSLNPYNQNDIIETRVAEPYSYVQFIMGRDHQDHGRANHPWLTGTSGWAYYATTNFILGVRTGFDTLTVDPCIPAAWSGFEVTREWRGATYHISVQNPNGVSKGVQSILVNGEAVDAINAQPAGSENQVTVILG", "text": "FUNCTION: Catalyzes the reversible phosphorolysis of chitobiose (N,N'- diacetylchitobiose or (GlcNAc)(2)) into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. SIMILARITY: Belongs to the glycosyl hydrolase 94 family."}
{"protein": "GWTLNSAGYLLGPHAIDNHRSFNDKHGLA", "text": "FUNCTION: Contracts smooth muscle of the gastrointestinal and genitourinary tract, regulates growth hormone release, modulates insulin release, and may be involved in the control of adrenal secretion. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the galanin family."}
{"protein": "ARRRRRSSRPQRRRRRRRHGRRRRGRR", "text": "FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. SUBCELLULAR LOCATION: Nucleus. Chromosome."}
{"protein": "MIPGNRMLMVVLLCQVLLGGASHASLIPETGKKKVAEIQGHAGGRRSGQSHELLRDFEATLLQMFGLRRRPQPSKSAVIPDYMRDLYRLQSGEEEEEEQSQGTGLEYPERPASRANTVRSFHHEEHLENIPGTSESSAFRFLFNLSSIPENEVISSAELRLFREQVDQGPDWEQGFHRINIYEVMKPPAEMVPGHLITRLLDTRLVHHNVTRWETFDVSPAVLRWTREKQPNYGLAIEVTHLHQTRTHQGQHVRISRSLPQGSGDWAQLRPLLVTFGHDGRGHTLTRRRAKRSPKHHPQRSRKKNKNCRRHSLYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHLNSTNHAIVQTLVNSVNSSIPKACCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR", "text": "FUNCTION: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis (PubMed:14973287, PubMed:15206957, PubMed:10049358). Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction (PubMed:17301089). Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical BMP pathways such as ERK/MAP kinase, PI3K/Akt or SRC cascades. For example, induces SRC phosphorylation which, in turn, activates VEGFR2, leading to an angiogenic response (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQGPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEVVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDISTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGPTRMEGNLPAKLRKMNSDRFT", "text": "FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ3 subfamily."}
{"protein": "MDLLVMLLSLLVSYLIFKIWKRIDSKRDQNCYILDYQCHKPSDDRMVNTQFSGDIILRNKHLRLNEYKFLLKAIVSSGIGEQTYAPRLFFEGREQRPTLQDGLSEMEEFYIDTIEKVLKRNKISPSEIDILVVNVSMLNSTPSLSARIINHYKMREDIKVFNLTAMGCSASVISIDIVKNIFKTYKNKLALVVTSESLSPNWYSGNNRSMILANCLFRSGGCAVLLTNKRSLSRRAMFKLRCLVRTHHGARDDSFNACVQKEDELGHIGVHLDKTLPKAATRAFIDNLKVITPKILPVTELLRFMLCLLLKKLRSSPSKGSTNVTQAAPKAGVKAGINFKTGIDHFCIHTGGKAVIDAIGYSLDLNEYDLEPARMTLHRFGNTSASSLWYVLGYMEAKKRLKRGDRVFMISFGAGFKCNSCVWEVVRDLNVGEAVGNVWNHCINQYPPKSILNPFFEKYGWIHEEEDPDTFKMPEGFM", "text": "SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family."}
{"protein": "APPGFTPFRS", "text": "FUNCTION: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle (By similarity). May target bradykinin receptors (BDKRB). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-related peptide family."}
{"protein": "MKKTFVKILSKSYVEGYPVGFFIGLIILAIFGSMVCIFSFMHYSEEENSNIQMDLERSSKQIIHNIQMNAMYLLSSIDTLKALYYVNPNFDRNDFNVFLNTTLKNSEFQYLFWIKKINNNDRNCFEEKFSKEIKDTFQIYSFDENTNSIHVAKNKSSYFPILHAFPDINKDIIGLDINSTDYMNETIKKSIFNKKPTVHLNKKVLLSKRNIDILIVSPIIVTKTLESTNETMEDMSHISSGLFLMEKNVQASRIEVENGNDFTIFLSTTNGEIVYQENYLNFKTLYQVHESGLFEDRLKYESSLKIADCVLKLWIFTTEEYENNSKTYLPLLVSIISAVILVLLITYSVDQRKQKSLIAKIMREKNNLINKILPLEVSVKLENGEDVVAERSNNACVFFLDIAGFTRFSSIHSPEQVIQVLIKIFNSMDLLCAKHGIEKIKTIGDAYMATCGIFPKCDDIRHNTYKMLGFAMDVLEFIPKEMSFHLGLQVRVGIHCGPVISGVISGYAKPHFDVWGDTVNVASRMESTGIAGQIHVSDRVYQLGKEDFNFSERCDIIHVKGKGRMKTWYLMGKKSSDFSLKKDFSRSRVQPSLFNRKQSHVHCIYPEFPSGLQALNIENNLNNTDAGCENCSKILKKTYAYSPDHSTSNYYYHGDDNSPPPPSLNSNDLIDGSEYHDDPFPSDSNVGYHDTSKDIKEDENEQNETLLFNQEQLKKKQIENIQRDLSLNDSIEAIKILNNNNNNNINDNNINNTNLNNNNNDININNSDNVNNYENNNNFSDKIENNDGDNNNINDNNYKSTNENNIKSKTLFKDSKSLINDIKMAKENCDNNDDNNNNNNNNNNNNNNDENVESKKNK", "text": "FUNCTION: Has a large extracellular domain which may be involved in the recognition of an extracellular signal present during germination, leading to activation or inhibition of cAMP synthesis by the cytoplasmic domain. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family."}
{"protein": "MRKFNLTALSVMLALGLTACQPPEAEKAAPAASGEAQTANEGGSVSIAVNDNACEPMELTVPSGQVVFNIKNNSGRKLEWEILKGVMVVDERENIAPGLSDKMTVTLLPGEYEMTCGLLTNPRGKLVVTDSGFKDTANEADLEKLSQPLADYKAYVQGEVKELVAKTKTFTEAVKAGDIEKAKSLFADTRVHYERIEPIAELFSELDPVIDAREDDFKDGAKDAGFTGFHRIEYALWVEKDVSGVKEIAAKLMTDVEALQKEIDALAFPPGKVVGGASELIEEVAGSKISGEEDRYSHTDLSDFQANVDGSKKIVDLFRPLIEAKNKALLEKTDTNFKQVNEILAKYRTKDGFETYDKLGEADRKALQASINALAEDLAQLRGILGLK", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the EfeM/EfeO family."}
{"protein": "MLTVKGLNKSFGENEILKKIDMKIEKGKVIAILGPSGSGKTTLLRCLNALEIPNRGELAFDDFSIDFSKKVKQADILKLRRKSGMVFQAYHLFPHRTALENVMEGPVQVQKRNKEEVRKEAIQLLDKVGLKDKMDLYPFQLSGGQQQRVGIARALAIQPELMLFDEPTSALDPELVGEVLKVIKDLANEGWTMVVVTHEIKFAQEVADEVIFIDGGVIVEQGPPEQIFSAPKEERTQRFLNRILNPL", "text": "FUNCTION: Part of the ABC transporter complex TcyABC involved in L- cystine import. Responsible for energy coupling to the transport system (Probable). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.14) family."}
{"protein": "MSGASSEDSSIFARCEDVDCNKKIPVELVRMHICYAMFHRTLAARGFGTQTQAKKKPTNKKKSTTSLTDFAVFMNHFRKSFRTDYNGALVKEGSKIGWEMWKSMTEDEKKDYLDKAADEEDEDEDTVEEQADDSDDAEDNEVKETDDDN", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMGB family."}
{"protein": "MSRLIIVFIVVTMICAATALSSKKSINEDEKDEKRSVAVAGAVIEGATLTFNVLQTVLKALGDISRKIAVGIDNESGMTWTAMNTYFRSGTSDVILPHTVPHGKALLYNGQKDRGPVATGVVGVLAYAMSDGNTLAVLFSIPFDYNLYSNWWNVKVYKGHRRADQRMYEELYYNLSPFRGDNGWHNRDLGYGLKGRGFMNSSGQSILEIHVTKA", "text": "FUNCTION: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cytolysis. Pore formation is a multi- step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. SUBCELLULAR LOCATION: Secreted Nematocyst Target cell membrane Note=Forms an alpha-helical membrane channel in the prey. SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily."}
{"protein": "MKFLKRGVALALLAAFALTTQPAQAYEKDKTYKITILHTNDHHGHFWRSEYGEYGLAAQKTLVDSIRKEVAQEGGGVLLLSGGDINTGVPESDLQDAEPDFRGMNLIGYDAMAVGNHEFDNPLTVLRQQEKWAKFPFLSANIYQKSTGERLFKPWAIFTRQDIKIAVIGLTTDDTAKIGNPEYFTDIEFRKPAEEAKVVIQELNMNEKPDVIIATTHMGHYDNGDHGSNAPGDVEMARSLPAGSLAMIVGGHSQDPVCMASENKKQVNYVPGTPCAPDKQNGIWIVQAHEWGKYVGRADFEFRNGEMKMVNYQLIPVNLKKKVTWDNGKSERVLYTPEIAENPQMLLLLTPFQNKGKVQLEVKIGSVNGLLEGDRSKVRFVQTNMGRVILAAQIARTGADFGVMSGGGIRDSIEAGDITYKSVLKVQPFGNIVVYADMSGKEVVDYLTRVAQMKPDSGAYPQLANVSFVAKEGKLTDLKIKGEPVDPAKTYRMATLSFNATGGDGYPRIDNKPGYVNTGFIDAEVLKEFIQQNSPLDAAAFTPKGEVSWL", "text": "FUNCTION: Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the 5'-nucleotidase family."}
{"protein": "MASELAMSSSDLPTSPLAMEYVNDFDLMKFEVKKEPVETDRIISQCGRLIAGGSLSSTPMSTPCSSVPPSPSFSAPSPGSGSEQKSHLEDYYWMSAYPQQINPEALGFSPEDAVEALISNSNQQQQQQQQQQLQAGYDGFARGQQYASSGGMPGEDMGSAAAVVSAVIAAAAAQNPHHHHHHHHHSVGHQAGVQPPGGGTGGGGSSGSSTSSSVVGALHPPAAHHHHHHHHLHFDDRFSDEQLVTMSVRELNRQLRGVSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHVLESEKNQLLQQVEHLKQEISRLLRERDAYKEKYEKLLGSGFRENGSSNSDNPSSPEYFMS", "text": "FUNCTION: Acts as a transcriptional activator or repressor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Maf subfamily."}
{"protein": "MQAFLKGTSISTKPPLTKDRGVAASAGSSGENKKAKPVPWVEKYRPKCVDEVAFQEEVVAVLKKSLEGADLPNLLFYGPPGTGKTSTILAAARELFGPELFRLRVLELNASDERGIQVVREKVKNFAQLTVSGSRSDGKPCPPFKIVILDEADSMTSAAQAALRRTMEKESKTTRFCLICNYVSRIIEPLTSRCSKFRFKPLSDKIQQQRLLDIAKKENVKISDEGIAYLVKVSEGDLRKAITFLQSATRLTGGKEITEKVITDIAGVIPAEKIDGVFAACQSGSFDKLEAVVKDLIDEGHAATQLVNQLHDVVVENNLSDKQKSIITEKLAEVDKCLADGADEHLQLISLCATVMQQLSQNC", "text": "FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the activator 1 small subunits family."}
{"protein": "MKTTYVNATIVTMNEQNEVIENGYIIVENDQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKDDEKKAIEEAEKYVKRYYKESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNENERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGMKVGIATDSVASNNNLDMFEEMRIATLLQKGIHQDATALPVETALTLATKGAAEVIGMKQTGSLEVGKCADFITIDPSNKPHLQPADEVLSHLVYAASGKDISDVIINGKRVVWNGECKTLDEERIIFEASRYKRGLQR", "text": "FUNCTION: Catalyzes the deamination of 5-methylthioadenosine and S- adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L- homocysteine, respectively. Is also able to deaminate adenosine. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family."}
{"protein": "DRICTGITSSNSPHVVKTATQGEVNVTGVIPLTTTPTKSHFANLKGTKTRGKLCPKCLNCTDLDVALGRPKCMGTIPSAKASILHEVKPVTSGCFPIMHDRTKXRQLPNLLRGYENIRLSTHNVINAETAPGGPYIVGTSGSCPNVTNGNGFFATMAWAVPKNNNNKTATNPLTVEVPFICTKGEDQITVWGFHSDDETQMVKLYGDSKPQKFTSSANGVTTHYVSQIGGFPNQAEDGGLPQSGRIVVDYMVQKSGKTGTITYQRGILLPQKVWCASGRSKVIKGSLPLIGEADCLHEKYGGLNKSKPYYTGEHAKAIGNCPIWVKTPLKLANGTKYRPPAKLLKER", "text": "FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host apical cell membrane; Single-pass type I membrane protein. Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. SIMILARITY: Belongs to the influenza viruses hemagglutinin family."}
{"protein": "MKRVQTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLVFREAGSIPEELHKEVPEAFLTLHKHGCLFRDLVRIQGKDVLTPVSRILIGDPGCTYKYLNTRLFTVPWPVKGCTINYTEAEIAAACQTFLKLNDYLQVETIQALEELAIKEKANEDAVPLCMAEFPRAGVGPSCDDEVDLKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGSEDESDDESSFEGRDPDTWHVGFKISWDIETPGLTIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVLNDSDNGDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYKICTDWWCEPMTQLEGLWKKMESVTNAVLREVKREGLSVEQRSEILSAVLIPLTMRQNLRKEWHARCQARVVRTLPAQQKPDCRPYWEKDDPSMPLPFDLTDVVSEIRSQLLEARS", "text": "FUNCTION: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. M6A demethylation by FTO affects mRNA expression and stability. Also able to demethylate m6A in U6 small nuclear RNA (snRNA). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA. Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping. Also acts as a tRNA demethylase by removing N(1)- methyladenine from various tRNAs. Has no activity towards 1- methylguanine. Has no detectable activity towards double-stranded DNA. Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single- stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3- methylcytosine. Ability to repair alkylated DNA and RNA is however unsure in vivo. Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation. Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (By similarity). Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Localizes mainly in the nucleus, where it is able to demethylate N(6)-methyladenosine (m6A) and N(6),2'- O-dimethyladenosine cap (m6A(m)) in U6 small nuclear RNA (snRNA), N(1)- methyladenine from tRNAs and internal m6A in mRNAs. In the cytoplasm, mediates demethylation of m6A and m6A(m) in mRNAs and N(1)- methyladenine from tRNAs. SIMILARITY: Belongs to the fto family."}
{"protein": "MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADEMNEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNVRINLQKEI", "text": "FUNCTION: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1- mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein Membrane, caveola; Peripheral membrane protein Membrane raft Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). SIMILARITY: Belongs to the caveolin family."}
{"protein": "MASTRIREARESDCGDIMRMIRELAEFEKLSHQVKISEEALRADGFGENPFFHCLVAEIIPAPGESQGSLVVGYGLYYFIYSTWTGRNVYLEDIYVMPQYRGQGIGTKIIKKVAEVALNKGCSQFRLAVLDWNKKAVNLYKFLGAQDLTESEGWLSFRFEGEAMRELAGR", "text": "FUNCTION: Catalyzes the N-acetylation of the amino acid thialysine (S- (2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene group substituted with a sulfur. May also catalyze acetylation of polyamines, such as norspermidine, spermidine or spermine. However, ability to acetylate polyamines is weak, suggesting that it does not act as a diamine acetyltransferase in vivo. SUBCELLULAR LOCATION: Cytoplasm Note=Intracellular organelles. SIMILARITY: Belongs to the acetyltransferase family."}
{"protein": "MEPIDPNLEPWNHPGSQPKTACNNCYCKQCCYHCQLCFTKKGLGISYGRRKRKQRRRTSESSQNHQDPVPKQPLSQPGGIETGQKKSKKEVESQTTSDQFA", "text": "FUNCTION: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. SUBCELLULAR LOCATION: Host nucleus, host nucleolus Host cytoplasm Secreted Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. SIMILARITY: Belongs to the lentiviruses Tat family."}
{"protein": "MGCCCCLPSIPESSRTIDEHLPLSRATPSSLSNAYSSPLSPPIPLAITNINLQTSPPKLPRTQGNSSEASPGLTQVVPEKKTWHVDDLTDFELKKQYREAIDECPICLEEYEIDNPKLLTKCGHDFHLACILAWMERSEACPVCDKELVLTES", "text": "FUNCTION: Possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E2 enzyme UBC8 in vitro (PubMed:20884812, PubMed:15644464). Plays combinatory roles with AIRP2 in the positive regulation of the abscisic acid-mediated drought stress response (PubMed:20884812). SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
{"protein": "MKHVFSGFQTFLKQVHSPIYLALAVVIFSAANPVTSRIIELGKTYEINGRNPISFCNVLFVGNLCALGLMILIFHPDWQLHKLRKLTRKDWFLLTVTAILSRAIAPGLMFSALEKTNVTNVVLIGRLEPVFTLILSILLLKISVNWLSMVATLISFVGVAVTVFWGVADPLDMVINFDFGLGESFVAIAAFISAITTILSKQQLQSIPVGIFTVYRSLLGTFVFFWIAVIIYGFDHFMDVSSPILWRWMLIYGAIIVVVGQVAWLAGLKNASFIQINLASLVTPILAIIFAYLILLETPTNAQYLGGILLLLGAILSFIDNLKTAKDKQASKPLNSREAMDTNVGFRGV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EamA transporter family."}
{"protein": "MSSESPNLPAAAGTVPDNHPPPPPVVTAAEAGSDDSPKGVASKLSAAGISNWAKNLKVPQPFASTQNDSGVENTEKSAFAKFTSGLGIRLSPKSPQTNDTTTEGTSSATESSFIGTITKGLVDTSKNAVKAVQVKARHAVSQNKRRYQEGGFDLDLTYITENIIAMGFPAGDMSSGFFGYVEGFYRNQMEEVINFLETQHKGKYKVYNLCSERLYDVSLFEGKVASFPFDDHNCPPIHLVTSFCQSAYSWLKEDIENVVVVHCKAGMARTGLMICSLLLYLKFFPTAEECMDFYNQKRCVDGKGLVLPSQIRYVKYFERILTYFNGENQPGRRCMLRGFRLHRCPYWIRPSITISDHNGVLFTTKKHPRTKDLSPEDFWFSAPKKGVMVFALPGEPGLTELAGDFKIQFHDRQGDFYCWLNTTMMENRVILKTSELDGFDKRKLPSPGFMVEVVLADINATIPTNPSSETASKTPEETSAANSSPVDGSASVPGPDKETENPDKDDVFSDNEGDSTGPTKTTSSASSQTPEAKKSADETAVLTKATEKVSISGNKGSSQPVQGVTVSKGEATEKPSGAGVNASSSSESEFKVMAADASVFSFGDEDDFESD", "text": "FUNCTION: Binds phosphatidic acid. Protein tyrosine phosphatase that exhibits also lipid phosphatase activity. Hydrolyzed poorly p- nitrophenyl phosphate (p-NPP). Can use PtdIns isomers as substrates. Removes efficiently phosphate from the D3 position of the inositol ring, less from the D4 position and not at all from the D5 position on monophosphorylated PtdIns isomers (PIPs). The presence of a phosphate group in the D5 position on PIP(2) isomers reduces lipid phosphatase activity. Mostly active on PtdIns(3)P and PtdIns(3,4)P(2), to a lower extent, on PtdIns(4)P and PtdIns(3,5)P(2), but barely against PtdIns(3,4,5)P(3) as substrate. SIMILARITY: Belongs to the PTEN phosphatase protein family."}
{"protein": "MSKRPGDLACDLERSLPALASLGTSLSHSQSLSSHFIPPPLEKRRAISDVRRTFCLFVTFDLLFISLLWIIELNTNTGIRKNLEQEVIHYSFQSSFFDIFVLAFFRFSGLLLGYAVLRLQHWWVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAAQAAVARGPLLFSGALSEGQFYSPPESFAGSDNESDEEVTGKKSFSAQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGARA", "text": "FUNCTION: Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes (By similarity). Creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB (By similarity). Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes (By similarity). May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane (By similarity). However, such results need additional experimental evidences; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes (By similarity). Does not activate transcriptional cholesterol sensing (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2. SIMILARITY: Belongs to the STARD3 family."}
{"protein": "MSDERYQQRQQKVKDRVDARVAQAQEERGIIIVFTGNGKGKTTAAFGTAARAVGHGKNVGVVQFIKGTWPNGERNLLEPHGVEFQVMATGFTWETQNREADTAACMAVWQHGKRMLADPLLDMVVLDELTYMVAYDYLPLEEVISALNARPGHQTVIITGRGCHRDILDLADTVSELRPVKHAFDAGVKAQMGIDY", "text": "FUNCTION: Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family."}
{"protein": "MTLSSQHYLVITALGADRPGIVNTITRHVSSCGCNIEDSRLAMLGEEFTFIMLLSGSWNAITLIESTLPLKGAELDLLIVMKRTTARPRPPMPASVWVQVDVADSPHLIERFTALFDAHHMNIAELVSRTQPAENERAAQLHIQITAHSPASADAANIEQAFKALCTELNAQGSINVVNYSQHDEQDGVK", "text": "FUNCTION: Negative transcriptional regulator of the glycine cleavage system operon (GCV). Does not autoregulate its own expression. It is not yet known how GcvR acts as a repressor. It does not seem to bind DNA. It could interact with GcvA and suppress its activatory activity. FUNCTION: Possible negative transcriptional regulator of the glycine cleavage system operon (GCV). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGQKRKDLSHAELMMMTIADIIKQLIEAHEQGKDVNLNKLKTKTSAKYGLSAQPRLVDIIAAVPPQHRKALVPKLKAKPIRTASGIAVVAVMCKPHRCPHINFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYLQTRHRVEQLKQLGHSVDKVEFIVMGGTFMALPEDYRDYFIRNLHDALSGHTSNNVAEAVKYSERSLTKCVGITIETRPDYCLKRHLSDMLSYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDAGFKVVAHMMPDLPNMGLERDTDQFVEFFENPAFRPDGMKLYPTLVIRGTGLYELWKTGRYKSYPPSTLVDLVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGTQCRDVRTREVGIQEIHHKVRPYQIELIRRDYVANGGWETFLSYEDPEQDILVGLLRLRKCSEESFRPELKGGVSIVRELHVYGSVVPVSSRDPSKFQHQGFGMLLMEEAERIAKEEHGSWKIAVISGVGTRNYYRKIGYELEGPYMVKRLQ", "text": "FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ELP3 family."}
{"protein": "MTRHIILDCDPGHDDAIALILALAHPDLVPLAVTTSAGNQTPDKTLNNALRILTLLNRGDIPVAGGATKPLTRELIIADNVHGETGLDGPALPEPSFSPQAITAVELMAQQIRQSTQPVTLVPTGPLTNIALLLASHSELHPKIERIVLMGGAAGVGNWTPAAEFNIFVDPEAADIVFKSGIPITMCGLDVTHQAQIMDEDIERIRAIPNPIAQCVAELLDFFMIYHRDPKWGFIGAPLHDPCTIAWLLKPELFEAQDCWVGIETQSELTLGMTVVDRYQLTGKTANATVLFGLDRLGFVDLLVDSLRVYDPTYLNRR", "text": "FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. SIMILARITY: Belongs to the IUNH family. RihA subfamily."}
{"protein": "MFRHVAQNLGSRNTSIQSYRLLRTRWERGYLKDLYHRRQILGADPAISRSSYPNCSVQVRNHHCSADKSTLQWAPIKTSIDNSSDDFAANTAEMKVLVEDLKAKISKIEQAGGEKAVKLHRSRGKMLARERIDGIVDAGSPFIEFSQLAGYEMYGKEEVPSGGILTGVGIVSGRVCVIVANDATVKGGTYYPITVKKHLRAQEIARENKLPCIYLVDSGGANLPRQADIFADSQHFGRIFYNQATMSSEGIPQLAVVMGSCTAGGAYVPAMSDQAIIVKGTGTVFLGGPPLVKAATGEEISAEELGGADLHCGESGVTDYYAHNDKHALYLARSCIAGLPPVEEHMTFNPNADEPLYPAEEIYGIVGSNLKKTYDVREVIARIVDGSRFHEFKERYGETLVTGFATIYGQRVGILANNGVLFAESAMKGSHFIELCCQRKIPLLFLQNITGFMVGRDAEAGGIAKHGAKLVTAVACAKVPKITVLVGGSYGAGNYGMCGRGYSPRYVFMWPNSRISVMGGEQAANVLSTVQKEKKKREGADWTDQQDLELRKPVEEKFEKEGHPYFASARLWDDGVIDPKDTRKVLGLAFQSTLQKPIPETKFGVFRM", "text": "FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3- methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the AccD/PCCB family."}
{"protein": "MGKDPRKPRGKMSSYAYFVQTRREEHKKKHPEASVNFSEFSKKCSERWKTMSAKEKGKFEDLAKLDKVRYEREMRSYIPPKGEKKKRFKDPNAPKRPSSAFFIFCADFRPQVKGETPGLSIGDVAKKLGEKWNNLTAEDKVPYEKKASRLKEKYEKDITAYRNKGKVPVSMPAKAAAPAKDDDDDDDDDDDDEDDDDDDDEDDE", "text": "FUNCTION: Binds preferentially single-stranded DNA and unwinds double- stranded DNA. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the HMGB family."}
{"protein": "MDIPVELRDYSKRRESEEAVANEGNSDDDGNEYLSGLRLTYLFLALILCMLLAVIDLTITATAVPHITDEFHSLNDIGWYASVFFMTVASSQSSWGKIYRYFDLKNMFLLAMGIFELGNVICGAAPTSNALIVGRAITGIGAAGVIAGCFTVAAFAVRPSKRPAFTGGLAATYGVGSSIGPIIGGVLSDRVSWRWCFYINLPIGGFAAIVLFLFFKSPAHSRNEADHRASWREKMLQMDFPGFFCCIAAVTCLLLALLWGGTTKSWNSSDVIGTLVGFFLFTALFAVVEWKSGERAMVVPRIMKQRVVLFGTIGGFFAGGAQFVLVYYVPIYFQAILGTSAQDSGVRNLPYIIGSTITTIVAGTTISATGYFTPLIVGGGALWTVSAGLIYTWSPTTTTGQWIGYQALAGLAVGLCYQPPILAAQALAAPTDVAATSAILLFFQTMGGAFMVSAAQTAFSNGLIHKLVQYSPGTDVQAVIATGLQELRVRYTGAELEAIIQSYMDGLKISFAIIIALTGASTVAGIFMPWKSFKTIQAEKNVENSD", "text": "FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of dibenzodioxocinones such as pestalotiollide B, a novel class of inhibitors against cholesterol ester transfer protein (CEPT) (PubMed:31474098). essential for dibenzodioxocinones biosynthesis and may be involved in the secretion of the cluster products (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLRQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVDQREIEQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGGDPGDAFGIVAPFARRPSVHSDLMYIREKASAGSQAKDKERCVIS", "text": "FUNCTION: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm, perinuclear region Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. RasD family."}
{"protein": "MYTLLSGLYKYMFQKDEYCILILGLDNAGKTTFLEQSKTRFNKNYKGMSLSKITTTVGLNIGTVDVGKARLMFWDLGGQEELQSLWDKYYAECHGVIYVIDSTDEERLSESKEAFEKVVSSEALDGVPILVLANKQDVETCLSIPDIKTAFSDCTCKIGRRDCLTQACSALTGKGVREGIEWMVKCVVRNVHRPPRQRDIT", "text": "FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. SUBCELLULAR LOCATION: Golgi apparatus Golgi apparatus, trans-Golgi network Note=Located in the trans-Golgi in the GTP-bound active state. SUBCELLULAR LOCATION: Golgi apparatus. Golgi apparatus, trans-Golgi network Note=Located in the trans-Golgi in the GTP-bound active state. SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
{"protein": "MLLENGWLVDARHVPSPHHDCRPEDEKPTLLVVHNISLPPGEFGGPWIDALFTGTIDPDAHPFFAEIAHLALSADCLIRRDGEVVQYVPFDKRAWHAGVSMYQGRERCNDFSIGIELEGTDTTPYTDAQYEKLVAVTQTLIGRYPAIADNITGHSDIAPERKTDPGPAFDWSRFHAMLTTSSDKEIT", "text": "FUNCTION: Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family."}
{"protein": "MSSQPKLRILCLHGYRQCDQSFRQKTGSTRKLVKALADFEFVNGIHSVAVDEHSETSRAWWFSNADQMSFSSREPTDVSVGFDESVNAVVKFIEDNGPFDGLLGFSQGASMVHLLIAKAQLGEIKLPGIRFAIFFSGFLSLSSKHDTLTSLRIKDFPSMHVFGDSDEIVARPKSEKLADQFDMEPIRIAHEGGHLVPSMSKHKERITQFLREQMAPIASA", "text": "SIMILARITY: Belongs to the LovG family."}
{"protein": "MLNFKTENTKYSLEEYTRYSKHLVLPQIQLEGQERLKEAKVLFIGAGGLGSPGIIYLAAAGIGSIGIIDDDIIDLSNLQRQILYRCNDIGYSKVEIAKKKILDLNPQCIVTVFKTRLSYENSIDIIRQYDIIIDGSDNFDTRYLLNDTCLELNKIHIYGAIFQFEGQVSVFNYQGGPVYRDFYSETENKESARDTCSNSGVLGLLPGIVGTLQATEAVKIVLGYKSILSGTILTYNSLTSSFNKFKIINTKFVLSTKKHWNKYYGSKSSTFVREISVIQLQKFLISRNPQYILIDVRNHEEYHKSHLIHSLNLPLQKIKGMNYSHINLQDKICFVYCSLDSRSIFASKFLIAQKLNIVRVRGGLNAWKNIIGDLDWTL", "text": "FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein moaD. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the HesA/MoeB/ThiF family."}
{"protein": "MAYRKRGAKRENLPQQNERLQEKEIEKDVDVTMENKNNNRKQQLSDKVLSQKEEIITDAQDDIKIAGEIKKSSKEESKQLLEILKTKEDHQKEIQYEILQKTIPTFESKESILKKLEDIRPEQAKKQMKLFRIFEPKQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQILIEMPDYLLLKDMAVENKNSRDAGKVVDSETANICDAIFQDEETEGVVRRFIADMRQQVQADRNIVNYPSILHPIDHAFNEYFLNHQLVEPLNNEIIFNYIPERIRNDVNYILNMDMNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKEKELVSTEAQIQKMSQDLQLEALTIQSETQFLAGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVIPNDMFLRESLVACELAIINTIVYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFTNNNRFRQVVIDGVLNQTLNDNIRNGQVINQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLVSYNYETLMACVTMNMQHVQTLTTEKLQLTSVTSLCMLIGNTTVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKSIVEDFLKRLQIFDVPRVPDDQMYRLRDRLRLLPVERRRLDIFNLILMNMEQIERASDKIAQGVIIAYRDMQLERDEMYGYVNIARNLDGYQQINLEELMRTGDYGQITNMLLNNQPVALVGALPFVTDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWIPTSTTKVYKQVPQPFDFRASMHMLTSNLTFTVYSDLLSFVSADTVEPINAVAFDNMRIMNEL", "text": "FUNCTION: Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication. SUBCELLULAR LOCATION: Virion Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus VP2 family."}
{"protein": "MSNTVTLRADGRLFTGWTSVSVTRSIESVAGYFELGVNVPPGTDLSGLAPGKKFTLEIGGQIVCTGYIDSRRRQMTADSMKITVAGRDKTADLIDCAAVYSGGQWKNRTLEQIARDLCAPYGVTVRWELSDKESSAAFPGFTLDHSETVYEALVRASRARGVLMTSNAAGELVFSRAASTATDELVLGENLLTLDFEEDFRDRFSEYTVKGYARANGAEGDDIDAKSIVSRKGTATDSDVTRYRPMIIIADSKITAKDAQARALREQRRRLAKSITFEAEIDGWTRKDGQLWMPNLLVTIDASKYAIKTTELLVSKVTLILNDQDGLKTRVSLAPREGFLVPVESDRKNRKGGDSNGGIDALVEDYYRRHPEKTPPWKE", "text": "FUNCTION: Forms the central cylindrical hub of the baseplate and plays an important role in baseplate and tail assembly (Probable). Core component of the initiator complex that triggers the tail tube polymerization during tail assembly (Probable). Forms a conduit that probably functions as an extension of the tail tube allowing viral DNA release during ejection. Might facilitate the interaction of the virus with the host cell surface through electrostatic interactions during virus entry into host cell. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Baseplate protein."}
{"protein": "CGILGLGGVGHMGVKAFGLHVTVISSSDKFVVDVAASNLDK", "text": "FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers, like coniferyl alcohol, sinapyl alcohol and 4-coumaryl alcohol (By similarity). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MNIINLGILAHIDAGKTSVTENLLFASGATEKCGRVDNGDTITDSMDIEKRRGITVRASTTSIIWNGVKCNIIDTPGHMDFIAEVERTFKMLDGAVLILSAKEGIQAQTKLLFNTLQKLQIPTIIFINKIDRDGVNLERLYLDIKTNLSQDVLFMQTVVDGLVYPICSQTYIKEEYKEFVCNHDDNILERYLADSEISPADYWNTIIDLVAKAKVYPVLHGSAMFNIGINELLDAISSFILPPESVSNRLSAYLYKIEHDPKGHKRSFLKIIDGSLRLRDIVRINDSEKFIKIKNLKTIYQGRKINVDEVGANDIAIVEDMEDFRIGDYLGTKPCLIQGLSHQHPALKSSVRPDRSEERSKVISALNTLWIEDPSLSFSINSYSDELEISLYGLTQKEIIQTLLEERFSVKVHFDEIKTIYKERPVKKVNKIIQIEVPPNPYWATIGLTLEPLPLGTGLQIESDISYGYLNHSFQNAVFEGIRMSCQSGLHGWEVTDLKVTFTQAEYYSPVSTPADFRQLTPYVFRLALQQSGVDILEPMLYFELQIPQAASSKAITDLQKMMSEIEDISCNNEWCHIKGKVPYNTSKDYASEVSSYTKGLGVFMVKPCGYQITKGDYSDNIRMNEKDKILFMFQKSNVIKIMERSGNFYKAIQ", "text": "FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. TetM/TetO subfamily."}
{"protein": "MTQEPGYTRLQITLHWAIAGLVLFNYIFGETMERAYDAVRQNVEPAGVGHYLHVVVGLAVLVLTLVRIGARFVLGVPEKGTTPGDKVAAGLQGLLYLLTLLVPALGMTAWGGGQAWAAGPHVLAANAIMLLALVHAVSALFHQYVLKDRLLLRMMRPR", "text": "FUNCTION: Cytochrome b562 is an integral component of the cytochrome b- c1 complex in the cyclic electron transfer system of photosynthetic bacteria. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b561 family."}
{"protein": "MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFEQVTEDCNENPEKDVLTELGDILAQAVNHAGIDSSSTGPTLTTHSCSVSSAPLNKPTPTSVAVTNTPLPGASATPELSPRKKPRKTTRPFKVIIKPPVPPAPIMLPLIKQEDIKPEPDFTIQYRNKIIDTAGCIVISDSEEEQGEEVETRGATASSPSTGSGTPRVTSPTHPLSQMNHPPLPDPLGRPDEDSSSSSSSSCSSASDSESESEEMKCSSGGGASVTSSHHGRGGFGGAASSSLLSCGHQSSGGASTGPRKKKSKRISELDNEKVRNIMKDKNTPFCTPNVQTRRGRVKIDEVSRMFRHTNRSLEYKNLPFMIPSMHQVLEEAIKVCKTMQVNNKGIQIIYTRNHEVKNEVDQVRCRLGSMCNLALSTPFLMEHTMPVTHPPDVAQRTADACNDGVKAVWNLKELHTHQLCPRSSDYRNMIIHAATPVDLLGALNLCLPLMQKFPKQVMVRIFSTNQGGFMLPIYETAAKAYAVGQFEKPTETPPEDLDTLSLAIEAAIQDLRNKSQ", "text": "FUNCTION: Stimulates viral early and late gene expression and thus play a crucial role in the regulation of productive infection. In addition, activates quiescent cells to reenter the cell cycle and up-regulates several E2F-responsive genes, which are responsible for pushing the cell into S phase. In S-phase, inhibits cellular DNA synthesis and blocks further cell cycle progression (By similarity). SUBCELLULAR LOCATION: Host nucleus. Note=Colocalizes with host PML- associated nuclear bodies. SIMILARITY: Belongs to the HHV-5 IE2 protein family."}
{"protein": "MEKKLPRRLEGKVAIVTASTQGIGFGITERFGLEGASVVVSSRKQANVDEAVAKLKSKGIDAYGIVCHVSNAQHRRNLVEKTVQKYGKIDIVVCNAAANPSTDPILSSKEAVLDKLWEINVKSSILLLQDMAPHLEKGSSVIFITSIAGFSPQGAMAMYGVTKTALLGLTKALAAEMAPDTRVNAVAPGFVPTHFASFITGSSEVREGIEEKTLLNRLGTTGDMAAAAAFLASDDSSYITGETLVVAGGMPSRL", "text": "FUNCTION: Involved with IBR3 and IBR10 in the peroxisomal beta- oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin. May be responsible for catalyzing the dehydrogenation step in the conversion of IBA (PubMed:20562230). May be involved in the peroxisomal activation of 2,4- dichlorophenoxybutyric acid (2,4-DB), a precursor of active auxins that inhibit root growth (PubMed:19043666). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MAPKKDKAPPPSSKPAKSGGKQKKKKWSKGKQKEKVNNLVLFDNATFDKLLSEAGKQKVVTAATLSERFRINGSLARRAIRELVSRGAIKMVCHHSSLQIYTRSTNEKVNPTAA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eS25 family."}
{"protein": "MGKTYSSPINPIPKAPKGLAIHHWLNFLQAAYRLQPGPSEFDFHQLRKFLKLAIKTPVWLNPINYSVLAGLIPKNYPGRVHEIVAILIQETPAREAPPSAPLAEDPQKPPPYPEQAQEASQCLPILHPHGAPAAHRPWQMKDLQAIKQEVSSSAPGSPQFMQTIRLAVQQFDPTAKDLHDLLQYLCSSLVASLHHQQLETLIAQAETQGITGYNPLAGPLRIQANNPNQQGLRKEYQNLWLSAFSALPGNTKDPTWAAILQGPEEPFGSFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGQTNSPLGEMLRACQTWTPRDKNKILMVQPKKTPPPNQPCFRCGQVGHWSRDCKQPRPPPGPCPVCQDPTHWKRDCPQLKTDTRDSEDLLLDLPCEAPNVRERKNSSGGED", "text": "FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. FUNCTION: Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome. FUNCTION: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). SUBCELLULAR LOCATION: [Capsid protein p24]: Virion. SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion. SUBCELLULAR LOCATION: [Matrix protein p19]: Virion."}
{"protein": "MDTRPLIGITMGDPASIGPEIAAKALANPEIYALCRPLLIGDSRVMARAFETTGVKLNLNPVATPAEGKYAHGTVDLIDLPVVDMGTLQWGQVQAQAGAAAFAYIKRSIELALEGAVDAVTTGPINKEALKAARIDFIGHTEIFGELTGSHDPLTMFETKGLRIFFLTRHVSLAQACRMITRDRVLDYIRRCTAALEQLGLVRPKLAVAGLNPHCGEHGLFGDEEVREIEPAVQQAQAEGYNVSGPHPADSVFWHAAQGRFDAVLSLYHDQGHIAAKMYDFERTVSITAGLPFLRSSVDHGTAFDIAGTGRASAVSLEEAIRVGAKYAAAFRRTR", "text": "FUNCTION: Catalyzes the NAD-dependent oxidation and subsequent decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone phosphate (DHAP). SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily."}
{"protein": "MVRMNVLADALKCINNAEKRGKRQVLLRPCSKVIIKFLTVMMKHGYIGEFEIVDDHRSGKIVVNLTGRLNKCGVISPRFDVPINDIEKWTNNLLPSRQFGYVVLTTSGGIMDHEEARRKHLGGKILGFFF", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS8 family."}
{"protein": "MAPPASTASSADPSKPTAQKLTEESDEKTLRKYFSTKVDDAQQKVADKSQNVRRLQAQRNELNTKVRMLKEELQQLHEQGSYVGEVSKAMDKKKVLVKVHPEGKYVVDVDKSIDINSLNTGARVALRADSYALHKLLPNKVDPLVSLMMVEKVPDSTYEMVGGLDKQIKEIKEVIELPVKHPELFDALGIAQPKGVLLFGPPGTGKTLLARAVAHHTECTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRVEGSSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDPALLRPGRIDRKIEFPAPDEKARADILKIHSRKMNLMRGINMAKIAEQIPGASGAEVKSVCTEAGMFALRERRIHVTQEDFEMAVGKVMQKDSEKNMSIKKLWK", "text": "FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins (PubMed:30265660). This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required (PubMed:30265660). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (By similarity). Belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides (By similarity). In addition, regulates gene expression in response to bacterial infection (PubMed:30265660). Binds to the GATA transcription factor elt-2 to control its transcriptional activity and thus the expression of elt-2-dependent genes in response to infection by Gram-negative bacteria such as P.aeruginosa (PubMed:30265660). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MAGEGINEDYPVEIHEYLSTFENSIGAVDEMLKTMMSVSRNELLQKLDPLEQAKVDLVSAYTLNSMFWVYLATQGVNPKEHPVKQELERIRVYMNRVKEITDKKKAGKLDRGAASRFVKNALWEPKPKNASKVANKGKSKN", "text": "FUNCTION: Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus, nucleolus Note=EXOSC10 is required for nucleolar localization. Colocalizes with TSNAX in the nucleus. SIMILARITY: Belongs to the C1D family."}
{"protein": "MVLNFRDKSCIFLAILCCLSLSCIVKASVSYDRKAVIINGQRRILLSGSIHYPRSTPEMWPGLIQKAKEGGLDVIETYVFWNGHEPSPGQYYFGDRYDLVKFIKLVHQAGLYVNLRIGPYVCAEWNFGGFPVWLKFVPGMAFRTDNEPFKAAMKKFTEKIVWMMKAEKLFQTQGGPIILAQIENEYGPVEWEIGAPGKAYTKWVAQMALGLSTGVPWIMCKQEDAPGPIIDTCNGYYCEDFKPNSINKPKMWTENWTGWYTDFGGAVPYRPVEDIAYSVARFIQKGGSLVNYYMYHGGTNFDRTAGEFMASSYDYDAPLDEYGLPREPKYSHLKALHKAIKLSEPALLSADATVTSLGAKQEAYVFWSKSSCAAFLSNKDENSAARVLFRGFPYDLPPWSVSILPDCKTEVYNTAKVNAPSVHRNMVPTGTKFSWGSFNEATPTANEAGTFARNGLVEQISMTWDKSDYFWYITDITIGSGETFLKTGDSPLLTVMSAGHALHVFVNGQLSGTAYGGLDHPKLTFSQKIKLHAGVNKIALLSVAVGLPNVGTHFEQWNKGVLGPVTLKGVNSGTWDMSKWKWSYKIGVKGEALSLHTNTESSGVRWTQGSFVAKKQPLTWYKSTFATPAGNEPLALDMNTMGKGQVWINGRNIGRHWPAYKAQGSCGRCNYAGTFDAKKCLSNCGEASQRWYHVPRSWLKSQNLIVVFEELGGDPNGISLVKRT", "text": "FUNCTION: Preferentially hydrolyzes para-nitrophenyl-beta-D- galactoside. Can hydrolyze para-nitrophenyl-beta-D-fucoside with 5 time less efficiency. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 35 family."}
{"protein": "MADFDEIYEEEEDEERALEEQLLKYSPDPVVVRGSGHVTVFGLSNKFESEFPSSLTGKVAPEEFKASINRVNSCLRKNLPVNVRWLLCGCLCCCCTLGCSMWPVICLSKRTRRSIEKLLEWENNRLYHKLCLHWRLSKRKCETNNMMEYVILIEFLPKTPIFRPD", "text": "SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Golgi apparatus Note=Associated and found in vesicular structures of Golgi complex. SIMILARITY: Belongs to the CHIC family."}
{"protein": "MGTRKKVQAFVRVRPTDDFAHEMIKYGEDNKSIDIHLKKDTRRGVVNNQQTDWSFKLDGVLHNASQDLVYETVAKDAVSQALDGYNGTIMCYGQTGAGKTYTMTGATENYKHRGILPRALQQVFRMIEERPTHAITVRVSYLEIYNENLFDLLSTLPYVGPSVTPMTIVENPQGIFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYMEAHSRTLSDEKYITSKINLVDLAGSERLSKTGSEGRVLKEATYINKSLSFLEQAIIALGDQNRDHVPFRQSKLTHALKDSLGGNCNMVLVTNIYGEAAQLDETLSSLRFASRMKLVTTEPAINEKYDAERMVKNLEKELALLKQELAIHDSLSNRTLVNYDPMDEIQIAEINSQVRRYLEGTLDEIDIINLRQIQEVFNQFRVVLSQQEQEVESALRRKYTLIDKNDFAAISAVQKVGLMDIEGNLVGEPDGQSFGLGVAPFSVKPGKKPKTKKTPKDQFSSSARKEGASSPVSGKDFDVASISKTQLIPSSKDGDLKDMLARERETSSIEPLISDSPKEELRAPRPSTPPSRTVAFEEFKNERGSEINRIFKENKSILNERKKRASETTQRINAIKQEIDETKDALNFQKSLREKQGEYENKGLMIIDEEEFLLILKLKDLKKQYRNEYQELRDLRAEIQYCQRLVDQCRHRLLMEFDIWYNESFMIPEDVQVALKLGSSIRPGMVPISRIVCLGEDDQDRFSHLQQTVLPEGLDSITFYNAKVKTDQKHNYMKTMVGLQQSHRK", "text": "FUNCTION: Essential for normal male fertility and for progressive motility of spermatozoa. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, cilium, flagellum Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family."}
{"protein": "MPSILLINGPNLNLLGTREPHLYGSTTLPQLEDNAKALAASKGVKLESFQSNHEGQIVDRIHEARGHTDAIIINPGAFTHTSVAIRDALIGVSIPFIEVHITNVHAREEFRHHSYLSDKAAACIIGLGTYGYEAAIEYAVREIISAKYVY", "text": "FUNCTION: Is involved in the catabolism of quinate. Allows the utilization of quinate as carbon source via the beta-ketoadipate pathway. SIMILARITY: Belongs to the type-II 3-dehydroquinase family."}
{"protein": "MGAAAVRWHLYLLLALGARGRLVGGSGLPGAVDVDECSEGTDDCHIDAICQNTPKSYKCLCKPGYKGEGRQCEDIDECENDYYNGGCVHDCINIPGNYRCTCFDGFMLAHDGHNCLDVDECQDNNGGCQQICVNAMGSYECQCHSGFFLSDNQHTCIHRSNEGMNCMNKDHGCAHICRETPKGGVACDCRPGFDLAQNQKDCTLTCNYGNGGCQHSCEDTDTGPMCGCHQKYALHADGRTCIEKDEAAIERSQFNATSVADVDKRVKRRLLMETCAVNNGGCDRTCKDTATGVRCSCPVGFTLQPDGKTCKDINECLMNNGGCDHFCRNTVGSFECGCQKGHKLLTDERTCQDIDECSFERTCDHICINSPGSFQCLCRRGYTLYGTTHCGDVDECSMNNGSCEQGCVNTKGSYECVCPPGRRLHWNQKDCVEMNGCLSRSKASAQAQLSCGKVGGVENCFLSCLGHSLFMPDSESSYILSCGVPGLQGKTLPKRNGTSSSTGPGCSDAPTTPIRQKARFKIRDAKCHLQPRSQERAKDTLRHPLLDNCHVTFVTLKCDSSKKRRRGRKSPSKEVSHITAEFEVEMKVDEASGTCEADCMRKRAEQSLQAAIKILRKSIGRNQFYVQVLGTEYEVAQRPAKALEGTGTCGIGQILQDGKCVPCAPGTYFSGDPGQCMPCVSGTYQDMEGQLSCTPCPSSEGLGLAGARNVSECGGQCSPGYFSADGFKPCQACPVGTYQPEPGRTGCFPCGGGLLTKHTGTASFQDCEAKVHCSPGHHYNTTTHRCIRCPVGTYQPEFGQNHCISCPGNTSTDFDGSTNVTHCKNQHCGGELGDYTGYIESPNYPGDYPANAECVWHIAPPPKRRILIVVPEIFLPIEDECGDVLVMRKSASPTSVTTYETCQTYERPIAFTSRSRKLWIQFKSNEANSGKGFQVPYVTYDEDYQQLIEDIVRDGRLYASENHQEILKDKKLIKALFDVLAHPQNYFKYTAQESKEMFPRSFIKLLRSKVSRFLRPYK", "text": "FUNCTION: Could function as an adhesive molecule and its matrix bound and soluble fragments may play a critical role in vascular biology. SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein."}
{"protein": "MAPKRTADGRRRKRGQKTEDNKVARHEESVADDFEDEKQKPRRKSSFPKVSQGKRKRGCSDPGDPTNGAAKKKVAKATAKSKNLKVLKEEALSDGDDFRDSPADCKKAKKHPKSKVVDQGTDEDDSEDDWEEVEELTEPVLDMGENSATSPSDMPVKAVEIEIETPQQAKERERSEKIKMEFETYLRRMMKRFNKEVQENMHKVHLLCLLASGFYRNSICRQPDLLAIGLSIIPIRFTKVPLQDRDAYYLSNLVKWFIGTFTVNADLSASEQDDLQTTLERRIAIYSARDNEELVHIFLLILRALQLLTRLVLSLQPIPLKSAVTKGRKSSKETSVEGPGGSSELSSNSPESHNKPTTSRRIKEEETLSEGRGKATARGKRGTGTAGSRQRRKPSCSEGEEAEQKVQGRPHARKRRVAAKVSYKEESESDGAGSGSDFEPSSGEGQHSSDEDCEPGPRKQKRASAPQRTKAGSKSASKTQRGSQCEPSSFPEASSSSSGCKRGKKVSSGAEEMADRKPAGVDQWLEVYCEPQAKWVCVDCVHGVVGQPVACYKYATKPMTYVVGIDSDGWVRDVTQRYDPAWMTATRKCRVDAEWWAETLRPYRSLLTEREKKEDQEFQAKHLDQPLPTSISTYKNHPLYALKRHLLKFQAIYPETAAVLGYCRGEAVYSRDCVHTLHSRDTWLKQARVVRLGEVPYKMVKGFSNRARKARLSEPQLHDHNDLGLYGHWQTEEYQPPIAVDGKVPRNEFGNVYLFLPSMMPVGCVQMTLPNLNRVARKLGIDCVQAITGFDFHGGYCHPVTDGYIVCEEFRDVLLAAWENEQAIIEKKEKEKKEKRALGNWKLLVRGLLIRERLKLRYGAKSEAAAPHAAGGGLSSDEEEGTSSQAEAARVLAASWPQNREDPEQKSEYTKMTRKRRAAEASHLFPFEKL", "text": "FUNCTION: In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes. FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen- bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1. SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions. SIMILARITY: Belongs to the XPC family."}
{"protein": "MSQTTASITTAQWQQKRDQFVSKGVSNGNRSLAVKGEGAELYDLDGRRFIDFAGAIGTLNVGHSHPKVVEAVKRQAEELIHPGFNVMMYPTYIELAEKLCGIAPGSHEKKAIFLNSGAEAVENAVKIARKYTKRQGVVSFTRGFHGRTNMTMSMTSKVKPYKFGFGPFAPEVYQAPFPYYYQKPAGMSDESYDDMVIQAFNDFFIASVAPETVACVVMEPVQGEGGFIIPSKRFVQHVASFCKEHGIVFVADEIQTGFARTGTYFAIEHFDVVPDLITVSKSLAAGLPLSGVIGRAEMLDAAAPGELGGTYAGSPLGCAAALAVLDIIEEEGLNERSEEIGKIIEDKAYEWKQEFPFIGDIRRLGAMAAIEIVKDPDTREPDKTKAAAIAAYANQNGLLLLTAGINGNIIRFLTPLVISDSLLNEGLSILEAGLRA", "text": "SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MSSAQSRGGKTGGKVGGKVGAKRHKKTQKEHINGITKPAIRRLARRGGVKRISFPIYEETRNVLRTFLTNVIRDSVAYTEHAGRRTVTAMDVVYALKRQGRTLYGFNS", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H4 family."}
{"protein": "MEDTGSGKNGKDDIQTKLDKKLGPEYISKRVGFGSSRVAYIEGWKAINLANQIFGYDGWSTEVKNVTIDFLDERQGRFSIGCTAIVRVSLADGTFREDIGYGTVENERRKASAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDEGNLFRPADELSEMSRSNMVGDAHTEGPSLKKRSLTNEDRNAVPSAPAQQTYRSNNHTTQKRAPKAQAVTASASPNEETSNQQQDPDDLLDDSFMFSDEIQDDDLLNMNTTTNNKNSTNSSTTTTTISDEATGIISPVTFVTAKAATSLQHKDPIPSGSMFDPKFQAQSIRHTVDQSVSTPVRATILKEKGLDSDRSSIYSKFAPKGKELSGTTTNSEPYVAAPQTSATESNRSTPTRSNAQLAGPQPAPQLQGPQRTQLGRPRMLQQPNRRNVS", "text": "FUNCTION: Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RAD52 family."}
{"protein": "MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVFPGDGASHTKVHFRYVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKFDEAEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSAEAASSSEELPKKEAPYTLVGSISEPGLGLLSWWTSN", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNA. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family."}
{"protein": "MDPEVTLLLQCPGGGLPQEQIQAELSPAHDRRPLPGGDEAITAIWETRLKAQPWLFDAPKFRLHSATLAPIGSRGPQLLLRLGLTSYRDFLGTNWSSSAAWLRQQGATDWGDTQAYLADPLGVGAALATADDFLVFLRRSRQVAEAPGLVDVPGGHPEPQALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARNETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVQRLLETEMWAELCPSAKGAIILYNRVQGSPTGAALGSPALLPPL", "text": "FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and UDP-galactose to galactose 1-phosphate and UMP. Preferred substrate is UDP-glucose. SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MASTVGVPSLYQVPHLEISKPNSKKRSNCLSLSLDKPFFTPLSLVRRTRRIHSSSLLVPSAVATPNSVLSEEAFKSLGLSDHDEYDLDGDNNNVEADDGEELAISKLSLPQRLEESLEKRGITHLFPIQRAVLVPALQGRDIIARAKTGTGKTLAFGIPIIKRLTEEAGDYTAFRRSGRLPKFLVLAPTRELAKQVEKEIKESAPYLSTVCVYGGVSYTIQQSALTRGVDVVVGTPGRIIDLIEGRSLKLGEVEYLVLDEADQMLAVGFEEAVESILENLPTKRQSMLFSATMPTWVKKLARKYLDNPLNIDLVGDQDEKLAEGIKLYAIATTSTSKRTILSDLITVYAKGGKTIVFTQTKRDADEVSLALSNSIATEALHGDISQHQRERTLNAFRQGKFTVLVATDVASRGLDIPNVDLVIHYELPNDPETFVHRSGRTGRAGKEGSAILMHTSSQKRTVRSLERDVGCHFEFISPPTVGDLLESSADQVVATLNGVHPDSIKFFSATAQKLYEEKGTDALAAALAHLSGFSQPPSSRSLLSHEKGWVTLQLIRDPTNARGFLSARSVTGFLSDLYRTAADEVGKIFLIADDRIQGAVFDLPEEIAKELLEKDVPEGNSLSMITKLPPLQDDGPSSDNYGRFSSRDRMPRGGGGSRGSRGGRGGSSRGRDSWGGDDDRGSRRSSGGGSSWSRGGSSSRGSSDDWLIGGRSSSSSRAPSRERSFGGSCFICGKSGHRATDCPDKRGF", "text": "FUNCTION: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts (PubMed:22576849, PubMed:23227895, PubMed:25043599). Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit (PubMed:22576849). Required for normal development of chloroplasts (PubMed:22576849, PubMed:23227895, PubMed:25043599). Required for the expression of transcripts encoding plastid-localized enzymes involved in abscisic acid (ABA) biosynthesis. Required for maintenance of ABA levels and response to salt stress (PubMed:23227895). Possesses RNA chaperone activity for proper splicing of introns in chloroplasts. Essential for chloroplast function and abiotic stress responses (PubMed:25043599). SUBCELLULAR LOCATION: Plastid, chloroplast Plastid, chloroplast stroma. SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily."}
{"protein": "MVFSSFPTYPDHSSNWQQQHQPITTTVGFTGNNINQQFLPHHPLPPQQQQTPPQLHHNNGNGGVAVPGGPGGLIRPGSMAERARLANIPLPETALKCPRCDSTNTKFCYFNNYSLTQPRHFCKACRRYWTRGGALRSVPVGGGCRRNKRTKNSSGGGGGSTSSGNSKSQDSATSNDQYHHRAMANNQMGPPSSSSSLSSLLSSYNAGLIPGHDHNSNNNNILGLGSSLPPLKLMPPLDFTDNFTLQYGAVSAPSYHIGGGSSGGAAALLNGFDQWRFPATNQLPLGGLDPFDQQHQMEQQNPGYGLVTGSGQYRPKNIFHNLISSSSSASSAMVTATASQLASVKMEDSNNQLNLSRQLFGDEQQLWNIHGAAAASTAAATSSWSEVSNNFSSSSTSNI", "text": "FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G- 3' consensus core sequence (By similarity). Binds to 5'-TAAAGT-3' motif in REV promoter to triggers its transcription, thus regulating adaxial- abaxial polarity and influencing leaf axial patterning in an auxin transport- and response-dependent manner (e.g. IAA6 and IAA19 genes expression) (PubMed:20807212). Probably involved in early processes for vascular development (PubMed:17583520). The PEAR proteins (e.g. DOF2.4, DOF5.1, DOF3.2, DOF1.1, DOF5.6 and DOF5.3) activate gene expression that promotes radial growth of protophloem sieve elements (PubMed:30626969). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MCDSKDNSGVSEKCGKKFTNYPLNTTPTSLNYNLPEISKKFYNLKNKYSRNGYGLSKTEFPSSIENCPAKEYSIMYDNKDPRFLIRFLLDDGRYIIADRDDGEVFDEAPIYLDNNNHPIISRHYTGEERQKFEQVGSGDYITGEQFFQFYTQNKTRVLSNCRALDSRTILLSTAKIFPIYPPASETQLTAFVNSSFYAAAIPQLPQTSLLENIPEPTSLDDSGVLPKDAVRAVKGSALLPCIIVHDPNLNNSDKMKFNTYYLLEYKEYWHQLWSQIIPAHQTVKIQERTGISEVVQNSMIEDLNMYIGADFGMHFYLRSSGFKEQITRGLNRPLSQTTTQLGERVEEMEYYNSNDLDVRYVKYALAREFTLKRVNGEIVKNWVAVDYRLAGIQSYPNAPITNPLTLTKHTIIRCENSYDGHIFKTPLIFKNGEVIVKTNEELIPKINQ", "text": "FUNCTION: Component of a binary toxin active against Culex and some Aedes mosquito larvae; mortality towards both C.quinquefasciatus and A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible to this toxin (PubMed:8419297). This subunit is responsible for localized binding to specific regions of the host larval gut. Binary toxin internalization into host gut cells requires both proteins (By similarity). SUBCELLULAR LOCATION: Spore, perispore. SIMILARITY: Belongs to the toxin_10 family."}
{"protein": "MNLQQQLSHCQQHQHLLQLTHFNHETAWQLGEKIKQQAELQGVALAINIRVNGQTLFSYAMPGTCAENADWLRRKRNVVELLGTSSYAAGLMLQQRQTSLEERYGVSLRDYAALGGGFPLQVKQAGIIGSVNVSGAPHLDDHNLLLQVLADFIGLPAGSIELLAPLTE", "text": "SIMILARITY: Belongs to the UPF0303 family."}
{"protein": "MYEIKQPFHSGYLQVSEIHQIYWEESGNPDGVPVIFLHGGPGAGASPECRGFFNPDVFRIVIIDQRGCGRSRPYACAEDNTTWDLVADIEKVREMLGIGKWLVFGGSWGSTLSLAYAQTHPERVKGLVLRGIFLCRPSETVWLNEAGGVSRIYPEQWQKFVAPIAENRRNRLIEAYHGLLFHQDEEVCLSAAKAWADWESYLIRFEPEEVDEDAYASLAIARLENHYFVNGGWLQGDRAILNNIGKIRHIPTIIVQGRYDLCTPMQSAWALSKAFPEAELRVVQAGHRAFDPPLVDALVQAVEDILPHLL", "text": "FUNCTION: Specifically catalyzes the removal of N-terminal proline residues from peptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S33 family."}
{"protein": "MPAFNRLLPLASLVLIYWVRVCFPVCVEVPSETEAVQGNSMKLRCISCMKREEVEATTVVEWFYRPEGGKDFLIYEYRNGHQEVESPFQGRLQWNGSKDLQDVSITVLNVTLNDSGLYTCNVSREFEFEAHRPFVKTTRLIPLRVTEEAGEDFTSVVSEIMMYILLVFLTLWLFIEMIYCYRKVSKAEEAAQENASDYLAIPSENKENSVVPVEE", "text": "FUNCTION: Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with NFASC may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN3B (TC 8.A.17) family."}
{"protein": "MADVSERTLQVSVLVAFASGVVLGWQANRLRRRYLDWRKRRLQDKLATTQKKLDLA", "text": "FUNCTION: Positively regulates mitochondrial complex assembly and/or stability (PubMed:29949756). Increases mitochondrial membrane potential while decreasing mitochondrial reactive oxygen species (By similarity). Increases mitochondrial respiration rate (PubMed:31296841). Increased mitochondrial respiratory activity promotes myogenic differentiation which facilitates muscle growth and regeneration (PubMed:31296841, PubMed:32393776). Increases mitochondrial calcium retention capacity (PubMed:29949756). Plays a role in maintenance of cellular lipid composition through its interaction with cytochrome b5 reductase CYB5R3 which is required for mitochondrial respiratory complex I activity (PubMed:30796188). Interacts with the mitochondrial trifunctional enzyme complex (MTE) and enhances fatty acid beta-oxidation (PubMed:29949755, PubMed:32243843). Not required for MTE formation or stability (PubMed:29949755). Modulates triglyceride clearance in adipocytes through its role in regulating fatty acid beta-oxidation and lipolysis (PubMed:32243843). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein Note=Preferentially binds to cardiolipin relative to other common cell membrane lipids. SIMILARITY: Belongs to the mitoregulin family."}
{"protein": "NCYIFNWGQEGQELLESANPGADFGLKMVLDIDQKEYIPFLQSTAAARIILHQQRSFPFLKDLGIYAMPGTETSIAVLEDQTQHLEAPYSSCTVDGSDIPVANIYSKFNSSYSIQSCLRSCFQEIMVKYCKCAYYLFPLLNGAHYCNNQEDPDWVPCYYNIWDTVSHREQCINMCQQPCNDSNYKMTISMADWPSAAAEDWIFHVLSYEKDTSLDITVNRDGIMRLNIYFEEFNYRSISESPTTNVVWLLSNLGGQFGFWMGGSVLCIIEFGE", "text": "FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane Note=Apical membrane of epithelial cells. SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1B subfamily."}
{"protein": "MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG", "text": "FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:10358076, PubMed:12228231, PubMed:15220471, PubMed:15890677, PubMed:18356527, PubMed:19221179, PubMed:20543840, PubMed:21245099). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (PubMed:10358076). Activity suppressed by insulin (PubMed:10358076). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (PubMed:17024043). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (PubMed:18356527, PubMed:19221179). Promotes neural cell death (PubMed:18356527). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (PubMed:20543840). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the cytoplasm and nucleus. Largely nuclear in unstimulated cells (PubMed:11311120, PubMed:12228231, PubMed:19221179, PubMed:21245099, PubMed:20543840, PubMed:25009184). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus (By similarity). Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). Insulin-induced phosphorylation at Ser-256 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteasomal pathway (PubMed:11237865, PubMed:12228231). Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation (PubMed:18356527). Phosphorylation by NLK results in nuclear export (By similarity). Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1 (PubMed:19221179, PubMed:21245099). SGK1-mediated phosphorylation also results in nuclear translocation (By similarity). Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide (By similarity). Retained in the nucleus on methylation (By similarity). PPIA/CYPA stimulates its nuclear accumulation (PubMed:31063815). Deacetylation by SIRT6, promotes its translocation into the cytoplasm (PubMed:25009184)."}
{"protein": "MDAETECCKCHLLDLPWEDVLVTHIFCYLPLRQLVRLQRVSKQFYALIQVYLANCRTFDLTQIGPSLPKEAFCNILRDNKVLQNLSVQNCSDWVTDTELLPVIGQNQHLLRVDMRGCDRLTRHSLVAVSLSCTHLQYLGLAHCEWVDSLSIRSLADHCGGLRSIDLTACRQLKDEAICYLSKKCLKMRSLSVAVNANITDVSVEEVAKNCRELEQLDLTGCLRVRNDSIRTVAEYCPKLQSLKVNHCHNVTESSLDPLRKRNVEIDVEPPLQRALVLLQDVVGFAPFINLQI", "text": "FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Acts as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBXL15 family."}
{"protein": "MSTETHDEPSGVAHTPASGLRGRPWPTLLAVAVGVMMVALDSTIVAIANPAIQQDLHASLADVQWITNGYLLALAVSLITAGKLGDRFGHRQTFLVGVAGFAVTSAAIGLSGSVAAIVVFRVLQGLFGALMQPSALGLLRVTFPPGKLNMAIGIWSGVVGASTAAGPIIGGLLVQHVGWEAVFFINVPVGLAALVAGLVILTDARAERAPKSFDVSGIVLLSGAMFCLVWGLIKAPAWGWGDLRTLGFLAAAVLAFAGFTLRESRATEPLMPLAMFRSVPLSAGTVLMVLMAFSFIGGLFFVTFYLQNVHGMSPVESGVHLLPLTGMMIVGAPVSGIVISRFGPGGPLVVGMLLTAASLWGMSTLEADSGMGITSLWFVLLGLGLAPVMVGTTDVIVSNAPAELAGVAGGLQQSAMQVGGSLGTAVLGVLMASRVGDVFPDKWAEANLPRVGPREAAAIEDAAEVGAVPPAGTLPGRHAGTLSEVVHSSFISGMGLAFTVAGAVALVAAAVALFTRKAEPDERAPEEFPVPASTAGRG", "text": "FUNCTION: Resistance to tetracenomycin C by an active tetracenomycin C efflux system which is probably energized by transmembrane electrochemical gradients. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. EmrB family."}
{"protein": "MVMLRSLLVSALAALAAASPIAEPADQSLEARQLGSSNDLTNGACKDVTLIFARGSTEMGNMGTVIGPPLCSALKSKLGADKVACQGVGGLYTGGLMQNALPQNTDPGAISTAKSLFEQASTKCPNTQIVAGGYSQGSAVIDNAVQQLSAEVKDKVKGVVFFGFTRNLQDKGQIPNYPKDNVKVFCAMGDLVCDGTLIVTAAHLTYTINAPEAASFLASKVQSA", "text": "FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (By similarity). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family."}
{"protein": "MTAFDADLRSLAAQTTLSRRTVIATSLATGFALAVQPVAAQTTIATDANGLIAGEVKIPMQDGVIPAYRAMPAEGGPFPTILVVQEIFGVHEHIKDVCRRLAKLGYFALAPELYARQGDVSTLTNIQQIVSEVVSKVPDAQVMSDLDAAVAFAKGTGKADTARLGITGFCWGGRITWLYAAHNPAVKAGVAWYGRLVGDSSALMPKNPVDVAADLKAPVLGLYGGADQGIPVATIDRMKEACRAAGKTCDFVVYPEAGHAFHADYRPSYRAEPAQDGWKRLQDWFRQYGVA", "text": "SIMILARITY: Belongs to the dienelactone hydrolase family."}
{"protein": "MESSALLTAGVLFLFVAVVAVPIAARLGIGAVLGYLIAGIAIGPWGLGFIRDVDAILHFSELGVVFLMFIIGLELNPSKLWTLRRSIFGVGAAQVGLSTLLLGGALYLTDFSWQSALIGGVGLAMSSTAMALQLMREKGMNRSESGQLGFSVLLFQDLAVIPALALIPILAGVQGDFGDWERIGLKVAAFLGMLIGGRYLVRPLFRFIAASGVREVFTAAALLLVLGSALFMETLGLSMALGTFIAGILLAESEYRHELEIAIEPFKGLLLGLFFISVGMALNLGILYTHIVKIMVAVLVLVAVKAAVLYFLARVNRMRRSERLQFAGVLSQGGEFAFVLFSAAASFNVLKGEQLPLLLVTVTLSMMTTPLLMQLIDRILARRYNVQDVPDEKPYVEDDEPQVIVVGFGRFGQVISRLLMANKMRITVLERDISAVSLMRSYGYKVYYGDATELELLRSAGADKARSIVITCNAPEDTMEIVHLCQQHFPNLEILARARGRVEAHELLQTGVRHFSRETFSSALELGRKTLVTLGMHPHQAMRAQQHFRRLDMRMLRELMPQLTGDVAQISRVKEARRELEDIFQREMQRERRRPSVWDEDDE", "text": "FUNCTION: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family. KefB subfamily."}
{"protein": "MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKTQRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKLETGPPMGVPPPPPPPPDYMLPPSLHAPEPKALVSGPPSGPLGDFGAPSLPMAVPGPHGPLAGYLYPAFSNRTIKSEYPEPYASPPQQPGPPYSYPEPFSGGPNVPELILQLLQLEPEEDQVRARIVGCLQEPAKSRPDQPAPFSLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVLDHIYRQVQYGKEDSILLVTGQEVELSTVAVQAGSLLHSLVLRAQELVLQLHALQLDRQEFVCLKFLILFSLDVKFLNNHSLVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT", "text": "FUNCTION: Transcriptional activator. Seems to be essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. Binds phosphatidylcholine and phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR5 subfamily."}
{"protein": "MGHIYLKLNERLSQIWCNKYTIIILVMMVKILLFIKMLSNGFENIMDYTMENCRNIDYYYSKYVNSSPHYMGLMGNFLIQKSMEQSVALSLKSISLLVSVSENVIDFMIDLWLGTWVCLIVSAIDGSVDVATNATESVIDLVNGTVSSVADEIDDGLSGLTKVVNKVLSAVNDIQNFFKGNDDESDINDQVKKVNLTINGLRTLSIPSSIDDKLVKLSANTPDFDTVKNKTKQAIAVPFDIIRNEIKSINASKLVGDPQYLEVPAIDTSGVKICSDNKSEINEVFDTIRKVFNASTMTILIVFILAALSLIVYNAWAEWRQWIRLKRFRDQYRHQTIMLKNPFDDMADEKVPQNVDILETYHLVFNRYQSGFGRWLSRRISSKLETQRNIQWLVTYLTSSTSLTLLALGLCGILMCCVQFAIIAIISNKINGKETEKMMTSMSTAMNDTVQQGMTDWSKSANLYINDTETQINRQVFGWIQNTTDTVNGTVTDLIEDIDNAISKAFNGTILYKPMDTVMQCVIGNKLEAISTALTWVHNTAQVNLPRVNGSELYQQLQQNLTDSNSTTSSTAELPNSTSIATQLKDNLISAANKILSQYKNTVVIELIVSSVFLALYFFQIPVAGIILAAQKHKSKHNNQNRP", "text": "FUNCTION: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRM1 family."}
{"protein": "MKKVTVDDFSSPENMHDVIGFYKKLTEHQEPLIRLDDYYGLGPAWVALRHDDVVTILKNPRFLKDVRKFTPLQDKKDSIDDSTSASKLFEWMMNMPNMLTVDPPDHTRLRRLASKAFTPRMIENLRPRIQQITNELLDSVEGKRNMDLVADFSFPLPIIVISEMLGIPPLDQKRFRDWTDKLIKAAMDPSQGAVVMETLKEFIDYIKKMLVEKRNHPDDDVMSALLQAHEQEDKLSENELLSTIWLLITAGHETTAHLISNGVLALLKHPEQMRLLRDNPSLLPSAVEELLRYAGPVMIGGRFAGEDIIMHGKMIPKGEMVLFSLVAANIDSQKFSYPEGLDITREENEHLTFGKGIHHCLGAPLARMEAHIAFGTLLQRFPDLRLAIESEQLVYNNSTLRSLKSLPVIF", "text": "FUNCTION: Cytochrome P450 whose physiological substrate is unknown. In vitro, is able to catalyze the selective hydroxylation of mevastatin to pravastatin, the widely used therapeutic agent for hypercholesterolemia. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MLPTILYSAILALSALTPSALAETRSSGCGKHPSLANGVIHLNGREYILKLPDRYDNNHAYHLVFGLHWRGGNMQNVANGESIQPWYGLETRAQGSTIFIAPNGKNAGWANNGGEDVAFIDAIIKQVEADLCVDQSSRFATGFSWGGGMSYSLACSRAKQFKAVSVLSGGVISGCDGGHDPIAYLGIHGINDGVLPFNGGVGLAQKFVQNNGCQQANIGAPPSGSKSSVRTDFKGCSKPVSFIAYDGGHDSAPLGVGSSLAPDATWKFFMAA", "text": "FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin. Active against paranitrophenyl-acetate, methyl ferulate and wheat arabinoxylan (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the faeC family."}
{"protein": "MAKFKRTDTNRSLENLLDQDKSAQMSKNGGSLAKQPTRKLIPGHGLEFNNLSYSVIKKVKKDGVWINKEAYLLNDISGQALRGEIMAIMGPSGAGKSTFLDALAGRIARGSLEGTVRIDGKPVTTSYMKMISSYVMQDDQLFPMLTVFETFMFAAEVRLPPSISRAEKKKRVHELLEQLGLTSATHTYIGDEGRRGVSGGERRRVSIGIDIIHKPSLLFLDEPTSGLDSTSAFSVVEKVKDIAKSGSIVLMTIHQPSFRIQMLLDRITVLARGRLVYLGSPTGVAAFLAGFARPVPDGENSLEYLLDVIKEYDESTVGLDPLVLYQRDGIKPDQAAKTPVRKPPKTPKIPRTPYAKSPWTKHISLKSSHFSTGNMNSQRDPKDHSDQQSDVNNFDYEDDDDEDEFDKSLERRAPHTPMSMQSGVYPRLASHFYKDFSVWLYNGVKGTPRRPPTWNNNGAIKAPISGSGFKSMSSSQFSMTQQTPGPGNKTPIFTPGRDVIEYSSYNPSYEEVFEIEEVLDEPVHRHKFANPWVREVLVLSWRTTLNVIRTPELFLSREIVLTVMGLVLSSFFKKLSHFDFKTINHLLNFYIFTICLVFFSSNDAVPTFIQERFIFIRETSHNAYRASSYVISSLIVYLPFFAIQGFTFAGITQYILHLNSSILSFWLILYSSLVTSNAYVMLVSALVPSYITGYAVVIATTALFFLTCGFFLKRTQIPLVWRWLHYISAIKYPFEALLINEFKGSKHCYDGDLSDLSPGPLGDVKFSALRNNSRAALPQNCTLIGEDVLFSMDIREENIWLDIVILLAWGVLYRLFFYVVLRFYSKNERK", "text": "FUNCTION: Together with STR2, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Located in the peri- arbuscular membrane of arbuscular mycorrhiza (AM). SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Stunted arbuscule (STR) subfamily."}
{"protein": "FEMQYCWSHSGVCRDKSERNNKPMAWTYCENRQKKCEF", "text": "FUNCTION: Does not show antimicrobial, myotoxic, hemolytic and cell- promoting activities. SUBCELLULAR LOCATION: Secreted."}
{"protein": "QPNLWRCEKDEEFVNCAPRCPQNCRNIRSYQPCLVLTPVCAPGCVCRSGKVKNDRGDCVSITDCFK", "text": "FUNCTION: Serine protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain- containing) family."}
{"protein": "MSASSQQQQSASSSSVASFNGGGFGGGLGIGGGFGGFGGMSSFNAQSSSSYSSSTVINSFASLGSQIAAIQGMMAGGSFTQTIAMQQMSQLAVSMQLALTQSAGCSCLTQVNSSNLDPAVHIYLNRSLSYFYRSLTSFHPSEVYFPNFRH", "text": "FUNCTION: Involved in the development of infection structures. The germ tube elongates across the leaf surface of the infected plant until it recognizes a stomate. Physical stimuli provided by the stomate induce differentiation of the germ tube to form a series of infection structures involved in host colonization."}
{"protein": "MMEMRVGIVGGGLAGLTAAIALAEKGFDVSIIGPRSTDSNSYLAQAGIALPLLEGDSIRIHVLDTIKAGKYINDEEIVWNVISKSSEAHDFLTSHGVTFTGNELEGGHSYPRIFTIKSETGKHIIPILEKHARELDVNFIRGFVEEIGINNGKLAGVFLQGELLKFDAVVIAAGGFSGLYRFTAGVKNNIGLLIGDVALKGVPLRDMEFVQFHPTGFIGKRTYLITEAVRGAGAKLVTGDGERFVNELETRDIVARAIYMKMLEGKGVFLDARGIENFKDRFPYIYSVLRGEGINPEKDLIPITPVAHYTIGGISVDAFYRTRIKGLYAIGESACNGFHGANRLASNSLLECVVSGLEVARTISREKPKREVNDAPYSFNELGDVDSIREVLWNHAGIVRDEWSLREGLRKLKEIEVDERLKLVAKAVIISALKREESRGAHYRKDYPFMRKEFEHSSFFYPNV", "text": "FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily."}
{"protein": "MSEERSKISLRSGGKRKNRPTISAPRQISAPIPQDNGMPQPPPEATMADEPRMTRPRPPPPGGKTSDLVKKRYSTRFGNMPTDFDPSSNPMPALPDLEKYMQAQVGSPPSRGGDAGGLGPMGREPPRVDIRTLRDPNFAPEQYVAEVLGEATEDEIRDYEDALKQLKARAAADLQQNVYQNRTQFIKISKEAEKLKGEMRTLRNLMLELKTNTTALRASSNSADSSGSLGPEFSTGLSKRDRRSSITDRTALWSAQMQALYKSVEGSQKFLPNSQGRHVVQNAGPWIELDNATYKSRRSMQIFLLNDHLLIASRKKRKIDGPGADARGPMTKLVADRCWHLLDVEVVDMAGTGDSSNGRNKLADAIMVRGGGQNESFIYRTEKPEDPEKTTLILNIRKTVEELRRNLQSERDATNKAKETINYFASRDPGLLQKTELLETLSDIKDMLIEVDGKQQNLRWVESQMDELDINIALQQIEPAVARIEMLKNLASGLKNNMIAQDFISFKVDERCARLATLVVRELVNSHNDQKKTKRNVTWLVRLGFEDRAREAYLEARSEVIQKRSRQCIFQGDLHLYIWEISFVYFMVIRNTVICFQSCFPPPMMSACVKWAKEEVDAFNVILARQLSSAEEGGEVWTECVNRAKEHASMLSDVGLDFRNLVGRNVGTSTTVPGGASAGLGLS", "text": "FUNCTION: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis. Also involved in assembly of the spliceosome (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle Note=Cell periphery. The polarization of exo84 requires actin cables (By similarity). SIMILARITY: Belongs to the EXO84 family."}
{"protein": "MENKSRYKTIDHVICVEENRKIHVWETLPKENSPKRKNTLIIASGFARRMDHFAGLAEYLSQNGFHVIRYDSLHHVGLSSGTIDEFTMSIGKQSLLAVVDWLNTRKINNLGMLASSLSARIAYASLSEINVSFLITAVGVVNLRYTLERALGFDYLSLPIDELPDNLDFEGHKLGAEVFARDCFDSGWEDLTSTINSMMHLDIPFIAFTANNDDWVKQDEVITLLSSIRSHQCKIYSLLGSSHDLGENLVVLRNFYQSVTKAAIAMDNGCLDIDVDIIEPSFEHLTIAAVNERRMKIEIENQVISLS", "text": "FUNCTION: Acyl transferase is part of the fatty acid reductase system required for aldehyde biosynthesis; it produces fatty acids for the luminescent reaction. SIMILARITY: Belongs to the LuxD family."}
{"protein": "ADLIQRRQRSEFQSDIKGILYTVIKKNPDL", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the peroxidase family."}
{"protein": "MSLLPTGTLILLVLFILVLITMTKNTSSLNVTKPVSAIAVLEGPVKGTVRFVEESSKVKISVDISGLKPNRKHGFHVHEAGDLTDGCTSACAHFNPFGTAHGGPDSKIRHVGDLGNILADKNGKAKYSFYDSMIKLRGKCNIIGRAIVVHADTDDLGLGGNAESLKTGNAGKRIGCAVIGYAKENFC", "text": "FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family."}
{"protein": "MEHQHNIEDGGKNSNNSFLCRQSSSRWTPTSDQIRILKDLYYNNGVRSPTAEQIQRISAKLRQYGKIEGKNVFYWFQNHKARERQKKRLIAAASATDNNNISSMQMIPHLWRSPDDHHKYNTATTNPGVQCPSPSSHGVLPVVQTGNYGYGTLAMEKSFRECSISPPGGSYHQNLTWVGVDPYNNMSTTSPATYPFLEKSNNKHYEETLDEEQEEENYQRGNSALETLSLFPMHEENIISNFCIKHHESSGGWYHSDNNNLAALELTLNSFP", "text": "FUNCTION: Transcription factor that plays a central role during developmental processes such as early embryogenesis and flowering, probably by regulating expression of specific genes. Required to specify stem cell identity in meristems, such as shoot apical meristem (SAM). May induce shoot stem cells activity in order to maintain the stem cell identity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family."}
{"protein": "MAAEEGGDGRRNMGNPPPPAPAESEEEDDNEMEVEDQDGKEAEKPNMINFDTSLPTSHMYLGSDMEEFHGRTLHDDDSCQVIPVLPHVMVMLIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVREREAHFGTTAEIYAYREEQEYGIETVKVKAIGRQRFKVLEIRTQSDGIQQAKVQILPERVLPSTMSAVQLQSLSRRHIFPSSKPKVWQDRAFRQWWQKYQKRKFHCASLTSWPPWLYSLYDAETLMERVKRQLHEWDENLKDESLPTNPIDFSYRVAACLPIDDALRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQDTEITTKNEIFSLSLCGPMAAYVNPHGYIHETLTVYKACNLNLSGRPSTEHSWFPGYAWTIAQCRICGNHMGWKFTATKKDMSPQKFWGLTRSALLPRIPEAEDELGHDRSPLLCL", "text": "FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 (Probable). Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (PubMed:20223979). Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons. Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (By similarity). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CRBN family."}
{"protein": "MVAIPRLARLSVPAWALSARGRFYATVSTPQTLVEKIVQKYAVGLSEGVKVRAGDYVMIKPEHVMTHDNTGPVISKFLSLSCSKLDNPRQPVFALDHDVQNQSETNQKKYKKIQAFAKEHGVDFYPAGRGIGHQIIVEEGYAWPGKMVVASDSHSNHYGGVGCLGTAIVRTDAAGIWATGKFWWQIPRIVSVSLDGRLSPGVTGKDVIVALAGLFNKDEVLNAAIEFTGSGVEHLSIDERLTIANMTTEWGAVAGVFPVDDKLKEWYQGILRKAELRKFISPTVPSTVGAKVHPRLNAARLDDAMTNRVVADPGAHYAARLSLDLSTLVPHVSGPNSVKVATALPKLLDPPIPINKAYLVSCTNSRASDIASAAQVLRGKKVAPGVEFYIAAASSRVQEDAEAAGDWQTLIDAGAKTLPAGCGPCIGLGVGLLEKGEVGISATNRNYKGRMGSPDAIAYLASPAVVAASAAKGVICGPESMDLSQLPQYEQPKFSIIEEGAAGEEKPVEVDEASLEPLLEGFPAYFEGPLLFAPQDNLTTDGMYPGKYTYQDDITPERQAEVVMENYDPTFAATARELRTALPTASSPSTLPGAILLSGYNFGTGSSREQAATAIKNAGIPLVICGSFGDIFKRNSINNGLILIESPSLIKDMTERFAKDGVRNKGGKDGKLTVVPEGWRIKVDSQRGLVTVNMGEEEEKTYPAAKVGRSVQELWVNGGLEGFIRASL", "text": "FUNCTION: Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the aconitase/IPM isomerase family."}
{"protein": "MLSGKAAYDLFVYGSLQEPEVVYVLLNRVPDHVSAVLSGFHRFRLKGRVYPTILPDGTGKVNGKVLKGITDDELKMLDEFEDVEYDRKTVEVMLTDTSEKLQVETYVWKNKDDPDLYGEWDFEEWRQHDKEDFVTATKKFLENRRLPEAKTRMDTFKTFFKQDLENGKPLDS", "text": "FUNCTION: Putative gamma-glutamylcyclotransferase. SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family."}
{"protein": "MDNIVYDFAKITFQAKDNRSPTTNSNLSWQLNQMALSDMEEMQDTSEPIAPPESDDNVSSESHDSDDVDSQLSRCEDNDDDSDCISGSSRRSSTFGARAGVARRRMPARVSKDNFNRICSAIMKPIKKKQRKELNTNAQTLKSIEKIYTSRRMKKFTPTNLETIFEEPSDENAADAEDDSEECSISSQVKVVKVWGRKLRRAISFSDGLNKNKILSKRRRQKVKKTFGKRFALKKISMTEFHDRLNKSFDSAMLEGDDAEAGGSAEAVNIPKTSMTMEDIQLPTMSSQHQFLMQPAGFE", "text": "FUNCTION: Potential cofactor involved in sensory organ development. Despite its interaction with the Polycomb group protein Asx, it does not regulate the expression of homeotic genes. SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome Note=In embryos, it is predominantly cytoplasmic. In third instar larvae, it is predominantly nuclear or cytoplasmic depending on tissues. Colocalizes with Asx on many binding sites on polytene chromosomes, but does not bind to homeotic genes loci."}
{"protein": "MIAFILLSLAAVLQQSFGTVDFDSESPRRPEKQREIVNMHNSLRRSVSPTASNMLKMEWYPEAASNAERWAYNCITGHSSNPSRVIDGIQCGENIYMSPVPITWTEIIQIWYDENKNFVYGVGANPPGSMIGHYTQIVWYKSYRIGCAAVYCPSTYYSYFYVCQYCPTGNFNGLYATPYKSGPPCGDCPSACVKGLCTNPCTVENKFTNCNTLV", "text": "FUNCTION: Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffeine- stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MEEKSLLQKLRSYPPAVFFMLGNEFCERFSFYGMKTILFIYLITEHEFSPSKATFIYHLFTCIAYLTPLIGSIMADSVFGRFKVILYGSSIYVVGHVLLSLGAVPFLSYPIRSSLDFSGLFVIAFATGCIKPCVSAFAADQFTEDQKDLRSQFFSFFYFAINGGSLFAIIITPILRGRVQCFGNAHCFPLAFGVPGVLMLLALILFLMGWSMYKKHPPSKENVGSKVVAVIYTSLRKMVGGASRDKPVTHWLDHAAPEHSQKMIDSTRGLLNVAVIFCPLIFFWALFDQQGSTWVLQARRLDGRVGHFSILPEQIHAINPVCVLILVPIFEGWVYPALRKITRVTPLRKMAVGGLLTAFSFAIAGVLQLKVNETMEFPPSLGRIYLQRVGNESLISDFRYKSDGRLIGDGMLPKGRTELDAGIYTFNTGLKNESQEIDISTPNKGYVMAVFRLKDAVEVVKFDYKVEKTDNGATRVFVVTAREDADTLVYAINKKGKILSSCELKSGSYVDVIPGIISDPNVRLYWGPKNSCSGVDCPNTVTLNAQMGAVHVLHIHPSTTEGDFNLLVRPNSVSILWSLPQYIIITLGEVLLSVTGLEFAYSQAAPNMKSVLTAMWLLTVFAGNLIDMMISGTRLIPHPALEFFFYSTLMVIVMGVFILLAMQYTYVEDNDDEITITESEKKDVIALTEIESGTATSDKKE", "text": "FUNCTION: Neuron-specific, H(+)-coupled oligopeptide transporter with broad specificity towards di- and tripeptides in a Na(+) and Cl(-)- independent manner. Shows H(+) channel activity in the absence of peptide substrates. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
{"protein": "MTEKEYNTRQTQNYALCPKCLSRIYRNPKDRDNSIIPLINNTQKCSICNNLLLNEDKIFKLILKKIKMLKIEFDTFLIATQINNQTITKNQKEIYKITNYHGNNDIKHQIRRDISRLIEEKLGKTYDYKNPEVVIMVKIRKKPYKHNPYPEISNVNIFIDSNPIFIEGKYRKLVRGIPQTKWPCTHCKGKGCEACDYTGQQYKDTVEDLISREILPMTNGNTTKFHGSGREDIDVRMLGEGRPFVIEVKHPFKRKIDLKFLRVLVNSHSDGKIEINDLKYVTKERKASIKNSSVESYKIYSAIAEFENGVTSKDIYNIEKLKTIDQRTPIRVEHRRADLIRTREIKNIEVERINSKKLHLIIKCQGGLYIKELISGDNNRTKPSVSSITNNQAECTQLDVLKVHIPE", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs. SIMILARITY: Belongs to the pseudouridine synthase Pus10 family."}
{"protein": "MKLGVFELTDCGGCALNLLFLYDKLLDLLEFYEIAEFHMATSKKSREKIDVALVTGTVSTQRDLEVLRDARNRSEYLIALGTCATHGSVQGVIENSKEAYRRVYGNGKPPVKLLNPKPVTDYVPVDFAIPGCPYDKEEVFQVLIDIAKGIEPVAKDYPVCLECKLNEYECVLLKKRIPCLGPVTAGGCNAKCPSYGLGCIGCRGPSLDNNVPGMFEVLKEILPDEEIARKLRTFARW", "text": "FUNCTION: Part of a bifunctional enzyme complex that functions as a hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity exhibited with NAD in addition to NADPH. The alpha and delta subunits form the hydrogenase component that catalyzes the reduction of protons to evolve hydrogen. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family."}
{"protein": "MGMRMMFTVFLLVALATTVVSFTSDRASDRRNAAVKAFDLISSTVKKGCCSHPACSGNNPEYCRQGR", "text": "FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Globular isomer (C1-C3; C2-C4) selectively inhibits neuronal (non- muscle) nAChR subtypes particularly human alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=35.7 nM) and alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs (IC(50)=569 nM), while the ribbon isomer (C1-C4; C2-C3) shows weak inhibition on alpha-3-beta-2/CHRNA3-CHRNB2, but not on all other receptors tested. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily."}
{"protein": "MVGGGGSGGGLLENANPLIYERSGERPVTAGEEDEEVPDSIDAREIFDLIRSINDPEHPLTLEELNVVEQVRIQVSDPESTVAVAFTPTIPHCSMATLIGLSIKVKLLRSLPQRFKMDVHITPGTHASEHAVNKQLADKERVAAALENTHLLEVVNQCLSARS", "text": "FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As a CIA complex component and in collaboration with CIAO1 and MMS19, binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Together with MMS19, facilitates the transfer of Fe-S clusters to the motor protein KIF4A, which ensures proper localization of KIF4A to mitotic machinery components to promote the progression of mitosis. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle. SIMILARITY: Belongs to the MIP18 family."}
{"protein": "MTNYKIDFSKGLVPAILQDNQTKQVLMLGYMNQEAFDKTIEDGVVCFYSRSKQRLWTKGETSGHTQRVKDIHVDCDNDTILIDVIPNGPTCHTGSQSCFNTEVPFSVQTLAQTVQDSAQSNNEKSYTKYLLTEGIEKITKKYGEEAFEVVIEAIKGDKKAFVSEVADELYHLFVLMHALGVDFSEIEAELARRHHKRNNFKGERQNIEQW", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family."}
{"protein": "MALGLSQVASQAASQTLDTAMAGSLTRAAGAQAQKIALDTENSILDGQMDSASKSLNSGQKAAKAIQF", "text": "FUNCTION: Major structure protein of the hrp pilus, which is a component of the type III secretion system (TTSS, Hrp secretion system) required for effector protein delivery, parasitism, and pathogenicity. The hrp pilus functions as a conduit for protein delivery into the host cell (By similarity). SUBCELLULAR LOCATION: Secreted Fimbrium Note=Extracellular and secreted via type III secretion system. SIMILARITY: Belongs to the HrpA type 2 family."}
{"protein": "MAYTGLTVPLIVMSVFWGIVGFLVPWFIPKGPNRGVIITMLVTCSVCCYLFWLIAILAQLNPLFGPQLKNETIWYLKYHWP", "text": "FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family."}
{"protein": "MLPGAWLLWTSLLLLARPAQPCPMGCDCFVQEVFCSDEELATVPLDIPPYTKNIIFVETSFTTLETRAFGSNPNLTKVVFLNTQLCQFRPDAFGGLPRLEDLEVTGSSFLNLSTNIFSNLTSLGKLTLNFNMLEALPEGLFQHLAALESLHLQGNQLQALPRRLFQPLTHLKTLNLAQNLLAQLPEELFHPLTSLQTLKLSNNALSGLPQGVFGKLGSLQELFLDSNNISELPPQVFSQLFCLERLWLQRNAITHLPLSIFASLGNLTFLSLQWNMLRVLPAGLFAHTPCLVGLSLTHNQLETVAEGTFAHLSNLRSLMLSYNAITHLPAGIFRDLEELVKLYLGSNNLTALHPALFQNLSKLELLSLSKNQLTTLPEGIFDTNYNLFNLALHGNPWQCDCHLAYLFNWLQQYTDRLLNIQTYCAGPAYLKGQVVPALNEKQLVCPVTRDHLGFQVTWPDESKAGGSWDLAVQERAARSQCTYSNPEGTVVLACDQAQCRWLNVQLSPQQGSLGLQYNASQEWDLRSSCGSLRLTVSIEARAAGP", "text": "FUNCTION: The 83 kDa subunit binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MVIVTNTSKITKGNGEKLIERFNKVGKVEFMEGFLGLEVLLTENTKDFDEVTVVTRWNTKDDFKNWTKSSAFRDAHSKREVPEYILENKISFYEVKVVRGPLTAAEAGNDSQAQAQ", "text": "FUNCTION: Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the biliverdin in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily."}
{"protein": "MVTDKTNASSSSLVDTPADETEVQPPINRRPTFLDRLMRRQTSPSSMEYSESDKKKDGPMENEQSKGVRESSLPPLSQLSLKGYKSSTKRRLLDDELASNIRNLLPARLQLFDEWDLVYSLEQHGVSLNTLYQRSNPDYQLSQLRKNKPEVGYGDSVISSMMSGNVNSMRERRRPQGYVLIIKDENNSKFGCFVNEHLRPMDQKRYYGNGECFLWKSELFTPSPSNSNSEEDISSHLATPQIRFKAFMYTGINDNIIYSNHDFIAIGSSKGQNGLWIDRSLYNGVSYSCDTFGNEILNSNSGDAKIGKFKIMGLELWRVGTLE", "text": "FUNCTION: May be involved in protection from oxidative damage. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the OXR1 family."}
{"protein": "MSKIFVNPSAIRAGMADLEMAEETVDLINRNIEDNQAHLQGEPIEVDSLPEEIGKLNINEAKPQSFENNPIDIDGRMNEDFQMKEVEDPSIQFQSYLDNIGIQIVRKMKTGERFFKIWSQTVEEIISYVGANFPNPSGKTTESKSTQTTPKKVKPEPPSAPTEKPEQLSRTSMAPETTSGPLALDWSATNDDDDVSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEARGVPGIIRLAKEGLRLPLRCILGWVASSHSKKFQLLVGSEKLSKIMQDDLNRYMSC", "text": "FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus (By similarity). SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm. SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm. SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus. SIMILARITY: Belongs to the lyssavirus protein P family."}
{"protein": "MENSENSVDAKSIKNSETKIFHGSKSMDSGIYMDNSYKMDYPEMGLCIIINNKNFHESTGMPSRSGTDVDAANLRETFTNLKYEVRNKNDLTREQIVALLDSVSREDHSKRSSFICVLLSHGEEGIIYGTNGPVDLKKLTGFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTEDDIACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLRLYAHELEFMHILTRVNRKVATEFESFSLDSAFHGKKQIPCIVSMLTKELYFYH", "text": "FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine- protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C14A family."}
{"protein": "MREYKVVVLGSGGVGKSALTVQFVTGSFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYERVPMILVGNKVDLEGEREVSYGEGKALAEEWSCPFMETSAKNKASVDELFAEIVRQMNYAAQPNGDEGCCSACVIL", "text": "FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells (By similarity). FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading (By similarity). FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Note=Associated with red blood cells- released vesicles. SUBCELLULAR LOCATION: Midbody Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Note=Localizes to midbody at telophase. May also localize to the Golgi and the gelatinase-containing granules of neutrophils. SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Note=Associated with red blood cells- released vesicles. SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side. Note=Associated with red blood cells-released vesicles. SIMILARITY: Belongs to the small GTPase superfamily. Ras family."}
{"protein": "MTAFVPVSLPSTSALNDAYVKSQLTKWDLLRNLRCVAVRYTKYYHKLQGQELLADLFRDEKVQEAFQVLRKGGAWGQLGGPVTKVDATLLASSLTRMDLFDKLTETSPPIVRSNGDIGKCMEDNREGFQVSDQLRELILVEESEHAALFSEAERDELLWRLFEHVVLGGACCQFEDKVEPYVETSKRLYKELVCAQKDPATGKVQTVSAVYKINSIQGDSGPLELYPSRSRQNFCYAAVDPVRRIVKILYHAYVPYW", "text": "FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Plays a role in outer and inner dynein arm assembly. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, flagellum axoneme Note=Localizes predominantly in the cytoplasm and weakly in flagella. Transported to the flagellar matrix in an intraflagellar transport (IFT)-dependent manner. SIMILARITY: Belongs to the CFAP300 family."}
{"protein": "MAQPLILGVSGASGLIYAVRAIKHLLAADYTIELVASRASYQVWQAEQNIQMPGEPSAQAEFWRSQAGVEKGGKLICHRWGDVGATIASGSYRCAGMVVLPCSMSTVAKLAVGMSSDLLERAADVQIKEGKPLVVVPRETPLSLIHLRNLTSLAEAGVRIVPAIPAWYHQPQSVEDLVDFVVARALDQLAIDCVPLQRWQGGMEGE", "text": "FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN. SIMILARITY: Belongs to the UbiX/PAD1 family."}
{"protein": "MAKHFRIGMIVPSSNTTMETEIPAMLQSRMKEIPEETFTFHSSRMRMMHVTKEELKKMDEESDRCAIELSDARCDVLAYACLVAIMCQGPGYHEKSEARLASLTAQNGGAAPVISSAGALIDGIRTLGAKKIALIAPYMKPLTNQVIEYITASGIEVTDSISLEIPDNLEVGRQDPMRLIEIVKNLDVSNADAVVLSACVQMPSLPAIQKVQDQLGLPVLSAATSTVYKILKSLNLKTYVPNAGSLLSGKY", "text": "FUNCTION: Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. SIMILARITY: Belongs to the maleate isomerase family."}
{"protein": "MKVLRAWLLCLLMLGLALRGAASRTHRHSMEIRTPDINPAWYASRGIRPVGRFGRRRATLGDVPKPGLRPRLTCFPLEGGAMSSQDG", "text": "FUNCTION: Stimulates prolactin (PRL) release and regulates the expression of prolactin through its receptor GPR10. May stimulate lactotrophs directly to secrete PRL. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTRTLLSWPGGRRLKWLVLAAWIGLLIVLQPLAGKLGDVESNDAAAWLPGNAESTEVLELSEKFQPADTSPTVIVYDRPSGITAADEAKARADATHFADGTGVVGEPYGPVRSDDGKALRTVVNVHLGKDGWEGLNAAAKDMRAIARPSAPDGLGVHVTGPTGYAADSAESFSSADFKLTLVTLLIVVTILVVTYRSPLLWLLPMISAGMSLVISQAIVYLLAKNAGLTVNAQTAMILTVLVLGAATDYALLLVARYREELRRHEDRHEAMAVALRRAGPAIVASAATVAVSMLVLLLAALNSTKGLGPVCAVGVLVGLLSMMTLLPALLVIFGRWVFWPARPKHGTEPDVTRGLWSRIARLVSGRPRAVWVTTSLLLGAVATLAVTLNADGLQQKDGFKTKPESVVGEEILTRHFPAGSGEPMVVIAKGASADQVHAALETVPGVIEVAPPQVKDGLAYVEATLGAGADSPAAMRSVTAARETLARLDGAQARVGGSSAVVHDMREASSRDRGLIIPVILAVVFCILALLLRALVAPLLLIASVVLSFFTALGLAALFFNHVFDFAGADSAFPLWVFVFLVALGVDYNIFLVTRIKEESDRLGTRQGALKGLTSTGGVITAAGLVLAGTFAALATLPLVFIAELGFTVAVGVLLDTMIVRSVLVTALTLDVGRWMWWPHPLARREDPSEDPAVSGMPDSIDSEASTTASR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily."}
{"protein": "MSHLSTINACKLLLFRRCLQAVLLTVGIQFLLLTIFLLFVNFQLLRPLHWISVTLSLVCSMYTWFASIPLVGAVVLYGMILCQQHLAERLYCPTRFRWLVHYAPRKLLFLAAHLLVGYLTAWLYTGYMHTDYRHLWYKCYDQECISAYHVYLLGMGIFAGCYYFVSVHMRQEVEIEFPIVNHLWGEKLREVLYSSLARSLIKSLLPTLAYTLLFWLFGGVVCHKLSHIFAVDLDERLEGFFGVATNGRLLFYGWLLTSQILSNMHLMRCFYSMFLSEEFPLAITKNRAAFVQEKEVTVVAALGLSNVYVVQCLAAKYLYNLVTAGDAEKRSELFQLTEPGNRPANWRSLCDQCLSLFGNFTDELIDSMQKISVLKGSPSSPPLTPISENASASLMAERVLTRQYNQMHGIRAIVSPRSNAVIDRPVDRIHRVPDWCERTSMQLEQSLQLLINRIPGIVYMFTEPEGAKTAFLLTHSLPLVFVIQALSQICVFSLKEDRYGVVQTDLPDIIRSMSRLKGELDKLSSVASNLRGPGSSFSVLRGAVRRSLFHICVAFGEYLSELIPSGEELHQLQTVINQE", "text": "FUNCTION: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Multi-pass membrane protein Note=Central core structure of the nuclear pore complex. SIMILARITY: Belongs to the NDC1 family."}
{"protein": "MLFRYLVWLFRFIEVKNVASISLLVIGSNSLTTAISNNTSTTILPTTSSNSLMTAIPNNTSTTISPTTSSNYLTSAISTNISDKEEDTPFSTDKTVFDGLSPITLYRTIRSTLNDTSTKTMTDHILTRPYRPTTVIFHSDTPQPVKNATQGNIIKKTYRQVLTFFIQPNPLFPCFKNHEVFLNLANILNTILCIILIKNV", "text": "SIMILARITY: Belongs to the asfivirus I196L family."}
{"protein": "MTTLDDKLLGEKLQYYYSTSEDEDSDHEDKDRGRGAPAISSTPAEAELAGEGISINTGPKGVINDWRRFKQLETEQREEQCREMERLIKKLSMSCRSHLDEEEEQQKQKDLQEKISGKMTLKEFGTKDKNLDDEEFLQQYRKQRMEEMRQQFHKGPQFKQVFEIPSGEGFLDMIDKEQKSTLIMVHIYEDGVPGTEAMNGCMICLATEYPAVKFCRVRSSVIGASSRFTRNALPALLIYKAGELIGNFVRVTDQLGEDFFAVDLEAFLQEFGLLPEKEVLVLTSVRNSATCHSEDSDLEID", "text": "FUNCTION: Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers (PubMed:23637185). Acts also as a positive regulator of hedgehog signaling and regulates ciliary function (PubMed:29290584). SUBCELLULAR LOCATION: Cell projection, cilium. SIMILARITY: Belongs to the phosducin family."}
{"protein": "MGSRSRTPSPSGKRRHHKSKHKKRSKSHHDHERPSTRTDRDKSSEVNNHGRHRERDRDRERDRHRSDRHTERDYRHSPSILKSRKRSSSSSSDSQYSEQESQRSKQKRSRFKKLDEQNQMQVERLAEMERQRRAKELEQKTIEEEAAKRIEMLVKKRVEEELEKRRDEIEQEVNRRVETAKAEMEREMMLELERRREQIREEERRREEDEKQKREELEEILAENNRKIEEAQRKLAEERLAIIEEQRLMDEERQRMRKEQEKRVKEEQKVILGKNNSRPKLSFSLKPGAL", "text": "SIMILARITY: Belongs to the UPF0430 family."}
{"protein": "KFELQPPPYPMDALEPHMSSRTFEFHWGKHHRAYVDNLNKQIDGTELDGKTLEDIILVTYNKGAPLPAFNNAAQAWNHQFFWESMKPNGGGEPSGELLELINRDFGSYDAFVKEFKAAAATQFGSGWAWLAYKPEEKKLALVKTPNAENPLVLGYTPLLTIDVWEHAYYLDFQNRRPDYISIFMEKLVSWEAVSSRLKAATA", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MAAPSSNYQLYGLKIGFPPGGLMRNKQMKFNDYGITVKEAIQIITNKQGMQNPDSYTLQITYSDEPSSINTSSGNIGSNNNSSSNTPLTGSLGMGPPPPSASIGGGGGGGDNGITNSGNIGSSSNSDLKKSTSSGIVNVNNSSNAPTRRLKWMDDNEKLISYPLGAHDVVIELKKKYQLIKVYDGKQTMNLIVDITKPLSDLMDLVSCKFKLRSTSDCKLFTYGKEINLNSNIKNLNIDTSLPFILRDNNDPNSLSLESIQWDNGNGFFVGGNGGIGGIGSDDDADDINNNLSVPAKSIINPVREGYLKKQDKKKSWKTRYFKLTDKYLYWYKSPTAIKASGMIICKDYHIKLAPSTHSKEVKLEFTPKHMIAGATTIIHYIKFENEQELKQWTVLPIVIESSNDSGSNNSNTSGGNQSMIGKKVFGVPIEKTVSGNNEIPAVVLQTIDYIEKKAMDIVGIFRLSGSVLTIEQWKAKYDKGEKVDLFQEVDPHAVAGLLKLYLRELPDPLLTYEKYDNFIAAQSIDDFPSRIKLIKHLVKSLPPVNYAVLSYLMAFVGKVATHSAANKMQVHNLSTVFGPNLIKDRQDSGDYGNNVQVLVEDTPIINALALSLIRDYQYIFTDKEIPEQKILAKSLYEYAGNDDGTTSEDDKDLLFPKGATIKVTQQGTDGWWTGEYQGKQGKFPASYVELLPHSPSTLLRTKSNSNLTKKKKFMLEMESTKTKNQEIDKNIKQLEITKKELESTINDLENEKAALENDPTIKAMMNLLANAKTNKDIAMIPKNIDVLFQKFEEYKSSHEALATTKTTLIDEYEQFNNNPKKRLDTKEKEQIQQKYDNLSIIIDKSQKIRSKSINSKKIINDDLVELKKIFSL", "text": "FUNCTION: Rho GTPase-activating protein involved in the signal transduction pathway. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MADEQEIMCKLESIKEIRNKTLQMEKIKARLKAEFEALESEERHLKEYKQEMDLLLQEKMAHVEELRLIHADINVMENTIKQSENDLNKLLESTRRLHDEYKPLKEHVDALRMTLGLQRLPDLCEEEEKLSLDYFEKQKAEWQTEPQEPPIPESLAAAAAAAQQLQVARKQDTRQTATFRQQPPPMKACLSCHQQIHRNAPICPLCKAKSRSRNPKKPKRKQDE", "text": "FUNCTION: Plays a role in interneurons differentiation (PubMed:26056227). Involved in neuronal development and in neuromuscular junction formation. FUNCTION: Plays a role in interneurons differentiation. Involved in neuronal development and in neuromuscular junction formation. SUBCELLULAR LOCATION: Cytoplasm Nucleus Postsynaptic cell membrane. SUBCELLULAR LOCATION: Cytoplasm Nucleus Postsynaptic cell membrane Note=Upon transfection into mouse primary hippocampal neurons, localizes at excitatory, but not inhibitory, postsynaptic sites."}
{"protein": "MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEDVAFKDLDVAILVGSMPRRDGMERKDLLKANVKIFKCQGAALEKYAKKSVKVIVVGNPANTNCLTACKSAPSIPKENFSCLTRLDHNRAKAQIALKLGVTSDDVKNVIIWGNHSSTQYPDVSHAKVKLHGKEVGVYDALKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAICDHVRDIWFGTPEGEFVSMGIISDGNPYGVPDDLLYSFPVTIKNKTWKVVEGLTINDFSREKMDLTAKELAEEKETAFEFLSSA", "text": "FUNCTION: Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family."}
{"protein": "MSETAEKAIEIWKIRRLVKQLINCHGNGTSMITLIIPPGEQISRYSNMLAEEYGTASNIKSRVNRLSVLSAITSTRERLKLYNKVPDNGLVIYCGEVIMEGNKTRKLNIDFEPFKPINTSQYLCDNKFHTEALAELLESDQRFGFIVMDGHQTLYGVVSGSAREVLQRFTVDLPKKHGRGGQSALRFARLRDEKRHNYVRKVAEGAVQHFITDDKPNVAGIVLAGSADFKTELGQSDLFDQRLQSRIIKTVDVSYGGDAGFNQAIELAADTLSNVKYVQEKKLIQRFFDEISLDSGKYCFGVVDTMNALQEGAVETLLCFADLDMIRYEFKNSEGNPVITYMTKEQEEKDSTNSFLLDKDTGAEMELVSSMLLSEWLAEHYKDYGANLEFVSDRSQEGMQFVKGFGGIGAVMRYQLDLSMLDPESDEFYSDSD", "text": "FUNCTION: Component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons (PubMed:19417105). The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:19417105). Sup45/eRF1 is responsible for stop codon recognition and inducing hydrolysis of peptidyl-tRNA (PubMed:19417105). Following GTP hydrolysis by sup35/eRF3, sup35/eRF3 dissociates, permitting sup45/eRF1 to accommodate fully in the A-site (PubMed:19417105). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family."}
{"protein": "MNHKSKKRIREAKRSARPELKDSLDWTRHNYCETFPLSPAACKDNVERADALQLTVEEFVERYEKPYKPVVLLNAQVGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMETTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVAREEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASCTNFPVVWHKTVRGRPKLSRKWYRILKQEHPDLAALADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSECDSGSETEGMMHRRKKRRTCSMMGNGDTTSQDDCVSKERSSSRIRESCGGRSYP", "text": "FUNCTION: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5- hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation. Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. Demethylates other arginine methylated-proteins such as ESR1. Has no histone lysine demethylase activity (By similarity). Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus Cytoplasm Note=Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the cell cycle. SIMILARITY: Belongs to the JMJD6 family."}
{"protein": "MKKITGIILLLLAVIILAACQANYIRDVQGGTVSPSSTAELTGVETQ", "text": "FUNCTION: Lysis proteins are required for both colicin release and partial cell lysis. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor."}
{"protein": "MADGSGARFPRFSELCAKYAAQLAAAETRSVYAFSARPITGGEPVSLGFLRGRVLLIENVASLUGSTVREYTQMNELQRRLGARGLVVLGFPCNQFGHQENAQNAEILPSLKHVRPGNGFEPNFMLFEKCEVNGARAHPLFAFLREALPAPSDDMSTLVSDPQLIAWSPVCRNDVAWNFEKFLVGADGTPVRRYSHRCQTLAVEPDIEALLPPPARGYYA", "text": "FUNCTION: May protect the virus and component of infected cells from oxidative damage by peroxides whose formation may be stimulated by infection. SIMILARITY: Belongs to the glutathione peroxidase family."}
{"protein": "MKEDSPPTVCVTGAAGFIGSWLVMRLLERGYIVRATVRNPGDMKKVKHLLELPKAETNLTLWKADLTQEGSFDEAIEGCHGVFHVATPMDFESKDPENEIIKPTIEGILSIIRSCAKAKTVKKLVYTSSAGTVNVQETQLPVYDESHWSDLDFIYSKKMTAWMYFVSKTLAEKAAMEAAKENNIDFVSIIPPLVVGPFINPTFPPSLITALSLINGAESHYSIIKQGQYVHLDDLCECHIFLYENPEAKGRYICSKQDATIHQLARMIKQKWPEYHVPTQFAGIDEELPTVSFSSKKLIDMGFKFKYDLEDMFKGAIDSCKEKGFLPYSTNEVKKGLFESSINGNVHGQKGNQKIGDEGVKLVN", "text": "FUNCTION: Bifunctional enzyme involved in flavonoid metabolism. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily."}
{"protein": "MSARITPQTPALQALRMRLHAQHQPVVLMRTDCHVCRAEGLAPRSQVLIIAGDRTVQALLYQIDSDLLKTGQIALSEAAWDALDIHEGDLVQVRHPPLLESLSAVRARIHGHRLQTTELQAIVRDVVDGRYTDVALSAFLTATAVLPLDMQETIHLTRAMVDVGDHLQWQAPIVVDKHCVGGLPGNRTTPLVVAIAAANGLVMPKTSSRAITSPAGTADTMETLAPVDLDLDTLRKVVEKEGGCVAWGGAMHLSPADDIFVRIERELDIDTQGQLIASVLSKKIAAGATHIVIDIPVGPTAKVRSRETAEHLAHHLSEVAASFGLVLRCLFTDGNQPVGRGIGPALEARDVLAVLRNEADAPQDLCDRVALVAGAVLELGGVAKEGDGIRLAHETISSGRAWEKFQRICAAQGGFREPPQALYVEPLLATTSGRAVHIDNRKLSRLAKLAGAPESPAAGIQLQVRLGDEVTRGQSLMFLHAQTSGEMAYALAYVHDIGDIVKIEP", "text": "SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily."}
{"protein": "MDNSHDSDSVFLYHIPCDNCGSSDGNSLFSDGHTFCYVCEKWTAGNEDTKERASKRKPSGGKPMTYNVWNFGESNGRYSALTARGISKETCQKAGYWIAKVDGVMYQVADYRDQNGNIVSQKVRDKDKNFKTTGSHKSDALFGKHLWNGGKKIVVTEGEIDMLTVMELQDCKYPVVSLGHGASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDANECHLNGHDREIMEQVWNAGPWIPDGVVSALSLRERIREHLSSEESVGLLFSGCTGINDKTLGARGGEVIMVTSGSGMGKSTFVRQQALQWGTAMGKKVGLAMLEESVEETAEDLIGLHNRVRLRQSDSLKREIIENGKFDQWFDELFGNDTFHLYDSFAEAETDRLLAKLAYMRSGLGCDVIILDHISIVVSASGESDERKMIDNLMTKLKGFAKSTGVVLVVICHLKNPDKGKAHEEGRPVSITDLRGSGALRQLSDTIIALERNQQGDMPNLVLVRILKCRFTGDTGIAGYMEYNKETGWLEPSSYSGEEESHSESTDWSNDTDF", "text": "FUNCTION: ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination (PubMed:21606333, PubMed:22977246, PubMed:32009150). The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis (PubMed:21606333, PubMed:22977246, PubMed:32009150). ATP or dTTP hydrolysis propels each helicase domain to translocate 2 nt per step sequentially along DNA (PubMed:30679383, PubMed:17604719). Mediates strand transfer when a joint molecule is available and participates in recombinational DNA repair through its role in strand exchange (PubMed:9096333, PubMed:8617248). Primase activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the lagging strand that the polymerase elongates using dNTPs and providing the primase is still present (PubMed:6454135, PubMed:9139692). SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family."}
{"protein": "MPIINGQKMACGPCIRGHRSTKCNHYNERVMVPVRKPGRPLSTCPCPPGKPCVCGGVRVAIPKKQKCHCPAGTVDSATSSEFDPSPVDTPISPASRTSSNRVTKSGSGSKSASRRQSLALANLERMDPNSINLIPSPNGNGMIGITAMVSPRDATFGHPMGMVPMGPRESFVPAPPPDFGGPMGYNMPPSMPPHMPPPHYPPHIQIPQHIKTENGGFVPMLNGTFVSPVPIPAFVDGPHPQGMQAFNGPPPPPPSNPVLEPSAMSKPKGGSGGGGCCGGGKKAPQIQAPPPVPAPLPTPPQQQMPNIMPPPQPQNAPSGGGGSCCSSKSSQPPPMPQMSPNAMQAPPQPGFGQGFMPQYQTPIDIKMENMHHHQPFQFPGQTVFTYPAEYGSWQMPINPAIWQQVVSRPPTQQQHETPISATAPNGNNGTVGGNSHECGCGEGCQCVGCLAHPFNSQMLQYVQNAYSPNSSHGNSGSADSSANASPSANPLNLASPVEIPSGPELPPSHQTQPQPPPRPNANESDGSSNAPTPPNEGSPALSNEEELTALDYYFVHLPISALCGGALDMCPCDESCECVGCLVHNTAGFPQGDGGFS", "text": "FUNCTION: Copper-sensing transcription factor that regulates copper uptake by transactivation of Ctr3, a high affinity copper permease. Binds to the palindromic UAS sequence 5'-TGTTGCTCANNNNAGAGCAACT-3'. Also transactivates Sod2, a mitochondrial manganese superoxide dismutase through the palindromic UAS sequence 5'-GTTTGCTCA-3' with 352 bp separating the two inverted repeats. Loss of function indirectly leads to rearrangement of mitochondrial DNA associated with senescence in wild-type strains. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNTSVPTSVPTNQSVWGNVSTGLDALISGWARVEQIKAAKASTGQGRVEQAMTPELDNGAAVVVEAPKKAAQPSETLVFGVPQKTLLLGFGGLLVLGLVMRGNK", "text": "SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Note=Part of the capsid inner membrane. Deeply embedded in the lipid bilayer. About 20% of the molecule extends to the exterior."}
{"protein": "MKNKVFASIGDAVKDIKVGRMVIVVDDPGRENEGDLICAAEKASPEVINFMTKYARGLICVPMKHERLKELEIENMVEKPTEKKGCSFTVSVDYKIGTTTGISAYDRSVTVRKLIDKTAKHEDFARPGHIFPLRCKEGGVLARTGHTEAAVDLVRLAGFYPAGIICEIMNNDGTMARMSDLIKFAKKHDLHIITIGELVNYRRRTEKFISEIVNVDLPTRYGDFKLVLFEDLITKDSHIAVVKGVVKNRQNVLVRVHSSCETGDIFHSLRCDCGDQLETALKAVGEAEQGVVLYIHQEGRGIGLANKLKAYRLQEKGMDTVEANKALGFDPDLRDYGIGAQMLSELGIKSINLMTNNPGKINGLESYGLKITKRVPLEISPSKSNEKYLKTKKEKMGHMLKKV", "text": "FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. SIMILARITY: In the C-terminal section; belongs to the GTP cyclohydrolase II family. SIMILARITY: In the N-terminal section; belongs to the DHBP synthase family."}
{"protein": "MFVFVGSTVSLTAIVAAPVLTWIWANHLEPNLLKLTRLDWRLPKKFAHLHGLRIVQISDLHLNQSTPDAFLKKISRKVSSLSPDMLVFTGDFICRAKVESSNKLKNFLCSLNAPLGCFACLGNHDYATYVSRDIHGKINTIPETSSRPLRRALTSVYQSLFSSSHNEFAEEFTPQDPNPHLLSILHNTPFQLLHNQSVTLSDVVNIVGLGDFFAKQFDPKKAFTNYNPTLPGIILSHNPDTIHYLKDYPGDVVFSGHSHGPQISLPWPKFANTITNKLSGLENPELARGLFSFPQEKRLLYVNRGLGGWKRIRFFSPPEICIMRCLYEP", "text": "FUNCTION: Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to form 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipooligosaccharide (LOS) to the outer membrane of the cell. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the metallophosphoesterase superfamily."}
{"protein": "MPKSGRDGGASKDSKYDLSKISARVDRVNVSGLLRTHNDYVMRAADGLFKASNFQDLMLEAMSTKSYLHELGIFKDVSVHIDVSRGADASPQGYEVTFKGNEMSRMMGSAGTEIGQNEGSLRTELTIPNILGRGENISLQGSYSSTRANDLQLKFWKPFFHTRFKENRPEMSFSIFRQTDRFDISSFQTTNIGYLVDFSAHTMVGVDLTHSLQYENAIRDVGLLNKSVPFAIRDHCGPKLASLLRYSVVYDNRDGNVFPTRGIYLKSVNEYCGLGGNVAYTSSTAHGELNVPLFAGLVAQFCARVGVVKETKNTTQLPISSLFYCGGPLTLRGFKFGGAGPVVESTPIGAQSFWCTGAHLWAPLPFAGVFKNLASHFRMHFFYNIGNNNSFSTENMRSAFGMGLAVKLAERARIELNYCVPVRHQDTDRILNGFQFGIGYEFV", "text": "FUNCTION: May play a role in the maintenance of the structure of mitochondrial cristae. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SAM50/omp85 family."}
{"protein": "MAGIVTEPWSVAENGNPSITAKGSSRELRLGRTAHNMSSSSLRKKSDLRVIQKVPYKGLKDFLSNLQEVILGTKLAILFPAIPAAIICTYCGVSQPWIFGLSLLGLTPLAERVSFLTEQLAFYTGPTLGGLLNATCGNATELIIAILALTNNKVAVVKYSLLGSILSNLLLVLGTSLFCGGIANIRREQRFDRKQADVNFFLLLLGFLCHLLPLLVGYLKNGEASAAVLSDMQLSISRGFSIVMLISYIAYLVFQLWTHRQLFDAQEQEDEYDDDVEQETAVISFWSGFAWLVGMTLVIALLSEYVVATIEEASDKWNLSVSFISIILLPIVGNAAEHAGAVIFAFKNKLDISLGVALGSATQIGLFVVPLTIIVAWILGINMDLNFGPLETGCLAVSIIITAFTLQDGSSHYMKGLVLLLCYFIIAICFFVDKLPQKQNAIHLGHQAMNNVVTATGGGVFSS", "text": "FUNCTION: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase. Involved in ion homeostasis in association with CAX3. May play a role in cold-acclimation response. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/proton exchanger (CAX) subfamily."}
{"protein": "MSEPQKSEPQKSEPQNGRGALFAGGLAAILASACCLGPLVLIALGFSGAWIGNLTVLEPYRPIFIGAALVALFFAWRRIYRPAQACKPGEVCAIPQVRATYKLIFWIVAALVLVSLGFPYVMPFFY", "text": "FUNCTION: Involved in mercury resistance. Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MerT family."}
{"protein": "MWGYFFGGNSQQKKDLPKKAIVELREHIQTLNKKKNHLQQQMDDQDQLARKYVSSKQTTLAKSALKRKKGYESNLLKVENQIETLETQLISIEGANLNLETMKAMKQGAKAMKQIHGEYDVDKVEDTMDEIREQVELADEISEAISRPVGNEFVDEDELDEELKELEAEAKEQEQEHRVPAQKAKPQPVSREEELPQFPSVNKKAPVVEEDEDEEALKALQAEMGL", "text": "FUNCTION: Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Also required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. SUBCELLULAR LOCATION: Cytoplasm Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNF7 family."}
{"protein": "MDFSGLFLTLSAAALFLCLLRFIAGVRRSSSTKLPLPPGTMGYPYVGETFQLYSQDPNVFFAAKQRRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQAIFFHQGDYHSKLRKLVLRAFMPDAIRNMVPHIESIAQESLNSWDGTQLNTYQEMKTYTFNVALISILGKDEVYYREDLKRCYYILEKGYNSMPINLPGTLFHKAMKARKELAQILANILSKRRQNPSSHTDLLGSFMEDKAGLTDEQIADNIIGVIFAARDTTASVLTWILKYLADNPTVLEAVTEEQMAIRKDKKEGESLTWEDTKKMPLTYRVIQETLRAATILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHNADIFSDPGKFDPSRFEVAPKPNTFMPFGSGIHSCPGNELAKLEISVLIHHLTTKYRWSIVGPSDGIQYGPFALPQNGLPIALERKP", "text": "FUNCTION: Involved in the oxidative degradation of abscisic acid, but not in the isomerization of the produced 8'-hydroxyabscisic acid (8'- OH-ABA) to (-)-phaseic acid (PA). Involved in the control of postgermination growth. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSTKKKPTITKQELYSLVAADTQLNKALIERIFTSQQKIIQNALKHNQEVIIPPGIKFTVVTVKAKPARQGHNPATGEPIQIKAKPEHKAVKIRALKPVHDMLN", "text": "FUNCTION: DNA-binding protein that plays a critical role in nucleoid compaction, genome replication and DNA replication and transcription (By similarity). Binds to both ssDNA and dsDNA with a binding site covering about 15 nucleotides (By similarity). Displays DNA- supercoiling activity only when associated with the viral DNA topoisomerase 2 (By similarity). FUNCTION: DNA-binding protein that plays a critical role in nucleoid compaction, genome replication and DNA replication and transcription (PubMed:28381576). Binds to both ssDNA and dsDNA with a binding site covering about 15 nucleotides (PubMed:28381576). Displays DNA- supercoiling activity only when associated with the viral DNA topoisomerase 2 (PubMed:28381576). SUBCELLULAR LOCATION: Virion Note=Found in association with viral nucleoid. SUBCELLULAR LOCATION: Virion Note=Found in association with viral nucleoid. SIMILARITY: Belongs to the bacterial histone-like protein family."}
{"protein": "MSWNQYPGGGHHQQGGYGYRPPPPQWAQQGPPPPPNMGYRPPPPPQAYYNNPPPPQQYQRPAPQQNGYQQGGYQQQQQSQGNYRTSNGGYVPPTGAPVEASYHHTGAGYTPPSGTPQRTSAPYGAGAPIRPPSQAQHYGPQLQGQGGQSAQPYFQYSQCTGKKKALCIGINYVGSSSALAGCINDAHNVQKFLIERYGYKSEDIVMLTDDARNPRQIPTRANILAAMHWLVQGAQPNDSLFFHYSGHGGQTPDLDGDEDDGYDEVIYPLDFKTAGHIVDDDITDCKGRHNIMVRPLPAGCRLTAIYDSCHSGTALDLPYIYSTEGVIKEPNLLAEAGQGLLSAGMSYLRGDTGGMLQGIMGIGKKVMNQNSGAMEKARQTKTSPADVISWSGCKDSQTSADTQEAGRATGAMSYAFIAALTKYPQQSYVQLLNTIRDELKGKYDQKPQLSASHPMDTNILFIC", "text": "FUNCTION: Involved in cell death (apoptosis). SIMILARITY: Belongs to the peptidase C14B family."}
{"protein": "MSEFWHKLGCCVVEKPQPKKKRRRIDRTMIGEPMNFVHLTHIGSGEMGAGDGLAMTGAVQEQMRSKGNHRDRPWSNSRAL", "text": "FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T- cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the CDC42SE/SPEC family."}
{"protein": "MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSIISPSSYENVSGKWGPEVFHHAPNVPIILVGTKMDMREDKETQDRLKEKKLYPVSYEQGLLKMKEINAFKYLECSALTQKGLKTVFDEAIRSVINPPVKKSKSKSGCNIL", "text": "FUNCTION: Overexpression promotes the formation of filopodia and membrane ruffles. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MISFSHWNSHIRSGLSLSMIPSANSRFAFIIQRNYIPVVNSQNTRWKRLCGTQSVWSPYKKKHVLVNRLKHISLFPKPIFARKFTTRQKSEDQKQWRILRITFLVLPFTVGGLWILYRVKNRKNNIFSFDELELEERSNRPRSIFGKIKQFFNILLRSFNLFIIFSPIIITLPFIALISFLHLRSLSSLTVSIWLRFLVTQLERAGATFIKLGQWAASRTDLFPPAFCKTLSKLHSHVTPHSLAYTQSVICKTYKVESIEEIFVNFNPIPIGVGAIAQVYTATIKKAATQQDNSYFTSMLQSIGFRQKNISDAPVTQDVAIKVLHPNVEKYISLDLQILGFFAKLINLVPSMKWLSLPDEVKVFGAMLNQQLNLHYEALHLNQFRLNFRGNRYVEFPAPYDDYTTNQILLEDYMPGIPLSAFLKHKSGPFNKLLANTGNNALFQMLIVDNFTHADLHPGNVLVKFYKGIPKTIFNQDNEINDSIYKILSTCSTEEWDSAMEELNILGYRPTLVFLDAGLVTKLSTQDQKNFLDLFQAVLTFHGYEAGLLMVERSRQTERVINKDIFALKMEHLLNEIQKSTLSLKSLQIGTILQEVMTMAREHHVRIEANFANTVLSILLVEGAGRQLYPEMDLLSNATPYLRSASSKSNVSLTNPMVQLWIALEARQFLLLSTSKETVEKWVKSDMIAPNI", "text": "SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein kinase family."}
{"protein": "MRGREVPLVLLALVLCLAPRGWAAPVTAGRGGALAKMYTRGNHWAVGHLMGKKSVAESPQLHEEESLKEQLREYAQWEEATRNLLSLLQAKGARGHQMPPWEPLSIHQPAWDSEDVSNFKDTGPQHEGRNPQLN", "text": "FUNCTION: [Neuromedin-C]: Induces an itch response through activation of receptors present on mast cells, triggering mast cell degranulation. FUNCTION: Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (By similarity). Contributes primarily to nonhistaminergic itch sensation (By similarity). In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to act on vasoactive intestinal peptide (VIP)-expressing cells in the auditory cortex, most likely via extrasynaptic diffusion from local and long-range sources, to mediate disinhibition of glutamatergic cells via VIP cell-specific GRPR signaling which leads to enhanced auditory fear memories (By similarity). Contributes to the regulation of food intake (By similarity). Inhibits voltage-gated sodium channels but enhances voltage-gated potassium channels in hippocampal neurons (By similarity). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen Secreted Cell projection, neuron projection Note=In neurons of the retrotrapezoid nucleus/parafacial respiratory group, expressed on neuron projections which project into the pre- Botzinger complex. SIMILARITY: Belongs to the bombesin/neuromedin-B/ranatensin family."}
{"protein": "MIKLSTVQLAQILQAKLIGDENVQVEKINTDTRKSVSNSLFFALKGEKFDAHQYLDQAVSQGALALVVQQENSSISVPQLVVKDTRIALGELAKWLREKINPRTVAMTGSSGKTTVKEMTASILQHTAADSEAVLFTNGNFNNDIGVPLTLLRLTEKHRFAVIELGANHQNEINYTTKLVQPNAALINNIAPAHLEGFGSLAGVVQAKGEIYRGLTKNGVAIINAEHNHLDIWQKEISNHAIQYFNGKDYSAKNIHHTSQGSTFTLISPQGEIEITLPYLGEHNVKNALAATALAMNVGATLTDVKAGLEQRSQVKGRLFPIQVTPNLLLLDDTYNANKDSLCAAIDVLKGYDAFRILCVGDMKELGENSLAIHREVGQYINLVNLDLVCSYGNESAVISEAVSGKHFTDKTEMVDFLVPLIENQLQQNKKVVVLGKGSRSMKMEDVIYSLKDKIKC", "text": "FUNCTION: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family. MurF subfamily."}
{"protein": "MDDTQHFCLRWNNYQSSITSAFENLRDDEAFVDVTLACEGRSIKAHRVVLSACSPYFRELLKSTPCKHPVILLQDVNFMDLHALVEFIYHGEVNVHQKSLQSFLKTAEVLRVSGLTQQQAEDTHSHLAQIQNLANSGGRTPLNTHTQSLPHPHHGSLHDDGGSSTLFSRQGAGSPPPTAVPSLPSHINNQLLKRMAMMHRSSAAAAAEETSHAFKRLRGSDNSLPLSGAVGSGSNNNSPDLPPLHARSASPQQTPADFSTIKHHNNNNTPPLKEEKRNGPTGNGNSGNGNGNGNGASNGNGISISDKLGSLTPSPLARAGADDVKSEPMDMVCSNNNANANDEHSNDSTGEHDANRSSSGDGGKGSLSSGNDEEIGDGLASHHAAPQFIMSPAENKMFHAAAFNFPNIDPSALLGLNTQLQQSGDLAVSPQGGSTGSLLSGVIVPGGSGGTPSNSSSNNNNNNSNNQQQKVEQQSSPHQLLQQQHHSTPHTNSPQLKQEQPKSGGGSCKSSDLHIAAGSERSLSRSSQGMPDAGGHSATPSPTAAYHKRERERERERERERERERERSLDHERDLERPGGTGSPPPPPPSHHSHFGQHPLSLLPSHHQLHATHHELSAAAAHHAHAHAHAAHAHALARAGSPMEHHHLLHHRRASLSPSGAVSSASGAGGRGGGAGGPGGPGGSLLSSVRAQDVAQANRLLLPLPLNACHRCDVCGKLLSTKLTLKRHKEQQHLQPLNNAVCNLCHKVFRTLNSLNNHKSIYHRRQKNHHSYFHHGAGVSQAGSPGSRLHQSLSSLSAAAAAANNSVNVGGGSVGGAGGNAVAAAAAAAAAAAELLLSPIVGAAAVAGGTASSTLQLAAAHQQQQQQSSPGIVKPCMDFL", "text": "FUNCTION: Broad-complex proteins are required for puffing and transcription of salivary gland late genes during metamorphosis. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MADLRKIKIDDTIIEVDPNMTLIQACEMAGIEVPRFCYHERLSIAGNCRMCLVEVVGGPPKPAASCAMQVKDLRPGPEGAPSEIRTNSPMVKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAMAYGVDFSRYREPKRATEDLNLGPLVETHMTRCISCTRCVRFTTEVAGITQMGQTGRGEDSEITSYLNQTLESNMQGNIIDLCPVGALVSKPYAFTARPWELTKTESIDVMDALGSSIRIDTKGREVMRILPRNHDGVNEEWISDKTRFVWDGLRRQRLDRPYIRENGRLRPASWPEALEAAARAMKGKKIAGLIGDLVPAEAAFSLKQLVEGLGGKVECRVDGARLPAGNRSAYVGTARIEDIDDAEMIQLIGTNPRDEAPVLNARIRKAWSKGAKVGLVGEPVDLTYDYAHVGTDRAALESLSSREISDETKARPSIVIVGQGAIARRDGEAVLAHAMKLAENSNSGLLILHTAAGRVGAMDVGAVTEGGLLAAIDGAEVVYNLGADEVDIDQGPFVIYQGSHGDRGAHRDIILPGACYTEESGLFVNTEGRPQLAMRANFAPGEGKENWAILRALSAELGATQPWDSLAGLRRKLVEAVPHLAQIDQVPQNEWQPLGRFDLGQASFRYAIRDFYLTNPIARSSPLMGELSAMAAARKAPAPLAAE", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
{"protein": "MALLNLFFCLVFSSPLMAMPPVLQGRKSMSPDSILKDTSTDDGARDFQGRKFPQFMMQLYQNIIRGRDKDLSNLEHPTLQESDTVQSFITKSYTTVGNHWTLFFDMSSISRSNELKLAELRFSLPSFRKSHSVTVDIYHTNDGKEKLFMGSFKTKPSAALDADCKVFNLTILLQNFLTRGKRLIKDEYIQAKGLHLKDLEKSATEKGTENVDTLKQDQYHVSDFAAERIMLVVFAKEQSHAKSDPPSLGKKLFPSKYGIDDNANKVNGFRRLRRNKKEKTQIHVSTGPPKPIEEIKPKCKKVDMFVDFQKIGWGSWIVYPKAYNAYRCESTCAVPLNETENATNHSYIKSLLPLSDMERKECPSCVPVKMMSMSMLYYENEDFILRHHEEMIVEECGFKDM", "text": "FUNCTION: Exhibits mesoderm-dorsalizing activity and neural-inducing activity, but lacks mesoderm-inducing activity. Regulates the expression of specific mesodermal and neural genes. Induces convergent extension movements at the embryonic midline by activating the fgf signaling pathway to induce t/bra expression in the organizer region. Acts with wnt11 to induce Spemann organizer cells and induce axis formation. The unprocessed protein antagonizes bmp-signaling (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MAEGQVLVLDGRGHLLGRLAAIVAKQVLLGRKVVVVRCEGINISGNFYRNKLKYLAFLRKRMNTNPSRGPYHFRAPSRIFWRTVRGMLPHKTKRGQAALERLKVLDGIPPPYDKKKRMVVPAALKVVRLKPTRKFAYLGRLAHEVGWKYQAVTATLEEKRKEKAKMHYRKKKQILRLRKQAEKNVEKKICKFTEVLKTNGLLV", "text": "FUNCTION: Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions (PubMed:36517592). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (By similarity). In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex (By similarity). Involved in methylation of rRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL13 family."}
{"protein": "MGKRSKTSRKGKKAWRANISSEDIEDFFEKTTRDALSGGNLSAAPSEDLFHVDKSHDLPVKRKIEKHRERVLRVDSILKKNPFVQLVPSSKPKLKKSKKTIVIEDKAPKQVQKSVGDDSVMADLWGDDSKGEHESNPRKIFKNPSIISAVEIEHPGCSYNPTTESHQDMLAEAVAQEMQKVYKTELGPAPVPLTIEGDTLSEDERYFLDVDNFSEGEDNENVENEVSEAGIKLKENPFVQLKPSSNTNLKKIEDKTPRQAQKSVGDDSVMVDLLGDDIKEDLKYFLEVGNVGEGEDNKDVKIEVSEAGNNVSRKTKRVTRVELNKRCRQKALRKKETKEKAKEKILNEIDSLPNILEEIAKEDEDKQNKHLRRVIAKQEVLKIRPPRLGKYKFEAPPVQVLLTEEMTGSLRKLKACCTLARDRFKSLEKRGILVPSKQIRRF", "text": "FUNCTION: May play a role in ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the NOP53 family."}
{"protein": "MESSDVELDFQRSVQAVLRELNTPNPALQSNQGMWRWSLHKKVERNPGKSSILVRILLRELEKAESEDGRRVIIPLLLTLMSVLTKATGIPEDLYHRAYTFCTRLLTLPAPYSTVALDCAIRLKTETAVPGTLYQRTVIAEQNLISELYPYQERVFLFVDPELVSASVCSALLLEIQAAQEQQTPEACMRHVVSHALQAALGEACHTGALNRKLQASSRRVLEYYFHAVVAAIEQVASEDSPSRLGHLEKMEEIYCSLLGPATTRRHCVGDLLQDRLPSIPLPSPYITFHLWTDQEQLWKELVLFLRPRSQLRLSADLDALDLQGFRLDRDLARVSTDSGIERDLPLGSDELPDPSSSEMERAALQRKGGIKKRVWPPDFFMPGSWDGPPGLHRRTGRPSGDGELLPGVSRVHTARVLVLGDDRMLGRLAQAYYRLRKRETKKFCLTPRLSLQLYYIPVLAPQVTGQDPEASRKPELGELASFLGRVDPWYESTVNTLCPAILKLAEMPPYLDTSRTVDPFILDVITYYVRMGTQPIYFQLYKVKIFTSLSHDPTEDIFLTELKVKIQDSKSPKEGSSPRRRGAAEGTGAELSMCYQKALLSHRPREVTVSLRATGLVLKAIPAGDTEVSGFFHCTSPNAASATDCSCLHVSVTEVVKSSNLAGRSFTTSTNTFRTSSIQVQSQDQRLLTLWLDKDGRRTFRDVVRFEVSPCPEPCSRTQKSKTSALNSHGQETEKNMAKPNSLLMPINTFSGIIQ", "text": "FUNCTION: Regulatory subunit of the PI3K gamma complex. Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. The PIK3CG:PIK3R6 heterodimer is much less sensitive to beta-gamma G proteins than PIK3CG:PIK3R5 and its membrane recruitment and beta-gamma G protein dimer-dependent activation requires HRAS bound to PIK3CG. Recruits of the PI3K gamma complex to a PDE3B:RAPGEF3 signaling complex involved in angiogenesis; signaling seems to involve RRAS. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Note=Translocated to the plasma membrane in a Ras-dependent manner (PubMed:19906996)."}
{"protein": "GIPCGESCVFIPCITGAIGCSCKSKVCYRNHVIAAEAKTMDDHHLLCQSHEDCITKGTGNFCAPFPDQDIKYGWCFRAESEGFMLKDHLKMSITN", "text": "FUNCTION: Probably participates in a plant defense mechanism (Probable). Active against Gram-negative bacteria E.coli ATCC 700926 (MIC=1.1 uM), K.pneumoniae ATTC 13883 (MIC=2.7 uM) and P.aeruginosa ATCC 39018 (MIC=4.7 uM) (PubMed:21596752). Has hemolytic and cytotoxic activity (PubMed:21596752). SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
{"protein": "CNGRDVPCDPDPAKNRRCCSGLECLKPYLHGTWYQDYCYYVEK", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 02 (HWTX- XVIc) subfamily."}
{"protein": "MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSCPGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSEKAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFVIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFDFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY", "text": "FUNCTION: Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn- glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MIENKVELVAELVLESIGKTEVVSRHTEGTKSCQVSFRIKDSPSEKGSTSFLSELVVIQTLDDNDKYTVVIRHGTSITMACVVGYSDFKLPTELKWPLERESLPVEPDLKPIMTQLKRQTAGSADMPKFDDEYQAQARQNQGTAPLNPYPGLTVTEPSFANPAGGYADGDLYPVGTSHPDWSGGLPNPLGNPSSQGGMIFDPNRRPAPRREDMPPGWMPGSKYDEPFGPGSGGFGGSGSGGFGGSGSGFI", "text": "FUNCTION: Plays a role in the establishment of transcriptional silencing boundaries, preventing the propagation of heterochromatic silencing. SIMILARITY: Belongs to the proteasome inhibitor PI31 family."}
{"protein": "MNIYDVSQKAGVSIATVSRVINGNPNVSEKTKQKVLDVMKEIGYTPNVFARGLGLNTMKTIGIMCSDSSDTFLANAVYHLEQNLRKNGYDSFLCCTGYELHTKQKYLKLLLSKRVDAIVMVGSSFLEANKKDNAYIMEAADEVPIMLINGYLSHPRIYCTLCDDHQAVYDAVSKLITQGRKEILYLYNSKSYSGLQKLSGYKAALAAHELPLDENLMQMCPNNLADTKNLLNSLVKQGLNYDAVVTAEDLLAIGTIKFIKDSGRQIPQDVSIIGYNNSLLTTCCDPELTSIDNHVETLCISTISTLMRVLNGNDVPNKTTISNDLIVRKTTNF", "text": "FUNCTION: Involved in control of pectin and galacturonic acid metabolism. Probably represses a comprehensive set of pectin fermentation genes by binding a conserved palindrome at or downstream of their transcription start site to block transcription. In the presence of galacturonic acid may activate transcription of acetate synthesis and other aspects of carbon metabolism. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MLRYCLHRLLIGLGMLLALTILIFVLLQLTPGDPIDAYINPNVAMTQAEMDALRAQLGLDRPLPVQYLAWLGQAVQGNLGHSLQRFNETVSGLIASRIGPTLLLMAAGLAIAIVIGVTTGIISAVRRNSFLDYSFSVLALLGISSPAFLTALLGLYVFSVRLKWAPSGGMLTPATDFSIPDLLRHLALPALVLSIGHAALIMRYMRSSMLETLNQDYVRTARAKGVREFWVVVKHTLRNAMLPVVTLIGSTIGLAVGGAIFIESVFNWPGMGLLLINAVETRDYPVIMGATLVIGACVIIVNILTDLAYAVIDPRIKVT", "text": "FUNCTION: Probably part of an ABC transporter complex that could be involved in peptide import. Probably responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family."}
{"protein": "MESNGSVSSMVNLEKFLCERLVDQSQPISERFRALFSLRNLKGPGPRNALILASRDSSNLLAHEAAFALGQMQDAEAIPALESVLNDMSLHPIVRHEAAEALGAIGLAGNVNILKKSLSSDPAQEVRETCELALKRIEDMSNVDAENQSSTTEKSPFMSVDPAGPAASFSSVHQLRQVLLDETKGMYERYAALFALRNHGGEEAVSAIVDSLSASSALLRHEVAYVLGQLQSKTALATLSKVLRDVNEHPMVRHEAAEALGSIADEQSIALLEEFSKDPEPIVAQSCEVALSMLEFENSGKSFEFFFTQDPLVH", "text": "FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L- lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor. SIMILARITY: Belongs to the deoxyhypusine hydroxylase family."}
{"protein": "MPTDLIRYGSISPEMLAYLWLLIEYKNSIMVAGEVATGKTTLLNAFSLFIPPQMKIVSIEDTPEIRLYHENWIAGTTRSGFGGEEYEITMMDLLKAALRQRPDYLIVGEVRGEEAKILFQAITTGHLALSTIHAKSPEAVIRRLNAEPMNIPKIMLEQLNAICMQVRLIYKGRFVRRTKSITEIVEYDPKIDDIILHDVFRWNPEDDTFEFSGESYLLRRIAEFIGISEKEIINELHSRAEFLRNLCKTKPNFEEFVKKICEYKEYHKGD", "text": "SIMILARITY: Belongs to the GSP E family."}
{"protein": "MRILAILLPILISFFISYITTVWVIRQAKKSRFVGKDINKPDKPEIPLLGGIGIIAGFIAGSFSLLLTDVRSERVIPAVILSSLLIAFLGLLDDIFNVRQSVRAFLPIFASVPLIVYSVGHSIISIPFLGPINFGIFYYIIIIPFALTITSNAFNMLEGLNGLGVGMGIIMLSALAYIGLTHTGPTYQAGLIALSAIFSLSAFLIFNKYPAKIFPGNVGTYFIGALIGAIGIAGFMYTALAILYIPYVVEFILKLRTNFKGVSFGKVDSSGRLYWDEKPHSLTHIVMKMGRFKEYQVVIILWGMEAIFAVIAVILQTTTIVI", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family."}
{"protein": "MDLLLGVLSSGILQNALPFVAGVGRVKRPKRVKLEEAFREAHLCRPVIPYRAPTPYTGGRVKALFVGINYTGTRNKLSGCVNDVRQMLGTLQRIQFPISECCILVDDMRFPNFTALPTRENIIKHMAWLVHDVRPGDVLFFHYSGHGTETKAERDSEELYDQCLVPLDYQVQGAILDDDLFELLVKGLPAGVRMTAVFDCCHSASLLDLPFAFVGNNNFYSGGRHEMRKVRANNFSMGDVVVFSGCDDSGTSADVSNVSSFGSGLVASGGAATQALTWALVNTSQLSYADIFIRTREILRQKGYKQVPQLSSSKPVDLYKPFSLFGPITVNTSLIHYVPQQYLQPWGPPQPYYPPPQPQQPYYPPPQPQQPYYPSSQLPTQYNNLAPTAGIPLMTSSSEVPPGQYPQALSGDQNGGVPPQYPSDQSTYYSSAQYLSGVGKPL", "text": "FUNCTION: Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:22402587). May play a role in apoptosis (PubMed:22402587). SUBCELLULAR LOCATION: Recycling endosome Note=Localizes to RAB11-positive recycling endosomes. SIMILARITY: Belongs to the peptidase C14B family."}
{"protein": "RYIELAVVADHGMFTKYRVHELVNTVNGFFRSKQDLIKVQKDKTLTSFGEWRERDLLPRI", "text": "FUNCTION: Prothrombin (F2) activator that is cofactor-independent. Also has fibrinolytic and fibrinogenolytic activity. It degrades the Aalpha- chain and more slowly the Bbeta-chain of fibrin and fibrinogen, while the gamma-chain is only partially and slowly affected. A dose-dependent procoagulant activity is shown in human plasma. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I subfamily."}
{"protein": "MASTVSPSTIAETPEPPPLSDHIRNAADISVIVIYFLVVMAVGLWAMLKTNRGTIGGFFLAGRDMAWWPMGASLFASNIGSNHYVGLAGTGAASGVATVTFEWTSSVMLLILGWIFVPIYIKSGVMTMPEYLKKRFGGERLQVYLSILSLFICVVLLISADIFAGAIFIKLALGLDLYLAIFILLAMTAVYTTTGGLASVIYTDTLQTIIMLIGSFILMGFAFNEVGGYESFTEKYVNATPSVVEGDNLTISASCYTPRADSFHIFRDAVTGDIPWPGIIFGMPITALWYWCTNQVIVQRCLCGKDMSHVKAACIMCAYLKLLPMFLMVMPGMISRILYTDMVACVVPSECVKHCGVDVGCTNYAYPTMVLELMPQGLRGLMLSVMLASLMSSLTSIFNSASTLFTIDLYTKMRKQASEKELLIAGRIFVLLLTVVSIVWVPLVQVSQNGQLIHYTESISSYLGPPIAAVFVLAIFCKRVNEQGAFWGLMVGLAMGLIRMITEFAYGTGSCLAPSNCPKIICGVHYLYFSIVLFFGSMLVTLGISLLTKPIPDVHLYRLCWVLRNSTEERIDIDAEEKSQEETDDGVEEDYPEKSRGCLKKAYDLFCGLQKGPKLTKEEEEALSKKLTDTSERPSWRTIVNINAILLLAVVVFIHGYYA", "text": "FUNCTION: Does not function as sodium/D-glucose symporter (PubMed:13130073, PubMed:20421923, PubMed:22766068). However, may function as a D-glucose sensor by generating a D-glucose-induced depolarization which is pH-independent, Na(+)-dependent at neutral pH and probably H(+)-dependent at acidic pH (PubMed:13130073, PubMed:22766068, PubMed:17110502, PubMed:20421923). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
{"protein": "MSVSEQDPNRAYRETQSQIYKLQETLLNSARTKNKQEEGQESNTHSFPEQYMHYQNGRNSAYDLPNVSSQSVLAFTEKHYPNKLKNLGTLYYNRFKEGSFDEDSTSYSDRHSFPYNLYDNTLPPPFLPAIGIQNINNIATLKITYEDIQASFNNIESPRKRNNEIWGCDIYSDDSDPILVLRHCGFKIGAPSGGSFHKLRRTPVNVTNQDNVTGNLPLLEGTPFDLEVELLFLPTLQKYPSVKRFDITSREWGSEATVIHDGLSYGIYSIVIKQRLDRDKPHEPNGYIKNLKWT", "text": "FUNCTION: Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RXT3 family."}
{"protein": "MARAKAVDFFSTKNNSSDSEEEEDKPAVDPRFVLADSDSEGEEEQEDGDEDEEEKGRTSKKKTKDFFELAGKTDDGDDEEEDEEDEEEEEEEKEKKPVKTSSTKAKTKPMTKEEIEKHNKKIAKTGVVYFSRIPPLMDPGKLRMLLQRFGIVDRIYLVPEDPKAQAVRIRHGGNRALAYTEGWAEFTKKRYAKTCASTLNGNTIGGKKGSQHYDDIMNAKYLPKFKWSDLSEQLAQETHNRQARLRTEISQATRENQTYIQSLEKSKAAERRRQRQEEEGGETEEKPAKKVHRDFYQGKTHSARAKEGKKELDGSVGSILGSVM", "text": "FUNCTION: Involved in the small subunit (SSU) processome assembly and function, and in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the ESF2/ABP1 family."}
{"protein": "MKLTTHHLRAGAALLLAGVLLAGCDQSSSDEKHIKVGVINGAEQDVAEVAKKVAKEKYGLDVELVGFSGSLLPNDATNNGELDANVFQHRPFLEQDNQTHGYKLVAVGNTFVFPMAGYSKKIKTVAQIKEGATVAIPNDPTNLGRALLLLQKEKLITLKEGKGLLPTALDITDNPRHLQIMELEGAQLPRVLDDPKVDVAIISTTYIEQTGLSPVNDSVFIEDKNSPYVNILVAREDNKNAENVKEFLQSYQSPEVAKAAETIFNGGAVPGW", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Lipid-anchor. SIMILARITY: Belongs to the NlpA lipoprotein family."}
{"protein": "MYKKIKLRDQQISELINLESKRQNSQIELIASENYASEDVILANGTSLSNKYGEGYPGKRYYGGCTFIDQIEKIAIERVKKLFKIEYANVQPYSGSSANAAVFAALLKPGDKILGLDLNAGGHLSHGYKINFSGMFYSGISYFLDENELLDYDAIEKIALKTKPNLIICGYSAYSRKIDFARFRQIADKVNAFLLADIAHIAGLIAAGQHPSPVGYAHIITSTTQKTLRGPRGGLILTNSKEIAAKIDKVVFPGIQGGPFFHTIAAKAVAFKEALEPWFKEYCAQIVKNASHFASEFIKKGIRIVSQGTENHLFTIDVLSSYNLNGKQAQILLESVNIITNKNTIPNDTLSPFVTSGLRLGTPAMTSRGFKEQEFSQMAEIIDFVLRKKELNALEIKEIKKKVKILTKNFPIKKSYWP", "text": "FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family."}
{"protein": "MKITRSLSTVEVHTGGEAFRIVTSGLPRAPGDTIVQRRAWLKENADEIRRALMFEPRGHADMYGGYLTEPVSPNADFGVIFVHNEGYSDHCGHGVIALSTAAVELGWVQRTVPETRVGIDAPCGFIEAFVKWDGEHAGPVRFVNVPSFIWQRDVSVETPSFGTVTGDIAYGGAFYFYVDGAPFDLPVREAAVEKLIRFGAEVKAAANAKYPVVHPEIPEINHIYGTIIANAPRHPGSTQANCCVFADREVDRSPTGSGTGGRVAQLYQRGLLAAGDTLVNESIVGTVFKGRVLRETTVGDIPAVIPEVEGSAHICGFANWIVDERDPLTYGFLVR", "text": "FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Together with LhpI, is involved in a t3LHyp degradation pathway to L-proline, which allows A.brasilense to grow on t3LHyp as a sole carbon source. SIMILARITY: Belongs to the proline racemase family."}
{"protein": "MASVQWHSRSRKYDSEWQASRLEVSAVEFSDYHPLKAITVTDSKSRRGGRKGSTSSSSSSSSSVAPDPLSSMLDGTDPLSLFAAASETPTLPHSVSAGELGRKRKEKEEEVGLDFEPWSSKRGEILSRFTTTEKLSINLFMGSDTSKASSPSSAVSEKVRTRLEELDDLEEGSQRELLNLSQQDYVNRIEELNQSLKEAWGSDQKVKALKIVIQCSKLLSDTSVIQFYPSKFVLITDILDTFGGLVYDRIWSMCADPHPLPESFSADDVNDTAKETCLNWFFKIASIRELVPRLYVEAALLKCNRFLTKCGIQETLQRLTAMIRGIGDPLVAVYARAYLCRVGMEVAPHLKDSLNKNFFDLLASFRQIHGDSVQNQLVLQRVEIPVYLTLYSPAINWILQCVAYRAPEVLLTEMMDRCKKLGNNALLLNSVMWAFRAEFVATRATDFIGMIKDCDEAGFPKHLLFASLGRSLSCADPPESERLSILNEAWKVITKVRSPRDYINCAEIWVEFTCRHFTKREVNTVLADIIKHMTPDRAFEDAYPQLQSVIKKILTYFHDFSMLFSMEKFLPFLDMFQKDSVRVEVCKSIMEVFIKHQQEPTRDPVILNALLHICKTMHDSVNALTLDDEKRSLALLINGFIRMVSFGRDFEQQLSFCVEARATFCNLEPVIIHLIHTVNQLAMETGRVMKGNHSRKTAAFVRACAAYSFITIPSLTNIFSRLNLYLLSGQVALANQCLSQADAFLKAAVSILPEVPRSISIEGKQRSSESFLLDFINNFLSTLLVVPDHPEQGVLYLVRGLLNMVQDYTWEDNSDAKVRVYISALPLLAAMSQESYLYTIPKVDSNETLYGGDPKFIAEINKLCETLIGQVLDHLKSLGRDEEVRRQGSLAFSLFGCLLAHGDLRNNKLNQLAVNLWNLSHKHGICDTRTSVRTLEHIKHQAQQTDMSHFSDMTARLSLQSRA", "text": "FUNCTION: Acts as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrins. The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. In the endosomes, drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. May be involved in copper-dependent atp7a trafficking between the trans-Golgi network and vesicles in the cell periphery. SUBCELLULAR LOCATION: Endosome. SIMILARITY: Belongs to the VPS35L family."}
{"protein": "MLTLLLIIPLVGALMLAPMQGNTRQSESQMKRLALGTSLINFVLSIVLWGEFDSSTSEYQFTQEFNQVNFCHLHIGVDGISLYFVLLTTFITPICILSNWDNIKEQLKYFLMCFLVLETLLIAVFVVLDILLFYVFFESVLIPLFLIVGIWGGSATRVRAAFLLFLYTLFGSLFMLLAFLVIYYNVGSTDFQVVSLSEINLESQKLLWLAVFISMAIKTPLLPFHVWLPRAHAEAPLAGSVILAGLILKLATYGYMRILIQFLPDATSYFSPLVQTIAVITLIYASLATLRQTDFKALVAYSSIGHMAVVVLGLFSNTIQGIDGALLLSIAHGVVSPALFILVGGVLYDRYHTRTIRYYRGMTAYMPLFSIMFFVFTIFNAAVPLSANWAGEFLCLAGAFQRNPVFAVLGSTGIVLSAAYSIWLYNRIAFGAWSKYLNYTTDLTRREFMLLLPLLFVAVVFGIFPNIILDSIHASTSGLIYSAS", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family."}
{"protein": "MLTQQLLSIGVNHFLTISVILFGLGMFAVMTRKNAIVILMGVELILNAANINFLTFSKYNGGMEGVMFSLFVIVLAAAEAAIALAIVINIFKTFKTVDVSSVDTMKE", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family."}
{"protein": "MGSTDEPGSSMHGVTGREQSYAFSVDGSEPTNTKKKYNLPVDAEDKATVFKLFSFAKPHMRTFHLSWISFSTCFVSTFAAAPLIPIIRENLNLTKHDIGNAGVASVSGSIFSRLVMGAVCDLLGPRYGCAFLVMLSAPTVFSMSFVSDAAGFITVRFMIGFCLATFVSCQYWMSTMFNSQIIGLVNGTAAGWGNMGGGITQLLMPIVYEIIRRCGSTAFTAWRIAFFVPGWLHIIMGILVLTLGQDLPGGNRAAMEKAGEVAKDKFGKILWYAVTNYRTWIFVLLYGYSMGVELSTDNVIAEYFFDRFHLKLHTAGIIAACFGMANFFARPAGGWASDIAAKRFGMRGRLWTLWIIQTSGGLFCVWLGRANTLVTAVVSMVLFSLGAQAACGATFAIVPFVSRRALGIISGLTGAGGNFGSGLTQLVFFSTSRFTTEEGLTWMGVMIVACTLPVTLIHFPQWGSMFFPPSNDSVDATEHYYVGEYSKEEQQIGMHLKSKLFADGAKTEGGSSVHKGNATNNA", "text": "FUNCTION: Involved in high-affinity nitrate transport. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family."}
{"protein": "MTLESIMACCLSEEAEEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFSAMQAMIRAMETLKIPYKYEHNKGHALLVREVDVEKVASFENPYVDAIKYLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRIATHGYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Golgi apparatus Nucleus Nucleus membrane. SIMILARITY: Belongs to the G-alpha family. G(q) subfamily."}
{"protein": "MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAKAYPGCQFLIEEKGQQFINNAQLQRPILHKANSGEASPALPKDTSFLKNPLVIYAQQMGFPLEEIKKVMGQKLKTTGNNYTCVEEFVSDLLCAQSETIADKPMKREISIEEKLRQLEEEKVCKVCMDRRITIVFIPCGHLVACAVCADVLDKCPICCTIIERRQKIFMS", "text": "FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins (By similarity). Acts as a direct caspase inhibitor (By similarity). E3 ubiquitin-protein ligase that acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of ripk2 downstream of NOD1 and NOD2, thereby transforming ripk2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (By similarity). A key apoptotic suppressor in eggs (PubMed:15853809). Acts as a positive regulator of Wnt signaling (PubMed:22304967). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the IAP family."}
{"protein": "MNLPEYHRLAAYITSDHSQDYTQDTNVAFIEEGPWDGEEEELITSFSTVEDLYTAICVREDNNQLDMALKFAPFASEIELPFYTALSQLKIDHDKLDDSARPVLGLYEPRATQSPDQSSRMRVLGNALSSNEVPSGHIRAEGKIKNVNTIEDFKNMDKQAMLQTSAKQIWDAINDGTIYSIPSLLSSFTILSFANLKKYTFTYWFAFPALHSEPAWRKVEQPPKFSAEETTALTEELGTWRYSHDNREHGFFLAKRVYPSSEHPQDPESESTSDLPFKWVIGSLREFESGFFNGVDAKNQYVSFVDPSTYHENPGWMLRNLLVLVRRRYKLDKVQILCYRDNHAKRHVPQSLILILESIYDPEYQSTAPDQIPKVTGWERNSLGKLTAKVTNLAQYMDPAQLADQAVDLNLKLMKWRIAPELNLDAIKNTKCLLLGAGTLGTYVSRLLMGWGVRKITFVDNASVSFSNPVRQPLFDFKDCIDGGAKKAYRASEALQEIYPGVDSTGHVMAVPMLGHPITDEAATKMNFELLQKLIEDHDAIFLLMDTRESRWLPTVMGKAAGKIVMNAALGFDTYVVMRHGVTPEDGGPAALGCYFCNDVVAPSDSVKDQTLDQQCTVTRPGVAPEASSKLVELLASVLQHPLKGAAPAPKLSSNHQSGQLEFDRDPPNHPLGLVPHQIRGFLAAYKTMLISGPSYDCCSACSPKIVNAYKEDGWEFIKRALTEKDYITELSGLAEVQRKAEAAANDVEWDSDEEGMEDEEPELL", "text": "FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy (PubMed:29417220). Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine (By similarity). Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes (By similarity). Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Required for normal mycelial growth and conidiogenesis, and regulates sclerotial formation (PubMed:29417220). Plays an essential role in pathogenesis (PubMed:29417220). SUBCELLULAR LOCATION: Cytoplasm Preautophagosomal structure. SIMILARITY: Belongs to the ATG7 family."}
{"protein": "MMNNKVYKRSDEPVFWGLFGAGGMWGAIFAPAVILIVGILLPLGMFPDALTFERALSFSQSIIGRIFWLLMIILPLWCGLHRLHHMMHDLKIHVPASSWVFYGLAAILSVVALIGIFTL", "text": "FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FrdD family."}
{"protein": "MAFSLQLQQIFVSYTRFCSQPKSITNPLISLKLPSIHPLAFAQNAAVSNIDTGVAAIDGSAEEVSLPPQLRRELMPKHVALIMDGNRRWAKMRGLPVALGYEAGIRAVRKIIELCGNWGIMVLTLFAFSSDNWLRPKVEVDILMSLFERALNDELENFAREGIRISIIGDSSKLPKSLQDLIAKAVKTTKENSRLHLVVAVNYSGQHDVVQACQTIAQKVKDDIIETKDINSFLIEQELQTNCIDFPCPDLLIRTSGELRLSNFLLWQLAYSELFFSHSHWPDFGEAEFLEALCSFQQRQRRYGRQSS", "text": "FUNCTION: Uses neryl diphosphate and geranyl diphosphate to catalyze the cis-prenyl chain elongation and produce polyprenyl diphosphate with a chain of 55 carbons. SUBCELLULAR LOCATION: Plastid, chloroplast Note=Localizes in punctuate patterns inside the chloroplasts. SIMILARITY: Belongs to the UPP synthase family."}
{"protein": "MERSDSRDLYNFVRASSLDKNSTLFDASQYEFFGQNLDDMELGGLDDDGVIAPVLGHADDDEYHLFDKGEGAGLGSLSDMDDLATTFAKLNRVVTGPKHPGVIGDRGSGSFSRESSSATDWTQDAELTSWLDEQDQEAKRWSSQPQSFAHSKPLYRTSSYPQQQPQLQHYNSEPIILPESNFTSFPPPGNRSPQASPGNLHRAPSLPGGSQLTYSAPSPLSNSGFHLSGLSQGPHYGGNLTRYASCGPTLGNMVQPHWVTDPGHLHGDHSGLLHNLVQQQHQQLPPRNAIMSQHLLALQQRQSYAQLAALQSQLYSSYPSPSRKVPFGVGEVREHKHKSSHRSRKNRGLSQQTSDAASQKSETGLQFRSKHMTSEEIESILKMQHSNSHSNDPYVNDYYHQAKLAKKSAGSKAISHFYPAQLKDHQPRSRNSSEQHPQVHVDALGKITLPSVRRPHALLEVDSSPGFNDGSGDHKGSGKHLEQEPLVAARVTIEDALGVLIDIVDIDRTLQNTRPQDGGAQLKRKRQILLEGLATALQLADPFSKTGQKSGMTAKDDIVFLRIATLPKGRKLLTKYLQLLVPGTENARVVCMAIFRHLRFLFGGLPSDTLAAETISNLAKAVTVCVQAMDLRALSACLAAVVCSSEQPPLRPIGSSAGDGASVVLISLLERAAEVVVVPRVMHGNSNDGLWRASFDEFFNLLTKYCRSKYDTIRGQNQGSAADVLELAIKREMPAELLRASLRHTNDDQRNYLLNFGRKPSAISESASHARGGQINSESVRG", "text": "FUNCTION: Activator of mRNA decapping. Involved in mRNA decay via decapping (By similarity). Involved in the regulation of root stem cell niche identity. Maintains root stem cell niche stability through the interaction with the negative regulator of jasmonate signaling AFPH2/NINJA, and the regulation of cell division (PubMed:26956135)."}
{"protein": "MPGPATDAGKIPFCDAKEEIRAGLESSEGGGGPERPGARGQRQNIVWRNVVLMSLLHLGAVYSLVLIPKAKPLTLLWAYFCFLLAALGVTAGAHRLWSHRSYRAKLPLRIFLAVANSMAFQNDIFEWSRDHRAHHKYSETDADPHNARRGFFFSHIGWLFVRKHRDVIEKGRKLDVTDLLADPVVRIQRKYYKISVVLMCFVVPTLVPWYIWGESLWNSYFLASILRYTISLNISWLVNSAAHMYGNRPYDKHISPRQNPLVALGAIGEGFHNYHHTFPFDYSASEFGLNFNPTTWFIDFMCWLGLATDRKRATKPMIEARKARTGDSSA", "text": "FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15610069, PubMed:15907797, PubMed:22745828). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069, PubMed:15907797). Involved in neuronal cell proliferation and differentiation through down-regulation of EGFR/AKT/MAPK and Wnt signaling pathways (PubMed:22745828). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
{"protein": "MRTVCLVKNQQPLGATIKRHEITGDILVARVIHGGLVERNGLLYAGDKLVEVNGVPVEGLDPEQVIHILAMSCGTIMFKVIPVSAPPVSSQTTVYVRAMIDYWPQEDPDIPCMDAGLPFLKGDILQIVDQSDALWWQARKISDIAICAGLIPSNHLLKRKQREFWWSQPYQPHTCLKSTRSKEEFVGDGQQFFIAGFRQQHANMRCTCSCYSAVGAPYEEVVRYQRQPADKHRLIVLVGPSGVGVNELRRQLIGCNPSCFQSAVPHTTRSPKSYEMDGREYHYVSRETFESLMYGHRMLEFGEYKGHLYGTSVNAVLAVLDEGKICVMDLEPQDIQLARTRELKPYVIFIKPPSMSSMRHSRRNAKIITDYFVDMKFKDEDLQEMEELAQKMESQFGQFFDHVIVNDNLQDARAQLLSAIQKAEEELQWVPEAWVSPGAES", "text": "FUNCTION: May play a role in retinal photoreceptors development. SUBCELLULAR LOCATION: Cytoplasm. Note=Localized at photoreceptor synaptic terminals in retina. SIMILARITY: Belongs to the MAGUK family."}
{"protein": "MFPLVEFCISNMAKGGDYVYDKLENDPDVDVLEYGCLNNCSVCSCGLYALVDGDTVEGDTPDELLKNIYKHIEENDFTNLL", "text": "SIMILARITY: Belongs to the UPF0349 family."}
{"protein": "MKKTRDNPCDKIELGNKTSQKGVSLVKKHIFEDIILQNALNFTEEVVEIFGDLLNKGMNITELVARIKELTDKLGRGAIEAIIEELDRIIKEDKRRKEKWVVERKDKKRLTTVLGDIEYERTYYKSKEDGRYTYLVDDALEIGRHDRIEKGVKIKLVENAIEESYERSSKKACPEELSKQTVLNAIREIGEVEVKREIKEKKEVRVLYIEADEDHVPLQDGRDETPRLVYIHEGREEKNGRNVLKNVYYKAYVGEKPEDIWIDVANYIEDNYKEEKIEKIYIAGDGAPWIKEGLKWILKSRFVLDRYHLNKYVLKATSKEPKYRDKIWRAINEGDKERVKKVFDELIKAAEEEREKEKIKEAKKYILNNWEGIKIYNEDEDVIGCSAEGHISHVFSARLSRNPLGWSREGLKLMAKLRVFSKNGGDLREVEWGKKKNINAGSYKLTKKQIKEAVRRVKTSTNEKINNITVLNIGKVTPIYRVLRALKYAQVI", "text": "SIMILARITY: Belongs to the UPF0236 family."}
{"protein": "METYKDSTQVSKSSLKKKIQGFGGFLSGMVMPNIGAFIAWGLITALFIKTGWLPNDNLSKLVDPMIHYMLPMLIGYQGGKLVYDTRGGVVGAIATMGMIVGASIPMFLGGMIIGPLGGYVIKKFDKAIENKIPTGFEMLVNNFSAGILGAALAIISYVAVGPVVAGASTGLGSIALAITNQGLLPLIAVVVEPAKILFLNNAINHGVFSPLGIEQVQHLGKSVFFLLEADPGPGLGILLAYSLYGKGSAKNSAPGAVIIHFLGGIHEIYFPYVLMKPFLLLAVIAGGICADLTFVLLKAGLVAAASPGSIIAILAMSPKGGQLPVLAGVAVGAIVSFVVASIILKGSKEKSKDNFEEAQNKMKEMKKESKNQTTANSENVKNNDELVSSDIKLIVFACDAGMGSSAMGESILKKELKNANIDGIKVQHYSVDSIPKEADVVFVQENLSERARKSAPDANIVTIKNFLDRSTYEGFMKKIKK", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MQGAQIISIGSAVPDLCINNKEISQIVETSDEWIVTRTGIQERRVLTGTNKSVVDLAYSAAMKALDKIHMDPLEIDLIILATSSPNDLFGSASQVQAKIGAARAVAFDLTAACSGFVLAIVTATQFIQNGSYKNILIIGADVLSKWIDWSDRKTCILFGDGAGAAIIQACYEEDNAILGFQLNTDGKQYKKLSITYKENNYSLNTLKLFQGQFQYISMNGKEVYKFAVSKVPASIIKCLNALHLSIQDVNWLLLHQANKRILQAVANRLSVDNYKIISNLSKYGNTSAASIPLALDEAWQNNQIAKEDIIVISGFGAGLTWGTVVIKWKC", "text": "FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the thiolase-like superfamily. FabH family."}
{"protein": "MPSIDCKRLQKLAPKSPENQSKCISRLRYMVMLDQVESDEGGNSSTRPYVWAVLLNAPPRNADEYIRYVRQGPSPMAQKIQNDVSRTLVVESQFHSRVSQSSLSRLLNAYVWKRGALYVQGMNVLASPFLYACKSENQAFQFFDRLLQNECPLYVLPNIDGVHRGAKLLDKCLEVLDHRLYTYLLSKGLTAKIYALPSILTLSACTAPLSEALTIWDFLFAYGIHLNILCVIAQMFIFREQLIDHPSPMTLLRTFPPLNAKNIMKITILLISKLPPELYNLLARHAWDSEAGVLIDRLT", "text": "FUNCTION: Has a dual role in the cell cycle. In mitosis, it is involved in maintenance of cdc2 kinase activity. It is subsequently required for regulation of septum formation. Could be involved in maintenance of cdc2 kinase activity by preventing, directly or indirectly, the degradation of cyclin or the dephosphorylation of 'Thr-167' of cdc2. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. SIMILARITY: Belongs to the BUB2 family."}
{"protein": "MAPSIQSLSMIHDSQECIKPIPAFYCCYLLRSCVRHASLYIGSTPDPARRLAQHNGDRNGAAKRTLRENLRPWEMVAIVSGFTSRVAALQFEWAWQNTKVSRHADLDGNVIQELGVRICPRTGKGVKGTAKPRTSLTNILANLHLLLRSPYFSKWPVEVRFFSADVHRVWQVWLQRVDGLLNDGIRVVTDFALDGISEVERKELLAGAGRVGTLDVGYNSIKEYVEKSQFLLEDGERINCGVCKQRLILQHDIIAVCSHSSCHCAAHLSCLSSHFLKDKDSDSELIPREGTCPACYGKLEWLTMMKEISLRLRGQEEVNRLFRRRRQAGTPKGQGLKSVRGRGRGHSEDESDALQVSTGLDIVDLTPCSDDPWTIDCAIGELGGIAHRPGGESSGNDSDATITPEMETPPQRRRRNQNTRTQRLGLQKSATINLSDWDDAEVIE", "text": "FUNCTION: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX1 family."}
{"protein": "MRERGEMREAKAPLIAEAAEHISHSHGSGSSGTGSHTSGGGGGWRGSRQYQRRSDALAYGNRYQKAAALVDLAEDGVGIPEDVLNDTRFERAMRFYFVYLRLDWLWSLNLFALILLNFLEKPLWCRGYSQHACDQRDLYFLGQLPYLSKTESLIYEGLTLVILVMDIFYPLSYEGLNLFWKNTINKLKVLLLFILACDILVFAFSPQPFRVAPYIRVAFLIMNIRELRMCAVTLVGMVGTYLNVLALSLLFLLFASWLAYVTFEDTPQGKTVFSSYGTTLYQMFILFTTSNNPDVWVPAYKSSRWSSLFFIVYVLLGVYFLTNLILAVIYDSFKEQLAKQVSQADCTRKSILEKAFGIIDATGQGYLNKEQCLSLLDELNKYRSLPKTSREDFELIFAELDQSGDFKVTSEEFATLCNTIAIKFQKEPPPSYLEKYPSFYHSALCEWLKSFVRSPLFEYIVIFVLLMNLVAVIIETTLDIENSSSQKVWQEVEFVFGWIYVIEMALKIFSLGFGAYWMEGQNKFDFVLTWTIFIGETLTFAFPSKLSFLSNGEWIRYLLLGRMLRLTRILLQVRRFRAFVATFFTLMSSLMPYLGIVFCTLCIYCSLGLQIFGGIVYAGNPTLEETDLFSNDYLLFNFNDYPSGMVTLFNLLVMGNWQAWMESYRQLTGSYWSLIYFVSFYLISVLLLLNLIVAFVLEAFFAEMELEKDGEADIQDPTLEGRNRRRSVRVRTKGTMVDILLHHMLSNELDGSQNRDQ", "text": "FUNCTION: May function as one of the major voltage-gated Ca(2+) channel (VDCC) across the plasma membrane. May be involved in the regulation of cytosolic Ca(2+) and in growth and development. Acts as the major ROS- responsive Ca(2+) channel and is the possible target of Al-dependent inhibition. Determines sensitivity to T.viride xylanase elicitor. Plays a regulatory role in elicitor-induced defense responses and hypersensitive cell death. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. Two pore calcium channel subfamily."}
{"protein": "SRQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEPFHKMKQFLSDEQNILALRSIQGRQRENPGQSLNRLFQEVPKRRNGSEGNITTRIRASETGSDEAIKSILEQAKRELQVQKTAEPAQPSSTSSSGTSDDAIRSILQQARREMEAQQAALDPALKPAPLSQADLAILSPKLIPSSPMSSVSSYPPLALSLKKPPTAPDTSASTLPNPPALKKESQDAPGLDLPGAAESAQGVLRHVKSELGRSGVWKDHWWSTVQPERKSAAPPEDAKSEEAGGTKEKGGGQGHGPIAASSRDPHHRRSTGRNGPALSPRTPQSSELSLTGASRSETPQNSPLPSSPIVPMSKPAKPSVPPLTPEQYEIYMYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREPFIRMQLWLNGELGQGVLPVQGQQQGPVLHSVTSLQDPLQQGCVSSESTPKTSASCSPAPESPMSSSESVKSLTELVQQPCPPIETSKDGKPPEPSDPPASDSQPATPLPLSGHSALSIQELVAMSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLSRPKPWHKLSLKGREPFVRMQLWLNDPNNVEKLMDMKRMEKKAYMKRRHSSVSDSQPCEPPSVGIDYSQGASPQPQHQLKKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRELFIEEIQAGSQGQAGARHSPSARSSGAAPSSEGDSCDGVEAAEGPGAADAEESAPAAAAKSQGGPAEAAVAPEEREEAPRPAEKRSRRPRGPGPGPGRRGGGGPAPGAPAAPAAAARGPSRRPGARAKPRRRRRRRRRHARGGGRRYLSRPARGGPCRARDGAHRSSALPSTSAPAAARRPSSLQSLFGLPEAAGARDSRDNPLRKKKAANLNSIIHRLEKAASREEPIEWEF", "text": "FUNCTION: Transcription factor involved in the control of neuronal differentiation in the brain. Regulates dendrite development and branching, and dendritic spine formation in cortical layers II-III. Also involved in the control of synaptogenesis. In addition, it has probably a broad role in mammalian development as a repressor of developmentally regulated gene expression. May act by preventing binding of positively-activing CCAAT factors to promoters. Component of nf-munr repressor; binds to the matrix attachment regions (MARs) (5' and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer function by binding to MARbeta, an ATC- rich DNA sequence located upstream of the TCR beta enhancer. Binds to the TH enhancer; may require the basic helix-loop-helix protein TCF4 as a coactivator. FUNCTION: [CDP/Cux p110]: Plays a role in cell cycle progression, in particular at the G1/S transition. As cells progress into S phase, a fraction of CUX1 molecules is proteolytically processed into N- terminally truncated proteins of 110 kDa. While CUX1 only transiently binds to DNA and carries the CCAAT-displacement activity, CDP/Cux p110 makes a stable interaction with DNA and stimulates expression of genes such as POLA1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CUT homeobox family."}
{"protein": "RTDTVSTPVSGNELLEAGEECDCGTPGNPCCDAATCKLRPGAQCAEGLCCDQCRFMKEGTVCRRARGDDMDDYCNGISAGCPRNPFHA", "text": "FUNCTION: Binds alpha-5/beta-1 (ITGAV/ITGB1), alpha-V/beta-3 (ITGAV/ITGB3) and alpha-M/beta-2 (ITGAM/ITGB2) integrins. Is a potent inhibitor of platelet aggregation induced by ADP, collagen, and thrombin. Induces neutrophil chemotaxis and inhibits the chemotaxis of human neutrophils toward fMLP, IL-8, and jarastatin itself. Directly activates an integrin-coupled signaling and modulate the MAPK pathway in different ways, leading the neutrophils to express different functional response. Jarastatin-treated neutrophils accumulates F-actin at the plasmalemma. Induces PTK2/FAK1 and phosphoinositide 3-kinase (PI3K) activation. Induces Erk-2 translocation to nucleus and a delay of the spontaneous apoptosis of neutrophils. Increases the IL-8 mRNA levels in neutrophils. When injected simultaneously with melanoma cells in mice, jarastatin, flavoridin (FL) and kistrin (KR), significantly reduce tumor lung colonization. Jarastatin inhibits B16F10 cell growth in vitro. When it interacts with melanoma cells, it induces actin cytoskeleton rearrangement, increasing actin polymerization and PTK2/FAK1 phosphorylation. Interferes with NF-kappaB translocation in melanoma cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily."}
{"protein": "MSAVGPGSNAGASVNGGSATAIATLLRNHKELKQRQGLFQAKQTDFFRYKRFVRALHSEEYANKSARQPEIYPTIPSNKIEDQLKSREIFIQLIKAQMVIPVKKLHSQECKEHGLKPSKDFPHLIVSNKAQLEADEYFVWNYNPRTYMDYLIVIGVVSIILALVCYPLWPRSMRRGSYYVSLGAFGILAGFFAVAILRLILYVLSLIVYKDVGGFWIFPNLFEDCGVLESFKPLYGFGEKDTYSYKKKLKRMKKKQAKRESNKKKAINEKAEQN", "text": "FUNCTION: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to SEC61 and SEC62. SEC62 and SEC63 are required for interactions between SEC61 and translocating polypeptides. SEC62 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC62 is essential for cell growth. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SEC62 family."}
{"protein": "MSKAHKPWPYRRRSQFSSRKYLKKEMNSFQQQPPPFGTVPPQMMFPPNWQGAEKDAAFLAKDFNFLTLNNQPPPGNRSQPRAMGPENNLYSQYEQKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKQPCEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLLEEGSATVPRLAERLTTELIMHIQKSLPLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWVGILATNTQKVKNIIHEEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLQKAMEIIQQAFINVAKKHFGEFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQMVFCQDQIYSVVLKKVREEIFNPLGTPSQNMKLNSHFPSNESSVSSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLTQARHALCQFSSKEIH", "text": "FUNCTION: Interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1). Acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. Exhibits antiviral activity also against simian immunodeficiency virus (SIV-mnd). May play a role in regulating nucleocytoplasmic transport and cell-cycle progression. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nuclear pore complex Note=Localization to nuclear pores requires GTP-binding. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family."}
{"protein": "MKHLRPQFPLILAIYCFCMLQIPSSGFPQPLADPSDGLDIVQLEQLAYCLSQWAPLSRQPKDNQDIYKRFLFHYSRTQEATHPVKTGFPPVHPLMHLAAKLANRRMKRILQRGSGTAAVDFTKKDHTATWGRPFFLFRPRNGRNIEDEAQIQW", "text": "FUNCTION: Implicated in the regulation of circadian rhythms through autocrine and/or paracrine actions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NmU family."}
{"protein": "MGNSDRKPGLIKRLWKWWRTPSRLALGTLLLIGFVGGIVFWGGFNTGMEKANTEEFCISCHEMRNTVYQEYMDSVHYNNRSGVRATCPDCHVPHEFVPKMIRKLKASKELYGKIFGVIDTPQKFEAHRLTMAQNEWRRMKDNNSQECRNCHNFEYMDTTAQKSVAAKMHDQAVKDGQTCIDCHKGIAHKLPDMREVEPGF", "text": "FUNCTION: Mediates electron flow from quinones to the NapAB complex. FUNCTION: Mediates electron flow from quinones to the NapAB complex. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the NapC/NirT/NrfH family."}
{"protein": "MKIGYIYAIENNLNDEVYIGSTLRTIEERFSEHKASARRRPTCTFHKFMSLHGIEHFKIIELKKIEVNSFFELQALEESYIRDYGSLNTINGVNKAAVHTRNEILVKRKIYSKECVKLPPLDEVIKIATKASLKKLEINEFIDLFIGEENKWNKMFDSDLSGIHISSLILNQLGYEGEFKNQQTCFKRFLKRNNIIIQEFSSSNPELKLYPSIQEEMKNMKTNVIANRKWLIANPRDLKKIIMKLNTKNGDAIREYYICMDELVQFYSQYSLSYDSNNN", "text": "SIMILARITY: Belongs to the IIV-6 019R family."}
{"protein": "MVGGGALRRVGKYEVGRTIGEGTFAKVKFAQNTESGESVAMKVVDRSSILKHKMADQIKREISIMKLVRHPNVVRLHEVLASRKKIFIILEFITGGELFDKIIRHGRLNEADARRYFQQLIDGVDFCHSKGVYHRDLKPENLLLDSQGNLKISDFGLSAWPAQGGALLRTTCGTPNYVAPEVLSHKGYDGALADTWSCGVILYVLLAGYLPFDEVDLTTLYGKIESAEYSFPAWFPNGAKSLIHRILDPNPDKRIRIEEIRNDEWFKKNYEPTREIESEEVNLDDVNAAFDDPEEDADHTLDDEAGPLTLNAFDLIILSQGLNLAALFDRRQDYDKLQNRFLSRKPAKVIMSSMEVVAQSMGYKTHIRNYKMRVEGLNANKTSHLAVMLEIFEVAPSIFMIELQRAAGDTSDYNKFINNYCSKLDDIIWNFPIEKSKSRISRLSKR", "text": "FUNCTION: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily."}
{"protein": "MTAALPSTLELLKDVHLGLPVPCHDPARLALLSGHYLYYHYGCDGLDDRGWGCGYRTLQTLCSWPGGQSSGVPGLPALQGALEAMGDKPPGFRGSRNWIGCVEASLCLEHFGGPQGRLCHLPRGVGLRGEEERLYSHFTTGGGPVMVGGDADAQSKALLGICEGPGSEVYVLILDPHYWGTPKNRCELQAAGWVGWQKVKSVFDSNSFYNLCFTRNL", "text": "FUNCTION: Thiol-dependent isopeptidase that recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins. SIMILARITY: Belongs to the peptidase C78 family."}
{"protein": "MYSFLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKAIKLQIWDTAGQESFRSITRSYYRGSAGALLVYDITRRDTFNHLTCWLKDARSYANSNMTIILIGNKSDMESKRAVSYEEGRQFADENGLIFLETSAKTASNVEEAFVNTASKIYEKIQKGDFDINNESFGIKLGAPTSKQDGTDQKPAGGGCCK", "text": "FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MNGKLYALSTGPGAPDLITVRAARILGSLDILYAPAGRKGGDSLALSIVRDYLGEQTEVRCCHFPMSADGAEKEAVWNEVAAALTAEVEAGKQVGFITLGDAMLFSTWIFLLQRIGCPEWLEIVPGVTSFAAIAARAKMPLAIERQSLAVISCTAPEAEIAQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMSEATLPGEQCWRHLHEVNDDRPLPYFSTILVNKQWEYAE", "text": "FUNCTION: Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway. SIMILARITY: Belongs to the precorrin methyltransferase family."}
{"protein": "MGNYKSRPTQTCTDEWKKKVSESYVITIERLEDDLQIKEKELTELRNIFGSDEAFSKVNLNYRTENGLSLLHLCCICGGKKSHIRTLMLKGLRPSRLTRNGFTALHLAVYKDNAELITSLLHSGADIQQVGYGGLTALHIATIAGHLEAADVLLQHGANVNIQDAVFFTPLHIAAYYGHEQVTRLLLKFGADVNVSGEVGDRPLHLASAKGFLNIAKLLMEEGSKADVNAQDNEDHVPLHFCSRFGHHDIVKYLLQSDLEVQPHVVNIYGDTPLHLACYNGKFEVAKEIIQISGTESLTKENIFSETAFHSACTYGKSIDLVKFLLDQNVININHQGRDGHTGLHSACYHGHIRLVQFLLDNGADMNLVACDPSRSSGEKDEQTCLMWAYEKGHDAIVTLLKHYKRPQDELPCNEYSQPGGDGSYVSVPSPLGKIKSMTKEKADILLLRAGLPSHFHLQLSEIEFHEIIGSGSFGKVYKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCQLNHPCVIQFVGACLNDPSQFAIVTQYISGGSLFSLLHEQKRILDLQSKLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTKQPGNLRWMAPEVFTQCTRYTIKADVFSYALCLWEILTGEIPFAHLKPAAAAADMAYHHIRPPIGYSIPKPISSLLIRGWNACPEGRPEFSEVVMKLEECLCNIELMSPASSNSSGSLSPSSSSDCLVNRGGPGRSHVAALRSRFELEYALNARSYAALSQSAGQYSSQGLSLEEMKRSLQYTPIDKYGYVSDPMSSMHFHSCRNSSSFEDSS", "text": "FUNCTION: May play a role in cardiac physiology. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Expressed at lower levels in the cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily."}
{"protein": "MTIWVDADACPNVIKEILYRAAERMQMPLVLVANQSLRVPPSRFIRTLRVAAGFDVADNEIVRQCEAGDLVITADIPLAAEAIEKGAAALNPRGERYTPATIRERLTMRDFMDTLRASGIQTGGPDSLSQRDRQAFAAELEKWWLEVQRSRG", "text": "SIMILARITY: Belongs to the UPF0178 family. SIMILARITY: Belongs to the UPF0178 family."}
{"protein": "MLQDPDSDQPLNSLDVKPLRKPRIPMETFRKVGIPIIIALLSLASIIIVVVLIKVILDKYYFLCGQPLHFIPRKQLCDGELDCPLGEDEEHCVKSFPEGPAVAVRLSKDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQDLDVVEITENSQELRMRNSSGPCLSGSLVSLHCLACGKSLKTPRVVGVEEASVDSWPWQVSIQYDKQHVCGGSILDPHWVLTAAHCFRKHTDVFNWKVRAGSDKLGSFPSLAVAKIIIIEFNPMYPKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRCNADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNVWKAEL", "text": "FUNCTION: Plasma membrane-anchored serine protease that directly induces processing of pro-uPA/PLAU into the active form through proteolytic activity (PubMed:24434139). Seems to be capable of activating ENaC (By similarity). FUNCTION: (Microbial infection) In gut epithelial cells, facilitates human coronavirus SARS-CoV-2 infection through, at least, the cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SUBCELLULAR LOCATION: [Transmembrane protease serine 4 catalytic chain]: Secreted Note=Activated by cleavage and secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MVAIDQHDTYSVRVISRSHLSKDIVQVELEESSQRPLPDYEPGSHVDIYVQDDLVRQYSLVKASDAQASYQIAFKVKRDQGSATELMCELLRVGATTRISAPRNAFALDPQARETVLICGGIGITPMVHMAMTLVKAKRPWSMHIASRDGDELDLLGPLGSCSEISRYISSQGDRLPIRDLAERAPANAHLYFCGPEGMLQEFLAATQHRDPATVHYEQFQAAPSTGNEFTVNLARSGAQYVVREGETILDVLRNAGHHVTSSCRQGICGMCETTLISGVPDHRDRLLTDSEKASGRTMLICCSRALSPELTLDL", "text": "SIMILARITY: Belongs to the PDR/VanB family."}
{"protein": "MVLSLQTLAKKVLAGQRPTKCHPHFLKCYGLWWHNGPMIFDQNQKKIWSPIFTDGVHINAALVKAVAENNYDLIKLFTEWGANIDYSLLSVNTERTRDLCRELGAKEQLKQEEVLYYFNIIKRNLTSSNIILCHEVFSHNPILETINRTKLRGIIYEQLEALMENTDILSELLTKYWYGIAIEFNLTKAIHYFYQRYVHLHQWRLMYALFYNNVCDLHELYAKEKIRMDMDEMLKWACRKNYNYLTIYYCCIVLGADINQAMFHSIQFYNIGNMFFCIDLGANAIEEGKTLALQKDKSFIASLLSINCYSMNDSLSLKETDPEVIKRMLKDYHSKNMSIAHKYYIKHGFNDI", "text": "FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the asfivirus MGF 360 family."}
{"protein": "MALDGIRMPDGCYADGTWELKMHVTDLNRDVSLRVTGEIHIGGVMLKLVEKLDVKKDWSDHALWWEKKKTWLLKTHWTLDKYGIQADARLLFTPQHKLLRLQLPNMKHMRVKVNFSDRVFKAVSDICKTFNIRHPEELSLLRKPRDPKKKKKKLEDAEEETLELEGPLLTPGSGSIYSSPGLYSKTMTPTYDSRDGSPLSPTSAWFGDSPLSEGNPSILAVSQPITSPDILVKMYKPQSLLDKAKINQGWLDSSRSLMEQDVKENEVLLLRFKYHSFFDLNPKYDAIRVNQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMSSDNHMNNSEKEVDEVDAALSDLEITLEGGKTSNTLGDITSIPELADYVKVFKPKKLTLKGYKQYWCTFKDITISCYKSREEAHGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVADGMNEIWLRCDTEKQYAQWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHMNPDPQIIEPITTDINPECLVSPRYLKKYKNKQPGFVRDLISARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFLAKFQGGKKDELIGITYNRLIRMDAGTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEPSLAFICAEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV", "text": "FUNCTION: Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling (By similarity). Required for normal embryonic development, including normal heart morphogenesis and normal angiogenesis. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cell cortex Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, stress fiber Cell junction, focal adhesion Membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side Nucleus Cytoplasm, myofibril, sarcomere, I band Cell surface Note=Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with integrins at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides (By similarity). SIMILARITY: Belongs to the kindlin family."}
{"protein": "MPALEVNSVPSSSEFPVAPEKLASIIETSARDASSDDLGACTESILVELSKASSAHKFVVSLTKVAFSDSEDFNLSIDSSIGGSWNKTKDGGYSHSVETEAGARLLATVVWVSK", "text": "SUBCELLULAR LOCATION: Cytoplasm Cell projection Note=Concentrates at cytoplasmic punctate structures and localizes at the mating projection tip. SIMILARITY: Belongs to the TDA2 family."}
{"protein": "MNMDFNLFMNDIVRQARQEITAAGYTELKTAEEVDEALTKKGTTLVMVNSVCGCAGGIARPAAYHSVHYDKRPDQLVTVFAGQDKEATARARDYFEGYPPSSPSFAILKDGKIMKMVERHEIEGHEPMAVVAKLQEAFEEYCEEV", "text": "FUNCTION: S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a dithiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB) in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE- SSB). Involved in maintaining redox homeostasis in response to disulfide stress conditions. SIMILARITY: Belongs to the bacilliredoxin family."}
{"protein": "MAQPVQSIDVLLIEHAELELALADPELHSNPAEARKAGRRFARLAPIVATHRKLISARDDLQTARELAAGDESFADEIAELESRIAELTTQLTDMLAPHDPHGPDDIVLEVKSGEGGEESALFAADLARMYIRYAERHGWTVTVLDETTSDLGGYKDATLAISHKGASDGDAVDGVWSRMKFEGGVHRVQRVPVTESQGRVHTSAAGVLVYPEPEEIGEVHIDESDLRIDVYRSSGKGGQGVNTTDSAVRITHLPTGVVVTCQNERSQLQNKTRALQVLAARLQAMAEEQALANASADRASQIRTVDRSERIRTYNFPENRITDHRIGYKAHNLDQVLDGDLDALFDALSAADKQSRLQQV", "text": "FUNCTION: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. FUNCTION: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family."}
{"protein": "MTFQFNFTIEDHLEDELTSLGDGALALHSSKESLVSERQKGTHRDKKCSTEQSDLLQDHLWEHKSERNEAPSQDPDSSFGAANSSSNLEPHEEKPCLKVAKEHAVPKDLKKVLENKVTETLPGLQHVNISIMKTTLLKENFPGENIISKSFSSHSDLISGVYEGGLKIWECTFDLLAYLTKAKVKFAGKKVLDLGCGSGLLGIMALKGGAKEIHFQDYNSVVIDEVTLPNVVANSTLEDEENDVNEPDVKRLRRSTVAQELCKCRFFSGEWSEFCKLVLSSEKLFEKYDLILTSETIYNPDYYVPLHQTFLRLLDKNGQVLLASKVHYFGVGGGTHLFQKFVEERNVFETRTLEIIDEGLKRCLIEMTFKYPT", "text": "FUNCTION: Protein-L-histidine N-tele-methyltransferase that specifically monomethylates RPL3, thereby regulating translation elongation. Histidine methylation of RPL3 regulates translation elongation by slowing ribosome traversal on tyrosine codons: slower elongation provides enough time for proper folding of synthesized proteins and prevents cellular aggregation of tyrosine-rich proteins. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Nucleus, nucleolus. SIMILARITY: Belongs to the methyltransferase superfamily. METTL18 family."}
{"protein": "MAAASAPVPGPGGASSTARGRIPAPATPYQEDIARYWNNEARPVNLRLGDVDGLYHHHYGIGAVDHAALGDPGDGGYEARLIAELHRLESAQAEFLLDHLGPVGPGDTLVDAGCGRGGSMVMAHQRFGCKVEGVTLSAAQAEFGNRRARELGIDDHVRSRVCNMLDTPFEKGTVAASWNNESSMYVDLHDVFAEHSRFLRVGGRYVTVTGCWNPRYGQPSKWVSQINAHFECNIHSRREYLRAMADNRLVPQTVVDLTPETLPYWELRATSSLVTGIEEAFIESYRDGSFQYVLIAADRV", "text": "FUNCTION: Catalyzes the SAM-dependent methylation of geranyl diphosphate (GPP) to yield (E)-2-methylgeranyl diphosphate (2-MeGPP). SIMILARITY: Belongs to the geranyl diphosphate 2-C-methyltransferase family."}
{"protein": "MESKVEQGVKNLNMENDHQEKEEKEEKPQDANKREPVVALPFEAGEYYVPRGSRRRFRVRQPIAHYRWDLMHRVGEPQGRMREENVQRFGEDMRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP", "text": "FUNCTION: Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the BEX family."}
{"protein": "MSKLARLEREEIMECQVMWEPDSKKDTQMDRFRAAVGTACGLALGNYNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDEVVDTSKGIADVPEWFRGSRLNYAENLLRHKENDRVALYVAREGREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREKIDISKIPNSVFLDDFLASGTGAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNWMVSALATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCIKSSVLLGSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVWGASGELVCTKPIPCQPTHFWNDENGSKYRKAYFSKFPGVWAHGDYCRINPKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVMAGRTVEHRGAFSNPETLDLYRDIPELQDF", "text": "FUNCTION: Converts acetoacetate to acetoacetyl-CoA in the cytosol (By similarity). Ketone body-utilizing enzyme, responsible for the synthesis of cholesterol and fatty acids (PubMed:22985732). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MMEEIPASYFKIEEFQFESGEKIQEAPVEYRTTGKPSLDDMGVIDNAVIYIHGWSGDCSSVRRIAALTEPGGALENFFVISISSLGSPGSASPSTTAMGKDFPEYTILDMVNFQRQFLDEKFGIRKVRGVIGTSMGGFQALQWAAEYPDEMEFLIPLVTSWQVRGINYALFSYMNHLIEGDPEFRAGTRPERALSLASMLMYLHGLSREYYQGLENAELESSMMDMGSEGALMDPYDVIWRNRAAMKHDLSGKLESIRARTLIFGVNQDRYFPPELDTIPMAQLIPKAELVLFDSECGHLGVNEIGKYNEIIVSFIGGD", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family."}
{"protein": "SCKVPFNECKYGADECCKGYVCSKRDGWCKYHIN", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 50 (Jztz-F7) subfamily."}
{"protein": "MKKTLAALIVGAFAASAANAAVVYNNEGTNVELGGRLSIIAEQSNSTIKDQKQQHGALRNQSSRFHIKATHNFGDGFYAQGYLETRLVSAQSGTESDNFGHIITKYAYVTLGNKAFGEVKLGRAKTIADGITSAEDKEYGVLNNSKYIPTNGNTVGYTFKGIDGLVLGANYLLAQERYKYGGAAGGAGGAGAVAGEVYPQKISNGVQVGAKYDANNIIAGIAYGRTNYRESIHEKDLGKKQQVNGALSTLGYRFSDLGLLVSLDSGYAKTKNYKDKHEKSYFVSPGFQYELMEDTNFYGNFKYERNSVDQGKKEREQAVLFGIDHKLHKQVLTYIEGAYARTRTNDKSKAEKTEKEKSVGVGLRVYF", "text": "FUNCTION: Forms pores that allow passive diffusion of small molecules across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Gram-negative porin family."}
{"protein": "MGHNSDKLYVTHSEHAAGSHTASSFGKRQETGKSEFQRLPFDCCALSLQPFKNPVAVISETKAGEAPRADVFDLLNIVPYIRKFKSNPVTGKPLETSQLIKLNFSRNAEGNLHDPITYKVFSPHIHIVFLKNTGNVFDMASLQLLAIKPKTWRDLVNDEPFKRKDIITIQDPENLAARDLREYDYVKKDLKVSEDELAGDPLRGINVDAAGGASKVLKMIAEKNKSGQSPAPTPSKIDDGKGQEKKEGVVAKRKVEQMAYNASNYSSGRAAASLTSTSLMPETKSERAMFDEEEYMFEELSRPTKDKERQKSKAYATITTNFGPLNVELHGDRAPKTVYNFVQLAKAGKYDNVVFHRLIPGFMVQGGDPTGTGRGGESYWGEPFRDEHGEKGAYKHDSRGVLSMANSGPRTNGSQFFFTFRPTPHLDGKHTVFGKLVGGEETLDKIERVNVRPGGDRPVRDIVIQGVTVLQDPFEAYQARLQARLARQDQSDAALKRRAEAQKEREKDRTTWLGTKLGEKGAVGKRRMEEDVGVGKYLKVGGEAGQRTTLDVVDYGVEKKKKKAGGFGDFSGW", "text": "FUNCTION: May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily."}
{"protein": "MFLLHTMIRVGDLDKSLQFYCDILGMNLLRKKDYPSGEFTLAFVGYGKESENAVIELTHNWGTDKYDLGNGFGHIALGVEDIYSTCDKIRDKGGKVVREPGPMKHGTTVIAFVEDPDGYKIELIQTSSKKD", "text": "FUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. SIMILARITY: Belongs to the glyoxalase I family."}
{"protein": "MASLKIPANIPLPEEDSEQLHKAFKGWGTNEGMIISILAHRNATQRSFIRAVYAANYNKDLLKELDGELSGDFERVVMLWTLDPTERDAYLANESTKLFTKNIWVLVEIACTRPSLEFFKTKQAYHVRYKTSLEEDVAYHTSGNIRKLLVPLVSTFRYDGNADEVNVKLARSEAKTLHKKITEKAYTDEDLIRILTTRSKAQINATLNHFKDKFGSSINKFLKEDSNDDYVQLLKTAIKCLTYPEKYFEKVLRRAINRMGTDEWALTRVVTTRAEVDLERIKEEYLRRNSVPLDRAIANDTSGDYKDMLLALLGHDHA", "text": "SIMILARITY: Belongs to the annexin (TC 1.A.31.1) family."}
{"protein": "MNPNNRSEHDTIKVTPNSELQTNHNQYPLADNPNSTLEELNYKEFLRMTEDSSTEVLDNSTVKDAVGTGISVVGQILGVVGVPFAGALTSFYQSFLNTIWPSDADPWKAFMAQVEVLIDKKIEEYAKSKALAELQGLQNNFEDYVNALNSWKKTPLSLRSKRSQDRIRELFSQAESHFRNSMPSFAVSKFEVLFLPTYAQAANTHLLLLKDAQVFGEEWGYSSEDVAEFYHRQLKLTQQYTDHCVNWYNVGLNGLRGSTYDAWVKFNRFRREMTLTVLDLIVLFPFYDIRLYSKGVKTELTRDIFTDPIFSLNTLQEYGPTFLSIENSIRKPHLFDYLQGIEFHTRLQPGYFGKDSFNYWSGNYVETRPSIGSSKTITSPFYGDKSTEPVQKLSFDGQKVYRTIANTDVAAWPNGKVYLGVTKVDFSQYDDQKNETSTQTYDSKRNNGHVSAQDSIDQLPPETTDEPLEKAYSHQLNYAECFLMQDRRGTIPFFTWTHRSVDFFNTIDAEKITQLPVVKAYALSSGASIIEGPGFTGGNLLFLKESSNSIAKFKVTLNSAALLQRYRVRIRYASTTNLRLFVQNSNNDFLVIYINKTMNKDDDLTYQTFDLATTNSNMGFSGDKNELIIGAESFVSNEKIYIDKIEFIPVQL", "text": "FUNCTION: Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. Has moderate level of toxicity to southern corn rootworm. SIMILARITY: Belongs to the delta endotoxin family."}
{"protein": "MSQENSVHRSSTKKTPIKIAFIHPDLGIGGAERLVVDAAVGLQSLGKEVVVFTSHCDKKHCFEEIRDGTIKVKVYGDWLPSSIFGRLSIFCSSLRQVYLTMILLTNYMHFDAIIVDQLSTCVPFLLLASQMILFYCHFPDKYLAKRGGILKKLYRIPFDTVEAESVRLADRIVVNSKFTASVFKKAFPKIRKPLRIVHPCVDIEAASKPLEFQLPEKILQRKLLISVNRFERKKDIRLAIDAFSALRDLSANRFPEYLLLVAGGYDIRVSENRRYLKELQEFCEQKDLSYTTVKDNWDNITVAPSTNVLFLLSVPSKVRDALISSSRILLYTPENEHFGIVPLEAMLRKVPVLAQTNGGPLETVIDGKNGWLRPRDAKIWGNVIYEATTSTTYDTAAMGEAGSEWVKNEFSTDAMARKFESEIMSGIRSITPEKRLMRRVNGLLAVFVLFMLFWGTCIIAATVPFAIIKLYFAQTYSSVKLGFMLGTCIVSVSFLTFTVYAKLTNL", "text": "FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MSAATKKRYITNKVGSEFYELAEEDIIAQVRQSRGNNLHEVLDQNGDSYVVSMPTKFRKAVWLRRDQFVVVRPIAEGDKVKGEIEYILDQDNVLYIRELGKWPSCFEEHALKMTREAKRGKANDKMIDDDMLPPSESEEEDDESEDEIEDTYDEDEETDDEEFDTYNPNRMQAPSK", "text": "SIMILARITY: Belongs to the EIF1AD family."}
{"protein": "MGFLFTPKHQKLVNQCYPPGRTPDKKPKGSETSYLLYYVNSRRPKLEKVSSYLVKRSTTDLNRRRSGNVSVTLELLAKIVENCNENMNIFIKDFIHIMTLVLNNNNFNNDPTIVGLIERVLEAICNHLDGSLVSGDSEFLELFKNFVTLYFKVANTKLNDTDLVLKGCLDFSKISNLGSIHQWSATAKNCVSIALTKFQERHPIYSEATIDSSFSEPGSPALKKKLTRTQTKVMGLDDVSNTGDYSILALNTFFNTTETDKLTIGLHALIEHLLETPNKELLQFICNGIPVQLRYIVILLFVRPLGTSSEKNMLLILKLISSLLTSAVSIIGLSVIDILRRLITVQLAKSDSTTVVKQIAVTIKDLNRKTYYKQQSSDMFAELSFKFIESGKPHHLELFQLDLDSLISVTSDQCLDLDLFGEFLPYVTDKTQLSKLLYPEAPHQVIFIRFFEKVSTLSKQDTEIAISTSFAYYKAASLLSGLAYYVNNNRPSDGYYAYHHHASKFLGLADYQTQVEFKRKDNDIFTKEDLLNYYSDAGSNIYSEKGRDILLVDHSDQNGTDIDQDTVRYSTPIPLPQISIPPTTTNGIGIKKSSPANDTYVTRSLKHNPVPNVKDLKNLVSSKKDKSNTKTLRGSQSVKSKVTNITFLLDELKNDGDEIKIADPDEEDIIGMEKQDLARSYSLRMNTISSTNSRTLIPSVENAEEHGDDFRDAHEDIEVSSSTRGRLFMV", "text": "SIMILARITY: Belongs to the EFR3 family."}
{"protein": "MDLISTFSLHFLLLACSLPPGAVSLRTALRKSGKVGPPLDIKLGALNCTAFSIQWKTPKRSGSSIIGYTVFYSEVGSDKSLRERSHNVPVGQDTLITEEVIGDLKPGTEYQVSVAAYSQTGKGRLSFPRHVTTLSQDSCLPPAAPQQPHVLVVSDSEVALSWRPGENEGSAPIQSYSVEFIRPDFDKSWTIIQERLQMDSMVIKGLDPDTNYQFAVKAMNAHGFSPRSWPSNTVRTLGPGEAGSGHYGPGYITNPGVSEDDDGSEDELDLDVSFEEVKPLPATKVGNKKFSVESKKTSVSNSVMGSRLAQPTSASLHETTVAIPPTPAQRKGKNSVAMMSRLFDMSCDETLCSADSFCVNDYAWGGSRCHCNLGKGGEACSEDIFIQYPQFFGHSYVTFEPLKNSYQAFQVTLEFRAEAEDGLLLYCGESEHGRGDFMSLALIRRSLHFRFNCGTGIAIIISETKIKLGAWHTVTLYRDGLNGMLQLNNGTPVTGQSQGQYSKITFRTPLYLGGAPSAYWLVRATGTNRGFQGCVQSLSVNGKKIDMRPWPLGKALNGADVGECSSGICDEASCIHGGTCAAIKADSYICLCPLGFRGRHCEDAFALTIPQFRESLRSYAATPWPLEPQHYLSFTEFEITFRPDSGDGVLLYSYDTGSKDFLSINMAAGHVEFRFDCGSGTGVLRSEAPLTLGQWHDLRVSRTAKNGILQVDKQKVVEGMAEGGFTQIKCNTDIFIGGVPNYDDVKKNSGILHPFSGSIQKIILNDRTIHVKHDFTSGVNVENAAHPCVGAPCAHGGSCRPRKEGYECDCPLGFEGLNCQKECGNHCLNTIIEAIEIPQFIGRSYLTYDNPNILKRVSGSRSNAFMRFKTTAKDGLLLWRGDSPMRPNSDFISLGLRDGALIFSYNLGSGVASIMVNGSFSDGRWHRVKAVRDGQSGKITVDDYGARTGKSPGLMRQLNINGALYVGGMKEIALHTNRQYLRGLVGCISHFTLSTDYHISLVEDAVDGKNINTCGAK", "text": "FUNCTION: Involved in both the retinal photoreceptor ribbon synapse formation and physiological functions of visual perception. Necessary for proper bipolar dendritic tip apposition to the photoreceptor ribbon synapse. Promotes matrix assembly and cell adhesiveness. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Synaptic cleft Presynaptic active zone Note=Detected in the synaptic cleft of the ribbon synapse around the postsynaptic terminals of bipolar cells (PubMed:18641643). Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic terminals (PubMed:18641643)."}
{"protein": "MLLLALSDAHIPDRATDLPVKFKKLLSVPDKISQVALLGNSTKSYDFLKFVNQISNNITIVRGEFDNGHLPSTKKDKASDNSRPMEEIPMNSIIRQGALKIGCCSGYTVVPKNDPLSLLALARQLDVDILLWGGTHNVEAYTLEGKFFVNPGSCTGAFNTDWPIVFDVEDSDEAVTSEVDKPTKENQSEDDDAKGGSTGKEQPGSYTPKEGTAGERENENESNVKPENQFKEDEVDMSDSDINGSNSPSFCLLDIQGNTCTLYIYLYVNGEVKVDKVVYEKE", "text": "FUNCTION: Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor VPS10. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS29-VPS26- VPS35 subcomplex may be involved in cargo selection. SIMILARITY: Belongs to the VPS29 family."}
{"protein": "MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGIRSIDDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWFDDATGKYHVNQYTGDENRTRVTQWETLDWVQEVQQRGAGEIVLNMMNQDGVRNGYDLTQLKKVRDVCRVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGELKAYLAGQGVEIRIC", "text": "FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family. SIMILARITY: Belongs to the HisA/HisF family."}
{"protein": "MAPVRGILGLQRAVSIWKESNRLTPALRSFSTQAASTSTTPQPPPPPPPPEKTHFGGLKDEDRIFTNLYGLHDPFLKGAMKRGDWHRTKDLVLKGTDWIVNEMKKSGLRGRGGAGFPSGLKWSFMPKVSDGRPSYLVVNADESEPGTCKDREIMRHDPHKLLEGCLIAGVGMRASAAYIYIRGEYVNERLNLEKARREAYAAGLLGKNACGSGYDFEVYIHFGAGAYICGEETALLESLEGKQGKPRLKPPFPANAGLYGCPTTVTNVETVAVSPTILRRGPEWFSSFGRKNNAGTKLFCISGHVNKPCTVEEEMSIPLKELIERHCGGVRGGWDNLLAIIPGGSSVPLIPKNICEDVLMDFDALKAVQSGLGTAAVIVMDKSTDVVDAIARLSYFYKHESCGQCTPCREGTGWLWMIMERMKVGNAKLEEIDMLQEVTKQIEGHTICALGDAAAWPVQGLIRHFRPELERRIRERAERELLQAAA", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 51 kDa subunit family."}
{"protein": "MPKRKSPENTEDKDGSKVTKQEPTRRSARLSAKPAPPKPEPKPRKTSAKKEPGAKISRGAKGKKEEKQEAGKEGTAPSENGETKAEEAQKTESVDNEGE", "text": "FUNCTION: Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMGN family."}
{"protein": "MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMINIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLASWLEDARQHANPNMTIMLIGNKCDLTHRRAVTTEEGEQFAKEHGLIFLETSARTAHNVEEAFINTAKEIYKKIQDGVFDVSNESYGIKVGYGGGNAGPQTVKPGEGGAAKSSSCC", "text": "FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MPAPRGPLRATFLALVAFGLLLQIDLSDVTNVTSSTKVPTSTSNRNSVDNATSSGPTTGINMTTTHESSVHNVRNNEIMKVLAILFYIVTGTSIFSFIAVLVAVVYSSCCKHPGRFRFADEEAVNLLDDTDDSGGSSPFGSGSRRGSQIPAGFCSSSPYQRLETRDWDEEEEASAARERMKHDPENVIYFRKDGNLDTSFVNPNYGRGSPLTIESHLSDNEEDPIRYYVSVYDELTASEMEEPSNSTSWQIPKLMKVAMQPVSLRDPEYD", "text": "SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HHV-5 UL132 family."}
{"protein": "MRVAIAGAGLAGLSCAKYLADAGHTPIVYERRDVLGGKVAAWKDEDGDWYETGLHIFFGAYPNMLQLFKELNIEDRLQWKSHSMIFNQPTKPGTYSRFDFPDIPAPINGVAAILSNNDMLTWEEKIKFGLGLLPAMIRGQSYVEEMDQYSWTEWLRKQNIPERVNDEVFIAMAKALNFIDPDEISATVVLTALNRFLQEKKGSMMAFLDGAPPERLCQPIVEHVQARGGDVLLNAPLKEFVLNDDSSVQAFRIAGIKGQEEQLIEADAYVSALPVDPLKLLLPDAWKAMPYFQQLDGLQGVPVINIHLWFDRKLTDIDHLLFSRSPLLSVYADMSNTCREYEDPDRSMLELVFAPAKDWIGRSDEDILAATMAEIEKLFPQHFSGENPARLRKYKIVKTPLSVYKATPGRQQYRPDQASPIANFFLTGDYTMQRYLASMEGAVLSGKLTAQAIIARQDELQRRSSGRPLAASQA", "text": "FUNCTION: This enzyme converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene. Also active with phytofluene and 1,2-epoxyphytoene as substrates. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family."}
{"protein": "MAKPARRKCKICKEWFHPAFSNQWWCSPEHGTKLALERRNKEREKAEKTAEKKRRREEQKQKDKIKIRKLALKPRSYWIKQAQQAVNAFIRERDRDLPCISSGTLTSAQWDAGHYRTTAAAPQLRFDERNIHKQCVVCNQHKSGNLVPYRVELINRIGQEAVDEIESNHNRHRWTIEECKAIKAGSNRKLKDLRNSRSEAA", "text": "SIMILARITY: Belongs to the ninG family."}
{"protein": "MPKRELWPAGLCSEPVTHIGSCGDMMSTTSTRSGSSDSSYDFLSAEEKECLLFLEKTIGSLEAEADSGLSTDESEPATSPRSFRALPTATQQAPQGKPEATDIQQVPVPKRVAQPSCPPESHSLGLRAGSYSLPRNLHLGRSQNLRESATQANSPVSEASEVFLEEPEKGQTSQGAKAKTIQPPAPSQKGTLDLSTVLIPPPEAFQDIRPKESGEESPPKKPGEQTHTPQVHSLERSPHSQKKVEMSSETVSHKATEKGWTEGLQQPQQPPAQSSQPTKAEELSLPSGVKPSIQQTPLTASKARKLPPNIVLKSSRSSFHSHPQNWLSNHTEATDSGPVSSLQEQRKARREALEKLGLPQDQDDPSLLVNKHTSTLKVREAQPQTPSQARAPARPASPALVSGTASAAGKVSPKKAVAPMDSLSKGWIPTQETPPGKVAEAKSMPIPIPKTLKENSSRTQPKPDPRLTLQESSIPGLRQMNFKSNTLERSGVGLSSYLSAAEKKDPSCQTSTSLGKSPFLDKVSPSAFRNSRPRPASLGMGKDFAGIQGGKLVGLEQDQCSQQPSFKGQSYDKLPRPPCISVKISPKGIPDGHRREALKKLGLLKE", "text": "FUNCTION: Putative androgen-specific receptor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SARG family."}
{"protein": "MFGNIGWGEFMVLLVAALVILGPERLPGAVSWVTKSLRQVREYASGASQQLKDELGPEFEDLRKPLADLNQLRGMTPRAVITKHLLDGDDSILTGNFDKPGSVSFDKSNPGTKAVSADPSTPTAPQNKPLAAGERPPIDLDAT", "text": "FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatB family."}
{"protein": "MEGKRSQGQGYMKKKSYLVEEDMETDTDEEEEVGRDRVRGSRGSINRGGSLRLCQVDRCTADMKEAKLYHRRHKVCEVHAKASSVFLSGLNQRFCQQCSRFHDLQEFDEAKRSCRRRLAGHNERRRKSSGESTYGEGSGRRGINGQVVMQNQERSRVEMTLPMPNSSFKRPQIR", "text": "FUNCTION: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' of AP1 promoter. Promotes both vegetative phase change and flowering. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mostly located in nucleus."}
{"protein": "MSAPTTSSSTDEDFAKPVKNGKTFANPKSFTNWGGIPGISDGFKFAFTETNHENVPCDKKILDVEIPVHNITADDFHSESDLFATWLGHATVLVDLEGVKFVTDPVWADRASFTSFAGPKRYRPPPMKLEDLPDLDFAVVSHDHYDHLDADAVKKITDRNPQIKWFVPLGMKKWMEGQGIGVDGSSTAVTELNWGESSEFVKNGKTYTIWCLPAQHWGQRGLFDRNHRLWSGWAVIGENRRFYYSGDTGHCDGEFKKFGEKLGPFDLAAIPIGAYEPRWFMKSQHINPEEAIEVHKLIRAKNSIGIHWGTYHMGSTEYYLEPRDKLKELMDAREDLKNTSFVTIEMGRIWEASDQ", "text": "FUNCTION: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid. NAEs are bioactive lipids that are involved in diverse physiological processes such as growth and lifespan. SIMILARITY: Belongs to the NAPE-PLD family."}
{"protein": "MKGSPLFHGLAPEEVDLALSYFQRRLYPQGKPIFYQGDLGQALYLVASGKVRLFRTHLGGQERTLALLGPGELFGEMSLLDEGERSASAVAVEDTELLALFREDYLALIRRLPLVAHNLAALLARRLREADLELDLLSFEEARNRVAYALLKLLRQGLGPLFQIRHHELAALAGTSRETVSRVLHALAEEGVVRLGPGTVEVREAALLEEIAFGLA", "text": "FUNCTION: Activates transcription. Positively regulates six promoters upstream of the TTHB186, TTHB147, TTHB178, TTHB159, TTHA0771 and TTHA0176 genes in a cAMP-dependent manner. Regulated genes include clustered regularly interspaced short palindromic repeat (CRISPR) associated (Cas) genes, and the genes encoding a putative transcriptional regulator, a protein containing the exonuclease III- like domain of DNA polymerase, a GCN5-related acetyltransferase homolog, and some T.thermophilus-specific proteins of unknown function. The consensus DNA-binding site of this transcriptional regulator is 5'- (CT)NNG(G/T)(G/T)C(A/C)N(A/T)NNTCACAN(G/C)(G/C)-3' in which N is G, A, T or C."}
{"protein": "MWLAILLALCCLTSDTHGARPPDFCSKDLISSVKPGFPKTIETNNPGVLKAARHSVEKFNNCTNDIFLFKESHVSKALVQVVKGLKYMLEVKIGRTTCRKTMHHQLDNCDFQTNPALKRTLYCYSEVWVIPWLHSFEVPVLLCQ", "text": "FUNCTION: Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cystatin family."}
{"protein": "MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV", "text": "FUNCTION: Glutamine--tRNA ligase (PubMed:26869582). Plays a critical role in brain development (PubMed:24656866). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MSEKVKFEKRESLKEKPDTANLGFGQYFTDYMLSVDYDADQGWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYKHNGEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLVDVERDWVPEGEGQSLYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGGDTLKSTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAYDKGELTEVFGSGTAAVISPVGTLRYEDREIVINNNEPGKITQKLYDTYTGIQSGKLEDKYGWRVEVPKY", "text": "FUNCTION: Acts on leucine, isoleucine and valine. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MRVLILSAFIACATAAPSAPVFGTLTPLTVPYIANIPTISPGDIQAAAIDAKVKVEDALRAAADRNQELLEQAIENQNEKVIEVNDLLKEKSQEAFWSTEDTKWQALTALQTAEAKIDGTLASNADLLGKAVLNGVVVSPVVSRIYSNVIQGVAAADCETPVLKAAEAPEGNKDEGNKDSVQVESSATESESDKAAAGFVRNLEAAQAAAQAQLLSETSAPTADTRAVIAASSEASAAAAPAASLSEASAQSASETGVSAASLSQSPVATPLSAAPLAPLPSSSVPLAGVPASAIAAAPLTAASLIASPLTLPTLNLEQQWVTGPVFVQPGLKAISPISLQTPFVPTLLKTPC", "text": "FUNCTION: Component of the cuticle of the pupa of Galleria mellonella."}
{"protein": "MDILLEEVRKVFGNTDEGKLAERLIVAYRQRGARGAREVLKKYLEELGVDVADIES", "text": "FUNCTION: Part of an actin-like archaeal cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Forms cell-spanning helical structures."}
{"protein": "MGGAFSTSKPKPAAGEEGGESAVVAVHSKAKWDELWDAHKNTTKLVVIDFSASWCGPCKMMEPVFKEMAGRFTDVAFLKVDVDELAEVARTWRVEAMPTFVLARGGEEVGRIVGADKDELEKTINTLRSSSSSTATTT", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may be involved in the redox regulation of a number of cytosolic enzymes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily."}
{"protein": "MKDMSLVNSKVLLVGSARGIGFSVLEHLLQAGAQVMAADCEWQLLLEQSESLLGRYPDQLTLKKLDLAEPEAVREQVNQWAEQVAGFDHLVCCAGILHVAPLHEMPMEQVSSIFTVNAFGVLACMQGVASSMKARQQGSMVIIGSNAANTPRMSIGAYGASKAALHMLVKCIGMELAPYGIRCNLVSPGSTRTAMQQQLWTEQYGEAQVIAGDAAQFRLGIPLNKIAEPADIAQAVLFLLSDNAGHITLHDLRVDGGATLDH", "text": "FUNCTION: Involved in an early step of the biosynthesis of the catechol siderophore vibriobactin. Vibriobactin is a chelating compound involved in transporting iron from the bacterial environment into the cell cytoplasm. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSYTIYLVEDEDNLNELLTKYLENEGWNITSFTKGEDARKKMTPSPHLWILDIMLPDTDGYTLIKEIKAKDPDVPVIFISARDADIDRVLGLELGSNDYISKPFLPRELIIRVQKLLQLVYKEAPPVQKNEIAVSSYRVAEDAREVYDENGNIINLTSKEFDLLLLFIHHKGHPYSREDILLKVWGHDYFGTDRVVDDLVRRLRRKMPELKVETIYGFGYRMMSS", "text": "FUNCTION: Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSCTIEKVLADAKELVERLREHDGAAESLIEQTTTLNKRVEAMKQYQEEVQELNEIARHRPRSTLVLGIQQENRQIRQLQHENKELRTSLKEHQSALELIMSKYREQMFRLLMASKKDDPGVIMKLKEQHSKELQAHIEKINEMTAVMRRAIEMDEQRGDREHNRIIKLEQENKRLREILQITKISFLNLHKEDASENSPHSAPVPNTDLILRKS", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIKE family."}
{"protein": "MQNDQQRFSLQNRTVLAHPYKRLGGAFTVKSPSVPNFHDKMHSDHSSSDSALVNGSFRANDHRSVEPSCLGQASPSEHDGNLSVIDLYGDEVESQRAEGEDDDDNNGDNGNEDLEEVHSDDLDLVPDDDNRQRVELEGAASATSANSNGINNTHFDRYGFKKQNNYISEAEYDKWWVEYSQYCVRRKHKWQLLLEKSGLPVTDDSPSRFPSKSERLKRYVRKGIPAEWRGNAWWHFARGQEKLNKNKGVYSQLLRKMKQIKKQNPNEKQVQDLDIIERDLNRTFPDNIHFQSSLHNKEGPPIIKSLRRVLVAFSLYNPKIGYCQSMNFLAGLLLLFLDEERAFWMLVIITSRYLPGVHNINLEGVNIDQGVLMLCVKEYIPEVWSYIKPSIDHHQKNNKTFSPSNKKVLFNMQKNEFLYRLPPITLCTASWFMSCFVGVVPIETTLRIWDCLFYEESHFLFKVSLAVLKLSEHDLSKIKPRNNSLNYSWGSNLNQRGGSMGQEDSDMEIFQVIQTFPKTLLNPNEIFEKIIFKRRFNLNRLDQDEIDRCRKFVAAQRLKFKTYGELLGNSTSEADLPINDNTDNKGIHITSDAVNEALSSEVYGFKKSLAGVHWNNSIKEKVKQMRKKKDKGD", "text": "FUNCTION: Regulates exocytosis by functioning as a GAP for SEC4. Stimulates specifically the GTPase activity of YPT6. Also required for efficient polarization of the actin patches. SUBCELLULAR LOCATION: Cytoplasm Bud Bud neck Note=Localizes to the presumptive bud site, the bud tip and the mother- bud neck."}
{"protein": "MNNYTIKDITRASGGFAMLAVDQREAMRLMFAAAGAKTPVADSVLTDFKVNAAKILSPYASAVLLDQQFCYRQAVEQNAVAKSCAMIVAADDFIPGNGIPVDNVVIDKKINAQAVKRDGAKALKLLVLWRSDEDAQQRLDMVKEFNELCHSNGLLSIIEPVVRPPRCGDKFDREQAIIDAAKELGDSGADLYKVEMPLYGKGARSDLLTASQRLNGHINMPWVILSSGVDEKLFPRAVRVAMEAGASGFLAGRAVWSSVIGLPDTELMLRDVSAPKLQRLGEIVDEMMAKRR", "text": "FUNCTION: Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA). SIMILARITY: Belongs to the aldolase LacD family."}
{"protein": "MILVEGKVAGKKYREPFSKGVLARSLTRSGMDPTDAYLLAAEVESYLKKEKKKIVTIDELVKIVYNKLKEKDEKIAEKYIRWRKIREYKEPLILLIAGASGVGTSSIAFEVANRLGIRNMISTDMIREVMRKMISKELIPSLHESTFTAYKSLRTPAPVEFDEVLVGFRDHVNVVTVGIEAVIERALTEGISIVIEGAHLVPGFIREELINKNNVAMFVLTVPDEKMHRSRFYSRCRQKWARRPLERYLKYFWAIRRIHDYIEMQARKHNIPIIENIDVVTTIDSIVKSLTEDLVHKDVGKYKG", "text": "FUNCTION: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3- diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3- bisphosphoglycerate, a thermoprotectant. SIMILARITY: Belongs to the 2-phosphoglycerate kinase family."}
{"protein": "MESLLRQLSICNELIAQGSCTAGHIDWLNDFCATFLDFASELKAHLPEVAPRWPAEGGTNIDVETIFLCLTQVVTCITQLERTINIEGASARATPMTRLHFLDRIDWCVRRIIFCLSQLHLQRANDQSNSLEDHTFVELMDLALDHLEAFMETLANTTPTNLLCIVEENELQLGSIVNHIVRHALAFANVALEADKKALSELCETLLSECATFLEDSGELNPGHRKLEGLSLERALYGLETYLNEALLHLIFACIVELENTPISKLRHAPDSEFTEQLVLDFDTNMDRIQQIGVLAIAFSQDIKTKTIVRSCLASLESLDACIVPALQSSALHPHHADILEHHFNEEILIFRNLIHEIIDSRSLINNYLDMLAESIHLAVKRPPRDHLLIVQMGSVLEEHFRLPVNYSELSQLDGKRLHTDFMLILSECLAVVSSPLGEPKRIVKRLKILYSVLAKLRHAIDRNKYVHEDSSASVPNVSSRRQFTNATRTLLRMKSKSKRQRSFVRQRRDCLVPNPQNCSISNSISHQGDLISFQLTEILRIN", "text": "FUNCTION: Required for the cellularization of the syncytial blastoderm embryo. Involved in the localization of the actin filaments just prior to and during plasma membrane invagination. Sry-alpha together with nullo and bnk may provide auxiliary functions, by acting both to stabilize a large and dynamic microfilament structure and regulate its functions (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Inner membrane-associated and cytoplasmic. Colocalizes with the structural transitions in the microfilament network during cellularization (By similarity)."}
{"protein": "MLVPPEMIAVQSKLIYQMNKYCADRVQARKAQIHKTIQEVCRVVQDVLKEVEVQEPRFISSLNDYNGRFDGLEVVSPTEFEIIIYLNQMGVLNFVDDGTLPGCAVLKLSDGRKRSMSLWVEFITASGYLSARKIRSRFQTLVAQACDKCAYRDSVKMIADTTEVKLRIRERIIVQITPAFKCAGLWPRSASHWPLPQIPWPHPNIVSEVKTEGFDMLSKECIALQGKNSAMEGDAWVLSFTEAENKLLQGGCRRRCLSILKTLRDRHLDLPGNPVTSYIMKTLLLYECEKHPREMEWDENCMGDRINGIFLQLISCLQCRRCPHYFLPNMDLFKGKSPGALENASKQVWRLTRIMLTNSRCLEEL", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the mab-21 family."}
{"protein": "MFMKSTGIVRKVDELGRVVIPIELRRTLGIAEKDALEIYVDDEKIILKKYKPNMTCQVTGEVSDDNLKLAGGKLVLSKEGAEQIISEIQNQLQNLK", "text": "FUNCTION: Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription. SIMILARITY: To B.subtilis Abh and SpoVT."}
{"protein": "MILSPADQERIETFWNYCLKHQYFNIGYPESADFDYSALFRFFKFSINNCGDWKDYSNYALNSFDFEKDVMAYFAEIFQIPFEESWGYVTNGGTEGNMFGCYLARELFPDSTLYYSKDTHYSVGKIAKLLQMKSCVIESLDNGEIDYDDLIHKIKTNKESHPIIFANIGTTMTGAIDDIEMIQERLAQIGIMRRDYYIHADAALSGMILPFVDHPQAFSFAHGIDSICVSGHKMIGSPIPCGIVVAKRQNVERISVDVDYISTRDQTISGSRNGHTVLLMWAAIRSQTNLQRRHRIQHCLKMAQYAVDRFQAVGIPAWRNPNSITVVFPCPSEHIWKKHYLATSGNMAHLITTAHHRDTRQIDSLIDDVIFDLQGASKRTVGF", "text": "SIMILARITY: Belongs to the group II decarboxylase family."}
{"protein": "MRTGKQYLKSLNDGRTVILDGEVVGNVLXH", "text": "FUNCTION: Monooxygenase that initiates the degradation of pyrrole-2- carboxylate, which allows Arthrobacter sp. strain Py1 to grow on pyrrole-2-carboxylate as sole carbon, nitrogen, and energy source. To a lesser extent, can also use pyrrole, pyrrole-2-aldehyde, and indole-2- carboxylate as substrate."}
{"protein": "MSTSGPAAPGDVPALPPPPPGPGSGPAPPAPAATARDTMDGRAELPIFPRAGVPPLAASDTVPAVPEGAGAARPAAPPRPTSFSVLDILDPNKFNSRRRRCVLLGPVVPATCAPCAPAACVAVPAASGRSPRAELERRALSAATGVAAAAGAEPTSAGDSYRADEAEANGYSSGSGRSPTADSEDEAPEDEDEEEAPEVQDAQGTEEPRGGSGGLGARGSGCPGAAEVEASPVDDTAAPGPRGNSPGAPGPPATATGAGSAGSTPQGAAVTTKPKRKRTGSDSKSGKPRRARTAFTYEQLVALENKFKATRYLSVCERLNLALSLSLTETQVKIWFQNRRTKWKKQNPGADTSAPTGGGGGPGPGAGPGAGLPGGLSPLSPSPPMGAPLALHGPAGYPAHSPGGLVCAAQLPFLSSPAVLSPFVLGSQTYGAPAFYAPHL", "text": "FUNCTION: May be required for the coordinated crosstalk of factors involved in the maintenance of energy homeostasis, possibly by regulating the transcription of specific factors involved in energy balance. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NK-1 homeobox family."}
{"protein": "GGGNDTSNETDTGTSGGETAAVDAEAVVQQKCISCHGGDLTGASAPAIDKAGANYSEEEILDIILNGQGGMPGGIAKGAEAEAVAAWLAEKK", "text": "FUNCTION: Natural electron acceptor for a formate dehydrogenase. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Note=May be released from the membrane upon cell disruption resulting in an abundant soluble form of the protein. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MRSIMEVETLKRLALMGANKEQVSLSSSIFATSLGMSPQTAARRLSALEEDGYITRVVTPEGQKVRITEKGITCLKSEYRDYCSIFEDGGAPVMRGKVVTGLGEGQYYISLDGYRNQFNDKLGFDPYPGTLNVRLTEPFIPAEHEAVVIAGFKGENRTFGGCKCYPVRIKGVRAAIIRPDRTSYPPNLIEIIAPIKLRESLGLRDGDEVEVTLE", "text": "FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). SIMILARITY: Belongs to the archaeal riboflavin kinase family."}
{"protein": "ADNKNPLEECFRETNYEEFLEIAR", "text": "FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (By similarity). Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis, and antiparasitic activities (By similarity). This protein has antibacterial activity (against E.coli, S.aureus, and B.dysenteriae), cytotoxic activity, as well as an ability to induce platelet aggregation (PubMed:12621545). Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation (By similarity). These different effects are probably due to different experimental conditions (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily."}
{"protein": "MDDDNGLELSLGLSLGGSSGKAKARDAPLEPKAEPQVEESSSKGGLQTPDAPSGKFYQKSADNHEQNSKQRHSPVAPQFGNFWGQPGNSSGPVVDGSVEPVSHQPQLSSYQDGRMPINSGNNSEEQKPVSGNHKLPSEEMNFQKKHQTASDQPDAFSKSSDGGAKNAPISISTDDGSTGENEDVAESEAEGSNSWLVAQREDSAKGSVVNKGSDRKRSADAAADGFKGKRQPSFSGSESSSGKLTPGNLISMQASNVVALPYQVPGQVSGPPVLTNAPNFHPVCTVQLRPPTNGGLAVQTMGSASQVAFGYPAVQLPTLETGSSWAFGAPPQALSSFTAKDKADQTGTKQVDDGKKPQEAGASSSAHAEDEKKADRGLSLMGSAIRPGIAPNVKFGGSGSYPDLPWVSTIGAGPNGRTISGVTYKFGRNEVKIVCACHGTHMSPEEFMRHASADAPAQDNSATLPAFPAGNQATSAEN", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Ninja family."}
{"protein": "MFFHATLARSFISALSVRGDDDAVDRLNYYYTPLILAVCCLVISAKQYGGTPIECWVNPHSRESMEEYIESYCWIQNTYWIPMYENVPDDHTAREEKQIGYYQWVPFILIAEALMFSLPCIFWRLCSFQSGLNIQTLINAACDAQALLDYSDRQKAVEAITCNFVDNLDLQSPNGRIRARGWIARIKFSRFLSGQCISIVYSFTKLLYSVNVVAQFFILNACLKSSEFVFFGFQVLSDIWAGRPWTETGHFPRVTLCDFEVRYLANLNRYTVQCALLINIINEKVFAFLWCWYMILAIITTCSFIYWIANSFIHSEKVDYVMKFIQIAESSEYKKLQKFEKDATVERLYTVIAFAPHLLDSFVSDFLKSDGILMLRMISNHAGDMIVVQLVRNLWQEYRERNWREFEEHEEMKDVEMRRIQGTRERIVIANPGQTKSFL", "text": "FUNCTION: Structural component of the gap junctions that specifically coordinates left-right asymmetry in the developing nervous system. Acts by forming gap junction network linking embryonic neurons and providing electrical coupling between cells, leading to promote or inhibit AWC signaling (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. SIMILARITY: Belongs to the pannexin family."}
{"protein": "MTFFEQVRRLRSAATTLPRRLAIAAMGAVLVYGLVGTFGGPATAGAFSRPGLPVEYLQVPSASMGRDIKVQFQGGGPHAVYLLDGLRAQDDYNGWDINTPAFEEYYQSGLSVIMPVGGQSSFYTDWYQPSQSNGQNYTYKWETFLTREMPAWLQANKGVSPTGNAAVGLSMSGGSALILAAYYPQQFPYAASLSGFLNPSEGWWPTLIGLAMNDSGGYNANSMWGPSSDPAWKRNDPMVQIPRLVANNTRIWVYCGNGTPSDLGGDNIPAKFLEGLTLRTNQTFRDTYAADGGRNGVFNFPPNGTHSWPYWNEQLVAMKADIQHVLNGATPPAAPAAPAA", "text": "FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha- trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM (By similarity). FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha- trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the mycobacterial A85 antigen family."}
{"protein": "MKHYVLVHGGCHGAWCWYKVKPVLEASGHRVTVVDLTASGVNMSKVEEIQTLADYAKPLLEVLESFGSEDKVILVAHSLGGISVGLAADMFPSKISVAVFITSFMPDTTNPHLFMFSKSFVGALWSLRHMGHMIVL", "text": "SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase family."}
{"protein": "MSAGVRSEPMKVVFINTQYVQTDARSFKTIVQELTGKNAVVADGPYEFSGQGYGGKDSSQRFCGVGKEAERGVETTEFDSFFREMPPVGELYNLWSDH", "text": "FUNCTION: May modulate WRKY transcription factor activities. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MALLDLKQFYELREGCDDKGILVMDGDWLVFQAMSAAEFDASWEEEIWHRCCDHAKARQILEDSIKSYETRKKAWAGAPIVLAFTDSVNWRKELVDPNYKANRKAVKKPVGYFEFLDALFEREEFYCIREPMLEGDDVMGVIASNPSAFGARKAVIISCDKDFKTIPNCDFLWCTTGNILTQTEESADWWHLFQTIKGDITDGYSGIAGWGDTAEDFLNNPFITEPKTSVLKSGKNKGQEVTKWVKRDPEPHETLWDCIKSIGAKAGMTEEDIIKQGQMARILRFNEYNFIDKEIYLWRP", "text": "FUNCTION: Plays an essential role in phage DNA replication by participating in the removal of DNA-linked RNA primers. Participates also in T7 DNA packaging, host DNA degradation and phage genetic recombination."}
{"protein": "MENEEGKREMTKKQSSRFKSICVFCGSSNGNKASYQDAAIDLAKELVMRKIDLVYGGGSIGLMGLVSQAVHDGGRHVIGVIPKLLMLQELTGETVGEVKEVADMHQRKAVMAKHSDAFITLPGGYGTLEELLEVITWAQLGIHDKPVGLLNVDGYYDALLLFIDKAVEEGFILPTARHIIVSAPTARELFIKLEEYVPQHK", "text": "FUNCTION: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms (By similarity). SIMILARITY: Belongs to the LOG family."}
{"protein": "MTPPKLRASLSPSLLLLLSGCLLAAARREKGAASNVAEPVPGPTGGSSGRFLSPEQHACSWQLLLPAPEAAAGSELALRCQSPDGARHQCAYRGHPERCAAYAARRAHFWKQVLGGLRKKRRPCHDPAPLQARLCAGKKGHGAELRLVPRASPPARPTVAGFAGESKPRARNRGRTRERASGPAAGTPPPQSAPPKENPSERKTNEGKRKAALVPNEERPMGTGPDPDGLDGNAELTETYCAEKWHSLCNFFVNFWNG", "text": "FUNCTION: Heparin-binding protein which binds to FGF2, prevents binding of FGF2 to heparin and probably inhibits immobilization of FGF2 on extracellular matrix glycosaminoglycans, allowing its release and subsequent activation of FGFR signaling which leads to increased vascular permeability. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the fibroblast growth factor-binding protein family."}
{"protein": "MAASRWLRAVLLFLCASDLLLLPPPNAYAADTPGEATPPPRKKKDIRDYNDADMARLLEQWEKDDDIEEGDLPEHKRPSAPIDFSKLDPGKPESILKMTKKGKTLMMFVTVSGNPTEKETEEITSLWQGSLFNANYDVQRFIVGSDRAIFMLRDGSYAWEIKDFLVSQDRCAEVTLEGQMYPGKGGGSKEKNKTKPEKAKKKEGDPKPRASKEDNRAGSRREDL", "text": "FUNCTION: Chaperone specifically assisting the folding of beta- propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs) (PubMed:31564437). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction (PubMed:12581525, PubMed:21397183). Plays an essential role in neuromuscular junction (NMJ) formation by promoting cell-surface expression of LRP4 (PubMed:24140340). May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE) cells. SUBCELLULAR LOCATION: Endoplasmic reticulum Note=Released from apoptotic cells and shed photoreceptor outer segments (PubMed:27184668). SIMILARITY: Belongs to the MESD family."}
{"protein": "MSWAQAILLARGASRGWGGICSTALTGAPFSQVPPQAPRGLRCSAAAHNPDSSLVPHPPEPPRRPVKALAVHEELFRPALDGARNKANFVRAVQNFTEYNVHKRGHVDFIYLALRKMREYGVERDLSVYNLLLDIFPKEVFRPRNIFHSIFLHYPRQQECGIAVLEQMENHGVMPNKETEFLLLQIFGRKSYPMLKLVRMKLWFTRFKNINPFPVPRDLPQDPVDLASLALRHMEPDLSARVTTYQMPLLKDSPNAMDPTETHIVGIQSPEQQSALARHDPARPIFVEGPFSLWLRDKCVYYHILRADLLPPEEREVEEIPEEWNLYYPMQLDLAYGRSSWDDYEFNIDEVEEGPVFAICVAGAHDQATLAKWIQGLQETNPALARIPVVFRLSGSSGELLPSSSELEEPPPPPPEGQEEEEDSQQRQQQGQS", "text": "FUNCTION: As part of the MCIA complex, involved in the assembly of the mitochondrial complex I. FUNCTION: Adapter protein that plays a role in different signaling pathways including TLRs and IL-1 pathways or innate antiviral induction signaling. Plays a role in the activation of NF-kappa-B by forming a signal complex with TRAF6 and TAK1/MAP3K7 to activate TAK1/MAP3K7 leading to activation of IKKs. Once ubiquitinated, interacts with the dissociated RELA and NFKB1 proteins and translocates to the nucleus where it induces NF-kappa-B-dependent gene expression. Plays a role in innate antiviral immune response by bridging the pattern recognition receptors RIGI and MDA5/IFIT1 to the MAVS complex at the mitochondrion (By similarity). Promotes proteolytic activation of MAP3K1. Involved in the BMP signaling pathway. Required for normal embryonic development (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion. SIMILARITY: Belongs to the ECSIT family."}
{"protein": "MPRGVAVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYIDSKGLVTWLKLNKKVVAQDLRKDNPLQFKFRVKFYPEEVTEELIQEITQRLFFLQIKEGILSDEVYCPPETSVLLASYAAQAKYGPHSASTKARLTEDTNILPKRVIEQHKMTKEQWYERVSNWHQEHLSLSKEDAITEYMKIAQDLEMYGVNYFEIRNKKGTDLWLGVDALGLNVYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIEKKAPDFVFYASRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAKEEKQAKKLEREQLAIEMKKRQETEEKYKRLQQQIREKELAEEKNREDLKRWEEESRAMQEKLKQQQMESEEYQSKVAAMEMQMNEATLEREMTAQEKEEMRARVEALAEEKARLEQSREESLKESAEFAEKLRLSQERERELQEAQEAAAAQHAAQLAAQREAQQLIPKDEGEEDEQDHELEVQQDDNDDLDDKESYLPDKHLLDKLQKLQSELQAMKDESKGEDRYDKIHQENIRAGRDKYQTLRNIRSGNTRQRIDTFENI", "text": "FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton Cell projection."}
{"protein": "MASLILGAPPRVTVALPSSRLSSSHSETAGVSLSCFTHQFSLSTSSSSSIPLVYCGRGDRKTAKGKRFNHSFGNARPRNKSKGRGPERVPVPPAPPRKDKFENDEKIKIDIDESLFSN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bTHX family."}
{"protein": "MSWAKQRVPFLDDDDGEEENDVQDDVDSPVPTRPLVIDEDAEPAAGTSGGLEGGGGDDEDGEDGHALPDLDDDLLLQFEPMLPRVYDLLLPSLDARLNFVNAGQKYAAFLKYVHGDCATCSHGEILREKTQLLTAIVSKLMDINGILEGKDESAPGK", "text": "FUNCTION: Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM1 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. SUBCELLULAR LOCATION: Host nucleus Note=Found associated with the external surface of the viral capsid during assembly and DNA packaging, but seems absent in extracellular mature virions. SIMILARITY: Belongs to the herpesviridae TRM2 protein family."}
{"protein": "MKPSCYDNVGKAVKRKCETTIAQKRDISLMDTGANTYLIRPNYKDKFKAGVAKECIGEILREQLYGVQYDPEEVPTLSRSLADSIKHKLKDMAFDRYKFIVQVVIGEQRGEGVKMAARCFWDADTDNYAQEIYMNDSLFCVAAAFAVYYY", "text": "FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system (By similarity). Required for proper retrograde ciliary transport (PubMed:26044572). SUBCELLULAR LOCATION: Dynein axonemal particle. SIMILARITY: Belongs to the dynein light chain Tctex-type family."}
{"protein": "MARSVTVIFLVLVSLAVVLAIQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDWSFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM", "text": "FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-2-microglobulin family."}
{"protein": "MFCIIHFGNPKNDKFLGSSTLYSQKLKTNNIKILCLQVFYYNIYESTNNNNNNKNKNKTLLLNNIRTYSTLSKGALSTTTTATTKKMSMDDSFELPTNLNHFLSYVPSLEYHMHKGQCGRIGVFGGSAEYTGAPFFAGITSLRLGADIVHIFAPSEGGTATAIKTLSPELIVHPLDQQMDPSTIIPWLLSIHVLIIGPGLGRSSIAWKSAKEVIKAARNINLPMVLDGDALRLICEDLELVKGYDKVILTPNFVEYRALSDAAKKLNNDNSNNILSPSDLAKALGNVVIVQKGQEDIITDGTISYSCDKAGMPRRCGGQGDVLAGVIGTFYAWTQNALKGKTSEELEHLKESIGENQSAAASAAYAGCVLVRYAAKLAFKNNRRSTITDDIIKSVPNALVWGFLTDDRGRPTI", "text": "FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. SIMILARITY: Belongs to the NnrD/CARKD family."}
{"protein": "MDVDALLQSIPPLAVYLLVSGVVGVESLGIPLPGEVVLVSAALLSSRHDLAVSSIGVGVVAVIGAAVGDSIGYAIGRRFGMPLFDHLGRRFPKHFGPGHVALVERLFNRWGVRAVFFGRFIALLRILAGPLAGALKMHYPRFLAANVSGAICWAGGTTALVYFAGMAAERWMERFSWIALIITVVVGIIAAILLRERTSRIIAELEMEYKNRRH", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DedA family."}
{"protein": "MRITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVKAIKEHGLRANYNGEELTAHLSVELQSEISSKEKTDLIILFTKAMQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLISGEEETAKKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAEVVQHVETCFDPSTIGLHYPSMYQDLIKNNRLTEIDYINGAVSRKGKKYNVATPYCDFLTQLVHSKEELLKAK", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ketopantoate reductase family."}
{"protein": "MSLFHHLVSRFLSLWLLIFLVFLVLSLGKSQKEALQVKVGIVLGSNVTLADLSLRAINMSLSEFYNTHNGFKTRIVLNVRDSKQTVVGAAASALYLIKKREVVAIIGPGTSMQAPFLINLGNQSKVPIISFSATSPLLDSLRSPYFIRATHDDSSQVQAISAIIESFRWREVVPIYVDNEFGEGILPNLVDAFQEINVRIRYRSAISLHYSDDQIKKELYKLMTMPTRVFIVHMLPDLGSRLFSIAKEIDMLSKGYVWIVTNGIADLMSIMGESSLVNMHGVLGVKTYFAKSKELLHLEARWQKRFGGEELNNFACWAYDAATALAMSVEEIRHVNMSFNTTKEDTSRDDIGTDLDELGVALSGPKLLDALSTVSFKGVAGRFQLKNGKLEATTFKIINIEESGERTVGFWKSKVGLVKSLRVDKVSHSSRRLRPIIWPGDTIFVPKGWEFPTNAKKLRIAVPKKDGFNNFVEVTKDENTNVPTVTGFCIDVFNTVMSQMPYAVSYEYIPFDTPDGKPRGSYDEMVYNVFLGEFDGAVGDTTILANRSHYVDFALPYSETGIVFLVPVKDGKEKGEWVFLKPLTKELWLVTAASFLYIGIMVWIFEYQADEEFREQMIIDKISSVFYFSFSTLFFAHRRPSESFFTRVLVVVWCFVLLILTQSYTATLTSMLTVQELRPTVRHMDDLRKSGVNIGYQTGSFTFERLKQMRFDESRLKTYNSPEEMRELFLHKSSNGGIDAAFDEVAYIKLFMAKYCSEYSIIEPTFKADGFGFAFPLGSPLVSDISRQILNITEGDAMKAIENKWFLGEKHCLDSTTSDSPIQLDHHSFEALFLIVFVVSVILLLLMLASRGYQERQHNASPNLPNDQANAAQEEVNEEGNVGDHIVEVDTALVRRKKLTSNTIPIRRVAPLSRLKSA", "text": "FUNCTION: Glutamate-gated receptor that probably acts as non-selective cation channel. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family."}
{"protein": "MAKFIKSGKVAIVVRGRYAGKKVVIVKPHDEGTKSHPFPHAIVAGIERAPLKVTKKMDAKKVTKRTKVKPFVKLVNYNHLMPTRYSLDVESFKSAVTSEALEEPSQREEAKKVVKKAFEEKHQAGKNKWFFQKLHF", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL27 family."}
{"protein": "MGAYLSQPNTVKCSGDGVGASRLPLPYGFSAMQGWRVSMEDAHNCIPELDSETAMFSVYDGHGGEEVALYCAKYLPDIIKDQKAYKEGKLQKALEDAFLAIDAKLTTEEVIKELAQIAGRPTEDEDEKEKVADEDDVDNEEAALLHEEATMTIEELLTRYGQNCHKGAPHSKSGAGTGEEPGSQGLNGEAGPEDPSRETSAEENGPTAKAHTGLSSNSECGTEAGQGGEPGTPTGEAGPSCSSASDKLPRVAKSKFFEDSEDESDEAEEEEEDSEECSEEEDGYSSEEAENEEDEDDTEEAEEDDEEEEMMVPGMEGKEEPGSDSGTTAVVALIRGKQLIVANAGDSRCVVSEAGKALDMSYDHKPEDEVELARIKNAGGKVTMDGRVNGGLNLSRAIGDHFYKRNKNLPPEEQMISALPDIKVLTLTDDHEFMVIACDGIWNVMSSQEVIDFIQSKISQRDENGELRLLSSIVEELLDQCLAPDTSGDGTGCDNMTCIIICFKPRNTAAPQPESGKRKLEEVLSTEGAEENGNSDKKKAKRD", "text": "SUBCELLULAR LOCATION: Cytoplasm Membrane; Lipid-anchor. SIMILARITY: Belongs to the PP2C family."}
{"protein": "MVAYRFLTLISLGLGSHCASALQYGYNQVSTHKDSAVVAGAFPAINGTHLQSPAFTSPGTVPRGFSDGTSGPTRDETMEGFMRRLARSNSWMTYHKADFKSEEGRKFPYMYLSASKSSIEKPSSHKLRVWLQGGVHGNEPAGDQSMLALLGDLAANQKWAAKLLEKMDILVLPRYNPDGVFYFQRYLATNFDPNRDHIKLARQQTRDIKELFARFSPHIATDMHEFTAGRAFGPKKDIIYAADALFSSAKNLNIDEGIRQLSEKLFAKRMGKDIEAAGLRWDPYIIQGESSSSKLLLREAGTDAKIGRNAMGLSQCVVFLCETRGIGIADQHFERRTLSGLVMVKSILQTAVDNFDEVYNTIERGIRRFTNSRNDIVLTDRSPIMERTFGMLNTTDATLFDYPIDFATTTPAQAVLTRSRPRAYLIPPSWPDIVKRLEVFGVKADKLPHSYVGPVEALNVTSVTFDKEYYEGVVTTTVETKLVERNIRLPAGSYLVKTNQKNAALAFVALEPENIDSFASFGVIPVSTGDQYPIFRVE", "text": "FUNCTION: Extracellular metalloprotease that contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M14 family."}
{"protein": "MLITLGWASLAALFSFSIAMVVWGRNGDGSMNF", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetN family."}
{"protein": "QFRPSYQIPP", "text": "FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent (By similarity). FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-potentiating peptide family."}
{"protein": "MFKNLIFLFFIGLATAIRFNLTDLECSRLRGPHCGTYLLKVVGTNATYVGEKSFIGLDALTESKGEFFQRMLEQEPRLIPRLFTIAENDTANFTPLTFTTYLKTCNPQSIENAMIPFVNTVTSEISFDAWAYTAQNSSRITGLSNQLMNSTLYNVQVATCTPGFSALLLDSPTINVFNNEEGMPSWCQPIELTPVCPLDEGFN", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol Note=Intracellular soluble fraction. SIMILARITY: Belongs to the VEL1 family."}
{"protein": "MTILVLGGRGKTASRLAALLDQAKTPFLVGSSSASPSDPYKSSQFNWLKRDTWERPFEQAGKHGLGTISSIYLVGPPVMDIAPPMIEFVDLARAKGVQRFVLLSASTVEKGGHSMGQVHAYLDSLAEVEYVALRPTWFMENLLEDPSREWIKNENQIITATGDGKIPFVSADDIASVAFHCLTEWGSHKTEYVILGPELLSYGQVAEILTTILGKKIIHRSLTETGLAELLVKKAGIPADFAAMLSAMEVDVKNGPQEVLNNSVVEVTGNPPRYFKDVAEHEKHVWA", "text": "FUNCTION: Festuclavine synthase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids (PubMed:28620689). The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4- dimethylallyl-L-tryptophan (PubMed:28620689). The second step is catalyzed by the methyltransferase ifgB that methylates 4- dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan (PubMed:28620689). The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:28902217). The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7- didehydroergoline (PubMed:28620689, PubMed:28902217). The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8- dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689). Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A (PubMed:28620689). Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689, PubMed:28902217). The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions (PubMed:28902217). SIMILARITY: Belongs to the fgaFS/easG family."}
{"protein": "MHSTMSVQHGLVALVLIGCLAHPWHVEACSSRTVPKPRSSISSSMSGTALPPTQAPVTSSTTMRTTTTTTPRPNITFPTYKCPETFDAWYCLNDAHCFAVKIADLPVYSCECAIGFMGQRCEYKEIDNTYLPKRPRPMLEKASIASGAMCALVFMLFVCLAFYLRFEQRAAKKAYELEQELQQEYDDDDGQCECCRNRCCPDGQEPVILERKLPYHMRLEHALMSFAIRRSNKL", "text": "FUNCTION: Ligand for the EGF receptor (Gurken). Involved in a number of unrelated developmental choices, for example, dorsal-ventral axis formation, glial migration, sensory organ determination, and muscle development. It is required for photoreceptor determination. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single- pass type I membrane protein Golgi apparatus membrane; Single-pass type I membrane protein Note=Relocalization to the Golgi apparatus and the plasma membrane is mediated by Star. In the presence of Rhomboid, Spitz is found only in the Golgi, not at the cell surface."}
{"protein": "MNSTGFNDTDSALFSNTSFLSCCNVSSVVTDSGFVSAALDERSVFIMRTVQIAVMCVLALTVVFGIFFLGCNLLIKSEGMINFLVTDRRPSKDVEAVIVGSY", "text": "FUNCTION: May be involved in the regulation of p53-dependent G2 arrest of the cell cycle. SUBCELLULAR LOCATION: Cytoplasm Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the reprimo family."}
{"protein": "MGISLSVLDIKIISTTVLFILSLLAGIAPYWMRNLNNSSRYLSWSNTFAGGVFFGAGMLHLFATADEDLQPYVQKYNYPFAALCLCVGFLITLFLELIINSIFIKSNTFASLHGHSHSHVHLSHGHSHHGKDNGSNGNPGSGVGIGMGSVGALNSKKNKTTSPTITPTTPSEGTTTTTTTTTATTAATAKEIVLEDEDEDEEKDIMDEIIIPDDYDENDDEQIYKKKQSKCARTKFRKFIDTIPTFSSTSTSSTSSSTKISEKQRLLDSSNSYYYNQNKYKGIIGSHIDIDKSGSGVGGFSNNNNNNNNNNNNNNKNNNNNNNNNFRTEIIIQPISTTSNNSVHHYPSSSVNYHPFITTTTTTCSNDNSNSNNNNSSNNNSSSANITPNTNKILSSSKSLSYRYNGDDEEPDIIIDYDDIDYNQEGRTRGNSLGSDSNVHNERIVLINSGIGNSGNIGSNNNNNNNGGGGGGGGNSNIDYNDNEENNNNNNKIESEILIKDTTTDSIKNMKGGEHQHQHLHQQEIIVVTKKSNILLPFILVIALSIHSLFEGLAMGVQSSEIRVFDILIAIFAHKILASFALGISTITSSNEKPSFLKLFLLVFVFSLTSPIGSILGMVIVGSGVTGSMVPPILQGIASGTFLYVAVVEIIPKELSHDSNDILIKSFLLLLGFSGMAVVAIWV", "text": "FUNCTION: May transport divalent cations (By similarity). May participate, with dstA, in the regulation of the differentiation of stalk cells during development. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family."}
{"protein": "MASNKVVISALLVVVVSVLAATTTMADHHQEQVVYTPGQLCQPGIGYPTYPLPRCRAFVKRQCVAPGTVDEQVRRGCCRQLAAIDSSWCRCDALNHMLRIIYRESGAADAGHPMAEVFRGCRRGDIERAAASLPAFCNVDIPNGVGGVCYWLPGTGY", "text": "FUNCTION: Seed storage protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cereal trypsin/alpha-amylase inhibitor family."}
{"protein": "METNPRKLRSYSYICLIVCIFVLVVCAILSRAEEKEGKGENDDHIPKIYSILVEGEPLAFRASTNINSKAMALEAKKIEEIHDEILGSTLEKGSYTKLYSFKHVINAIAVRTTASQAKKLGKTKGVKAVEEDKGVKLMTTYTPDFLELPQQVWQKISNEGDRRAGEDIVIGFVDTGINPTHPSFAALDLTNPYSSNLSRLHFSGDCEIGPFFPPGSCNGKIISARFFSAGARASGALNSSLDILSPFDASGHGSHVASIAAGNAGVPVIVDGFFYGRASGMAPRSRIAVYKAIYPSIGTLVDVIAAIDQAIMDGVDVLTLSVGPDEPPVDKPTVLGIFDLAMLLARKAGVFVVQAVGNNGPSPSSVLSYSPWVVGVAAGNTDRSYPAPLILDGGQTVQGVGLSGPTLGAPLVQHRLVLAKDAVRTNGSVLQPLTRDIEECQRPENFDPAAVFGSIVICTFSDGFYNQMSTVLAITQTARTLGFMGFILIANPRFGDYVAEPVIFSAPGILIPTVSAAQIILRYYEEKTFRDTRGVATQFGARARIGEGRNSVFAGKAPVVSRFSSRGPAFIDATRSPLDVLKPDILAPGHQIWGAWSLPSAFDPILTGRSFAILSGTSMATPHIAGIGALIKQLNPSWTPAMIASAISTTANEYDSNGEIISAEYYELSRLFPSNHFDHGAGHVNPARALDPGLVLPAGFEDYISFLCSLPNISPATIRDATGVLCTTTLSHPANLNHPSVTISALKESLVVRRSFQDVSNKTETYLGSVLPPNGTTVRLTPTWFTVPPQKTQDLDIEFNVTQVLNKFTFGEVVLTGSLNHIIRIPLSVKTI", "text": "FUNCTION: Serine protease required for epidermal surface formation in embryos and juvenile plants (PubMed:11731449, PubMed:17376810, PubMed:23318634). Involved in embryonic cuticle formation downstream of BHLH95/ZOU (PubMed:23318634). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MVKRRLSAFGNAFLIYFIIFRLCCCSPQTSHWCKYPALCLKSPDTHNENLVCDAYLSVIATKSEEKEASNPTTWDFTPTNKYQEPSFHTKTSLNGSDTISSNFLSKYEYSNGTSTSEFIDSISPPLVNETSTISSSKKLEQNYSVTEVIDTNIITSSSVTLPISEDGSSTSAAATIDSNIDEKTVAFSEEKRFNFASTDCAAAVIKTNPEAVGSSSILTENKDKYMLNKCSAENKFVVIELCEDIYVDTVQIANFEFFSSIFRDFKVSVSGKYPKYESSWMELGTFTALNLRTLQSFHIENPLIWAKYLKIEFLTHYGSEFYCPVSLLRVYGKTMIEEFEEANEDFLEQKVNDGSAIKADEIRKPQESPIFVDEEDTDVQSKPVRKNPSVELNSTDTLLSSTVISKSLSTVVIGNETGKSESYPATSTRSFNDISPSSSSSYSTAQISTFPSNQESIYKNINKRLSTLEERKKAFDEIVEKILTNYGKHNAKNMNFTQLLHELNSTLQLEISKLSKSVVKPSLFALQAKLELLSAENEYFQSQITSLYQESSFQKRLLMLQLTVLIVLTVYMAVSRLPENLPTTRSSSNNPIEASRPPFSRDEQDISKANDFRVSASSAVYTVGPELLQRKKRDPNTSIRSIHEREQDKIIHSRSHSVC", "text": "FUNCTION: May be involved in membrane protein folding. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the SLP1 family."}
{"protein": "MTTSQKHRDFVAEPMGEKPVGSLAGIGDALGKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL", "text": "FUNCTION: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. SUBCELLULAR LOCATION: Nucleus Chromosome Nucleus envelope Cytoplasm Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. SIMILARITY: Belongs to the BAF family."}
{"protein": "MNMPQSLGNQPLPPEPPSLGTPAEGPGTTSPPEHCWPVRPTLRNELDTFSVHFYIFFGPSVALPPERPAVFAMRLLPVLDSGGVLSLELQLNASSVRQENVTVFGCLTHEVPLSLGDAAVTCSKESLAGFLLSVSATTRVARLRIPFPQTGTWFLALRSLCGVGPRFVRCRNATAEVRMRTFLSPCVDDCGPYGQCKLLRTHNYLYAACECKAGWRGWGCTDSADALTYGFQLLSTLLLCLSNLMFLPPVVLAIRSRYVLEAAVYTFTMFFSTFYHACDQPGIVVFCIMDYDVLQFCDFLGSLMSVWVTVIAMARLQPVVKQVLYLLGAMLLSMALQLDRHGLWNLLGPSLFALGILATAWTVRSVRRRHCYPPTWRRWLFYLCPGSLIAGSAVLLYAFVETRDNYFYIHSIWHMLIAGSVGFLLPPRAKTDHGVPSGARARGCGYQLCINEQEELGLVGPGGATVSSICAS", "text": "FUNCTION: May function as a regulator of the EGFR pathway. Probable tumor suppressor which may function in cell growth, proliferation and adhesion. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Multi-pass membrane protein Cytoplasm Nucleus Mitochondrion Endoplasmic reticulum Note=Also detected in mitochondrion and endoplasmic reticulum (PubMed:17641538). SIMILARITY: Belongs to the TMEM8 family."}
{"protein": "MSTGAQTKAAAASQHADGPRLLADVGGTNARFALETGPGEITQIRVYPGAEYPTLTDAIRKYLKDAKIGRVNHAAIAIANPVDGDQVRMTNHNWSFSIEATRRALGFDTLLVVNDFTALAMALPGLTDAQRVQIGGGTRRQNSVIGLMGPGTGLGVSGLIPADDRWIALGSEGGHATFAPMDEREDLVLQYARRKYPHVSFERVCAGPGMEIIYRALAARDKKRIAANVDTADIVERAHAGDALALEAVECFCAILGTFAGNLAVTLGALGGIYIGGGVVPKLGELFMRSPFRARFEAKGRFEAYLANIPTYLITAEYPAFLGVSAILAEQLSNRTGGASSAVFERIRQMRDALTPAERRVADLALNHPRSIINDPIVNIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTGTIPMSHSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAYGDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITSSNTPLAKRATVALETDHIEMRESQLSMISRILHLVMIDILAVGVAIRRAAPNAELAEAMARAKARAGASAGDEAADVLDWLSHGAAPAAKD", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the bacterial glucokinase family."}
{"protein": "MYMQVETRTSTRLHLKRAPGIRSWSLLVGILSTGLAAAYYSGDSLGWKLFYVTGCLFVAVQNLEDWEEAIFNKNTGKVILKTFSLYKKLLTLLRAGHDQVVVLLKDIQDVNVEEEKVRYFGKGYMVVLRFATGFSHPLTQSAVMGRRSDVEAIAKLITSFLELHRLESPSERSQSSDSEPDGPGGQS", "text": "FUNCTION: Functions as a chaperone necessary for a stable expression of the CYBA and CYBB subunits of the cytochrome b-245 heterodimer (By similarity). Controls the phagocyte respiratory burst and is essential for innate immunity (PubMed:28351984). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CYBC1 family."}
{"protein": "MAANATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSVSVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI", "text": "FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP- bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. Involved in craniofacial development. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites. SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily."}
{"protein": "MVWQGPQRRLLGSLNGTSPATPHFELAANQTGPRCLEVSIPNGLFLSLGLVSVVENVLVVAAIAKNRNLHSPMYYFIGCLAVSDLLVSVTNVLETAVMLLVEAGALAAQAAVVQQLDDIIDVLICGSMVSSLCFLGAIAVDRYLSIFYALRYHSIVTLPRAWRAISAIWVASVLSSTLFIAYYNHTAVLLCLVSFFVAMLVLMAVLYVHMLARARQHARGIARLRKRQHSVHQGFGLKGAATLTILLGIFFLCWGPFFLHLSLMVLCPQHPICGCVFQNFNLFLTLIICNSIIDPFIYAFRSQELRKTLQEVVLCSW", "text": "FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH (By similarity). The activity of this receptor is mediated by G proteins which activate adenylate cyclase (By similarity). Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSIRVGQKAPDFTATAVFDQEFGTIRLSDYLDKRYVVLFFYPLDFTFVCPTEITAFSDRFKEFKELSTEVLGVSVDSEFSHLAWTQIDRKSGGLGELEYPLVSDLKKEISSSYNVLTEDGVALRALFIIDKEGIIQHSTVNNLSFGRNVDEALRTLQAIQYSQENPDEVCPVNWKPGSKTMKPDPVGSKVYFEAI", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily."}
{"protein": "MDNNSVDSLIPIIITGPSGVGKGTLIDKLRKEYEGSFGHIVSHTTRKPREGEINGVHYHFTDIPTMTEGIKNGDFIEHANVHGNFYGTSKKALKDVSDKNKICILDIDVQGCESVKKANIPCKFIFISPPTFETLQERLIGRGTENEETLKKRLETAKKEMVYRDIPGFFDHVIVNNVLDVAYGELKSIISPFISFQSKSNK", "text": "FUNCTION: Essential for recycling GMP and indirectly, cGMP. SIMILARITY: Belongs to the guanylate kinase family."}
{"protein": "MASQPLEEPAESQASDELECKICYNRYNLKQRKPKVLECCHRVCAKCLYKIIDFGDSPQGVIVCPFCRFETCLPDDEVSSLPDDNNILVNLTCGGKGKKCLPENPTELLLTPKRLASLVSPSHTSSNCLVITIMEVQRESSPSLSSTPVVEFYRPASFDSVTTVSHNWTVWNCTSLLFQTSIRVLVWLLGLLYFSSLPLGIYLLVSKKVTLGVVFVSLVPSSLVILMVYGFCQCVCHEFLDCMALPS", "text": "FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway. Also plays a role in the inhibition of TLR-triggered innate immune response by mediating 'Lys'-48-linked ubiquitination and subsequent degradation of NF-kappa-B component RELA. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cytoplasm."}
{"protein": "MFVLFLIVCYFILIFNIIVPKIADKLRLEHEAFTKYRQIYGNKFRCIGDNLINYSFTPFGVKANYLVNKNTKMPAICNDIKNINSLIAVTCDDASKFIKHRNICERAYTELFL", "text": "FUNCTION: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. SUBCELLULAR LOCATION: Virion membrane; Single-pass type III membrane protein Note=Component of the mature virion (MV) membrane. The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis (By similarity). SIMILARITY: Belongs to the chordopoxvirinae A21 family."}
{"protein": "MPRSLSRSVSPRPRSPSLSPPRPDSRSSRGRSLTPDDIPAYKRKRSPSPNPRDRPASPPTRRRRSQSPYRNSNRAEIDRPNVKDIDPNRRRARENALLEKQINMALADDGDADGTVATTKKSADEIARAEFAKLLGSRSGGAYIPPAKLRAMQAEAAKDKTSAEYQRISWDALKKSINGLINKVNISNIKHIVPELFGENLIRGRGLFARSVMRAQASSLPFTPVFAALVAIINTKLPQVGELVLIRLISQFRRAYKRNDKTVCHATSTFIAHLCNQYVAHEIVALQILLLCLDRPTDDSIEVAVGFMREVGQFLSENSPKANNTVFERFRAVLHEGQISKRCQYMIEVLFQVRKDKYKDNPAVPEGLDLVEEEEQITHRVTLDDELQVQESLNLFKADPNFVQNEERYNAIKREILGDSDDESGTESGSEYSESEDDEDEDVAPEKAGIQDMTETNLINLRRTIYLTIMNSLNFEEAVHKLMKVNIPEGREIELCNMVIECCSQERTYSNFYGLIGERFCKLHRIWTDAFQEAFQKYYDTIHRYETNKLRNIGRFFGHLLASDGISWAVLHVVHMNEEETTSSSRIFVKIVLQEMVEEMGINRVAERFRIPDLKPAFAGMFPMDNPKNARFSINYFTSIGMGKVTEDMREYLQNAPKLLAAQQAALAAAESSDSDTDSSSDISSSSDSDSDTDSDASSYSRRSRRRRYSSDSRSPPPRRRRYSSDSRSPSPPPRRRQYSDEPRSPSPPPRRRRYSDDSRSPSPPPRRRYSGDSRSPSPPPRRRYADDSRSPSPPPHRRRYSDDSRSPSPPPRRRRYSDNSRSPSPPPRRR", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CWC22 family."}
{"protein": "MTDLPASVRWQLWIVAFGFFMQSLDTTIVNTALPSMAKSLGESPLHMHMIIVSYVLTVAVMLPASGWLADRVGVRNIFFTAIVLFTAGSLFCAQASTLDQLVMARVLQGVGGAMMVPVGRLTVMKIVPRDQYMAAMTFVTLPGQVGPLLGPALGGVLVEYASWHWIFLINIPVGIVGAIATLCLMPNYTMQTRRFDLSGFLLLAAGMATLTLALDGQKGLGISPAWLAGLVAVGLCALLLYLWHARGNARALFSLNLFRNRTFSLGLGGSFAGRIGSGMLPFMTPVFLQIGLGFSPFHAGLMMIPMVLGSMGMKRIVVQVVNRFGYRRVLVASTLGLAAVSLLFMFSALAGWYYVLPLVLFLQGMINASRFSSMNTLTLKDLPDDLASSGNSLLSMVMQLSMSIGVTIAGLLLGLYGQQHMSLDAASTHQVFLYTYLSMAAIIALPALIFSRVPDDVGSNTVLRRRNRSGS", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
{"protein": "MRTVLVALLALVALTQAISPLDLIKEEWHTYKLQHRKNYANEVEERFRMKIFNENRHKIAKHNQLFAQGKVSYKLGLNKYADMLHHEFKETMNGYNHTLRQLMRERTGLVGATYIPPAHVTVPKSVDWREHGAVTGVKDQGHCGSCWAFSSTGALEGQHFRKAGVLVSLSEQNLVDCSTKYGNNGCNGGLMDNAFRYIKDNGGIDTEKSYPYEGIDDSCHFNKATIGATDTGFVDIPEGDEEKMKKAVATMGPVSVAIDASHESFQLYSEGVYNEPECDEQNLDHGVLVVGYGTDESGMDYWLVKNSWGTTWGEQGYIKMARNQNNQCGIATASSYPTV", "text": "FUNCTION: Important for the overall degradation of proteins in lysosomes. Required for differentiation of imaginal disks. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MKTQTTHAAEQHAAKRRWLNAHEEGYHKAMGNRQVQMIAIGGAIGTGLFLGAGARLQMAGPALALVYLICGIFSFFILRALGELVLHRPSSGSFVSYAREFLGEKAAYVAGWMYFINWAMTGIVDITAVALYMHYWGAFGDVPQWVFALGALTIVGTMNMIGVKWFAEMEFWFALIKVLAIVIFLVVGTIFLGTGQPLEGNATGFHLITDNGGFFPHGLLPALVLIQGVVFAFASIELVGTAAGECKDPQKMVPKAINSVIWRIGLFYVGSVVLLVLLLPWNAYQAGQSPFVTFFSKLGVPYIGSIMNIVVLTAALSSLNSGLYCTGRILRSMSMGGSAPKFMAKMSRQHVPYAGILATLVVYVVGVFLNYLVPSRVFEIVLNFASLGIIASWAFIMVCQMRLRQAIKEGKAADVSFKLPGAPFTSWLTLLFLLSVLVLMAFDYPNGTYTIASLPLIAILLVAGWFGVRRRVAEIHRTAPVTADSTESVVLKEEAAT", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family."}
{"protein": "MANKQDLIAKVAAATELTKKDSAAAVDAVFAAVTEYLSKGEKVQLIGFGNFEVRERAARKGRNPQTGKETKIAASKVPAFKAGKALKDAVK", "text": "FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Seems also to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs and acting as a nidus for in situ immune complex formation. SIMILARITY: Belongs to the bacterial histone-like protein family."}
{"protein": "MSSHKGSVVAQGNGAPASNREADTVELAELGPLLEEKGKRVIANPPKAEEEQTCPVPQEEEEEVRVLTLPLQAHHAMEKMEEFVYKVWEGRWRVIPYDVLPDWLKDNDYLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGFVLFLFLGILTMLRPNMYFMAPLQEKVVFGMFFLGAVLCLSFSWLFHTVYCHSEKVSRTFSKLDYSGIALLIMGSFVPWLYYSFYCSPQPRLIYLSIVCVLGISAIIVAQWDRFATPKHRQTRAGVFLGLGLSGVVPTMHFTIAEGFVKATTVGQMGWFFLMAVMYITGAGLYAARIPERFFPGKFDIWFQSHQIFHVLVVAAAFVHFYGVSNLQEFRYGLEGGCTDDTLL", "text": "FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:25855295, PubMed:12802337). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localized to the cell membrane and intracellular organelles. SIMILARITY: Belongs to the ADIPOR family."}
{"protein": "MATAATIPSVATATAAALGEVEDEGLLASLFRDRFPEAQWRERPDVGRYLRELSGSGLERLRREPERLAEERAQLLQQTRDLAFANYKTFIRGAECTERIHRLFGDVEASLGRLLDRLPSFQQSCRNFVKEAEEISSNRRMNSLTLNRHTEILEILEIPQLMDTCVRNSYYEEALELAAYVRRLERKYSSIPVIQGIVNEVRQSMQLMLSQLIQQLRTNIQLPACLRVIGYLRRMDVFTEAELRVKFLQARDAWLRSILTAIPNDDPYFHITKTIEASRVHLFDIITQYRAIFSDEDPLLPPAMGEHTVNESAIFHGWVLQKVSQFLQVLETDLYRGIGGHLDSLLGQCMYFGLSFSRVGADFRGQLAPVFQRVAISTFQKAIQETVEKFQEEMNSYMLISAPAILGTSNMPAAVPATQPGTLQPPMVLLDFPPLACFLNNILVAFNDLRLCCPVALAQDVTGALEDALAKVTKIILAFHRAEEAAFSSGEQELFVQFCTVFLEDLVPYLNRCLQVLFPPAQIAQTLGIPPTQLSKYGNLGHVNIGAIQEPLAFILPKRETLFTLDDQALGPELTAPAPEPPAEEPRLEPAGPACPEGGRAETQAEPPSVGP", "text": "FUNCTION: Required for normal Golgi function. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the COG8 family."}
{"protein": "MTPSISWRLLLLAGLCCLVPSYLAEDVQETDTSQKDQSPASHEMATNLGDFAFSLYRELVHQSNTSNIFFSPVSIATAFALLSLGSKGDTQTQILEGLQFNLTQTSEADIHKVFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQSEVFSVNFAKSEEARKMINDFVEKGTQGKIVDAVKDLDEDTVFALANYIFFQGKWKTPFDPEHTTEADFHVNESTTVRVPMMNLMRMLDVHYCSTLSSWVLMMDYLGNATAVFLLPDDGKMQHLEQTLNKELISKFLLNRHRSLAEIHFPRLSISGSYNLKALMAPLGITRVFNNGADLSGITEENAPLRLSKAVHKAVLTIDERGTEAAATTIVEAVFMSLPPILHFNHPFVFTIVETHTQTPLFVGKVVDPTRK", "text": "FUNCTION: Inhibitor of serine proteases. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
{"protein": "MSEELKYELPGLERKAHECESTRPEGPGDATKPDELATTASVYGKLMASAAKLKATFAAGDREGKRIAAAIRAAAGAYQKIEEQKAAELNRQMNGSDAPPPAAEAVVPDMSGIPGPLTIPSMEYPSAAAAADEMDWEAAARIIHSGDTQALSMKYFRDQWRDYQSTLEGHGRHFANPAEGWSGAAAETCAEAQRRLSTWWADMGAECGRLAQEATTFVDAHDKLVANHPTMDDVKAFEEAEWESEWDRQYAWAIKQEKSEDALEAYANGSQIQEIRPGKPPSIGGLPAVNDGDVQATPTSTTGGPGGPGSGSGGGSGGGASGGSGGGTPEMPELPSTDPSMSPMSTNSAGEEQSSGSPSSGGSSSGGSPSGGSPSGGGAPSSGGMPEGGLPTDMPGGPDIPGLDDPSLKPASAGGGGGGGVGGGGGGGMPAAPLGPAVGADSVSPSPSSTRGGGVGVPTGTGGGAGGMMGGGMGGMGAGHGQGQGKEKKRDPKLAPDEDLYTEDRAHSEGVIGHRPRREKDSGKQQ", "text": "FUNCTION: Involved in DNA conjugation, at least in the recipient strain (PubMed:18554329). SUBCELLULAR LOCATION: Secreted Note=Secreted via the ESX-1 / type VII secretion system (T7SS) (By similarity). SIMILARITY: Belongs to the EspB family."}
{"protein": "MQVNNLGFIASILFVLVPTVFLLILFIQTGKQSES", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface (By similarity). Involved in assembly of monomeric PSII from the CP43-less intermediate. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbM family."}
{"protein": "MGSKEDAGKGCPAAGGVSSFTIQSILGGGPSEAPREPVGWPARKRSLSVSSEEEEPDDGWKAPACFCPDQHGPKEQGPKHHPPIPFPCLGTPKGSGGSGPGGLERTPFLSPSHSDFKEEKERLLPAGSPSPGSERPRDGGAERQAGAAKKKTRTVFSRSQVYQLESTFDMKRYLSSSERACLASSLQLTETQVKTWFQNRRNKWKRQLSAELEAANMAHASAQTLVSMPLVFRDSSLLRVPVPRSLAFPAPLYYPGSNLSALPLYNLYNKLDY", "text": "FUNCTION: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMX homeobox family."}
{"protein": "MVKFFQPKISPLPDGIDLKGSTAVVTGASAGMGLELTRQLLQLNISTVILAVRNVAKGENVVKQLRGDPHIRTYNGNATLKVMELDMDKYDSVQRFAKHLRDEIPIVNFLILNAGIGLLKHDRSPSGHDRTLQVNYYSNALLIAELLPYLKASAERTTIPTRITWVGSRAFETTSLQKTPLQPNERVLEHMDKKEFFAPFQRYGDSKLLCLLFMCSLARQIDPKKVIINMLCPGMVNTNMSDVLPVYLRAVINVVKAIRARPVEVGVWIILNAALVAGPDSHGKFLIDKDIASESQYISSPAGQEVQKKIWEETIEELSRLTTLPPEVN", "text": "FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides (PubMed:22508998, PubMed:24863423). The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA (PubMed:22508998). 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione (PubMed:22508998, PubMed:24863423). The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde (PubMed:22508998, PubMed:24863423). Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE (PubMed:24863423). The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids (PubMed:24863423). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MTKIETLVERARRLKEKGLTTEEIADELNVSRETALWLITRVGETPPSDIYVEWRELTKPSRLRLVAMAMADMIVSEVKEDIEVVVGIATSGIPLAAMVAEELGCEFTIYYPRKFKTDEEKPKGGILSENFARVSGKKCAIVDDITSTGRSIKEAIEVIEANDGKAVCAAVIVNKRGGNEIEGIPLLSMLKILRI", "text": "SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family."}
{"protein": "MSRKYRKKLSRDDIRAVGFDFIEFLDDRETRSTTDRNTLKEIYNEQFRDRDGVRDPNFSSVLFALTRSSRTRVTRSEVFFDKKIRVRQNDQWSRPYRSQQNHATPHLNDAISRPSTTRVSDPSSVPEPENRVIARRRLAKTIMRQGNSEDMSVFFADKYGVRVSSELQIEDGKIHWCVEGAEVHELKLFVENTGQEAILFTCFSALHYLQYFTLDDSQRVRKDNPHRLEPNETYEVILRFKSDQIGVYPATLAFEFKENQDTRPFHIVRFIEAQHRSELTAQLGPTEPFRPKRLDTNQPMKWSIDEGFKPESSSQNFLKFVVPLDNYNCPSYTSALIEVLKGNRSSGKQLQEHQLTLESDLSFNNYMDRFDLLLYLEEDQMRMDIKRYNKKDVSMVRDRDKKLLVLELPGVSENRPSVLRGDHLLLTKSEELQNSNVTKYKGYVHRVELDQVKLGFSKRLLERFIDNMKFSVEFTINRLPLRLQHRAVHMVVQHHLKDVLFPVASRRLNPVSPSALRLFDQKLEKNPEQKTAVCNIVAGTSKPAPYLVFGPPGTGKTVTIVEAIKQVEKNTGGARILACAPSNSAADQLGEKLITSQHVDARNIYRIYASSRNPKEIPKVLENNSNVEGENIIFPCKEDLMPYKIVVCTLVTAGRLVSGGFPVGHFSHIFVDEAGHAVEPEIVISVAGLLNAETGQLVLAGDPKQLGPILRSPFAIKYGLGLSLLERLMTQNELYQKGDTGFDNRYVTKLLQNYRSHPSILKVPNELFYDNELKACADEISSRQYCTWEHLPKRGFPVIFHGVVGKDERESTSPSFFNTSEIDKIMDYLKKLLLTQAKKGIAKISPKDIGIIAPYRKQVEKIRQAIKIHRELKSLSGIEELKVGSVEEFQGQERKVIIVSTVRSSKEHIILDDKFNIGFLKNEKRFNVAVTRAKALLIMVGNPIILRTDEIWGRFMNYCIQERGYTGYDITHLEETDVIAERLLSLNIRQEITVETEESVVQQFLSPPWRHEH", "text": "FUNCTION: Probable RNA helicase. Required for RNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily."}
{"protein": "MKVAEEYDKGVPMMLAPQMGAIDATVESIRYRAQLIARNQKLDSGVAATGMIGFAAGFLFSLLMVIVLPLLFW", "text": "FUNCTION: Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MtrF family."}
{"protein": "MRAWIFFLLCLAGKALAAPQEALPDETEVIEDVTTEEPVGANPVQVEVGEFEEPTEDVEEIVAENPCQNHHCKHGKVCEVDDNNSPMCVCQDPSSCPATSGVFEKVCGTDNKTYDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKFIPPCLDTELTEFPLRMRDWLKNVLITLYERDEDNNLLTEKQKLKVKKIHENEKRLEAGDHTVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFEACDLDNDKYIALEEWASCFGIKEKDIDKDLVI", "text": "FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane Note=In or around the basement membrane. SIMILARITY: Belongs to the SPARC family."}
{"protein": "MGPRAKTISSLFFLLWVLAEPAENSDFYLPGDYLLGGLFSLHANMKGIVHLNFLQVPMCKEYEVKVIGYNLMQAMRFAVEEINNDSSLLPGVLLGYEIVDVCYISNNVQPVLYFLAHEDNLLPIQEDYSNYISRVVAVIGPDNSESVMTVANFLSLFLLPQITYSAISDELRDKVRFPALLRTTPSADHHIEAMVQLMLHFRWNWIIVLVSSDTYGRDNGQLLGERVARRDICIAFQETLPTLQPNQNMTSEERQRLVTIVDKLQQSTARVVVVFSPDLTLYHFFNEVLRQNFTGAVWIASESWAIDPVLHNLTELRHLGTFLGITIQSVPIPGFSEFREWGPQAGPPPLSRTSQSYTCNQECDNCLNATLSFNTILRLSGERVVYSVYSAVYAVAHALHSLLGCDKSTCTKRVVYPWQLLEEIWKVNFTLLDHQIFFDPQGDVALHLEIVQWQWDRSQNPFQSVASYYPLQRQLKNIQDISWHTINNTIPMSMCSKRCQSGQKKKPVGIHVCCFECIDCLPGTFLNHTEDEYECQACPNNEWSYQSETSCFKRQLVFLEWHEAPTIAVALLAALGFLSTLAILVIFWRHFQTPIVRSAGGPMCFLMLTLLLVAYMVVPVYVGPPKVSTCLCRQALFPLCFTICISCIAVRSFQIVCAFKMASRFPRAYSYWVRYQGPYVSMAFITVLKMVIVVIGMLATGLSPTTRTDPDDPKITIVSCNPNYRNSLLFNTSLDLLLSVVGFSFAYMGKELPTNYNEAKFITLSMTFYFTSSVSLCTFMSAYSGVLVTIVDLLVTVLNLLAISLGYFGPKCYMILFYPERNTPAYFNSMIQGYTMRRD", "text": "FUNCTION: Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family. TAS1R subfamily."}
{"protein": "MKFGIEFVPSDPALKIAYYAKLSEQQGFDHVWITDHYNNRDVYSTLTVLALNTNSIKIGPGVTNSYTRNPAITASSIASIAEISGGRAVLGLGPGDKATFDAMGIAWKKPLATTKEAIQAIRDFISGKKVSMDGEMIKFAGAKLAFKAGNIPIYMGAQGPKMLELAGEIADGVLINASHPKDFEVAVEQIKKGAEKAGRDPSEVDVTAYACFSIDKDPVKAVNAAKVVVAFIVAGSPDLVLERHGIPVEAKSQIGAAIAKGDFGALMGGLVTPQMIEAFSICGTPDDCMKRIKDLEAIGVTQIVAGSPIGPAKEKAIKLIGKEIIAKM", "text": "FUNCTION: Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the mer family."}
{"protein": "MESTLGSDLARLVRVWRALIDHRLKPLELTQTHWVTLYNINRLPPEQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHTCANDRRAKRIKLTEQSSPIIEQVDGVICSTRKEILGGISSDEIAVLSGLIDKLEKNIIQLQTK", "text": "FUNCTION: Transcription regulator that can specifically activate or repress expression of target genes. Required for expression of the virulence gene inv. FUNCTION: Transcription regulator that can specifically activate or repress expression of target genes. SIMILARITY: Belongs to the SlyA family."}
{"protein": "MALLVWQDDLNIGIDVIDQQHRRIIEMLNHLHVAQASMQRAAVGEVIDEVVDYTMSHFAFEEELMEEAGYPFCAAHKRVHEVFIKRVSEYRMRFQAGEDISDELRTMLSRWLFNHIRGDDQAYAEQVKAHLNQFAREHQGGGWLGRTLKRFFG", "text": "FUNCTION: Oxygen-binding protein. May be involved in a storage mechanism or for delivery to oxygen-requiring enzymes. The oxygen- binding site contains two iron atoms. SIMILARITY: Belongs to the hemerythrin family."}
{"protein": "MAKQARAVQTWRSIVDAAASVFDDYGYERAAISEILRRAKVTKGALYFHFASKEAIAQAIMDEQTSTVEFEQEGSPLQSLVDGGQQFAFALRHNSMARAGTRLSIEGVFLGGPHPWGDWIDATARMLELGQERGEVFPQIDPMVSAKIIVASFTGIQLVSEADSGRADLRGQVAEMWRHILPSIAHPGVIAHIKPEGRVDLAAQAREKAEREEQEARIAAEAKGAGSDAATDSGSRSGGSGLRGGGSGRGPRAGGAGDEGDEEPAGAGVAAGGVVA", "text": "FUNCTION: Represses adpA expression by binding to the promoter region in the absence of A-factor, causing repression of streptomycin production and of sporulation. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MQFSNLDTLRTRGTRKWTQFDDDVIPMFVAESDFPTAPAIKEAIIDACEREMFGYTPAPHAHHLGEAVADFYDWRYGWRPDAAKIFPVADVVRGVLLAIQYFTDGDVIVPVPAYFPFLPIAEAAGRNRIDISSDKGLEGGLDMAEVEEAFKNGAGSIIVTNPFNPGGWMFTSEELDQICDIARRYKGRVLVDEIHAPLTYGKRHVCAAANNPDVCITVTATSKAWNVAGLKCAQMIFTNDEDVKTWNAINPVAKDGVGTLGIIAAEAAYESGREHLDWQVEQLKANRDWLVENLPSLIPGIRFEIPDATYLMFLDFKDTKLGVDKPAAYLLKHARVALSEGVDFGPGGEHRARMNFATSPEILKEATERIARAIEVV", "text": "FUNCTION: Catalyzes the cleavage of the cysteine-S bond in various cysteine-S-conjugates (PubMed:17191898, PubMed:18515361). Cleaves L- cystathionine, as well as S-substituted cysteine conjugates S-benzyl-L- cysteine and S-ethyl-L-cysteine (PubMed:17191898). Releases four human body odoriferous sulfanylalkanols: 3-methyl-3-sulfanylhexan-1-ol (3M3SH), 3-sulfanylhexan-1-ol, 2-methyl-3-sulfanylbutan-1-ol and 3- sulfanylpentan-1-ol; the release is obtained after the sequential hydrolysis of the Cys-Gly bond of the odorless Cys-Gly-S-conjugate precursors by the dipeptidase TpdA, then the cleavage of the resulting Cys-S-conjugates by MetC (PubMed:17191898, PubMed:18515361). SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily."}
{"protein": "MEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSPKHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADITVSEEPIPQSPDMDVLLESLKCLCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQQLFQELHGVRLLTDALELTLGVAPKENPPVMLPAQETERAMEILKVLFNITFDSVKREVDEEDAALYRYLGTLLRHCVMVEAAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLEFMGVNMDVISALLAFLEKRLHQTHRLKECVAPVLNVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSRHRVIQPMGMSPRGHLTSLQDAMCETMEGQLSSDPDSDPD", "text": "FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)- alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Colocalizes with GNAI1 and RGS14 at the plasma membrane (By similarity). Colocalizes with RIC8A in CA2 hippocampal neurons. SIMILARITY: Belongs to the synembryn family."}
{"protein": "MLSQLAMLQGSLLLVVATMSVAQQTRQEADRGCETLVVQHGHCSYTFLLPKSEPCPPGPEVSRDSNTLQRESLANPLHLGKLPTQQVKQLEQALQNNTQWLKKLERAIKTILRSKLEQVQQQMAQNQTAPMLELGTSLLNQTTAQIRKLTDMEAQLLNQTSRMDAQMPETFLSTNKLENQLLLQRQKLQQLQGQNSALEKRLQALETKQQEELASILSKKAKLLNTLSRQSAALTNIERGLRGVRHNSSLLQDQQHSLRQLLVLLRHLVQERANASAPAFIMAGEQVFQDCAEIQRSGASASGVYTIQVSNATKPRKVFCDLQSSGGRWTLIQRRENGTVNFQRNWKDYKQGFGDPAGEHWLGNEVVHQLTRRAAYSLRVELQDWEGHEAYAQYEHFHLGSENQLYRLSVVGYSGSAGRQSSLVLQNTSFSTLDSDNDHCLCKCAQVMSGGWWFDACGLSNLNGVYYHAPDNKYKMDGIRWHYFKGPSYSLRASRMMIRPLDI", "text": "FUNCTION: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKFTTAAVLSALVSAEIAFAAPGGNGFARRQARRQARAAGLKASPFRQVNAKEATVESNWGGAILIGSDFDTVSATANVPSASGGSSAAGTAWVGIDGDTCQTAILQTGFDWYGDGTYDAWYEWYPEVSDDFSGITISEGDSIQMSVTATSDTSGSATLENLTTGQKVSKSFSNESSGSLCRTNAEFIIEDFEECNSNGSDCEFVPFASFSPAVEFTDCSVTSDGESVSLDDAQITQVIINNQDVTDCSVSGTTVSCSYV", "text": "SIMILARITY: Belongs to the peptidase G1 family."}
{"protein": "MLGQSSLVGYSNTQAANRVFVYEVSGLRQTDANENSAHDIRRSGSVFIKVPYARMNDEMRRISRLGGTIVNIRPYQADSNEQN", "text": "FUNCTION: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=This protein occurs in the rod, it is associated with phycocyanin. SIMILARITY: Belongs to the phycobilisome linker protein family."}
{"protein": "MPVAVGPYGQSQPSCFDRVKMGFVMGCAVGMAAGALFGPFSCLRIGMRGRELMGGIGKTMMQSGGTFGPFMAIGMGIRC", "text": "FUNCTION: Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage (By similarity). FUNCTION: Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MGR2 family."}
{"protein": "MQGDPEVLRLLNEQLTTQLTAINQYFLHSKMQDNWGFTELAEHTRAESFDEMRHAEAITDRILLLDGLPNYQRLFSLRIGQTLREQFEADLAIEYEVMDRLKPAIILCREKQDSTTATLFEQIVADEEKHIDYLETQLELMDKLGVELYSAQCVSRPPS", "text": "FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. SIMILARITY: Belongs to the bacterioferritin family."}
{"protein": "MGSLLFSWKGTQQKDVTIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSVHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRVNVQPELVS", "text": "FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. SIMILARITY: Belongs to the protein prenyltransferase subunit beta family."}
{"protein": "MNYRGIYRRRYVFVLLLLVAVVNISYGWTVLKNKDYKRRYLSPSGVEKVRKHLSRKYVASRNNTQTFKKHYFSNTWAVHIDPPDNDVADRIAKKHGFTNIGKIGNIEGHYHFKHEEIGERELEKARHKTALLNLEDEVKFAEQQKILERVKRDGIPNDPYFKDMWYLLNTGQASGPAGVDMNVVPVWKKNITGRGIVISVLDDGLDWTHPDLEANYDQTASIVLNDNDNDPMPRDSDADNCHGTRCAGEAAAIANNGICGTGVAYNAKIGGVRMLDGQATDALEASALGFRGDHIDIYINCWGPKDDGKTFGKPGPMAAKALRLGAEQGRNRLGSIFVWATGNGGLTDDDCNCDGYTTSIFTISIGCIGDHGLSAYYTEKCSSTLAVTFNGASHKEGRENKMVTTDLYHQCTEEFKGTSASAPLAAGIIALTLEANPLLTWRDVQALIVHTAQITSPVDEGWKRNGAGFHFNHKFGFGRLDANAMVNAAQSWKNLPAQRKCTAASGFDHQDIPRGDSLFINIPTVACESSSAQIAKVEHVVLTVSFVHRRRGDVSIDLISPKDTKSQMLSPRKYDDSDEGLDEWSFMTVYNWGENPKGIWRLKITDNPNQDDVMNLFNGDNTDDVESLEERVIDTQTKQNKAEWEKMRKENPYFDVPYPTGVRKDKVLGSTEINDNSFDTPHTETFKIIRNHIPEVNLQNNDNMNTLNFDPVTGRKKNSINKKIINSRKRNFLTFRNFLKKSKKVQVQQEETGTQRVQVNAGYENPRISCESGYTTCSGVLINYKLTFYGTGE", "text": "FUNCTION: Probably involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily."}
{"protein": "MKCANAAALLFFVLCDIGVHGGEIVAELLHSNVTVKWQTDYERQTVDFSIWFGAKTPDLLFLGFSDFGDMNSSDVLMYDNVKREIMDSYTNRDYKIIPDLSQDFQQLRRRKDHFVVRRKLTTCDSRDYAFQRGTTQFYIAASFGYRNLVDIRDKKWILDKKFGKVIEGPTDQPSTDEGVSSLERDVQLVIVNSNSPDPVPNVETTYECIIRKMPFDTVHKTYHIVRMEPYITPGNEHLVHHMEVFLCRDEVEEWSGNCNDPKKPKKSKSCSHVIAAWAMGEGPIHYPREAGLPIGGKGKNEYVMVEIHYNNPELHKGVMDTSGFQFYVTGLLRIYDAGIMELGLIYSDANSVPPNQKAWAMNGYCPSQCTQNLPEEGINIFASQMHAHLTGRKLWTSQYRDGVQIGDVNRDEHYSPHWQHLQQLRPMVRVMPGDTLVTTCVYDTRRRSNVTFGGYGITDEMCVNYIYYYPASEVEVCKSAISNSTLRAYFSQRHGMDGKTMKISDMYNGVKDWSNGVDEEFYNVLNVGNVNMNCLKSNGESFEFKSKDPRQGWENMARPRLFSGSFIRTRDRFQCPAINDMINFE", "text": "FUNCTION: Converts tyramine into octopamine, a neurotransmitter involved in pharyngeal pumping and egg laying. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the copper type II ascorbate-dependent monooxygenase family."}
{"protein": "MAVACSPEKDQSLLQLQKVDSSRVILSPVLSSPMETNQPICIPSPYTDRGHDFPTIPFYSATNFSYANPPAISDRPSVHQTLSPSLFWPSHGHVGTTLPLHHLQARPQHGQAVQSPWVELSPLDNVLTSSKSARRRSQENEEGEVSSGGKADLHFCAVCHDYASGYHYGVWSCEGCKAFFKRSIQRHNDYICPATNQCTIDKNRRKSCQACRLHKCYNVGMTKCGMRKERGNFRDPQMRRVTRLSSQGRTSGPSVLNGPAVGPLNTPQPPALTSKQLIERIMEAEPPEIYLMKDMRRPLTEANIMMSLTNLADKELVHMITWAKKIPGFLELGLLDQVHLLECCWLEVLMIGLMWRSVDHPGKLIFSPDLSLSREEGSCVQGFLEIFDMLIAATSRVRELKLQREEYVCLKAMILLNSNMCLSSSEGSEELQSRSKLLRLLDAVTDALVWAIAKTGLTFRQQYTRLAHLLMLLSHIRHVSNKGMDHLHGMKMKNMVPLYDLLLEMLDAHIMHSSRLPRRSPQQETVEQCDAPARPHSPGTSGPTNTWTPSCTGGRGEPQ", "text": "FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily."}
{"protein": "MVSHKCVEEFGYASYLVPSNARAPRSARKRRSIEKRISKEDDNMCAIDLLATVAGHLSFESGSSLMSIDKLIEDHRVKEEFPEEEKPLMPVALSPYRGSLSPCGFSSVINGKVENEVDGFSYSGGSDACQVGNFSQDVKPDIDGDAVVLDARPNVVVSLGSSSRTEVPSIGNCVSHGVRDDVNLFSRDDDENFSKYIHPRVTKHSPRTVPRIGDRRIRKILASRHWKGGSRHSDTKPWRNYYLHQQRSYPIKKRKNFDHISDSVTDDYRMRTKMHRGSRKGQGASFVASDSHVKLRIKSFRVPELFIEIPETATVGSLKRMVMEAVSTLLSDGHRVGLMVQGKKVRDDNKTLHQTGISQDNSHLDSLDFSLEPSSEMPQLLTSHPLGHACEELLPVCQATKIDNVLESDHHDSALFPSDSLGNNNVTEDSKAMISVALNELSSQSQPPSRKSRRSEQQQQQAAQRRIRRPFSVAEVEALVQAVEKLGTGRWRDVKLCAFEDADHRTYVDLKDKWKTLVHTAKISPQQRRGEPVPQELLNRVLNAHGYWTQQQMQQLQQNVNKLEQETQSQTTEGLLLL", "text": "FUNCTION: Binds specifically to the plant telomeric double-stranded DNA sequences 5'-GGTTTAG-3'. At least 4 repeats of telomeric sequences are required for binding. Induces DNA bending. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MEIYLVTGNMNKKEEFLKMMDEELNVEFVNINLEEIQAQDIVEINEHKVKTAYNILKKQDNNKNKKRYVITDDTGLFISKLNNFPGPYIKWMQKALGSKGIADVVSRLDDNTCHAICTYSVYDGKDVHSFKGITNGKIVEPRGNNKFGWDNIFQPESLSKTFGEMTFDEKQNLSPRFKAFVQLKEFLMNEHKKYNNEF", "text": "FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HAM1 NTPase family."}
{"protein": "MAVSVTKEEMDYTIKPEAGASNISTEDWPLLLKNYDKLMVRTGHFTPIPAGCSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWMKRILRAEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCVIRLHDKIPGGEAQFKRALETLTGALFQRPPLISAVKRQLRIRTIHESKLYEFDNDRHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGAMDENNGLVTLHDVLDAQWMYDNQRDESYLRRVIQPLESLLTTYKRIVVKDSAVNAVCYGAKLMIPGLLRFEAGIEVNEEVVLMTTKGEAIAIGIAQMSTVELSTCDHGVVAKVKRCIMERDLYPRRWGLGPVALEKKKLKSAGKLDKYGRANEDTPAKWKTEYKDYSAPEEASAHAASESTAKEDVAAALTTEQDEAPSSPQSKMDVDETKEEKKRKRHEGETAEERAERKRKKKEKKEKKERRKSKQEKEDSDDSD", "text": "FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the pseudouridine synthase TruB family."}
{"protein": "MSATTLPNVSVAIIGAGIGGLTLGAFLRRLGIPFVILERTAVLTPLGAGISLAPNCLAALEQLGLYETIRQNAQELRGINVYREKRCWGTIDFGLAKQWFGYNVLSIERYEFHRYLYEAAGGAGVVQLGWDVARIEGLENADGDLRVISADGREVHTDIVVGADGIRSVTRRILSRSMGLQPENTIRFTGRVHMSGYTKPLSHLSTTDLGIGHWMLYNDCILTTWPCKENRQWFIGVKAAPPDEKSPDRSVWKGATSDTVNAVYGSRFHPFGEDGTVEASMYAIPAPAIAGNSRDDKLSIIPNASSLATSSRKPTSRTWFGAEWRSWVMVYRT", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA (PubMed:32077283). The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA (PubMed:32077283). A tetramic acid is formed and released from the PKS- NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively (PubMed:32077283). The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo- methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
{"protein": "MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP", "text": "FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class- switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'- TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'- TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity). FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class- switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'- TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'- TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MASKIGSRRWMLQLIMQLGSVLLTRCPFWGCFSQLMLYAERAEARRKPDIPVPYLYFDMGAAVLCASFMSFGVKRRWFALGAALQLAISTYTAYIGGYVHYGDWLKVRMYSRTVAIIGGFLVLASGAGELYRRKPRSRSLQSTGQVFLGIYLICVAYSLQHSKEDRLAYLNHLPGGELMVQLFFVLYGVLALAFLSGYYVTLAAQILAVLLPPVMLLIDGNVSYWHNTRRVEFWNQMKLLGESVGIFGAAVILATDG", "text": "FUNCTION: May activate NF-kappa-B signaling pathways. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein."}
{"protein": "MLLCSLTLTLILLAVSGTKCDVKEFCAACSGVPGIPGSPGLPGRDGRDGVKGDPGPPGPIGPPGGMPGSPGHDGLIGPPGPPGERGDKGEPGERGPPGPPAYPDEELQTTLHDIRHQILQLMGALSLQGSMLAVGEKVFSTNGQVVDFDAIRESCARAGGRIAVPKSLEENAAIASLVTKHNTYAYLGLEEGPTAGDFYYLDGAPVNYTNWYPGEPRGRGKEKCVEMYTDGQWNDRSCLQYRLAICEF", "text": "FUNCTION: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air- liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages. SUBCELLULAR LOCATION: Secreted Secreted, extracellular space, extracellular matrix Secreted, extracellular space, surface film. SIMILARITY: Belongs to the SFTPA family."}
{"protein": "MRTVLNILNFVLGGFATTLGWLLATLVSIVLIFTLPLTRSCWEITKLSLVPYGNEAIHVDELNPAGKNVLLNTGGTVLNIFWLIFFGWWLCLMHIATGIAQCISIIGIPVGIANFKIAAIALWPVGRRVVSVETAQAAREANARRRFE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MEGKEEDVRLGANKFSERQPIGTAAQGAADDKDYKEPPPAPLFEPGELKSWSFYRAGIAEFVATFLFLYITILTVMGVSKSTSKCATVGIQGIAWSFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRALFYIIMQCLGAVCGAGVVKGFQQGLYMGNGGGANVVAPGYTKGDGLGAEIVGTFILVYTVFSATDAKRNARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNRDHAWNDHWIFWVGPFIGAALAAIYHQVIIRAIPFKSRS", "text": "FUNCTION: Water channel required to facilitate the transport of water across cell membrane. Active as heteromers with PIP1-1, PIP2-1, PIP2-4 or PIP2-5, but not as homomers. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC 1.A.8.11) subfamily."}
{"protein": "MSDSLGDEYAPAFAPFLGFAGCAAAMILSCAGAAIGTAKSGIGISGIGTFKPELIMKSLIPVVMSGILSVYGLVVSVLIAGGLSPTENYSLFNGFMHLACGLSVGFACLASGYSIGIVGDEGVRQFMHQPRLFVGIVLILIFAEVLGLYGMIIALILNTKGSG", "text": "FUNCTION: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family."}
{"protein": "AHIDCDKECNRRCSKASAHDRCLKYCGICCEKCNCVPPGTYGNEDSCPCYANLKNSKGGHKCP", "text": "SIMILARITY: Belongs to the GASA family."}
{"protein": "MASSSTWGLLLLAGLCCLVPISLAEGLQGHAVQETDVPRHDHEQHQEAACHRIAPNLADFAFSLYRQVARQSNTSNIFLSPVTIARAFAMLSLGTKGATHAEILEGLQFNLTEKAEAEIHEGFQHLLHTLNQPDNQLQLTTGNGLFIDEKAKLVPKFLEDVKNLYHSEAFSINFRDTEEAKKCINDYVEKGSQGKIVDLVDELDKDTVFALVNYIFFKGKWEKPFEVEQTTEEDFHVDEETTVKVPMMNRLGMFDLHHCDKLSSWVLLMDYVATATAFFILPDQGKLHQLEDMLTKEIRAKFLEKRYPSSANLHLPKLTISGTYDLKSLLGNLGITKVFSDEADLSGVTEEQPLKLSKALHRAVLTIDEKGTEATGATILEAIPMSIPPNVKFNKPFLFLIYDTKTKAVLFMGKVMNPTQK", "text": "FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
{"protein": "MNAALIAALLILGALTLDATAYSSTCERIPCTNNSDCHGPDLCQCRPPRGDDFGYFCSEY", "text": "FUNCTION: Tick salivary platelet aggregation inhibitor that plays an important part in the anti-hemostatic strategy of ticks (Probable). Inhibits platelet aggregation induced by ADP, thrombin and thromboxane A2 (TXA2) (PubMed:25152502). Blocks platelet adhesion to soluble collagen (most probably through the binding to alpha-2/beta-1 integrin (ITGA2/ITGB1)) and binds to purified glycoprotein IIb/IIIa (ITGA2B/ITGB3) in a dose-dependent manner (PubMed:25152502). In vivo, reduces thrombus weight effectively in a rat arteriovenous shunt model and inhibits thrombosis in a carrageenan-induced mouse tail thrombosis model (PubMed:25152502). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ixodegrin family."}
{"protein": "MELVQVLKRGLQQITGHGGLRGYLRVFFRTNDAKVGTLVGEDKYGNKYYEDNKQFFGRHRWVVYTTEMNGKNTFWDVDGSMVPPEWHRWLHSMTDDPPTTKPLTARKFIWTNHKFNVTGTPEQYVPYSTTRKKIQEWIPPSTPYK", "text": "FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFA12 subunit family."}
{"protein": "MEDPLSIAVRFALYTDLMMLFGLALFGLYSLRGAERRSGAVLPFRPLLSATALIGLLLSVVSIVLMAKAMSGASEWLEAVPHAEMMVTQTELGTAWLIRMAALVGAAVTIAFNLRVPMASLLMVSLLGGVALATLAWTGHGAMDEGSRRFWHFSADILHLWSSGGWFGALVAFALMLRPNKVETLQSVQVLSRTLSGFERAGAVIVAFIVLSGVVNYLFIVGPQVSGVVESTYGVLLLGKLALFGLMVGLASANRFVLSPAFERAVHRGEYARAARSIRYSMALELGAAVLVLGLIAWLGTLSPEMEAGM", "text": "FUNCTION: Exact function not known. Involved in copper resistance. Appears to be involved in copper uptake in conjunction with CopC. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CopD family."}
{"protein": "MTKEMQTLALVPQGSLEAYIRAANAYPMLTAEEERELAERLHYQGDLDAAKQLILSHLRFVAHIARNYSGYGLPQADLIQEGNIGLMKAVRRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNQDEVELVARELGVTSKDVREMESRMAAQDMTFDPTPDDEARDGQSMAPVLYLQDKSSDFAEGIEEDNWESNAADKLAYALEGLDERSQHIIRARWLDDDNKSTLQELADQYGVSAERVRQLEKNAMKKLKMAIEA", "text": "FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. RpoH subfamily."}
{"protein": "MPDPRPLTPDQTHGRGHAEAAVDWEASRLYRLAQSERRAWTVAWAALAVTALSLIAIATMLPLKTTIPYLIEVEKSSGAASVVTQFEPRDFTPDTLMNQYWLTRYVAARERYDWHTIQHDYDYVRLLSAPAVRHDYETSYEAPDAPDRKYGAGTTLAVKILSAIDHGKGVGTVRFVRTRRDADGQGAAESSIWVATVAFAYDQPRALTQAQRWLNPLGFAVTSYRVDAEAGQP", "text": "FUNCTION: Component of the type IV secretion system ptl required for secretion of assembled pertussis toxin (PTX) through the outer membrane. Could possess peptidoglycanase activity. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the virB8 family."}
{"protein": "MLENLCTLPLSADLFTQVLHPSEPLLTVGLASGKVETFRLPNDDDEEDESGRRTSTSSGRGMIKSIWSTRRHKGSCRHLAYSHDGSAMYSAGTDSVVKHFSPETGNVISKIGLPPRNSATSTTDCPAILHVLSPQTLLLGTDSGGLYIFDLRENGSLNPKPVRKHVPHADYISSITPLPASAESTSGFPKQWVSTGGTTLAVTDLRHGIVATSEDQEDELLCSTIIPTGLGPKKMRSNAVVAVGTGNGILTLWDRGAWDDQQERINVAGGRTKKDGESLDAIVRVPDELGWGKKVIVGVGDGSLSIVDLKRREVQFVLKHDEVEGVSALTFDYQNRLISGGGRTVKVWAESGDDDLDEEEEEEAEATGFKRPARSDSDSDDDSEDERPQKSSNKKQKKGKGNQARSVAFPGLD", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the WD repeat WDR55 family."}
{"protein": "MKKIEAIIKPFKLDEVKEALQEVGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKVEVVLADENAEAVIEAIRNAAQTGRIGDGKIFVSNVEEVIRIRTGETGLDAI", "text": "FUNCTION: In nitrogen-limiting conditions, when the ratio of Gln to 2- ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. SIMILARITY: Belongs to the P(II) protein family."}
{"protein": "MAACATHSSLMLAYAAASTRSQDLTPTPSLFSFASSRPNHLSFPLLLLGGSRDRRCAAIDRASNHKFIVSAVAAEADLDTEEDLEQTATAVLDPPKPKKGKAALVLKRDRTRSKRFLEIQKLRETKKEYDVNTAISLLKQTANTRFVESVEAHFRLNIDPKYNDQQLRATVSLPKGTGQTVIVAVLAQGEKVDEAKSAGADIVGSDDLIEQIKGGFMEFDKLIASPDMMVKVAGLGKILGPRGLMPNPKAGTVTANIPQAIEEFKKGKVEFRADKTGIVHIPFGKVNFTEEDLLINFLAAVKSVETNKPKGAKGVYWKSAHICSSMGPSIKLNIREMIDFKPPTAN", "text": "FUNCTION: This protein binds directly to 23S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL1 family."}
{"protein": "MTSGVSGSSSQDPTLAAQLAQSSQKAGNAQSGHDTKNVTKQGAQAEVAAGGFEDLIQDASAQSTGKKEATSSTTKSSKGEKSEKSGKSKSSTSVASASETATAQAVQGPKGLRQNNYDSPSLPTPEAQTINGIVLKKGMGTLALLGLVMTLMANAAGESWKASFQSQNQAIRSQVESAPAIGEAIKRQANHQASATEAQAKQSLISGIVNIVGFTVSVGAGIFSAAKGATSALKSASFAKETGASAAGGAASKALTSASSSVQQTMASTAKAATTAASSAGSAATKAAANLTDDMAAAASKMASDGASKASGGLFGEVLNKPNWSEKVSRGMNVVKTQGARVASFAGNALSSSMQMSQLMHGLTAAVEGLSAGQTGIEVAHHQRLAGQAEAQAEVLKQMSSVYGQQAGQAGQLQEQAMQSFNTALQTLQNIADSQTQTTSAIFN", "text": "SIMILARITY: Belongs to the chlamydial CPn_0808/CT_579/TC_0868 family."}
{"protein": "MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFLYSDGQSETILGGLGLRMGSSDCRVKIATKANPWIGNSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSAPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYSATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGTQWAEIYRNHFWKEHHFEGIALVEKALQAAYGASAPSMTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLEPAVVDAFNQAWHLFAHECPNYFI", "text": "FUNCTION: Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity). SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily."}
{"protein": "MGFLKGKKGLIVGVANNKSIAYGIAQSCFNQGATLAFTYLNESLEKRVRPIAQELNSPYVYELDVSKEEHFKSLYNSVKKDLGSLDFIVHSVAFAPKEALEGSLLETSKSAFNTAMEISVYSLIELTNTLKPLLNNGASVLTLSYLGSTKYMAHYNVMGLAKAALESAVRYLAVDLGKHHIRVNALSAGPIRTLASSGIADFRMILKWNEINAPLRKNVSLEEVGNAGMYLLSSLSSGVSGEVHFVDAGYHVMGMGAVEEKDNKATLLWDLHKEQ", "text": "FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily."}
{"protein": "MPRSSATARKSHSNRQDHGGGGSGKKPSKQKSSGHLNATYNGTAGSETGPSSQVDWPSHRSGDQSIAAAAAKSNGPVDSLKADTNGRGYPGGYAKGNADMSYGQTNGGVSPNGGLAGPASRRTDKSVTGTKRTTSNASVNPFQLASTILRSCPMYDTIAILIFLLQLPPMVLTLVQFLFASLTFMPPSGTASGSFTSNFDIFQGPAGTPSLGTMIAMDGFCLLVWGLFMWTWAQNFALDLAHVQVAITLGGGGAGKNGGVNALCVGIVLILHLIRSKGIQDFVVGHLVSAKIISPDLLSHYSYLMPAEFKRTESQSSPSWIRSLLAVHILAQAGTAMARRSMTKNRTPAPSRSGKRVDTEASAGSQTQIDSAFESAASVSSYLGPDGQIITAAHKDGRDRLISAKKRRRQANQVRSRQPFWAALASTKVTVMREYEHSRALSKTARGLATTEDDLQGVSLDDGLVWITYVDSSTIKFAAGDFASSDDHSASGVCEAGRVSSEDAEPFYVCVNGAPWATVVITKEHDPSKASNTIYWRGEISGLAPNCAYTCSFVKCDTDEEICAMSVKTPAANDAEQANSVPAPPQPSYRPSSPTTTLKNSIINAEAKLNEKRARLRKAKNDHKLAISKIKKELDNYTNRLQSGTDENRQKQRSLQLERNIRQTEEATAALDNQIDNLGNVPDDEYQEWVEQKAKYERELELLKSAKAEIAATRTANARELSSLESELNSTTQRRERLQGRRTRVNEQYERIISANAQGLNERERRAAEQFAREQDQSKLEQSFNEQFASISQSVQDYQLRTSQLWQQCTAVEQALQQQLLMEPAPLTPEGELPGTSTFADAPSVPLGTLASNMPSHRSLLGQSFPPLKSSPLQHYASPIGTAPSHPTSPIAAPSYQPFSSSPFGNAASFLDPDFVYRDRSFSNRSARSSLYGSEFPDAITARRVPFGVDPFELGNEKRRGSGSDSTPLNGPSGLRPISSPFQRAASRASGTGSGGSGGSGSGSGSPSSARGKGN", "text": "FUNCTION: component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Involved in resistance to acriflavine, and required for normal growth on a range of sole carbon sources, including fructose, cellobiose, raffinose, and starch, and reduced utilization of amino acids, including GABA and beta-alanine, as sole carbon and nitrogen sources. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acrB family."}
{"protein": "MKLIRVTLFLCALAILLLVTPTSSLQLKHPYSSPSQGLSKKIVTKMATRKLMIISSEYVMTSTSHEGSSEQLRVTSSGKSKDEEKKLSEEEEEKKALAKYLSMDYRTFRRRRPVHNKALPLDP", "text": "FUNCTION: [GLV6p]: Signaling peptide (root growth factor) required during root gravitropism in a PIN2-traffic dependent manner (PubMed:23370719). May be involved in maintaining the postembryonic root stem cell niche (PubMed:20798316). Root growth factor that regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells (By similarity). SUBCELLULAR LOCATION: [GLV6p]: Secreted. SIMILARITY: Belongs to the RGF family."}
{"protein": "MVATPSISSQTKGVVRQVIGPVLDVEFPAGKLPKILNALRIEAKNPAGQDIALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEAIDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNTKDTAPIHRAAPKLTDLETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGGVSVFGGVGERTREGNDLYEEFKESGVINADDLTQSKVALCFGQMNEPPGARMRVGLSALTMAEHFRDVNKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTDVGELQERITSTLEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLARALAAKGIYPAVDPLDSTSTMLQPSVVGDEHYKTARAVQSTLQRYKELQDIIAILGLDELSEEDRLTVDRARKIEKFLSQPFFVAEIFTGMSGKYVKLEDTIAGFNMILSGELDDLPEQAFYLVGNIDEVKAKAEKIKSEK", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family."}
{"protein": "MKIVRYIALFGILSGLAVACTPSTSVIPNDAIRLNQLGYYPNQEKIAVVDSGKVEEFVIWDAVSGEQVFVGKSLYTAKSAWSDKTRTTLDFSAVTTPGKYILKVNGASVTFLIKDSVLSPLADAALKSFYYQRTAMPIEEQYAGQWHRMAGHPDNHVLIHPSAASPDRPAGTIVSSSKGWYDAGDYNKYIVNSGYSIGLMQSIYQLFLDYFSRQKINIPESNNHTPDLLDEMQFNLDWMLTMQDPEDGGVYHKLTTPFFEGFVKPVDCKQQRYVVQKSVTAALDFAAVMAQSSRLFASYEEDYPGFSKRALLAAEKAYAWAEKHPEAYYNQNLLNQKYQPAIATGEYGDTHADDEFFWAASELYFSTGKEIYREEAIKKAPQIYTAPGWGNTFALGIFAWLQPGRELNEADRRFADSLKTELLKYADKVIEGAEQTPFHAPYGNDAKDFFWGCLAEKCMNQGVSLMYAYLQTGKDVYLTNAYRNMDYILGRNATGFCYVTGLGTKSPKHPHHRLSASDDIEDPIPGFLVGGPNPGQQDGAFYPTASPDESYVDTEDSYASNEVAINWNAALVALASSLDALAVYSVK", "text": "FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides. May be superfluous in xyloglucan degradation compared to BoGH5A (AC A7LXT7), the other Xyloglucan- specific endo-beta-1,4-glucanase. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family."}
{"protein": "MADEDYNDVDDLGYEDEPAEPEIEEGVEEDVEMKENDDVNGEPIEAEDKVETEPVQRPRKTSKFMTKYERARILGTRALQISMNAPVMVELEGETDPLEIAMKELRQRKIPFTIRRYLPDGSFEEWGVDELIVEDSWKRQVGGD", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family."}
{"protein": "MEELRCPEAKLAPPEVVIATEAPPPSLVDRYFTRWYKADVKGKPCEDHCILQHSNRICVITLAGSHPVLQSGKAIQRISYQISNNCSRLENKVSGKFKRGAQFLTELAPLCKIYCSDGEEYTISSCVRGRLMEVNENILHQPSLLQEKPSTEGYIAVVLPKFEESKSVTEGLLTQQQYEEVVVKRTNATATTP", "text": "FUNCTION: Actin-binding protein that regulates actin polymerization, filopodia dynamics and increases the branching of proximal dendrites of developing neurons. SUBCELLULAR LOCATION: Nucleus speckle Cell projection, lamellipodium Nucleus Cell projection, growth cone Cell projection, dendrite Note=Localizes to somata and dendrites in cortical neurons. Colocalizes with G- and F-actin in growth cones and proximal dendrites (PubMed:24782708). Colocalizes in the nucleus with PTK2 (PubMed:24782708). SIMILARITY: Belongs to the ABITRAM family."}
{"protein": "MHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYREHRDSDTYRCEDRSPSFGEDYYGSSRCHHRRRSREREPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDTLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR", "text": "FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine- rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre- mRNA in endothelial cells (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasmic vesicle, secretory vesicle, acrosome. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily."}
{"protein": "MELQLAIDLLNKEDAAELANKVKDYVDIVEIGTPIIYNEGLPAVKHMADNISNVKVLADMKIMDAADYEVSQAIKFGADVITILGVAEDASIKTAIEEAHKNNKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLESLRTVKSVIKNSKVAVAGGIKPDTIKEIVAESPDLVIVGGGIANADDPVEAAKQCRAAIEGK", "text": "FUNCTION: Catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate. SIMILARITY: Belongs to the HPS/KGPDC family. HPS subfamily."}
{"protein": "MERNISVEELNQIPTPKKEVEIVERKGIGHPDSVADGIAEAVSRSLSKYYLEHYGRILHHNTDQVEVVGGQSAPKYGGGLVLEPTYILLSGRATTKVGNDRVPYKSITIKAAKDYLRNNFSHLDVDADVMIDSRIGQGSVDLVEVYDTSKLEANDTSFGVGFAPLSETENIVLKTERYLNGSLKKKLPMVGYDIKVMGFRQKDTINLTVAAAFVDKYIKDADEYFNLKDQLKDLVLDNAVEETDKEVKVYINTADIRENSKSVGYLTVTGMSMENGDDGSVGRGNRVNGLITPYRAMSMEAAAGKNPVTHVGKLYNVLANKIANDIVQEEGNDIAEVLVRIVSQIGRPIDDPHVASVQVIYEGNVDHSKHKNNIRNLVNDRLAHVSDLTMQFVEGKITVF", "text": "FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. SIMILARITY: Belongs to the AdoMet synthase 2 family."}
{"protein": "MKIEKLIIKDFRSHALTKVNFSSGINLIIGQNGSGKSSILDALLVGLYWPSKPKDLKKDDFERINGSGTEITVFFEKGNVKYQIHRNIGRGLAFVKYHDGSSWKTLETGQKPVRDWMEKLVPYDVFLNAIYIRQGEIDAILESDESREKVVRQVLGLDRYENSYKNLLDVRKEIDARIKAIEDYLKSTENIDELIGNLEKELTSVLREINEISPKLPELRGELGGLEKELKELEKTAEELAKARVELKSEEGNLRELEAKKSGIQSMIRETEKRVEELKEKVKELESLEEKAKEYERLSRFYRNFTEGINRIEKLLATYSQQAENLRERIDELSKKEARVKELLKEKEGLQKELGALEEDLKAYQRAKELMANLERLKKRLTLSEEEIEKLEAEIQKARERKEEIMKELEEIGSRRGELKSIAGERNKALMELKKAKGRCPVCGRELTEEHRKELLEKYTAELKEISAEMKELEKREKKLRAELVEVEKTLKKERELFALKEVLEQIRETEEKLKEYDLEKLEEANEKAEELKKKLAGLEGEIKSLEDEIKKGELLKKKLALVEKKLRELEEERASLLGELKKLGFGDVKELEERLKELEPAYKRYIELRPARDELKREEDLLKSLKLDLTAILKEIEKTSKRVEELRKRVEELEKSYDKDRHEELKGKTRELSNELAGLEARLKSLEERRDEVKASLEKLREEKETRKEKAKELEKLKKARERVQRLREKVKAYKNLLKEGALAKVGEMASEIFEELTEEKYSGVTVKAEENKVRLGVVYNGKEYGLGFLSGGERIALGLAFRLALSLYLAGEISLLILDEPTPYLDEERRRRLVDIMQRYLRKIPQVIVVSHDEELKDAADRVIRVSLENGVSVVREAEVG", "text": "FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex. SIMILARITY: Belongs to the SMC family. RAD50 subfamily."}
{"protein": "MKLQVLPLSQEAFSAYGDVIETQKRDFFHINNGLVERYHDLALVEILEQDRTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA", "text": "FUNCTION: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the anaerobic utilization of allantoin as sole nitrogen source. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate. SIMILARITY: Belongs to the ureidoglycolate lyase family."}
{"protein": "MAERGRLGLPGAPGALNTPVPMNLFATWEVDGSSPSCVPRLCSLTLKKLVVFKELEKELISVVIAVKMQGSKRILRSHEIVLPPSGQVETDLALTFSLQYPHFLKREGNKLQIMLQRRKRYKNRTILGYKTLAAGSISMAEVMQHPSEGGQVLSLCSSIKEAPVKAAEIWIASLSSQPIDHEDSTMQAGPKAKSTDNYSEEEYESFSSEQEASDDAVQGQDLDEDDFDVGKPKKQRRSIVRTTSMTRQQNFKQKVVALLRRFKVSDEVLDSEQDPAEHIPEAEEDLDLLYDTLDMEHPSDSGPDMEDDDSVLSTPKPKLRPYFEGLSHSSSQTEIGSIHSARSHKEPPSPADVPEKTRSLGGRQPSDSVSDTVALGVPGPREHPGQPEDSPEAEASTLDVFTERLPPSGRITKTESLVIPSTRSEGKQAGRRGRSTSLKERQAARPQNERANSLDNERCPDARSQLQIPRKTVYDQLNHILISDDQLPENIILVNTSDWQGQFLSDVLQRHTLPVVCTCSPADVQAAFSTIVSRIQRYCNCNSQPPTPVKIAVAGAQHYLSAILRLFVEQLSHKTPDWLGYMRFLVIPLGSHPVARYLGSVDYRYNNFFQDLAWRDLFNKLEAQSAVQDTPDIVSRITQYIAGANCAHQLPIAEAMLTYKQKSPDEESSQKFIPFVGVVKVGIVEPSSATSGDSDDAAPSGSGTLSSTPPSASPAAKEASPTPPSSPSVSGGLSSPSQGVGAELMGLQVDYWTAAQPADRKRDAEKKDLPVTKNTLKCTFRSLQVSRLPSSGEAAATPTMSMTVVTKEKNKKVMFLPKKAKDKDVESKSQCIEGISRLICTARQQQNMLRVLIDGVECSDVKFFQLAAQWSSHVKHFPICIFGHSKATF", "text": "FUNCTION: Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. SUBCELLULAR LOCATION: Endoplasmic reticulum Mitochondrion. SIMILARITY: Belongs to the PACS family."}
{"protein": "MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP", "text": "FUNCTION: Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response (PubMed:7516997, PubMed:10456871, PubMed:11406581, PubMed:11598100, PubMed:12438337, PubMed:12621045, PubMed:24331465, PubMed:23532847, PubMed:19237546, PubMed:35008838, PubMed:35110732, PubMed:35545676). Triggers inflammation by mediating cleavage of host proteins, which can both promote host pathogenesis by triggering sterile inflammation and/or restrict streptococcal infection, depending on host immune statue and infection site (PubMed:35110732, PubMed:35545676, PubMed:35008838). Cleaves host gasdermin-A (GSDMA) in epithelial cells, promoting GSDMA activation and formation of gasdermin pores, triggering pyroptosis (PubMed:35110732, PubMed:35545676). Pyroptosis triggers the elimination of the infected skin cell, depriving the pathogen of its protective niche, while inducing an inflammatory response (PubMed:35110732, PubMed:35545676). This ultimately prevents bacterial penetration of the epithelial barrier and a subsequent systemic dissemination of the pathogen (PubMed:35110732, PubMed:35545676). Also mediates cleavage of the cytokine precursor interleukin-1 beta (IL1B) to its mature form, resulting in inflammation and septic shock (PubMed:28331908, PubMed:32719155). SpeB-mediated maturation of IL1B plays a dual role depending on infection site: while IL1B inflammatory response prevents bacterial growth during invasive skin infections, it promotes streptococcal infection of the nasopharynx by disrupting colonization resistance mediated by the microbiota (PubMed:28331908, PubMed:32719155). Inhibits host autophagy be catalyzing cleavage and inactivation of key autophagy factors, such as CALCOCO2, NBR1 and SQSTM1 (PubMed:24331465). Cleaves and inhibits a number of complement factors, such as C2, C3-beta chain of C3, C4, C5 or SERPING1, thereby promoting evasion of host immunity (PubMed:18160402, PubMed:23532847, PubMed:35008838). May also impair adaptive immunity by catalyzing cleavage and degradation of host immunoglobulins to promote immune system evasion; the relevance of this activity is however unsure in vivo (PubMed:11406581, PubMed:11598100, PubMed:12438337, PubMed:12496168, PubMed:23569114, PubMed:35008838). Catalyzes maturation and release of the peptide hormone bradykinin from the precursor Kininogen-1 (KNG1) to produce hypotension during septic shock (PubMed:8760820). Also involved in bacterial translocation across the host epithelial barrier by mediating cleavage and degradation of host epithelial junction proteins, such as CDH1 and OCLN (PubMed:23532847). Additionally, has been involved in degradation of fibronectin and vitronectin, two host extracellular matrix proteins involved in tissue integrity (PubMed:7516997). Also able to catalyze cleavage and degradation of streptococcal proteins, such as C5a peptidase, EndoS or SmeZ (PubMed:7730368, PubMed:16980693, PubMed:18182097, PubMed:24799625). Degradation of streptococcal proteins is however strictly regulated to preserve integrity of other virulence factors (PubMed:24799625). SUBCELLULAR LOCATION: Secreted Host extracellular space Host cytoplasm. SIMILARITY: Belongs to the peptidase C10 family."}
{"protein": "MVSNPVHGLPFLPGTSFKDLTKTAFHRSQTLGYRNGYAVVRRPTVGIGGDRLQVNQLSQADLDELASKIPILTYGQARQAPPAAFVPAHVAFDKKVLKFDAYFQEDVPMSIEEHYRIRQVHIYYYLEDDSMSVIEPVVENSGIPQGKLIKRQRLSKNDRGDHYHWKDLNRGINITIYGKTFRIVDCDKFTQVFLESQGIELNPPEKMALDPYTELRKQPLRKYVTPTDFDQLKQFLTFDKQVLRFYAIWDDTDSMFGECRTYIIHYYLMDDTVEIREVHERNDGRDPFPLLMNRQRMPKVLVENAKNFPRCVLEISDKEVLEWYTAKDFIVGKPLTILGRTFFIYDCDPFTRQYYQEKFGISDLPRIDMSKKEPPPMKQELPPYNGFGLIEDSAQNCFALIPKAPQKDVIKMLMNENKVLRYLATLESPFPEDKGRRFVLSYFLATDMISIFEPPVRNSGIIGGKYLGRTKVVKPGSSVENPVYYGPSDFFIGAVIEVFGHRFVILDTDDYVLKYMESNAAQYSPEALLSIQNHIRKQEAPAPELDGQQAEEDPGVRDLEALIDTIQKQLKDRPCRDNIREAFQIYDKEASGYVDRETFFKICGSYQLPVDDSLIKELIRMCSHGEDKIDYYNFVRAFSN", "text": "FUNCTION: Microtubule-associated protein which regulates cell division and neuronal migration during cortical development. Necessary for mitotic spindle organization. Necessary for radial and tangential cell migration during brain development, possibly acting as a regulator of cell morphology and process formation during migration. May enhance calcium influx through CACNA1E and stimulate programmed cell death (By similarity). Microtubule inner protein (MIP) part of the dynein- decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (PubMed:34715025). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, cilium axoneme."}
{"protein": "MPGEATETVPAIEQQLLQPQAETGSGTESDSDESVPELEEQDSTQVTAQVQLVVAAEIDEEPVSKAKQRRSEKKARKARFKLGLQQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYMVFGEAKIEDLSQEAQLAAAEKFKVQGEAVSNIQENTQTPTVQEGSEDEEVDETGVEIKDIELVLSQANVWGAKAVRALKNSNDIVNAIMELTM", "text": "SIMILARITY: Belongs to the NAC-alpha family."}
{"protein": "MIQTFFDFPVYFKFFIGLFALVNPVGIIPVFISMTSYQTAAARNKTNLTANLSVAIILWISLFLGDTILQLFGISIDSFRIAGGILVVTIAMSMISGKLGEDKQNKQEKSETAVRESIGVVPLALPLMAGPGAISSTIVWGTRYHSISYLFGFFVAIALFALCCWGLFRMAPWLVRVLRQTGINVITRIMGLLLMALGIEFIVTGIKGIFPGLLN", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0056 (MarC) family."}
{"protein": "MAGLVLSGCAIKPFSQSLPIPTKRFITNPSNINLLHPKDPIFSPNFHGFSRWAVKVSAPLRIPSIDQQDLDLDLERERISSLDVQEEEIFDAGAPPPFKLADIRAAIPKRCWVKDPWRSMSYVVRDVAIVLGLAAAAAHLNNWLVWPLYWAAQGTMFWALFVLGHDCGHGSFSNNAKLNSVVGHLLHSSILVPYHGWRISHRTHHQNHGHVENDESWHPLTEKTFKSLDWITRTLRFTLPFPMLAYPFYLWNRSPGKSGSHFDPSSDLFVPAEQKDVITSTICWTTMLALLFGLNFVVGPVQMLKLYGIPYLINVMWLDFVTYLHHHGHEDKLPWYRGKEWSYLRGGLTTIDRDYGWINNIHHDIGTHVIHHLFPQIPHYHLIEATEAAKPVLGKYYREPKKSSPIPFHLLGELVRSLKKDHYVSDTGDVLYYQTDDKLSKEK", "text": "FUNCTION: Chloroplast omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 18:3, and probably also 16:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycerol. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family."}
{"protein": "MLGLKGCLTILIGYVIAVCALFSSRGRNPSLTDWEKLKDQKISNIDNFGLTGQHLLEFFQENLPFLSFSEEKYRHKHVSLYYDVFKEYILRRASSKKCLPVDSAIAKLNKDVNPMPVHSHNDYWRKLPLFEGLAYGASSTEADVWNIDEKILAVGHNEAYLDPVELTLDKLYTGPLLEILDEVNCQDSDADRKNGVFFNSPETSLFFYIDFKSDDNELTYKLLMEQYFKSLIDSGYLTYYDMKKDEIIWRPVTVILTGNYPTSLDILDNGNDNGYFESSQRFAFLDAPLLSLEPKYSKLSVAATVSFSQLMKHCGSDHWKVSLRGRMDSNEISCAKSIIDGAHALKLKTRIWGAPTWPANLVETISRQIIHDLGSDLLNLDNLFMASSLI", "text": "SIMILARITY: Belongs to the AIM6 family."}
{"protein": "MKRTHLFIVGVYVLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVAQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSGDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDDEDDDDDNSDEEDNDDSDDDDDDE", "text": "FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium- binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. SIMILARITY: Belongs to the calsequestrin family."}
{"protein": "MSVEIESIEHELEESIASLRQAGVRITPQRQAILRYLISSHTHPTADEIYQALSPDFPNISVATIYNNLRVFKDIGIVKELTYGDSSSRFDFNTHNHYHIICEQCGKIVDFQYPQLNEIERLAQHMTDFDVTHHRMEIYGVCKECQDK", "text": "FUNCTION: Manganese-dependent repressor that controls a regulon of oxidative stress resistance and iron-storage proteins. Regulates expression of genes encoding antioxidant proteins, such as katA, ahpCF, bcp and trxB. Also regulates expression of the iron-storage protein ftn, the ferritin-like protein mrgA, the ferric uptake regulator fur, the manganese transporter operon mntABC, and its own expression. May act as a hydrogen peroxide and organic hydroperoxide sensor. Required for full virulence in a murine skin abscess model of infection. FUNCTION: Manganese-dependent repressor that controls a regulon of oxidative stress resistance and iron-storage proteins. May act as a hydrogen peroxide and organic hydroperoxide sensor (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Fur family."}
{"protein": "MAPKKAPAATTEKKVKKAPTTEKKNKKKRSETFAIYIFKVLKQVHPDVGISKKAMNIMNSFINDSFERIALESSKLVRFNKRRTLSSREVQTAVKLLLPGELARHAISEGTKAVTKFSSSSN", "text": "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Macronuclei. SIMILARITY: Belongs to the histone H2B family."}
{"protein": "MKKNRLLFRVIILLILSGAVGFTLYQGFFADKEKMQIGKEAPNFVVTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIALDADETDIAVKNFVNQYGLKFPVAIDKGQKIIGTYGVGPLPTSFLIDKDGKVVEQIIGEQTKEQLEGYLKKITP", "text": "FUNCTION: Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Note=The thioredoxin-like motif is exposed on the outside of the membrane. SIMILARITY: Belongs to the thioredoxin family. ResA subfamily."}
{"protein": "MDPCECSKTGKCSCGGSCTCTNCSCTSCKKSCCPCCPSGCSKCASGCVCKGKTCDTSCCQ", "text": "FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family."}
{"protein": "YNRLCIKPRDWIDECDSNEGGERAYFRNGKGGCDSFWICPEDHTGADYYSSYRDCFNACI", "text": "FUNCTION: TAP is a slow, tight-binding inhibitor of blood coagulation, specific for factor Xa."}
{"protein": "MDPLKICENYLTFRSIIKGSTFSPGVFRRWRFHALADVVGNIVEREEGRFWEIVPETHTLWALFRGGFTVAPFTEILTSLQLENRGRQLAFLAFLSFLLRNWPSDSVVSEDARLDLVCAPAWSRIQIWSQAARLINDLPESVFEGQGSVVEEECGEEHLARDSDDPFFD", "text": "SIMILARITY: Belongs to the adenoviridae E1B 19 kDa protein family."}
{"protein": "MQQQHLFRLNILCLSLMTALPAYAENVQAGQAQEKQLDTIQVKAKKQKTRRDNEVTGLGKLVKTADTLSKEQVLDIRDLTRYDPGIAVVEQGRGASSGYSIRGMDKNRVSLTVDGLAQIQSYTAQAALGGTRTAGSSGAINEIEYENVKAVEISKGSNSVEQGSGALAGSVAFQTKTADDVIGEGRQWGIQSKTAYSGKNRGLTQSIALAGRIGGAEALLIRTGRHAGEIRAHEAAGRGVQSFNRLAPVDDGSKYAYFIVEEECKNGGHEKCKANPKKDVVGEDKRQTVSTRDYTGPNRFLADPLSYESRSWLFRPGFRFENKRHYIGGILERTQQTFDTRDMTVPAFLTKAVFDANQKQAGSLRGNGKYAGNHKYGGLFTSGENNAPVGAEYGTGVFYDETHTKSRYGLEYVYTNADKDTWADYARLSYDRQGIGLDNHFQQTHCSADGSDKYCRPSADKPFSYYKSDRVIYGESHKLLQAAFKKSFDTAKIRHNLSVNLGYDRFGSNLRHQDYYYQSANRAYSLKTPPQNNGKKTSPNGREKNPYWVSIGRGNVVTRQICLFGNNTYTDCTPRSINGKSYYAAVRDNVRLGRWADVGAGLRYDYRSTHSDDGSVSTGTHRTLSWNAGIVLKPADWLDLTYRTSTGFRLPSFAEMYGWRSGDKIKAVKIDPEKSFNKEAGIVFKGDFGNLEASWFNNAYRDLIVRGYEAQIKDGKEQVKGNPAYLNAQSARITGINILGKIDWNGVWDKLPEGWYSTFAYNRVRVRDIKKRADRTDIQSHLFDAIQPSRYVVGSGYDQPEGKWGVNGMLTYSKAKEITELLGSRALLNGNSRNTKATARRTRPWYIVDVSGYYTVKKHFTLRAGVYNLLNHRYVTWENVRQTAAGAVNQHKNVGVYNRYAAPGRNYTFSLEMKF", "text": "FUNCTION: Neisseria acquires iron by extracting it from serum transferrin (TF) in its human host. Acts as a TF receptor and is required for TF utilization. Binds both apo- and holo-TF, via the TF C- terminus. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family."}
{"protein": "MQLNKLMLGFMLCASALADDGQQAAEPHTSANFCKIDKDQQVGSTCDITFHELNEINEQIRPQLARLVKTDFFRYFKLDLYKECPFWSDNNGYCVNRACAVDVVDDWESVPDIWQPEVLGGLDEDSVKSEGGESDECSFLNELCGRRREFARPEPLSIDYCDVTDFTNKDSVLVDLVANPERFTGYGGEQSAQIWSAIYKENCFTLGEQGFCLAKDVFYRLISGLHASIATHLSNDYLDTKTGKWGPNLELFMARVGNHPDRVANIYFNFAVVAKALWKIQPYLERVEFCNVYDTNVKDMISNVVSRLDSRVFNEDLLFQDDISMRMKDDFRRRFKNVTKIMDCVHCDRCRMWGKVQTTGYATSLKILFEMDAGDEKARQRVVDKLTKYELIGLFNTFDRISKSVNAINNFERMYHSQMETNTSSIAAFFQNNFFRLGFTETEDQETSNATADMPLPEDSASDNEPYFADLKIPARRSKKQTKEESTSALQQELQGVYHALQFIWNSYVNLPRNLLILVLDVANTWFNNFIGVPTQINILGDDASD", "text": "FUNCTION: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Does not oxidize all pdi related proteins, suggesting that it can discriminate between PDI1 and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the EROs family."}
{"protein": "MPHIDVKFFPRDLSDAQQQALADELTQVIVKHLQSKESSVSVALKEVQPEQWKSEVWDTEIAPQLDTLARKPGYEM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family. PptA subfamily."}
{"protein": "IPLPPHPGHPGYINFSYEVLTPLKWYQSMMRHEYPSYGYEPMGGWLHHQIIPVLSQQHSPSHSLPPQHHIPIMAAQQPAPPQQPVMPVPGQHPMAPTQHHQPNLPQPGQQPYQPQPAQQPQPHQPIQPIQPIQPIQPMQPMQPMQPMQPMQPMQPQTPVHAVRPLPPQPPLPPMFPMQPMSPMLPDMEAWPATDKTKREEVD", "text": "FUNCTION: Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the amelogenin family."}
{"protein": "MYTPIPQSGSPFPASVQDPGLHIWRVEKLKPVPIARESHGIFFSGDSYLVLHNGPEEASHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERPVQHREVQGNESDLFMSYFPRGLKYYREGGVESAFHKTTSGARGAAIRKLYQVKGKKNIRATERPLSWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQVEIITDGEEPAEMIQVLGPKPALKEGNPEEDITADQTRPNAQAAALYKVSDATGQMNLTKVADSSPFASELLIPDDCFVLDNGLCAQIYIWKGRKANEKERQAALQVADGFISRMRYSPNTQVEILPQGRESPIFKQFFKNWK", "text": "FUNCTION: Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. Uncapping occurs either when Ca(2+) falls or when the concentration of polyphosphoinositide rises, both at low and high Ca(2+). SUBCELLULAR LOCATION: Nucleus Cytoplasm Melanosome Cell projection, lamellipodium. Cell projection, ruffle. Note=In macrophages, may be predominantly cytoplasmic. Nuclear localization was observed in fibroblasts. In macrophages, present at the membrane-cytoplasm interface. In activated macrophages, concentrated in the ruffles of the leading lamellipodia. SIMILARITY: Belongs to the villin/gelsolin family."}
{"protein": "MELRSWLLWVVAAAGAVVLLAADAQGQKIFTNTWAVHIPGGPAVADRVAQKHGFHNLGQIFGDYYHFWHRAVTKRSLSPHRPRHSRLQREPQVKWLEQQVAKRRAKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKEAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNADDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIVEILVEPKDIGKRLEVRKAVTACLGEPNHITRLEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPAGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLSTPPESSGCKTLTSSQACVVCEEGYSLHQKSCVQHCPPGFIPQVLDTHYSTENDVEIIRASVCTPCHASCATCQGPAPTDCLSCPSHASLDPVEQTCSRQSQSSRESRPQQQPPALRPEVEMEPRLQAGLASHLPEVLAGLSCLIIVLIFGIVFLFLHRCSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL", "text": "FUNCTION: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed:18713856). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (By similarity). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-45) (By similarity). By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells (PubMed:18713856). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein Cell membrane; Single- pass type I membrane protein Secreted Endosome membrane; Single-pass type I membrane protein Note=Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin. SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily."}
{"protein": "MFGPFKPAPHIAELPAEKIDSTYKRLRWQVFAGIFFGYAAYYFVRANFDLAQPGLIQAGLYSKAELGVIGSAAGLAYGLSKFVMAGMSDRSNPRVFLPFGLLLSGLCMTLMGLFPWATSGIAIMWVMIFLNGWFQGMGWPPCGRTMVHWWSKSERGTIVSIWNTAHNIGGMVPGAMVLLASAIFFSTHGIEAQAKDVWQQSLYFPGIAAMIFAIPVYFVMRDTPQSCGLPSIEKWRNDYPDDYNEKTYENDLTAKEIFVTYVLKNKLLWYIAIANVFVYLIRYGVLKWSPVYLSEVKHFNIKGTAWAYTIYELAAVPGTLLCGWVSDKVFKGKRGLTGFIFMILTTAAVVAYWMNPATPEAELANYSAWYENPYQLTDFVLMTLIGFLIYGPVMLIGLHALELAPKKAAGTAAGFTGLFGYLGGTVSASAVIGWAAQHYGWDGGFYVMIGGGVLAVLLLLIVMVEEGKHKAKLGDTYGTK", "text": "FUNCTION: Responsible for glycerol-3-phosphate uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family."}
{"protein": "MNLFGKSNFNCVFSSSLDWFHSSRLSEKVGTKKNRICRETESFYALCLSHRRYLCYALEGLLPSRPRGRRASTYNCSDNLGYIRGLNGKQKQLIKKLVHICMIDGKKTRSRAIVYKTFHRLAPHGDVIKLLVNAIENVKPICEVKKVRISGTTRLVPSIIATNRQETLAIRWMLESAAKRRMGKKSISLDQCLYAEILEASQKMGIARKKRDDLHKLAEANRSFSHYRWW", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly to 18S rRNA where it nucleates assembly of the head domain of the small subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS7 family."}
{"protein": "MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTISGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPKFYDE", "text": "FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MDILALGWVSVLALFTWSIAMVVWGRNGF", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetN family."}
{"protein": "MSLVCSVIFIHHAFNANILYKDYAFSDGEILMVDNAVRTHFEPYERHFKEIGFNENTIKKYLQCTNIQTVTVPVPAKFLRASNVPTGLLNEMIAYLNSEERNHHNFSELLLFSCLSIFAACKGFITLLTNGVLSVSGKVRNIVNMKLAHPWKLKDICDCLYISESLLKKKLKQEQTTFSQILLDARMQHAKNLIRVEGSVNKIAEQCGYASTSYFIYAFRKHFGNSPKRVSKEYRCQRRTGMNTDNTMNALAI", "text": "FUNCTION: Induces the expression of gadE and mdtEF. Could also regulate the expression of other genes involved in acid resistance (By similarity)."}
{"protein": "MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNDTDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL", "text": "FUNCTION: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain (PubMed:27344019). Inhibits nicotine- induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Cell membrane; Lipid-anchor, GPI-anchor Synapse, synaptosome Membrane raft Cell projection, dendrite Perikaryon Note=Colocalizes with alpha-3:beta- 4- and alpha-7- nicotinic acetylcholine receptors (nAChRs) in the primary cortex and hippocampus."}
{"protein": "MEQFKGLQKSLYIWTDSGELDKRVQALKEATGGEVAVENVHRLSFSSYANSSFDLIVIECAQLTDNYVKLLHMLKPSGKLHLFAYIGPAANLLQEIKLSGFINCSEDAAANTLTAEKPGYETGSSARLSFAKKSPSMNVWKISGDDEELIDEEELLDEEDKQKPDPAGLRVCSTTGKRKACKNCSCGLAEELEDEKKTKAATENAKSSCGNCYLGDAFRCSTCPYLGMPAFKPGEKVQLADNLLKSDI", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space. SIMILARITY: Belongs to the anamorsin family."}
{"protein": "MTIAMLLTLHLICVALSVSLFVARYWWRYCGHALAAARWTRIVPPVIDTLLLLSGIGLIVKTHILPFTESGSWLTEKLFGVIIYIVLGFIALDYRQARSQQARFIAFPLALVVLYIIIKLATTKIPLLG", "text": "FUNCTION: Required for maximal expression of sirC, not required to invade host cells. FUNCTION: Required for maximal expression of sirC, not required to invade host cells. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SirB2 family."}
{"protein": "MMRALLLAIGLGLVAALQAQEFPAVGQPLQDLLGRWYLKAMTSDPEIPGKKPESVTPLILKALEGGDLEAQITFLIDGQCQDVTLVLKKTNQPFTFTAYDGKRVVYILPSKVKDHYILYCEGELDGQEVRMAKLVGRDPENNPEALEEFKEVARAKGLNPDIVRPQQSETCSPGGN", "text": "FUNCTION: Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MASLRLSVLLVSVSWLLLLVSGLRAGPRTLVLMENINLRETHSLFFRSLSDRGFDLSFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINIETISSFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDPGQHTLIVADSENLLKAPTIVGKTPLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVVFSGSLDFFSDSFFNSAVQKAASGSNRYAKTGNYELAMALSRWVFKEEGVLRVGEVSHHRVGESSPPSAYTVTDLVEYSIVIEKLSDGKWVPFDGDDIQLEFVRIDPFVRTFLKKNGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSTTQISVRPLQHTQYERFIPSAYPYYASAFSVMFGLFIFSIVFLHMKEKEKSD", "text": "FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the DDOST 48 kDa subunit family."}
{"protein": "QLRAFVCRLSSVIFYETMYVGIVLLGLIAFDRFLKIIRPLRNIFLKKTVFAKTVSVFIWSFFFFISLPNMILSNKEATPSSVKKCASLKGPLGLKWHQIVNNISQFIFWTVFVLMLVFYVVIAKKVYDSYRKSKSKDRKNNKKLEGKVFVVVAVFFVCFAPFHFTRVPYTYSQTNNKTDCRLQNQLFIAKETTLFLAATNICMDPLIYIFLCKKFTEKLPCMRGRKTIASSQENQSSQTDNITLG", "text": "FUNCTION: Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MGAIMQANENMGSKLPKTDGKVIYLAGGCFWGLEAYMERIYGVVDASSGYANGKTQSTNYQKLHESDHAESVKVVYDPKKISLDKLLRYYFKVVDPVSVNKQGNDVGRQYRTGIYYVDNADKKVIDNALKELQKSVKGKIAIEVEPLKNYVRAEIYHQDYLKKNPNGYCHIDLKKADEVIVDSDKYTKPSDEVLKKKLTQLQYEVTQNKRTEKPFENEYYNKEEEGIYVDITTGEPLFSMADKYDSGCGWPSFSKPISKDVVKYEDDESLNMRRTEVLSRIGKAHLGHVFNDGPKELGGLRYCINSASLRFIPLKDMEKEGYGEFIPYIKKGELKKYIHDKTH", "text": "FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). SIMILARITY: In the N-terminal section; belongs to the MsrA Met sulfoxide reductase family. SIMILARITY: In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family."}
{"protein": "MGVFNYEAETPSVIPAARLFKSYVLDGDKLIPKVAPQVISSVENVGGNGGPGTIKNITFAEGIPFKFVKERVDEVDNANFKYNYTVIEGDVLGDKLEKVSHELKIVAAPGGGSIVKISSKFHAKGYHEVNAEKMKGAKEMAEKLLRAVESYLLAHTAEYN", "text": "SIMILARITY: Belongs to the BetVI family."}
{"protein": "MWTLGRRSVASFLPRSALPGFAPTRAGAPRPAKDLSLSGLPGLRIGTAKAPARSQSSLSLRCLNQTLDVKKQSVCWINLRTAGTLGDAGTLDDTTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGRNWVYSHDGVSLHELLATELTQALKTKLDLSALAYSGKDTCCPAQC", "text": "FUNCTION: [Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation. May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity). FUNCTION: [Extramitochondrial frataxin]: Modulates the RNA-binding activity of ACO1. May be involved in the cytoplasmic iron-sulfur protein biogenesis. May contribute to oxidative stress resistance and overall cell survival. SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Frataxin mature form]: Mitochondrion. SIMILARITY: Belongs to the frataxin family."}
{"protein": "MSIQKSTNSSSLAEVIDRILDKGIVIDAFARVSVVGIEILTIEARVVIASVDTWLRYAEAVGLLRDDVEENGLPERSNSSEGQPRFSI", "text": "FUNCTION: It is not clear if the 2 type A proteins in this organism are functionally redundant (PubMed:9573198). FUNCTION: When a minimal gvp locus (gvpA2-gvpR-gvpN-gvpF-gvpG-gvpL- gvpS-gvpK-gvpJ-gvpT-gvpU, called pNL29) is expressed in E.coli gas vesicles are made. FUNCTION: Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell. SUBCELLULAR LOCATION: Gas vesicle shell. SIMILARITY: Belongs to the gas vesicle protein type A family."}
{"protein": "MEIKNIKEFEKASKKLQKDTLKIALALLFLIGAALLALIFGQANSKGLLLIFAAVIGGYMAMNIGANDVSNNVGPAVGSKAISMGGAILIAAICEMLGAIIAGGEVVSTIKGRIVSPEFINDAHIFINVMLASLLSGALWLHVATLIGAPVSTSHSVVGGIMGAGMAAAGMVAVNWHFLSGIVASWVISPLMGALIAMFFLMLIKKTIAYKEDKKSAALKVVPYLVALMSLTFSWYLIVKVLKRLYALNFEIQLACGCILALLIFILFKRFVLKKAPQLENSHESINELFNVPLIFAAALLSFAHGANDVANAIGPLAAISQTLEDANSPIGNTLSSVPLWIMVVGAAGIALGLSLYGPKLIKTVGSEITELDKMQAFCIALSAVITVLLASQLGLPVSSTHIVVGAVFGVGFLRERLREQSRRRFARIRDNIVAAHFGEDLEEIEGFLERFDKANLKEKSLMLESLKKSKNTAIALELKKKEKKSLKKVYKEEVIKRSILKKIVTAWLVTVPVSALLGALLFVALGFIEKYF", "text": "FUNCTION: Potential transporter for phosphate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family."}
{"protein": "ALYITEECTYCGACEPECPVTAISAGDDIYVIDANTCNECAGLDEQACVAVCPAECIVQG", "text": "FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions."}
{"protein": "MDSLLMKQRKFLYHFKNVRWAKGRHETYLCYVVKRRDSATSFSLDFGHLRNKSGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVADFLRGYPNLSLRIFAARLYFCEDRKAEPEGLRRLHRAGVQIAIMTFKDYFYCWNTFVENREKTFKAWEGLHENSVRLSRQLRRILLPLYEVDDLRDAFRTLGL", "text": "FUNCTION: Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Predominantly cytoplasmic. In the presence of MCM3AP/GANP, relocalizes to the nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MAAVGSLLGRLRQSTVKATGPALRRLHTSSWRADSSRASLTRVHRQAYARLYPVLLVKQDGSTIHIRYREPRRMLAMPIDLDTLSPEERRARLRKREAQLQSRKEYEQELSDDLHVERYRQFWTRTKK", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL55 family."}
{"protein": "MPRHCSAAGCCTRDTRETRNRGISFHRLPKKDNPRRGLWLANCQRLDPSGQGLWDPTSEYIYFCSKHFEENCFELVGISGYHRLKEGAVPTIFESFSKLRRTAKTKGHGYPPGLPDVSRLRRCRKRCSERQGPTTPFSPPPRADIICFPVEEASAPATLPASPAVRLDPGLNSPFSDLLGPLGAQADEAGCSTQPSPEQHPSPLEPQPASPSAYMLRLPPPAGAYIQNEHSYQVGSALLWKRRAEAALDALDKTQRQLQACKRREQRLRLRLTKLQQERAREKRAQADARQTLKDHVQDFAMQLSSSMA", "text": "FUNCTION: Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors. SUBCELLULAR LOCATION: Nucleus Chromosome."}
{"protein": "MGKRRSRGRSQLLSTMTKKQKKHLRDFGEEHPFYDRVSKKEVKPQICQLSESSDSSHSESESESEQEHVSGYHRLLATLKNISEEEEEEEEEEEEEEEDKEEVDDSAVGDSEMNGEDGGEDVRVEETAESSETQDHMSLADNSKGKDGEEPPGVSQKSSEEFTDVKHESLFSLETNFLEEESGGSYSQRTSQDPFQHHINKELQEKEIQAAASSPAATQQLKWPVLGHLVFSSKFQKMETFKPPKDIDLKSLHLQKPLESTWAKTNSQFLSGPGPQKSSSCFTPLQKELFLIMNSYRDLFYPERTALKNGEEVRHVYCLHAINHVLKANAQVLANNSRRRTQKLGVGDDDDFRDQGLTRPKVLIVVPFREAALRVVQLFISLLEGDSKKKIIVSNKKRFQGEYGSDPEERPPNLKRPEDYEAVFVGNIDDHFRIGVAILQRSIRLYAPFYSSDILIASPLGLRTIIGGEGEKKRDFDFLSSIELLIIDQADIYLMQNWEHVLHLMNHMNLLPLDSHGVNFSRVRMWSLNNWSKYYRQTLLFGALQDAQINSVFNKHCVNAQGQVAVRNVPMTGSISHVLVQLPHVFQRMEAQDLASVIDARFHFFINKILPQYRDAVMSHTLIYVPSYFDFVRLRNYFKKEELNFTHICEYTQRSGVSRARHFFLQGEKQFLLLTERFHFYKRYTIKGIRNLIFYELPTYAHFYSEVCNMLRATSRGEEATWTCTVLYSKYDAQRLAAVVGVERAAQMLQSPKSVHLFITGEK", "text": "FUNCTION: Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver (By similarity). Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP25 family."}
{"protein": "MAALVKFFQHPGVRRFSIFVVLTGVLYLFKSMINLILLTFIFTFLMDRLELVVRQFVSQFFRVSQRVVITFLYMLLAVLLTVGGFVFYPVVAAQIQQLVKQIKHIAYHPDSIPFFDEITSVFGDINISSYVKEGFNVVYTYLADISTFGLQVVMALILSMFFLFEKKRLSEFMAKFKTSKLRVFYEEIAFFGSKFARTFGKVLEAQFIIALVNCILTFIALWIMHFPQLFGLSIMVFFLGLIPVAGVVISLIPLSIIAYSTGGGMYVLYIVLVIFAIHAIETYFLNPKLMSAKTELPIFFTFTVLIFSEHFFGIWGLIIGIPIFVFLLDILDVTNKEDRSKGPRENSDKK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family."}
{"protein": "MKRSISFRPTLLALVLATNFPVAHAAVPKDMLVIGKAADPQTLDPAVTIDNNDWTVTYPSYQRLVQYKTDGDKGSTDVEGDLASSWKASDDQKEWTFTLKDNAKFADGTPVTAEAVKLSFERLLKIGQGPAEAFPKDLKIDAPDEHTVKFTLSQPFAPFLYTLANDGASIINPAVLKEHAADDARGFLAQNTAGSGPFMLKSWQKGQQLVLVPNPHYPGNKPNFKRVSVKIIGESASRRLQLSRGDIDIADALPVDQLNALKQENKVNVAEYPSLRVTYLYLNNSKAPLNQADLRRAISWSTDYQGMVNGILSGNGKQMRGPIPEGMWGYDATAMQYNHDETKAKAEWDKVTSKPTSLTFLYSDNDPNWEPIALATQSSLNKLGIIVKLEKLANATMRDRVGKGDYDIAIGNWSPDFADPYMFMNYWFESDKKGLPGNRSFYENSEVDKLLRNALATTDQTQRTRDYQQAQKIVIDDAAYVYLFQKNYQLAMNKEVKGFVFNPMLEQVFNINTMSK", "text": "FUNCTION: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
{"protein": "MPFRSNNPLTRDELLSRFFPQFHPVTTFNSGLSGGSFLIEHQGQRFVVRQPHDPDAPQSAFLRQYRALSQLPACIAPKPHLYLRDWMVVDYLPGEVKTYLPDTNELAGLLYYLHQQPRFGWRITLLPLLELYWQQSDPARRTVGWLRMLKRLRKAREPRLLRLSPLHMDVHAGNLVHSASGLKLIDWEYAGDGDIALELAAVWVENTDQHRQLVNDYATRAKIYPAQLWRQVRRWFPWLLMLKAGWFEYRWRQTGDQQFIRLADDTWRQLLIKQ", "text": "FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine phosphate. SIMILARITY: Belongs to the thiamine kinase family."}
{"protein": "MRSTPPASAGRSTPPALAGHSTPPALAGHSTLCGRPVAGDRALIMAIVNRTPDSFYDKGATFSDAAARDAVHRAVADGADVIDVGGVKAGPGERVDVDTEITRLVPFIEWLRGAYPDQLISVDTWRAQVAKAACAAGADLINDTWGGVDPAMPEVAAEFGAGLVCAHTGGALPRTRPFRVSYGTTTRGVVDAVISQVTAAAERAVAAGVAREKVLIDPAHDFGKNTFHGLLLLRHVADLVMTGWPVLMALSNKDVVGETLGVDLTERLEGTLAATALAAAAGARMFRVHEVAATRRVLEMVASIQGVRPPTRTVRGLA", "text": "FUNCTION: Has very low affinity for the DHPS substrate 6-hydroxymethyl- 7,8-dihydropterin-pyrophosphate, but can bind the inhibitor dapsone. Seems to lack dihydropteroate synthase activity, and does probably not function in folate metabolism (By similarity). FUNCTION: Has very low affinity for the DHPS substrate 6-hydroxymethyl- 7,8-dihydropterin-pyrophosphate, but can bind the inhibitor dapsone. Seems to lack dihydropteroate synthase activity, and does probably not function in folate metabolism. SIMILARITY: Belongs to the DHPS family."}
{"protein": "MAERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGKRKTLNASDVLSAMEEMEFQRFVTPLKEALEAYRREQKGKKEASEQKKKDKDKKDCEEQDKSREEEDEDEERLDEEEQNEEEEVDN", "text": "FUNCTION: Accessory component of the DNA polymerase epsilon complex (By similarity). Participates in DNA repair and in chromosomal DNA replication (By similarity). Forms a complex with CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1 (By similarity). Does not enhance nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling complex (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSPKKAKKRLEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD", "text": "FUNCTION: Contractile protein that plays a role in heart development and function (By similarity). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (PubMed:15331360). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band."}
{"protein": "MKLGRATLALLLLVPCVVRAVEPISLGLALAGVLTGYISYPRLYCLFAECCGQKRSLSREALQKDLDNKLFGQHLAKRVILNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQMWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVDEVSYQKAIFIFLSNAGAERITDVALDFWRSGKQREEIKLRDMEHALAVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEEDEDIINKVAEEMTFFPKEEKVFSDKGCKTVFTKLDYYLDD", "text": "FUNCTION: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Nucleus inner membrane; Peripheral membrane protein Cell projection, growth cone. Cytoplasmic vesicle membrane. Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus envelope is mediated by the interaction with TOR1AIP2. Upon oxidative stress, redistributes to protusions from the cell surface. SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily."}
{"protein": "MSHLVSSSLGTTTTATPTSRSPHTNHSTPYNQNSITSNRSSPVPKNSVNSRIIPQTMNPPIDMKSNNILNPEKDTDTSRGDHSESKASSISSASGTTTTNNNNVSNNNSTGKTQIVFIHKLYDMLHDESISHLIWWSPSLDSFYVTPGEEFSRVLSQYFKHTNIASFIRQLNMYGFHKVNEPFLNQDDQQQQQQLQSNRWEFRHSTNQFRKGDTESLKNIKRRSSKTLNAQKEVVNIKSLPPTSHPMEYNTGYSYQNEDSAHYFVHHHSITTMQSPADMRPRSPSTPIPMQPLAQQQQQQQQQQQQQQQQLPSQPVPNGPPVFSGPIPPGAVNQSPQEYLTRPSILNNVQGSFENATNFKFVELTNQINLLRNDFFTMNNRYEILQNELKYQTADSMAVLEILEKLSNDNRIATDIRDLKNVVSQRMQRLNNQFIPQQSNFAPHIPGQQQQQQHGNSVSSNYHLESTNVSRNPSTTNLNVAPQPYPLNPHYTIYANNRASGSSEINNGVFRAREDSNNSKRNLSVYDPLQPVPSRNSSRILIEESTPTHPPTNFNPQQSQSQSQVQLGPAMPPQGFRNRAESTYSPLSHSSNKSQILNKAPTPVNHSPLVQQQQKEAKQELNDSSVAPPSQSSLPVTRPLSRQQQQQQQTLHHPSTTSSRTNSLPNPVAEHPAPQSSYFMQRNSFNTVYEHQKSLRVPSPKRVRYATPPRSIPEQPISSTAPTTMITSTSKPTSTSGAAISRSENHSVVSLTGGALPSVSELDKSIRTGSSVSLPPIKSIKDNDNKNDNGNSDDNGNDHKKRKLE", "text": "FUNCTION: Transcription factor that plays a role of repressor of filamentous growth and flocculation. Antagonizes functions of SFL2 and FLO8. Plays a role in the hyphal repression induced by secreted factors like dodecanol by competitors such as Pseudomonas aeruginosa and Burkholderia cenocepacia. SUBCELLULAR LOCATION: Nucleus Note=Localizes to the nucleus in both yeast and hyphal cells. SIMILARITY: Belongs to the HSF family."}
{"protein": "MRSLRRVLLQLVLLAGVAFRGVRFDDAADAAAAAQGSSDLFELPSPSPTLALPGGGDEGASTEIIAAPWPGRHGLFTPPRSTSQPARAVVQPAADFGSQLQFYDNGTIQLVDLLSKLPRWQFSTGPPLSKHITTSKPDLNYVIYLDGSETSDLIEVHNGSGVRLPWKLEEFIAETPYIRDSFVTIGSKVSTTFVVNADSGEIIYKHSLPVALNEVGGPLVEEIPSKLDAARSGTSANIIVVVRTDYSISASDLGEHLFNWTRTSFTANYYARYGHQDMLAQSSCLRGNIPCIRTEGPPIKLYLPDSSSDNAIVLRPVNEVSAVDALEPLLPPKKLPQPAGESNVALDSAQNQTADIALGHFVPADTELTNSVTKFSYRWLFPTFLMLLIMACLVKLADASKYCRQFVIRFLKPFMRDEKLMDPRGKSEGTSKRRKARKKDGLINSTQIFSASDKEGNGTGGSTEAQSNKAHDSTNVELPNGLNGRQIGKLCVYSKEIGKGSNGTVVFEGSYGGREVAVKRLLRSHNDIASKEIENLIASDQDPNIVRMYGFEQDNDFVYISLERCRCSLADLIQLHSVPPFSNTKGTDIELWRQDGLPSAQLLKLMRDVVAGIVHLHSLGIIHRDLKPQNVLISKEGPLRAKLSDMGISKRLQEDMTSVSHHGTGFGSSGWQAPEQLRHGRQTRAIDLFSLGCLIFYCITKGKHPFGEYYERDMKIINNQFDLFIVDHIPEAVHLISQLLDPDPEKRPTAVYVMHHPFFWSPELCLSFLRDTSDRIEKTSETDLIDALEGINVEAFGKNWGEKLDAALLADMGRYRKYSFESTRDLLRLIRNKSGHYREFSDDLKELLGSLPEGFVQYFSSRFPKLLIKVYEVMSEHCKDEEAFSKYFLGSSA", "text": "FUNCTION: Involved in endoplasmic reticulum (ER) stress response. Senses unfolded proteins in the lumen of the ER via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP50 mRNA to generate a new C- terminus, converting it into a potent unfolded-protein response (UPR) transcriptional activator, which then induces transcription of UPR target genes, such as luminal-binding protein (BiP) chaperones. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MEFSPPLQRATLIQRYKRFLADVITPDGRELTLHCPNTGAMTGCATRGDTVWYSTSDNTKRKYPHTWELTQSQSGAFICVNTLWANRLTKEAILNESISELSGYSSLKSEVKYGAERSRIDFMLQADSRPDCYIEVKSVTLAENEQGYFPDAVTERGQKHLRELMNVAAEGLRAVIFFAVLHSAITRFSPARHIDEKYAQLLSEAQQRGVEILAYKAEISAESMALKKSLPVTL", "text": "FUNCTION: Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism. SIMILARITY: Belongs to the SfsA family."}
{"protein": "MENMENDENIVVGPKPFYPIEEGSAGTQLRKYMERYAKLGAIAFTNAVTGVDYSYAEYLEKSCCLGKALQNYGLVVDGRIALCSENCEEFFIPVIAGLFIGVGVAPTNEIYTLRELVHSLGISKPTIVFSSKKGLDKVITVQKTVTTIKTIVILDSKVDYRGYQCLDTFIKRNTPPGFQASSFKTVEVDRKEQVALIMNSSGSTGLPKGVQLTHENTVTRFSHARDPIYGNQVSPGTAVLTVVPFHHGFGMFTTLGYLICGFRVVMLTKFDEETFLKTLQDYKCTSVILVPTLFAILNKSELLNKYDLSNLVEIASGGAPLSKEVGEAVARRFNLPGVRQGYGLTETTSAIIITPEGDDKPGASGKVVPLFKAKVIDLDTKKSLGPNRRGEVCVKGPMLMKGYVNNPEATKELIDEEGWLHTGDIGYYDEEKHFFIVDRLKSLIKYKGYQVPPAELESVLLQHPSIFDAGVAGVPDPVAGELPGAVVVLESGKNMTEKEVMDYVASQVSNAKRLRGGVRFVDEVPKGLTGKIDGRAIREILKKPVAKM", "text": "FUNCTION: Produces green light with a wavelength of 544 nm. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family."}
{"protein": "MNNPAQLRQDTEKEVLALLGSLVLPAGTALAATGSLARSELTPYSDLDLILIHPPGATPDGVEDLWYPIWDAKKRLDYSVRTPDECVAMISADSTAALAMLDLRFVAGDEDLCAKTRRRIVEKWRQELNKNFDAVVDTAIARWRRSGPVVAMTRPDLKHGRGGLRDFELIKALALGHLCNLPQLDAQHQLLLDARTLLHVHARRSRDVLDPEFAVDVAMDLGFVDRYHLGREIADAARAIDDGLTTALATARGILPRRTGFAFRNASRRPLDLDVVDANGTIELSKKPDLNDPALPLRVAAAAATTGLPVAESTWVRLNECPPLPEPWPANAAGDFFRILSSPKNSRRVVKNMDRHGLWSRFVPEWDRIKGLMPREPSHISTIDEHSLNTVAGCALETVTVARPDLLVLGALYHDIGKGFPRPHEQVGAEMVARAASRMGLNLRDRASVQTLVAEHTAVAKIAARLDPSSEGAVDKLLDAVRYDLVTLNLLEVLTEADAKATGPGVWTARLEHALRIVCKRARDRLTDIRPVAPMIAPRSEIGLVERDGVFTVQWHGEDLHRILGVIYAKGWTITAARMLANGQWSAEFDVRANGPQDFDPQHFLQAYQSGVFSEVPIPALGITATFWHGNTLEVRTELRTGAIFALLRTLPDALWINAVTRGATLIIQAALKPGFDRATVERSVVRSLAGS", "text": "FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism (By similarity). SIMILARITY: Belongs to the GlnD family."}
{"protein": "MNASQQIHVFSSHWKVESVIISLIFSMIFLVGTVGNCLVLAVLIRNGQMNTKSTNLFILNLGLADLCFIVFCVPLQATIYTMDEWVFGAFVCKAVHFIIYLTMYASIFTLAAVSLDRYLAIRYPLRSRETRTPRNALTSISLVWALSLFFSSPYLSYYQQMDLDGTTVCIPAWSVHHRQAMDICTFIFGYLIPVLILGITYARTIRYLWTSVDPMQDMSESRKAKRKVTKMIIIVAVLFCLCWLPHHLVILCMWFGHFPLNHTTYVLRILSHLVAYANSCLNPIVYALVSKHFRKGFKKVFGCAFRNRVVNRIHTVQPAQTVSLMEAASSEGSNHCDGSTRGRLWSKSSKKMMTSAFMTFNVT", "text": "FUNCTION: Receptor for the hormone galanin (PubMed:24517231). Receptor for the hormones spexin-1 and spexin-2 (PubMed:24517231, PubMed:31474838). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MGYVKVVKTSPYFSRYQVKYRRRRQGKTDYRARLRLVRQDKNKYNTHKYRLVVRFSNKNVTCQIVYSTIQGDVVMAAAYSKELPNYGLKVGLTNYSAAYCVGLLVARRILTKLNLADTYKGQEEPDGEDYNVEPVEDGPKPFYCLLDTGLKRTSTGSKVFAAMKGALDGGLDIPHNEKRFVGYADKKLDTEVLQKYIYGGHVAEYQETMQEEEPEKYQAHFSSYVENEIEPDGIEDMYKEVHAKIRENPCPPKKERTKPADAKRWSPQAHL", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the universal ribosomal protein uL18 family."}
{"protein": "MSSIGGKLQKSLHKIRAGALGIPLPKHIQEVSIQYSLDSRLGHMGAKKFVKECLPSLYYNNYGLKFNVNHRLPNDQTPTFSIISNNKVIYSYDMRSKQLETISSDIQKALKELHHESSPENIKEAHKQDYSPPSN", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mL61 is not essential in cells grown at 30 degree Celsius but is required for mitochondrial translation in cells grown at 18 degree Celsius. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL61 family."}
{"protein": "MGNLLGGVSFREPTTVEDCDSTWQTDSEPEPEQPGPAGGGEGQQHDEPEQPKQPPERAGGRPRASPVPEDHAEAAGAEQGGESTEGNAKPKRSFYAARDLYKYRHQYPNFKDIRYQNDLSNLRFYKNKIPFKPDGVYIEEVLNKWKGDYEKLEHNHTYIQWLFPLREQGLNFYAKELTTYEIEEFKKTKEAIRRFLLAYKMMLEFFGIKLIDKTGNVARAGNWQERFQHLNESQHNYLRITRILKSLGELGYESFKSPLVKFILHEALVENTIPNIKQSALEYFVYTIRDRRERRKLLRFAQKHYTPSENFIWGPPKKELPERSKAQKTPTLPASGSNGQTSTHKKSKDSKISPGASHVNSKSVEEKKGASREPGEEADKPSPEPGSGDPKPRNTEKDSAADQSDSPPEKTVPDTAGKGECPTSSEKDGEGEDQSKDSENPENAGCHAEVVAQQNATNPQTSSG", "text": "SIMILARITY: Belongs to the opioid growth factor receptor family."}
{"protein": "MIETSKRSRIINKINNVVISDYKGAIFVWGPKSTGKYTTIKHVLESNSRIYCEADCNEHYSTASLFRSLLSTLRNINKFGRRKPINYDDDDEYINNDINKDNEEDNNNNNNNNNNNNNNNNNNNNNNNNNNNDGYDDGYDDDYDYKDKSLNERIELLKINDLSKEFNNMIIKSQIYSKKIPATSIPSVSEMVQVLYEKASTNETISIILRHSEKLMKFEGEFFYSLFKIEEFTDHPVCLYLLSEIPTERILSTGKEFKPIRNIHFPQYEPNEICSIVLNFKPNFSIINYNQNNNDSNNSNNNNNNNNHLKLKEEDNIKLYNKLVELVVRVFHTTTRDIIDIIFVCHNLFPNYIEPIYNGTCGVEDSDSILYQNIESKIVKSLRNITEKDEIVLEDQKRQQETYQIYPPQQVPQQQKQQEKEKEKEKGRQLASYSDAKNIPYHMKIVLISCFLASSFSRNKDKLLYTKEAVKRQSLSNEKTTGSKWFHFQRAREIGYKLFPSEKKALFQESIFKSLASLKYLETISSIEPAFTYKFKCTRRVHLEFIKQISASINFKIDTYLEAAQFQIISK", "text": "FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC1 family."}
{"protein": "MVEVRHSIPCEETKRLELSLSQQTYSQQYASIYFARLTALRPRITEAASKKWPDKQRLERVLDVKSDEDCWVVATAYMTTALKPNVMNDVTQLHTIVTTTEESPYVSPEDAASGDIEYALEDDYGRIDCSGSFLYDAGVVTGVVLAVLGHEDEQGRFVVVDVCFPGIFSHSIPMTTDESQAQPEYIAAVSGLGLSNDGIEGIQVHQLVDFLRGTLPHVSSFSPSSIKRLIILGNCLAPSIEIADSASASVPIGKKKVKRYGYDTSAYNPNPTFQLDNFLDQVCSSIDVTLMPGPYDYSSTILPQQPLHPALLTKSKVWLGSSLQTVTNPTWLSLGNHFVLATSGQNINDLRKYHPKKSSLQCMENTLLWNHITPTSPDTLWCYPFTDKDTFVMEEMPDLYLCGNQPKFGCKTVINEGNRIQLVSVPEFRKTGVLVLINMHTLNVEIIQFRPMSVKAETPITS", "text": "FUNCTION: Required for replication of the leading DNA strand and for completion of lagging strand synthesis. It is essential for cell cycle progression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA polymerase delta/II small subunit family."}
{"protein": "MSTQTKKVTRTIITSSSGGGGGGGGGRASYSSSGRFSGGGGRMRAGGVTSRRSVGSSYSAGGGGRVNAVMAAGVMASVGGPAGALQTLSDARMTRAHEKQELSHLNDRFASYIDKVRYLQERNSKLEAQIKIQESREAPNIKDLYEKELRDLRALVDELSNDKAQLEIERNNWQEQAEDYKMKWQDEAGLRSELEAEIERLKKELDAATMARLDLENKLSTAQEEIDFLKRVHDEEIRQLQDQLNESLTIVEVDSRAASTFAPGPDLTEALREIRTQYEELGRVNREDADVKYKQKFSELAHQRERDNEALMTARTEVTELRRNLNSLVAENEALKSKNHALEGSLAELEARMQLEIEEYQAAIRDLEQELETKTSEMAQQMQAYKMLMDTKMALDMEIAAYRKLLEGEEIRLFGESKEGVQQTSSSSSSSYQYSMKSGSGGGGGGSSSGKQQVTVSVSSGEEK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MNLRQVEAFRAVMLTGQMTAAAELMLVTQPAISRLIKDFEQATKLQLFERRGNHIIPTQEAKTLWKEVDRAFVGLNHIGNLAADIGRQAAGTLRIAAMPALANGLLPRFLAQFIRDRPNLQVSLMGLPSSMVMEAVASGRADIGYADGPQERQGFLIETRSLPAVVAVPMGHRLAGLDRVTPQDLAGERIIKQETGTLFAMRVEVAIGGIQRRPSIEVSLSHTALSLVREGAGIAIIDPAAAIEFTDRIVLRPFSIFIDAGFLEVRSAIGAPSTIVDRFTTEFWRFHDDLMKQNGLME", "text": "FUNCTION: Positive regulatory protein for the occ operon involved in octopine catabolism and uptake. Also acts as a negative regulator of its expression. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MTAIKGKLQELGAYVDEELPDYIMVMVANKKSQKQMTDDLSLFLGSNTTRFTTWLQGVLDKLRSVTPESNSMKTSDAIIFESSMPSLKSLSNSRDDLAKDVPTLTVSSTRHGRYDSSTSSHVQATGSSGSVARLTSAVKPLREFSPSEAVIDIKLDLDDPFNEDLSLATEIANLSRKRTALSASYRTLRPTAEVYRPPGIGQHAYHTNENNSSLHRFPQSSFVSGRSLKLQSSMTVGSSRIQDVSDLSETYKTAFRLASEKSLREEETSRKRRLPVASSVVKVKKLITDEEEVEEEGEEDEEGTDCIFRTAGISSSVSVPAKPERRPSLPPTKQANKNLILKAISEAQDCISKTTNYSTAAPQKQTVPVIPRSRLLPEEEQLMLLQNRSSLLNYPSHLQELQHQAMPEPLHKLDLLSRLQPNLEEEIELPNPVNSEEAEILRPLDSRSFILKRPKLSKEPSPQIQNNSVSPPCPAQPLPGRMIQPREAPTYEKPASPKFIVTLDGVPSPPGYISDQEVDESMCYTEQGETCVEQLGVVARPEQNYPMQLVTEPLCTNDVVMENTSSGTKEKIRERCKYWPACKNADSCAYHHPTSPCKSFPNCRFADKCFFIHPNCKYDAKCKKADCPFTHASKRFPVPPVKPVSTTSSSHPSSQPCRYFPACKKTDCSFYHPKHCRFNTQCTRPDCKFYHPAVSVPARHTLKWTRAQASD", "text": "FUNCTION: May bind to RNA. SUBCELLULAR LOCATION: Nucleus speckle Note=Colocalizes with poly(A) RNA in nuclear speckles. SIMILARITY: Belongs to the ZC3H14 family."}
{"protein": "MKIINILFCLFLLMLNGCNSNDTNNSQTKSRQKRDLTQKEATQEKPKSKEELLREKLNDNQKTHLDWLKEALGNDGEFNKFLGYDESKIKSALDHIKSELDSCTGDKVENKNTFKQVVQEALKGGIDGFENTASSTCKNS", "text": "FUNCTION: An outer membrane protein that may participate in pathogenesis. Some human Lyme disease patients have antibodies against this protein (PubMed:10948116). The Mlp proteins probably undergo intragenic recombination, generating new alleles (Probable). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the Multicopy lipoprotein (Mlp) family."}
{"protein": "MDKEVTKIESDDTSSVEIKVLLFARARELTGVPDLTLKMPSGSTTQKCLDELVLKFPSLEEVRSCVVLALNEEYTTDSAIVQHRDELAIIPPISGG", "text": "FUNCTION: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily."}
{"protein": "MDDCRFETSELQASVMISTPLFTDSWSSCNTANCNGSIKIHDIAGITYVAIPAVSMIQLGNLVGLPVTGDVLFPGLSSDEPLPMVDAAILKLFLQLKIKEGLELELLGKKLVVITGHSTGGALAAFTALWLLSQSSPPSFRVFCITFGSPLLGNQSLSTSISRSRLAHNFCHVVSIHDLVPRSSNEQFWPFGTYLFCSDKGGVCLDNAGSVRLMFNILNTTATQNTEEHQRYGHYVFTLSHMFLKSRSFLGGSIPDNSYQAGVALAVEALGFSNDDTSGVLVKECIETATRIVRAPILRSAELANELASVLPARLEIQWYKDRCDASEEQLGYYDFFKRYSLKRDFKVNMSRIRLAKFWDTVIKMVETNELPFDFHLGKKWIYASQFYQLLAEPLDIANFYKNRDIKTGGHYLEGNRPKRYEVIDKWQKGVKVPEECVRSRYASTTQDTCFWAKLEQAKEWLDEARKESSDPQRRSLLREKIVPFESYANTLVTKKEVSLDVKAKNSSYSVWEANLKEFKCKMGYENEIEMVVDESDAMET", "text": "FUNCTION: Probable lipase required downstream of MPK4 for accumulation of the plant defense-potentiating molecule, salicylic acid, thus contributing to the plant innate immunity against invasive biotrophic pathogens and to defense mechanisms upon recognition of microbe- associated molecular patterns (MAMPs). Participates in the regulation of various molecular and physiological processes that influence fitness. Together with SG101, required for programmed cell death (PCD) triggered by NBS-LRR resistance proteins (e.g. RPS4, RPW8.1 and RPW8.2) in response to the fungal toxin fumonisin B1 (FB1) and avirulent pathogens (e.g. P.syringae pv. tomato strain DC3000 avrRps4 and pv. maculicola, turnip crinkle virus (TCV), and H.arabidopsidis isolates CALA2, EMOY2, EMWA1 and HIND4). Together with EDS1, confers a basal resistance by restricting the growth of virulent pathogens (e.g. H.arabidopsidis isolates NOCO2 and EMCO5, E.orontii isolate MGH, and P.syringae pv. tomato strain DC3000 or expressing HopW1-1 (HopPmaA)). Necessary for the salicylic acid-(SA-) dependent systemic acquired resistance (SAR) response that involves expression of multiple defense responses, including synthesis of the phytoalexin camalexin and expression of pathogenesis-related genes (e.g. PR1, ALD1, BGL2 and PR5) in response to pathogens, triggering a signal amplification loop that increases SA levels via EDS5 and SID2, but, together with EDS1, seems to repress the ethylene/jasmonic acid (ET/JA) defense pathway. May also function in response to abiotic stresses such as UV-C light and LSD1- dependent acclimatization to light conditions that promote excess excitation energy (EEE), probably by transducing redox signals and modulating stomatal conductance. Regulates the formation of lysigenous aerenchyma in hypocotyls in response to hypoxia, maybe via hydrogen peroxide production. Modulates leaf senescence in insect-infested tissue and triggers a phloem-based defense mechanism including antibiosis (e.g. green peach aphid (GPA), M.persicae) to limit phloem sap uptake and insect growth, thus providing an EDS1-independent basal resistance to insects. Also involved in regulation of root meristematic zone-targeted growth arrest together with EDS1 and in a VICTR-dependent manner. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Can move to the cytoplasm when in complex with EDS1. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MLIPYSPHTIWKTICATLLLSLAFFSQAEQDDSVEFNIHMLDAEDRDNVDLSRFSTSNYIIPGMYYLDIRLNGRDFPRQNINYIEVADNHSVACIDPTLLKKLTINQENQKYIKQISPDCFDISQLPGISIKNDGGVLDITLPRSLMKYEESDWTPPELWDSGVSGLIFDYTLTGTSTRPNKGNNNNTLTGYGQAGLNLGEWRLRAEYQGNYSSEYSSNNRFDWNQIYAYKPLPDLAAKLTVGETYLNSQIFDSFRFTGANLQSDERMLPPSLQGYAPEIHGIANTNAKVTVTQNGRLIYETTVPAGPFVINHLQNTVQGQLDVRVEEQNGKINEFQVQTANLPYMTRPGSVRFNTSLGQSSVNNHKMQGPLFYQGDFSWGMNNTWSLYGGTLLTAKDYNAWSLGIGHDMGRFGTLSGDITQSYSKTYDNEKINGMSFKLNYAKTFDEYHSTITFAGYRFSEKTFRSFSQYIDERYNGINNNGYEKEMYTITGNKTFWADDAEKSTTLYLSYRHQNYWDKNTQEQYGVTVSRNFSIMGIEQINTNLSAFRTQYKGNTDDTLSFNISLPLGSGRNIGYNLQDNNGKVTQMASYADNRDYNNLWRIRAGLSSDKKANTDGYYQHRSQYAEINANASYQQDNYLAVGATIKGGFTATRYGAALHSSSMTSSTARIMVDTDGVAGVPFNGQSTTTNRFGIGVLTDLTSYNNVDARIDVDKMDQDIETRKAIASTTLTEGAIGYYQFPVRQGERLMAVLQTTDNKYPPFGAEVTNQKGESIGMVMEEGLVYIAGVNLNESLNVIWNGKTQCSITIPAEITDPLKHQSLVCQDR", "text": "FUNCTION: Involved in the export and assembly of PMF fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
{"protein": "MAESDSGESTSSVSSFISSSSSSRLSEFVDAKTELQDIYHDLSNYLSNFLTILEETVLLKDRQMLEHLCAFSSRVEAIAKVLSRDRMKVAFFGRTSNGKSAVINALLHEKILPSAMGHTTSCFCQVQANGSNETEHVKVEQEDEHMELSALSQLASAHSPGALKPSTLLQVNMAKNRCSILDYDVVLMDTPGVDVTAQLDDCLDSYCMDADVFILVLNAESTVSRVERQFFKDVASKLSRPNLFILNNRWDKASSLEPEMEQKVKDQHMERCVNLLVDELGVYSTAQEAWERIYHVSALEALHIRNGQITNPSGQTQQRYQEFLRFENDFSNCLAVSALKTKFGPHLLSAQKILNQLKSTLICPFIEKVSRLIDENKERRANLNAEIEDWLILMQEDREALQYCFEELTEMTQRVGRCVLNDQIKTLIPSSVLSFSQPFHPEFPAQIGQYQRSLCAHLDKLLEDRVLQCLSIPLQRKILDIEKEIGLPIAENSCDWQLIYGLDCQSYMSDFQPDLRFRFSLGFTALWHRLEGNLPLHASPFRIQKLQNGHKKCSPLPPLVNGNHWQMLESLVKSKGSLGTVLLSAMAIRSFNWPIVLILGGLVGSFYIYEYAAWTTAAQERSFKSQYARLLQQRLRSDVQQTVSGFELQLRQHLATVRNCWEAQSNETLNDLNVRTAELTKQIQSMEVLQLSLKKFRDKGQLLASRLGDFQETYLTKS", "text": "FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis (PubMed:9230308, PubMed:18799731). In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission (PubMed:9230308, PubMed:18799731). Essential for fertility (PubMed:9230308). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily."}
{"protein": "MSQMRVTDFFSQSKRGTAAQNSKGRKVEAVLETRRAVTRSRAASVKAEEFLKAPCTPERASPTVSQCIGPSSKKRTRQDSDSEPLRTQQRQGKSARKKLKLPEGEHGGSVQQQLFSPCNKVALEHVTPSSLGKKIKDMVNVSLSPKFNELARNPTTPETKSPAKENLLELKSRLQRIQELAQKVNLPAASSEGKVTITDLKARLKRAQELDTKIRAKAEKTETQAIDLTEQPAQESEKAPAYQRFHNLAQDAAPGLTLPYKYKVLAEMFRSMDTIVGMLFNRSETITFSKVKQGVQDMMRKQFEQRNVGQIKTVYPNAYKYRQEKNIPTFKDGVKKTDYQLTIEPLVAEGDMLSGRPHLSASRLLERKQLFHRSLTSIVKQHHRVFLTSLNPPMLVPDDKLTRWHPRFNVDEVLDVTPAELPLPPQVERLTTAQEVLSKARGLITPKMEKALANLALKTAENAGETKNVSTEETKSTATTSTSTALKGVSQSLLERIRAKEAQKLQAIMTRRPQQEERLLMMSRLPELARILRNVFVAEKKPALTLEVTCSRVIASCRSSMSPGEMEKHLALLSEILPDWLSIHPVRKDTYYKLNQSMDLNLILERLAKKTKEEESL", "text": "FUNCTION: DNA replication licensing factor, required for pre- replication complex assembly. Cooperates with cdc6 to promote the loading of the mini-chromosome maintenance complex onto chromatin to form the pre-replication complex necessary to initiate DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Cdt1 family."}
{"protein": "MESLIQHILSATSSLSMPSVDSDKLQLLLTRFPQATLSWLSGIDGLSVHQFKVVATHVIKESYSHLSPSVAVLLAKPSDYYKLVVHGLTQKQWNEFDDKVTDAPRTAISWLYNQILVVGQPWMKSLNEGLKEYLPGWLHTCLRMLANLWFGAERVLHGISHAVSDITTYQPWMSCRRCVAHSPKESLLGEATTTSNPRESSWFSWLLCGGVVAATVYGFYKWVTITETIDRQDLAKQRPTHMQKCYEEVKARLEEESKGFIHDRMEDELTKIVLEPAEIDNDGKVLKSEVAQYLVKNHGRFVRSLVTMAKNEFAGVPKPTEANQLAVWRYLYRVCDKKGVNPSDTQKSISAALPFVFLPSAYDQDQAITMNCDDTKKVLERYADTFRHTTPLQKLVTNPLVGANWTAWARSIFISDPETGLRFAKXGCIEKWQGVQCKRTRVRHPRLRCHFKDRDPKVRSIYRIAGLGDQYEFGLHNNSAANLERGLAERVYMVKNYKTDFVASLDPAFCPAPEPVRGIFKRLDKYKKEIVRRVGRKSPITDEMFLSYYDGPQLTTYSKAVISLSERPVAVQDSYLKTFIKAEKLNLTLKTDPCPRVIQPRHPRYNVELGKYLKHIEHPIYKAIDRIWGGKTIFKGMNVEAMGAEIHKKMCKYSNPCAIGFDASRFDQHVSVEALRFEHSIYKSIHGYPELLSLLLKWQIHNQGTAHTNDGFFKYLVDGKRMSGDMNTSLGNCILASLIVKDLVDSLGVDAQLVNNGDDNVLICSVDDEEVVVKALYDHWMKYGFEVVAEQPVYITEQIEFCQMKPVFDGTQYVLVRNPTVTMSKDACSITPFYTANSARKWCRAVGEAGLSLTGGMPIKQAYYQCMIRNGINKGNIHKSKEFRYGLSYVLHHGKSDRKARPISAATRYSFYLAFGYTPDEQTALEGYYDSLELEWTESRLGIPARTPECLLLRLLPKIPLQPKSPTKPVQRTASKPDLPDSQWQQALAAPL", "text": "FUNCTION: RNA-dependent RNA polymerase that plays an essential role in the virus replication. SUBCELLULAR LOCATION: Host membrane. SIMILARITY: Belongs to the tombusviridae RNA polymerase family."}
{"protein": "MHLSSLSLSLTALAIVSPSAAYPHLGSSQPVLHTNSDTTQSRADAIKAAFSHAWDGYLQYAFPHDELHPVSNGYGDSRNGWGASAVDALSTAVIMRNATIVNQILDHVAKIDYSKTNTTVSLFETTIRYLGGMLSGYDLLKGPVSDLVQDSSKIDVLLTQSKNLGDVLKFAFDTPSGVPYNNLNITSGGNDGAKTNGLAVTGTLALEWTRLSDLTGDTTYADLSQKAESYLLNPQPKSAEPFPGLVGSNINISNGQFTDAQVSWNGGDDSYYEYLIKMYVYDPKRFGLYKDRWVAAAQSTMQHLASHPSTRPDLTFLASYNNGTLGLSSQHLTCFDGGSFLLGGTVLNRTDFINFGLDLVSGCHDTYNSTLTGIGPESFSWDTSDIPSSQQSLYEKAGFYITSGAYILRPEVIESFYYAWRATGQETYREWIWSAFSAVNDYCRTDSGFSGLTDVNAANGGSRYDNQESFLFAEVMKYSYMAFAEDAAWQVQPGSGNQFVFNTEAHPVRVSST", "text": "FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle lumen. SIMILARITY: Belongs to the glycosyl hydrolase 47 family."}
{"protein": "MNMEEQILNDYLLSQGRLQSIISLEQWRQLFPQRYREDPLIERLYEYCTQQRQKRLAKLRANIHLESQVIGKSRIDRMLATNVEKLQTVSHASTLHDVEEFYTSHSAKPLDISEINERLSEAVQSAYTKLNEEKERCTQLTLKMNSQIASLSDFQWSKEPNVDESIHLVESLIESLEKAAPSAIEELD", "text": "FUNCTION: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Note=Localized at the central region, but not at the outer repeats, of the centromere and remains at the centromere during mitosis and meiosis. SIMILARITY: Belongs to the NKP2 family."}
{"protein": "MAENLACGETSESWIIDNDDDDINYGGGFTNEIDYNHQLFAKDDNFGGNGSIPMMGSSSSSLSEDRIKEMLVREIEFCPGTDYVKRLLSGDLDLSVRNQALDWILKVCAHYHFGHLCICLSMNYLDRFLTSYELPKDKDWAAQLLAVSCLSLASKMEETDVPHIVDLQVEDPKFVFEAKTIKRMELLVVTTLNWRLQALTPFSFIDYFVDKISGHVSENLIYRSSRFILNTTKAIEFLDFRPSEIAAAAAVSVSISGETECIDEEKALSSLIYVKQERVKRCLNLMRSLTGEENVRGTSLSQEQARVAVRAVPASPVGVLEATCLSYRSEERTVESCTNSSQSSPDNNNNNNNSNKRRRKQ", "text": "FUNCTION: Acts on the G1 phase of the cell cycle to control cell division rate in both shoot and root meristems. The complex formed with CDKA-1 phosphorylates plant retinoblastoma protein. SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily."}
{"protein": "MALLSVIRRWHFREHLSIREICRRTGLSRNTIRKYLRAGGAEPKFNVPERPSKLDPFADRLSAWLKTESKKSRKQKRTMKQLHSDLVSLGYEGSYNRVAAFAREWRDDRQRELQTTGRGTFVPLAFEPGEAFQFDWSEDWAIIGNERTKLQVAHTKLSYSRAFIVRAYLLQTHEMLFDAHNHAFRVFGGIPGRGIYDNMRTAIDKVGRGKERDVNVRFMAMASHYVFEPEFCNPASGWEKGQVEKNVQDARHRFFQPVPRFPSLEALNDWLEQRCKEFWAKTPHGQMRGTIADIWVEEVPALMPASRPFDGFVEYTKRVTPTCLVHLERNRYSVPASLANRPVSLRVYPDRVVVAAEGQIVCEHRRVIDRSHDRPGQTIYDWRHYLAVVQRKPGALRNGAPFVELPDVFRTLQQYLLKKPGGDREMVDILALVLQHDEQAVLSAVDMALRSGVPTKTHVLNLLHRLVDGKSLTPPTLDAPQALTLTNEPKANVERYDTLRKTEVRHAS", "text": "FUNCTION: Required for the transposition of the insertion element. SIMILARITY: Belongs to the transposase IS21/IS408/IS1162 family."}
{"protein": "MTMDREKERELELESAMYTNCLLLGLDPNVIGLGASNGTPRVGLFRHSNPKLGEQLLYFILSSLRGPAQSSKDFDKVWPIFDSAQSRDFRKVVQAIISELESQGALPRSNSRVSSLATCCGPRFVELLWQLSLHALREVHRRTFPADVASNPLPSSLTDVSFSHAATLLPVTKARIVLERRRFLKNAETAVQRQAMWSNLAHEMTAEFRGLCAEEAYLQQELEKLNDLRNKVKQEGEVWDDLVSSSSQNSHLVSKATRLWDSIMARKGQHEVLASGPIEDLIAHREHRYRISGSALLAAMDQSSQVPRAELLSAHSDDSASLADDKELSDGSYTNMHDHSLVDSFETASSQASDETLSRVDDRGGKINQTVDVAEVIRRWTHALQRIHKQSLLLAKANDGDGPDILRTASDGGTSGHVESLAATLTEHQQHLASFQVLINQLKEVSPAIQKSISECTEMVNSLPPTLPPVTRSNGQASSLLQSQGSGRIMEGVSNDVAELTSTMSNVQLEKVSASPTLKLPQLFSSTPTSSGKGGNGQKRQTMASQVNKMESLSEKNSTDQALSNARPDNLPTDTSSSFVHNLKKSVREAALLIPSSAGSSRDSQSDEGSEHYFVPLSATGFSRFPSETKALPLRGSRALTSLSEPSFLEPNVPDSFAPSKYSDIPDTYDDLDSFKDYDNGNGFLSVAGSNSVASDAQQSFYDIDDQVFSPPLLMDSSLLSDAYEDLLAPLSETEAALMEH", "text": "FUNCTION: Contributes to the assembly of the acentrosomal spindle and phragmoplast microtubule arrays as part of the augmin complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, phragmoplast Note=Preferentially localizes to microtubules minus ends. SIMILARITY: Belongs to the HAUS6 family."}
{"protein": "MTVGTLSVVSSTASDTASHVSDTRKRQYQRDEALRKKIISELGKKSGNFESPVRKIRRNGEPGTVDSAALDPALTVHMQSLVTETAQLMAAKRQNCVLVVDDDEQLAGIVTATDIATRCVGAGLNARQTLIADIMSTSPLCITSDTRFDDALLLMIEHKFRHLPVVSDGGPDGSAGDEGDVIGIINMRACLREPLNRIARQQEAAQKLVEALEGAQEEIENKSVSGNTNSSSVSGNHAAEFLEYVESLKKKASGLEIMSLIDSSEEPFLVGTRTTVAEATESMARSGVSAVLVMDNGAVSGVFTAHDVVLRVLAAGLDPYRSSVIRVMTPHPDCALASLRVSTALERMIEGKFSNLPVVDESDAIIGMLSLFHLATAIEQTPEEEEEVFDQAENDAGIEPSNGFEDQQQQLLGNSNEVVENYDVNPPLPLNPLPSNTQQSESTYEYSARQLPKPPVQAWQNENLSSNNKPQEYVGVENDYNFSNNPPTAMSEQSFHPSVSQKPMDTPENGSNSFAASPYLQPYNSASQLAPSYVGSLPQYHGNPSFVEQALQDLVQPTDSASQIFPLNPQSPSQFTIKYRSIAGRVHRLRLDGINSVSDLRTAVEEREKEQLVTLTYIDDEGDVVELVSDSDLREAILLARRRGLPRLEVRGVAAFTNHLESSHPPISTVDSSIGSASVVEKGVANSIVDIHQPTAKADKGNSKKPIYIGIVSSSIVILAVSMWYLRRKR", "text": "FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Multi-pass membrane protein."}
{"protein": "MNSPDQIPFNTQLYTPPAQPITSTDYFSKKGNAPKLAVDVDLEPRTVPSFSHRHTEVTKYISPVDKLSPDVETPAEVGPANFIPNMSQYRFLLVDDNSINLKILTKILLRLYPRAHIVELCDSTSVLAYLASTPPFDCVFLDIEMPVVSGTELAYRIRQSPKLCRLPLIAVTTRTQEEDLAQYKDVGIDWTFGKPFNYPYRVVLDVVDNVLRQRINEL", "text": "FUNCTION: Required for stress adaptation, morphogenesis and virulence."}
{"protein": "MENSLGSYEKELNLKATELRLGLPGSDEPEKRATARSNKRSSPEASDEESISNGSDVTKEDNVVPPAKAQVVGWPPIRSYRKNNVQQKKEEESEGNGMYVKVSMAGAPYLRKIDLKVYKSYPELLKALENMFKCIFGEYSEREGYNGSEYAPTYEDKDGDWMLVGDVPWNMFVSSCKRLRIMKGSEAKGLGCF", "text": "FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin- responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Aux/IAA family."}
{"protein": "MGSKYPRSLRCCLPLWAFGLQVTFILLFYFLIGQDPIQADHKFMAIYQVIQDLTLVAALGFGFLSSSFRRHGWSSVAFSFFMLALGVQGTILLDYFLNWVLDWNMIKNPFSPFLSIQRATISTLPLLISAGAVLGKVNLVQLAVMVLVEAMTFGAIRVADKKVFRIEDHIIMMYGHVFGAYFGLTVAWWLSKSLPRRRHENAQTEKVQMTTSSSLFAMLGTLFLWIFWPSINSALLEGTKKKNAVFNTYYALAVSTVTATSMSALSHPKGKINMVHIHNAVLAGGVAVGAPSCLISSPWIAMVLGLTAGLISIWGAKCPQVCLSDLLLNPSGIHYTFGLPGLLGALTYYCLHIIAESRPSNLWIVTQTITDVGALSFAMAMGMVTGLLTGCLLSVKVWRAPHAVKYFDDQAFWEFPHLAVEF", "text": "FUNCTION: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily."}
{"protein": "MEPDDSQLSDILKDARIPDSQDIGVNLTQNLSFDTVQKMIDGVFTPIFSQGTEDSLEKDILKTPGISTIYNGILGNGEETKKRTPKISDAFEPDLNTSGDVFDSDKSEDGLMNDESYLSNTTLSQVVLDSQKYEYLRVRTEEEQQLVIEKRARERFIRKSMKIAEETALSYENDGSRELSETMTQKVTQMDFTETNVPFDGNDESSNLAVRVQSDMNLNEDCEKWMEIDVLKQKVAKSSDMAFAISSEHEKYLWTKMGCLVPIQVKWKLDKRHFNSNLSLRIRFVKYDKKENVEYAIRNPRSDVMKCRSHTEREQHFPFDSFFYIRNSEHEFSYSAEKGSTFTLIMYPGAVQANFDIIFMCQEKCLDLDDRRKTMCLAVFLDDENGNEILHAYIKQVRIVAYPRRDWKNFCEREDAKQKDFRFPELPAYKKASLESINIKQEVNLENMFNVTNTTAQMEPSTSYSSPSNSNNRKRFLNECDSPNNDYTMMHRTPPVTGYASRLHGCVPPIETEHENCQSPSMKRSRCTNYSFRTLTLSTAEYTKVVEFLAREAKVPRYTWVPTQVVSHILPTEGLERFLTAIKAGHDSVLFNANGIYTMGDMIREFEKHNDIFERIGIDSSKLSKYYEAFLSFYRIQEAMKLPK", "text": "FUNCTION: Transcriptional activator that binds the same DNA consensus sequence as p53 (PubMed:11696333, PubMed:15242600, PubMed:28560849). Has a role in normal development to ensure proper meiotic chromosome segregation (PubMed:11557844, PubMed:12445383). Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation (PubMed:11696333, PubMed:11557844, PubMed:12445383, PubMed:15273685, PubMed:17186023, PubMed:18836529, PubMed:21901106). Regulates germline apoptosis in response to DNA damage (PubMed:11696333, PubMed:15273685, PubMed:15707894, PubMed:16319925, PubMed:17276923, PubMed:17186023, PubMed:17347667, PubMed:19015549, PubMed:26598553). Its pro-apoptotic activity is inhibited when bound to ape-1 in vitro (PubMed:12524540). Plays a role in cell cycle arrest in the germline in response to DNA damage by UV-C light (PubMed:17347667). However, not required for survival in response to DNA damage induced by UV-C light, indicating that it is unlikely to be involved in DNA repair (PubMed:17347667). Required for induction of ced-13 in response to DNA damage (PubMed:15605074). Regulates DNA damage-induced apoptosis by inducing transcription of the programmed cell death activator egl-1 (PubMed:12445383, PubMed:19521535). Regulates germline proliferation by activating phg-1 (PubMed:17186023). Modulates lifespan (PubMed:17895432, PubMed:18836529, PubMed:28560849). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the p53 family."}
{"protein": "MNTPDPWSSPEVQFCFAAANSSCPRKARPALVVCAMYLIMIGAIVMTMLGNMAVIISIAHFKQLHSPTNFLILSMATTDFLLSCVVMPFSMIRSIESCWYFGDLFCKVHSCCDIMLCTTSIFHLCFISVDRHYAVCDPLHYVTQITTRVVGVFLLISWSVPIFFAFGLVFSELNLIGAEDFVAAIDCTGLCVLIFNKLWGVLASFIAFFLPGTVMVGIYIHIFTVAQKHARQIGTGPRTKQALSESKMKATSKKESKATKTLSIVMGVFVLCWLPFFVLTITDPFIDFTTPEDLYNVFLWLGYFNSTFNPIIYGMFYPWFRKALRMIVTGTIFRSDSSTSSLHPAHP", "text": "FUNCTION: Olfactory receptor specific for 2-phenylethylamine, a trace amine present at high concentration in the urine of carnivore species, playing a key role in fear and avoidance responses. 2-phenylethylamine acts as a kairomone in the chemical detection of carnivore odor and triggers fear in mice. This receptor is probably mediated by the G(s)- class of G-proteins which activate adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSLQADFDKAAKDVRKLKTRPDDEELKELYGLYKQSVIGDIDIECPALLDLKGKAKWEAWNLQKGLSKEDAMNAYISKAKELIEKYGI", "text": "FUNCTION: Binds medium- and long-chain acyl-CoA esters. SIMILARITY: Belongs to the ACBD7 family."}
{"protein": "GFGCPNDYPCHRHCKSIPGRXGGYCGGXHRLRCTCYR", "text": "FUNCTION: Has antibacterial activity against M.luteus and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the invertebrate defensin family. Type 2 subfamily."}
{"protein": "MKVHEFSNGFSSSWDQHDSTSSLSLSCKRLRPLAPKLSGSPPSPPSSSSGVTSATFDLKNFIRPDQTGPTKFEHKRDPPHQLETHPGGTRWNPTQEQIGILEMLYKGGMRTPNAQQIEHITLQLGKYGKIEGKNVFYWFQNHKARERQKQKRNNLISLSCQSSFTTTGVFNPSVTMKTRTSSSLDIMREPMVEKEELVEENEYKRTCRSWGFENLEIENRRNKNSSTMATTFNKIIDNVTLELFPLHPEGR", "text": "FUNCTION: Promotes differentiation and/or maintenance of the vascular procambium, the initial cells of the developing vasculature (PubMed:20044450). Part of the TDIF-TDR-WOX4 signaling pathway that plays a crucial role in the maintenance of the vascular meristem organization during secondary growth (PubMed:20729381). Is required for promoting the proliferation of procambial/cambial stem cells but not for repressing their commitment to xylem differentiation in response to the TDIF signal (PubMed:20729381). Acts redundantly with WOX14 downstream of the TDR/PXY receptor kinase to regulate procambial cell proliferation and differentiation in vascular tissue, independently of any role in vascular (PubMed:23578929). Acts as a cambium regulator in the inflorescence stem (PubMed:21926336). Is required for auxin- dependent cambium stimulation in the inflorescence stem (PubMed:21926336). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family."}
{"protein": "MGKPTLLEPGHLYNVPAEHKNDVPIHYIITWIKQRLPEFGGAIPTSLADRVLIIKSRTGSGKSTALPVHVFRILRNENTHSFQKYLGRSVICTQPRVLTAVTLAKDIGASTHYPDMILGQTVGYQTKPLTEKPNRGLIYATAGVLLAQLHTMTDDEIASRYAFMIIDEAHERALGIDLMLMYIKSMLERMLQRGSIGALRIPFVILTSATIDTHKYSTYFGIGKENIILVEGRQYGVETHWPLYNTNNYIKTACETALTIHKENIHDRPTEADILIFMPGMAEIRFLSMLLNNANMDLAKEKLPLMLILPIDSEAIAQENEAYLGLKAEIKNLWVKNPLTAKVEKPLRRVIVSTVVAETGLTIETLKYVIDPGWNRSIETYYPEWAGGLITRPAAQSRIEQRKGRVGRVFPGHFYPLYTKHVFEQIPAQQYPEIITEGPGAIFLSIVVETIKKNKEGVFKAEEIDMLDPPPTDALASAIERAIVAGLLTRGEKGLQLTQLGDIASRFSFLSIEEARMCFSGYFWQAAISDIATILAVVSVADKKLTNLLDSKQRNGAMLAEAVLAGIPPFLQNIDNAYTNIHLLLADDLLEGLFIFEGFQHAIVYFINNKVNNVAKHLREWCEKKMLKYSSMVQILARREDILNELAIVGLNPFHHWQNRLASANAETFLKRVCTLKQCMYEAYRLNCFCYDEHRLLYTGRNGIHFSYHDAVIKNPSCIVTPRIMLSPVSKQYMEWRLEPSFVSVLDGFVNVDINFLLPRQEIPNILGGVEDEEEEPPLPIQVFLHKYVKTHFHFSGKSFKELKMKPGQTIKFPETTLINMIPDIPKNVVQTYLEISVCHQYSFKRLIYCETFYTDMDDVQHENSVELIGLPMAAHHLTINDFNKLYHLLKPDGFLMVYDLHQSQEAFWLHSLQDALGHHTIRRDMDFHTIPEWETIFKECGFTPIFSKQPSEHELFIVFKK", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein Virion. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily."}
{"protein": "MNKNVMIKGLTALTILTSLGFAENISDQPHSIAKAEKNIKEVTDATKAPYNSVVAFAGGTGVVVGKNTIVTNKHIAKSNDIFKNRVSAHHSSKGKGGGNYDVKDIVEYPGKEDLAIVHVHETSTEGLNFNKNVSYTKFAEGAKMKDRISVIGYPKGAQTKYKMFESTGTINHINGTFMEFDAYAQPGNSGSPVLNSKNELVGILYAGSGKDESEKNFGVYFTPQLKEFIQNNIEK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1B family."}
{"protein": "MAIILPELPYAYDALEPYIDAETMHLHHDKHHQTYVNNANAALEKHPEIGEDLEALLADVESIPADIRQALINNGGGHLNHALFWELMTPEKTAPSAELAAAIDATFGSFEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGKKPILGLDVWEHAYYVKYRNVRPDYIKAFFSVINWNKVDELYAAAK", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a critical role against oxidative stress, affecting both the survival and the virulence of S.pneumoniae. FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a critical role against oxidative stress, affecting both the survival and the virulence of S.pneumoniae (By similarity). SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MSRRRHSDENDGGQPHKRRRTSEPLEIEDRLESLICRVGEKSTSSLESNLEGLAGVLEADLPNYKNKILRILCFVARLLPEKMTVYTTLVGLLNARNYNFGGEFVEAMIRHLKETIKLNAYNEAIYLVRFLCDLVNCHVIAAPSMVAMFESFVGVTQEEDIPQVRSDWYVYAVLSSLPWVGKELYEKKDVEMDQILSQIEAYLKQRQKLHLSILQVWSAEKPHPQEEYLDCLWAQVQKLKKDRWQERHIQRPYLAFDSVLCEALQHNLPPFTPPPHTEDSVYPVPRVIFRMFDYTDAPEGPVMPGSHSVERFVIEENLHCILKSHWRERKTCAAQLLSYPEKNKIPLNYHIVEVIFGELFQLPSPPQIDVMYTTLLIELCKLQPGSLPQVLAQASEMLYTRLDTMNTTCIDRFINWFSHHLSNFQFRWNWEDWADCLSQDLDKPKPQFVREVLEKCMRLSYHQRILDIVPATFSALYPANPSNVIKYGDESNSALPGYSVAVILTNAIKNKASDKEIFNILKDIPNPNQDDYDDEGIGFNPLKIEVFVQTLLNLASKSFSHSFSALAKFHDIFKALSESDEGKLHILRVVYDVWKNHPQMIAVLLDKMIRTQIVDCAAVANWIFSPELSPDFTRFYIWEILHSTIRKMNKHVQKIQKELEDTKQRLAKQHKHRDSDDNDEDSGRKDGPLEEQIERLQEKVESAQSEQKNLFLVIFQRFIMILTEHLVRCETGGIDVNTAWYKNCRERLQQIFLQHHQTIQQYMVTLENLLFTAELDHHILTVFQQFCALQS", "text": "FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC), promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of parn, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the NCBP1 family."}
{"protein": "MQHLKNIKSGNPKTKEQYQLTKNFDVIWLWSEDGKNWYEEVKNFQPDTIKIVYDENNIIVAITRDASTLNPEGFSVVEVPDITSNRRADDSGKWMFKDGAVVKRIYTADEQQQQAESQKAALLSEAENVIQPLERAVRLNMATDEERARLESWERYSVLVSRVDPANPEWPEMPQ", "text": "FUNCTION: Acts catalytically in the formation of tail protein dimers. SIMILARITY: Belongs to the tfa family."}
{"protein": "MGRFLLVTLSLLVMAFFLNGANSCCCPQDWLPRNGFCYKVFNDLKTWDDAEMYCRKFKPGCHLASLHSNADAVEFSEYITDYLTGQGHVWIGLRDTKKKYIWEWTDRSRTDFLPWRKDQPDHFNNEEFCVEIVNFTGYLQWNDDSCTALRPFLCQCKY", "text": "FUNCTION: Galactose-binding lectin that binds to and agglutinates erythrocytes in a calcium-dependent manner. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the true venom lectin family."}
{"protein": "MAKQYDMVECPFCDEVSKYEKLAKIGQGTFGEVFKAKHRQTGKKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNTHVKFTLSEIKKVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGGGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVWPNVDKYELYQKLELPKGQKRKVKDRLKAYVKDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKNMLSTHNQSMFEYLAPPRRRGGHMPQQPANQGRNPAATNQTEFDRVF", "text": "FUNCTION: Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P- TEFb), which facilitates the transition from abortive to production elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II), SUPT5H and RDBP. The CDK9/cyclin-K complex has also a kinase activity toward CTD of RNAP II and can substitute for P-TEFb in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MTQAVLGIIGGSGIYDLPGLEGAHEEVIKSPWGEPSAPLRRGTIAGLPIVFLPRHDKGHRLSPSDINYRANIDVLKRAGVTDLISLSACGSFKEEMPPGTFVLVDQFVDRTHKRESSFFGRGCVAHVSMAHPVSPRLRIHLAAAAEAEGIAIARGGTYVCMEGPQFSTYAESMTYKTSGYSVIGMTNMPEAKLAREAEICYATVAMVTDFDCWHPDHDAVTVQDIIRVLTSNADKAKALVARLAKDFPREHEPCPIGSDRALDTALITAPEARDPELLKKLDAVAGRVLRG", "text": "FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily."}
{"protein": "MAFTCSDIFKIIIAIILPPLGVFLERGCASSFWINIVLTILGYIPGIIHALYVILKY", "text": "FUNCTION: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0057 (PMP3) family."}
{"protein": "MKSALSVVVAAAGVQQASATFGLLGGGGISFNFGLDWSGAKTFPCPGNVVNKCTPEQENGWDWSDVATGSLNTYAGFNFGGGWSCESNFGKRGDIQGRTFGLGKVISGSCDQGDEAGLSIGVGASAGIDAFSIDSFDMSTEFDARLEFHYDMPDGSVCKQTSDCKRGGSTIVNKQCGGAKKVRVIYPKQIIHKGISFSKKCKISCHKIKWHCGKPTPKPSTSVLTLPSTSTKVIQTTPVTTLQTYTTPSQQTTTPEKETTSSKETTTSAQQTTPGKETTPAQQTTPSKETTPVQQTTSGKETTPAQQTTPGKETTSSQETTSAHQTTPGKETTPAQQTTPGKETTPAQQTTPGKETTPAQQTTPGKETTPAQQTTPGQQTTPSQPTTAATTTPATTFVTTYDTTSTVYTTSTKTITSCGPEVTDCPGKTGPHIVTVTIPVSTTICPVTETRTQSQGVPTTVILPSKSETTVKEQPTPEQPTPEQPTGEKPNPVTSQPPQSTQTPPCPPVVPRCLNTFVDLKAKCADNKDASCFCPDKDFVKNIFDCIYAHGESDNIISEAISFFQGICGRYIPENPVIATGAETITQIITVTGTPHITQVPYTTVVVATTITENSSTQTISTEVTIPNIVMPTPTGGVPNQPPATASVPAGQNPPPVTGQNPPPAVTDQSPPPAITTGTGGVIPPKPTGSVPVTAGSGRVGAGLGMVLAVAAFVAAL", "text": "FUNCTION: Cell surface adhesion protein that plays a key role in virulence by allowing adherence to the insect host surface (PubMed:17337634). Required to orientate the cytoskeleton and stimulate the expression of genes involved in the cell cycle (PubMed:17337634). Is also involved in achieving the septin hourglass shape and subsequent separation of cells (PubMed:17337634). SUBCELLULAR LOCATION: Secreted, cell wall Cell membrane; Lipid-anchor, GPI-anchor Note=Found anchored in the cell membrane as well as a covalently-linked GPI-modified cell wall protein (GPI-CWP) (By similarity). Heterogeneously and randomly distributed within the cell wall structure (PubMed:17337634). SIMILARITY: Belongs to the RBT5 family."}
{"protein": "MPDLLLLGLIGALTLLLLLTLLAFAGYSGLLTGVTVSAGSPPIRNITVAYKFHVGSYGDTGHLFTESCSISPKLRSIAVYYDNPHTVPPEKCRCAVGSILSEGEESPSPELIHLYQKFGFKIFSFPAPSHVVIATFPYTTPISIWLAARRVHPALDTYIKERKLCAHPRLEIYHQDKIHFMCPLARQGDFYVPEVKETERKCRELAEATDTQTDGTGADTSDASSVSLDVRPGSRETSATTLSPGAGNRGWDDGDNRSEHSYSESGASGSSFEELDLEGEGPLGEPRLNPEAKLLGPPRELSTPERGEE", "text": "FUNCTION: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins. Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein Cytoplasmic vesicle, autophagosome Cytoplasm, cytosol Nucleus Chromosome Note=Is trafficked from tubular ER to growing autophagosomes via its cytosolic LIR motif. Also found in the cytosol, nucleus and chromatin. In response to formation of covalent DNA-protein cross-links (DPCs), localizes to the nuclear periphery, and associates with DNA replication forks."}
{"protein": "MGETLGDSLIDPESDSFADTLSASTSQETTMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISTPHYEDIPFSRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY", "text": "FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily."}
{"protein": "MSFSQDMDNEYEKLIRRMNPPRVVIDNDSCKKATVIRVDSANEYGILLEVVQILTDLNLTITKAYISSDGGWFMDVFNVTDQDGNKVTDEVVLDYIQKSLGPEACFSTSMRSVGVIPSTDSTVIELTGCDRPGLLSELSAVLTHLKCSVLNAEIWTHNTRAAAVMQVTDDLTGCGISDPERLSRIKNLLRNVLKGSNTPREAKTVVSHGEVHTDRRLHQMMFEDRDYEHRLVDDDSSIQDERQRPDVCVDNWLDKDYSVVTVRCKDRPKLLFDTVCTLTDMQYVVFHGSVDTEGTEAFQEYYVRHIDGSPVKSEAEKQRVIQCLEAAIKRRVSEGLKLELCTTDRVGLLSNVTRIFRENSLTVTRAEVKTKGGKALNTFYVSDASGYSIDAKTIDSIRQTIGQTILKVKNNPQEQQQRQKSPSHESPTRFLFGGLFKSKSFVNFGLVRSYS", "text": "FUNCTION: May bind amino acids."}
{"protein": "MSTRTKALNAYRHGLRATRIAFRNDAEVLLAARAKMRSGMLCPPDPKLTTEDQIQHLEDVAVFLRRNLVQGKKVDGSSTKEPRYHLNIHKDTELGDNETIADPTARVKTNLKARPFKCSDKKQ", "text": "FUNCTION: Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool (By similarity). FUNCTION: Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family. MZM1 subfamily."}
{"protein": "MVRVLRGLPWRGLWLLLAHQLFLVTACQDAHYGTLMQELCLSRFQKDMEAMERTLWCDWGKTIGSYGELTDCTRNLAERLGCFWPNVEVDRFFVAVHRHYFRSCPASGRALGDPPSTILCPFVVLPITVTLLVTALVVWRSKRAESIV", "text": "FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the RAMP family."}
{"protein": "MDLKAQSIPFAWLDRDKVQRLTNFLSNLENLENVDLREHPYVTNSCVVREGEDVDELKTLYNTFILWLMYHYVLSKRKPDYNAIWQDITKLQNVVNEYLKSKGLNKGNFENMFTNKEKFESQFSDIHRALLRLGNSIRWGSNVPIDTPYVNLTAEDSSEIENNLQDAEKNMLWYTVYNINDPWDENGYLVTSINKLVYLGKLFVTLNQSWSKLEKVAMSQIVTTQNHLSGHLRKNENFNAVYSQRVLQTPLTGQRVESFLKIITSDYEIIKSSLESYSASKAFSVPENGPHSLMDFASLDGRMPSDLSLPSISIDTKRPSADLARLKISQPKSLDAPLKTQRRHKFPESDSVDNAGGKILIKKETLGGRDVRATTPVSSVSLMSGVEPLSSLTSTNLDLRDKSHGNYRIGPSGILDFGVKLPAEAQSNTGDVDLLQDKTSIRSPSSGITDVVNGLANLNLRQNKSDVSRPWSKNTAANADVFDPVHRLVSEQTGTPFVLNNSDVAGSEAKLTTHSTETGVSPHNVSLIKDLRDKDGFRKQKKLDLLGSWTKEKNDKAIVHSREVTGDSGDATETVTARDSPVLRKTKHANDIFAGLNKKYARDVSRGGKGNSRDLYSGGNAEKKETSGKFNVDKEMTQNEQEPLPNLMEAARNAGEEQYVQAGLGQRVNKILAEFTNLISLGEKGIQDILHNQSGTELKLPTENKLGRESEEANVERILEVSDPQNLFKNFKLQNDLDSVQSPFRLPNADLSRDLDSVSFKDALDVKLPGNGEREIDLALQKVKAGERETSDFKVGQDETLIPTQLMKVETPEEKDDVIEKMVLRIRQDGETDEETVPGPGVAESLGIAAKDKSVIAS", "text": "SUBCELLULAR LOCATION: Virion tegument Note=Also found in dense bodies. SIMILARITY: Belongs to the herpesviridae large structural phosphoprotein family."}
{"protein": "MLRSCAARLRTLGALCLPPVGRRLPGSEPRPELRSFSSEEVILKDCSVPNPSWNKDLRLLFDQFMKKCEDGSWKRLPSYKRTPTEWIQDFKTHFLDPKLMKEEQMSQAQLFTRSFDDGLGFEYVMFYNDIEKRMVCLFQGGPYLEGPPGFIHGGAIATMIDATVGMCAMMAGGIVMTANLNINYKRPIPLCSVVMINSQLDKVEGRKFFVSCNVQSVDEKTLYSEATSLFIKLNPAKSLT", "text": "FUNCTION: Has acyl-CoA thioesterase activity towards medium and long- chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane. SUBCELLULAR LOCATION: Cell membrane Cell projection, ruffle membrane Cytoplasm Mitochondrion Mitochondrion inner membrane; Peripheral membrane protein Mitochondrion intermembrane space Note=Released from the mitochondria into the cytosol in response to apoptotic stimuli. SIMILARITY: Belongs to the THEM4/THEM5 thioesterase family."}
{"protein": "MQGMALNQLLACLKWLGEFQVLACIPLKGSIHARDVADLTGVPETQLCRVVRLMATAGFLHEPRPGQIAHTVLSGAFVTDLSLLDAGMFLSETAAPVALHMATATERQSDLQASNSAYSVAFNTSQPFEAACVERSRLHRQWSAYSRCAGDAEDKTVELFGQLNWRSLGSATIVDSCAQSTDLVLELAKLYPSLHFVVQMNNAAAVQQEACRRPESEDVKRRMKIQERMPSAPQTVKDAAVYILRLPATLRPSAVQILAELRAHLGALRANSSATLILATPLLPEPGTLDPDSEARARVRDLARLQLTNETDLELSELIELVNGVHDSNGRFRVVSKLRSRDSAATAALGIKYQAVPTAP", "text": "FUNCTION: Transcriptional coactivator; part of the gene cluster that mediates the biosynthesis of an emodin derivative that may be involved in black Sigatoka disease of banana (PubMed:30735556). With MYCFIDRAFT_198930, coregulates the production of the PKS8-1 cluster product (Probable). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MIPRIMSTQHPDNYSIPFFASSPILEGEDEITEAFYAFSVLGADEQMWDFEGKEVDEFVVKKLLERYPTFFKNNILGKDIRLTPRVPNPSVEKEEAKLLLETLQGIARSADYARIFYGDNIAPIFEVILPMTTSVEEIERVYWLYKKAVVWISREKIYDITVREWIGDFFPEKINVIPLFETKSALIKAAKITEAYILNRKNDIEYQRVFFARSDPAMNYGLITAVTYVKRALYEVLKVEEELSIPIYPIIGVGGPPLRGGMRPDNVDAVVKEYPSVQTFTIQSSFKYDYPTKDVVKAVEKIKSTKRKLPIPVEIPPFLVNYEAEYQKQIRILAPYINSVAKRIPRRRKRKLHIGLFGYSRNVNGITLPRAITFTAALYSIGIPPELLALNSLTDSQLETISEYYINVYEDLEFAMRFFSPKVAEKVGLKELAERVKEFKPEQIPEYIEEAEIVFKGEGDVMKLAQLRGFLG", "text": "FUNCTION: Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. SIMILARITY: Belongs to the PEPCase type 2 family."}
{"protein": "MTHDHAHSRGVPAMIKEIFAPHSHDAADSVDDTLESTAAGIRTVKISLLVLGLTALIQIVIVVMSGSVALAADTIHNFADALTAVPLWIAFALGAKPATRRYTYGFGRVEDLAGSFVVAMITMSAIIAGYEAIARLIHPQQIEHVGWVALAGLVGFIGNEWVALYRIRVGHRIGSAALIADGLHARTDGFTSLAVLCSAGGVALGFPLADPIVGLLITAAILAVLRTAARDVFRRLLDGVDPAMVDAAEQALAARPGVQAVRSVRMRWIGHRLHADAELDVDPALDLAQAHRIAHDAEHELTHTVPKLTTALIHAYPAEHGSSIPDRGRTVE", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family."}
{"protein": "RRRRSQGSEVNLTGQGQPCHSCGERCPGFLAHKWRKICQHCQCPWEEHGHTASNQDLERSLCRLVSGSQRDSLCDSSSDSSVEKYAWVPSGLNPVQVHHFFKCFPEKKIPYINSPGEKYRLKQLLHQLPPHDSEARYCCSLQGEEEEELLLLFSQKRRLENLGRGCVRPISGTMSGTVCQQCGHQINVGEVAVFASRAGLGFCWHPQCFTCAQCLELLCDLIYFYQDGKVYCGRHHAELKRPRCLACDEVIFSLECTQAEGFHWHTRHFCCFECECPLGGQRYIMKDQRPFCCSCYERLYAQYCDSCGECIGIDEGQLTYGGQHWHASESCFCCGRCGECLLGRPFLPRHGQIYCSRSCSMLHTKSERPFSPSQMDLSFQKETKDVGTSTNHELEGDSITNCTLAGSRTSLSVIDQTPTQAAPARSLHSSLRGAPKGFSRECPNRRSLPDLSSHTRTPTRVTFQLPSHSEIKESISFSRPSFTSSSSSDEEEGYFLGEPIPLPPFLRSPGYTAPPTHVPTSTRKQKKKKDKSCFLS", "text": "FUNCTION: Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity). PCP is maintained by two molecular modules, the global and the core modules (PubMed:23140624). Proteins of the core module include the proteins Frizzled (Fz), Disheveled (Dsh), Van Gogh (Vang), Prickle (Pk), Flamingo (Fmi, Celsr) and Diego (Dgo) (PubMed:23140624). The core module proteins develop subcellular asymmetry, accumulating in two groups on opposite sides of epithelial cells (PubMed:23140624). Distinct proximal (Vang, Pk and Fmi) and distal (Fz, Dsh, Dgo and Fmi) complexes segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (PubMed:23140624). Directional information to orient polarization with respect to the tissue axes is provided by the global module which involves Wnt proteins (PubMed:23140624). Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). Required for proper assembly, stability, and function of mitochondrial membrane ATP synthase (mitochondrial complex V) (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion Note=Recruited by vangl2 to anterior cell borders. This polarity is controlled by wnt proteins (By similarity). Wtip is involved in the recruitment of prickle3 to the basal body (By similarity). SIMILARITY: Belongs to the prickle / espinas / testin family."}
{"protein": "MEFPKNLRYSEEHEWVRVEGNKAYIGITSFAQAELGDIVFVELPEVGATIQQDEPFGSVESVKTVSELYAPVTGKVVEVNGELEDAPELVNSSPYEQAWMIVVELSDTAELDKLMDADKYEAMVKE", "text": "FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. FUNCTION: Is also involved in protein lipoylation via its role as an octanoyl/lipoyl carrier protein intermediate. SIMILARITY: Belongs to the GcvH family."}
{"protein": "MEYNTILNNTSKTRVCYFFDQDVGNYFYGPYHPMKPHRLCLTNNLVLNYGLHKKMHLYKARPADAEDMLKFHSEDYVDFLERVTPENINEWKDVKRFHIGEDCPVFPGLYDYCSIYSGGSIEGALKLNHRMYDIAINWSGGLHHARKDEASGFCYVNDIVLAILELLKFHARVLYIDIDVHHGDGVQEAFYLTDRVMTVSFHKFGGDFFPGTGDIDEIGAKTGKLYSVNVPLADGIDDKNYLNIFKPVIQGVMDYYRPSVIVLQCGADSLRFDRLGCFNLTIKGHAECVRFVKSFNIPTLVLGGGGYTVRNVARCWTYETSVCVDTEVNNELPYNDYIQFYSPDFQLIPDYTGLPFKYENANTKSYLESLRIKILENLRILQWAPSVQIQDVPPDIMPIDFDRDEDSKENMDKRKKKHNDFS", "text": "FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). May play a role in the regulation of the timing of gene expression during the development and in the definition aspects of the phenotype that mediate social behavior in genetically heterogeneous groups. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily."}
{"protein": "MNRFSTRLMGATATPPPAPPKARSNENLDKIDMSLDDIIKLNRKEGKKQNFPRLNRRLQQSSARQFRMRVRWGIQQNSGFGKNSLSRRGRVMPGKRRPYGVITGLAARKATGIRKGISPMNRPPLSDKNIERYFPALKRKANLLRQNEVQRKPVAALKRPNQLNRKNNIPNNFTRSGNKLSHQKDTRQATFLFRRGLKVQAQLNSEQLLDDVVAKRTRQWRTSTTNGGILTVSIDNPGAVQCPVTQKPRLTRTAVPSFLTKRDQSDIKKVPKGVPLQFDINSVGKQTGMTLNERFGILKEQRATLTFNKGGSRFVTVG", "text": "FUNCTION: Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus speckle. SIMILARITY: Belongs to the UIF family."}
{"protein": "MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM", "text": "FUNCTION: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (Probable). The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans- signaling'. Alternatively, 'cluster signaling' occurs when membrane- bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable). FUNCTION: IL6 is a potent inducer of the acute phase response. Rapid production of IL6 contributes to host defense during infection and tissue injury, but excessive IL6 synthesis is involved in disease pathology. In the innate immune response, is synthesized by myeloid cells, such as macrophages and dendritic cells, upon recognition of pathogens through toll-like receptors (TLRs) at the site of infection or tissue injury (Probable). In the adaptive immune response, is required for the differentiation of B cells into immunoglobulin- secreting cells. Plays a major role in the differentiation of CD4(+) T cell subsets. Essential factor for the development of T follicular helper (Tfh) cells that are required for the induction of germinal- center formation. Required to drive naive CD4(+) T cells to the Th17 lineage. Also required for proliferation of myeloma cells and the survival of plasmablast cells (By similarity). FUNCTION: Acts as an essential factor in bone homeostasis and on vessels directly or indirectly by induction of VEGF, resulting in increased angiogenesis activity and vascular permeability (PubMed:17075861, PubMed:12794819). Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF (PubMed:12794819). Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance (PubMed:20823453). 'Trans-signaling' in central nervous system also regulates energy and glucose homeostasis (By similarity). Mediates, through GLP-1, crosstalk between insulin- sensitive tissues, intestinal L cells and pancreatic islets to adapt to changes in insulin demand (By similarity). Also acts as a myokine (Probable). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (By similarity). Also has a pivotal role in iron metabolism by regulating HAMP/hepcidin expression upon inflammation or bacterial infection (PubMed:15124018). Through activation of IL6ST-YAP-NOTCH pathway, induces inflammation-induced epithelial regeneration (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily."}
{"protein": "MPQLAGKLILAGLIPLGAWVLHGFASCNGLIQMFEDFGKQTVLSDGVTDYTGAFTGLEGLDRLLRTLLNFFWPVANGHDWALSLHAFMFAGQGVPLLVLNMLEGARPGNKSLVVSYVTVFGILYMVVGLAIMAPLYLFLHLLTSRTATAPSKAKVAVDPNTAKAVGFGVFVGYVLPTIFMSLPHPSLLSTDTKVLSVVFWQAVPLWASVCAYFASTALGQSATSRSSSNLPSALGAVYAASLIIATATHVATFAISANLSDTWSGIFTFLIPPNPFNTDMRISSFLEGATWFLQWDYTMMSLAYMVWAIGIRHGVEVPRSSHHFETLGKIALRSMAKLLVMGPIGAALSLVWERDQLLWQLDSESGEKGEKNRSRRMSRKWMFS", "text": "FUNCTION: Epoxide hydrolase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis (PubMed:30952781, PubMed:35418536). The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781). On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781). Finally, ascofuranol is oxidized into ascofuranone by ascJ (PubMed:30952781, PubMed:35418536). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family."}
{"protein": "MLEHLSSLPTQMDYKGQKLAEQMFQGIILFSAIVGFIYGYVAEQFGWTVYIVMAGFAFSCLLTLPPWPIYRRHPLKWLPVQDSGTEDKKPGERKIKRHAKNN", "text": "FUNCTION: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Dispensable for SPC enzymatic activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SPCS1 family."}
{"protein": "MASFISDFGLIWYLRELNKKEFMKFKDFLIQEILELKLKQVSSTKVKKASREDLANLLLKCGENQAWDMTFRILQKINRKDLTERATGAIVGNPNLYRDHLKKKLTHDCPKKFNVRIQDFIKETFIQNDXDAFENLLISKGTERKPHMVFLKGMAGVGKTLMLKNLMLAWSKGLVFQNKFSYAFYFCCQDVKQLKTASLAELISREWPSPSAPIEEILSQPEKLLFIIDSLEGMEWDLTKQESELCDDCMEKQPVSTLLSSLLRRKMLPESSLLLSTTPETFEKMEDRIQCTDVKTATAFDERSMKIYFHRLFQDRKRAQEAFSLVRENKQLFTICQVPLLCWMVATCLKEEIEKGGDPVSLCRRTTSLYTTHIFSLFIPQSAQYPSKKSQDQLQGLCSLAAEGMWTDTFVFGKEALRRNGIFDSDIPTLLDIGMLGKIREFENSYIFLHPSVQEVCAAIFYMLKRHVEHPSQDVKNIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLGVFFGHRLSKNIHHKLYQCLETLSGNAELQEQIDGMRLFSCLFEMEDEAFLVKAMNCMQQINFVAKNYSDFIVAAYCLKHCSTLKKLSFSTENVLNEGDQSYMEELLICWNNMCSVFVRSKDIQELRIKDTNFNEPAIRVLYESLKYPSFTLNKLVANNVSFGDNHVLFELIQNSSLQYLDLSCSFLSHNEVKLLCDILNQAECNIEKLMIAHCKLSPDDCKIFGSILMSSKSLKVLNLASNNLNQGISSLCKALCHPHCTLEYLVPRSNHCIVNFLLKLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTGVMLLCDAIKHPNCHLKDLQLEACEITDASNEELCYAFMQCETLQTLNLMGNAFEVSRMVFFPRKSELMLFIFLHLSRLWITDFDNEFQAFLLSVKKKNHFLTIRGSVEADGEKKGGDSDARTMGELSNEI", "text": "FUNCTION: Required for cytoplasmic lattice formation, thereby modulates the distribution of organelles during oocyte maturation and zygote development (PubMed:31575650). Required for preimplantation development in female fertility (PubMed:31575650). May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Expressed and colocalizes with NLRP5 at the oocyte subcortex. SIMILARITY: Belongs to the NLRP family."}
{"protein": "MALDILAVAPLYQGPDINKIRLMAETTKKSTTPPKPLTPSRTKLTTIETKRIMSVLDETIHKVELVTLLSNVASSSQSLEGMLGEDIMKAVREHVDLCQTLLDHVNYLQEEEQRLQEEEGFEDEPWFRDLVFSIELQKSRLPPLRQQIRESTKNVLRLLLRNPQAASLLQVQSLGRSEEAQSFIDSLVELRGFLFEKLLTSPMEARDKTQFIQDITRRNRRNQEIIDTLENELAACMRNRDAEVEKENFVVQELKNHLHQVLKFSENSLLRTKQEAEKQQKADFRASQARVAKIQQEILLLRSQFHNLVMENREAEQALRKKKYKVETEIENWIQKYDLEMSEKQDEYEELDIIHKEEKLQLEELKQRHSVLVEEFSQIQAEREIKAKERLEAEQEMVRMVRAATLIQALWKGYLVRSMLRSKKKKRNKGKVKDKEKGKGKEKGKGKGKEKGKGKEKGKGKKGKGKK", "text": "FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the DRC10 family."}
{"protein": "MDLGKTVEYGTHRQDAIAQIDVPDQVLYTIGSFILIIGSVGIIGNMLVLYAFYRNKKLRTAPNYFIINLAISDFLMSATQAPVCFLSSLHREWILGDIGCNVYAFCGALFGITSMMTLLAISINRYIVITKPLQSIQWSSKKRTSQIIVLVWMYSLMWSLAPLLGWSSYVPEGLRISCTWDYVTSTMSNRSYTMMLCCCVFFIPLIVISHCYLFMFLAIRSTGRNVQKLGSYGRQSFLSQSMKNEWKMAKIAFVIIIVFVLSWSPYACVTLIAWAGHGKSLTPYSKTVPAVIAKASAIYNPIIYGIIHPKYRETIHKTVPCLRFLIREPKKDIFESSVRGSIYGRQSASRKKNSFISTVSTAETVSSHIWDNTPNGHWDRKSLSQTMSNLCSPLLQDPNSSHTLEQTLTWPDDPSPKEILLPSSLKSVTYPIGLESIVKDEHTNNSCVRNHRVDKSGGLDWIINATLPRIVIIPTSESNISETKEEHDNNSEEKSKRTEEEEDFFNFHVDTSLLNLEGLNSSTDLYEVVERFLS", "text": "FUNCTION: Photoreceptor implicated in non-image-forming responses to light. May be able to isomerize covalently bound all-trans retinal back to 11-cis retinal (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily."}
{"protein": "MNTGFFFFVIMATGLVLTFDTIHAEDKLKCTKTDDCAKYCSQFTDVHPACLGGYCECLRWEGGISS", "text": "FUNCTION: inhibits Kv1.3/KCNA3 channel (1 uM of the toxin inhibits currents by 64.1%). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 30 subfamily."}
{"protein": "MGRVIRAQRKGAGSVFRAHTKKRKGEPKLRHLDYAERHGYLKGVVKQIIHDPGRGAPLAVVNFRDPYRFRLSKQLFIAAEGMYTGQFVYCGRRAQLQIGNVLPIGLMPEGTIVCNLEEKTGDRGKLARTSGNYASVIAHNPDTKRTRVKLPSGAKKVLPSANRAMIGIVAGGGRIDKPILKAGRAYHKYKVKRNCWPKVRGVAMNPVEHPHGGGNHQHIGKASTVKRGTPPGRKVGLIAARRTGRIRGGKGDEKFKEKEKK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
{"protein": "MRLETIRQSMRATGAKDCHIDRVLRAWTQAKPLESGARRHQPENFLPQALRTALPALQEELSALARVRSEHPGEDGSSRLLVELADGQTVESVLLPRDGLCISTQIGCAVGCTFCMTGRDGLLRQVSSAEMVAQVVLGRGRRKVTRVVFMGMGEPSHNMDNVLEAIDTLGTYGGIGHKNLVFSTVGDRRVFDRLPQQRVVPALALSLHSTRAELRAELLPKAPHIDPTELVELAEHYARTTGYPIQYQWTLIDGINDSIEEMDGIVRLLTGKYAIMNLIPYNATATLDYRRPSLEHITTLTKYLHAKGIRTTVRNSAGQDVDGGCGQLRARTLDAGTATDAQKISLKHLKTGTRSAA", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family."}
{"protein": "MALVFSALLLLGLCGKISSEGQPAFHNTPGAMNYELPTTKYETQDTFNAGIVGPLYKMVHIFLSVVQPNDFPLDLIKKLIQNKKFDISVDSKEPEIIVLALKIALYEIGVLICAILGLLFIILMPLVGCFFCMCRCCNKCGGEMHQRQKQNAPCRRKCLGLSLLVICLLMSLGIIYGFVANQQTRTRIKGTQKLAKSNFRDFQTLLTETPKQIDYVVEQYTNTKNKAFSDLDGIGSVLGGRIKDQLKPKVTPVLEEIKAMATAIKQTKDALQNMSSSLKSLQDAATQLNTNLSSVRNSIENSLSSSDCTSDPASKICDSIRPSLSSLGSSLNSSQLPSVDRELNTVTEVDKTDLESLVKRGYTTIDEIPNTIQNQTVDVIKDVKNTLDSISSNIKDMSQSIPIEDMLLQVSHYLNNSNRYLNQELPKLEEYDSYWWLGGLIVCFLLTLIVTFFFLGLLCGVFGYDKHATPTRRGCVSNTGGIFLMAGVGFGFLFCWILMILVVLTFVVGANVEKLLCEPYENKKLLQVLDTPYLLKEQWQFYLSGMLFNNPDINMTFEQVYRDCKRGRGIYAAFQLENVVNVSDHFNIDQISENINTELENLNVNIDSIELLDNTGRKSLEDFAHSGIDTIDYSTYLKETEKSPTEVNLLTFASTLEAKANQLPEGKPKQAFLLDVQNIRAIHQHLLPPVQQSLNTLRQSVWTLQQTSNKLPEKVKKILASLDSVQHFLTNNVSLIVIGETKKFGKTILGYFEHYLHWVFYAITEKMTSCKPMATAMDSAVNGILCGYVADPLNLFWFGIGKATVLLLPAVIIAIKLAKYYRRMDSEDVYDDVETVPMKNLEIGSNGYHKDHLYGVHNPVMTSPSRY", "text": "FUNCTION: May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis (PubMed:19228982). Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment. Endoplasmic reticulum Endoplasmic reticulum-Golgi intermediate compartment Note=Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine. SIMILARITY: Belongs to the prominin family."}
{"protein": "MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKTSTKLHVGNISPTCTNKELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPVDRSGRVADFTEQYNEQYGAVRTPYTMGYGDSLYYNNAYGALDAYYKRCRAARSYEAVAAAAASAYNYAEQTLSQLPQVQNTAMASHLTSTSLDPYDRHLLPTSGAAAAAAAAAAAAVTAASSSYYGRDRSPLRRATGPVPTVGEGYGYGHESELSQGSSAARNSLYDMARYEREQYADRARYSAF", "text": "FUNCTION: RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU- rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA- guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Nucleus speckle Cytoplasm Cytoplasmic granule Note=Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases its subcellular relocalization from the nucleus to the cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK signaling pathway. Primarily localized in nucleus and nucleoli under cell growth conditions and accumulated in the cytoplasm and cytoplasm perinuclear granules upon muscle cell differentiation (By similarity)."}
{"protein": "MMKVLVVVALLVTLISYSSSEGIDGLEADELLSLMANEQTRKECIPKHHECTSNKHGCCRGNFFKYKCQCTTVVTQDGEQTERCFCGTPPHHKAAELVVGFGKKIFG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 04 (U1-Lctx) subfamily."}
{"protein": "MFDYETLRFIWWLLIGVILVVFMISDGFDMGIGCLLPLVARNDDERRIVINSVGAHWEGNQVWLILAGGALFAAWPRVYAAAFSGFYVAMILVLCSLFFRPLAFDYRGKIADARWRKMWDAGLVIGSLVPPVVFGIAFGNLLLGVPFAFTPQLRVEYLGSFWQLLTPFPLLCGLLSLGMVILQGGVWLQLKTVGVIHLRSQLATKRAALLVMLCFLLAGYWLWVGIDGFVLLAQDANGPSNPLMKLVAVLPGAWMNNFVESPVLWIFPLLGFFCPLLTVMAIYRGRPGWGFLMASLMQFGVIFTAGITLFPFVMPSSVSPISSLTLWDSTSSQLTLSIMLVIVLIFLPIVLLYTLWSYYKMWGRMTTETLRRNENELY", "text": "FUNCTION: A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested (PubMed:8626304). Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2 family."}
{"protein": "MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAATHDGPQSPGAGGPTCSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQAAPDDTQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSTRLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPTPSMGGPGTPDSRPPFLSRPARGLYSRSGSLSGRSSLKAEAENTSEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATGTGTFSPGASPGSEARTTGDISVEKLNLGTDSDSSPQKSSRDPPSSPSSLSSPIQESTAPELPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDFVAGGC", "text": "FUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. SUBCELLULAR LOCATION: Cytoplasm Nucleus Endosome Cell membrane; Peripheral membrane protein Cleavage furrow Midbody Note=Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily."}
{"protein": "MFGTESSLSMFLNTLTPKFYVALTGTSSLISGLILIFEWWYFRKYGTSFIEQVSVSHLRPLLGGVDNNSSNNSNSSNGDSDSNRQSVSECKVWRNPLNLFRGAEYNRYTWVTGREPLTYYDMNLSAQDHQTFFTCDSDHLRPADAIMQKAWRERNPQARISAAHEALEINEIRSRVEVPLIASSTIWEIKLLPKCATAYILLAEEEATTIAEAEKLFKQALKAGDGCYRRSQQLQHHGSQYEAQHRRDTNVLVYIKRRLAMCARRLGRTREAVKMMRDLMKEFPLLSMFNIHENLLEALLELQAYADVQAVLAKYDDISLPKSATICYTAALLKARAVSDKFSPEAASRRGLSTAEMNAVEAIHRAVEFNPHVPKYLLEMKSLILPPEHILKRGDSEAIAYAFFHLAHWKRVEGALNLLHCTWEGTFRMIPYPLEKGHLFYPYPICTETADRELLPSFHEVSVYPKKELPFFILFTAGLCSFTAMLALLTHQFPELMGVFAKAFLSTLFAPLNFVMEKVESILPSSLWHQLTRI", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ST7 family."}
{"protein": "MSNSFCVVYKGSDTDINNIQRDFDGKGEALSNGYLFIEQNGHYQKCEMERGTAYLIGSLYNRTFLIGLAGVWEGEAYLANDAELLALLFTRLGANALALAEGDFCFFIDEPNGELTVITESRGFSPVHVVQGKKAWMTNSLKLVTAAEGEGALWFEEEALVCQSLMRADTYTPVKNAQRLKPGAVHVLTHDSEGYSFVESRTLTTPASNQLLALPREPLLALIDRYLNAPLEDLAPRFDTVGIPLSGGLDSSLVTALASRHFKKLNTYSIGTELSNEFEFSQQVADALGTHHQMKILSETEVINGIIESIYYNEIFDGLSAEIQSGLFNVYRQAQGQVSCMLTGYGSDLLFGGILKPGAQYDNPNQLLAEQVYRTRWTGEFATHGASCYGIDIRHPFWSHSLISLCHALHPDYKIFDNEVKNILREYADSLQLLPKDIVWRKKIGIHEGSSVNQAFANVLGSTVDNYQTKSRFTYRVYQAFLRGRLSITDVTPSQLKDLIKKD", "text": "FUNCTION: Involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Catalyzes the ATP- dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5- carboxymethylproline."}
{"protein": "MVLNANHLQTKKTIKETLLAPRFYTTDFDEISRYDISSNFEEIEAIVNEFRSDYNKKHFIRDEEFDRHWSQIDAQTKQMFVEFLERSCTAEFSGFLLYKELARKLKEKMPVLAEGFLLMSRDEARHAGFLNKAMADFNLTLDLGFMTKNRRYTFFKPKFIFYATYLSEKIGYWRYITIYRHLEKHPEHRIYPIFKFFESWCQDENRHGDFFAAIVKSQPYLLEGFISKLWCRFFLLAVFATMYLNDCQRGEFYKSIGLDPRQFDIYVIQKTNESAAKLFPTVLDLDNPRFFECLDKCACYNKLLLEIDDREQPFFNQVLNVFYKFYLYFLLVLNFIMLYFLRTVNCNSFTRMVK", "text": "FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the AcsF family."}
{"protein": "MDQVSRSLPPPFLSRDLHLHPHHQFQHQQQQQQQNHGHDIDQHRIGGLKRDRDADIDPNEHSSAGKDQSTPGSGGESGGGGGGDNHITRRPRGRPAGSKNKPKPPIIITRDSANALKSHVMEVANGCDVMESVTVFARRRQRGICVLSGNGAVTNVTIRQPASVPGGGSSVVNLHGRFEILSLSGSFLPPPAPPAASGLTIYLAGGQGQVVGGSVVGPLMASGPVVIMAASFGNAAYERLPLEEDDQEEQTAGAVANNIDGNATMGGGTQTQTQTQQQQQQQLMQDPTSFIQGLPPNLMNSVQLPAEAYWGTPRPSF", "text": "FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). Binds an AT-rich DNA sequences in the FLOWERING LOCUS T (FT) promoter (PubMed:22442143). Acts redundantly with AHL18, AHL27 and AHL29 in the regulation of flowering and regulation of the hypocotyl elongation. Plays a role in both photo- and skotomorphogenesis (PubMed:19517252). Acts as a chromatin remodeling factor that modifies the architecture of FLOWERING LOCUS T (FT) chromatin by modulating both H3 acetylation and methylation leading to the regulation of FT expression during flowering induction (PubMed:22442143). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSGPCGEKPVLEASPTMSLWEFEDSHSRQGTPRPGQELAAEEASALELQMKVDFFRKLGYSSTEIHSVLQKLGVQADTNTVLGELVKHGTATERERQTSPDPCPQLPLVPRGGGTPKAPNLEPPLPEEEKEGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTLEHRKQPCPYGRKCTYGIKCRFFHPERPSCPQRSVADELRANALLSPPRAPSKDKNGRRPSPSSQSSSLLTESEQCSLDGKKLGAQASPGSRQEGLTQTYAPSGRSLAPSGGSGSSFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFSVPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRSPWGRAGSLAKEQASVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHPSE", "text": "FUNCTION: (Microbial infection) Exhibits antiviral activity against HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA species. FUNCTION: (Microbial infection) Binds to Japanese encephalitis virus (JEV) and Dengue virus (DEN) RNAs. FUNCTION: Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay (PubMed:19909337). Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation (PubMed:26320658). Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL) (By similarity). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By similarity). Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR (By similarity). Self regulates by destabilizing its own mRNA (By similarity). Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (PubMed:19909337, PubMed:26320658, PubMed:26134560, PubMed:22561375). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (PubMed:22055188). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (PubMed:22055188). Also plays a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (PubMed:24048733). Affects the overall ubiquitination of cellular proteins (By similarity). Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (By similarity). Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes (PubMed:24048733). Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (PubMed:25861989). Prevents stress granule (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite- induced oxidative stress, heat shock and energy deprivation (By similarity). Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti- inflammatory M2 state (By similarity). May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (PubMed:16574901, PubMed:18364357). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (PubMed:19185603). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial pro-inflammatory cytokine production (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, P-body Rough endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic granule Note=Predominantly localized in the cytoplasm. Colocalizes with GW182 on many granule-like structures, probably corresponding to cytoplasmic GW bodies (GWBs), also called processing bodies (P bodies). Colocalizes with calnexin on the surface of the rough endoplasmic reticulum (RER) membrane and with translationally active polysomes (By similarity). Colocalizes with ZC3H12D in cytoplasmic mRNA processing P-body, also known as GW bodies (GWBs) (PubMed:22055188, PubMed:26134560). SIMILARITY: Belongs to the ZC3H12 family."}
{"protein": "MNPYGPSRVPEGEVYRPDRLNRKATLVAIVGAAILAFAFALVLWMGLKQTNLPAFGPSNVTRAVASATIAAVLIVTGFLTWLWLRDEHQSNPRWELEDVKPRPKWRTALTYLASYLSPAALVVAVLAIPLSATRLYLDGISVDQGFRTQFLTRMADDIGLSDMNYIDMPTFYPAGWFWLGGRLANLLGLPGWEAFQPWAIVSMAVAASVLVPVWQRITGSLPVATGIALVTTCIILAMNSEEPYAAIVAMGIPAMLVLASRIAKGDKFALAGGIIYLGVSATFYTLFTGAIALSAVAVCIVVAAIVQRSIKPLLWLAVLGGGSIVIALISWGPYLLASINGAERSGDSATHYLPLEGTQFPVPFLASSVVGLLCLVGLIYLVVRFHNNEVRAMWVGIAVFYAWMGMSMAITLLGNTLLGFRLDTVLVLIFATAGVLGIADFRLASVYQLYPTQITERTATHLTNLIVVLVLLGGLYYAQDLPQKNARAIDLAYTDTDGYGERADLYPAGAARYYKDINDHLLDQGFEPSETVVLTDELDFMSYYPYRGYQAFTSHYANPLGEFGNRNAFIEDLAIRSWDELADPQQFSDALNTSPWTIPEVFIFRGSIDDPDAGWKYDVAEDLYPNNPNVRFRGVYFNPESFDQMWQTKQVGPFVVVTHNE", "text": "FUNCTION: Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the cell wall (PubMed:16595677). Catalyzes the addition of the first key arabinofuranosyl (Araf) residue from the sugar donor decaprenyl-phospho-arabinose (DPA) on the C-5 of a 6-linked galactofuranosyl (Galf) of the galactan domain, thus 'priming' the galactan for further elaboration by other arabinofuranosyltransferases (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 85 family."}
{"protein": "MPLRASEHAYRPLGPGTPPVRARLPAAAWVGVGTIIGGVVIIAALVLVPSRASWALSPCDSGWHEFNLGCISWDPTPMEHEQAVGGCSAPATLIPRAAAKQLAAVARVQSARSSGYWWVSGDGIRARLRLVDGVGGIDQFCEEPALRICYYPRSPGGFVQFVTSTRNALGLP", "text": "FUNCTION: Important virulence factor of HSV neurotropism. Seems to be required for glycoprotein B-induced fusion. Dispensable for growth in vitro (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=In transfected cells, it is retained within the ER. SIMILARITY: Belongs to the herpesviridae HHV-1 UL45 family."}
{"protein": "MHNNGRMLGVIGGSGFYTFFGSDTRTVNSDTPYGQPSAPITIGTIGVHDVAFLPRHGAHHQYSAHAVPYRANMWALRALGVRRVFGPCAVGSLDPELEPGAVVVPDQLVDRTSGRADTYFDFGGVHAAFADPYCPTLRAAVTGLPGVVDGGTMVVIQGPRFSTRAESQWFAAAGCNLVNMTGYPEAVLARELELCYAAIALVTDVDAGVAAGDGVKAADVFAAFGENIELLKRLVRAAIDRVADERTCTHCQHHAGVPLPFELP", "text": "FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Prefers MTA, with 2% activity on adenosine, 0.8% activity on S-adenosyl-L- homocysteine and no activity on other tested nucleosides. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily."}
{"protein": "MNLQIEMEHHRGVLIVRLSGELDHHTSDMVRMQMDEAIQRRQCEHIVLSLKNLQFMDSSGLGVILGRYKLINQKGGEMAVCDVNPPVHRLLDMSGLFKIMPIYDNEVNALTELEVVS", "text": "FUNCTION: In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition. SIMILARITY: Belongs to the anti-sigma-factor antagonist family."}
{"protein": "MKGSDALIMALRNMAATLGVYDLMEVRVFLERSCRFVQERYRAIYVDAYMSMVVDSVLDLKAGFSGTPEMDDARYSLRDALKRLDEINAPTIVGLTVLYRTYVKGEPLHPPGTPFPGGFEVEKKDGVHYCPVKDKQSDNPEALCDICIARQSPLP", "text": "SIMILARITY: Belongs to the UPF0305 family."}
{"protein": "MNLKILVGLFILGIIILSAMTFLNFTTIVAQDKGDQQPKGPIVYTYTEYNGTYFPHILTVVYYPCNATCSNLGFPSVWPVSNENQCHNAVVNTTCQALIEGVDWQLPLLNYVGGVAIPLSTPPCKLPWAQQLGVKGALVYYTQMVGEPLGVTLACGLLYATEDSMPGSITAINPVTGKIVWMANGLAGPAMNNPVVWHGIVYVSVGGVCFTFSQFVHFEDHQYCKIHRGRCGAVYAFNATNGQLLWMRFTYGEAMPAPAIYDGILAYVTGGGCFVGVNATTGQTLWVDHFPGFIANMASVNYYVLPNGTPLFIAGFTYTAPPYGYIIAVNGLNGHEAWNATMPAPYVGANTGLGDVAPAVDQQLGIVVDNDIANFSNGYVDMVTFALNATNGKPLWAVNTGRGPIPPAYKGGMPLIVGNVVYDGNPSLGTVNAICIKTGKILWSTKLPCLQTPPKFPGGPRGSPTYYHGLLWVSAGQYVYVINPKNGDILTFYWIGGRLGIMNPVIAGNTMFLSNSYGWIVAIPLSQIYPAYIYY", "text": "FUNCTION: Catalyzes the hydrolysis of tetrathionate to generate elemental sulfur, thiosulfate and sulfate. SUBCELLULAR LOCATION: Cell surface Note=Associated with the S-layer in the pseudo-periplasmic space. SIMILARITY: Belongs to the tetrathionate hydrolase family."}
{"protein": "MMEFKVSPLTKIISLSGFLALGFLLVILSCALFHNYYPLFDILIFLLAPIPNTIFNAGNKYHTSDFMSDSSNTGQDLAHFLTGMLVTSGIALPVVFYHCQLIGHLSCIMCMIGGLIIYSSIVIFKWFFKKDFNEDDSLFG", "text": "FUNCTION: Involved in protein transport from endosomes to the vacuole. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OB-RGRP/VPS55 family."}
{"protein": "MMRQSLQAVLPEISGNKTSLLRKSVCSDLLTLFNSPHSTLPSLLVSGMPEWQVHNPSDKHLQSWYCRQLRSALLFHEPRIAALQVNLKEAYCHTLAISLEIMLYHDDEPLTFDLVWDNGGWRSATLENVS", "text": "FUNCTION: Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during oxidative stress. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GpW/Gp25 family. IraD subfamily."}
{"protein": "MGSAPLPACLLALSLAGTVLAPGCGAAQGRLAHKLLHDLFANYSSALRPAEDTERALNVTLQVTLSQIIDMDERNQVLTSYLWVRQAWLDAHLAWDKDAYGGIDSIRIPSSYVWRPDIVLYNNADERFGGSMETNVVLRSDGHIMWDSPAITKSSCKVDVSYFPFDGQQCRLTFGSWTYNGNQIDLRNLLDTGDLTDFVENVEWEVLGMPATRNVVTYGCCSEPYPDVTYTLLLRRRASFYIFNLLLPCVMISFLAPLGFYLPADSGEKVSLGVTVLLALTVFQLLVAESMPPSESVPLIGKYYIATMTMITASTALTIFIMNIHHCGPGARPVPPWARRLILHHLARALCVCEVGESCGRPQREGTGGMGPRDPPGEGVEPGLCPRSRCLCHHHAVLSSVGYIAGVFRRHRTAQRRAAEWKKVAKVMDRFFMWVFFLMVFLMSVLVIGKAA", "text": "FUNCTION: Ionotropic receptor with a probable role in the modulation of auditory stimuli. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi- pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-10/CHRNA10 sub- subfamily."}
{"protein": "MCDYKVSERAYAKLIFHAAKYPHQAVNGLLLAEKTSKGSQVEIVDAIPLFHQCLYVTPMAEVALMLIDAHAEREGLVIAGYYAAPENFYDNQVDKTPAAKIADKIQENFKNACFVVVDNKLMTLQHDRAAIQVFNCPGDSGARWSKAKFTLSQASDTLEGVSLLLKRGAMRDLVDFDNHLDNPDKNWTNDFLNQPLNDLQKLY", "text": "FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized multi-pass membrane proteins like rhodopsins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the EMC8/EMC9 family."}
{"protein": "MAESAGASSFFPLVVLLLAGSGGSGPRGVQALLCACTSCLQANYTCETDGACMVSIFNLDGMEHHVRTCIPKVELVPAGKPFYCLSSEDLRNTHCCYTDYCNRIDLRVPSGHLKEPEHPSMWGPVELVGIIAGPVFLLFLIIIIVFLVINYHQRVYHNRQRLDMEDPSCEMCLSKDKTLQDLVYDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQGKPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNSGGVHEEYQLPYYDLVPSDPSIEEMRKVVCDQKLRPNIPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI", "text": "FUNCTION: Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine- threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type- 1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily."}
{"protein": "MDIISTTFDQINTHIKFTNQKKIEFQNHIEKEWEIITQLESNEQFTVYMSKKLKGPNFTNNRFGLCTVKKIKSQYFNENEILNHIKLRDNKYVLKYYGCGKDNNQDVYIYLEFIEYSIPISKVKLIPNDSSIDNFNNVSNTIIELVTCKLVESLNCIHKDNKIVHGNIKGENILLVNDESEYGFSVKFINFSLNIGYEDSIHLDMFNLGCVLIQMLGCDCTKDENIDFLFSKIPNHLVEKFKKVISQLLSKNINNQILTDIISNKITTSLPKYSTLIGEPNDGLIYIGIQNNSDGLILPLFNQPICKKTFTYGVYYLSLSSFHRQLNVGVIPESIHTLELASFNQTILPGVIPTSVRTLKLPSYNKTLTQGSIPKGVRTLLLSSFNQPLTTDIIPKTVTILKLQSFNQPIEWGALPCSLVELSLASYKQPLQWGVIPYYISTLELPLASAPFSEGSIPSGVSKLIQQGEIQQINKPIKINNENNQNYMSCSQNEFDSKLTLILNSKITRESLFFGLKYLELSTFNQSFETLPIPETVEYLKLPMYNQPLTPKLLPSGIKFLILPSFNHPIRGESIPPSVIHLVFNKLFSVIESIPSSVKYLDLGDEYYVYPGHLLHSVLSFRSGLKFRVTDPIPYSQSLTNLNLYNFNIELLKNGISSNVTSLTLGSNFTNIESLSNLPSSVTNLSFGITTLNEKAISDITKYVKSTVTTITVNNEQIRKKIN", "text": "SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family."}
{"protein": "MRRLHRNLSLLFLICILNEYRIESQTLSPPITDRFKCLTNGCCDHHEWCRFWASIGECNANKDWMTENCQLACGTCTAPAAPLLPVTTTASSFNGGGFVQTTTQSSGPTTTITIPPSSLTSVTSCERVKDSIAQASELMSISRLINPVEDNFGRNMLSIDDITRSVPTGCVPQLSDVGVDCRKSLCYHLMYRTLDGTCNNLEKPMQGAAFRRFNRHFPAQYDDGKGEPISSLNQSRPSAREANRVMLSSAQSVVHDKFNNMMMQWGQFMSHDMSKTTLQPSANCKTCDPVPSKCMPIPIGEKDPNLGFKSKQCLKVSRSAPICRVEPREQLNENTAYIDGSMIYGSSLKDLHKFRDGRTGFLRVTRFNNQNVLPFDQSKCANKDKCTASFTAGDIRANLFIGLSSLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSFDKVIGPYKGYDTNVDATIANEFTTSAFRFGHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVKRPHRMTPAITEKMFGSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADMILDRNLRAGLARNYNTTNDVDFYVGSMLEDPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGIFTRSQMEEIKKSSLSRIICDNADNFELVSQDAFLLPGSNLTPCSKIPKMDLSKWRAL", "text": "FUNCTION: Plays an essential role in cuticle biogenesis. Required in combination with bli-3 for correct formation of cross-links in cuticle collagens. SIMILARITY: Belongs to the peroxidase family."}
{"protein": "MQKNAAHTYAISSLLVLSLTGCAWIPSTPLVQGATSAQPVPGPTPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTNFGFDTVPRYLQGLFGNARADVEASGGNTFNGKGGANASNTFSGTLTVTVDQVLVNGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNTVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM", "text": "FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family. SIMILARITY: Belongs to the FlgH family."}
{"protein": "MEIFESFGIEGEVTKQWEPATDEILWCRNESGTLSRMERFRNEPPVGVKWTHGTLQQGRVEEIMKKRITEISGVEVEYSTELSDLTINTRESSNSKASACSVTIRSVADDQEAHRSSETIRARYIIGADGGRSSIRDLMGVAMEGTKGTAIWGVMDILGGSDFPDFGATSVVRSDSDGAVDFVRREEGLTRIYVELNKCAAGWEALERDTITPELILEKCRYIIRPYKLEVDYVEWWSSFTVWQRLSKSMIVHDRVFLVGDAVHTHSPLCGMGMNTGIQDSFNLGWKLAGVVQGQLNYDILQTYETERRPVAEALLDTDRTVLDLFHAPLGPEAEALLAKVPALQVYLGGRGICYHESVLTCRLAQTLGDLTAGECLPDVTVFDYATGRPSSTHSWIKGNGGWAIIVWAGDVSRPSQMNLVQSLSRDMIELRDSLGKSGSMIDFFLIHCSAWPSVELADFPPLFFPTTKTIGRPNGRIFVDEKAVYDGLHISRAEGGVAIVRPDKHIAWAGGLQEVDSLQRYLRQVFRPQPE", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines (PubMed:33242032). The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A (PubMed:33242032). NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl- transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety (PubMed:33242032). The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G (PubMed:33242032). Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H (PubMed:33242032). The N- acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C (PubMed:33242032). SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family."}
{"protein": "MALAPSKVSPFSGFSLSDGVGAVRNPTCSVSLSFLNKKVGSRNLGVSASTVPLTGVIFEPFEEVKKEELAVPTAGQVSLARQYYADECESAINEQINVEYNASYVYHSLFAYFDRDNVALKGFARFFKESSEEEREHAEKLMKYQNTRGGRVVLHPIKNVPSEFEHVEKGDALYAMELALSLEKLVNEKLRSVHSVADRNKDPQLADFIESEFLSEQVEAIKKISEYVAQLRMVGKGHGVWHFDQSLLHDGHAA", "text": "FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. SIMILARITY: Belongs to the ferritin family."}
{"protein": "MPTPNIPSDFDFLDATLNLERLPVEELAELRKSEPIHWVDVPGGTGGFGDKGYWLVTKHADVKEVSRRSDVFGSSPDGAIPVWPQDMTREAVDLQRAVLLNMDAPQHTRLRKIISRGFTPRAIGRLEDELRSRAQKIAQTAAAQGAGDFVEQVSCELPLQAIAELLGVPQDDRDKLFRWSNEMTAGEDPEYADVDPAMSSFELISYAMKMAEERAVNPTEDIVTKLIEADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITHGMIAFAQNPDQWELYKKERPETAADEIVRWATPVSAFQRTALEDVELGGVQIKKGQRVVMSYRSANFDEEVFEDPHTFNILRSPNPHVGFGGTGAHYCIGANLARMTINLIFNAIADNMPDLKPIGAPERLKSGWLNGIKHWQVDYTGAGKASVSGAPGTCPVAH", "text": "FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en- 3-one (aldehyde), to finally yield the carboxylic acid (25S)-3- oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MPIEIVCKIKFAEEDAKPKEKEAGDEQSLLGAAQGPAAPRDLATFASTSTLHGLGRACGPGPHGLRRTLWVLALLTSLAAFLYQAASLARGYLTRPHLVAMDPAAPAPVAGFPAVTLCNINRFRHSALSDADIFHLANLTGLPPKDRDGHRAAGLRYPEPDMVDILNRTGHQLADMLKSCNFSGHHCSASNFSVVYTRYGKCYTFNADPQSSLPSRAGGMGSGLEIMLDIQQEEYLPIWRETNETSFEAGIRVQIHSQEEPPYIHQLGFGVSPGFQTFVSCQKQRLTYLPQPWGNCRAESKLREPELQGYSAYSVSACRLRCEKEAVLQRCHCRMVHMPGNETICPPNIYIECADHTLDSLGGGSEGPCFCPTPCNLTRYGKEISMVKIPNRGSARYLARKYNRNETYIRENFLVLDVFFEALTSEAMEQRAAYGLSALLGDLGGQMGLFIGASILTLLEILDYIYEVSWDRLKRVWRRPKTPLRTSTGGISTLGLQELKEQSPCPNRGRAEGGGASNLLPNHHHPHGPPGSLFEDFAC", "text": "FUNCTION: Probable cation channel with high affinity for sodium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC4 subfamily."}
{"protein": "MLSFQYPDVYRDETSVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDVLCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQGSNGINGILKWVKLIDNFEGEYDYITNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLRNVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTREELEPRVFREVTVKGIDASDYQTIQVFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTTSKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDSKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGPGKPTAKVIEEVSDMFAFIARCLNIEWIQ", "text": "FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has high activity on the succinyl- (suc-) peptide-4- methylcoumaryl-7-amide (MCA) substrates suc-Gly-Pro-Leu-Gly-Pro-MCA, suc-Gly-Pro-MCA and suc-Ala-Ala-Ala-MCA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S9A family."}
{"protein": "MNVIDHVRDMAAAGLHSNVRLLSSLLLTMSNNNPELFSPPQKYQLLVYHADSLFHDKEYRNAVSKYTMALQQKKALSKTSKVRPSTGNSASTPQSQCLPSEIEVKYKMAECYTMLKQDKDAIAILDGIPSRQRTPKINMMLANLYKKAGQERPSVTSYKEVLRQCPLALDAILGLLSLSVKGAEVASMTMNVIQTVPNLDWLSVWIKAYAFVHTGDNSRAISTICSLEKKSLLRDNVDLLGSLADLYFRAGDNKNSVLKFEQAQMLDPYLIKGMDVYGYLLAREGRLEDVENLGCRLFNISDQHAEPWVVSGCHSFYSKRYSRALYLGAKAIQLNSNSVQALLLKGAALRNMGRVQEAIIHFREAIRLAPCRLDCYEGLIECYLASNSIREAMVMANNVYKTLGANAQTLTLLATVCLEDPVTQEKAKTLLDKALTQRPDYIKAVVKKAELLSREQKYEDGIALLRNALANQSDCVLHRILGDFLVAVNEYQEAMDQYSIALSLDPNDQKSLEGMQKMEKEESPTDATQEEDVDDMEGSGEEGDLEGSDSEAAQWADQEQWFGMQ", "text": "FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). APC7 is not required for the assembly of the APC/C complex, but has an enzyme-substrate adapter activity mediating the processive ubiquitination of specific substrates (PubMed:34942119). Involved in brain development through the specific ubiquitination and clearance of MKI67 from constitutive heterochromatin after neuronal progenitors exit mitosis (PubMed:34942119). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus Cytoplasm, cytoskeleton, spindle Note=Localizes to spindle during metaphase and to cytoplasmic microtubules during interphase. SIMILARITY: Belongs to the APC7 family."}
{"protein": "MRLGYLIVGCAVALLATTDGVVDASSKHKQLSTDVPRPADDISSERFLRSQDTPEDDGNPAHEDRGYLTVLTNAAMHPLRERKMKNQIANLIKMDATDAELYAAGVQPHRLFDVIRHKDESVEMSLSQWVTMVHQHQFPSDYIWKSQAYRRFKQYAGFYDGMQRNGQRVASTT", "text": "FUNCTION: Effector that leads to host programmed cell death. SUBCELLULAR LOCATION: Secreted Host nucleus Host cytoplasm. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "VQNPGASAIQCRAAVLRKEGQPMKIEQVLIQAPGPNQVRVKMVSSGLCATDAHLVWGEQKISDLGGIGCPAIAGHEGAGIVESVGENVTEFVPGDSVLTSFQPQCGQCESCLRPSTNICKKYDLIKSTTDVSTARTLDGQPITSLFGLGVYSEYITTTEHHVFKVNKAANLEHASIISCSVGTGFYSATNLAAVYEGSTCAVWGLGGIGINTLFGCKYNKAKHIIGIDVNEDKREIAAEFGCTEFINPKTLGQPVEQYLMDKFGGVDFAFDCVGYKPILDQAAVSLAIDGTMVIIGAAAKEVKFEMPAFNFLFNRKVVGGLLGSKKTKVAYQELCDMYVDGTYDVDRLVSNKFSLDQINEAFQTLKDGNCIRSIVVFK", "text": "FUNCTION: Catalyzes the NAD(+)-dependent oxidation of geraniol to geranial, playing an important role in the biosynthesis of neral, an alarm pheromone. Cannot use NADP(+). Also acts as a farnesol dehydrogenase by catalyzing the oxidation of (2E,6E)-farnesol to (2E,6E)-farnesal, with lower activity compared to geraniol dehydrogenase activity. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIVGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIAEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSNHAY", "text": "FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6- bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (By similarity). In addition, may also function as scaffolding protein (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band Cytoplasm, myofibril, sarcomere, M line Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+). SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family."}
{"protein": "MARASPLLMICLVLGSSFATYNLVTMIIHYGSADSLATEDGGLFFDPIVEMPEHVKNTKTSKAPFHIALTATDAIYNKWQCRIMYYWYKKQRSLPGSEMGGFTRILHSGKADNLMDEIPTVVVDPLPEGLDRGYVVLNRPWAFVQWLEKANIEEEYILMAEPDHVFVRPLPNLAFGENPAAFPFFYIKPKENEKIVRKYYPEENGPVTNVDPIGNSPVIIRKDLIAKIAPTWMNISMKMKEDPETDKAFGWVLEMYGYAVASALHGVRHILRKDFMLQPPWDTETFNKYIIHYTYGCDYNLKGELTYGKIGEWRFDKRSHLRGPPPRNLPLPPPGVPESVATLVKMVNEASANIPNWDTL", "text": "FUNCTION: Glycosyltransferase involved in the O-arabinosylation of several proteins including extensins and small signaling peptides (By similarity). Catalyzes the transfer of the initial L-arabinose to the hydroxyl group of Hyp residues (By similarity). Probably involved in the arabinosylation of CLAVATA3/ESR-related (CLE) signaling peptides that move from root to shoot, to interact with SUNN receptor kinase signaling that regulates nodulation (Probable). Involved in long distance nodulation signaling events (PubMed:28592666). Involved in the autoregulation of nodulation (AON), a long distance systemic signaling from root to shoot and back again, which allows legumes to limit the number of root nodules formed based on available nitrogen and previous rhizobial colonization (PubMed:28592666). Functions in the root, upstream of the shoot receptor kinase SUNN and via CLE peptide, to control AON (PubMed:28592666). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein."}
{"protein": "MATSTSTEAKSASWWNYFFLYDGSKVKEEGDPTRAGICYFYPSQTLLDQQELLCGQIAGVVRCVSDISDSPPTLVRLRKLKFAIKVDGDYLWVLGCAVELPDVSCKRFLDQLVGFFNFYNGPVSLAYENCSQEELSTEWDTFIEQILKNTSDLHKIFNSLWNLDQTKVEPLLLLKAARILQTCQRSPHILAGCILYKGLIVSTQLPPSLTAKVLLHRTAPQEQRLPTGEDAPQEHGAALPPNVQIIPVFVTKEEAISLHEFPVEQMTRSLASPAGLQDGSAQHHPKGGSTSALKENATGHVESMAWTTPDPTSPDEACPDGRKENGCLSGHDLESIRPAGLHNSARGEVLGLSSSLGKELVFLQEELDLSEIHIPEAQEVEMASGHFAFLHVPVPDGRAPYCKASLSASSSLEPTPPEDTAISSLRPPSAPEMLTQHGAQEQLEDHPGHSSQAPIPRADPLPRRTRRPLLLPRLDPGQRGNKLPTGEQGLDEDVDGVCESHAAPGLECSSGSANCQGAGPSADGISSRLTPAESCMGLVRMNLYTHCVKGLVLSLLAEEPLLGDSAAIEEVYHSSLASLNGLEVHLKETLPRDEAASTSSTYNFTHYDRIQSLLMANLPQVATPQDRRFLQAVSLMHSEFAQLPALYEMTVRNASTAVYACCNPIQETYFQQLAPAARSSGFPNPQDGAFSLSGKAKQKLLKHGVNLL", "text": "FUNCTION: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38 (PubMed:23084991)."}
{"protein": "MHIPDGYLGPITCAFFYLIMIPIWYKSIKELKKLDPRKLPLLGVLTAFSFLVMMFNLPVPDGTTAHMVGGTLIAILMDNPWVATIAISIVLIIQAIFFGDGGITCIGANCFNMGVVLPFVGYYVYKFLRDKVGEVIASGIGAYVGIVAAAIVAGFEFGLQPFIEPGYCPYPFTVSVPAMAFAHLITAGPAAAVVTAIVVWYVKKVRPDLFTSKEQQVSGVNA", "text": "FUNCTION: May be involved in metal transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiM family."}
{"protein": "MAPKLFTFVSALSGLASLASAFHAEAKSNIAVYYGQGVNQPRLAEFCAETSYDIINIGFINSFPEQNPLTGLPGSDFGNQCWADTFVVDGIASQLYSHCPNIAEDIPKCQAAGKKVFLSLGGATPTYWFDTIDASTKLADFLWGAFGPVTDAWTVADKPRPFGNAVVDGFDFDIEFFGSKGYANMIKRFRRRFGEVPDQTFYISAAPQCSIPDEQLSVAIKNAVIDFVWVQFYNTPGCSARDFVLGTKNGFNYDSWVEVIKAGANPNAKLYVGLPASGAAANLGYYLTPEEVKPLVKKYMDKYPETFGGVMLWEATQARNNQIDGVGYNEKIREILYDLDPNHPPPTTSPTPTPTPSTTTTSTTSTTSTTSATSTTSTTSTTSTTSTTPTTSTTSTTSTTTPTPSPSPSTASSSTTETVTPSPKPSPSESSTTSETSSLPSTSTPVVSETPSETKTPTSSSAPPLSSSSPVGGSSSTASSSTSTPSETPSASSTRAVSETSTHISTSTSSGPETSLTGSSTSVPATSSSVPSSAISPSSTPVISETPRPPVTSSSSSTFVSSTSTSTDCSESSTAIGTHSSSSISETPSASTPAASPSTSPETTKTLTVFPTPGSSVSTGTTSASTLSSSVPATSGGHTETSTVSTSSANQTPSASTSKPLIPTNSASSTSTGSVTSTPSAPGVPSSSAGSDETATTSTTDSEPTSTSSGSVTAKPTTTEPATTTTIIVTSYTSICPTGFTTITTTITSTYCPGTASATATAIAPTTDVPGSGSGSSPAQPTITADIPEGWTTTVTVCTVCAATPTTVTLTLPPATTTEESTSAQPTGEVPSSDGSGSGEVSTTTVVVVPAPTGNAGDGVPAPGANVGEEYTAAPGSATTSKPLIGGGASGAHTAYPYASSTFHIIPSASAHVPVPSGSGSSPSGTQGGASPTFTGAGSRYDVVKGVPALVALALSLLAVL", "text": "FUNCTION: GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation (By similarity). FUNCTION: GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted, cell wall Cell tip Note=Localizes at the germ tubes of conidia, at hyphal branching sites and hyphal tips. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Secreted, cell wall Cell tip Note=Localizes at the germ tubes of conidia, at hyphal branching sites and hyphal tips. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class III subfamily."}
{"protein": "MVKTPITDAIAAADTQGRFLSNTELQAVNGRYQRAAASLEAARALTANAQRLIDGAAQAVYQKFPYTTQTSGPNYAADARGKSKCARDIGHYLRIITYSLVAGGTGPLDEYLIAGLNEINDAFELSPSWYIEALKYIKANHGLSGQAANEANTYIDYVINALS", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=Part of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family."}
{"protein": "MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELYNLRTPAQLQAAYPYVQWVDYMNALLPEGLNVAEDEMINLSVPSFFEDLGKLLAKTPKRVIANYMFWRIHGFSVGFLSEEFRKRQLQYATALSGRQEQEARWKECVDIATSSMDEVCEDDFDSLGISVGSLYVGKHFHKDSKANALEMVNEIRNVFNDILDEVNWMDAKTKKEAKLKLHSMATHIGYPDEMLDNEKLAAYYAKLDIDPDKYFESFLGMNIFGTDYSFNKLRLPVNKTDWVRHARPAIVNAFYSSLENSIQFPAGILQGHFFNAQRPKYMNFGAIGYVIGHEITHGFDDQGRQFDVKGNLRDWWHPDTQKAYLAKAKCIIEQYGNYTERATGLNLNGINTQGENIADNGGVKESYIAYRRWAEKHGPEAKLPGLDYTPEQMFWVAAGQTWCAKYRKESLKMRITTGVHSPSEFRVLGSLSNMKDFAKDFHCPEGSPMNPVQKCEVW", "text": "FUNCTION: Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues (PubMed:15554877, PubMed:17157960). Functions in female fertility, embryogenesis and memory formation (PubMed:24395329, PubMed:27629706). Required in females for normal patterns of egg laying, probably due to its function in sperm retention and preventing sperm displacement by rival ejaculates (PubMed:24395329). Also required for normal patterns of hatching due to its important role in early embryonic development (PubMed:24395329). Required in the dorsal paired medial neurons for the proper formation of middle-term memory (PubMed:27629706). Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep3 and Nep4 in normal long-term memory formation (PubMed:27629706). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Secreted Note=A secreted form exists that is probably produced by proteolytic cleavage (Probable). In embryos, adult Malpighian tubules and testes, detected in the soluble fraction but is not detected in the membrane fraction (PubMed:15554877, PubMed:17157960). SIMILARITY: Belongs to the peptidase M13 family."}
{"protein": "MNLLDPFMKMTDEQEKGLSGAPSPTMSEDSAGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQPGKADLKREGRPLPEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTYTGSYGISSTAATPASAGHVWMSKQQAPPPPPQQPPQAPPAPQAPPQPQAAPPQQPAAPPQQPQAHTLTTLSSEPGQSQRTHIKTEQLSPSHYSEQQQHSPQQIAYSPFNLPHYSPSYPPITRSQYDYTDHQNSSSYYSHAAGQGTGLYSTFTYMNPAQRPMYTPIADTSGVPSIPQTHSPQHWEQPVYTQLTRP", "text": "FUNCTION: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development (PubMed:24038782). Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6 (PubMed:8640233). Also binds to some promoter regions (By similarity). Plays a central role in successive steps of chondrocyte differentiation (By similarity). Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes by lowering beta-catenin (CTNNB1) signaling and RUNX2 expression (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells and transactivating COL10A1 along with MEF2C (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Mechanistically, helps, but is not required, to remove epigenetic signatures of transcriptional repression and deposit active promoter and enhancer marks at chondrocyte-specific genes (By similarity). Acts in cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3) transcription factors (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells: involved in the lung epithelium during branching morphogenesis, by balancing proliferation and differentiation and regulating the extracellular matrix (By similarity). Controls epithelial branching during kidney development (By similarity). FUNCTION: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development. Specifically binds the 5'- ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6. Also binds to some promoter regions. Plays a central role in successive steps of chondrocyte differentiation. Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes. Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis. Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes by lowering beta-catenin (CTNNB1) signaling and RUNX2 expression. Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells and transactivating COL10A1 along with MEF2C. Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. Mechanistically, helps, but is not required, to remove epigenetic signatures of transcriptional repression and deposit active promoter and enhancer marks at chondrocyte-specific genes. Acts in cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3) transcription factors. In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells: involved in the lung epithelium during branching morphogenesis, by balancing proliferation and differentiation and regulating the extracellular matrix. Controls epithelial branching during kidney development. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKHFLTLRDFSKEEILSLVNHASELKKEPKKLLQDKTLAMIFEKNSTRTRMAFELAITELGGKALFLSSNDLQLSRGEPVKDTARVIGAMVDFVMMRVNKHETLLEFARYSKAPVINALSELYHPTQVLGDLFTIKEWNKMQNGIAKVAFIGDSNNMCNSWLITAAILGFEISIAMPKNYKISPEIWEFAMKQALISGAKISLGYDKFEALKDKDVVITDTWVSMGEENEKERKIKEFEGFMIDEKAMSVANKDAILLHCLPAYRGYEVSEEIFEKHADVIFEEARNRLYVVKALLCFLDNQRGRE", "text": "FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase (ArgG) involved in the final step in arginine biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
{"protein": "MLQDNNGPAVKRAKPSERLQCEYFMEKKKRRCGMTRSSQNLYCSEHLNLMKKAANSQVHNKNGSEAEKERERVPCPLDPNHTVWADQLKKHLKKCNKTKLSHLNDDKPYYEPGYNGENGLLSSSVKIDITAEHLVQSIELLYKVFEGESMDELPLRQLNNKLMSLKRFPQLPSNTKHAVQQSSLIENLVDAGAFERPESLNFIEFGCGRAEFSRYVSLYLLTQLTSLPAEHSGSNSNEFVLIDRATNRMKFDKKIKDDFSEIKSNSPSKPISCPSIKRIKIDIRDLKMDPILKSTPGDDIQYVCISKHLCGVATDLTLRCIGNSSILHGDDNNGCNPKLKAICIAMCCRHVCDYGDYVNRSYVTSLVEKYRAHGSILTYETFFRVLTKLCSWGTCGRKPGTAITDIVNVVESFEGAEPYTITIKERENIGLMARRVIDEGRLVYVKEKFTEFNAELIRYVESDVSLENVAMLVYKK", "text": "FUNCTION: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the methyltransferase TRM13 family."}
{"protein": "ATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDRDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTESTDVAQLPSRVPRDAARYHFFLYKHTHEGDLLESVVFIYSMPGYKCSIEERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFKQAFAKPKGPGGKRGHKRLIRGPGENGDDS", "text": "FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, perinuclear region Cell projection, stereocilium Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin subfamily."}
{"protein": "MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI", "text": "FUNCTION: Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:17493578, PubMed:1851637, PubMed:8319693, PubMed:8500694, PubMed:18311922, PubMed:32404334). Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to the specific bioactive lipid (12S)-hydroperoxyeicosatetraenoate/(12S)-HPETE (PubMed:17493578, PubMed:22984144, PubMed:24282679, PubMed:8319693, PubMed:8500694). Through the production of bioactive lipids like (12S)- HPETE it regulates different biological processes including platelet activation (PubMed:8319693, PubMed:8500694). It can also catalyze the epoxidation of double bonds of polyunsaturated fatty acids such as (14S)-hydroperoxy-docosahexaenoate/(14S)-HPDHA resulting in the formation of (13S,14S)-epoxy-DHA (PubMed:23504711). Furthermore, it may participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro- resolving mediators (SPMs) like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively down-regulate the immune response and have anti-aggregation properties with platelets (PubMed:32404334). An additional function involves a multistep process by which it transforms leukotriene A4/LTA4 into the bioactive lipids lipoxin A4/LXA4 and lipoxin B4/LXB4, both are vasoactive and LXA4 may regulate neutrophil function via occupancy of specific recognition sites (PubMed:8250832). Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to (13S)- hydroperoxyoctadecadienoate/ (13S-HPODE) (By similarity). Due to its role in regulating both the expression of the vascular endothelial growth factor (VEGF, an angiogenic factor involved in the survival and metastasis of solid tumors) and the expression of integrin beta-1 (known to affect tumor cell migration and proliferation), it can be regarded as protumorigenic (PubMed:9751607, PubMed:16638750, PubMed:22237009). Important for cell survival, as it may play a role not only in proliferation but also in the prevention of apoptosis in vascular smooth muscle cells (PubMed:23578768). SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane. Note=Membrane association is stimulated by EGF. SIMILARITY: Belongs to the lipoxygenase family."}
{"protein": "MTIWEISEKADYIAQRHRRLQDQWHIYCNSLVQGITLSKARLHHAMSCAPDKELCFVLFEHFRIYVTLADGFNSHTIEYYVETKDGEDKQRIAQAQLSIDGMIDGKVNIRDREQVLEHYLEKIAGVYDSLYTAIENNVPVNLSQLVKGQSPAA", "text": "FUNCTION: Regulatory protein for the formate hydrogenlyase system. Could act by directly interacting with FhlA or by preventing the binding of FhlA to the upstream activatory sequence (PubMed:1625581). Also down-regulates expression of the hyf operon (PubMed:12426353). FUNCTION: Regulatory protein for the formate hydrogenlyase system. Could act by directly interacting with FhlA or by preventing the binding of FhlA to the upstream activatory sequence (By similarity)."}
{"protein": "MVDMGGLDNLIANTAYLQARKTSDADSKELQRRRRSLMLPGPQSCEQLRQAMPADFNSLCEQQPIGRRLFRDFLATVPAYQEAMGFLEEVQSWELAEEGPAKGSTLQALVATCAVAPNPGQPHSFLSPALVTKCQAATTDEERASLVEQAKAEAMAFLQDQPFREFLVSPFYDKFLQWKVFEMQPVSDKYFEEFRVLGKGGFGEVCAVQVKNTGKMYACKKLDKKRLKKKSGEKMALSEKEILEKVSSPFVVSLAYAFESKSHLCLVMSLMNGGDLKFHIYSVGERGLDMNRVIFYSAQMTCGVLHLHSLGIVYRDLKPENVLLDDLGNCRLSDLGLAVQIQDGKPVTQRAGTNGYMAPEILMEKASYSYPVDWFAMGCSIYEMVAGRTPFKDYKEKISKEDLKQRTLKEEVRFQHQSFTEEAKDICRLFLAKTPEQRLGSREKSDDPRKHHFFKTINFPRLEAGLVDPPFVPDPSVVYAKDVDEIEDFSEVRGVEFDDKDKQFFQRFATGAVPIAWQEEIIETGLFEELNDPNRPAGCGEGNSSRSGVCLLL", "text": "FUNCTION: Retina-specific kinase involved in the shutoff of the photoresponse and adaptation to changing light conditions via cone opsin phosphorylation, including rhodopsin (RHO). SUBCELLULAR LOCATION: Membrane; Lipid- anchor. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily."}
{"protein": "MSEPNEVIEEFETYLDLEGKSPHTIRMYTYYVRRYLEWGGDLNAHSALRFLAHLRKNGYSNRSLNLVVQALRAYFRFEGLDDEAERLKPPKVPRSLPKALTREEVKRLLSVIPPTRKRDRLIVLLLYGAGLRVSELCNLKKDDVDLDRGLIVVRGGKGAKDRVVPIPKYLADEIRAYLESRSDESEYLLVEDRRRRKDKLSTRNVWYLLKRYGQKAGVEVTPHKLRHSFATHLLEEGVDIRAIQELLGHSNLSTTQIYTKVTVEHLRKAQEKAKLIEKLMGE", "text": "FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerA subfamily."}
{"protein": "MSDYVYDLMKKHHSVRQFKDKALSDETVQKLVEAGQSASTSSYLQTYSIIGVDDPEIKKQLKEVSGQPYVVDNGYLFVFVLDYYRHNLINENVDFDMQTSFESAEGLLVGAIDVALVSENVALAAEDMGYGIVYLGSLRNDVARVKEILDLPEYAFPLFGMAVGEPADDENGAPKPRLPFEHVFHKNVYNSNAKEQREAIQKYDEEISEYYKERTNGKRQETWSQQVAGFLSGKTRLDMLEELNKSGLMKK", "text": "FUNCTION: Reduces FMN, organic nitro compounds and disulfide DTNB. Involved in maintenance of the cellular redox state and the disulfide stress response (By similarity). SIMILARITY: Belongs to the flavin oxidoreductase frp family."}
{"protein": "MGRTRKANVCPRLSRRALGFYTRDAGVVQRTNLGILRALVCQESTKFKNVWTTHSKSPIAYERGRIYFDNYRCCVSSVASEPRKLYEMPKCSKSEKIEDALLWECPVGEILPDPSDYKSSLIALTAHNWLLRISATTGEILEKIYLASYCKFRYLSWDTPQEVIAVKSAQNKGSAAARQAGTQPPVLLYLAVFRVLPFSLVGILEINRKVFENVTDATLSHGILIVMYSSGLVRLYSFQAIIEQFMQQKLDLGCACSQGGTTGTVGEAPFGIPCNVKITDSPPPLFEVSSLENAFQIGGHPWHYIITPNKKKQKGVFHICALKDNSLAKNGIQEMECCSLESDWIYFHPDASGRIIHVGPNQVKVLKLSEVENNSSQHQISEDFVIWANREDRKENLITVTASGRVVKRNVNLLDDDPEQETFKVVDYEDELNLLSVVAVTQIDAEGKAHLDFHCNEYGTLLKSIPLVESWDVVCITTGTLSCKGFLYKRHLLGHVLVSPDSPVP", "text": "FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Nucleus, nucleolus Note=Has been shown in human and mouse to be a nucleolar protein, while sequence analysis programs clearly predict 2 transmembrane regions."}
{"protein": "MASKGSPSCRLVFCLLISAAVLRPGLGWYTVNSAYGDTIVMPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLSLSENYTLSINNAKISDEKRFVCMLVTEDNVFEAPTLVKVFKQPSKPEIVNRAAFLETEQLKKLGDCISRDSYPDGNITWYRNGKVLQPVDGEVSILFKKEIDPGTQLYTMTSSLEYKTTKSDIQMPFTCSVTYYGPSGQKTIYSEQAIFDIYYPTEQVTIQVLPPKNAIKEGDNITLQCLGNGNPPPEEFMFYLPGQAEGIRSSNTYTLTDVRRNATGDYKCSLIDQRNMAASTTITVHYLDLSLNPSGEVTKQIGDTLPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADDISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA", "text": "FUNCTION: Cell adhesion molecule that mediates both heterotypic cell- cell contacts via its interaction with CD6, as well as homotypic cell- cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6 (By similarity). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (By similarity). Mediates homotypic interactions with cells that express ALCAM. Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM (By similarity). Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon Cell projection, dendrite Note=Detected at the immunological synapse, i.e, at the contact zone between antigen- presenting dendritic cells and T-cells. Colocalizes with CD6 and the TCR/CD3 complex at the immunological synapse."}
{"protein": "MLLKNCETDKQRDIRYACLFKELDVKGNGQVTLDNLISAFEKNDHPLKGNDEAIKMLFTAMDVNKDSVVDLSDFKKYASNAESQIWNGFQRIDLDHDGKIGINEINRYLSDLDNQSICNNELNHELSNEKVNKFSRFFEWAFPKRKANIALRGQASHKKNTDNDRSKKTTDSDLYVTYDQWRDFLLLVPRKQGSRLHTAYSYFYLFNEDVDLSSEGDVTLINDFIRGFGFFIAGGISGVISRTCTAPFDRLKVFLIARTDLSSILLNSKTDLLAKNPNADINKISSPLAKAVKSLYRQGGIKAFYVGNGLNVIKVFPESSIKFGSFEVTKKIMTKLEGCRDTKDLSKFSTYIAGGLAGMAAQFSVYPIDTLKFRVQCAPLDTKLKGNNLLFQTAKDMFREGGGQIILQRCHSRYSGHISLCCIRFGDFFCLKKMVYCQTGKDPEPTTRSGHSKQPGCTSNGCIQWNCRSFCCLSNQSFKNKTTSPRNICTSLCV", "text": "FUNCTION: Calcium-dependent mitochondrial solute carrier. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSSTSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHIFLLMEKVNNSCQK", "text": "FUNCTION: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D- glycero-D-galacto-nononic acid (KDN) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CMP-NeuNAc synthase family."}
{"protein": "MDESALERYFEDSIANDSGFILEEELGLHSPALSSTQDSTYLSGRAGPSRESGAELDLSFLPDDLSTQEELGHHDNTAQAEDRAVSQDSAVCLDYDSQNSATPAATFDQQNPSLLGGGVHNSPFYSMTPMTPMTPMTPVTERSGIIPQLQNIVSTVNLGCPLDLKFIALQARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPARFMDFKIQNMVASCDVCFPIRLEGLVLTHQQFSSYEPELFPGLIYRMVKPRIVLLIFVSGKVVLTGAKERAEIYEAFENIYPILRGFRKQ", "text": "FUNCTION: TATA box-binding transcription factor. Members of the TBP family are differentially required to regulate transcription and development during early embryogenesis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TBP family."}
{"protein": "MNWRVVDSVVSTDTNSVFTLISSQQSFKLILWYKATFYLSSGDTLSINGASITVNNHPVELTLYRTTVYNARFWQTIVNSNTHCAGNHRQSVGRCGYRRKCKLLYCPFQKH", "text": "FUNCTION: Involved in the stabilization of the sigma stress factor RpoS. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IraM/RssC family."}
{"protein": "MEMLNAIILILFPIIGFVLIFSFPTKTLKAKTASPSNPTSYQLIGSILSFNKNRHRLLQWYTDLLRLSPSQTITVDLLFGRRTIITANPENVEHILKTNFYNFPKGKPFTDLLGDLLGGGIFNSDGELWSSQRKLASHEFTMRSLREFTFEILREEVQNRLIPVLSSAVDCGETVDFQEVLKRFAFDVVCKVSLGWDPDCLDLTRPVPELVKAFDVAAEISARRATEPVYAVWKVKRFLNVGSEKRLREAIKTVHLSVSEIIRAKKKSLDIGGDVSDKQDLLSRFLAAGHGEEAVRDSVISFIMAGRDTTSAAMTWLFWLLSQNDDVETKILDELRNKGSLGLGFEDLREMSYTKACLCEAMRLYPPVAWDSKHAANDDILPDGTPLKKGDKVTYFPYGMGRMEKVWGKDWDEFKPNRWFEEEPSYGTKPVLKSVSSFKFPVFQAGPRVCIGKEMAFTQMKYVVGSVLSRFKIIPVCNNRPVFVPLLTAHMAGGLKVKIKRREQCDSMYI", "text": "FUNCTION: Hydroxylase involved in the oxidation of the plant hormone jasmonoyl-L-isoleucine (JA-Ile), a bioactive phytohormone of the jasmonate-mediated signaling pathway. Converts JA-Ile to 12-hydroxy-JA- Ile. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "KLSGCFGFKLDRIGTMSGLGC", "text": "FUNCTION: Scorpion venom natriuretic peptide that increases the perfusion pressure, glomerular filtration rate and urinary flow in the isolated perfused rat kidney assay. Induces a decrease of the percentages of renal transport for sodium, potassium and chloride and an increase of the urinary cGMP concentration. Also down-regulates the mRNA expression of natriuretic peptide receptor-A (NPR1) in the kidneys whereas it up-regulates those of NPR-B (NPR2), NPR-C (NPR3) and guanylyl cyclase C (GUCY2C) mRNAs. May exhibit hypotensive and vasodepressor activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family."}
{"protein": "MSSGLWNQEKVTSPYWEERLFYLLLQECSVTDKQTQKLLRVPKGSIGQYIQDRSVGHSRVPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRIRLSKGLQVDVGSPVRVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTVQVEPPPLEINSRVSLKVGESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTVLLHINDIIPDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPMPSSSGNAHGLEVGSLAEVKENPPFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHTYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK", "text": "FUNCTION: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Negatively regulates NF- kappa-B activation by deubiquitinating upstream signaling factors. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (By similarity). Removes also 'Lys-63'-linked polyubiquitin chains of MAP3K1 and MA3P3K3, which inhibit their interaction with MAP2K1 and MAP2K2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, cilium basal body Note=Detected at the microtubule cytoskeleton during interphase (By similarity). Detected at the midbody during telophase (By similarity). During metaphase, it remains localized to the centrosome but is also present along the spindle (By similarity). SIMILARITY: Belongs to the peptidase C19 family."}
{"protein": "MAQACWGCYPWLVLICACAWGHPKSLNQREDVRNCSTSPPYLPVTAVNTTAQLTALREQMLTQNLSAYIIPDTDAHMSEYIGECDQRRAWITGFIGSAGIAVVTERKAALWTDSRYWTQAERQMDCNWELHKEVSTGHIVTWLLTEIPVGGRVGFDPFLFSIDSWESYDVALQDADRELVSITVNLVDLVWGSERPPLPNAPIYALQEAFAGSTWQEKVSNIRSQMQKHHERPTAVLLSALDETAWLFNLRSSDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLQYLNSSCNSSMCVQLEDYSQIRDSIQAYTSGDVKIWIGTRYTSYGLYEVIPKEKLVEDDYSPVMITKAVKNSREQALLKASHVRDAVAVIRYLAWLEKNVPTGTVDEFSGAKRVEEFRGEEEFFSGPSFETISASGLNAALAHYSPTKELHRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLVFPAATSGRVVEAFARKALWDVGLNYGHGTGHGIGNFLCVHEWPVGFQYGNIPMAEGMFTSIEPGYYQDGEFGIRLEDVALVVEAKTKYPGTYLTFEVVSLVPYDRKLIDVSLLSPEQLQYLNRYYQAIREKVGPELQRRGLLEELSWLQRHTEPLSARAAPTTSLGSLMTVSALAILGWSV", "text": "FUNCTION: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MNTATGVIALLVLATVIGCIEAEDTRADLQGGEAAEKVFRRSPTCIPSGQPCPYNENYCSQSCTFKENENANTVKRCD", "text": "FUNCTION: Insecticidal toxin that reversibly and voltage-independently blocks both mid-low- (M-LVA) and high-voltage-activated (HVA) calcium channels (Cav) in cockroach DUM neurons. Also causes a modest block of insect sodium channel currents (Nav). Induces potent excitatory symptoms, followed by flaccid paralysis leading to death in house crickets (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 01 (omega toxin) subfamily."}
{"protein": "MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTAGTSDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQVNGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDAKIAEQRFGINIPHKFNVHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLISRSTLRRQGKEGSKEGNGIGVNSSSRFGIDNFEFIRVLGKGSFGKVMLARIKETGELYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHEKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHEILRHPFFKEIDWAQLNHRQLEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQL", "text": "FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1- CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization. SUBCELLULAR LOCATION: Cytoplasm Note=Associates with cell membrane during keratinocytes differentiation. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily."}
{"protein": "MKITSLHFLIFHKNLNYVSSKVKAKKIFYQRALNNIYLCTIRTMIVDIAEIKKRDNHALDTQESQELVNKIKEIKNSDEQNNSNNNNNNSSSSNFCSNNNSPFSHKETKLMVKEEVPNSIVKNILNNNSCATSIINNKFYTQINNIIPVKPEAMKEENINVSTVNTENDISKEKKENSHYFCDEIKVMKKEYSKDDFVTDVKLEMNDKEEEEEEKQKIGQESTHINIKVEKDTFNECNNSNVNEKKRNRSVDIHNELSNKRILTEDVVVKCNIKNDVKIIVTWNMNSITVRYKNKKKWDEFMNFFNNLNADVLCFQEVRLPAMNLSEPCDNKNKNKNKNDGIRDRGKIKNSDQKSLADYEIMEQILNDDFKDYNAYFSLANIKYSGQLVLVKKNIHIESIRYNLFFENNAHIHHDEGRVILVEFSNFFLLSTYTPNNGFDHVKFERRRLFDEQLQKFVTILRNEKQKPLVWTGDLNIAPEDIDLSHPAEFRRMKKGNVPKEFIGQPGCTDFERKNFQKILTAGNLVDSYRYLQNIKLNEDKKNNIKHTPNINDNIYTWRCPFLLGKSCNKAMRIDHFIVSKEFLNRINKIHIQGFSVFHNNFYGSDHCPVILYLKNE", "text": "FUNCTION: Multifunctional protein that plays a central role in mitochondrial DNA base excision repair (BER) pathway induced by oxidative stress. Has apurinic/apyrimidinic (AP) endonuclease activity towards double-stranded DNA (dsDNA) (PubMed:33743509). Has nucleotide incision repair (NIR) activity; acts on dsDNA with oxidized bases thymine glycol and 5,6-dihydro-2'-deoxyuridine (PubMed:33743509). Has 3'-5' exonuclease; can use dsDNA templates with 3'-OH termini including blunt-end, gapped and mismatched 3'-recessed (PubMed:33743509). Has 3'- phosphatase activity; cleaves 3'-phosphate from blunt, recessed and gapped dsDNA templates, followed by 3'-5' exonuclease activity (PubMed:33743509). Has RNase H-like activity; cleaves RNA on 3'- recessed RNA-DNA duplex (PubMed:33743509). Plays a role in merosome infection of host erythrocytes (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family."}
{"protein": "MLYLILFLIAPIYAGVLLPTKPSIDPFYNAPEGFKNATVGDILQFRKTPKSITGGFVPLNVQNSWQFLVRSEDSFGNPNVIVTTVIEPVNADPSKIASYQVSENAARADCAPSYALQFGSDVSTLATQAETYLLAPLLDKGYYVVSPDYEGPKSTFTVGKQSGQAVLNSIRASLKSGKITNIAEDAKVLMWGYSGGSLASGWAAALQPDYAPELSRNLLGVALGGFITNVTATVEATDDTIFAGIAANVLGGIANEYPEFKSILQNDTNKSSIFNKINNHCLTDSFIKYVGARFLTGDNKVFKSGWNIFKNLVVSKIVKDNGLVYQKQLIPTIPVFIYHGSMDQISPILNPKKTYQNWCDAGISSIEFAEDLTNGHFTESIVGAPAALTWIIDRFSNKPPVDGCQHVVRTTNYEYPNVSSSILDYFKAAMDVVAQQGLGPNIQKDQLEIKSNL", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "SPPVCGNKILEQGEDCDCGSPANCQDRCCNAATCKLTPGSQCNYGECCDQCRFKKAGTVCRIARGDWNDDYCTGKSSDCPWNH", "text": "FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits aggregation induced by ADP, thrombin, platelet-activating factor and collagen. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily."}
{"protein": "MDDDQQFCLRWNNHQSTLISVFDTLLENETLVDCTLAAEGKFLKAHKVVLSACSPYFATLLQEQYDKHPIFILKDVKYQELRAMMDYMYRGEVNISQDQLAALLKAAESLQIKGLSDNRTGGGVAPKPESSGHHRGGKLSGAYTLEQTKRARLATGGAMDTSGDVSGSREGSSSPSRRRRKVRRRSMENDAHDNSNSSVLQAAASNQSILQQTGAGLAVSALVTTQLSSGPAAGTSSQASSTQQQQPLTSTNVTKKTESAKLTSSTAAPASGASASAAVQQAHLHQQQAQTTSDAINTENVQAQSQGGAQGVQGDDEDIDEGSAVGGPNSATGPNPASASASAVHAGVVVKQLASVVDKSSSNHKHKIKDNSVSSVGSEMVIEPKAEYDDDAHDENVEDLTLDEEDMTMEELDQTAGTSQGGEGSSQTYATWQHDRSQDELGLMAQDAQQRDPQDLSRKENTAPDVASTAEIQRSFQRSILNGKQRDEQKIQLPGSRRKRLSVTEVSDMLFEFYKTKSAKVPKAEQPHRQVSPTSGEILDPSTISAIAVYGTASETASKNLNADEVMRVQNATATRVVGAAAGAAASFHPRPKYTLKTAASSTEHTTAIPTSVLVANSAAALTPKPQAAVIAEALMRNGLHNFQQQLRAQEILRQQTPHRRIKEENDVEIAGGDITPTKILENLLRKQQERDLRHSECENEPGYSTEDDEEGRYHAFDDIHLMEQSGGKFGNNSGMGMFNANAHGGSASSILDAHQAFRNLEFTLSDYGGSSSNGSTTSPNGIGLDGEPVYECRHCGKKYRWKSTLRRHENVECGGKEPSHQCPYCPYKSKQRGNLGVHVRKHHTDLPQLPSKRRSKYSMNRENGMSGSMSDDSQGKLIIDFNGKGELETK", "text": "FUNCTION: Putative transcription factor required for axon growth and guidance in the central and peripheral nervous systems. Repels CNS axons away from the midline by promoting the expression of the midline repellent sli and its receptor robo. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSYKLTYFSIRGLAEPIRLFLVDQDIKFIDDRIAKDDFSSIKSQFQFGQLPCLYDGDQQIVQSGAILRHLARKYNLNGENEMETTYIDMFCEGVRDLHVKYTRMIYMAYETEKDPYIKSILPGELAKFEKLLATRGNGRNLILGDKISYADYALFEELDVHQILDPHCLDKFPLLKAFHQRMKDRPKLKEYCEKRDAAKVPVNGNGKQ", "text": "FUNCTION: Appears to play a central role in the parasite detoxification system. SIMILARITY: Belongs to the GST superfamily. Pi family."}
{"protein": "GQGCSYGCHPKNISISVESCGITEFILTTICEGQCYLEDPVYISHDEQKICNGDWSYEVKHIEGCPVGVTYPVARNCECTACNTGNTYCGRLPGYVPSCPSF", "text": "FUNCTION: Involved in gametogenesis and steroidogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family."}
{"protein": "MAGKLMRAVQYDGYGGGAAGLKHVEVPIPSPGKGEVLIKLEAISLNQLDWKLQNGMVRPFLPRKFPFIPATDVAGEVVRIGQDVKNFKPGDKVVAMLGSFGGGGLAEYGVASEKLTVHRPPEVSAAESSGLPIAGLTAHMALTQHIGLNLDKSGPHKNILITAASGGVGQYAVQLAKLGNTHVTATCGSRNFDLVKSLGADEVIDYKTPEGAALKSPSGKKYDAVIHCASPLPWSVFKPNLSKHGKVIDITPGPRVMLTSAMTKLTCSKKRLVTLLVVIKGEHLSYLVELMREGKLKTVIDSKFSLSKAEEAWAKSIDGHATGKIVVEP", "text": "FUNCTION: NADPH-dependent single-electron reducing quinone reductase (PubMed:20424175). Involved in haustorium initiation in parasitic plants through redox cycling of exogenous haustorium-inducing factors (PubMed:20424175). Can use 9,10-phenanthrenequinone (PAQ), 1,2- naphthoquinone, 5-hydroxy-1,4-naphthoquinone (juglone) and 2,6- dimethoxy-p-benzoquinone (DMBQ) as substrates, but has no activity with menadione, diamide, 2,3-dimethoxy-5-methyl-1,4-benzoquinone or 1,4- naphthoquinone (PubMed:20424175). SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
{"protein": "MVKVAYVQMNPQILEPDKNYSKAEKLIKEASKQGAQLVVLPELFDTGYNFETREEVFEIAQKIPEGETTTFLMDVARDTGVYIVAGTAEKDGDVLYNSAVVVGPRGFIGKYRKIHLFYREKFFFEPGDLGFRVFDLGFMKVGVMICFDWFFPESARTLALKGADVIAHPANLVMPYAPRAMPIRALENKVYTVTADRVGEERGLKFIGKSLIASPKAEVLSMASETEEEVGVAEIDLYLVRNKRINDLNDIFKDRREEYYFR", "text": "FUNCTION: Nitrilase that hydrolyzes preferentially aliphatic nitriles like malononitrile and fumaronitrile in vitro. These dinitriles are converted to the corresponding monoacid mononitriles, showing the enzyme is regioselective. Cannot hydrolyze compounds with a nitrile group bound to an aromatic ring or amino acid. Its biological role is unknown. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily."}
{"protein": "MAALKALVSGCGRLLRGLLAGPAATSWSRLPARGFREVVETQEGKTTIIEGRITATPKESPNPPNPSGQCPICRWNLKHKYNYDDVLLLSQFIRPHGGMLPRKITGLCQEEHRKIEECVKMAHRAGLLPNHRPRLPEGVVPKSKPQLNRYLTRWAPGSVKPIYKKGPRWNRVRMPVGSPLLRDNVCYSRTPWKLYH", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family. Mitochondrion-specific ribosomal protein mL66 subfamily."}
{"protein": "MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV", "text": "FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain family."}
{"protein": "MPLPSRASSTPKISKACVPCRTRKIKCNAAVVGLPCGSCVSRECPDECVLSARKRRTVKGRNAETPRSRKNIPDTNGSVLSPRQQQLPTNVSRQATDSSHSDPVEESIHASHTGSSLRNDTPHSRDRRPPGQTQADLLYLNILQDTVNDTSAAQTDASDHQSNDEPDDSFNSQIHHWNPPPQLDDVDNEYLAKKKVFELPPPRFMENIVKAYFDYVHPFAPILNRTDFIQSYRSGSCCLFLLHAVAAAASLYVTHDVLIGCGYQDRSTAQASFFSKAKLFHDFHCQGDPLSMLQGSMILGAIILDHPSDRDFQYWFHNSVRRASKMGVQNACLRDDGSQKLYRRIWWVLHNRDIFHFFINTQNMRLLANAPPIRPLTEADWETEDMEQWSGILSPISQAQKVSLIAQCELAQIFGNVMSVVTSSTPSAEEIHKRILPLDAWRTSLPERMQLMASFANGEKYHLEALTTSYRFECIMCRLLRRGRWQMSDGGLREWAQQRFRSAIFELDTIVKRVMINNTIQKLPTTFITTITALLALHIESALDAAESSLIRSMARISVQHTMLALDQIRDTPAIKRALPAFEIVLSKNKLYPMSTSDTEQISTIQTIPQDQTLSDGQILQPPPTDMTLPQDDQSFLYGDFIGFDFLDRWQMEQLDFTGIY", "text": "FUNCTION: Transcription factor that is involved in the formation of the two Fusaric acid derivatives, dehydrofusaric acid and fusarinolic acid, serving as a detoxification mechanism (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSLTAPLRAGQMNFYDEPYNPVLNLHIQPSVKDENQRSTWPIIDTSNTSTQIARAHFEKHPPNNLRKSNFFHFVIALYDRNSQPIEVERTQFAGFVEKEKEVDGQDTRNGIHYRLSLMFQNGIRSEHDLFVRLIDSSTKQAITYEGQDKNPEMCRVLLTHEVMCSRCCEKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVLCSSARIDGPLLAVSDNMFVHNNSKHGRRTKRTDASDDSEYSESAELPSSVPVIKALFPSEGWIQGGTQVVLIGENFFEGLQVAFGTASPNWGESVQLISPHAIRVTTPPKHSAGPVDVTLQYKSKTYSRGTPLRFSYITLAEPGIEYGFQRLQKLLPKYPGDPERLPKDQILKRAAELAEALYNRTSTESLSSYYHTQFDATSDYAARTHTSPRSTLPYGAGPPALSSAVYQTSYPTVNATPAANFLNTQTGFATFGAVNPFAATLQSSSRLS", "text": "FUNCTION: Transcription factor (PubMed:28056346). Involved in motor neuron fate determination and maintenance, acting as an activator of gene expression in a subset of motor neurons (PubMed:28056346, PubMed:18817768). May act in concert with GFI1 homolog pag-3 in motor neuron fate determination (PubMed:18817768). Required to maintain the expression of transcriptional repressors bnc-1 and cfi-1, which play roles in the cell fate of motor neurons (PubMed:28056346). May play a role in the expression of proteins essential for axonal pathfinding and/or neuronal differentiation in both sensory and motor neurons (PubMed:9502737). Cooperates with jmjd-3.1 and wdr-5.1 to ensure robust transdifferentiation of the Y rectal cell to the PDA motor neuron during larval development (PubMed:25124442). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the COE family."}
{"protein": "MSRYTGPRLKIMRALGVDLPGLGRKSMQERNQPPGQHGARKVAARKSEFGLQLMEKQKLRYNYGVTERQLRRVVLDAKRQKGVTGGKIVELLERRLDNLVFRAGFAPTTRLRANS", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS4 family."}
{"protein": "MTNTKGKRRGTRYMFSRPFRKHGVVPLATYMRIYKKGDIVDIKGMGTVQKGMPHKCYHGKTGRVYNVTQHAVGIIVNKQVKGKILAKRINVRIEHIKHSKSRDSFLKRVKENDQKKKEAKEKGTWVQLNGQPAPPREAHFVRTNGKEPELLEPIPYEFMA", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family."}
{"protein": "MVFRKSLLKLAVFALGACVAFSNANAAEGKLESIKSKGQLIVGVKNDVPHYALLDQATGEIKGFEVDVAKLLAKSILGDDKKIKLVAVNAKTRGPLLDNGSVDAVIATFTITPERKRIYNFSEPYYQDAIGLLVLKEKKYKSLADMKGANIGVAQAATTKKAIGEAAKKIGIDVKFSEFPDYPSIKAALDAKRVDAFSVDKSILLGYVDDKSEILPDSFEPQSYGIVTKKDDPAFAKYVDDFVKEHKNEIDALAKKWGL", "text": "FUNCTION: Common antigen and a major cell adherence molecule. Most probably involved, with PEB1C, in a binding-protein-dependent transport system for an amino acid. May be involved in binding to intestinal cells. SUBCELLULAR LOCATION: Cell surface. SIMILARITY: Belongs to the bacterial solute-binding protein 3 family."}
{"protein": "MAVLQKSMSFSLMGTLAASCLLLIALWAQEANALPINTRCKLEVSNFQQPYIVNRTFMLAKEVSLADNNTDVWLIGEKLFRGVSAKDQCYLMKQVLNFTLEDVLLPQSDRFQPYMQEVVPFLTKLSNQLSSCHISGDDQNIQKNVRRLKETVKKLGESGEIKAIGELDLLFMSLRNACV", "text": "FUNCTION: Cytokine that contributes to the inflammatory response in vivo. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-10 family."}
{"protein": "MTTTIRQFTSSSSIKGSSGLGGGSSRTSCRLSGGLGAGSCRLGSAGGLGSTLGGSSYSSCYSFGSGGGYGSSFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQRQAPGPARDYSQYYRTIEELQNKILTATVDNANILLQIDNARLAADDFRTKFETEQALRLSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGESEISELRRTMQALEIELQSQLSMKASLEGNLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLTQYKKEPVTTRQVRTIVEEVQDGKVISSREQVHQTTR", "text": "FUNCTION: Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair. Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state. Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway. Involved in tissue repair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial 'stem cells'. Acts as a promoter of epithelial proliferation by acting a regulator of immune response in skin: promotes Th1/Th17-dominated immune environment contributing to the development of basaloid skin tumors. May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGATEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGNDPTSVDPMVLEQYVVVADYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVVQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKLGPSSPAHSGALDLDGVSRHQNAMGREKELLNNQRDGRFEGRLVPDGDVKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKSLSGWWYIQMEDKEGWAPATFIDKYKKTSSASRPNFLAPLPHEMTQLRLGDAAATENNTGPEAVGPSRPLPEAPHGAVDSGMLWSKDWKGGKEAPRKASSDLSASTGYEEISDPTQEEKPSLPPRKESIIKSEEELLERERQKMEPLRGSSPKPPGMILPMIPAKHAPLARDSRKPEPKLDKSKFPLRNDMGLECGHKVLAKEVKKPNLRPISRSKAELSEEKVDPTSQNLFMKSRPQVRPKPTPSPKTEPAQSEDHVDIYNLRSKLRPAKSQEKALLDGESHHAAGSHDTALSRSFLPGEGPGHGQDRSGRQDGLSPKETPCRAPPRPAKTTDPGPKNVPVPVQEATLQQRPVVPPRRPPPPKKTSSSPLSCRPLPEVRGAQREESRVAPAAGRALLVPPKAKPFLSNSSVGQDDMRGKGGLGPRVTGKVGETREKAASFLNADGPKDSLYVAVANFEGDEDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP", "text": "FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation. SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC- transformed cells. SIMILARITY: Belongs to the SH3PXD2 family."}
{"protein": "MASLIQVRDLLALRGRMEAAQISQTLNTPQPMINAMLKQLESMGKAVRIQEEPDGCLSGSCKSCPEGKACLHEWWALR", "text": "FUNCTION: May function as a transcriptional regulator that controls feoABC expression. SIMILARITY: Belongs to the FeoC family."}
{"protein": "MTMGDKKSPTRPKRQAKPAADEGFWDCSVCTFRNSAEAFKCSICDVRKGTSTRKPRINSQLVAQQVAQQYATPPPPKKEKKEKVEKPDKEKPEKDKDISPSVTKKNTNKKTKPKSDILKDPPSEANSIQSANATTKTSETNHTSRPRLKNVDRSTAQQLAVTVGNVTVIITDFKEKTRSSSTSSSTVTSSAGSEQQNQSSSGSESTDKGSSRSSTPKGDMSAVNDESF", "text": "FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:22325148, PubMed:28596365). Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (PubMed:28596365). May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites (PubMed:22325148, PubMed:28596365). Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes (By similarity). May also regulate the ubiquitin-mediated proteasomal degradation of other proteins like FANK1 to regulate apoptosis (PubMed:17874297). May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1 (By similarity). May bind to DNA (PubMed:19170609). May play a role in the repression of tumor growth and metastasis in breast cancer by down-regulating SRRM3 (PubMed:27748911). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus, nucleoplasm Note=Primarily found in the nucleus. Detected in a punctate pattern likely to represent Polycomb group (PcG) bodies."}
{"protein": "MFLIDSHCHIDQMNIDQKNDDLLHQEIEKILNKAYENHVKKFLTVSTSIQNFYKTKKLLSTYDSIFYSCGIHPLYCQKEIECLNELKKLSYDKCVIALGETGLDYYYSFETKNLQEKFFREHIRIAITLNKPIIIHSRNAIKDTIKILKEENAEKCGGILHSFTESEKSAFELLDMGFYISFSGIITFKKSIELCNTLKKIPLEKLLIETDSPYLAPIPYRGKKNQPAYLLDIAKKIALIKEISLKELAKITTNNFFTLFNLNF", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family."}
{"protein": "MSLLMISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTFLQQKWQQVWQEINMECKHVKDIMSTLEGFKLDSSPVKTTQHEFPSHDGEVWSLPVPVERRPSPGPRKRQSVQCNDNKSHNNRFSAAAKGPNLPSARNANNVKMKPVRAREKKDALIKNKSSADVSETEVKRFDGSGYDKDLIEALERDIISQNPNIRWDDIADLEEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNISSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGASENEDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRINLKELELADDVNIECIAENMDGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSRDDMHMPTTMEDFEMALKKVSKSVSASDIEKYEKWIFEFG", "text": "FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. In mitotic spindles this could allow depolymerization of the microtubule end proximal to the centrosome, and subsequent poleward microtubule flux. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, spindle Note=Predominantly cytoplasmic. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with katnb1. SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily."}
{"protein": "MFPIASRRILLNASVLPLRLCNRNFTTTRISYNVIQDLYLRELKDTKLAPSTLQDAEGNVKPWNPPQKPNLPELELQGPEALKAYTEQNVETAHVAKESEEGESEPIEEDWLVLDDAEETKESH", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase h subunit family."}
{"protein": "MAEFLDDQETRLCDNCKKEIPVFNFTIHEIHCQRNIGMCPICKEPFPKSDMETHMAAEHCQVTCKCNKKLEKRLLKKHEETECPLRLAVCQHCDLELSILKLKEHEDYCGARTELCGNCGRNVLVKDLKTHPEVCGREGEEKRNEVAIPPNAYDESWGQDGIWIASQLLRQIEALDPPMRLPQRPLRAFESDVFHDRTTNQRNITAQVSIQNNLFEEQERQERNRGQQPPKEGGEDGANLDFMLALSLQNEGQASSVAEQDFWRAVCEADQSHGGPSSLSDIKGAADETMLPCEFCEELYPEELLIDHQTSCNPSRALPSLNTGSSSPRGVEEHDVIFQNFLQQAASKQLDSLMGLSSSRLVEESIIIPCEFCGVQLEEEVLFHHQDQCDQRPATATNHVTEGIPRLDSQPQENSPELPRRRVRHQGDLSSGYLDDIKQETANGPTSCLPPSRPFNNMTATYNQLSRSTSGPRPGCQPSPPRVLKLNNSDSQDIQGRNQNSQNGAIAPGHISVIRPPQSLYPENIVPSFPHGPAGRYGASGRSEGGRNSRVTPAAANYRSRTAKAKPSKQQGAGDAEEEEEE", "text": "FUNCTION: Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity)."}
{"protein": "MMTVAAEIRGSNPEKLLAPVLSAFWDEDESWTLDVYRRHEGYEGLRKALAMAPDDLIAYVKESGLRGRGGAGFPTGMKWQFIPQGDGKPHYLVVNADESEPGTCKDIPLLFANPHSLIEGIVIACYAIRSSHAFIYLRGEVVPVLRRLHEAVREAYAAGFLGENILGSGLDLTLTVHAGAGAYICGEETALLDSLEGRRGQPRLRPPFPAVAGLYACPTVVNNVESIASVPAILNKGKDWFRSMGSEKSPGFTLYSLSGHVAGPGQYEAPLGITLRQLLDMSGGMRPGHRLKFWTPGGSSTPMFTDEHLDVPLDYEGVGAAGSMLGTKALQCFDETTCVVRAVTRWTEFYAHESCGKCTPCREGTYWLVQLLRDIEAGKGQMSDLDKLNDIADNINGKSFCALGDGAASPIFSSLKYFREEYEEHITGRGCPFDPAKSTAWADRTEVKA", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 51 kDa subunit family."}
{"protein": "MADSASESDTDGAGGNSSSSAAMQSSCSSTSGGGGGGGGGGGGGKSGGIVISPFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYFNEMSAQGLRPRTVSSPIPYTPSPSSSRPISPGLSYASHTVGFTPPTSLTRAGMSYYNSPGLHVQHMGTSHGITRPSPRRSNSPDKFKRPTPPPSPNTQTPVQPPPPPPPPPMQPTVPSAATSQPTPSQHSAHPSSQP", "text": "SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton Note=May be a cytoskeletal protein."}
{"protein": "MNRFTAYAALFFMFSLCSTAKEAGFLHPAFNFRGTSTMSASSGDYSAAPTPLYKSWALPSSLNLTTQPPPPLTDRSYYELVQALTSKMRLDCQTVGDMTWRHLSEMLFASWNSVKEVSLKAASVTLWAIINIWFGLYWTLARLITLFLWTFSIEALCLILLGCITSLIYKGALSLSEHLPVFLFMSPLKIIWRAAFSKRNYKNERAVEGYKGFSVPQKPPKSAVIELQHENGSHLGYANCIRLYSGENALVTAEHCLEGAFATSLKTGNRIPMSTFFPIFKSARNDISILVGPPNWEGLLSVKGAHFITADKIGKGPASFYTLEKGEWMCHSATIDGAHHQFVSVLCNTGPGYSGTGFWSSKNLLGVLKGFPLEEECNYNVMSVIPSIPGITSPNYVFESTAVKGRVFSDEAVKELEREASEAVKKLARFKSLTDKNWADDYDSDEDYGLEREAATNAPAEKTAQTNSAEKTAPSTSAEKTALTNKPLNGQAAPSAKTNGNSDIPDAATSAPPMDKMVEQIITAMVGRINLSEIEEKIVSRVSQKALQKPKQKKRGRRGGKNKQNSLPPTSTQSTSGAPKKEAAPQASGSAGTSRATTTPAPEAKPSGGKNSAKFTPSWRIKQQDSAGQKPDLKLNSKA", "text": "FUNCTION: Precursor from which the VPg molecule is probably released at the onset of the RNA synthesis. Essential for virus replication. Participates, together with the proteins P0 and P7, in the inhibition of the induction of aphid-induced host phytohormones (PubMed:31758809). This could play a role in the attraction to the infected plants by aphids (PubMed:31758809). SUBCELLULAR LOCATION: [Protein P1]: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase S39B family."}
{"protein": "MAARTSQRALARVASGCHPKSTTVTEATARGSARDVRHLAACGVLINRTLPPCAAVLPKEICARTFFRISAPLVNKRKEYSERRILGYSMQEMYDVVSGMEDYQHFVPWCKKSDIISRRSGYCKTRLEVGFPPVLERYTSIVTLVKPHLVKASCTDGKLFNHLETIWRFSPGLPGYPRTCTLDFSISFEFRSLLHSQLATLFFDEVVKQMVAAFERRACKLYGPETNIPRELMLHEIHHT", "text": "FUNCTION: Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ10 family."}
{"protein": "MVHFTPEDKTNITSVWTKVDVEDVGGESLARLLVVYPWTQRFFDSFGNLSSASAVMGNPKVKAHGKKVLTSFGEGVKNMDNLKGTFAKLSELHCDKLHVDPENFRLLGNVLIIVLASRFGKEFTPEVQASWQKLVSGVSSALGHKYH", "text": "FUNCTION: Hemoglobin epsilon chain is a beta-type chain found in early embryos. SIMILARITY: Belongs to the globin family."}
{"protein": "MMMKYEAVIIGGGPVGFMLASELAIAGVGTCVIERLEKPVPHSKALTLHPRTLELLEMRGILERFVSKGSKIPTGHFSMLDTRLDFSGLDTSCPYTLLLPQSKTEKLLEDHARSLGTEVFRGAEALAVTQNGEAVQTIFKDRDGSVRTITSKFAVGADGAGSTVRKQAKIEFPGTDSTVTAALGDVVLLSPPPSGVLSLCTKEGGVMIVPLSPDRYRVVVISPYRTQTPKDVPVTEEELKADLLRICGTDFGLTDPSWMSRFGNAARQAKRYRDGRIFLAGDAAHIHFPAGGQGLNVGLQDAMNLGWKLAAAIKGSAPSWLLDSYHDERHPAAEGLLRNTEAQTKLIDFTQAGLHLRSMMSELLAFPDVNRYVAGQISALDVRYEADRTMPPNRLNGARLPDMKLILSDGNSERLYSFLQNGTFVLLSLRQEADDHIEVKGLRTVTASLAEPNEKLRNVHTILIRPDGHVAWAVDASAPDCSEVIQKGISRWFSVTSRV", "text": "SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family."}
{"protein": "MQTDEPTGTATSAIRIPPLISLRTTLMVAGLLGNVVAVAAYGLFSRTERYGAVGNPDPGSFIGVAEPVGYFGASLSSALCLGALIYFVMMVWPQADGLIDAQAFRIHLAEERVSIGWLAFALTMVVVQAANDSGVTPAELRTGAALFNAITTSETSRAWIVVTICALLVTLTLRVIIRYSDHFVLLIPAVIGVIATAVTGNAGQGPDHDYATSAVIVFALAIAALSGLKITAALTEVTPSRAVLIVQVVCGVLALAYGAELVYLLSPGAAMIDSDFGRLGLVAGVLVTLVCFSDCWALVMGRPHSDHRTRLTALAMMAVTAATAAMSVQTAPRFLTHRFTAWDVFLGYELPQPPNIVRFFTVWRFDSLIGATAIVLGIGYVAGFVRVRRAGNTWPVGRLVAWLTGCVALVFTSSSGVRTYGSAMFSVHMAEHMTLNMFIPVLLVLGGPVTLALRALSAAGDGQQPGPREWLTWLMHSSVTAFLSHPVTNFILFVGSPYIVYFTPLFDTLVRYHWGHEFMAIHFLLVGYIFYWAIIGIDPGPRRLPYLARIGLLFAVMPFHAFFGIALMTMTSAISAEFYRSVNLPWLASIDADQHIGGAIAWSATELPVIIVIVALMAQWARQDHRVAVREDRHADSTYADDDLNAYNAMLRELSRMRR", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.tuberculosis Rv0102."}
{"protein": "MARNKLVSGSHGIWKYFNPAFYLRRPRRLALLIILFVSVSMVVWDRQSLSRDYQFEVSKLNEEVLRLQQMLEEIKSVTEDVSVNSLKDVQEDPVDAQRMQRVKEAMVHAWSSYEKYAWGQDELQPQTKDGVDSFGGLGATMIDALDTLYIMGLDEQFQKAREWVASSLDFDKDYAASMFETTIRVVGGLLSAYDLSGDKIFLEKAMDIADRLLPAWDTQSGIPYNIINLKHGNAHNPTWAGGDSILADSGTEQLEFIALSQRTGDPKYQQKVEKVISVLNKNFPADGLLPIYINPDTANPSQSTITFGAMGDSFYEYLLKVWVFGNKTSAVKHYRDMWEKSMNGLLSLVKKSTPLSFTYICEKSGNSLIDKMDELACFAPGMLALGASGYSDPAEGKKFLTLAEELAWTCYNFYQSTPTKLAGENYFFNSGSDMSVGTSWNILRPETVESLFYLWRLTGNKTYQEWGWNIFEAFEKNSRIESGYVGLKDVNTGVKDNKMQSFFLAETLKYLYLLFSPTTVIPLDEWVFNTEAHPLKIKSRNDQVNLKQSNKVLLRKPAFRIRQRHYGRITKK", "text": "FUNCTION: Class I alpha-mannosidase essential for early N-glycan processing. Progressively trims alpha-1,2-linked mannose residues. Produces Man(5)GlcNAc(2) from Man(8)GlcNAc(2), but only Man(6)GlcNAc(2) from Man(9)GlcNAc(2). Has difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 47 family."}
{"protein": "MASTDPGTGTPLDESVPGIKRAMRQSTKNTPRAGRNLPAAIAVGLSIGGVLVATLVFAPRIWVVLCAGAIFVASHEVVRRLREAGYVIPAIPLLIGGQFTVWLTWPYRTVGALAGFGATVVVCMIWRLVMHDNSKQHESREALAGPPVSNYLRDASATVFLAAWVPLFASFAALLVYPKDGAGRVFCLMIAVVASDVGGYTVGVLFGKHPLVPRISPNKSWEGFAGSLVCGTTATILTATFLAGKTPWVGALLSFVLVLTCTLGDLVESQVKRDLGIKDMGRLLPGHGGLMDRLDGVLPSAVVAWTMLTLLP", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDS family."}
{"protein": "MEMPTSDGSLSEGLISYLIRERGSAPQCAPEKHLSRLKQDVANTKMELKATLKEAQLASCSVELLLPLFKNTVEGISLENANLSASSLKKIFEQNDILSKELDTFNRVKLALEHLIKQTDYEQIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQFLQISYVTMFR", "text": "FUNCTION: Acts as a suppressor of ciliogenesis, specifically, the initiation of ciliogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Cytoplasm, cytoskeleton, cilium basal body Note=Localizes to centrioles in proliferative cells and basal bodies in ciliated cells. Disappears during ciliogenesis but reappears, albeit at a lower levels once ciliogenesis has completed. SIMILARITY: Belongs to the ODF2 family."}
{"protein": "MALSDEQVKSELSKMQAFIEKEAKEKAKEIKLKADEEYEIEKASIVRSETAAIDSTYEQKLKKASLAQQITKSTIGNKTRLRILSTKDEVLHEIFDEAEAELKKITKDKKQYKPVLVGLIEEGVLALMEPKVSIKVREQDVDVAKEAITEAAKNFEEKAKFKVEISIDDKNFLAKDIAGGIVVVNGSGKIEVDNTLEERLKILSEEALPAIRLELFGPSTTRKFFD", "text": "FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the V-ATPase E subunit family."}
{"protein": "MAEFETTFADLGLKAPILEALTDLGYEKPSPIQAECIPHLLDGRDVLGMAQTGSGKTAAFSLPLLNNIDPELRAPQILVLAPTRELAVQVAEAMTEFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTAYGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQALERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLSKRRLEKFAAKVQQQLESSDLDQYRALLAKIHATAEGEELDVETLAAALLKMAQGERSLIVPPVAPMRPRREFRDRDDSFDRRGDRNDRGPRGDREDRPKRERRDVGDMELYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLLGDAQPRTERRGGGERREGGRGFGGERREGGRGFGGERREGGRGEGRRFSGERREGRAPGRDDASAPRRDDSAGRRRFGGDA", "text": "FUNCTION: DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. DeaD/CsdA subfamily."}
{"protein": "MDLTGAHMLKIHRPSIDHPFGVDLWHLFEQLSIKTIGWNPSEFEYIPGKTPMSQWSSVIVSITAYYVIILSGRAIMTNRKPLKQRRLFQLHNFILTIISGALLALLVEEVFRNYMRNGLFYCVCDSRHFTQRLVTLYYLNYLTKYLELMDTVFLFLKKKPLAFLHCYHHGITALLCFTQLLGRTSVQWGVIGLNLYVHVIMYSYYFLAACGRRVWWKQWVTRVQIIQFVLDLILCYFGTYSHIAFRYFPWLPHVGDCSGSLFAAFFGCGVLSSYLFLFIGFYINTYIKRGAKKNQRKAAGKADNTSVAAAAGSEALAATTATNASPFSARSRKL", "text": "FUNCTION: May be involved in the synthesis of very long chain fatty acids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ELO family."}
{"protein": "MNYQRSFEDLEFNAIKWWPQELSATVAEASVLPILISSQDLFISILKLSGTHPEQIFDVINAAQISANLFLKHLVVLADYGGEMIKRLGKEFQEIFPRMDSTLEYYMNYTFKGEQYTYIFKKLPIKGLDNSKLAIDGKAIIEIKPLSDLYRDMIMILLYGSTTEQFNLAGLEKCEIGTILGKNEIIYTYITQKYLYVSRITNGANTNSLGQIAQTYVCDILSKYLPNDYSVTRNGKILLSDLNSQDSTKTSFDILVEFADKKVGIEVSFQVTTNSTIERKAGQARDRQNRMHAHYYWIAYVIDGAGNFERSGAVRAICRYSDCTVAYSESEIAVLAAFIQEKFNA", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGYRCC-3' and cleaves after G-1."}
{"protein": "MALNLQDKQAIVAEVSEVAKGALSAVVADSRGVTVDKMTELRKAGREAGVYMRVVRNTLLRRAVEGTPFECLKDAFVGPTLIAYSMEHPGAAARLFKEFAKANAKFEVKAAAFEGELIPASQIDRLATLPTYEEAIARLMATMKEASAGKLVRTLAAVRDAKEAA", "text": "FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. FUNCTION: Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA. FUNCTION: Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uL10 family. SIMILARITY: Belongs to the universal ribosomal protein uL10 family."}
{"protein": "MHLRIHARRSPPRRPAWTLGIWFLFWGCIVSSVWSSSNVASSSSTSSSPGSHSQHEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSILGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTGGELVIPLLVEDPLATPPIATRAPSITLPPTFRPLLTIIETTKDSLSMTSEAGLPCLSDQGSDGCDDDGLVISGYGSGETFDSNLPPTDDEDFYTTFSLVTDKSLSTSIFEGGYKAHAPKWESKDFRPNKVSETSRTTTTSLSPELIRFTASSSSGMVPKLPAGKMNNRDLKPQPDIVLLPLPTAYELDSTKLKSPLITSPMFRNVPTANPTEPGIRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLMKEKQQSSKSGHKKQKNKDREYYV", "text": "FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling (By similarity). SUBCELLULAR LOCATION: Presynaptic cell membrane; Single- pass type I membrane protein. SIMILARITY: Belongs to the neurexin family."}
{"protein": "MRRMTIGTVDGLHYELHGGPIAGREVVLLSSGLGGSGAFWAPQMQALTQRWPVVTYDHRGTGRSVRELPPRYTLAHMADDMVKVMDALGLAKAHVVGHAAGGNAGLQLALDHPDRLAKLVVVNGWSRPDPHIRRCFDTRLHLLNDTGPEAYVHAQPIFLYPADWISRNHTRLMAEEAHHVAAFPPREVMLARINALLAFDIDARLEDITHRVLISASADDMLVPMSCSQRLAGRLPNADFQQVAWGGHGFTVTDPETFNEALVSFLEGA", "text": "FUNCTION: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously. SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD family."}
{"protein": "MAAGQGGWLRPALGLRLLLATAFQAVSALGAEFASEACRELGFSSNLLCSSCDLLGQFNLLPLDPVCRGCCQEEAQFETKKLYAGAILEVCGUKLGRFPQVQAFVRSDKPKLFRGLQIKYVRGSDPVLKLLDDNGNIAEELSILKWNTDSVEEFLSEKLERI", "text": "FUNCTION: May be involved in redox reactions associated with the formation of disulfide bonds (By similarity). May contribute to the quality control of protein folding in the endoplasmic reticulum. May regulate protein folding by enhancing the catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Note=The association with UGGT1/UGCGL1 is essential for its retention in the endoplasmic reticulum. SIMILARITY: Belongs to the selenoprotein M/F family."}
{"protein": "MKRSKELITKNHSQEETSILRCWKCRKCIASSGCFMEYFENQVIKDKDDSVDAQNICHVWHMNIESLPEWISCLIQKAQWTVGKLNCPFCGARLGGFNFVSTPKCSCGQLAAVHLSKSRTDYQPTQAGRLMRPSVKYLSHPRVQSGCDKEVLLTGGGSKNRNHRLLNMARNNNDPGRLTEALCLEVRPTYFEMKNEKLLSKASEPKYQLFVPQLVTGRCTTRAFHRKSHSLDLNISEKLTLLPTLYEIRGKTTAYSRLNETQPIDLSGLPLQSSKNSCSFQNPSSFDPGMLLQRFSVAPHETQTQRGGEFQCGLEAASVYSDHTNTNNLTFLMDLPSAGRSMPEASDQEEHLSPLDFLHSANFSLGSINQRLNKRERSKLKNLRRKQRRRERWLQKQGKYSGVGFLDHMTLNNEMSTDEDNEYAEEKDSYICAVCLDVYFNPYMCYPCRHIFCEPCLRTLAKDNPSSTPCPLCRTIISRVFFQTELNNATKTFFTKEYLKIKQSFQKSNSAKWPLPSCRKAFHLFGGFHRHAAPVTRRQFPHGAHRMDYLHFEDDSRGWWFDMDMVIIYIYSVNWVIGFIVFCFLCYFFFPF", "text": "FUNCTION: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus envelope."}
{"protein": "MRFKVSKLMAYILRHSPWEFGLEPDEEGFVSIEELVNAVRKVYPWVTEEYIREIVERDEKGRYEIRGNKIRARYGHSYPVILRHEEDKESKVLYHGTVRRNLKGIMREGIKPMKRQYVHLSINYEDAYNTGRRHGEDVVVLIIDAECLRNKGYKILKAGKKVRIVKHVPVDCISGIL", "text": "FUNCTION: Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''- cyclic phosphate (APPR>P). May function as an ADP-ribosylase (By similarity). SIMILARITY: Belongs to the KptA/TPT1 family."}
{"protein": "MLKRLLKRPSLNLLAWLLLAAFYISICLNIAFFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACLFILVGAAAQYFIMTYGIVIDRSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPATSRLRSVLFRGANILVSVLLILLVAALFYKDYASLFRNNKELVKSLSPSNSIVASWSWYSHQRLANLPLVRIGEDAHRNPLMQNEKRKNLTILIVGETSRAENFSLNGYPRETNPRLAKDNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVLWNDNDGGCKGACDRVPHQNVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHRPTYYNRYPPQFRKFTPTCDTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVDQNCLQKQAQTQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRRVSE", "text": "FUNCTION: There are several lipid A forms in this strain, including a phosphoethanolamine (1-O-P-pEtN) form; overexpression of this gene leads to higher levels of the 1-O-P-pEtN form of lipid A. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phosphoethanolamine transferase family. EptA subfamily."}
{"protein": "MADQNERAFQKQFGVNLNRKVKPGITKKKLLRRSRDVGLGFKTPREAIDGTYIDKKCPWTGDVRIRGRILTGVVRKAKMQRTIVIRRDYLHFVRKYSRFEKRHRNMSVHCSPVFRDVEHGDIVTIGECRPLSKTVRFNVLKVSKGQGAKKSFKKY", "text": "SIMILARITY: Belongs to the universal ribosomal protein uS17 family."}
{"protein": "MCQTMRCILVACVALALLAAGCRVEASNSRPPRKNDVNTMADAYKFLQDLDTYYGDRARVRFGKRGSLMDILRNHEMDNINLGKNANNGGEFARGFNEEEIF", "text": "FUNCTION: Integral part of the sensory system that mediates food signaling, providing the neural basis for the regulation of food response; coordinates larval foraging and social behavior changes during development. Required in dopaminergic (DA) neurons that innervate the mushroom body for satiety to suppress appetitive memory performance; a key factor in the internal state of hunger in the brain. NPF neurons coordinately modulate diverse sensory and motor neurons important for feeding, flight, and locomotion. NPF/NPFR pathway exerts its suppressive effect on larval aversion to diverse stressful stimuli (chemical stress and noxious heat) through attenuation of TRP channel- induced neuronal excitation. NPF neural signaling system plays a physiological role in acute modulation of alcohol sensitivity in adults, rather than a general response to intoxication by sedative agents. Activation and inhibition of the NPF system reduces and enhances ethanol preference, respectively. Sexual experience, the NPF system activity and ethanol consumption are all linked; sexual deprivation is a major contributor to enhanced ethanol preference. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family."}
{"protein": "MSKPAITLWSDAHFFSPYVLSAWVALQEKGLSFHIKTIDLDSGEHLQPTWQGYGQTRRVPLLQIDDFELSESSAIAEYLEDRFAPPTWERIYPLDLENRARARQIQAWLRSDLMPIREERPTDVVFAGAKKAPLTAEGKASAEKLFAMAEHLLVLGQPNLFGEWCIADTDLALMINRLVLHGDEVPERLVDYATFQWQRASVQRFIALSAKQSG", "text": "FUNCTION: Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. SIMILARITY: Belongs to the GST superfamily."}
{"protein": "MASSETQPRFGQSVKGLLSDKVTSCSGDVIALTRQVLKGSRSQELLSQAARNMVIQEDAILHSEDSLRKMSIITTHLQYQQEAIQKNVEHSKNLQDQLRHLMK", "text": "FUNCTION: As part of a BORC-like complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, this complex may couple lysosomes to microtubule plus-end-directed kinesin motor. SUBCELLULAR LOCATION: Lysosome membrane. SIMILARITY: Belongs to the BORCS7 family."}
{"protein": "MALVVEDIVKNFGEGLSETKVLKGINFEVEQGEFVILNGASGSGKTTLLTILGGLLSQTSGTVLYNDAPLFDKQHRPSDLRLEDIGFIFQSSHLVPYLKVIEQLTLVGQEAGMTKQQSSTRAIQLLKNIGLEDRLNVYPHQLSGGEKQRVAIMRAFMNNPKIILADEPTASLDADRATKVVEMIRQQIKEQQMIGIMITHDRRLFEYADRVIELEDGKITD", "text": "FUNCTION: Part of the ABC transporter complex hrt involved in hemin import. Responsible for energy coupling to the transport system (By similarity). FUNCTION: Part of the ABC transporter complex hrt involved in hemin import. Responsible for energy coupling to the transport system (Probable). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. HrtA family."}
{"protein": "MGKGKPRGLNSARKLRVHRRNNRWAENNYKKRLLGTAFKSSPFGGSSHAKGIVLEKLGIESKQPNSAIRKCVRVQLIKNGKKVTAFVPNDGCLNFVDENDEVLLAGFGRKGKAKGDIPGVRFKVVKVSGVSLLALWKEKKEKPRS", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
{"protein": "MVNLKCPICGGEITVEDDALPGELVEHECGAQLEVVKQNGKLSLRLAEQIGEDWGE", "text": "FUNCTION: Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-ornithine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine."}
{"protein": "MKFDSRVMLNSANNNSPQHPVSAPSDINMNGYNRKLPQKRGYEMPKYSDPKKKMCKERIPQPKNTVAMLNELRHGLIYKLESQTGPVHAPLFTISVEVDGQKYLGQGRSKKVARIEAAATALRSFIQFKDGAVLSPLKPAGNLDFTSDEHLENGIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQNVSKSAITVDGQKKVPDKGPVMLLYELFNDVNFECINIDGAQNNCRFKMTVTINEKKFDGTGPSKKTAKNAAAKAALASLCNISYSPMVVPQKNVPLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMSVNGAVLNDSHAEIVSRRCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQLRTKIESGEGTIPVKSSDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPPPYHLNKPRLALVTSAEPRNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLELFSAFKREDLGSWLKKPIEQDEFGLAE", "text": "FUNCTION: Has A-to-I RNA editing activity on extended dsRNA: edits RNA- binding protein Rnp4F. A-to-I editing of pre-mRNAs acts predominantly through nervous system targets to affect adult nervous system integrity, function and behavior. Essential for adaptation to environmental stresses, such as oxygen deprivation, and for the prevention of premature neuronal degeneration, through the editing of ion channels as targets."}
{"protein": "SLWEFGQMILKETGKLPFPYYGAYGCYCGWGGRRGPKDATDRCCYVHDCKQICECDKAAAVCFRERKYMAYLRVLCKK", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits myotoxin and anticoagulant activity (PubMed:18602430). Displays edema-inducing activities in mouse paw (PubMed:18602430). Also displays cytotoxic activity against some cell lines and myotubes, and antimicrobial activities against E.coli, C.albicans and Leishmania (PubMed:18602430). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily."}
{"protein": "MSFGSCSRHALFTPGALPGSFRTMTTSCVKRVYTAQIRGGDALGKRLPSVSSFPGQLPRHGSHFQSLAFFSTSRRRQTPPPPSPPTTSQSPTVPSKASTTPPTSLNTSKPVATESQDKTDWSIIAKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARVLTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANAADNKGATVAVDSLINYEAVKSFNNEKYEVAQYDTTLKAYEKASVKIATSLAALNSGQNFIFSSALTMMMLLGAQGIVKGTMTVGDLVLVNQLVFQLSLPLNFLGTVYRELRQSLIDMDVMFNLQSLDSATKDSPTAKPLHLKGGEIEFRNVAFAYHPERPIFRDLSFKIPAGQKVAIVGPSGCGKSTVFRLLFRFYDSSSGQILIDGQDIKTVTLDSLRRSIGVVPQDTPLFHADILHNIRYGNLEATDEQVYEAARKAHVEGTIQRLPEKYATKVGERGLMISGGEKQRLAVARVLLKDPPVLFFDEATSALDVYTETELMRNINSILTGQGKTSVFIAHRLRTISDADLIIVLQDGYVAEQGTHEQLLAMPGGVYHGLWQAQLTESTQPTEEEIERQREELEIVDEKKKQQT", "text": "FUNCTION: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily."}
{"protein": "MSHEAHNGTKLFKVQFTPDEEVLEHITDKQGVTPQSNTAAQRIVAVKNIIKNDDLHVDEATPESWREQNYVDVLGVDTEDTLQNGPGTGGGDVYSFYTIKRSNKMAQLATEMARTPAKTVSFSVSDNPEEAVSPPANKQTENKTPSKGRKNEFISTTPHRLRKRLSAPSQPSDSESDYSASNSDEELEEKSSAAKTPSKVSQTPGKTPSKKGKKNTASNLVEEYFEAHSSSKVLTSDRTLQRLQTPKLDQETLRKLLDQTPSAFADELHRISKKHEALFYKWMLQLHLGFNIILFGLGSKQSLIEKFRTSLLQDSLHIVINEFFPSITAKSILNSITEEALGHPGAFRSPLDQMDFILQRFKDDPSLELYLLIHNLDSQMLRGEKCQQVLGQLASIPNLHLLASVDHINAPLMWDQSKQSLYNWLWYETTTFGSYIEETSYENSLLVKRSGALALSSLTHVLRSLTPNARGIFRLLAEYQMANKDNPSYTGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGMDGVEYLLIPLDLGTLTDFLEMEDKDT", "text": "FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC2 family."}
{"protein": "MYMARCGPKNNVLCFPFQLSFLFSKRLINKRFKYTLQTEDEKNMMGSLSKNKIITPEDVEFKLAQLREFSNTLKERIHNTKSVNSDGHQSNSIAPISEDSRNVNVTKISSVPNEEKSKNLSDLIHSSFLEKMDHLVPKVIRERVADDDILAKNLFDRSHSNWAPVIDRLYVSEKRFMDIDSREFSVWLNGTVKYLPFHSILHLDEMLLEQINGDVVKFNTHMYECIFNNLGNLKPTNFNQDGTNDKVILKMKELLERYDKALKITEERINKKEGFPSKVPKMTQAILNNCLKYSTKCSSFHDMDYFITKFRDDYGITPNKQNLTTVIQFYSRKEMTKQAWNTFDTMKFLSTKHFPDICTYNTMLRICEKERNFPKALDLFQEIQDHNIKPTTNTYIMMARVLASSSSNAVVSEGKSDSLRLLGWKYLHELEDKNLYRHKKDDLNLFLAMMALAAFDGDIELSRALYYLFIAKKYKTLCANWKGNILVDQDTIWKSTLMPEMLNYLMLAYARFDPRNLPVLSGYEKGIELRRKFLREFDSSMRLDDTDKLVKFKLPFLPISDLNSEAQVLAESNAIWSFNLENGGTRNTLTSSNEAALEDIKKYRQLLDSFAQEAEDFNEFKFKVMYEVTKMQRESINVNVFNKISLHTYLSIPINLKQQKEFLRRLTFFTFQQHEFEAVIKRLYEGYRNIPSSHTRDQNSISTEAISVSKPETTEDLNLIMHDIWYITCLRHKIMMDTTLYELVMKAAIEFQNEDLAKKVWNDRGKFRTTVPFLKMDQRIRIAKDQKFAHLMVEFFTKQGKYSDAIAIILSSKNRFNWTYSMVRNLHKALEEIEDRNSVEILLDVVNKKSHAKALKWEEQELNM", "text": "FUNCTION: RNA-binding protein involved in the specific removal of group I introns in mitochondrial encoded transcripts. Maintains the stability of the small subunit mitochondrial 15S rRNA and thus the expression of the mitochondrial genome (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the CCM1 family."}
{"protein": "MGQAGCKGLCLSLFDYKTEKYVIAKNKKVGLLYRLLQASILAYLVVWVFLIKKGYQDVDTSLQSAVITKVKGVAFTNTSDLGQRIWDVADYVIPAQGENVFFVVTNLIVTPNQRQNVCAENEGIPDGACSKDSDCHAGEAVTAGNGVKTGRCLRRENLARGTCEIFAWCPLETSSRPEEPFLKEAEDFTIFIKNHIRFPKFNFSKSNVMDVKDRSFLKSCHFGPKNHYCPIFRLGSVIRWAGSDFQDIALEGGVIGINIEWNCDLDKAASECHPHYSFSRLDNKLSKSVSSGYNFRFARYYRDAAGVEFRTLMKAYGIRFDVMVNGKGAFFCDLVLIYLIKKREFYRDKKYEEVRGLEDSSQEAEDEASGLGLSEQLTSGPGLLGMPEQQELQEPPEAKRGSSSQKGNGSVCPQLLEPHRST", "text": "FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the P2X receptor family."}
{"protein": "MRFSAFLTLLLVAFVASCSTFASAESVAEGRRLRADAAPVPVNKDNVAKLAGGFLEKLKTNTALTKAANTIKNSNADEAAVRKAITTFAAAKESAKMSDEGIAKISAMMAGTVQKNPKSWPRLRKFAKVTLGATVAGFAIYGAYKALFDRKSSTAATTTTTTGSA", "text": "FUNCTION: Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves. SUBCELLULAR LOCATION: Secreted Host mitochondrion membrane; Single-pass membrane protein Host endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MLAPEARGDLIHFTENTRDAMETFFNSYDLAEYSEVNPNKLNRKETDELLGVIRERFKSELVITDEDFVKHLAFALIRAANITTSVKVNYVGAYEYTIGGKKFLVKDAWVFPLIKECMKKFNKPNPVRTFCATFEDAYIVIARSLPKLFLNRTIGKRGIPSGYEFLGADFLTATSVCLNDHEKAIVLQASRAAIDRAVSSSVDGKIVSLFDLGRLS", "text": "FUNCTION: Component that constitutes the tail found at one end of the virion. Together with Hsp70h and p64, encapsidates the 5'-terminal portion of the viral genome. Movement protein that is involved in local cell-cell movement via plamodesmata. At least five viral proteins, CP, CPm, p6, p64 and Hsp70h are essential for cell-cell movement. SUBCELLULAR LOCATION: Virion. Note=Integral virion tail component."}
{"protein": "MKLSLLSTFAAVIIGALALPQGPGGGGSVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDAIGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTIEALRAVGINHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGNIVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVFDTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACRWQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPVIPGGLTVDDIEVSCPSEPFPEIATASGPLPSLAPAP", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily."}
{"protein": "MTITRILTCLLICLFIRIPAAGTKTTQLIFKRFTEETCQNDPCLNGGTCTPGKLSCTCATGWMGRYCHRKCRNIYKSCDRWAVEDKCHTILTQTNFFDVNCAISCKMCSPDPNYVAPEIPLAPALEPMQFFLGKWHSRASKGLRFPTDLYDTEYEEIIDIAPANVPMFGPPSLNFTSTSWFGDDTRVVHGFITLKPNSFPPEVAILSTSNEGLNMIELGTLKHHVLTLNVSYMQVHPTMDSKVLPLGATRRLRRVGSLLEMTVAKLFSENKVSQFKKMFKKIADYAF", "text": "FUNCTION: Plays an important role in determining body shape and sensory ray morphology, possibly by acting as a signaling molecule outside the expressing cell. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
{"protein": "MTGASRRSARGRIKSSSLSPGSDEGSAYPPSIRRGKGKELVSIGAFKTNLKILVGLIILGIIVIYFVINRLVRHGLLFDESQKPRVITPFPAPKVMDLSMFQGEHKESLYWGTYRPHVYFGVRARTPLSLVAGLMWLGVKDEMYVMRHFCENSDDLSTFGWREHNGRDYGRQELVENDMVIETSFVKSKGDGLGYGGDWAVRIDVKNKGLNDDVKRSAHLFFYLADEGGNVLNLGQDGLDFQGSSLLVSGSREDVGDWQIHLKSQNQLETHYSGFKTPHIYNLSDLVQQNLALQARKFGRLQLSDTSEDSSNIYIFQISGRLPFTIDIPFISGIKGESSNVEKRLTSLTGLPLSDLLKKKHQEFDAKFNECFKLSEKHDSETLGVGRTAIANMLGGIGYFYGQSKIYVPKSTQPGSRDNFLLYWPAELYTAVPSRPFFPRGFLWDEGFHQLLIWRWDIRITLDIVGHWLDLLNIDGWIPREQILGAEALSKVPEEFVVQYPSNGNPPTLFLVIRDLIDAIRMEKFVASEKDEVLSFLERASVRLDAWFQWFNTSQKGKEIGSYFWHGRDNTTTQELNPKTLSSGLDDYPRASHPSEDERHVDLRCWMYLAADCMHSITELLGKEDKLSKENYNSTVKLLSNFNLLNQMHYDSDYGAYFDFGNHTEKVKLIWKEVIQENGQLSRQLVRKTFGKPKLKLVPHLGYVSFFPFMSRIIPPDSPILEKQLDLISNRSILWSDYGLVSLAKTSSMYMKRNTEHDAPYWRGPIWMNMNYMILSSLYHYSIVDGPYREKSKAIYTELRSNLIRNVVRNYYETGYIWEQYDQVKGTGKGTRLFTGWSALTLLIMSEDYPIF", "text": "FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor. Required for the accumulation of seed storage proteins, the formation of protein bodies, cell differentiation, cellulose biosynthesis and organization (in cell walls), cell shape determination and organization (e.g. epidermal cells), and embryo development. Involved in root development. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 63 family."}
{"protein": "METVVIVAIGVLATIFLASFAALVVVCRQRYCRPRDLLQRYDSKPIVDLIGAMETQSEPSELELDDVVITNPHIEAILENEDWIEDASGLMSHCIAILKICHTLTEKLVAMTMGSGAKMKTSASVSDIIVVAKRISPRVDDVVKSMYPPLDPKLLDARTTALLLSVSHLVLVTRNACHLTGGLDWIDQSLSAAEEHLEVLREAALASEPDKSLPNPEGFLQEQSAI", "text": "FUNCTION: Functions as a negative regulator of MYRF in oligodendrocyte differentiation and myelination. Interacts with the C-terminal of MYRF inhibiting MYRF self-cleavage and N-fragment nuclear translocation. The secreted form promotes differentiation of T helper 1 cells (Th1). FUNCTION: Functions as a negative regulator of MYRF in oligodendrocyte differentiation and myelination. Interacts with the C-terminal of MYRF inhibiting MYRF self-cleavage and N-fragment nuclear translocation (PubMed:25946230). The secreted form promotes differentiation of T helper 1 cells (Th1) (PubMed:25946230). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Cell membrane; Single-pass type II membrane protein Secreted Secreted, extracellular exosome Note=Secreted by exosomes through a non-classical pathway. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Cell membrane; Single-pass type II membrane protein Secreted Secreted, extracellular exosome Note=Secreted by exosomes through a non-classical pathway. SIMILARITY: Belongs to the TMEM98 family."}
{"protein": "MKKVFFLILILNCVVGALSNKNICKISLLLSGDYNDIGVNYMFNYARTQVEKNLNINSIVFTNLENNQNAINNAIIESINKGSNFLISTINSHSNFIINYSRLYKNKEIFWLIKGNDNERPIPDDLPRVKILNINSDLSFYYLGFISSLISKTGKIGFISTKNIETDYQRLTNAFYIGAINSNPNITFLVCSNNFNNQNNNKKISYKISKLLISKGVDFIGSDQDDNSIQLAVIDNGGIGLGLTGFEYSKIYNDKFPFSFKLEWSQLLIDITNTIINGSWVDYDIIYITSFSRLNGTTNFTPEIEPIINYNFIPKIYQKQINDEINKLKNHSTNYYFPHLCNNLFNNIYNQKQTNGCITNEQFSNSHLLNASNIKIIDNKEILEFVDSYSNSIKISILSVSIFCIFICVLGMIFITVLRNARILKSSSPSFLLLILFGCIVIFTGCILFSQPATDKTCQGRVWLLSIGYTIFLGSLLIKNWRVWLLFDNKKLRKRSITNWKLYPWVAGILVVDVLILALWQGLGDIKSESRIIGTSFYQYTNVCTNNDQGSIALYILLAFHGLKLLGTCFISFKIKLVDIEEFNESKPITTSVFIILFCIFTIILLIAPSSSSSSASSPQPIASLETIICICSVTTTAISIGLLFGDKIYFITTQGLGLNQTFAKSSSFSLDKKDCDDDDDDSSDGSDHSNSNKNKNKNKNRNQSEKKKRPNSIKPIGLFSKSKQESVVFNPPSNNDLTNELALPIEGIKEGHGHDSENNDEYEHHEDEDHEYEGEGEDEDHEDEYEVENDIEQEQEQESSNISISTKKNNENEIISDT", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the BMP lipoprotein family. SIMILARITY: In the C-terminal section; belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily."}
{"protein": "MTRNQLHNWLNAGFFGLLLLLIHVQGQDSPEANPIRNTHTGQIQGSLIHVKDTKAGVHTFLGIPFAKPPVGPLRFAPPEAPEPWSGVRDGTAHPAMCLQNLDMLNEAGLPDMKMMLSSFPMSEDCLYLNIYTPAHAHEGSNLPVMVWIHGGALVIGMASMFDGSLLTVNEDLVVVTIQYRLGVLGFFSTGDQHARGNWGYLDQAAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSQGLFHGAIMESGVALLPDLISETSEMVSTTVAKLSGCEAMDSQALVRCLRGKSEAEILAINKVFKMIPAVVDGEFFPRHPKELLASEDFHPVPSIIGVNNDEFGWSIPVVMGSAQMIKGITRENLQAVLKDTAVQMMLPPECSDLLMEEYMGDTEDAQTLQIQFTEMMGDFMFVIPALQVAHFQRSHAPVYFYEFQHPPSYFKDVRPPHVKADHADEIPFVFASFFWGMKLDFTEEEELLSRRMMKYWANFARHGNPNSEGLPYWPVMDHDEQYLQLDIQPAVGRALKAGRLQFWTKTLPQKIQELKASQDKHREL", "text": "FUNCTION: Hydrolase with high activity towards palmitoylcarnitine. Is also active with p-nitrophenylacetate and alpha-naphthylacetate. May also hydrolyze retinyl esters (By similarity). SUBCELLULAR LOCATION: Microsome Endoplasmic reticulum. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family."}
{"protein": "MALSTATKAATDALAANRAPTSVNAQEVHRWLQSFNWDFKNNRTKYATKYKMANETKEQFKLIAKEYARMEAVKDERQFGSLQDALTRLNAGVRVHPKWNETMKVVSNFLEVGEYNAIAATGMLWDSAQAAEQKNGYLAQVLDEIRHTHQCAYVNYYFAKNGQDPAGHNDARRTRTIGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPLIVAVTEWAAANGDEITPTVFLSIETDELRHMANGYQTVVSIANDPASAKYLNTDLNNAFWTQQKYFTPVLGMLFEYGSKFKVEPWVKTWNRWVYEDWGGIWIGRLGKYGVESPRSLKDAKQDAYWAHHDLYLLAYALWPTGFFRLALPDQEEMEWFEANYPGWYDHYGKIYEEWRARGCEDPSSGFIPLMWFIENNHPIYIDRVSQVPFCPSLAKGASTLRVHEYNGQMHTFSDQWGERMWLAEPERYECQNIFEQYEGRELSEVIAELHGLRSDGKTLIAQPHVRGDKLWTLDDIKRLNCVFKNPVKAFN", "text": "FUNCTION: Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. SIMILARITY: Belongs to the TmoA/XamoA family."}
{"protein": "MKKITLALSAVCLLFTLNHSANALVSSPSTLNPGTNVAKLAEQAPVHWVSVAQIENSLTGRPPMAVGFDIDDTVLFSSPGFWRGKKTYSPDSDDYLKNPAFWEKMNNGWDEFSIPKEVARQLIDMHVRRGDSIYFVTGRSQTKTETVSKTLADNFHIPAANMNPVIFAGDKPEQNTKVQWLQEKNMRIFYGDSDNDITAARDCGIRGIRILRAANSTYKPLPQAGAFGEEVIVNSEY", "text": "FUNCTION: Dephosphorylates several organic phosphate monoesters such as 3'-UMP, 5'-UMP and pNPP (PubMed:6256351). Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and nucleotides (PubMed:3049613). Also displays significant phosphomutase activity since it is able to catalyze the transfer of the phosphate group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions. One of the physiological functions of the phosphohydrolytic activity of the enzyme is believed to be the scavenging of organic phosphate esters that otherwise cannot pass the cytoplasmic membrane (PubMed:6256351). FUNCTION: Dephosphorylates several organic phosphate monoesters (PubMed:14501135, PubMed:17570338). Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds (By similarity). SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the class B bacterial acid phosphatase family. SIMILARITY: Belongs to the class B bacterial acid phosphatase family."}
{"protein": "MILLIDNYDSFTYNLAQYLSELNIKVLVKRNDKITLDEIKNLNIQGIIISPCPGGPEDSGISQGIIKYLGNQIPILGVCLGHQTIGHVFGGKIIKAPKLIHGKPSIIFHDGKGVFQNLKNPITATRYHSLIIEKESCPDELEITAWTEDGLIMGIQHKKYKQLQGIQFHPESILTESGKQILQNFINCLN", "text": "SUBCELLULAR LOCATION: Plastid, cyanelle."}
{"protein": "MSGYQRRPGATPLSRARSLAIPDAPAFYERRSCLPQLNCERPHGRDLDSPFFGIRPAFMCYVPSPVLASVGDTDFGYGKGKCSKQSPSGAHGTHFGDDRFEDLEEANPFSFREFLKTKNLGLSKEDPASRIYAKEASRHSLGLDHNSPPSQTGGYGLEYQQPFFEDPTGAGDLLDEEEDEDTGWSGAYLPSAIEQTHPERVPAGTSPCSTYLSFFSTPSELAGPESLPSWALSDTDSRVSPASPAGSPSADFAVHGESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAKMIKEESDYHDLESVVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSNFQRENEALRCGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNLVAEILKSIDRISEVKDEEEDS", "text": "FUNCTION: Endosome-associated protein that plays a role in membrane receptor sorting, cytokinesis and ciliogenesis (PubMed:23108400, PubMed:25278552, PubMed:27767179). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552). Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1 (PubMed:23108400). Plays a role in the formation of cilia (PubMed:27767179). Involved in cargo protein localization, such as PKD2, at primary cilia (PubMed:27767179). Involved in the presentation of the tumor necrosis factor (TNF) receptor TNFRSF1A on the cell surface, and hence in the modulation of the TNF-induced apoptosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Early endosome Endosome Recycling endosome Midbody Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, cilium basal body Note=Colocalizes in a WASHC2-dependent manner with the retromer CSC complex at endosomes (PubMed:25278552). During cytokinesis colocalized with PTPN13 at the midbody (PubMed:23108400). Colocalizes with IFT88 and gamma-tubulin at the basal body of primary cilia (PubMed:27767179). Colocalizes with IFT88 and pericentrin at the centrosome (PubMed:27767179). SIMILARITY: Belongs to the ENTR1 family."}
{"protein": "MAKSKNHTNHNQNKKAHRNGIKRPQKHRYDSLKYRDAKFRRNQKFANRGTVEAIRQAKASA", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family."}
{"protein": "MGRRRVEIKRIENKSSRQVTFCKRRNGLMEKARQLSILCGSSVALFIVSSTGKLYNSSSGDSMAKIISRFKIQQADDPETLDLEDKTQDYLSHKELLEIVQRKIEEAKGDNVSIESLISMEEQLKSALSVIRARKTELLMELVKNLQDKEKLLKEKNKVLASEVGKLKKILETGDERAVMSPENSSGHSPPETLPLLK", "text": "FUNCTION: Transcription factor involved in the negative regulation of flowering time in short days, probably through the photoperiodic and vernalization pathways. Prevents premature flowering, particularly in the cv. Landsberg erecta background. In non-inductive photoperiods (e.g. short days), required for flowering through VIL2-mediated maintenance of the epigenetically repressed state of MAF5 via H3K9me2 and plant homeodomain / polycomb repressive complex 2 (PHD-PRC2)- dependent H3K27me3. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MNVYLLLASGILCALMTVFWKYRRFQRNTGEMSSNSTALALVRPSSTGLINSNTDNNLSVYDLSRDILNNFPHSIAMQKRILVNLTTVENKLVELEHILVSKGFRSASAHRKST", "text": "SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
{"protein": "QPWIPFV", "text": "FUNCTION: Induces contraction of intestinal smooth muscle in isolated guinea pig ileum. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Peroniin subfamily."}
{"protein": "MSNLNKDTEHTNGGGNVEEEVRTLFVSGLPVDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVTFDSRAGAEAAKNALNGIRFDPENPQTLRLEFAKANTKMAKSKLMATPNPTNIHPALGAHFIARDPYDLTGAALIPASPEAWAPYPLYTTELTPAIPHAAFTYPAAAAAAAALHAQMRWYPPSEATQQGWKSRQFC", "text": "FUNCTION: RNA-binding protein involved in the regulation of smooth muscle cell differentiation and proliferation in the gastrointestinal system (PubMed:22683258, PubMed:25064856). Binds NOG mRNA, the major inhibitor of the bone morphogenetic protein (BMP) pathway (PubMed:25064856). Mediates an increase of NOG mRNA levels, thereby contributing to the negative regulation of BMP signaling pathway and promoting reversible dedifferentiation and proliferation of smooth muscle cells (PubMed:25064856). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MINITAITTEHQLLKNIPIERVEQPDIAWYWVDFYGPEDTETALLRDFFHFHPLAIEDCFQHMQRPKLDHYDGYRFYVIHALNKETLETEEVDIFQGEKFVVTFHLHETPGIAKVRERLYASPDILKKGPGHISYMIMDQLVDEYFPLVYKIEDRLNEIEESRPHKTYGTLMNEVFDLRTDLLHLRRTIIPMRDLLYRILSLDHVKEQRETKAYFSDIYDHLLKLSEIVESNRDMTSDLRDSYVTLNSNRMNAIMMTLTIVSTIFIPLTFIAGVYGMNFDFMPELHWKYGYFAVLGLMAALVIGMLIWFVHKGWFNIFK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family."}
{"protein": "MNPIQSFHCKLRSLATVLDGETARLLRALDGEDSEDFEDSSARILCDLYSEVQTLKDDVNAHLDKARLESRESTHFIKAAKVLMKKNSADIIKLREFFQKYGYQARDKEDSACEHRVSNSSPGLAVCKDTQEPGVKQELSEPRVPRGSAPEEPLRSPQLSDFGLQRYMVSQGPANPRQETVSLKEDRASETTPAKDPSVQVLKTPRCALKMDDFECVTPKLEHFGISEYTMCLNEDYTMGLKNMKSIKSSPLSGVGGEAVETGPVTSDNSFAIPGPMIQQLEKNDVEYINSPLPPKFCTPGLKIPSSMDSTDLVSIDYPLSKPNSSPTDLEDKDCAPLILNSDECYQSFADPHSPTITSYENFTTPSPPKVTAIPEDILQMLKYNSNLASPIDVKAMPLRRGFTSKGQSTRGAANKENW", "text": "FUNCTION: Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex, it mediates the microtubule-stimulated oligomerization. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Note=Localizes to the outer kinetochore and spindle microtubules during mitosis in a NDC80 complex-dependent manner. SIMILARITY: Belongs to the SKA3 family."}
{"protein": "MAAAAPSPSSSAFSKTLSPSSSTSSTLLPRSTFPFPHHPHKTTPPPLHLTHTHIHIHSQRRRFTISNVISTNQKVSQTEKTETFVSRFAPDEPRKGSDVLVEALEREGVTDVFAYPGGASMEIHQALTRSSIIRNVLPRHEQGGVFAAEGYARATGFPGVCIATSGPGATNLVSGLADALLDSVPIVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVVREAFFLARSGRPGPILIDVPKDIQQQLVIPDWDQPMRLPGYMSRLPKLPNEMLLEQIVRLISESKKPVLYVGGGCSQSSEDLRRFVELTGIPVASTLMGLGAFPTGDELSLSMLGMHGTVYANYAVDSSDLLLAFGVRFDDRVTGKLEAFASRAKIVHIDIDSAEIGKNKQPHVSICADIKLALQGLNSILESKEGKLKLDFSAWRQELTEQKVKHPLNFKTFGDAIPPQYAIQVLDELTNGNAIISTGVGQHQMWAAQYYKYRKPRQWLTSGGLGAMGFGLPAAIGAAVGRPDEVVVDIDGDGSFIMNVQELATIKVENLPVKIMLLNNQHLGMVVQWEDRFYKANRAHTYLGNPSNEAEIFPNMLKFAEACGVPAARVTHRDDLRAAIQKMLDTPGPYLLDVIVPHQEHVLPMIPSGGAFKDVITEGDGRSSY", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TPP enzyme family."}
{"protein": "MVTHRRKGGSGPPQKPPPRIVDRSSFDADKKKIKVEKLYHKANNPDNDWPFSFGSVFKMLLSIRISGAIWGIINDCDEVYNYWEPLHLFLYGEGFQTWEYSPVYAIRSYFYIYLHYIPASLFANLFGDTKIVVFTLIRLTIGLFCLLGEYYAFDAICKKINIATGRFFILFSIFSSGMFLASTAFVPSSFCMAITFYILGAYLNENWTAGIFCVAFSTMVGWPFSAVLGLPIVADMLLLKGLRIRFILTSLVIGLCIGGVQVITDSHYFGKTVLAPLNIFLYNVVSGPGPSLYGEEPLSFYIKNLFNNWNIVIFAAPFGFPLSLAYFTKVWMSQDRNVALYQRFAPIILLAVTTAAWLLIFGSQAHKEERFLFPIYPFIAFFAALALDATNRLCLKKLGMDNILSILFILCFAILSASRTYSIHNNYGSHVEIYRSLNAELTNRTNFKNFHDPIRVCVGKEWHRFPSSFFIPQTVSDGKKVEMRFIQSEFRGLLPKPFLKSDKLVEVTRHIPTEMNNLNQEEISRYVDLDSCDYVVDVDMPQSDREPDFRKMEDNWKPVDSLPFIDVSKSTGFHGLLRAFYVPFLSAKHNVMTTCTLYRKSNL", "text": "FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid- linked oligosaccharides. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 22 family."}
{"protein": "MAAVPRGLLSRINQFLSIRSITPSSSESLPHCSSFFLIRRFSSDTGLMDGGGSDIIGAQTRIIEAKQGEMSSRSKRTGIIAVKCGMTALWDKWGKRIPISILWVDDNIVSQVKTVEKEGIFALQIGCGQKKPKHLSKAVVGHFRAQGVPLKRKLREFPVTEDALLPVGTSLGVRHFVPGQYVDVTGITRGKGFQGCMKRHGFSGMPASHGASLSHRSGGSTGQRDAPGKVFKGRKMAGRMGADQRTVKNVWVYKIDPARNLMWVRGQVPGAEGNFVFIKDAWCKKPDISKLPFPTYLAPEDEDPSELEPLVADLGEVDPFMLAE", "text": "FUNCTION: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL3 family."}
{"protein": "FLPLLAGLAANFLPTIICKISYKC", "text": "FUNCTION: Has a non-hemolytic activity. Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLAATTHPTASVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQKVEMENQIYAIPEDIMQGSGTQLFDHIAGCLANFMDKLQIKDKKLPLGFTFSFPCIQTKLDESFLVSWTKGFKSRGVEGRDVVTLIRKAIQRRGDFDIDIVAMVNDTVATMMTCGYDDQNCEIGLIVGMGSNACYMEEMRYIDTVEGDEGRMCINMEWGAFGDDGTLDDIRTEFDQEIDMGSLNPGQQLFEKMISGMYMGELVRLILVKMAKEELLFRGKLSPELLTTGRFETKDVSEIEGEKDGIQKAREVLVRLGMDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLQKTVRRLVPNCDIRFLCSEDGSGKGAAMVTAVAYRLAYQHRARLKTLEPLKLSREQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYSIPQDIMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNRLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNTEWGAFGDNGCLDDFCTEFDVAVDELSLNPGKQRFEKMMSGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALQQVRAILQHLGLESTCDDSIIVKEVCTVVAQRAAQLCGAGMAAVVDKIRENRGLDTLKVTVGVDGTLYKLHPHFAKVMRETVKDLAPKCDVSFLESEDGSGKGAALITAVACRIREAGQR", "text": "FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D- fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6- phosphate. Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein Cytoplasm, cytosol Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane. The interaction with the mitochondrial outer membrane via the mitochondrial-binding peptide (MBP) region promotes higher stability of the protein. Release from the mitochondrial outer membrane into the cytosol induces permeability transition pore (PTP) opening and apoptosis. SIMILARITY: Belongs to the hexokinase family."}
{"protein": "MKHFLRMLIQVCLYFYCKFLWRCLKFVMRKLTGRCELQRICYNTKPGASRTMKIETSLRDSKSKLLQTSVSVHPDAIEKTIEDIMELKKINPDVNPQLGISLQACLLQIVGYRNLIADVEKLRREAYDSDNPQHEEMLLKLWKFLKPNTPLESRISKQWCEIGFQGDDPKTDFRGMGLLGLYNLQYFAERDATAAQQVLSDSLHPKCRDITKEEISKFSKAEWEKKRMDKAIGYSFAIVGINITDLAYNLLVSGALKTHFYNIAPEAPTLSHFQQTFCYLMHEFHKFWIEEDPMDIMEFNRVREKFRKRIIKQLQNPDMALCPHFAASEGLINM", "text": "FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family."}
{"protein": "MAKSKSSQGASGARRKPAPSLYQHISSFKPQFSTRVDDVLHFSKTLTWRSEIIPDKSKGTLTTSLLYSQGSDIYEIDTTLPLKTFYDDDDDDDNDDDDEEGNGKTKSAATPNPEYGDAFQDVEGKPLRPKWIYQGETVAKMQYLESSDDSTAIAMSKNGSLAWFRDEIKVPVHIVQEMMGPATRYSSIHSLTRPGSLAVSDFDVSTNMDTVVKSQSNGYEEDSILKIIDNSDRPGDILRTVHVPGTNVAHSVRFFNNHLFASCSDDNILRFWDTRTADKPLWTLSEPKNGRLTSFDSSQVTENLFVTGFSTGVIKLWDARAVQLATTDLTHRQNGEEPIQNEIAKLFHSGGDSVVDILFSQTSATEFVTVGGTGNVYHWDMEYSFSRNDDDNEDEVRVAAPEELQGQCLKFFHTGGTRRSSNQFGKRNTVALHPVINDFVGTVDSDSLVTAYKPFLASDFIGRGYDD", "text": "FUNCTION: Transcriptional modulator with roles in meiotic regulation and silencing."}
{"protein": "MDGYYSLSPISVLHRIKDSFHFAVSALLANLFSALFTFFFALVGTLLGALTGALIGQETESGFIRGAAVGAISGAVFSIEVFESSLLLWQSDESGIGCLLYLIDVIASLLSGRLVRERIGPAMLSAVQSQMGAVESQFQDHTDIFDTAISKGLTGDSLNRIPKVRITDTSPEIVSCSVCLQDFQVGETVRSLPHCHHMFHLPCIDKWLRRHASCPLCRRHL", "text": "FUNCTION: May be involved in the early steps of the plant defense signaling pathway. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RING-type zinc finger family. NIP subfamily."}
{"protein": "MTVEEKIIDAFDRLFMEDVSDIKDEDLFDAGVLDSLGTVELIVELENLFEIKVPISEFGREDWNTVNKIVEGVKELQNA", "text": "FUNCTION: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DltC family."}
{"protein": "DQDEGVSTEPTQVGPAELHNDETCVGPLVYRN", "text": "FUNCTION: Could enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract. Exhibits both simulatory and inhibitory actions on the release of pituitary gonadotropins (By similarity). Binds to heparin and gelatin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the seminal plasma protein family."}
{"protein": "MFLKAGRGNKVPPVRVYGPDCVVLMEPPLSKRNPPALRLADLATAQVQPLQNMTGFPALAGPPAHSQLRAAVAHLRLRDLGADPGVATTPLGPEHMAQASTLGLSPPSQAFPAHPEAPAAAARAAALVAHPGAGSYPCGGGSSGAQPSAPPPPAPPLPPTPSPPPPPPPPPPPALSGYTTTNSGGGGSSGKGHSRDFVLRRDLSATAPAAAMHGAPLGGEQRSGTGSPQHPAPPPHSAGMFISASGTYAGPDGSGGPALFPALHDTPGAPGGHPHPLNGQMRLGLAAAAAAAAAELYGRAEPPFAPRSGDAHYGAVAAAAAAALHGYGAVNLNLNLAAAAAAAAAGPGPHLQHHAPPPAPPPPPAPAQHPHQHHPHLPGAAGAFLRYMRQPIKQELICKWIDPDELAGLPPPPPPPPPPPPPPPAGGAKPCSKTFGTMHELVNHVTVEHVGGPEQSSHVCFWEDCPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFDGCDRKFANSSDRKKHSHVHTSDKPYYCKIRGCDKSYTHPSSLRKHMKIHCKSPPPSPGPLGYSSVGTPVGAPLSPVLDPARSHSSTLSPQVTNLNEWYVCQASGAPSHLHTPSSNGTTSETEDEEIYGNPEVVRTIH", "text": "FUNCTION: Essential for neural crest development, converting cells from an epidermal fate to a neural crest cell fate. Binds to DNA (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
{"protein": "MTLAYETVSENRSFGGIQGVYRHQSQATGTPMTFAIYLPPDARHGKVPVLWYLSGLTCTHENAMTKAGAQEWAAEYGIAVIFPDTSPRGEGVANDETYDLGQGAGFYVDATEAPWAPHFRMWHYVTHELPELVFNNFPLDREAQGITGHSMGGHGALTIAMTFPERYRSVSAFAPIAHPSESDWGRKQFAAYLGDDKAAWKRHDSTILMREKGYPGEVLIDQGASDQFLDLLKPEALAHAMAERRQPGTFRMQQGYDHSYFFVQSFMADHIRWHAERLG", "text": "FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate (Probable). SIMILARITY: Belongs to the esterase D family."}
{"protein": "MFLVNSFLKGGGGGGGGGGGLGGGLGNVLGGLISGAGGGGGGGGGGGGGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRTHYSNIEANESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKRWQAIYKQFDTDRSGTICSSELPGAFEAAGFHLNEHLYNMIIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQEWLQLTMYS", "text": "FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Translocates to the plasma membrane upon calcium binding."}
{"protein": "MRGKKRIGLLFLLIAVVVGGGGLLLAQKVLHKTSDTAFCLSCHSMSKPFEEYQGTVHFSNQKGIRAECADCHIPKSGMDYLFAKLKASKDIYHEFVSGKIDSDDKFEAHRQEMAETVWKELKATDSATCRSCHSFDAMDIASQSESAQKMHNKAQKDSETCIDCHKGIAHFPPEIKMDDNAAHELESQAATSVTNGAHIYPFKTSHIGELATVNPGTDLTVVDASGKQPIVLLQGYQMQGSENTLYLAAGQRLALATLSEEGIKALTVNGEWQADEYGNQWRQASLQGALTDPALADRKPLWQYAEKLDDTYCAGCHAPIAADHYTVNAWPSIAKGMGARTSMSENELDILTRYFQYNAKDITEKQ", "text": "FUNCTION: Part of the anaerobic respiratory chain of trimethylamine-N- oxide reductase TorZ. Required for electron transfer to the TorZ terminal enzyme. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the TorC/TorY family."}
{"protein": "GGCINHGQPCDGDKNDCQCCRDNGYCNCDGIFGLKWNCKC", "text": "FUNCTION: Not toxic to mice by intracerebroventricular injection. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 04 (omega-agtx) family. 03 (type II/III omega-agtx) subfamily."}
{"protein": "MRLEIGNIFIKDIQFGEQTKVENGVLYVNKDEMIKKLSVIEHIKSVDLDIARPGESVRITPVKDVIEPRVKVEGPGGIFPGVISKVETDGSGRTHVLKGAAVVTTGKVVGFQEGIVDMSGVGAEYTPFSKTLNLVVIAEPEDGIEQHRHEEVLRMVGLNAGVYIGEAGRSVTPDEVKVYETDTIFEGAAKYPNLPKVGYVYMLQTQGLLHDTYVYGVDAKKIVPTILYPTEVMDGAILSGNCVSSCDKNPTYVHCNNPMVEELYAMHGKEINFVGVIITNENVYLADKERSSDWTAKLCKFLGLDGAIVSQEGFGNPDTDLIMNCKKIEMEGVKTVISTDEYAGRDGASQSLADADVRANAVVSNGNANMVIVLPPMDKTIGHIQYIDTIAGGFDGSLRADGSIEVEIQAITGATNELGFGYLSAKGY", "text": "FUNCTION: In the first step of glycine reductase, the substrate is bound to component PB via a Schiff base intermediate. Then the PB- activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination."}
{"protein": "MSTSKSENYLSELRKIIWPIEQYENKKFLPLAFMMFCILLNYSTLRSIKDGFVVTDIGTESISFLKTYIVLPSAVIAMIIYVKLCDILKQENVFYVITSFFLGYFALFAFVLYPYPDLVHPDHKTIESLSLAYPNFKWFIKIVGKWSFASFYTIAELWGTMMLSLLFWQFANQITKIAEAKRFYSMFGLLANLALPVTSVVIGYFLHEKTQIVAEHLKFVPLFVIMITSSFLIILTYRWMNKNVLTDPRLYDPALVKEKKTKAKLSFIESLKMIFTSKYVGYIALLIIAYGVSVNLVEGVWKSKVKELYPTKEAYTIYMGQFQFYQGWVAIAFMLIGSNILRKVSWLTAAMITPLMMFITGAAFFSFIFFDSVIAMNLTGILASSPLTLAVMIGMIQNVLSKGVKYSLFDATKNMAYIPLDKDLRVKGQAAVEVIGGRLGKSGGAIIQSTFFILFPVFGFIEATPYFASIFFIIVILWIFAVKGLNKEYQVLVNKNEK", "text": "FUNCTION: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADP/ATP translocase tlc family."}
{"protein": "MLLLPLPLLLFLLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN", "text": "FUNCTION: Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Mast cell granules. SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily."}
{"protein": "MPAEGGKTDMERIGLFSEMEYITVGDKYVSQFNRPFNEAASKNKQMLPGGSKEMSDLQAGYFDPHFVRIFEGEGYINLNQVRRRDMVEAAKKNLGKAFLPSNGEKKPCGLGSYYGTIGGPVPFFSAQSKPREKYKAPGKNLYTNPGKKGTGYGYANITIGKQFSHSADFYDAAKLKYKKANEEHHRLLKGAPFKLNLHPRDYFDANPYFSEESLPPIKKEEKKKTISNTFKPSSPGKKPGGMKAGTFDPYPSHSADPYVAKLANISGKDDKIFHPPSGPKSRPVESIMTLNVRRALNSKNYKTSSVPSY", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the UPF0602 family."}
{"protein": "MALKHMQIFLFVAIFSSFCFSITLSRPLDNELIMQKRHIEWMTKHGRVYADVKEENNRYVVFKNNVERIEHLNSIPAGRTFKLAVNQFADLTNDEFRSMYTGFKGVSALSSQSQTKMSPFRYQNVSSGALPVSVDWRKKGAVTPIKNQGSCGCCWAFSAVAAIEGATQIKKGKLISLSEQQLVDCDTNDFGCEGGLMDTAFEHIKATGGLTTESNYPYKGEDATCNSKKTNPKATSITGYEDVPVNDEQALMKAVAHQPVSVGIEGGGFDFQFYSSGVFTGECTTYLDHAVTAIGYGESTNGSKYWIIKNSWGTKWGESGYMRIQKDVKDKQGLCGLAMKASYPTI", "text": "FUNCTION: Cysteine protease that may have a developmental senescence specific cell death function during apoptosis, heavy metal detoxification, and hypersensitive response. SUBCELLULAR LOCATION: Vacuole Note=Localized in senescence-associated vacuoles (SAVs) with intense proteolytic activity that develop in the peripheral cytoplasm of mesophyll and guard cells. SIMILARITY: Belongs to the peptidase C1 family."}
{"protein": "MPIFFYLFTTLIIISSLCVVLSKNSVYSVLWLIFAFINGSGLMILLGAEFLAMMLIVIYVGAVAVLFLFVIMMLDMHFNKAIMQLKEKPILSIFVSLIMFADLVVIILLGTKNIHFSSDLSFAIASDVSNTKAIGKILYTDFMIPFQIAGLILFVAMIGCITLTLRKRDGVKRQNIAKQLSHNKENAVLMTKPLINKGIENIKYE", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 6 family."}
{"protein": "MAFYPLQIAGLVLGFLGMVGTLATTLLPQWRVSAFIGSNIIVFERIWEGLWMNCVRQAKARLQCKFYSSMLALSPALEAARALMCVAVALSLIALIIGICGMKKIQCTGSNERAKAYLLGTSGVLFILTGIFVLIPVCWTANIIIRDFYNPAVHVGQKRELGAALFLGWASVAVLFIAGGLLCGFCCCNRKKQRDGYPAPRPSMPRTDERRRNMTRQSETPTSYV", "text": "FUNCTION: Channel-forming tight junction protein with selectivity for anions, including chloride and bicarbonate, and for solutes smaller than 9 Angstrom in diameter. In the kidney proximal tubule, may be involved in quantitative reabsorption of filtered anions. Does not affect water permeability. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the claudin family."}
{"protein": "MKLAYWMYAGPAHIGTLRVASSFRNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIVDRHVLARGSQEKVVENITRKDKEERPDLIVLTPTCTSSILQEDLQNFVDRASIASNSDVILADVNHYRVNELQAADRTLEQVVRYYLDKARRQGTLSQSITEKPSVNIIGMFTLGFHNQHDCKELKRLLQDLGIQVNEVIPEGGSVENLRNLPKAWLNLVPYREVGLMTALYLEKEFGMPYVATTPMGIVGTAEFVRQIQSHINKWAPMFLGKLVDYEPYIDQQTRFISQAAWFSRSIDCQNLTGKKVVVFGDTTHAASMTKILAREMGIHVVCAGTYCKHDADWFKEQVQGYCDEILVTDDHTQVGDMIARIEPAAIFGSQMERHIGKRLDIPCGVISAPVHIQNFPLGYRPFLGYEGTNQIADLVYNSFTLGMEDHLLEMFGGHDTKEVITKSLSTDTDFTWDSESQLELTKIPGFVRAKIKRNTEKFARQNGVAKITVEVMYAAKEALNA", "text": "FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ChlB/BchB/BchZ family."}
{"protein": "MKSYNVLPLAYISLFLMLFYQVWAQFPRECANIEALRRGVCCPDLLPSSGPGTDPCGSSSGRGRCVAVIADSRPHSRHYPHDGKDDREAWPLRFFNRTCQCNDNFSGHNCGTCRPGWRGAACNQKILTVRRNLLDLSPEEKSHFVRALDMAKRTTHPQFVIATRRLEDILGPDGNTPQFENISVYNYFVWTHYYSVKKTFLGTGQESFGDVDFSHEGPAFLTWHRYHLLQLERDMQEMLQEPSFSLPYWNFATGKNVCDVCTDDLMGSRSNFDSTLISPNSVFSQWRVVCESLEEYDTLGTLCNSTEGGPIRRNPAGNVGRPAVQRLPEPQDVTQCLEVRVFDTPPFYSNSTDSFRNTVEGYSAPTGKYDPAVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRYNADISTFPLENAPIGHNRQYNMVPFWPPVTNTEMFVTAPDNLGYAYEVQWPGQEFTVSEIITIAVVAALLLVAAIFGVASCLIRSRSTKNEANQPLLTDHYQRYAEDYEELPNPNHSMV", "text": "FUNCTION: Plays a role in melanin biosynthesis (PubMed:2245916). Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid (PubMed:7813420). May regulate or influence the type of melanin synthesized (PubMed:7813420, PubMed:2245916). Also to a lower extent, capable of hydroxylating tyrosine and producing melanin (PubMed:1537333). SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane protein Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. SIMILARITY: Belongs to the tyrosinase family."}
{"protein": "MVSLVLADTADSSDLSKAAITVEESTSAQQPKFFNYHEFVITKYRALDEESCEEHGPENPICITHFPNIYVPEESDEFRTTRVVRIPRRFESSTEFPNFSTQLPGSEPAALPDTHNKEFVPAGEFEGQWYGETSVSPLSNYLDQAEWTEIVTRINSLLEAAYNPITRRNFVNVILDLLTLNLWSIIEPYLFVNPLQSVEDYVSEINRSESFRLKGIKIIPPRESSYLSVCIDSPAWIKPCTAINEPLLTHCDTLIVLL", "text": "FUNCTION: The ERF2-ERF4 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ERF4 family."}
{"protein": "MAFEALTGINGDLITRSWSASKQAYLTERYHKEEAGAVVIFAFQPSFSEKDFFDPDNKSSFGEIKLNRVQFPCMRKIGKGDVATVNEAFLKNLEAIIDPRTSFQASVEMAVRSRKQIVFTGHSSGGATAILATVWYLEKYFIRNPNVYLEPRCVTFGAPLVGDSIFSHALGREKWSRFFVNFVSRFDIVPRIMLARKASVEETLPHVLAQLDPRKSSVQESEQRITEFYTRVMRDTSTVANQAVCELTGSAEAFLETLSSFLELSPYRPAGTFVFSTEKRLVAVNNSDAILQMLFYTSQASDEQEWSLIPFRSIRDHHSYEELVQSMGKKLFNHLDGENSIESTLNDLGVSTRGRQYVQAALEEEKKRVENQKKIIQVIEQERFLKKLAWIEDEYKPKCQAHKNGYYDSFKVSNEENDFKANVKRAELAGVFDEVLGLMKKCQLPDEFEGDIDWIKLATRYRRLVEPLDIANYHRHLKNEDTGPYMKRGRPTRYIYAQRGYEHYILKPNGMIAEDVFWNKVNGLNLGLQLEEIQETLKNSGSECGSCFWAEVEELKGKPYEEVEVRVKTLEGMLGEWITDGEVDDKEIFLEGSTFRKWWITLPKNHKSHSPLRDYMMDEITDT", "text": "FUNCTION: Positive regulator of basal resistance and of effector- triggered immunity specifically mediated by TIR-NB-LRR (TNL) resistance proteins. Disruption by bacterial effector of EDS1-TIR-NB-LRR resistance protein interactions constitutes the first step in resistance activation (PubMed:22158819). Acts redundantly with salicylic acid to regulate resistance gene-mediated signaling (PubMed:19578402). Triggers early plant defenses and hypersensitive response independently of PAD4, and then recruits PAD4 to potentiate plant defenses through the accumulation of salicylic acid (PubMed:11574472). Nuclear localization is essential for basal and TNL- conditioned immunity and for reprogramming defense gene expression, while cytoplasmic EDS1 is required to induce a complete immune response (PubMed:20617163). Heterodimerization with PAD4 and/or SGA101 is necessary for TNL-mediated effector-triggered immunity (PubMed:24331460). Contributes to nonhost resistance against E.amylovora (PubMed:22316300). Loss of EDS1-PAD4 interaction compromises basal but not TNL-triggered resistance (PubMed:21434927). Necessary for systemic acquired resistance (SAR) signal generation and perception (PubMed:24755512). Has no direct lipase activity (PubMed:16040633). Putative lipase activity is dispensable for immune functions (PubMed:24331460). SUBCELLULAR LOCATION: Nucleus Cytoplasm Microsome Note=Found in both the nucleus and diffuse in the cytosol when associated with PAD4, in the nucleus and in punctate spots in the cytoplasm when interacting with SRFR1, SNC1 or RPS4, only in the nucleus when associated with SAG101 and in the cytosol when it dimerizes. Found in the nucleus when interacting with VICTR and PAD4. Interacts with AvrRps4 and HopA1 effectors in microsomes."}
{"protein": "MKPHFRNPVERMYQDTFSDNFYNRPILSHRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSKLKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLHQDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLAKAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLEEHSQALSGRLRAILQNQGN", "text": "FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase- dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also against simian foamy virus (SFV). After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. May inhibit the mobility of LTR retrotransposons. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, P-body Note=Mainly cytoplasmic, small amount are found in the nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MKVVVRAPFYPTESLEKVLSSIFNLFDAPKESCAVVGEGKGRYIECVFHNHKPLEKFRRLLRQQRILDAARSYVERGLREGEVKFYLNKQAAFAGKVSFCTYEAGESPLGSIIVVIELGKCSPDEFLNWLAPRTVNGKPVGEVSELKCLEQGSG", "text": "SIMILARITY: Belongs to the UPF0201 family."}
{"protein": "MVHNISLSSRKALHNVHLPYMVQLPKPTGYNVALKNAAEGYDKARRMVAWLYDIADYESSIPQTFTLQQKTDKYTWELSDNFPPHLAVVPPDQSVSAPSIFSPVRLAQTLLIMSSLWYDDHTDLAPGPEQNTMQKLTQWNQERHKDQGWLIKDMFNAPNIGLRNDWYTDEVFAQQFFTGPNSTTITLASDVWLTAFTSEAKAQGKDKVIALFESAPPNSFYVQDFSDFRRRMGAKPDEELFNDSDGAMRYGCAAVALFYLTAMGKLHPLAIIPDYKGSMAASVTIFNKRTNPLDISVNQANDWPWRYAKTCVLSSDWALHEMIIHLNNTHLVEEAVIVAAQRKLSPSHIVFRLLEPHWVVTLSLNALARSVLIPEVIVPIAGFSAPHIFQFIRESFTNFDWKSLYVPADLESRGFPVDQLNSPKFHNYAYARDINDMWTTLKKFVSSVLQDAQYYPDDASVAGDTQIQAWCDEMRSGMGAGMTNFPESITTVDDLVNMVTMCIHIAAPQHTAVNYLQQYYQTFVPNKPSALFSPLPTSIAQLQKYTESDLMAALPLNAKRQWLLMAQIPYLLSMQVQEDENIVTYAANASTDKDPIIASAGRQLAADLKKLAAVFLVNSAQLDDQNTPYDVLAPEQLANAIVI", "text": "FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 13S-hydroperoxy fatty acids. SIMILARITY: Belongs to the lipoxygenase family."}
{"protein": "MEAYIRQKRASPGMVQASDLQINRPMSGMRSNSRELHAYDGPMQFISSPQNPDQILTNGSPGGINPVAMNTSRNHSNNMRSLSTINQEADLIEEISSHELEDEESSPVTVIEQHQQSASHSANSTQSQKPRARQHSFSDNLDEDDYTNRNVAGAAPVRPAGMASSPYKDATLDGSSNGTGNGTGGESEGDVIGNIDQFVMQPAPQGVLYKCRITRDRKGMDRGLFPIYYLHLERDYGKKIFLLGGRKRKKSKTSNYIVSCDPTDLSRNADGFCGKLRSNVFGTSFTVFDNGNKESTESPRLDLAVIIYDTNILGFKGPRNMTVILPGMTEDDQRVKISSADPKQQGILDLWKMKNMDNIVELHNKTPVWNDETQSYVLNFHGRVTQASVKNFQLVHDSDPEYIVMQFGRTSEDVFTMDYRYPLCAMQAFAIALSSFDGKIACE", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TUB family."}
{"protein": "MTIVSPDKLPSARAVELTAPLDDIYQILNEDGAVIIKNFIPLELVDKINKEVDPYLAQHAAGPNHMSEIYKLTVGSKTKHMGNLTMASKSFRDEVLNHPSMHAISEKLFRANFGDYWLNRAAVLEVDSGEKAQGLHRDDSLYPWKAFLTKDSPELMVNFFIALTEFREENGATRLVLGSHKWEDSTRYPSPEQTIPAEMQAGDAIVYLASLFHGAGQNRSQKTRRGLSITTHPAHFTPMESHIDVPRAIIENMTPLAQKMIGWRTWSTNHGVPVWTVRDGRMEDELKLKSLESPKQIQAAVI", "text": "FUNCTION: Dioxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B (PubMed:30090271). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI (PubMed:30090271). Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3- pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase olcH to yield geranylgeranyl-HPPO (PubMed:30090271). Geranylgeranyl pyrophosphate is provided by the cluster-specific geranylgeranyl pyrophosphate synthase olcC (PubMed:30090271). The FAD-dependent monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD catalyzes the cyclization of the terpenoid component, resulting in the formation of the tricyclic terpene moiety seen in predecaturin E (PubMed:30090271). The cytochrome P450 monooxygenase then catalyzes the allylic oxidation of predecaturin E, which is followed by spirocylization with concomitant loss of one molecule of water to form decaturin E (PubMed:30090271). Decaturin E is the substrate of the cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29 position to form decaturin F (PubMed:30090271). The short-chain dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27-one intermediate, and subsequent hemiacetal formation probably leads to the formation of decaturin C (Probable). The dioxygenase olcK may be a peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into decaturin A once decaturin C is shuttled into the peroxisome by the MFS transporter olcL (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B (PubMed:30090271). In the absence of olcJ, decaturin E may be shunted to a pathway in which it is oxidized to a ketone, possibly by olcF, to form decaturin D, which undergoes further allylic oxidation to yield decaturin G (PubMed:30090271). Moreover, in the absence of oclK or oclL, oclB can convert decaturin C into 15-deoxyoxalicine A (PubMed:30090271). SUBCELLULAR LOCATION: Peroxisome matrix. SIMILARITY: Belongs to the PhyH family."}
{"protein": "MGGSGNWIRSLISNRKPVNDQQEKLSDKSSKKKWKLWRISSESLASSSFKSRGSYAASSLGSELPSFSADEAFTTAMAALIRAPPRDFLMVKREWASTRIQAAFRAFLARQAFRALKAVVRIQAIFRGRQVRKQAAVTLRCMQALVRVQSRVRAHRRAPSDSLELKDPVKQTEKGWCGSPRSIKEVKTKLQMKQEGAIKRERAMVYALTHQSRTCPSPSGRAITHHGLRKSSPGWNWYDDVGTFSRKSSESSVLSEYETVTVRKNNLSSTRVLARPPLLLPPVSSGMSYDSLHDETSTSSTSQSPVAFSSSVLDGGGYYRKPSYMSLTQSTQAKQRQSGLSCNGDARRSAGSDQCTDLYPPGNVWAKSQRS", "text": "FUNCTION: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus envelope Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the IQD family."}
{"protein": "MASLRYRRFLKLCEEWPVDETRVGRDLGAFIRQRVAQAFREGESTQVDDPDACDEMYASLNRMNTNYYREKYPRLQDTSFTEVTAEEYKMVLASDNLKQMEEMKKGMWKRLRDKFNVKPSEENS", "text": "FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). May play a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production. May be involved in cytochrome b translation and/or stability. SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid Mitochondrion."}
{"protein": "MTQNIRPLPQFKYHPKPLETGAFEQDKTVECDCCEQQTSVYYSGPFYCVDEVEHLCPWCIADGSAAEKFAGSFQDDASIEGVEFEYDEEDEFAGIKNTYPDEMLKELVERTPGYHGWQQEFWLAHCGDFCVFIGYVGWNDIKDRLDEFANLEEDCENFGIRNSDLAKCLQKGGHCQGYLFRCLHCGKLRLWGDFS", "text": "SIMILARITY: Belongs to the UPF0167 family."}
{"protein": "MFEKGYVDENYIRVPKDRLFSFIVRVLTKLGVPEEDAKIVADNLVMADLRGVESHGVQRLKRYVDGIISGGVNLHPKIRVIREGPSYALIDGDEGLGQVVGYRSMKLAIKKAKDTGIGIVIARNSNHYGIAGYYALMAAEEGMIGISMTNSRPLVAPTGGIERILGTNPIALAAPTKDKPFLLDMATSVVPIGKLEVYRRKGKDIPEGWAINREGNITTKVEEVFNGGALLPLGGFGELLGGHKGYGLSLMVDILSGILSGGTWSKYVKNTSEKGSNVCHFFMVIDIEHFIPLEEFKEKISQMIEEIKSSRKHPEFERIWIHGEKGFLTMETRLKLGIPIYRKVLEELNEIAKRVGVEGL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family."}
{"protein": "MSNLKHCSNCKHNGLITESNHEFCIFCQSIFQLSNKVSKKSNFHVSNKLIHLRNVLRRLLSNQCSSDVIVELKSVMTKNNISSTDIDANFVSSFLKANEKINKKDYKLVFEIINHIKEEKLNLDTSKINEVIEIFKHLVFFCQENTPSKTINYSFFLDKIFSLTSVTNNLKPQTVKNYTKNNSNQLVWENFLDYMKKKKINTSVYDYGHEYVFVDYGFTTCSLEV", "text": "FUNCTION: Acts with RNA polymerase to initiate transcription from late gene promoters. SIMILARITY: Belongs to the nucleo-cytoplasmic large DNA viruses (NCLDVs) VLTF-3 family."}
{"protein": "MYKAQYLWLFGLVLISRSATERTTPKINFTTVVGLKTTPAMRSSSASSLGGSLPMVINTWNFTDANFLAWRILNVTQGGLRQTRNAVVEGCTRCEQQQCDRTVGYGGSPDELGETTLDAMIMDGSSMDVGAVAGLRGIKDAIRVARHVLEHTKHSILVGDLASQFAQAMGFRSESLATPESKAMWMEWTAANCQPNFWRNVHPDPSISCGPYKPKATPLTRWKEDRARTEYSIGHLNHDTIGMIAIDAANNIHAGTSSNGARHKIPGRVGDSPIPGAGAYADNEVGAAVATGDGDIMMRFLPTLLAVEAMRAGKKPAEAAEVGIRRISKHYKDFSGAVIAVDRLGQYGAACYGMTEFPFVVSNPSKTDIPSRQESVKCITGKEAVNVV", "text": "FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. SIMILARITY: Belongs to the Ntn-hydrolase family."}
{"protein": "MEPPDARAGLLWLTLLLSGYSGAQAELHVSVPPRVEVMRGEQIALDCTPREHPENYVLEWLLVDASGARHRLASVEPQGSEFLGTIHNSRGRRPPYKIDSLGRLVIAEAQVGDERDYVCVVKAGAAGTSEATSSVRVFATPEATEVAPNKGTLSVMEQFAQEIATCSSNNGNPVPRITWYQNGQRLDVPMELNSKGYMTSRTVREASGLYSLTSTLYLRLHKEDRDASFHCAAHYDLPSGQHGRLDSHTFRLTLHYPTEHVEFWVGSPSTTEGWVREGDAVQLLCQGDGSPSPEYSFFREQGNQEEQLNVNLKGNLTLEGVHRSQSGIYGCRVEDYDADEEVQLVKKLKLHVAYLDPLELSVPEEFSVFLNSSGTVVNCSARGLPAPIVRWTKDSVTVADGPILSLDSVTFDSAGTYTCEASTPTVPLLSRTQSFQLVVQGAPELKPNEIKPKSGTSWTEGDEVMLTCSARGFPEPKLTWSQRGDTTPAEPPFEGRGWMSSSLTLKVTSALSREGVSCEASNIHGKNGHVFHFGSVAPQTAQAGVAVMAVAVSVGLLLLVVAAFYCMRRKGRPGCCQRAEKGAPPAREPELSHSGSERPEHTGLLMGGPSGGGRGGNGGFGDEC", "text": "FUNCTION: Laminin alpha-5 receptor. May mediate intracellular signaling (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MNFSLLTTEMLTALLGIGLLAIGLLNRKKDSHRGVAYAAVFGLLGILVVTFFQYGINTNTFHQLWILDDYSVFMKEIFLVAAILVILSAIDYVDGLPRFKTEFYALLVFATLGMMVMASANDLVTLYVGMELMTITFFILVAYILGDGRSSEAGVKYLLLGGASSAVLLYGLSLLYGLTGTTVIPDLLARLTWSPALAIAVVTIIAGFGFKISAVPFHMWSPDIYEGAPTPVTGFLAAASKAAGFAVLVRLFLEGMPLQGGADWLTVIAVLAGVTMVIGNVVAIPQTNIKRMLAYSSVAQAGYLLVGLMSTDAPGVKGILFYAMLYVVANMGAFAVATAVGRAIGSDEIADYAGLSQRQPLLASVMTISLLSLAGIPPLAGFVGKLYLFSAIMDKGVLWPAFLGFVMSMVSVYYYLNVSLYMWRDDPKDDRPIPVSGPMKLTVIFSMVVTVILGIYPGPLAEVATVAAKSLF", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."}
{"protein": "MQLFHLCLIISCSCPTVQASKLCLGWLWDMDIDPYKEFGATVQLLSFLPHDFFPSVRDLLDTASALFRDALESPEHCSPHHTALRQAILCWGELMTLATWVGANLQDPASRELVVTYVNINMGLKFRQLLWFHISCLTFGRETVIEYLVSFGVWIRTPQAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC", "text": "FUNCTION: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury during adult infections. SUBCELLULAR LOCATION: Secreted Host nucleus. SIMILARITY: Belongs to the orthohepadnavirus precore antigen family."}
{"protein": "MATYNYPEFGAGLWHFANYIDRYAVDGYGPALSTIDQINAAKEVGELSYVDLPYPFTPGVTLSEVKDALKDAGLKAIGITPEIYLQKWSRGAFTNPDPAARAAAFELMHESAGIVRELGANYVKVWPGQDGWDYPFQVSHKNLWKLAVDGMRDLAGANPDVKFAIEYKPREPRVKMTWDSAARTLLGIEDIGLDNVGVLLDFGHALYGGESPADSAQLIIDRGRLFGMDVNDNLRGWDDDLVVGTVHMTEIFEFFYVLKINNWQGVWQLDQFPFRENHVEAAQLSIRFLKHIYRALDKLDIPALQAAQEAQNPLQAQRIVQDALLSSITVSE", "text": "FUNCTION: Involved in catabolism of D-apiose. Catalyzes isomerization of D-apiose to apulose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the xylose isomerase family."}
{"protein": "MSSKHSDPLERFYKQFQAFVQNNPNVISAARAAAQIPESAKAVVVLSPYSLQHVFPREWVTKSYRKTIVERPERLLASSMGISAAITMYPSLFTLKSSHQRKGSLMAPHVLKVHGSSWPAELIELCQMADAKLLKGEIEVPDTWNSGDIYLSSKTIKALQGTIGAIETGVDSIFKGPSAEHISNRAFVAIRPPGHHCHYGTPSGFCLLNNAHVAIEYAYDTYNVTHVVVLDFDLHHGDGTQDICWKRAGFKPEEEPEDSSYDDFGKKFAEFPKVGYFSMHDINSFPTESGFATKENIKNASTCIMNSHDLNIWNIHLSKWTTEEEFNVLYRTKYRTLFAKADEFFRSAKLEMNQQGRPFKGLVVISAGFDASEFEQTSMQRHSVNVPTSFYTTFTKDALKLAQMHCHGKVLSLMEGGYSDKAICSGVFAHLIGLQNQDWVKEWGSEQVVKEIVRGCKPAWKPYKTKRAKDVIRIWAEEVIRLGRAMIPEFDDIIFKDAVNSAPSNSLLKATVEPASTSTIAQRIIRSHRSNASPEKELHENKPRSTEKQEQREIRSDTKVKQLSSNNRAAETQIPFLQQEFSSEDEDEEYVYDEELNKTFNRTVEDITIDDISRHLETLEIEKKGDEDSDHELKEKNWKNSHQRRLQGNGMYKIPSNTKPHRIRQPQNANTPTYDDSDISMISHVSRKHTTRSGGRW", "text": "FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily."}
{"protein": "MAVGIFGLIPSSSPDELRKILQALSTKWGDVVEDFESLEVKPMKGAMTNEVFMVSWPRKETNLRCRKLLVRVYGEGVELFFNRDDEIRTFEYVARHGHGPTLLGRFAGGRVEEFIHARTLSATDLRDPNISALVASKLRRFHSIHIPGDRIMLIWDRMRTWVGQAKNLCSNEHSTEFGLDDIEDEINLLEQEVNNEQEIGFCHNDLQYGNIMIDEETNAITIIDYEYASYNPIAYDIANHFCEMAADYHSNTPHILDYTLYPGEEERRRFICNYLTSSGEEAREEDIEQLLDDIEKYTLASHLFWGLWGIISGYVNKIEFDYIEYSRQRFKQYWLRKPKLLSFFPS", "text": "FUNCTION: Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylcholine biosynthesis (By similarity). SIMILARITY: Belongs to the choline/ethanolamine kinase family."}
{"protein": "MKTTFLVSLATAALSSTAAAVSVSGSAEGFAKGVTGGGSATAVYPDTIDELVSYLGDDEARVIVLSKTFDFTDSEGTTTETGCAPWGTDAACQVAINQNDWCTNYQPDAPSVSVTYDNAGTLGITVNSDKTLIGEGSAGVIKGKGLRLVSGTSNVIIQNIAITDINPKYVWGGDAITLNDVDMVWIDHVTTARIARQHIVLGTEADNRVTISNSFINGESDYSATCDGYHYWGIYLDGSSDMVTMKGNYIYHTSGRSPKVQGNTLLHAVNNYWHDNSDHAFEIGEGAYVLAEGNVFQNIPTVAEDPIEGELFASPSESANEVCSTYLGRVCELNGFGSSGTFNQADTDFLSKFEGKNIASADSYSSVASSVASSAGNTL", "text": "FUNCTION: Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 1 family."}
{"protein": "MFLKNILSVLAFALLIDAAPVKRSPGFVTLDFNVKRSLVDPDDPTVEAKRSPLFLEFTPSEFPVDETGRDGDVDKRGPVAVTLHNEAITYTADITVGSDNQKLNVIVDTGSSDLWIPDSNVICIPKWRGDKGDFCKSAGSYSPASSRTSQNLNTRFDIKYGDGSYAKGKLYKDTVGIGGVSVRDQLFANVWSTSARKGILGIGFQSGEATEFDYDNLPISLRNQGIIGKAAYSLYLNSAEASTGQIIFGGIDKAKYSGSLVDLPITSEKKLTVGLRSVNVRGRNVDANTNVLLDSGTTISYFTRSIVRNILYAIGAQMKFDSAGNKVYVADCKTSGTIDFQFGNNLKISVPVSEFLFQTYYTSGKPFPKCEVRIRESEDNILGDNFLRSAYVVYNLDDKKISMAPVKYTSESDIVAIN", "text": "FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family."}
{"protein": "MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ", "text": "FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (PubMed:12917326). FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm. FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:7931346). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:7931346). Binding generally results in the modulation of the activity of the binding partner (PubMed:7931346). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (By similarity). FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Melanosome. SUBCELLULAR LOCATION: Nucleus Cytoplasm Melanosome. SUBCELLULAR LOCATION: Nucleus Cytoplasm Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the 14-3-3 family. SIMILARITY: Belongs to the 14-3-3 family."}
{"protein": "MHLLLFQLLVLLPLGKTTRHQDGRQNQSSLSPVLLPRNQRELPTGNHEEAEEKPDLFVAVPHLVATSPAGEGQRQREKMLSRFGRFWKKPEREMHPSRDSDSEPFPPGTQSLIQPIDGMKMEKSPLREEAKKFWHHFMFRKTPASQGVILPIKSHEVHWETCRTVPFSQTITHEGCEKVVVQNNLCFGKCGSVHFPGAAQHSHTSCSHCLPAKFTTMHLPLNCTELSSVIKVVMLVEECQCKVKTEHEDGHILHAGSQDSFIPGVSA", "text": "FUNCTION: Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part through a BMP- inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DAN family."}
{"protein": "MGRKKIQISRILDQRNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSANRLFQYASTDMDRVLLKYTEYSEPHESRTNTDILETLKRRGIGLDGPELEPDEGPEEPGEKFRRLAGEGGDPALPRPRLYPAAPAMPSPDVVYGALPPPGCDPSGLGEALPAQSRPSPFRPAAPKAGPPGLVHPLFSPSHLTSKTPPPLYLPTEGRRSDLPGGLAGPRGGLNTSRSLYSGLQNPCSTATPGPPLGSFPFLPGGPPVGAEAWARRVPQPAAPPRRPPQSASSLSASLRPPGAPATFLRPSPIPCSSPGPWQSLCGLGPPCAGCPWPTAGPGRRSPGGTSPERSPGTARARGDPTSLQASSEKTQQ", "text": "FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MEF2 family."}
{"protein": "MYSFEQAITQLFQQLSLSIPDTIEPVIGVKVGEFACHITEHPVGQILMFTLPSLDNNNEKETLLSHNIFSQDILKPILSWDEVGGHPVLWNRQPLNNLDNNSLYTQLEMLVQGAERLQTSSLISPPRSFS", "text": "FUNCTION: Positive regulator of YopE."}
{"protein": "METKPNPRRPSNTVLPYQTPRLRDHYLLGKKLGQGQFGTTYLCTEKSTSANYACKSIPKRKLVCREDYEDVWREIQIMHHLSEHPNVVRIKGTYEDSVFVHIVMEVCEGGELFDRIVSKGHFSEREAVKLIKTILGVVEACHSLGVMHRDLKPENFLFDSPKDDAKLKATDFGLSVFYKPGQYLYDVVGSPYYVAPEVLKKCYGPEIDVWSAGVILYILLSGVPPFWAETESGIFRQILQGKLDFKSDPWPTISEAAKDLIYKMLERSPKKRISAHEALCHPWIVDEQAAPDKPLDPAVLSRLKQFSQMNKIKKMALRVIAERLSEEEIGGLKELFKMIDTDNSGTITFEELKAGLKRVGSELMESEIKSLMDAADIDNSGTIDYGEFLAATLHMNKMEREENLVAAFSYFDKDGSGYITIDELQSACTEFGLCDTPLDDMIKEIDLDNDGKIDFSEFTAMMRKGDGVGRSRTMMKNLNFNIADAFGVDGEKSDD", "text": "FUNCTION: May play a role in signal transduction pathways that involve calcium as a second messenger. Functions as regulator of the calcium- mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA- responsive transcription factors ABF1 and ABF4 in vitro. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily."}
{"protein": "MFIDGKWILREDLDILNPYTLEIIERITALDREETKYAIEVATENKDVMKELNPSKRYSLLMKIAEHISSKKDLFANTISVDVGKPIKQSRIEVDRTITAFRLSALYAKELRGETIPSENEIIFTKKEPVGVVGAITPFNFPLNLITHKIGPAIATGNAVVLHPSSKAPITAIYLTKVIEHVLKKMNIERGVFNLTTGNGEIVGDEIAKNEKINFLSFTGSVEVGELISKSSYMKKVALELGGNNPLIVLKDSDIELAAKSAVKSKFLNSGQVCISVGKVIVEEEVLETFTKKVIEETKKLVLGNPLDEKTDLGPLITPESALRVEILIKESISEGGELLIGGNRSNSLISPAVLNIDEDNILSKVEAFGPILPILKAKDDEHALNIANNSKYGLQAGIFTNDINKAMKFANKLEYGGVIVNGSPTFRKDNMPFGGIKKSGLGKEGIKYAVEEMCETKTVVIHNM", "text": "FUNCTION: Involved in F420 biosynthesis through the oxidation of lactaldehyde to lactate. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MASDAEWVLESVLGFVSGPVWTVPVLEFMEHKCSVFDDDEENKLSYTDIHNEYKELVETLLTQHLNEVGISEEQFQEACAAPLAHSATLKNILQPVLAVEDFKIFKAMMVQKNIELQLQAIRIIQERNGVLPDCLQHGSDIISDLEQEEMKLVSEALRLSKEEYEREQLRRSAKELNCTFGEHSKTKQSNGSERTPSNTELPDQSHEIEQQPVKMQESPYEEASMKLKEMSNTEAAEAWLEQARKEAGILSSVTNLSQAEKEQLQKRAEYLRRRREELLAKKQESKKMAHNSEVHEEKATCSKQEMTEEEKKSLQRRKQLAEKLKEEVILCEKSGTAS", "text": "SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, cilium, flagellum. SIMILARITY: Belongs to the CFAP36 family."}
{"protein": "MGPPESAAELAAEAVELREPELQLADPASPGEEHVDVEAEGAPGRGRCWPCGAWACGSRGEPEAKKKAPCPGLGLFYTVLSAFLFSVASLFVKKVQGVHAVEISAFRCVVQMLVIIPCLIYRKTGFIGPKGQRLFLFLRGVFGSSAMILMYYAFQTTSLADATVIAFSCPVFTSIFAWIFLKEKYSLWDAFFTLFAIAGVILIVRPPFIFGSDTSGMRESYSEHIKGTFAAIGHAVLAAITLVILRKMGKSVDYFLSIWYYVILGLPEAIIILFVIGEWSLPYCGLDRLFLILIGLLGLGGQIFITKAVQIEKAGLVAIMKTMDIVFAFIFQIAFFDNVPTWWTVGGALCVVVSTTGATIRRWLQGSK", "text": "FUNCTION: May play a role in intracellular calcium sensing and homeostasis. May act as a negative regulator of plasma membrane calcium-transporting ATPases preventing calcium efflux from the cell (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane. SIMILARITY: Belongs to the TMEM20 family."}
{"protein": "MAAAAARVVLSSAARRRLWGFSESLLIRGAAGRSLYFGENRLRSTQAATQVVLNVPETRVTCLESGLRVASEDSGLSTCTVGLWIDAGSRYENEKNNGTAHFLEHMAFKGTKKRSQLDLELEIENMGAHLNAYTSREQTVYYAKAFSKDLPRAVEILADIIQNSTLGEAEIERERGVILREMQEVETNLQEVVFDYLHATAYQNTALGRTILGPTENIKSISRKDLVDYITTHYKGPRIVLAAAGGVSHDELLDLAKFHFGDSLCTHKGEIPALPPCKFTGSEIRVRDDKMPLAHLAIAVEAVGWAHPDTICLMVANTLIGNWDRSFGGGMNLSSKLAQLTCHGNLCHSFQSFNTSYTDTGLWGLYMVCESSTVADMLHVVQKEWMRLCTSVTESEVARARNLLKTNMLLQLDGSTPICEDIGRQMLCYNRRIPIPELEARIDAVNAETIREVCTKYIYNRSPAIAAVGPIKQLPDFKQIRSNMCWLRD", "text": "FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:29576218) (Probable). Preferentially, cleaves after an arginine at position P2 (By similarity). Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (PubMed:22354088). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase M16 family."}
{"protein": "MKSTFKEERIKDDSKRRDLFVFVRQTMCIAAMYPFGYYVNGSGVLAVLVRFCDLTYELFNYFVSVHIAGLYICTIYINYGQGDLDFFVNCLIQTIIYLWTIAMKLYFRRFRPGLLNTILSNINDEYETRSAVGFSFVTMAGSYRMSKLWIKTYVYCCYIGTIFWLALPIAYRDRSLPLACWYPFDYTQPGVYEVVFLLQAMGQIQVAASFASSSGLHMVLCVLISGQYDVLFCSLKNVLASSYVLMGANMTELNQLQAEQSAADVEPGQYAYSVEEETPLQELLKVGSSMDFSSAFRLSFVRCIQHHRYIVAALKKIESFYSPIWFVKIGEVTFLMCLVAFVSTKSTAANSFMRMVSLGQYLLLVLYELFIICYFADIVFQNSQRCGEALWRSPWQRHLKDVRSDYMFFMLNSRRQFQLTAGKISNLNVDRFRGTITTAFSFLTLLQKMDARE", "text": "FUNCTION: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to pentanol, ethyl acetate, and propyl acetate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Heteromeric odorant receptor channel (TC 1.A.69) family. Or2a subfamily."}
{"protein": "MNINNIPELYTTDKRCYTKNQSWWVAATNNFSPLICILFPVVISFVLKETVDNNSPLSKLIIVLFPFLYSAVQHLLLFHGMWASHHRPRGLLSKMPYYSLDFLFLTFGIISALSIIAFTVEKWQGDDDLLFHAITLPFLIISPTYLLSTSCNPTTGQIQFTDTAITALIDLIILSSYIIGITLTVLFRNRNVCCPFPFIFAFASFILILLRSLKETFFPSKQSSSSSLWRKGIFVFIVISSIPGYLLTVCGPIAVFSQHFNCFANSD", "text": "SIMILARITY: Belongs to the UPF0328 family."}
{"protein": "MANETVLYDYWRSSASYRVRIALNLCGEAYRSVPVDLLAKAHRAPEHLARNPQGLVPVLDIDGERLTQSLAIIEYLAETRDGTGLLPAHPIDRQRVRALSYAVAMDIHPVCNLGVVARVMAGAGDGEAARREWMQKFIGEGLAAFERMLDHPATGAFCHGDRPTMADLCLVPQVYNARRWDVDLAACPLLVAIDRRCAGIDAFQRAHPDRAKP", "text": "SIMILARITY: Belongs to the GST superfamily. Zeta family."}
{"protein": "MAHVITRINAREILDSRGNPTVEVDLETTLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQQAIKNINEIIAPKLIGLDCREQKKIDNMMVQELDGSKTEWGWSKSKLGANAILAISMAICRAGAAANKTSLYKYLAQLAGKNTEKMILPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEAMRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNAHEALDLLVASIKKAGYENKVKIAMDVAASEFYNIETKTYDLDFKTPNNDKSLVKTGQELVDLYIELVKKYPIISIEDPFDQDDWENYAKLTEAIGKDVQIVGDDLLVTNPTRIEKALEKKACNALLLKVNQIGSITEAIEACLLSQKNNWGVMVSHRSGETEDVFIADLVVALRTGQIKTGAPCRSERNAKYNQLFRIEESLGANGSFAGDKFRLQLN", "text": "FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2- phosphoglycerate to phosphoenolpyruvate (By similarity). In addition to glycolysis, involved in various processes such as parasite development and invasion (PubMed:21949403, PubMed:24474798). Plays an essential role during ookinete invasion of the mosquito vector midgut by mediating the interaction of the ookinete with the midgut epithelium and, further, by binding to mammalian host plasminogen in the blood meal, whose conversion to active plasmin promotes the invasion process (PubMed:21949403, PubMed:24474798). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton Cell surface Cell membrane; Peripheral membrane protein; Cytoplasmic side Vacuole Note=Partially localizes to the nucleus in rings and trophozoites. Localization to the nucleus and food vacuole is higher in early and mid-stage trophozoites compared to the late- stage trophozoites and schizonts (By similarity). In the nucleus, localizes to heterochromatin region (By similarity). In rings, nuclear localization is dependent on the actin cytoskeleton (By similarity). Localizes to the cell surface of merozoites (By similarity). In gametocytes, predominantly localizes to the actin cytoskeleton (By similarity). In the trophozoite food vacuole, colocalizes with hemozoin, a product of heme detoxification (By similarity). In sporozoites, localizes to punctate structures beneath the cell membrane (By similarity). Localizes to the cell surface of ookinetes, especially on the apical pellicle complex that is involved in invasion (PubMed:21949403, PubMed:24474798). When phosphorylated at Thr-339, localizes to the cytoskeleton (By similarity). When phosphorylated at Ser-42, localizes to the cytoplasm (By similarity). When ubiquitinated at Lys-138, acetylated at Lys-133 and Lys-375 and phosphorylated at Tyr-139, localizes to the food vacuole (By similarity). When triubiquitinated at Lys-138, appears to colocalize with hemozoin in the food vacuole (By similarity). SIMILARITY: Belongs to the enolase family."}
{"protein": "GCTPEYCSMWCKVKVSQNYCVKNCKCPGR", "text": "FUNCTION: Reduces potassium currents through Kv1.2/KCNA2 and Kv1.3/KCNA3 voltage-gated potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 20 subfamily."}
{"protein": "MDVTQSNATKDDANITVTPWPYTETAAAFIILVVSVIILVSIVGNVLVIVAVLTSRALRAPQNLFLVSLACADILVATLVIPFSLANEIMGYWFFGSTWCAFYLALDVLFCTSSIVHLCAISLDRYWSVTKAVSYNLKRTPKRIKSMIAVVWVISAVISFPPLIMTKHDEKECLINDETWYILSSSLVSFFAPGFIMITVYCKIYRVAKQRSSTVFVAKNGLERQPSQSETCFVRKDKFEKESPSSNSSESNQRQEELDDIDLEESATSDNKPKSSRFSNRRRVDGARCCPQRTCRISWVSSQEQSSKQLAVASKTKVAQMREKRFTFVLTVVMGVFVLCWFPFFFTYSLHAICGDSCEPPEALFKLFFWIGYCNSSVNPIIYTIFNRDFRKAFKKICLLDCAAHLRDSCLGTLGRLNAKCIFECHQKSNQEETAN", "text": "FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MRWNTFWGILCLSLLAVGTCQDDAENIEYKVSISGTSVELTCPLDSDENLKWEKNGQELPQKHDKHLVLQDFSEVEDSGYYVCYTPASNKNTYLYLKARVCEYCVEVDLTAVAIIIIVDICITLGLLMVIYYWSKNRKAKAKPVTRGTGAGSRPRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRAV", "text": "FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR- mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development (PubMed:19956738, PubMed:24899501). Participates also in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MLTMDKCKHIGQLRLAQDHSILNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNATGDLKLLRSMLSAIKSQNYQCTTRSGRVLRSMGTSDDTYYLHDGTQSLLQNEDQMYTALWHRRRILMSKIFRTWFEQSPTGRKRQEEQFQEKIAKREVKKRRQELEYQVKAELETIHPRKSLRLQGLAQSTTVEIVPVQVPLQTPASPAKDKVVSTSEDVRLKKASDSSGKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVTASDKTRSPYKHPSITDTVYQMNECQETDTGSAPSRHPSLSLGLSGGASKSRKMELIQPREPSSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQHELETTGTRLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCNGKDIASQPCRVTEMLAKFTETEALEGKIYVCDHCNSKRRRFSSKSVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRESLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLSGSQHPNEEADTSSNEILS", "text": "FUNCTION: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Promotes also the deubiquitination of histone H2A and H2B. Recruited to RNF8/RNF168-ubiquitinated chromatin surrounding double stranded breaks (DSBs), promotes hydrolysis of such ubiquitin conjugates, thus negatively regulating protein recruitment to damaged chromatin (By similarity). Participates in nucleotide excision repair (NER) pathway by deubiquitinating DDB2 to prevent its premature degradation so it can remain on damaged chromatin (By similarity). Promotes FOXP3 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability and increased regulatory T-cell lineage stability. Plays also a positive role in innate immune response to DNA viruses by deubiquitinating STING1, selectively removing its 'Lys-48'- linked polyubiquitin chains and stabilizing it (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Peaks in interphase, with relatively low levels maintained throughout mitosis. SIMILARITY: Belongs to the peptidase C19 family. USP44 subfamily."}
{"protein": "MQWASVLLLAGLCSLSQGQYDEDSHWWIQYLRNQQSTYYDPYDPYPYEPSEPYPYGVEEGPAYAYGAPPPPEPRDCPQECDCPPNFPTAMYCDNRNLKYLPFVPSRMKYVYFQNNQISAIQEGVFDNATGLLWVALHGNQITSDKVGRKVFSKLRHLERLYLDHNNLTRMPGPLPRSLRELHLDHNQISRVPNNALEGLENLTALYLHHNEIQEVGSSMRGLRSLILLDLSYNHLRRVPDGLPSALEQLYLEHNNVYTVPDSYFRGSPKLLYVRLSHNSLTNNGLATNTFNSSSLLELDLSYNQLQKIPPVNTNLENLYLQGNRINEFSISSFCTVVDVMNFSKLQVLRLDGNEIKRSAMPVDAPLCLRLANLIEI", "text": "FUNCTION: Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily."}
{"protein": "MADKVQTTLLFLAVGEFSVGILGNAFIGLVNCMDWVKKRKIASIDLILTSLAISRICLLCIILLDCFTLVLYPDVYATGKEMRIIDFFWTLTNHLSIWFATCLSIYYFFKIGNFFHPLFLWMKWRIDRVISWILLGCVVLSVFISLPATENLNADFRFCVKAKRKTNLTWSCRVNKTQHASTKLFLNLATLLPFCVCLMSFFLLILSLRRHIRRMQLSATGCRDPSTEAHVRALKAVISFLLLFIAYYLSFLIATSSYFMPETELAVIFGESIALIYPSSHSFILILGNNKLRYVSLKVIWKVMSILKGRKFQQHKQI", "text": "FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor T2R family."}
{"protein": "MASPFSGALQLTDLDDFIGPSQSCIKPVTVAKKPGSGIAKIHIEDDGSYFQVNPDGRSQKLEKAKVSLNDCLACSGCVTSAETILITQQSHEELRKVLDANKVAAPGQQRLVVVSVSPQSRASLAARFQLDSTDTARKLTSFFKKIGVHFVFDTAFARNFSLLESQKEFVQRFREQANSREALPMLASACPGWICYAEKTHGNFILPYISTARSPQQVMGSLIKDFFAQQQLLTPDKIYHVTVMPCYDKKLEASRPDFFNQEYQTRDVDCVLTTGEVFRLLEEEGVSLSELEPVPLDGLTRSVSAEEPTSHRGGGSGGYLEHVFRHAAQELFGIHVADVTYQPMRNKDFQEVTLEREGQVLLRFAVAYGFRNIQNLVQKLKRGRCPYHYVEVMACPSGCLNGGGQLKAPDTEGRELLQQVERLYSMVRTEAPEDAPGVQELYQHWLQGEDSERASHLLHTQYHAVEKINSGLSIRW", "text": "FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect (By similarity). SIMILARITY: Belongs to the NARF family."}
{"protein": "MTRTVIAQGTFDILHPGHVHYLEEAAAMGDELLVIVARKSNVDHKEKPICPAAQRRDVVAALEAVDDAIVGHEEDIFAPIEAIDPDVIALGHDQHHDDDAIEAELERRGIDCTVERASAREPEREDEILSTRLIIDRILERRG", "text": "FUNCTION: Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. SIMILARITY: Belongs to the archaeal FAD synthase family."}
{"protein": "MANINIPDDLVSKYSEDVKDLTQKAGSIPSSKSLIPQTAFTPDELRRSLKFWQVTTKVAATVASDWTNLATALTNGTFSATHLRTLCELAFNLKAPTGTGTIFIHEIADPWKGCIDANAPDTVAIPATDSDVNMSTVSSGSTASGTEDAEVKMKAISFLCCTLLRLSVKEPSHIMQAINSIRQRFGSLYGVSSPTLNSVTFNRSQLSRIKQGIETYPSARGTVFYYTRYADATHGYTTKEYGICRFLLFQHLELEGMHIYKMLLALLGEWSTVPIGLLLTWIRNPRSKLAINEIVKIVKELDKPEVDKGWKYARMVNNTFFLDLSSRRNTYLCAVLASLNKKNVPQGSGEYADPTNIAVIKNMDQSVKSQVATDVTLIERIYEKYLVSAGGDEAGTAYALSRGVKRSSPPSQEGGQSGQSGGTPMEVDGASGRGAAGPAPKKTRSGL", "text": "FUNCTION: Encapsidates the genome, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non- specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the nucleorhabdovirus nucleocapsid protein family."}
{"protein": "MWATHGLAVALALSVLPASRALRQGDCEVCISYLGRFYQDLKDRDVTFSPASIEKELIKFCREARGKENRLCYYIGATEDAATKIINEVSKPLSHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGETCKGCAEKSDYIRKINELMPKYAPKAASSRTDL", "text": "FUNCTION: Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. Following secretion by the ER/SR, directly binds to 3-O- sulfogalactosylceramide, a lipid sulfatide in the outer cell membrane of target cells. Sulfatide binding promotes its cellular uptake by endocytosis, and is required for its role in alleviating ER stress and cell toxicity under hypoxic and ER stress conditions. SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum lumen Sarcoplasmic reticulum lumen Note=Retained in the endoplasmic reticulum (ER), and sarcoplasmic reticulum (SR) under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. SIMILARITY: Belongs to the ARMET family."}
{"protein": "MAKLDDATLAQLFTEARSHNGWNPEPLPESVLRELYALTKFGPTAANGSPARFYFVTSAEAKERLAKLSSGSNGPKIMQAPCTVIIGYDLDFPQTLPKLFPHAPGAKDWFNDPVAKEWCALRNSSLQGGYFMIGARALGLDVGPMSGFDNAAVDAEFFAGTNIKSNFIVSIGHGTDEGLFPRNPRLDFDEAAKIL", "text": "SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily."}
{"protein": "MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKMKNGMTVLMMGSADALPEEPSAKTVFVEDMTEEQLATAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSGRETDSSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNANDKNSPPKEIKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVRRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ", "text": "FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:16190881). Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (By similarity). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (PubMed:19726649). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily."}
{"protein": "MKQAKIIGLSTVIALSGIILVACGSKTSEQKNIQFSIPTDVASLDTTILTDQYSYDVAGNVEEGLTRVDSKGNAALALAKSIDVSKDGLTYTVTLKDNLKWSNGDKLTAKDFVYSWKRAVDPKTGSEYAYLMGAVSGANDIISGKSSLDTLGIKAESDTEFTVTLAQPTPYFKFLLSEPVYYPLDQKVVDKYGKQYGTSSDKTVYNGPFMFKSDKAWTGTNKNFSIYANPNYYDKSAVKSKQIDFQVISNANTGAQLYKQGKLDFTLLSTTDLINANKKTEGYTVFKQARTDYIEYNQSGKNASSPDAQKALANQDIRQALNLATNRAEVVKTALPGSTAATSFTPVGMSKTSTGEDFATYAKQDYSYDPTKAKELWAKGLKELGLTKLSLSLEAAGDLAPSEATANFLQTAYQQNLPGLTVNLKLVPFKQRLNDAQNGNFDMVLSGWGGDYAEPSTFLQLFTTGQSYNDGKFSSKTYDDAFKAATTTPDVLEPAKVDEHYKAAEAALYEGSYINPIDFQANPALMNPKITGLEFHSTGLAYDLKSAYIK", "text": "FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide transport (PubMed:11409543). Binds di- and tripeptides with high affinity. Requires a free N-terminal alpha-amino group and an alpha- peptide bound contiguous with the N-terminal amino group, has a strong selectivity for L-residues, and shows preference for dipeptides containing methionine or arginine, followed by hydrophobic tripeptides consisting of leucine or valine residues (PubMed:10769143). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family."}
{"protein": "MDLASAPRGESPPLKAPLVEIEAAEVERSLPQENAAPEEKGSNSQSEYESDSDALDDEWETQSLYEDAIQMIRDDQLRDGTIPGACTLEEAIEFRKRLHEVGKAQFVEETIARDTVTAKKLCTAFGILPPSFLEGAPDEAYHPLLAIAISREFARRQKLPQYNSVDDAVKLLKESKNIIVLTGAGISTSLGIPDFRSKDTGLYSKLENLGLNDPQEVFDIRIFREDPGIFYSIAKDILPTEKKFSPTHGFIRLLQDKGKLLTNYTQNIDNIEANAGVFPENIVQCHGSFATATCVKCQYKVAGDEIYDDIKKGLIPECAQCRKRIAEDSQKPQGQKRKRNSTSAHKDRSKSGEDSSDGEDYEIPTPGVMKPDITFFGEDLPDEFGRRLLHHDRDKVDLVIVIGTSLKVAPVAEVPGVLPPHIPQIYISRTPVAHTNFDIDLLGDCDVVVSELCRRAGWELKHEMISPDEKVDVTPVFGYGSRHVFKVSG", "text": "FUNCTION: NAD-dependent histone deacetylase, which could function in telomeric silencing, cell cycle progression and chromosome stability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the sirtuin family. Class I subfamily."}
{"protein": "MATQQRPFHLVVFGASGFTGQFVTEEVAREQVSPERTSHLPWAVAGRSREKLLRVLERAAMKLGRPTLSSEVGIIICDITNPASLDEMAKQATVVLNCVGPYRFYGEPVIKACIENGTSCIDISGEPQFLELMYWKYHEKAAEKGVYIIGSSGFDSIPADLGVIYTRNKMNGTLTAVESFLTISSGPEGLCVHDGTWKSAVYGFGDKSNLKKLRNESDMKPVPIVGPKLKRRWPISYCRELNSYSIPFLGADVSVVKRTQRYLHENLEQSPVQYAAYINVGGITSVIKLMFAGLFFLFFVRFGIGRQLLIKFTWLFSFGYFSKQGPTQKQIDASSFTMTFFGQGFSQGVSPVKNKPNIRICTQVKGPEAGYVSTSIAMVQAAMILLNDASDLPKAGGVFTPGAAFSRTKLIDRLNEHGIEFSVISSTEV", "text": "SIMILARITY: Belongs to the saccharopine dehydrogenase family."}
{"protein": "MTAAAPTDVCIIISAKNAADTIARAVASALAEPEAAEVVVIDDGSTDDSASVARAADDGTGRLNVVRFEENRGPAAARNHAIAISHSPLIGVLDADDFFFPGRLGQLLSQDGWDFIADNIAFIDAAQAATAHGRIDRFAPTPRLIDLVGFVEGNISRRGVRRGEIGFLKPLMRRAFLDQHGLRYNETLRLGEDYDLYARALANGARYKIIHSCGYAAVVRGNSLSGSHRTIDLKRLYEADRAILAGSRLSSDAEAAVRRHERHIRDRYELRHFLDLKNQQGFGRAFGYALTHPAALPAIIGGILADKTERFRPSGSPAPVALGGKGDVRYLLETLAVDQPQK", "text": "FUNCTION: Glycosyltransferase required for the synthesis of succinoglycan (EPS I). Needed for the addition of the sixth sugar (glucose), catalyzes the formation of a beta-1,6 linkage between the fifth and sixth sugar. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MGKKKNSNKSAAAAPAVKHNDRWSSIELGEAKSAAVSHYKEPSKEPKFVHPAKLEKVKRIHDGLNIDRVLSHGPVPKQNGGTKRKHVEVTTQKLENKKPKVEVKKEDEKSKNKKMKNQNKHTALVQNETSTRSTYFVEEPDNENKVTLISNGREIAFKKTEVVESDDEQMIGLDSDEELEDEDETDIDEDEMMIDPKDIERYINFESVEDEEDMEDEEIEDEEFEDEEFEDEEEEADEQEEEEEDVSDEESVVSEMDADSDDEGFIAGKDREAHVISKDKFTRNAPAVDFDKFPFTDEDSVVTSSRAFGFMISPCDVQTFFDKFYQSNVLVVRRKQPTYFGNLFSTARLGELLEKNHLEYGRNINIAQYKNGVRTTLNGQGRAYPQIVKQHLHNMCSVQLVNPQTYDDRIWYLCEVIQEQFGCFVGANTYLTPAGSSGFAPHWDEIDAFLLQVEGRKYWRVWAPESAEEELPLESSDNFTEDDMKGREPVFEGWIEKGDMIYIPRGYIHQARTDSKVHSLHVTVSTGRQWSFANLMEKVVPEAIGVLTDTRHKLRRGLPTGLFDMGGVIDLDYSQEDHFVEKFKMVVDRHMSMLRNLVADQLLESSVDSLAKEFMKQALPPRLTEQEKKLSVLGSSTNLLGDDLVDFTARTKVRLIRRHTQRLLMESEDACFISHRINNSRLFEGRPEQIVEYPISGIDAYRVLSNSYPEWRTLYEIFSLRETKTKSRKENLAAIQLLFQIGVLLVKN", "text": "FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys- 4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Mediates response to multiple stress stimuli, including heat shock and osmotic, oxidative, and ethanol stress. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ROX family. NO66 subfamily."}
{"protein": "MNIIYSTVNSLRDRYTPASHTSTFRNTGEITPEEFVAAGDYLVFKFPSWTWSDAETPAKRVAHLPPEKQYLVTRNVPCHRRLNDDFAGDAGHEEAVVEGGKNSGDDGWLRTGGLASSQPLKARDVRTVDDAGNVADRGAIDDEDDIPDMEEEEDDEAIIQDGSHGKHSGSRTYSLYITYSPWYKTPRMYMLGYQPNGQALIPHLMMEDIVGDYKDKTVTLEDFPFFATSVKTASIHPCKHAPVMKTLLDRADAALKLRKERQKAGLEVGSNQGLEGLEAQVVKLAVSGTGTDVANDANDEWEEVQHDAADQDVAIRVDQYLFIASVTPGIEHDFTMGV", "text": "FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C- terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATG3 family."}
{"protein": "MLKYHFPNVCEDELINIYSYGDFKGQGKYICLFKIENQSFLFWRNDKGNKIYTNLESISVEIINTNNTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVYTQDLIDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLNVYTQDLIDTYNQSQNCDCGCK", "text": "FUNCTION: A protein probably derived from this gene is found in cuboidal crystalline inclusions, but is not toxic even when coexpressed with upstream ORF1. The protein runs anomalously as a 50 kDa band in gels."}
{"protein": "MEELSSVGEQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPRLLLAFQKKEHEKEVQNRKRGKRPRGRPRKHTVTSSCSRRSKLKEPDAPSKSKSSSSSSSSTSSSSSSDEEEDDSDLDSKRGPRGRETHPVPQKKAQILVAKPELKDPIRKKRGRKPLPPEQKAARRPVSLAKVLKTTRKDLGTSAAKLPPPLSAPVAGLAALKAHTKEACGGPSTMATPENLASLMKGMAGSPSRGGIWQSSIVHYMNRMSQSQVQAASRLALKAQATNKCGLGLDLKVRTQKGGELGGSPAGGKVPKAPGGGAAEQQRGNHSGSPGAQLAPTQELSLQVLDLQSVKNGVPGVGLLARHAPAKAIPATNPATGKGPGSGPTGANMTNAPTDNNKGEKLTCKATALPAPSVKRDTVKSVAASGGQEGHTAPGEGRKPPALSELSTGEENSSSDSDPDSTSLPSAAQNLSVAIQTSQDWKPTRSLIEHVFVTDVTANLITVTVKESPTSVGFFNLRHY", "text": "FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (By similarity). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3) (PubMed:16537902). Plays a role in the lineage differentiation of the germ layers in embryonic development (PubMed:22226355). Involved in sexual development, acting as activator of NR5A1 expression (By similarity). SUBCELLULAR LOCATION: Nucleus speckle Chromosome Note=Localizes to the inactivated X chromosome in females."}
{"protein": "MSMHYEDYMRQVVEPMRRELTERGFKELLTPEEVEQYMESAEGTTLVVINSVCGCAAGLARPAAVTSLAHDKHPDHLVTVFAGQEKEATAKMREYLAPNPPSSPSMALFKGKELVHFIPREEIEGAEPEALIRRLAMAYNEHCE", "text": "SIMILARITY: Belongs to the UPF0403 family."}
{"protein": "MASLFGDDGVDDLFNDNIPTDPDQLPSDGEGEKLFADDEDNGVEPGSQDAQIVEPKKRAVRNPRPRLTVETLRGPRGIQTIEDYFKDIKFKGKGYEKTDLDEVLRRLQHWGHRMYPTYTFDDVLNNIERLGKKKPLQVHMARYRLGQLEQMRAHEAEALEEAQDEQQEGAGDEPFDEFDALLGEQIAMSRLAPPSPQQWKMSTASSNSTLATPSFSRGNAVMSTPYSGVNATFDRSGASVAPAFDRNGAPLASMDISDYGQPLPPSQPPTPAAKKLSNEQMARIAENRRLAQERLKAKQQQESGSKS", "text": "FUNCTION: Required for normal progression of S-phase. Important for cell survival after DNA damage or replication stress (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CSM3 family."}
{"protein": "MPEGPSVRKFHHLVSPFVGQQVVKTGGSSKKLNPTSFQSLWLQDSQVHGKKLFLRFDPDEEAVSLGNSLLSEPLREGEQKDKARHHQEASDPSSWSPGGDSAVPSGDDGLQCLGGDTPAGGAERWLQVSFGLFGSIRVNEFSRAKKANKRGDWRDPVPRLVLHFSGSGFLAFYNCQMTWRFSSPVVSPASDILSEKFHRGQALEALGREQPICYTLLDQRYFSGLGNIIKNEALFRAGIHPLSPGSLLGLPRLEALVDHVVAFSADWLQGKFQGTRQHTQIYQKEQCPAGHQVVRESLGPPGGFQRLTWWCPQCQPRLSADEPKQLQPS", "text": "FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5- hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FPG family."}
{"protein": "MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEADGGLKSWRESCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEAQTAKEFIKIIEHAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKVDWNKILSYKIGKEMQNA", "text": "FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (By similarity). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the F-actin-capping protein alpha subunit family."}
{"protein": "MQPWLWLVFSMKLAALWSSSALIQTPSSLLVQTNHTAKMSCEVKSISKLTSIYWLRERQDPKDKYFEFLASWSSSKGVLYGESVDKKRNIILESSDSRRPFLSIMNVKPEDSDFYFCATVGSPKMVFGTGTKLTVVDVLPTTAPTKKTTLKMKKKKQCPFPHPETQKGLTCSLTTLSLLVVCILLLLAFLGVAVYFYCVRRRARIHFMKQFHK", "text": "FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A palmitoylation site in the cytoplasmic tail of CD8B chain contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. Once LCK recruited, it initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). Additionally, plays a critical role in thymic selection of CD8+ T- cells. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein. Note=Requires the partner CD8A for efficient cell surface expression. The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail palmitoylation."}
{"protein": "MALTQEDIINAVAEMSVMEVAELVSAMEEKFGVSAAAAVVAGPGGGEAEEAEEQTEFDLVLTSAGEKKVNVIKVVREITGLGLKEAKAAVDGAPATLKEGMSKEDGDEAKTKLEEAGASVELK", "text": "FUNCTION: Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation. FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family."}
{"protein": "MNKKRDFIDTKDFSKEEILFMIEIGRKMKESIKNGHYPQLLKHKTLGMIFEQSSTRTRVSFETAMTQLGGHAQYLAPGQIQLGGHESVGDTAKVLSRLVDILMARVERHQTVVELANTAAIPVINGMSDYNHPTQELGDAITMFEHLPKGKKIEDCKIVFVGDATQVCASTMFMATKLGMDFVQFGPKGFQLREEHLKVAEENCEVSGGSYLITEDVDIALKDADFIYTDVWYGLYEAELSEEERMKTFYPKYQVNKELISKAAPHVKFMHCLPATRGEEVTDEVLDAPYSVVIDEAENRLTAMRALLVYFMNPYVKEAGFAVAEKYDAELELLLRNGAGL", "text": "FUNCTION: Catalyzes the phosphorolysis of N-carbamoylputrescine to form carbamoyl phosphate and putrescine. Is involved in the degradation pathway of the polyamine agmatine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. PTCase family."}
{"protein": "MVPPVQVSPLIKLGRYSALFLGVAYGAKRYNYLKPRAEEERRIAAEEKKKQDELKRIERELAEAQEDSILK", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase e subunit family."}
{"protein": "MGSRRITLLGALFAVLAVAIEGRTLLTHNLKAEAAETVDAVSSVVAGSAGRQLLVSEPHDYNYEKVGFDWTGGVCVNTGTSKQSPINIETDSLAEESERLGTADDTSRLALKGLLSSSYQLTSEVAINLEQDMQFSFNAPDEDLPQLTIGGVVHTFKPVQIHFHHFASEHAIDGQLYPLEAHMVMASQNDGSDQLAVIGIMYKYGEEDPFLKRLQETAQSNGEAGDKNVELNSFSINVARDLLPESDLTYYGYDGSLTTPGCDERVKWHVFKEARTVSVAQLKVFSEVTLAAHPEATVTNNRVIQPLNGRKVYEYKGEPNDKYNYVQHGFDWRDNGLDSCAGDVQSPIDIVTSTLQAGSSRSDVSSVNLMTLNTDAFTLTGNTVNIGQGMQINFGDPPAGDLPVIRIGTRDVTFRPLQVHWHFFLSEHTVDGVHYPLEAHIVMKDNDNLGDSAGQLAVIGIMYKYGDADPFITDMQKRVSDKIASGAITYGQSGVSLNNPDDPFNVNIKNNFLPSELGYAGYDGSLTTPPCSEIVKWHVFLEPRTVSVEQMEVFADVTLNSNPGATVTTNRMIQPLEGRTVYGYNGAAA", "text": "FUNCTION: Reversible hydration of carbon dioxide. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
{"protein": "MSEEEKPKPKLSPALAAKMAAMKKKQEGGEEAAASQEGGEKPKAKLSPMMAARMAAKKSGDASPAPDKPKAEPVDENRDPEPHEMAYRVIKEKFGDAVSDLDNNPLMPFFTVENVDAWQAIAFFMREDERLRFDYMACLSGVDYGDGRLGVVYNFDALATHKHKLTVKVFCSKEDPRIPSVAEIWLTADWHEREAYDMYGIVFEGHPDMRRILCPDDWDGYPLRKDYKVQEVYHGIKVPY", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 30 kDa subunit family."}
{"protein": "MGSAFDPLVTATEDLAAVNSAPPLSNLTQEELKKIAAYKAVEFVESGMVIGLGTGSTAKHAVARISELLREGKLKDIIGIPTSTTTHEQAVSLGIPLSDLDSHPVVDLSIDGADEVDPALNLVKGRGGSLLREKMIEGASKKFVVIVDESKLVKYIGGSGLAVPVEVVPFCCDFTRGKLEELFRDSGCVAKLRMKIGSNGEEAAPAVTDNRNYVVDLYLERDIGDLEVASEAILRFPGVVEHGMFLGMATTLIVAGKFGVTVKDRFG", "text": "FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribose 5-phosphate isomerase family."}
{"protein": "MASSSTLANDDWKQGLAAPPKDLRPQTEDVTATQGSRFEDFGLRRELLMGIYTAGFERPSPIQEQAIPMALTGRDILARAKNGTGKTASFIIPTLNRINTSLSHIQALILVPTRELALQTSQVCKTLGAHIPNLQVMITTGGTTLRDDILRLQQPVHILVGTPGRILDLGSKGIAGLNKCGIFVMDEADKLLSEDFMPVIEQTLALCPQERQVMLFSATFPWTVKEFKDQHMVQPYEINLMDELTLKGVTQYYAYVEESQKVHCLNTLFSKLQINQSIIFCNSTNRVELLAKKVTELGYSCFYSHAKMQQAHRNRVFHDFRNGMTRNLVCSDLLTRGIDIQAVNVVINFDFPRTAESYLHRIGRSGRFGHLGLAISLLTLEDRHNLYRIESELGTEIAPIPAVIDPVLYVAPAMVEEERESPPPKPAAIAAPPAQQQPQQRQRQHPPVPSHQVAHHSPAAAPIQQQQQQQQQQQQPQYQLAYGQGPPQPQVPFQQANSSPAPAPLPSYPQQAPTQAQGPAQMQSPPSEPATQPQASAQIPVQGQTPPIQPRAQQQGQQQPSQPGQAEGQSQPNRRPNTGGFRGNGRGQGHRGRGRGRGGQPGHPGAGASQSQQAQA", "text": "FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity). Blocks autophagy in nutrient-rich conditions by, at least partly, binding and repressing the expression of a set of ATG genes, including ATG3, ATG7, ATG8, ATG19, ATG20 and ATG22 (PubMed:26098573). VAD1-mediated repression of autophagy is regulated by TOR-dependent phosphorylation of the decapping enzyme DCP2 (PubMed:26098573). Regulates multiple virulence- associated genes (PubMed:15765146). Repression of autophagy by VAD1 also regulates the pathogenesis (PubMed:26098573). SUBCELLULAR LOCATION: Cytoplasm, P-body Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily."}
{"protein": "MAHIPSGGAPAAGAAPMGPQYCVCKVELSVSGQNLLDRDVTSKSDPFCVLFTENNGRWIEYDRTETAINNLNPAFSKKFVLDYHFEEVQKLKFALFDQDKSSMRLDEHDFLGQFSCSLGTIVSSKKITRPLLLLNDKPAGKGLITIAAQELSDNRVITLSLAGRRLDKKDLFGKSDPFLEFYKPGDDGKWMLVHRTEVIKYTLDPVWKPFTVPLVSLCDGDMEKPIQVMCYDYDNDGGHDFIGEFQTSVSQMCEARDSVPLEFECINPKKQRKKKNYKNSGIIILRSCKINRDYSFLDYILGGCQLMFTVGIDFTASNGNPLDPSSLHYINPMGTNEYLSAIWAVGQIIQDYDSDKMFPALGFGAQLPPDWKVSHEFAINFNPTNPFCSGVDGIAQAYSACLPHIRFYGPTNFSPIVNHVARFAAQATQQRTATQYFILLIITDGVISDMEETRHAVVQASKLPMSIIIVGVGNADFAAMEFLDGDSRMLRSHTGEEAARDIVQFVPFREFRNAAKETLAKAVLAELPQQVVQYFKHKNLPPTNSEPA", "text": "FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Exhibits calcium- dependent cell membrane binding properties. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane Note=Translocates to the cell membrane and the nucleus in a calcium-dependent manner. Colocalizes with CD2 at the cell membrane. SIMILARITY: Belongs to the copine family."}
{"protein": "MDLVYGLVWLLTVLLEGISGQGVYAPPTVRIVHSGLACNIEEERYSERVYTIREGETLELTCLVTGHPRPQIRWTKTAGSASDRFQDSSVFNETLRITSIQRHQGGRYYCKAENGLGSPAIKSIRVDVYYLDDPVVTVHQSIGEAKEQFYYERTVFLRCVANSNPPVRYSWRRGQEVLLQGSDKGVEIYEPFFTQGETKILKLKNLRPQDYANYSCIASVRNVCNIPDKMVSFRLSNKTASPSIKLLVDDPIVVNPGEAITLVCVTTGGEPMPSLTWVRSFGTLPEKIVLNGGTLTIPAITSDDAGTYSCIANNNVGNPAKKSTNIIVRALKKGRFWITPDPYHKDDNIQIGREVKISCQVEAVPSEELTFSWFKNGRPLRSSERMVITQTDPDVSPGTTNLDIIDLKFTDFGTYTCVASLKGGGISDISIDVNISSSTVPPNLTVPQEKSPLVTREGDTIELQCQVTGKPKPIILWSRADKEVAMPDGTMQMESYDGTLRIVNVSREMSGMYRCQTSQYNGFNVKPREALVQLIVQYPPAVEPAFLEIRQGQDRSVTMSCRVLRAYPIRVLTYEWRLGNKLLRTGQFDSQEYTEYPLKSLSNENYGVYNCSIINEAGAGRCSFLVTGKAYAPEFYYDTYNPVWQNRHRVYSYSLQWTQMNPDAVDRIVAYRLGIRQAGQQRWWEQEIKINGNIQKGELITYNLTELIKPEAYEVRLTPLTKFGEGDSTIRVIKYTGEFHCGFEDGNICLFTQDDTDNFDWTKQSTATRNTKYTPNTGPNADRSGSKEGFYMYIETSRPRLEGEKARLLSPVFSIAPKNPYGPTNSAYCFSFFYHMYGQHIGVLNVYLRLKGQTTIENPLWSSSGNKGQRWNEAHVNIYPITSFQLIFEGIRGPGIEGDIAIDDVSIAEGECAKQDLPTKNSVDGAVGILVHIWLFPVIILISILSPRR", "text": "FUNCTION: May be involved in cell-cell interactions. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor."}
{"protein": "MAELLAIKWDDNRDKLILLDQTILPNKIEYIEYDTAEGVYDSIKDMIVRGAPAIGVTAAYGLYFAAKVAPEDNFENFFKYLKEKSSYLDSSRPTAVNLSWALKVMESKALENKDKDVKEIKSILREEAKRIHEEDIEICKAIGENLITLLKDGVGILTHCNAGQLATSKYGTATSPMYLAKEKGWNFKVYSDETRPRLQGSTLTALELYEAGIDVTTITDNMAAMVMSQGKIDAVIVGCDRIAANGDTANKIGTMGVSILAKYFGIPMYIAAPTPSIDMNTKTGKDIPIEERNSEEITSRFGVWTAPKGVKVYNPGFDVTPHENITAIVTEKGIVYPPFKENLKKLFEK", "text": "FUNCTION: Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1- phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family. DrdI subfamily."}
{"protein": "MDPSEYFAGGNPSDQQNQKRQLQICGPRPSPLSVHKDSHKIKKPPKHPAPPPNRDQPPPYIPREPVVIYAVSPKVVHATASEFMNVVQRLTGISSGVFLESGGGGDVSPAARLASTENASPRGGKEPAARDETVEINTAMEEAAEFGGYAPGILSPSPALLPTASTGIFSPMYHQGGMFSPAIPLGLFSPAGFMSPFRSPGFTSLVASPTFADFFSHIWDQD", "text": "FUNCTION: Regulator of plant defense response. May contribute to MPK4- regulated defense activation by coupling the kinase to specific WRKY transcription factors. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MFSTKKSQGNLHKYIQRQSTDEFAVKAREHNYRARSAFKLIEINEKFKFLKPESTVIDIGCAPGSWLQVVVQKCPNGYASGVDLQNVLPIRGADILSLSDITDPAVKLKIREKLAHRQVDVVLSDMAPNPTGDNATDHLRLIELCRSVFRLFSVENEIELVKNGVYLCKIWDGSARAEFVRELSDRFSTVKTVKPTACRDNSAELYLFCRNFKK", "text": "FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 808 (Um808) in the mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family."}
{"protein": "MESTNLKNAKHETLVMDPISFQSKAQEVSRFSENSNPNFVSHSTPLEKSSKSSAQKNPKWKPNPVPAVFSPRNRIRERRFVVVKKNSRKEKNDSASVDCKCGAKTISNMKKCVCIAYETLRASQEEFFNNRRESVSEIGESSQNLEDGNEQVEFGDSDETRVSLMKRRREKVLEEARMSIPEFGKVMHLVKAFEKLTCFPLSKVTSKEEEDQIKQPLKWELPGMSQPKCSESETDQFTWSSSFYPSSGLILTATNLGLEQPHASVSSSWDNSVSSLNSNGGRRGRRNSFESSASMGSRRSTKKQIKVTSLKPFKLRTEERGRMKEEEFAKKLHEMTLEKAKKRIPIAQGLPWTTDEPENLVKPHVKDITIPVDLKLHSDIRAVERAEFDYQVTEKINLVEQYKTERERQQKLAEEEEIRRLRKELVPKAQPMPYFDRPFIPKRSNKHPTVPRDPKFNIPQHKKIRCCSTSSWSDTGSYMSDLLYQQDL", "text": "FUNCTION: Binds directly to microtubules (PubMed:29167353). Microtubule-destabilizing protein involved in the PIF3-dependent positive regulation of hypocotyl cell elongation via the modulation of cortical microtubules dynamic in response to light and ethylene signaling (PubMed:29167353, PubMed:31638649). Promotes submergence- induced and ethylene-dependent underwater hypocotyl elongation (PubMed:31638649). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Associated with microtubules. SIMILARITY: Belongs to the TPX2 family."}
{"protein": "MLKIILPTIMLLPTALLSPAKSMWTNTTMYSLLIASISLHWLTPSYYPTKTLTLWTGMDQISTPLLVLSCWFLPLMIMASQGHLQHEPHKRKRMFISTLIIIQPFIILAFSATELMLFYISFEATLIPTLILITRWGNQPERLSAGIYLLFYTLISSLPLLVSILYLHTNTGTLHLPIIKLTHPNLPASWTSLLSSLALLMAFMVKAPLYGLHLWLPKAHVEAPIAGSMLLAALLLKLGGYGIMRVTLLMEPVSNFLHYPFLTLALWGALMTSSICLRQTDLKSLIAYSSVSHMGLVIAASMIQTQWSFSGAMILMISHGLTSSLLFCLANTNYERTHSRILILTRGLQPLLPLMSVWWLLANLTNMALPPTTNLMAELTIMVALFNWSSPTIILTGTATLLTASYTLYMLLSTQRGTLPSHITTTPNSNTREHLLMTLHIIPMLTLILKPELISGTPL", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family."}
{"protein": "MANFIKPYNDDPFVGHLATPITSSSLTRALLKNLPAYRFGLTPLLRGLEIGLAHGYFLIGPFAQLGPLRNSDIGLLAGFLSTIGLILILTLGLTIYGAAAFGQEKSNGSELQTKKSWDQFKGGFFVGACGSAGFAFICLSSIPTFALN", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaL family."}
{"protein": "MSKSFQQSSLGRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDTDQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNKEWSQHINGASHSRRCQLLLEIYPEWNPDNDTGHTMGDPFMLQQSTNPAPGILGPPPPSFHLGGPAVGPRGNLGAGNGNLQGPRHMQKGRVETSRVVHIMDFQRGKNLRYQLLQLVEPFGVISNHLILNKINEAFIEMATTEDAQAAVDYYTTTPALVFGKPVRVHLSQKYKRIKKPEGKPDQKFDQKQELGRVIHLSNLPHSGYSDSAVLKLAEPYGKIKNYILMRMKSQAFIEMETREDAMAMVDHCLKKALWFQGRCVKVDLSEKYKKLVLRIPNRGIDLLKKDKSRKRSYSPDGKESPSDKKSKTDAQKTESPAEGKEQEEKSGEDGEKDTKDDQTEQEPSMLLESEDELLVDEEEAAALLESGSSVGDETDLANLGDVSSDGKKEPSDKAVKKDPSASATSKKKLKKVDKIEELDQENEAALENGIKNEENTEPGAESAENADDPNKDTSENADGQNDENKEDYTIPDEYRIGPYQPNVPVGIDYVIPKTGFYCKLCSLFYTNEEVAKNTHCSSLPHYQKLKKFLNKLAEERRQKKET", "text": "FUNCTION: May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs. May bind to specific miRNA hairpins. SUBCELLULAR LOCATION: Nucleus matrix."}
{"protein": "MQEKTKRIIKEDIEAVRAYSDCFDVEMPDLDENGEVIGLPAPYPREVAGTVRSGYRIYDLAKKAKERGWPIQNPILGRNTAEETYGESQEMYAYADKFDETLFHFVHAEATRHIDPLKGRELINQSRGKGGITPIGEREFIAMGGGSKHPVRINATGDTPHLSIINALIAGFDGTDIGPVIHVHFGGRGIHDYKTKVVNGYKAIQICAENNIFVQLDSHKHLNNIGGTDGMALAMCLLSEGLAVHAGLPWELSAIQMNVAGINIYADLAVMRAFRKACHSKSIIAVPETFQNPPGNLVAEAAHFSRMAVTAKLGGADFYRPKAAESVGIPTGDSMGQAIWGTEDVFGHVVNPDIQSPVIDAREAEIIDEALAVLEATLHLEGLTLEAMTDDFWKQWSDEALIDLIVAAGKAGVLDSQRAAGWDLKRHVVVNRDKDGITRYVKGYTPLGVDASRCAQSDEDVEVHVEKAPTRPEKIVLATVGADAHVNGINVIREAFQDAGYDVVYLRGMNLPESVAEVAAEVGADAVGVSNLLGLGMELFPRVSKRLEELGLRDKMVVCAGGRIAEKEEEHRQFEEKIQKEGSAFMGMDGFFGPGSSPEDCVKIIGDMINAKKA", "text": "FUNCTION: Involved in the fermentation of nicotinate to ammonia, propionate, acetate and carbon dioxide."}
{"protein": "MSATSVDQRPKGQGNKVSVQNGSIHQKDAVNDDDFEPYLSSQTNQNNSYPPMSDPYMPSYYAPSIGFPYSLGEAAWSTAGDQPMPYLTTYGQMSNGEHHYIPDGVFSQPGALGNTPPFLGQHGFNFFPGNADFSTWGTSGSQGQSTQNSAYSSSYGYPPSSLGRAITDGQAGFGNDTLSKVPGISSIEQGMTGLKIGGDLTAAVTKTVGTALSSSGMTSIATNNVPPVSSAAPKPTSWAAIARKPAKPQPKLKPKGNVGIGGSAVPPPPIKHNMNIGTWDEKGSVVKAPPTQPVLPPQTIIQQPQPLIQPPPLVQSQLPQQQPQPPQPQQQQGPQPQAQPHQVQSQQPQLQNRWVAPRNRGTGFNQNNGTGSENFGLGVVPVSASPSSVEVHPVLEKLKAINNYNPKDFDWNLKNGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDAAYRSLNGKGPLYLLFSVNGSGHFCGVAEMKSVVDYNAYAGVWSQDKWKGKFEVKWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIIATFKHTTSIFDDFAHYEKRQEEEEAMRRERNRNKQ", "text": "FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)- containing RNAs, and regulates their stability (PubMed:32905781, PubMed:32943573). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:32943573). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex or PAN3 (PubMed:32943573, PubMed:32905781). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:32943573). Acts as a negative regulator of type I interferon response by down-regulating interferon-stimulated genes (ISGs) expression: acts by binding to FOXO3 mRNAs (PubMed:30591559). Binds to FOXO3 mRNAs independently of METTL3-mediated m6A modification (PubMed:30591559). Can also act as a regulator of mRNA stability in cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting their degradation (By similarity). Recognizes and binds m6A-containing circular RNAs (circRNAs); circRNAs are generated through back-splicing of pre-mRNAs, a non-canonical splicing process promoted by dsRNA structures across circularizing exons (By similarity). Promotes formation of phase-separated membraneless compartments, such as P- bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (By similarity). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (By similarity). May also recognize and bind N1- methyladenosine (m1A)-containing mRNAs: inhibits trophoblast invasion by binding to m1A-methylated transcripts of IGF1R, promoting their degradation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, P-body Cytoplasm, Stress granule. SIMILARITY: Belongs to the YTHDF family. YTHDF3 subfamily."}
{"protein": "MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTREGSFRVTTATEQAEREEIMKQLQDAKKAETDKTVGPSVAPGNSAPSPSSPTSPTLDPTASLEMNNPHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNTVPEVEGEAESISSLCSQITSAFSTPCEDPFSSAPMTKPVTLVAPQSPVLQANGTDSALHVLTAKPASTALAPVAMPVRETNPWAHAPDAANKEIAAIHSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPAAIAPPAPPFQGHAFLTSQPVPVGVVPPLQPAFVSTQSYPVANGMPYPASNVPVVGITPSQMVANVFGTAGHPQATHPHQSPSLAKQQTFPQYETSSATTSPFFKPSAQHLNGSAAFNGVDNSGLVSGNRPAQVPPGTCPVDPFEAQWAALESKPKQRTNPSPTNPFSSDAQKAFEIEL", "text": "FUNCTION: Regulates clathrin-mediated receptor endocytosis (By similarity). Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Endosome membrane; Peripheral membrane protein; Cytoplasmic side Note=Localizes to perinuclear endosomes in an AAK1-dependent manner."}
{"protein": "MVKSSLQRILNSHCFAREKEGDKRSATLHASRTMPLLSQHSRGGCSSESSRVALNCCSNLGPGPRWCSDVPHPPLKIPGGRGNSQRDHSLSASILYSDERLNVTEEPTSNDKTRVLSIQSTLTEAKQVTWRAVWSGGGLYIELPAGPLPEGSKDSFAALLEFAEEQLQADHVFICFPKNREDRAALLRTFSFLGFEIVRPGHPLVPKRPDACFMVYTLEREDPGEED", "text": "FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin- independent proteolytic destruction by the 26S proteasome (PubMed:16916800, PubMed:18508777). Triggers ODC degradation by inducing the exposure of a cryptic proteasome-interacting surface of ODC (By similarity). Stabilizes AZIN2 by interfering with its ubiquitination (PubMed:18062773). Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (PubMed:19449338). SIMILARITY: Belongs to the ODC antizyme family."}
{"protein": "MYKKLITFLFVIGAVASYSNNEYTPFNKLSVKLYIDGVDNIENSYTDDNNELVLNFKEYTISIITESCDVGFDSIDIDVINDYKIIDMYTIDSSTIQRRGHTCRISTKLSCHYDKYPYIHKYEGDERQYSITAEGKCYKGIKYEISMMNDDTLLRKHTLKIGFTYIFDRHGHSNTYYSKYDF", "text": "SUBCELLULAR LOCATION: Host endoplasmic reticulum. SIMILARITY: Belongs to the orthopoxvirus OPG192 family."}
{"protein": "MSFAVARMTKLKADNLVGIGNHDQRKTTNHSNEDIDVSHSHLNYDLVAGRTDNFKTDIEAYINENKASKRAVRKDAVLVNEWIITSDKDFFEQLDEAETRKYFETAKQYFADNYGDENIRYAVVHMDEKTPHMHMGIVPFDDDKKLSAKRIFNREALQRIQEELPQYLKENGFDVQRGNKNKERKNLSVPEYKAMREELKKIETEKQETQAKLADTKKQLDEIKPRDTKKIASKPTLMNKNKVTVDKSDLADLEQRAVTSDAYNFEKIHLEVENHSLRNDLSEAKGRNYELRKENERLQKLVGTLQGIIRNVDEFLHKKLGINLPEKWLERAGLKEPSKKAPESSQERSEGHHEELDGPSL", "text": "SIMILARITY: Belongs to the plasmid mobilization pre family."}
{"protein": "MITLLLYLCVICNAIVLIRADSIADPWPEARHLLNTIAKSRDPMKEAAMEPNADEFVGFYVPMDYSPRNEEKNYQSIWQNEITDSQRHIYELLVQSSEQFNNSEATYTLSQIHLWSQYNFPHNMTLAHKYLEKFNDLTHFTNHSAIFDLAVMYATGGCASGNDQTVIPQDSAKALLYYQRAAQLGNLKAKQVLAYKYYSGFNVPRNFHKSLVLYRDIAEQLRKSYSRDEWDIVFPYWESYNVRISDFESGLLGKGLNSVPSSTVRKRTTRPDIGSPFIAQVNGVQMTLQIEPMGRFAFNGNDGNINGDEDDEDASERRIIRIYYAALNDYKGTYSQSRNCERAKNLLELTYKEFQPHVDNLDPLQVFYYVRCLQLLGHMYFTGEGSSKPNIHMAEEILTTSLEISRRAQGPIGRACIDLGLINQYITNNISQAISYYMKAMKTQANNGIVEFQLSKLATSFPEEKIGDPFNLMETAYLNGFIPAIYEFAVMIESGMNSKSSVENTAYLFKTFVDKNEAIMAPKLRTAFAALINDRSEVALWAYSQLAEQGYETAQVSAAYLMYQLPYEFEDPPRTTDQRKTLAISYYTRAFKQGNIDAGVVAGDIYFQMQNYSKAMALYQGAALKYSIQAIWNLGYMHEHGLGVNRDFHLAKRYYDQVSEHDHRFYLASKLSVLKLHLKSWLTWITREKVNYWKPSSPLNPNEDTQHSKTSWYKQLTKILQRMRHKEDSDKAAEDSHKHRTVVQNGANHRGDDQEEASEILGFQMEDLVTMGCILGIFLLSILMSTLAARRGWNVRFNGAQLNANGNRQQEQQQQQQAQGPPGWDFNVQIFAI", "text": "FUNCTION: Component of the endoplasmic reticulum quality control (ERQC) system involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin- conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M. Stabilizes the HRD1 ubiquitin- protein ligase. Also functions in recruiting misfolded protein substrates in conjunction with YOS9. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the sel-1 family."}
{"protein": "MRHLRFLPQEIISSETGIEILEFVVNTLMGDDPEPPVQPFDPPTLHDLYDLEVDGPEDPNEGAVNGFFTDSMLLAADEGLDINPPPETLVTPGVVVESGRGGKKLPDLGAAEMDLRCYEEGFPPSDDEDGETEQSIHTAVNEGVKAASDVFKLDCPELPGHGCKSCEFHRNNTGMKELLCSLCYMRMHCHFIYSPVSDDESPSPDSTTSPPEIQAPAPANVCKPIPVKPKPGKRPAVDKLEDLLEGGDGPLDLSTRKLPRQ", "text": "FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF- mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN- beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By similarity). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the adenoviridae E1A protein family."}
{"protein": "MARRIKFQRLAEMRPTMTRFSTVALIVSKSSPNIFYDKMSGTERGVLSLTIRDSPNHLTNCKCWGQRDCVDEYAAMLQIGHVVDIVGAKVMSIPFAAPGEQRYQPQATVSCALVVNEGSGYVVRHDNDDFGQITILQQLLHQPIRPLGAVLKLADVRSGLGFPDKIITTNVNLLVVVAAVRPVRQIKRKLQGPLSEVQELLQCLEVIVIDASYPEGMLLSVWQPDWIQRAQQWQPRRTVLHLIDVRVSYSNFHRSLVLSHSNCTLICENPQAAGDDCRLLLAFAATVPLTTFSGCDQAELDNMPAVASIQAQMTVRQIYSRAEGELQDPSIHQFTAVLYGMVTKFDLDGLTSHVNRKCIACQQHIPRNLQDCASDACQQYFSLDNDEPRSISYFNINIHLSDQTGTLVEARLAGHPAERILGLRAEDFERLAEREKSELKWRFLLKYFEVRLMIKKPVGVRNHLVIVVVDMQAIPLEKLVANMVVF", "text": "FUNCTION: Single-stranded DNA-binding protein required for meiosis. May be involved in the resolution of recombination intermediates into crossovers in the meiotic recombination pathway. SIMILARITY: Belongs to the MEIOB family."}
{"protein": "MNWLNQHKKAIILAASAAVFTAIMIFLATGKNKEPVKQAVPTETENTVVKQEANNDESNETIVIDIKGAVQHPGVYEMRTGDRVSQAIEKAGGTSEQADEAQVNLAEILQDGTVVYIPKKGEETAVQQGGGGSVQSDGGKGALVNINTATLEELQGISGVGPSKAEAIIAYREENGRFQTIEDITKVSGIGEKSFEKIKSSITVK", "text": "FUNCTION: Needed for both DNA binding and transport. It is absolutely required for the uptake of transforming DNA but not for binding. Its role in binding may be indirect. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Note=Localizes in a nonuniform, punctate manner in competent cells, unlike some other competence proteins is not localized to the cell poles (PubMed:16009133)."}
{"protein": "RPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAHEITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQPEPEIPPELPPPRPHVRCC", "text": "FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy (By similarity). SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Lysosome membrane; Lipid-anchor; Cytoplasmic side Golgi apparatus membrane Cytoplasmic vesicle, autophagosome. SIMILARITY: Belongs to the small GTPase superfamily. Rab family."}
{"protein": "MLLLWILSLFLETVAGGEVCFDRLGCFSDNKPWAGTSERPRKGLPWDPSAINVRFLLYTNENPNNYQRITADSSVIRSSDFKTDRKTRFIIHGFIDKGEENWLADLCKALFQVESVNCICVDWRGGSRTLYSQASQNIQVVGAEVAYLINFLQSQLDYPPSSVHIIGHSLGSHAAGEAGRRTNGAIGRITGLDPAEPYFQYTPEIVRLDPSDAQFVDVIHTDGNPIIPNLGFGMSQTVGHLDFFPNGGLQMPGCQKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYIDSITNPKGFAGFSCDSYSSFSSNKCFPCATGECPQMGHYADKFPGKTKENFQNFYLNTGDKSNFSRWRYRIAVTLSGQKVTGHVLVSLFGDAGNTKQYEIYRGSLKPGNNHSNEIDSDVDVGDLQKVKFIWYNNVINITLPKVGASRITVTRSDGRVFDFCSQDTVREEVLLTLQPC", "text": "FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MSVTKSTEGPQGAVAIKLDLMSPPESAKKLENKDSTFLDESPSESAGLKKTKGITVFQALIHLVKGNMGTGILGLPLAVKNAGILMGPLSLLVMGFIACHCMHILVKCAQRFCKRLNKPFMDYGDTVMHGLEANPNAWLQNHAHWGRHIVSFFLIITQLGFCCVYIVFLADNLKQVVEAVNSTTNNCYSNETVILTPTMDSRLYMLSFLPFLVLLVLIRNLRILTIFSMLANISMLVSLVIIIQYITQEIPDPSRLPLVASWKTYPLFFGTAIFSFESIGVVLPLENKMKNARHFPAILSLGMSIVTSLYIGMAALGYLRFGDDIKASISLNLPNCWLYQSVKLLYIAGILCTYALQFYVPAEIIIPFAISRVSTRWALPLDLSIRLVMVCLTCLLAILIPRLDLVISLVGSVSGTALALIIPPLLEVTTFYSEGMSPLTIFKDALISILGFVGFVVGTYQALDELLKSEDSHPFSNSTTFVR", "text": "FUNCTION: Electrogenic proton/amino acid symporter with a high selectivity for the small side chains amino acids glycine, alanine and proline, where both L- and D-enantiomers are transported. Extension of the backbone length, as in beta-alanine and 4-aminobutanoate or methylation of the amino group, as in sarcosine and N,N- dimethylglycine, are also tolerated but decrease transport efficiency. A free carboxyl group is preferred. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane Recycling endosome membrane. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family."}
{"protein": "MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHRYVSAIKTLWNDPGIQECYDRRREYQLSDSAKYYLTDVDRIATSGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIVTYPWFQNSSVILFLNKKDLLEDKILFSHLVDYFPEFDGPQRVAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNAQ, required for heart development (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Cytoplasm. SIMILARITY: Belongs to the G-alpha family. G(q) subfamily."}
{"protein": "MRFAWTALLGSLQLCALVRCAPPAASHRQPPREQAAAPGAWRQKIQWENNGQVFSLLSLGSQYQPQRRRDPGATAPGAANATAPQMRTPILLLRNNRTAAARVRTAGPSAAAAGRPRPAARHWFQAGYSTSGAHDAGTSRADNQTAPGEVPTLSNLRPPNRVEVDGMVGDDPYNPYKYTDDNPYYNYYDTYERPRPGSRYRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMAMYNLRCAAEENCLASSAYRXDVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDASTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYNADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYSNNVVRCEIRYTGHHAYASGCTISPY", "text": "FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space. SIMILARITY: Belongs to the lysyl oxidase family."}
{"protein": "MSLFKIRMPETVAEGTRLALRAFSLVVAVDEHGGIGDGRSIPWNVPEDMKFFRDLTTKLRGKNVKPSPAKRNAVVMGRKTWDSIPPKFRPLPGRLNVVLSSTLTTQHLLDGLPDEEKRNLHADSIVAVNGGLEQALRLLASPNYTPSIETVYCIGGGSVYAEALRPPCVHLLQAIYRTTIRASESSCSVFFRVPESGTEAAAGIEWQRETISEELTSANGNETKYYFEKLIPRNREEEQYLSLVDRIIREGNVKHDRTGVGTLSIFGAQMRFSLRNNRLPLLTTKRVFWRGVCEELLWFLRGETYAKKLSDKGVHIWDDNGSRAFLDSRGLTEYEEMDLGPVYGFQWRHFGAAYTHHDANYDGQGVDQIKAIVETLKTNPDDRRMLFTAWNPSALPRMALPPCHLLAQFYVSNGELSCMLYQRSCDMGLGVPFNIASYALLTILIAKATGLRPGELVHTLGDAHVYSNHVEPCNEQLKRVPRAFPYLVFRREREFLEDYEEGDMEVIDYAPYPPISMKMAV", "text": "FUNCTION: Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP. SIMILARITY: In the N-terminal section; belongs to the dihydrofolate reductase family. SIMILARITY: In the C-terminal section; belongs to the thymidylate synthase family."}
{"protein": "MSSIPAGTDPGSCGANFKNDRKRRDKINDRIQELLSIIPKDFFRDYYGNSGSNDTLSESTPGALGLSSKAKGTGTKDGKPNKGQILTQAVEYISHLQNQVDTQNREEVELMVKATQLAKQTGTIVNDINLENTSAEVALSRIGVGPLAATNDDSVRPPAKRLSSFEYGGYGEYGNGS", "text": "FUNCTION: Required for a novel path of interorganelle communication between mitochondria, peroxisomes and the nucleus, thereby maintaining a functional metabolic interaction between the tricarboxylic acid and glyoxylate cycles. Transcription factor that regulates CIT2 gene expression. Binds to two identical sites oriented as inverted repeats 28 bp apart in a regulatory upstream activation sequence element (UASR) in the CIT2 promoter. The core binding site is 5'-GGTCAC-3'. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MQFWKVHGARNDFVLVDETEEEVVPESDKPDFARWACDRRSGVGADGVVFIRSDPPSVEMRIFNRDGSEAEFCGNAARCVVKYVTEVRGENVKILRTLSGAHRVEVQGGWIAVEVPEAEIKKVVELGYEVDAGVPHFVRLTERDPIHDFGGLTDEAKTIFSEYEPKGGVNVTYAAPSVDELRVRTFERGVGWTPACGSGVVAASLVYSEIFGPFEEVSVRTAGGCLRVSLSDGPLLIGRAEIVYKGELRGDWRENTDHQRRRHSLSRSPSGRPRLQECR", "text": "FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diaminopimelate epimerase family."}
{"protein": "MEPPQCVEELEDDVFQPEDGEPGTQPGSLLSADLFAQSQLDCPLSRLQLFPLTHCCGPGLRPVSQEDKATQTLSPASPSQGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAGSALGEQPPEGQFLQHRAEVQIARKLQCIADQFHRLHMQQHQQNRDRAWRQVFLFLQNLALNRRENREGVGPW", "text": "FUNCTION: May play a role in apoptosis. SIMILARITY: Belongs to the Bcl-2 family."}
{"protein": "MAKDNSEKLQVQGEEKKSKQPVNFLPQGKWLKPNEIEYEFGGTTGVIGMLIGFPLLMYYMWICAEFYHGKVALPKAGESWMHFIKHLYQLVLENGIPEKYDWTIFLTFWVFQIIFYYTLPGIWTKGQPLSHLKGKQLPYFCNAMWTLYVTTTLVLVLHFTNLFRLYVIIDRFGRIMTCAIISGFAFSIILYLWTLFISHDYHRMTGNHLYDFFMGAPLNPRWGILDLKMFFEVRLPWFTLYFITLGACLKQWETYGYVTPQLGVVMLAHWLYANACAKGEELIVPTWDMAYEKFGFMLIFWNIAGVPYTYCHCTLYLYYHDPSEYHWSTLYNVSLYVVLLCAYYFFDTANAQKNAFRKQMSGDKTGRKTFPFLPYQILKNPKYMVTSNGSYLLIDGWYTLARKIHYTADWTQSLVWALSCGFNSVFPWFFPVFFLVVLIHRAFRDQAKCKRKYGKDWDEYCKHCPYVFIPYVF", "text": "FUNCTION: C-24(28) sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8125337, PubMed:10722850, PubMed:12882006). ERG4 Catalyzes the last step of ergosterol biosynthesis by converting ergosta-5,7,22,24(28)-tetraen-3beta-ol into ergosterol (PubMed:10722850, PubMed:12882006). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4- dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3- beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron- containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C- methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl- methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen- 3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERG4/ERG24 family."}
{"protein": "MLSRLARTQISRSALLSQTRQLSFDLNETQKEIQAAALKFSKEVLVPNAAKFDESGEFPWEIIRQAHSLGLMNPQIPEKYGGPGMTTLETTLIVEALSYGCTGLQLGIMGPSLAIAPVYIAGNEEQKKKYLGALAAEPIIASYCVTEPGAGSDVNGVKTKCEKKGNEYIINGSKAWITGGGHAKWFFVLARSDPNPKTPAGKAFTAFIVDGDTSGITRGKKEKNMGQRCSDTRTITFEDVRVPEENVLGPPGAGFKVAMSAFDMTRPGVAAGALGLSWRCLDESAKYALQRKAFGTEIANHQAVQFMLSDMAINLELARLITYKSATDVDNGVRSSYNASKSASQRIPRIRRLLMLFRCNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRIVISRMLLGHVAQNGTSRM", "text": "FUNCTION: This enzyme is specific for acyl chain lengths of 4 to 16. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MDTFSTKSLALQAQKKLLSKMASRAVASAFIDDTSSEVLDELYRATKEFTRSRKEAQKLVKNLVKVAVKLGVLLRAGQLGAEELARLQRLRQQARRLAMTAVSFHQVDFTFDRRVLATTLLECRDLLHQAAGAHLTAKSHGRINHVFGHLADCDFLAALYSPAEPYRSHLRRICDGLTRMLDEDSI", "text": "FUNCTION: Acts as a negative regulator of mTOR activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TNFAIP8 family."}
{"protein": "MVDVPRNFRLLEELEEGQKGKGDGNISWGLEDDSDMTLTRWTASIIGPPRTPYESRIYNLQIQCGGNYPREPPTVRFTTKVHMVGVNQSNGVIDKRNLTTLRNWSNSYMIKTVLEDIRKNMMMAKENLKLQQPAEGAMF", "text": "FUNCTION: Involved in protein ubiquitination, but has no ubiquitin ligase activity on its own (PubMed:15530417). The uev-1-ubc-13 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63 (PubMed:15530417, PubMed:24595290). Involved in sorting Lys-63-linked polyubiquitinated maternal membrane proteins for degradation by targeting to multivesicular bodies (PubMed:24595290). Required for glr-1-containing glutamate receptor trafficking in neurons (PubMed:21179194). May have a role in synaptic transmission at motorneurons (PubMed:21179194). May be involved in the ubiquitination and growth of intracellular polyglutamine protein aggregates (PubMed:17663792, PubMed:22494772). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Cell projection, dendrite Perikaryon. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MSNQIYSARYSGVDVYEFIHSTGSIMKRKKDDWVNATHILKAANFAKAKRTRILEKEVLKETHEKVQGGFGKYQGTWVPLNIAKQLAEKFSVYDQLKPLFDFTQTDGSASPPPAPKHHHASKVDRKKAIRSASTSAIMETKRNNKKAEENQFQSSKILGNPTAAPRKRGRPVGSTRGSRRKLGVNLQRSQSDMGFPRPAIPNSSISTTQLPSIRSTMGPQSPTLGILEEERHDSRQQQPQQNNSAQFKEIDLEDGLSSDVEPSQQLQQVFNQNTGFVPQQQSSLIQTQQTESMATSVSSSPSLPTSPGDFADSNPFEERFPGGGTSPIISMIPRYPVTSRPQTSDINDKVNKYLSKLVDYFISNEMKSNKSLPQVLLHPPPHSAPYIDAPIDPELHTAFHWACSMGNLPIAEALYEAGTSIRSTNSQGQTPLMRSSLFHNSYTRRTFPRIFQLLHETVFDIDSQSQTVIHHIVKRKSTTPSAVYYLDVVLSKIKDFSPQYRIELLLNTQDKNGDTALHIASKNGDVVFFNTLVKMGALTTISNKEGLTANEIMNQQYEQMMIQNGTNQHVNSSNTDLNIHVNTNNIETKNDVNSMVIMSPVSPSDYITYPSQIATNISRNIPNVVNSMKQMASIYNDLHEQHDNEIKSLQKTLKSISKTKIQVSLKTLEVLKESSKDENGEAQTNDDFEILSRLQEQNTKKLRKRLIRYKRLIKQKLEYRQTVLLNKLIEDETQATTNNTVEKDNNTLERLELAQELTMLQLQRKNKLSSLVKKFEDNAKIHKYRRIIREGTEMNIEEVDSSLDVILQTLIANNNKNKGAEQIITISNANSHA", "text": "FUNCTION: Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSNPRSLEEEKYDMSGARLALILCVTKAREGSEEDLDALEHMFRQLRFESTMKRDPTAEQFQEELEKFQQAIDSREDPVSCAFVVLMAHGREGFLKGEDGEMVKLENLFEALNNKNCQALRAKPKVYIIQACRGEQRDPGETVGGDEIVMVIKDSPQTIPTYTDALHVYSTVEGYIAYRHDQKGSCFIQTLVDVFTKRKGHILELLTEVTRRMAEAELVQEGKARKTNPEIQSTLRKRLYLQ", "text": "FUNCTION: Non-apoptotic caspase involved in epidermal differentiation. Is the predominant caspase in epidermal stratum corneum (PubMed:15556625). Seems to play a role in keratinocyte differentiation and is required for cornification. Regulates maturation of the epidermis by proteolytically processing filaggrin (By similarity). In vitro has a preference for the substrate [WY]-X-X-D motif and is active on the synthetic caspase substrate WEHD-ACF (PubMed:16854378, PubMed:19960512). Involved in processing of prosaposin in the epidermis (By similarity). May be involved in retinal pigment epithelium cell barrier function (PubMed:25121097). Involved in DNA degradation in differentiated keratinocytes probably by cleaving DFFA/ICAD leading to liberation of DFFB/CAD (PubMed:24743736). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase C14A family."}
{"protein": "MTTSARDTGLDSHELARLHELARHSHAVITRHQDAGGAYPAAPTFSAYRGYAWLRDGSFTAEGISRYGDVASAGRFHDWVDGVLRRRRGQVDDLLAAVDRGEVPSNEGMLPTRFTFDGNDGSDPWWDFQTDGYGMWLWSVVTHAARHGLDLERWRAGIDVAVDYLLAFWDRPCYDWWEEHVEHRHVSTLGAIHGGLVAVGTCAALRSAPWSAATLQVAARIRSLVSAEGVVDGHLVKWLGSSAVDGSLPACVVPFGLVPPDDDVAAMTRAAVAKDLDVDGGVHRFAADVFYGGGQWILLSALLGWNLAAAGDTAGALRHLRWIADQADADGDLPEQVPHHLLHPGSRAEWVARWGTVATPLLWSHGMYLILADELGLLPPAAKDA", "text": "FUNCTION: Involved in the intracellular degradation of the cyclic tetrasaccharide cyclobis-(1-6)-alpha-nigerosyl (CNN) formed extracellularly from starch. Catalyzes the hydrolysis of alpha-1,6- glucosidic linkage from the non-reducing end of isomaltose to yield beta-D-glucose and D-glucose. Can also act on panose and isomaltotriose at a lower rate. It displays low or no activity toward CNN and the general GH15 enzyme substrates such as maltose, soluble starch or dextran. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 15 family."}
{"protein": "MNYGTNNHYANEYGMELNEYFKHHFNYEELAGWYTMQVLKYLVRAGKKEGESYDKDRNKALDYAGELANLSNENELTEYTTDDIMGFAQDIADDFKQWKDERNNFKSEFTKEEIKAIDERYLEFIEEV", "text": "FUNCTION: Involved in the sensitivity of the virus to the host AbiV system. SIMILARITY: Belongs to the skunalikevirus SaV protein family."}
{"protein": "MPAKIHISADGQFCDKDGNEIQLRGVNLDPSVKIPAKPFLSTHAPIENDTFFEDADKVSFINHPLVLDDIEQHIIRLKSLGYNTIRLPFTWESLEHAGPGQYDFDYMDYIVEVLTRINSVQQGMYIYLDPHQDVWSRFSGGSGAPLWTLYCAGFQPANFLATDAAILHNYYIDPKTGREVGKDEESYPKMVWPTNYFKLACQTMFTLFFGGKQYAPKCTINGENIQDYLQGRFNDAIMTLCARIKEKAPELFESNCIIGLESMNEPNCGYIGETNLDVIPKERNLKLGKTPTAFQSFMLGEGIECTIDQYKRTFFGFSKGKPCTINPKGKKAWLSAEERDAIDAKYNWERNPEWKPDTCIWKLHGVWEIQNGKRPVLLKPNYFSQPDATVFINNHFVDYYTGIYNKFREFDQELFIIIQPPVMKPPPNLQNSKILDNRTICACHFYDGMTLMYKTWNKRIGIDTYGLVNKKYSNPAFAVVLGENNIRKCIRKQLSEMQKDAKSMLGKKVPVFFTEIGIPFDMDDKKAYITNDYSSQTAALDALGFALEGSNLSYTLWCYCSINSHIWGDNWNNEDFSIWSPDDKPLYHDTRAKTPTPEPSPASTVASVSTSTSKSGSSQPPSFIKPDNHLDLDSPSCTLKSDLSGFRALDAIMRPFPIQIHGRFEFAEFNLCNKSYLLKLVGKTTPEQITVPTYIFIPRHHFTPSRLSIRSSSGHYTYNTDYQVLEWFHEPGHQFIEICAKSKSRPNTPGSDTSNDLPAECVIS", "text": "FUNCTION: Ergosteryl beta-glucosidase involved in the ergosteryl beta- glucoside (EG) catabolic pathway and vacuole formation via hydrolysis of EG to generate glucose (PubMed:26116408). Is also able to hydrolyze cholesteryl beta-glucoside and sitosteryl beta-glucoside to generate glucose; and C6-7-nitro-2,1,3-benzoxadiazole (NBD)-GlcCer to generate C6-NBD-ceramide (Cer) (PubMed:26116408). SUBCELLULAR LOCATION: Cytoplasm, cytosol Vacuole membrane; Peripheral membrane protein Note=Localizes in the cytosol until the initial logarithmic phase, then targets to a yet unidentified organelle with a granule structure in the middle logarithmic phase, and finally localizes at the vacuole membranes in the stationary phase. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family."}
{"protein": "MSNNPEMNYTSKELDAMSNEELARLGTELDGVTVAYRKERFPVEGDPASKRASRTVGIWFGIGIVSALAFLAVYLFMPWEYKGLGEDGLWIYTFYTPLLGLTSGLAILSLGIGVIFYIKKIIPSEISVQRRHDGPSEEIDRRTITALLNDSWETSTLGRRKVLKSMLGIGGVLAGLTIIAPLGGMVKNPWKKGELGIQGDGTLWTSGWTLHEKGVKLYLGRDTGVTAEKHETSVGTHYSTQGVSRLIRMRPEDLAAAAMETVFPLPAEFVNDGDKYDASADVYEEQMHSIHGPRNAVMLIRLRNSDANKVIEREGQEDFHYGDYYAYSKICTHIGCPTSLYEAQTNRILCPCHQSQFDALHYGKPVFGPAARALPQLPITVDEEGYLVAAGNFIEPVGPAFWERRS", "text": "FUNCTION: Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Rieske iron-sulfur protein family."}
{"protein": "MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPTHQTFFSSSEKLEIGDVAFITENRKPVRIQALSYYREVVKRKNIRVNAFEMVRKVTKTQNNTFVIETSKETYTTPYCIIATGYYDHPNYMGVPGEDLPKVFHYFKEGHPYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEYSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFRSGEKELITIKNDFVFAMTGYHPDHQFLEKIGVEIDKETGRPFFNEETMETNVEGVFIAGVIAAGNNANEIFIENGRFHGGHIAAEIAKRENH", "text": "FUNCTION: S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a NADPH-dependent bacilliredoxin reductase, which debacillithiolates (removes BSH) the S- bacillithiolated BrxB (BrxB-SSB), and to a lesser extent BrxC (BrxC- SSB). Involved in a redox cascade increasing the efficacy of BrxB function by reducing BrxB-SSB and thus reactivating it. Has NADPH- dependent oxidase activity under aerobic conditions producing hydrogen peroxide (H(2)O(2))."}
{"protein": "MREQPKNQISPDGLKVWRLQEIIISAVCLLIVIAVAVLSYYFHWPYWISGVLGAVWLLGSIVTVFIIPKVRHKVWRYEVHEHEIDIQSGIFVVTRVIVPMVRVQHVDTSQGPLLKKYNLATVKISTAATVHSIPALEMEEADRLRDSISRLARVTDDDV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0699 family."}
{"protein": "MWKLWRAEEGAAALGGALFLLLFALGVRQLLKQRRPMGFPPGPPGLPFIGNIYSLAASSELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLICAERR", "text": "FUNCTION: A cytochrome P450 monooxygenase involved in activation of vitamin D precursors. Catalyzes hydroxylation at C-25 of both forms of vitamin D, vitamin D(2) and D(3) (calciol) (PubMed:12867411, PubMed:15465040, PubMed:18511070). Can metabolize vitamin D analogs/prodrugs 1alpha-hydroxyvitamin D(2) (doxercalciferol) and 1alpha-hydroxyvitamin D(3) (alfacalcidol) forming 25-hydroxy derivatives (PubMed:15465040, PubMed:18511070). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:12867411, PubMed:15465040, PubMed:18511070). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MLMPKKNRIAIYELLFKEGVMVAKKDVHMPKHPELADKNVPNLHVMKAMQSLKSRGYVKEQFAWRHFYWYLTNEGIQYLRDYLHLPPEIVPATLRRSRPETGRPRPKGPEGERPARFTRGEADRDTYRRSAVPPGADKKAEAGAGSATEFQFRGGFGRGRGQPPQ", "text": "FUNCTION: Component of the 40S ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. FUNCTION: Component of the 40S ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family."}
{"protein": "MAYLKIVLVALMLVLAVSAMRRPDQQDQDISVAKRVACKCDDDGPDIRSATLTGTVDLGSCDEGWEKCASYYTVIADCCRRPRS", "text": "FUNCTION: Binds specifically to the voltage-gated sodium channel (Nav) and delays its inactivation. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type II subfamily."}
{"protein": "MRGQQTPPQQPTRVRTPRENENEVLGVIEQMLGASRVRVRCMDGKLRMGRIPGKLKRKIWVREDDVVIVTPWEVQSDEKCDVIWRYTKGQVDWLNRKGYLDFMR", "text": "FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits. SIMILARITY: Belongs to the eIF-1A family."}
{"protein": "MAVIQDIIAALWQHDFAALADPHIVSVVYFVMFATLFLENGLLPASFLPGDSLLILAGALIAQGVMDFLPTIAILTAAASLGCWLSYIQGRWLGNTKTVKGWLAQLPAKYHQRATCMFDRHGLLALLAGRFLAFVRTLLPTMAGISGLPNRRFQFFNWLSGLLWVSVVTSFGYALSMIPFVKRHEDQVMTFLMILPIALLTAGLLGTLFVVIKKKYCNA", "text": "FUNCTION: May be a membrane transporter required for proton motive force (PMF)-dependent drug efflux. Required, with YqjA, for the proper export of certain periplasmic amidases and, possibly, other Tat substrates. May play a role in determining membrane lipid composition. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DedA family."}
{"protein": "MAADEEPDSPSGALQTAAEEEETKTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPVFPTQDEEVMMLTERVNEAQRFARMELREHGEKKKRKREDAGDDDDKEGAIGVRNKVAGGKMKKRKGR", "text": "FUNCTION: Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Note=Localizes in the nucleolar-organizing region during ribosome biogenesis. SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily."}
{"protein": "MNGALDHSDQPDPDAIKTFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATTTNANPLSTTTGALGALTSPVAASTANSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQAMNGFQIGMKRLKVQLKRSKNDSKPY", "text": "FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. May be involved in mRNA translation repression and stability. Mediates exon inclusion in TNNT2 pre-mRNA. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. SIMILARITY: Belongs to the CELF/BRUNOL family."}
{"protein": "MDITELLAFSAKQGASDLHLSAGLPPMIRVDGDVRRINLPPLEHKQVHALIYDIMNDKQRKDFEEFLETDFSFEVPGVARFRVNAFNQNRGAGAVFRTIPSKVLTMEELGMGEVFKRVSDVPRGLVLVTGPTGSGKSTTLAAMLDYLNNTKYHHILTIEDPIEFVHESKKCLVNQREVHRDTLGFSEALRSALREDPDIILVGEMRDLETIRLALTAAETGHLVFGTLHTTSAAKTIDRVVDVFPAEEKAMVRSMLSESLQSVISQTLIKKIGGGRVAAHEIMIGTPAIRNLIREDKVAQMYSAIQTGGSLGMQTLDMCLKGLVAKGLISRENAREKAKIPENF", "text": "FUNCTION: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:10377148, PubMed:15629932, PubMed:18174131). Acts as a molecular motor to provide the energy that is required for T4P retraction while antagonist PilB ATPase activity is required for T4P extension (PubMed:26809217). Promotes also PilU retractation activity through direct interaction (PubMed:31626631). SUBCELLULAR LOCATION: Cytoplasm Note=Localizes to cell poles. SIMILARITY: Belongs to the GSP E family."}
{"protein": "MLFNYLRKPNPTNLLTSPDSFRYFEYGMFCMGWHTPATHKIIYYITSCLIFAWCAVYLPIGIIISFKTDINTFTPNELLTVMQLFFNSVGMPFKVLFFNLYISGFYKAKKLLSEMDKRCTTLKERVEVHQGVVRCNKAYLIYQFIYTAYTISTFLSAALSGKLPWRIYNPFVDFRESRSSFWKAALNETALMLFAVTQTLMSDIYPLLYGLILRVHLKLLRLRVESLCTDSGKSDAENEQDLIKCIKDHNLIIDYAAAIRPAVTRTIFVQFLLIGICLGLSMINLLFFADIWTGLATVAYINGLMVQTFPFCFVCDLLKKDCELLVSAIFHSNWINSSRSYKSSLRYFLKNAQKSIAFTAGSIFPISTGSNIKVAKLAFSVVTFVNQLNIADRLTKN", "text": "FUNCTION: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Heteromeric odorant receptor channel (TC 1.A.69) family. Or2a subfamily."}
{"protein": "MNNKLIYRSVRFATHNSQLLLPPLVLYRRILRQHKLLPGPQREMGDQYVRNEFKLHKDIDNPLHIVGFLASWQDYLHMISNGKWKDATLSSETLEKLSPEQTVQLYELMKETQKLHQDNEIESSKDVKRNNKD", "text": "FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDH2 of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. Acts together with SDHAF1 (SDH6). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion intermembrane space Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily."}
{"protein": "MYPRGVKRSQHDRHKQTAFRTIKRSITHRPTSKFISHFAKNFRGKLAPLKQLDESRLDALSLTELEQLKTIIEEKQQEKRAQNNAITFLPNLPTVPFADTNFSIKSLGLRPYNGDARDPKQRIRDRFPQTHERICLLTNDILETDLLLRYRQCLDSLTREENQQLMGDRIFSLTNSPCLAFTVATVEEACSYFKFHDLHNLPVNPQDLFMYTITVMKFEFFNKLNMAKLTCVFNDNGHGDIEYRKLRQLCGKPVLDREMPNSEFEVQQQTPDSFRHPIQQAMSIVVTFARILRQIKEHIIRTKKPQFIRDFDTERVAERYECGLISRLIGKQFSNHKCDDVSCQNRIERIMAPWKPSLFFCTYFAKDAPKFKLFPNLPHEYRNLSFTCPKVDMEPSCSYSTSRDLPQTSHRSHKNQGTPKVKSKVCVEKPDTSNLTTTKTTTEILIEESMETDNKIPDPRELNFNQAKQDEIVIININENVNSKHESESSVEMDLDLDYEADTCETNLNTYSSDSE", "text": "FUNCTION: Immediate early (EI) protein that plays many roles during productive infection including regulation of viral gene expression and nuclear export of intronless viral RNAs. SUBCELLULAR LOCATION: Virion tegument Virion Host nucleus. Host cytoplasm. Note=Shuttles between host nucleus and cytoplasm. SIMILARITY: Belongs to the HHV-1 ICP27 protein family."}
{"protein": "MLSALALSTSSLCLSRYPLRASTVFLASSNIPFPSVSASLARPVATSAIPERPDLLMSPHGGLKAMMYLPLTNSLHQSTCSWLTGPRGFSSPPLFRIRFLLLIMSDSISLTDITISPGTLYSARTLLLRAAVLALTRKPMSFLHFKAACW", "text": "FUNCTION: Disrupts the host mitochondrial membrane potential and induces apoptosis probably by inducing host CASP8 and CASP9."}
{"protein": "MGGCPVRKRRRNGSKEGNHHSTQPKRNKRNPIFQDSQDTEFSWSDNERSSSRINIPERASGPEGNLNQIVTEPDANFPQFLHEGLSKPVYVINWFMSFGPEIKLNTSQQGRNQAV", "text": "SIMILARITY: Belongs to the FAM104 family."}
{"protein": "MPLFGSIFSPKKTPPRKSASLSNLHSLDRSTRELELGLDYGTPTMNLAGQSLKFENGQWVADSVISGGVDRRETQRLRKRNQQLEEENNLLRLKVDILLDMLSETTAESHLKDKELDELKVTNRRRK", "text": "FUNCTION: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta- catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation. SUBCELLULAR LOCATION: Nucleus speckle Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Golgi apparatus Golgi apparatus, trans-Golgi network. SIMILARITY: Belongs to the chibby family."}
{"protein": "MGEEAPEEYELGGGEDERVMEWETGLPGADELTPLSQPLVPAGLAAAFRIPPEPGRTLLDVHRASAATVSRLRRASSSSSSSFPAFASKGAGTGADEAESGGGADGGNGNTNNSSSKRARLVWTPQLHKRFVEVVAHLGMKNAVPKTIMQLMNVEGLTRENVASHLQKYRLYVKRMQGLSNEGPSPSDHIFASTPVPHASLHDQVPSPYHPHPHHHSYNNAAYAATVSSYHHYHHANH", "text": "FUNCTION: Transcription factor that is essential for the generation of the circadian clock oscillation. Binds to specific sites on CCA1 promoter leading to CCA1 activation (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGPRRLPWARPGPALGLLLLALAGAVPAAGGSCSLLEEGNTIQKLHEDCFCYVQNRTMHLQYIWSTVQVKINSTRTFRFVPTPEKSNCRNSETVFEFAACAVQILWRPETSTETFLKIKQYGEDFCFRIQPFKEELYTVSMTREMLDGKLLFLFAAGIFLFHFANSLSRSTNFFYLSGIILGVLALLVFVLLALKRFIPRRSTFWILLSGCWMSSLYLIYCFKENMQWLWSEHRIYVLGYFVAVGTLSFATCYQHGPLTSELSITLFTWTLQLTAFVFIYCGVNIPQVAYAIIAVKPSPKGLGYPPAAAWHIGRKMKNHFQSKKVVVRCLTEEEYREQGETETVRALEELRSFCKNPDFSSWLAVSKLQSPHRFAGFVLGSPHVSPAETKAHDEEYGIGSSFLEEQLFETRTESEQDETTSYIHEGDDENEDEIHEPISFPYATELL", "text": "SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane protein; Nucleoplasmic side. SIMILARITY: Belongs to the NEMP family."}
{"protein": "MRILVLGVGNILLTDEAIGVRIVEALEQRYILPDYVEILDGGTAGMELLGDMANRDHLIIADAIVSKKNAPGTMMILRDEEVPALFTNKISPHQLGLADVLSALRFTGEFPKKLTLVGVIPESLEPHIGLTPTVEAMIEPALEQVLAALRESGVEAIPREAIHD", "text": "FUNCTION: Protease involved in the C-terminal processing of HybC, the large subunit of hydrogenase 2. Specifically cleaves off a 15 amino acid peptide from the C-terminus of the precursor of HybC. SIMILARITY: Belongs to the peptidase A31 family."}
{"protein": "MPWWPWRRWRRWRRRRGNWRRRVAPRRYRRTARRARRRRKAVRRRRRRRVRRRGYYRRYRRRRRYKRRLLILKQWQPTTNLRLTVKGLIPVVVMGKGKTQNNFGQWEQTVPLEGESYGGSFTIRKFTLQTLYEDYLKLRNRWSRSNTDLELIRYTGLNLRLYRHEFSDYIVHYSLETPMEVGLESHMLAHPLKMIMSSKHVTVPSLLTKKGGRRYLRLKIPPPKLMMTQWYFQKEFCQVGLVLLSISTATLMHPWMAPFVNSPALTIYAVNHKTYSDMSILPSNNQGSTKNELIETLYTAEHTYNPMAQRIWGNIKPQNTNFTPENYWNKWNEIHTKIKTNRQSELTQLKQMRKRLELTTENDYQDPNFGLSYGLYSPLLLYPEMYFPEQSKVYQKARYNPLLDQGIGNVVWTEPLTKKTCDYASQAYNVIKDAPLYLALFGYIDICSKLAKDKSFYLSNRVCVKCPYTVPQLLSKTNATLGHVILSENFMRGLVPSKDSYVPLYMRGKWYPSIYHQEEVIEAIVSSGPFVPRDQITKSLDITIGCRFGFRIGGNLLNPKQVGDPCKQPTHPLPAPGGGDLLRAVQVSDPRKVGIQFHPWDLRRGMLSTSSIKRMLQDSDDDESIEFPPKAWPGDPVPVGRTLEERCSSSLYHLLQEQATPPPFKKPRTEDQEENPEETTQLQLFQELQRQRELQLQLKRGFRGLVEEMIKSHRHLALDPYLK", "text": "FUNCTION: Self assemble to form an icosahedral capsid. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the anelloviridae capsid protein family."}
{"protein": "MRIEKCYFCSGPIYPGHGMMFVRNDCKVFRFCKSKCHKNFKKKRNPRKVRWTKAFRKAAGKELTVDNSFEFEKRRNEPVKYQRELWNKTIDAMKRVEEIKQKRQAKFIMNRLKKNKELQKVQDVKEVKQNIHLIRAPLAGKGKQLEDKMVQKLQEDVDMEDVS", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of GTPBP4/NOG1 to pre-60S particles (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family."}
{"protein": "MSRLAVVFGGSRGIGRAASKLLAQRGHRIVLLSRNKEAAQSTAQSLPGENHLGLSCDVSKEEEVQKAFETINKTCGTVGFLVNAAGINRDALLLRSKSEDMLSVLHTNLLGSMLTCKAAVRNMLSHGGAIVNIGSVVGVKGNAGQCVYSASKAGLEGFTRSLAKEVASRNIRVNLVAPGLIHTDMTAGLAEEAAVRTIPLGRFGEPAEVAQAMLFLLESPYITGQILLVDGGLQLLM", "text": "FUNCTION: The heterotetramer with HSD17B8 has NADH-dependent 3- ketoacyl-acyl carrier protein reductase activity, and thereby plays a role in mitochondrial fatty acid biosynthesis. Within the heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD. The homotetramer has NADPH-dependent quinone reductase activity. Both homotetramer and the heterotetramer have broad in vitro substrate specificity and can reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o- quinones and p-quinones. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MPLIEVDLLNPTAASEAKAHKMKRLVPTPNSYFLEIKCPKCGATTTTFSHAHRQILCQKCGQPLGQPTGGKLKLTQQCKFRIKK", "text": "FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Required for proper rRNA processing and maturation of 18S rRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family."}
{"protein": "MKATTYAPFAKPLYVMVKPVGAVCNLACEYCYYLEKANLYKENPKHVMSDELLEKFIDEYINSQTMPQVLFTWHGGETLMRPLSFYKKAMELQKKYARGRTIDNCIQTNGTLLTDEWCEFFRENNWLVGVSIDGPQEFHDEYRKNKMGKPSFVKVMQGINLLKKHGVEWNAMAVVNDFNAEYPLDFYNFFKEIDCHYIQFAPIVERIVSHQDGRHLASLAEGKEGALADFSVSPEQWGNFLCTIFDEWVKEDVGKFFIQIFDSTLANWMGEQPGVCTMAKHCGHAGVMEFNGDVYSCDHFVFPEYKLGNIYSQTLVEMMHSERQHNFGTMKYQSLPTQCKECDFLFACNGECPKNRFSRTADGEPGLNYLCKGYYQYFQHVAPYMDFMKKELMNQQAPANIMKALKDGSLKIEY", "text": "FUNCTION: Involved in 'Ser-type' sulfatase maturation under anaerobic conditions. Links the heparin and the chondroitin sulfate utilization pathways which contribute to the colonization of the intestinal tract. May catalyze the activation of chondro-6-sulfatase, i.e. the post- translational modification of a specific serine residue into 3- oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S- adenosyl-L-methionine (SAM). Is also able to oxidize a cysteine residue in a synthetic substrate to FGly in vitro, but not in a recombinant Cys-type sulfatase in vivo. But since B.thetaiotaomicron possesses only Ser-type sulfatases, the oxidation of serine residues to FGly is the sole physiological activity. SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family."}
{"protein": "MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRAEALKVSCGKCGNGLGHEFLNDGPKPGQSRFUIFSSSLKFVPKGKETSASQGH", "text": "FUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family."}
{"protein": "MPLGGFAGLKEKLNPGKEELKNNVGDSLGNLQKKIDGSNVTEEDNIELTEDGRPVAAPKRSPPLLDCGCFGLPKRYIIAMLSGLGFCISFGIRCNLGVAIVEMVNNNTVYINGTAVMQPAQFNWDPETVGLIHGSFFWGYIVTQIPGGFISNKLAANRVFGAAIFLTSVLNMFIPSAARVHYGCVMFVRILQGLVEGVTYPACHGMWSKWAPPLERSRLATTSFCGSYAGAVIAMPLAGILVQYVGWPSVFYIYGVFGIIWYIFWILLAYNSPAVHPTISEEERNYIETSIGEGANLMSSTEKFKTPWREFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFPISKVGILSAVPHMVMTIIVPIGGQLADFLRSRKILSTTTVRKIMNCGGFGMEATLLLVVGFSHTRAVAISFLILAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGALTKHKTRLEWQHVFVIASMVHYTGVIFYAIFASGEKQDWADPENTSDEKCGIIGEDELADETEPSSDSGLATRQKTYGTTDNSSGRKQGWKKKRGVTMQAEDDHESNHYENGEYQTQYQ", "text": "FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter that mediates the uptake of L-glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane (By similarity). In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification (By similarity). At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is electrogenic (By similarity). Moreover, operates synergistically with SLC18A3/VACHT under a constant H(+) gradient, thereby allowing striatal vesicular acetylcholine uptake (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Cell membrane; Multi-pass membrane protein Synapse, synaptosome. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily."}
{"protein": "TELGTDPNAKTPSSSSSASSALSSSSSSSASSPBHRKPMDEDDNQV", "text": "FUNCTION: Phosvitin is believed to be of importance in sequestering calcium, iron and other cations for the developing embryo."}
{"protein": "MNVNYLNDSDLDFLQHCSEEQLANFARLLTHNEKGKTRLSSVLMRNELFKSMEGHPEQHRRNWQLIAGELQHFGGDSIANKLRGHGKLYRAILLDVSKRLKLKADKEMSTFEIEQQLLEQFLRNTWKKMDEEHKQEFLHAVDARVNELEELLPLLMKDKLLAKGVSHLLSSQLTRILRTHAAMSVLGHGLLRGAGLGGPVGAALNGVKAVSGSAYRVTIPAVLQIACLRRMVSATQV", "text": "SIMILARITY: Belongs to the UPF0174 family."}
{"protein": "MASSNRHWPSMFRSKHATQPWQTQPDMAGSPPSLLSGSSAGSAGGGGYSLKSSPFSSVGEERVPDPKPRWNPRPEQIRILEAIFNSGMVNPPRDEIPRIRMQLQEYGQVGDANVFYWFQNRKSRSKNKLRSGGTGRAGLGLGGNRASAPAAAHREAVAPSFTPPPPILPAPQPVQPQQQLVSPVAAPTSSSSSSSDRSSGSSKPARATSTQAMSVTTAMDLLSPLAAACHQQMLYQGQPLESPPAPAPKVHGIVPHDEPVFLQWPQSPCLSAVDLGAAILGGQYMHLPVPAPQPPSSPGAAGMFWGLCNDVQAPNNTGHKSCAWSAGLGQHWCGSADQLGLGKSSAASIATVSRPEEAHDVDATKHGLLQYGFGITTPQVHVDVTSSAAGVLPPVPSSPSPPNAAVTVASVAATASLTDFAASAISAGAVANNQFQGLADFGLVAGACSGAGAAAAAAAPEAGSSVAAVVCVSVAGAAPPLFYPAAHFNVRHYGDEAELLRYRGGSRTEPVPVDESGVTVEPLQQGAVYIVVM", "text": "FUNCTION: Transcription factor which may be involved in developmental processes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family."}
{"protein": "MATKFPKFSQDLAQDPTTRRIWYGIATAHDFEMHDGMTEENLYQKIFASHFGHLAIIFLWTSGNLFHVAWQGNFAQWVADPLNTRPIAHAIWDPHFGEAAIEAFTQSDASCAVNIAYSGVYHWWYTIGMRTAADLYQGSIFLMVLAALMLFAGWLHLQPKFRPSLAWFKNAESRLNHHLAGLFGVSSLAWAGHLIHVAIPASRGETVNWGNFMSTPPHPAGLAPFFSGNWSVYAANPDTTGHVFNTSEGAGTAILTFLGGFHPQTQAMWLTDIAHHHLAIAVIFIIAGHMYKTNFGIGHSMKEILKTHRSPEGTPFGGMLGAGHDGLYDTINNSLHFQLGLALAALGVVTSLVAQHMYSMPSYAFIAQDFTTQAALYVHHQYIAIFLMCGAFAHGAIFFVRDYDHEANKNNVLGRVLEHKEAIISHLSWVSLFLGFHTLALVHNDVVVAFATPEKQILLEPVFAQFVQAASGKALYGFNVLLVNPDSAASIASDYIAGPHFWLDAINSGVNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDSFYLAVFWALNTAGWLTFYWHWKHLSIWQDNVAQFNESSTYLMGWFRDYLWLNSAQLINGYNPFGSQQLAVWAWMFLFGHLV", "text": "FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6 (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family."}
{"protein": "MATSDSNMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRAAGVDGVMVDVWWGIIELKGPKQYDWRAYRSLFQLVQECGLTLQAIMSFHQCGGNVGDIVNIPIPQWVLDIGESNHDIFYTNRSGTRNKEYLTVGVDNEPIFHGRTAIEIYSDYMKSFRENMSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPRIGEFQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPESTGFFKSNGTYVTEKGKFFLTWYSNKLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKVENHAAELTAGYYNLNDRDGYRPIARMLSRHHAILNFTCLEMRDSEQPSDAKSGPQELVQQVLSGGWREDIRVAGENALPRYDATAYNQIILNAKPQGVNNNGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHADQDYCANPQKYNHAITPLKPSAPKIPIEVLLEATKPTLPFPWLPETDMKVDG", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 14 family."}
{"protein": "MKDGEETPSVDGSTSASNREKLGTDLEIGPVDLSDGGKEEKVKDPNLVDWDGPDDPENPLNWTSKRKITATCSIALITFLTPLGSSMFAPGVGQLVKDFNVTSTELSSFVVSVYLLGYCFGPLIIAPLSELYGRQYVYHVCNILYVIWTIACAFAPEIGSLVVFRFFAGLAGSCPLTIGAGSIADMFVQEQRGGAMAAWALGPLIGPVVGPVAGAYLAQAKGWRWSFYVLAMAAGAITISSLFSIRESYAPTLLARKTKKLQKETGNMNLRSALDTGRTPKELFLYSIVRPTKMLFRSPIVFLLSLYVGVIYGYLYLLFTTITSVFQQQYNFSQGAVGLTYLGLGVGSLIGLFLIGATSDRLLNYLAAKNGEKKPEYRLPPMVPGAIFVPISLFMYGWTAYYQTHWIVPIIGTSFLGTGMMITFMCVSTYLVDAFTNYAASVMAANTVFRSLAGALLPLAGPKMYAVLGLGWGNSLLGFIALAFCALPVIFWIYGERIRTSPKFQVTF", "text": "FUNCTION: MFS-type transporter involved in penicillin production, most likely through the translocation of isopenicillin N from the cytosol to the peroxisomal lumen across the peroxisomal membrane. SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein Note=Probably recruited to the peroxisomal membrane by pex19. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MACLNPVPKLYRSVIEDVIEGVRNLFAEEGIEEQVLKDLKQLWETKVLQSKATEDFFRNSIQSPLFTLQLPHSLHQTLQSSTASLVIPAGRTLPSFTTAELGTSNSSANFTFPGYPIHVPAGVTLQTVSGHLYKVNVPIMVTETSGRAGILQHPIQQVFQQLGQPSVIQTSVPQLNPWSLQATTEKSQRIETVLQQPAILPSGPVDRKHLENATSDILVSPGNEHKIVPEALLCHQESSHYISLPGVVFSPQVSQTNSNVESVLSGSASMAQNLHDESLSTSPHGALHQHVTDIQLHILKNRMYGCDSVKQPRNIEEPSNIPVSEKDSNSQVDLSIRVTDDDIGEIIQVDGSGDTSSNEEIGSTRDADENEFLGNIDGGDLKVPEEEADSISNEDSATNSSDNEDPQVNIVEEDPLNSGDDVSEQDVPDLFDTDNVIVCQYDKIHRSKNKWKFYLKDGVMCFGGRDYVFAKAIGDAEW", "text": "FUNCTION: May function as a testis specific transcription factor. Binds DNA in conjunction with GTF2A2 and TBP (the TATA-binding protein) and together with GTF2A2, allows mRNA transcription. SUBCELLULAR LOCATION: Nucleus Note=Mainly localizes in the annulus and partly in acrosomal cap area of spermatozoa. SIMILARITY: Belongs to the TFIIA subunit 1 family."}
{"protein": "MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNCEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVEGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAGLTKIMLLLSVTDDTYDAYGTYNELKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRAYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQHGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM", "text": "FUNCTION: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MSIEVGSKLQGKITGITNFGAFVELPGGSTGLVHISEVADNYVKDINDHLKVGDQVEVKVINVEKDGKIGLSIKKAKDRPQARPRNDFRPKESFEQKMNKFLKDSEDRLSSLKRNTESKRGGRGARRG", "text": "SIMILARITY: Belongs to the peptidase U57 family."}
{"protein": "MTAPTKMTFFSRFEADILAGKKTITIRDESEKDYQPGTTVEVSTLEEGRVFCQLKILSVEPIAFSELNEFHAEQENMTLATLKEVIQEIYPGIEQLYVIQYQRV", "text": "FUNCTION: Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C). SIMILARITY: Belongs to the N(4)-acetylcytidine amidohydrolase family."}
{"protein": "MSLSLKTRRFGRPVRPQLVLLLLFALCLLSVFISAYYLYGWKRGLEPSGSEAQSPDCDEPKISPSRLLPMKPLKPVDSSRTDPLVLVFVESLYSQLGQEIVAILESSRFKYRTEIAPGKGDMPTLTDKDRGRFALIVYENILKYVNLDAWNRELLDKYCVEYGVGIIGFFKANENSLLSAQLKGFPLYLHSNLGLKDCSINPKSPLLYITRPNQVEKGDLPGEDWTVFQSNHSTYEPVLLAKTKSAESIPHLSVDAALHTTVVQDLGLHDGIQRVLFGNNLNFWLHKLVFVDAVSFLTGKRLSLPLNRYVLVDIDDIFVGKEGTRMKVEDVKALYDTQMELRTHIPNFTFNLGFSGKFFHTGTDAEDEGDDLLLSYVKQFWWFPHMWSHMQPHLFHNQSVLAEQMALNRKFAVEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKQIWGIKVTSTEEYPHLKPARYRRGFVHNGIMVLPRQTCGLFTHTIFYNEYPGGPVELDKIINGGELFLTVLLNPISIFMTHLSNYGNDRLGLYTFKHLVQFLNTWTNLKLETLPPVQLAHKYFQIFPEEKDPLWQDPCEDKRHKDIWSKEKTCDRFPKLLIIGPQKTGTTALYLFLGMHSDLSSNYPSSETFEEIQFFNGQNYHKGIDWFMEFFPIPSNTTSDFYFEKSANYFDSELAPRRVAALLPKAKIITILINPADRAYSWYQHQRAHDDPVAMKYTFQEVITAGPEAPQRLRALQNRCLVPGWYSTHIERWMNHFHANQILVLDGKLLRTEPANVMETVQKFLGVTNAMDYHKTLAFDPKKGFWCQLLDGGRTKCLGKSKGRKYPDMDSDSRSFLMDYYRDHNIELSKLLYKMGQTLPTWLREELQSTR", "text": "FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Golgi apparatus, trans-Golgi network membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily."}
{"protein": "MSEEHQESYHSDNLIDLMNHTLTNDHLQLLKKLGEMAAKLRMNLFLVGGTVRDMLRGVPGGDLDLVIEGDALAFSQNVANVLGGKVKHHEPFATATWVGAENLKLDIVSARAESYAKPGALPTIRHSHITDDLARRDFSINAMAIHLHPASYGQLVDPFHGRHDLTNGLIRILHSQSFIDDPTRLLRGVRFVSRFNYRFEQKTANLALATQPALTNALANVSPERIVHELKLLCHETDPVSSFSKLEDLHVWQALLGLTFSSSSATHLSRLQEEQNGEPLHWFQAIATVGFLEDNWKASLVPFAITAMEQRFLQNIEDIQKRLTNMTRFSTDYLHKQLYQVPEEPLRFYALSSGEEMQKVLDLYLHQRKQLQPLLTGHDLMELGMKPSPLFKECLLLHECEQLKGTIENKQDALQFAREFFNHKQPL", "text": "FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family."}
{"protein": "MAKKITATNPRLVKLIEILKQESYKNQAKIWKDIARRLAKPRRRRAEVNLSKINRYTKEGDVVLVPGKVLGAGKLEHKVVVAAFAFSETAKKLIKEAGGEAITIEELIKRNPKGSNVKIMA", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family."}
{"protein": "MHTLVFCSFKGGTGKTTLSLNVGCNLAQFLGKKVLLADLDPQSNLSSGLGASVRSNQKGLHDIVYTSNDLKSIICETKKDSVDLIPASFLSEQFRELDIHRGPSNNLKLFLNEYCAPFYDICIIDTPPSLGGLTKEAFVAGDKLIACLTPEPFSILGLQKIREFLSSVGKPEEEHILGIALSFWDDRNSTNQMYIDIIESIYKNKLFSTKIRRDISLSRSLLKEDSVANVYPNSRAAEDILKLTHEIANILHIEYERDYSQRTT", "text": "FUNCTION: Required for growth within mammalian cells. SIMILARITY: Belongs to the ParA family."}
{"protein": "MLVQITALAFLAGIASAGVVVGGYGDGVGVGLGGLGGGLGGVGVGLGGVGVVGGGHGVVDLHTPAHYQFKYGVEDHRTGDRKQQAEVRVGDVVKGEYSLAEPDGTVRVVKYTADDHNGFNAVVSRVGHAVHPQVLVRKAVVPVATHGVVGVGGLGGLGGVGLGGVGLGGVGLGGGLGGVGLLGGRGGLDRGILGGHGGSELKFKRALI", "text": "FUNCTION: Cuticular proteins play a significant role in determining the physical properties of cuticles."}
{"protein": "MALLKPFLSRTFSSFFATITGGRNLIDSIEELITTNYWLIFVMIIVCTCSAPSNGAFFLNDPYGYPFVSLQDDSIESVSATTITTTTIISTIITTTTATQRIFQEKAKTFGQSAEEIQKVKYYLEKIQKFEAKQHPEEIRQQHTTKNSEAIKDDLQIAVEVAKFEKRQKDSITLNPEENGQYYEGDIVLDAQQAHEIYESMIQHGRRTKRKFIRSELRRWDSHKPIIYSFDGSHTIREQRVIELALEHWHNITCLNFERRDDEIQENRIVFTDVDGCASNVGRHPLGEPQFVSLAPECIRLGVIAHEVAHALGFWHEQSRPDRDNYVTVRWENIDRDSKGQFLKELPTDVDNGDVPYDYGSIMHYRSKAFGRYEDLFTLNTNIMDYQKTIGQRDQLSFNDIRLMNVIYCSDSCAQKLPCQRGGYTDPRRCGRCRCPDGFTGKLCERIMPGFGADCGGRIELTSSWKRITSPNYPRDFKEGQECSWLLVAPPGQRVQLRFYGEFEMYCKVRHSLCMDYIEIRNSTDFANTGMRYCCYGTPKSSIMSATEDMLVLFRSFYRGGKGFQAQVRALPTTVFNIRTVRSMDEFNANLNKHAVADS", "text": "FUNCTION: Metalloprotease which cleaves the carboxyl terminus of procollagens to mature collagens. Probably involved in cuticular collagen maturation. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MDEPESESPASILASVRAQEAQFELLSRALEEERRHVTAQLDRVWVTPQEPPLANGSLTRRQQDGLPFLYTPTRMEAHSVHADERYVIDDSSYKSCTLTDESRCSEIPIQTVVGYSQTLDRPYREAAGSGGAYTTVPRNYHFRGPGVDSTMPLISQSPHPGYSSLSRPNQRYRSVDPFRGPGYGPQPQVRGGGLGGSQSDLLSGRIYGSEDAYGLEDDRRSLGGFIDGPDYATTGRRGANGGDPRRRLRSYEDPLSDHFGSIPTSGSLSSLGPAPLTLAPNSGPWRHPELPEVLAMLSYTLDAVRLNAAAYLQHLSYRNEDVKREVCRLRGIPPLISLLEDPRAPIRLAACGALKNLSYGPARENKMAVKNCDGVPALARLLRRRGEGIEGRELAECVTGTLWNLSSLDSVKMELVDQALYTLTQEILVPHSGWQQDGGMQDRVEGKPRHVEWEPALVNTTGCLRNISSERSEARRKMRECEGLVDSVVHILRSEVSHGLVDSKLLENVVCLLRNISYHVHREIPHAEKYMESPQNASAETQNPSCFGVRRGKGKKASEEAVDTVDFPKQTMPAQGYDLLFQPEIVRLYISLVKSSHTPAVLEASAGAIQNLCAGNWVYGRCIRAAVRQEKGLSSLADHLTHESERVVRAICGALRNLCGDNRNRELIGKHALNSLVARLSSSSAQSSALSEDTNVCVINTIHEVISGNLEAAKRLRESQGIERLVLINKGGGRSEREIRAAGFCLQTIWGYKELRRPLEKDGWKKSDFQVSTAATSSVQGYDDSTLPLIDRNLKNEKKSVNADIPLNDFIADQFTHNGDSSNRLPTRSDELSELDPLKECSVSAGGSLNLGDAEDQRV", "text": "FUNCTION: Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Required for gastrulation, axial elongation and development of the craniofacial skeleton and eye. SUBCELLULAR LOCATION: Cell junction, adherens junction Cytoplasm Nucleus Cell membrane. SIMILARITY: Belongs to the beta-catenin family."}
{"protein": "MRRSTDPRNLLVRRGPLLVDGESAISELDPGFFPTGDAPKMSSTTRRRFNLIAFTPGPVTVISSLVYLALLIPLLLVHTIVPSAPKSNPKGVDLSEAWNDLQHLTSGFHPYNSHRNDEIHQWLLQRVGHILDASRKAHEDDAMGSVAPDVFVFDDQQSNLTFSGGGVGNKPITGVYFEGKNIIVYIRGLEDDKENWWDSPGGKPKGKGGVLVNAHYDSVSTGFGATDDGVGVVSVLQLIKFFTSPGNLPRKGLVLLLNNGEEDYLNGARAYSQHPLSKYTHTFLNLEGAGAGGRAALFRTTDTEVTRFYKSSPHPFGSVLAADGFKMGLIRSETDYAVFKGVLGLRGLDVAFIEPRARYHTDQDDVRHTSIDSVWHMLSAAIATTKGLVSYTGSEFDGRAPGKGMVNSGVGTHGVWFDLFGSSFAVFRLHTLFAISVTLLVVCPIVLFVIGIILSKMDKMYLFSIHETIPETKEKVSVRGLRGLFRYPIILVVSSGILIGLSYLLAKVNPFIVHSSSYAVWSMMLSSWIFMTWFLSCIADFFRPSALHRAYTFTWQLLVMWVLLVISTVYVNQHDIAAGYFIVFYFAGTFLATLISYLELFALPNKTQYAREQSQYPSRLGSNRSSRILSPSADELPTGGDNNGEIYDGEEEPTESSSLLGRQRRTTFANYTRTGRDLASSESGTYEDHSETGVFGEEQKWSASLPTWTWVLQFLFVGPVVIMFIGQLGLFLTSAMNQVGADGVGLLVVYIAIAVFSVLLLIPLSPFIHRFTYHVPTFLLLVFIATLIYNLAAFPFSAENRLKIFFVQELNLDTGRNQVSLTGVDPYVQDIIRAIPSASKENISCDSELDSGRRKCSWPGLAPEVVQDEPTDRWLSFNISKPSSQETKDTPVLHARLHVSGKNTRACRVNFERPIRDYSLPGSALDDRMPHTLPQGISEIRLWSRTWENVWTVDVQWDAEDMDELHGRVVCLWSDANQLGSIPALDELRLFAPPWVAISKLKDGLVEVSRGF", "text": "FUNCTION: May be involved in vacuolar sorting and osmoregulation. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M28 family."}
{"protein": "MSPKIRQTIYLLGTAAPALLGIVLIWGGLDAESAADLGDIIAGVVSILVSGAPAVAAGTVRSQRKDGTLSTSPVDQVTKGVEQVLAARQSAEAEVAKVKQALETAVSGSLPQLGPLATQILNVADDTVWRP", "text": "FUNCTION: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron- scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis. Participates with the endolysin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles from the host cell. SUBCELLULAR LOCATION: Host cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Mycobacterium phage D29 holin family."}
{"protein": "MAGITEHSTIMNDANFKEENAHLSDASIHFGSSEQDKTPSDYELDDVLDLYNDTTEDDADDADDVNNYIMSPSSSLSSESEHALDALVYPIYSHHNILEHENNSDYASITPSNHPAFTSCAYLQNPVVDSNNEYESKFRLSLEIPPTDFLSTSTELSKRESCLSTETSSSKFSAVTAATITNETQSEKRSSQTDPSLPFKTNSLNCDVTYEEGPLTKKLRGPKKYKPSHSSWDIYGFKKANQFYTVDQYNTWYGPYSRYLERREQRWKLFLQENGIDYIHQSPSIFPSRSAKTQRFIRKGIPPEYRGNAWFYYSGGYELLQRNPKLYETLWRCACIKKPSDSDLIERDLYRTFPDNVHFRHKSKHSRNSSDASEHSSEEPDVPMISKLRRVLMTFATYLPENGYCQSLNFLAGFFLLFMSEEKAFWMLVITCRKYLPKMHDANLEGANIDQSVLMASVRESLPAVWSRISLNFDGIPVNDIVAKLPPITLVTAAWFMSAFVGILPTETALRVWDCFFYEGSKVLFMTALCILRLGEDDIKSKSEQTEVFQVIQDLPKSLLDANAFLSLCFRRNFRRTPSQKDIERRREKVAKKRNSSASKLEMSDSSKHHLSRSSSRFSKSHIISQLHNHLKKST", "text": "FUNCTION: Regulates exocytosis by functioning as a GAP for ypt2. SUBCELLULAR LOCATION: Cytoplasm Membrane; Multi-pass membrane protein."}
{"protein": "MEEFDSEDFSTSEEDEDYVPSGGEYSEDDINELVKEDEVDVEEETHIIKGTKRKAERFMPRKRKQGGLSLEEEDEEDAGRESGGSGSEEEDTATEQEEGTESEDARKKKEDELWASFLNDVGPKSKVPPSTPVKTGEETEETSSSNLVKAEEQEKPKETEKVKITKVFDFAGEEVRVTKEVDPTSKEAKSFFKQSEKEKPQPNVPSAVSSLPAGSGLKRSSGMSSLLGKIGAKKQKMSTLEKSKLDWENFKEEEGIAEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP", "text": "FUNCTION: May play a role during embryogenesis. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore."}
{"protein": "MSFTGKYQLESQEGFVEFMKAVGLPDDMIEKGKDIKSVSEIEENGNQFKVTVTTGSKVLTNSFTIGQEADIETLTGERVKTIVNREGNKLKVVLNRITSITELVDANTLVNTLTLGGLVYKRISKRVA", "text": "FUNCTION: Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family."}
{"protein": "MMSKNFRFSVRTFTNTTARLANYGKPQNPPIDPTLHMRISPIERTGETIDVKRARLVYQSRKRGILESDLLLSRFAKKYLKQMTMEELDEYDKLLDEADWDIYYWATKNYDTTPLPKKWEDSKILKLLQKEAENEERVILRMPELDEGDFINGGKETSLSEVKN", "text": "FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the SDHAF2 family."}
{"protein": "MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNAYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP", "text": "FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. EZH2 can also methylate non- histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the CLOCK-BMAL1 transcriptional activation of PER1/2. Involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription. SUBCELLULAR LOCATION: Nucleus Note=Localizes to the inactive X chromosome in trophoblast stem cells. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily."}
{"protein": "MEDNLPVNVREYQELAKKALPKMAYDYINGGAEDEHTLRENIAAYTRIILRPRVLVDVSKIDMSTTLLGYTMRSPIIVAPTGGHKLAHPEGEKATARAAASCNAIMVLSFSSSCKIEDVASSCNAIRFYQLYVYKNRNVSATLVRRAESCGFKALLLTVDTPMLGRREADIRNKMVFPRSGNLEGLMTIDDHDTTNGSQLERFARATLDPSLSWKDIEWLKSITSMPIFLKGIVTAEDARRAVEAGVAGVIVSNHGARQLDYAPATIAALEEVVRAVAGAVPVLVDGGIRRGTDVFKALALGARAVMXXXPVFFGLAARGEAGARHVIEMLNGELEVAMALCGCRSVGEITRSHVMTEGDRIRSLL", "text": "FUNCTION: Oxidase that catalyzes the oxidation of a broad range of 2- hydroxyacids to the corresponding 2-oxoacids, with a reduction of O2 to H2O2. May be involved in a general medium- and long-chain fatty acid catabolic pathway such as alpha-oxidation. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
{"protein": "MFNDRPQTDRMFFPPERPEVTSELSNNVVLTTLNDLYNWARLSSVWPLMYGTACCFIEFAGLIGSRFDFDRFGLVPRASPRQADLIITAGTITMKFAPALVTLYQQMPEPKYVIAMGACTITGGMFSTDSPTTVRGVDKLIPVDVYIPGCPPRPEAIFDAIIKLRKKMATEDFRERYDTIAQTHRYYTAAHRMKAVADPLTSEYIRLESRQAAPPALAAAIEMGIPLDLQRTPQLEEQIRDGEHRDARA", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family."}
{"protein": "MKQATALDILKTGKNVFLTGSAGSGKTYTLNEYIHYLRARRVPVATTASTGIAATHMNGITIHSWSGIGIKDELTERDLVNLSRKKVLKDRLQETAVLIIDEISMLHAKQLNLVNQVLKHMRQNDKPFGGIQVVVAGDFFQLPPVGSRGESNRDKFAFMSQAWLDAGFKICYLSEQHRQQSGEGEDAQITLDNILNQIRGENGVSAAAIAALQNTFYQDVDVNRTRLYTHNVNVNKINEHELALLEGETVTYNAIAHGDNKLVETLKKSVRTSDELTLKTGAKVMFIKNNSELGVSNGTMGELIGFTTIKPLKLSIATIDDGSADEDGSAEALDEALETLEDAEALAQNESDKPLVSTDRYPIVRLNSGRQVIAEGEEWIVEDESGEILASYTQIPLTLAWAITIHKSQGMTLDAAEIDLSKTFELGQGYVALSRLKSLEGLKLLGMNDLSLRLDPLARGADSRFKDLSLEAQQAFEDIEREVLQESHERFVIASGGTLNKANIAAFEKEYKNRKKKQAQKLAQKDKLSNQLSDHSESTLMATRILLEESLSIAEIAQSRGLAQSTIMGHVARLRRQDPSLNCEHLRPDEAILNKVSKAVDAIIAAGDPNDFNAADDSTQSVKGGDDFDKQRIKLRPIYEYLKQQIDYNTIRLALVFID", "text": "FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase that efficiently unwinds G-quadruplex (G4) DNA structures. May be involved in resolving commom issues that arise during DNA replication, recombination, and repair. SIMILARITY: Belongs to the helicase family. PIF1 subfamily."}
{"protein": "MVNSLKKQTFTEMRPGVKVPAKETILTPRFYTTDFDEMAKMDISVNEDELMAILEEFRADYNRHHFVRNEEFAQSWDHIDGETRRLFVEFLERSCTAEFSGFLLYKELGRRLKNKSPILAECFTLMSRDEARHAGFLNKAMSDFNLSLDLGFLTKSRKYTFFKPKFIFYATYLSEKIGYWRYITIYRHLEAHPEDRIYPIFRFFENWCQDENRHGDFFDAIMRARPEFLNDWQAKLWCRFFLLSVFATMYLNDIQRADFYASIGLNACDYDKYVIEKTNETSGRVFPVILDVENPEFYARLEFCIKNNEKLTKIANSNNPGFVKFFQKFPLYLSNGWQFLKLYLMKPIETATMQSSVR", "text": "FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME). SIMILARITY: Belongs to the AcsF family."}
{"protein": "MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRDDDGVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGTTPLHVAAKAGQTLQAELLVVYGADPGSPDVNGRTPIDYARQAGHHELAERLVECQYELTDRLAFYLCGRKPDHKNGHYIIPQMADRSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNLELSARSQSELDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQPPGPVPPPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGTPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVPFTPSSPLLSCSQEGSRHASKLSRHGSGADSDYENTQSGDPLLGLEGKRFLELSKEDELHPELESLDGDLDPGLPSTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALEPVRSSLRLLNASAYRLQSECRKTVPPEPGAPVDFQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ", "text": "FUNCTION: GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through PAK1 activation, positively regulates microtubule nucleation during interphase. Plays a role in the regulation of cytokinesis; for this function, may act in a pathway also involving ENTR1 and PTPN13 (By similarity). May promote cell motility both by regulating focal complex dynamics and by the activation of RAC1 (By similarity). May act as scaffold for MAPK1/3 signal transduction, recruiting MAPK1/3 to focal adhesions after EGF stimulation via a Src-dependent pathway, hence stimulating cell migration (By similarity). Plays a role in brain development and function (PubMed:25792865, PubMed:33010377). Involved in the regulation of spine density and synaptic plasticity that is required for processes involved in learning (PubMed:20043896, PubMed:29554125). Plays an important role in dendritic spine morphogenesis and synapse formation (PubMed:12695502). In hippocampal neurons, recruits guanine nucleotide exchange factors (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in turn locally activate RAC1, which is an essential step for spine morphogenesis and synapse formation (PubMed:12695502). May contribute to the organization of presynaptic active zones through oligomerization and formation of a Piccolo/PCLO-based protein network, which includes ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its interaction with liprin-alpha family members, may be required for AMPA receptor (GRIA2/3) proper targeting to the cell membrane (By similarity). In complex with GABA(A) receptors and ARHGEF7, plays a crucial role in regulating GABA(A) receptor synaptic stability, maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory synaptic transmission, by locally coordinating RAC1 and PAK1 downstream effector activity, leading to F-actin stabilization (By similarity). May also be important for RAC1 downstream signaling pathway through PAK3 and regulation of neuronal inhibitory transmission at presynaptic input (PubMed:21499268). Required for successful bone regeneration during fracture healing (PubMed:25138700, PubMed:24586541, PubMed:32460388). The function in intramembranous ossification may, at least partly, exerted by macrophages in which GIT1 is a key negative regulator of redox homeostasis, IL1B production, and glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (PubMed:32460388). May play a role in angiogenesis during fracture healing (PubMed:24586541, PubMed:31502302). In this process, may regulate activation of the canonical NF-kappa-B signal in bone mesenchymal stem cells by enhancing the interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1, eventually leading to enhanced production of VEGFA and others angiogenic factors (By similarity). Essential for VEGF signaling through the activation of phospholipase C-gamma and ERK1/2, hence may control endothelial cell proliferation and angiogenesis (PubMed:19273721). SUBCELLULAR LOCATION: Cytoplasm Presynapse Postsynapse Postsynaptic density Cell junction, focal adhesion Cell projection, lamellipodium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Note=Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytosolic complexes, containing at least PXN/paxillin, ARHGEF7 and PAK1, and membrane protrusions. During cell migration, moves from the disassembling adhesions into the cytosol and towards the leading edge. In adherent cells, localizes to adhesions. Recruitment to adhesions may be mediated by RAC1 and active tyrosine- phosphorylated PXN (By similarity). May be present in both excitatory and inhibitory synapses. In hippocampal neurons, recruitment of GIT1 to synapses is regulated by ephrinB activation and ephrinB downstream effector GRB4/NCK2. In hippocampal neurons, partially colocalizes with PCLO (By similarity). Interaction with GRIN3A limits GIT1 synaptic localization (By similarity). Localization to the centrosome does not depend upon the presence of gamma-tubulin (By similarity)."}
{"protein": "MDNGVETPQGQKTQPINLPPVRKKLRKHEGLGKGVKRKLFAEDSSPLKKQISACSDMETLSSPVKSECESRSASLDESFGKCKHEIACDCSAIEELLCHESLLDSPMKLSNAHTIFSSNKWKLELEKIIASKQIFLDMSENAELAAYGETLCNLRIFEKISSPFLFDVQSEERSYSVVYVPHNKELCGQFCQPEKTMARVLGVGAYGKVFDLDKVAIKTANEDESVISAFIAGVIRAKSGADLLSHECVINNLLISNSVCMSHKVSLSRTYDIDLHKFEDWDVRNVMNYYSVFCKLADAVRFLNLKCRINHFDISPMNIFLNHKKEIIFDAVLADYSLSEMHPNYNGTCAIAKEYDKNLQLVPISRNKFCDMFNPGFRPLVANAMILVNVCGAFDGENNPLRHCNLDLCAFAQVVLSCVLRMTDKRGCREAQLYYEKRLFALANEACRLNPLKYPFAYRDACCKVLAEHVVLLGLLFYRDVVEIYEKLYDFLDERGEFGSRDLFEATFLNNSKLTRRQPIREGLASLQSSEYGEKLLHDLRELFLINSTADLDKDTSSLFHM", "text": "FUNCTION: Phosphorylates the antiviral nucleoside analog ganciclovir. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. HCMV ganciclovir subfamily."}
{"protein": "MAVHKEVNFVAYLLIVLGLLVLVSAMEHVDAKACTLECGNLGFGICPRSEGSPENRICTNCCAGYKGCNYYSANGAFICEGESDPKKPKACPRNCDPHIAYSKCPRSEGKSLIYPTGCTTCCTGYKGCYYFGKNGKFVCEGESDEPKANMYPAM", "text": "SIMILARITY: Belongs to the protease inhibitor I20 (potato type II proteinase inhibitor) family."}
{"protein": "MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPADTSDMEAAWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPVVSKALSSALDDTEVKKVMEECKRLQSEVQRLREENKQLKEEDGLRMRKPVLSNSPAPAPATPGKEEGLSTRLLALVVLFFIVGVIIGKIAL", "text": "FUNCTION: Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family."}
{"protein": "KEGYPVDWGNCKYECMSDEYCKDLCADRKATSGYCYKLNWSCYCKGLPDDSPIKTPGKCRSGR", "text": "FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily."}
{"protein": "MAGTSAPGSKRRSEPPAPRPGPPPGTGHPPSKRARGFSAAAAPDPDDPFGAHGDFTADDLEELDTLASQALSQCPAAARDVSSDHKVHRLLDGMSKNPSGKNRETVPIKDNFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDKEKEFSKKLQSLQSELQFKDAEMNELRTKLQTSERANKLAAPSVSHVSPRKNPSVVIKPEACSPQFGKTSFPTKESFSANMSLPHPCQTESGYKPLVGREDSKPHSLRGDSIKQEEAQKSFVDSWRQRSNTQGSILINLLLKQPLIPGSSLSLCHLLSSSSESPAGTPLQPPGFGSTLAGMSGLRTTGSYDGSFSLSALREAQNLAFTGLNLVARNECSRDGDPAEGGRRAFPLCQLPGAVHFLPLVQFFIGLHCQALQDLAAAKRSGAPGDSPTHSSCVSSGVETNPEDSVCILEGFSVTALSILQHLVCHSGAVVSLLLSGVGADSAAGEGNRSLVHRLSDGDMTSALRGVADDQGQHPLLKMLLHLLAFSSAATGHLQASVLTQCLKVLVKLAENTSCDFLPRFQCVFQVLPKCLSPETPLPSVLLAVELLSLLADHDQLAPQLCSHSEGCLLLLLYMYITSRPDRVALETQWLQLEQEVVWLLAKLGVQSPLPPVTGSNCQCNVEVVRALTVMLHRQWLTVRRAGGPPRTDQQRRTVRCLRDTVLLLHGLSQKDKLFMMHCVEVLHQFDQVMPGVSMLIRGLPDVTDCEEAALDDLCAAETDVEDPEVECG", "text": "FUNCTION: Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein. SUBCELLULAR LOCATION: Nucleus Note=Redistributes to discrete nuclear foci upon DNA damage. SIMILARITY: Belongs to the ATRIP family."}
{"protein": "MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK", "text": "FUNCTION: Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors. FUNCTION: Plays a central role in autophagy (PubMed:18570871, PubMed:21358617, PubMed:23184933, PubMed:23974797, PubMed:28445460). Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530, PubMed:23974797, PubMed:26783301). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis (PubMed:25275521). Protects against infection by a neurovirulent strain of Sindbis virus (PubMed:9765397). May play a role in antiviral host defense. SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion. SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion Nucleus Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Endoplasmic reticulum membrane; Peripheral membrane protein Mitochondrion membrane; Peripheral membrane protein Endosome Cytoplasmic vesicle, autophagosome Note=Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells (By similarity). SIMILARITY: Belongs to the beclin family."}
{"protein": "MGLRTSSGSPLVKPKLYKTSASNVISLAEKQDRFLNLGELTDLNTYFSSGNRRLDIAKVISLNANLIISRAADRIFVGGSPLSFLERPQAAVTLTSDQASSTSIQSTKGLGNGNIFQNFFKSTSEAPTGFKPINVVRYGSSNMKKSIRDLDWFLRYVTYAIVAGDTSILIVNTKGLRELIDKACSSSAAIVALKEMKNVSLSLFNYDIESQNIVRLYFNTLVSEFESPASSSKVRKRNSLDLQGLAIPDIYLVAADKSLRYVMKPNLSNTEKAQVIKACYRQVFERDIAKAYGLSLLELESKLKNLQISVKEFIRALGKSTLYRKNFYEGFTNSRVVELAFRHFMGRGLSSLQEFRKYFAILSSNGLDALIDSIINNSEYAEYFGEETVPYIRGYGQEAQECRNWGSQFALFKYSAPFRTIPQFITLFADYTQLPPSQHCYGKLNDPLNIQFGAIFKNSYVNEQSRPVLFPRGSRRILVYKGAGIFNQLGSPNALEKPPSNVSIAKWSKETDLNFILNAAYLRVFGRYVYEEEKIALRPLENEFKRRSISVRDFVGQLAKSDVFRSLYWSRLYICKSIEYIHIRLLGRPTYGRTEINNYFDIVYKSGFYAFVDSLVNSREYIKCFGNDTVPYDRYSTPEAVSSSIFRLSFINSVSYKSLKPKIEKFIQLGVARDAKSLSSLNSKVFQGVSQARSQKRVFKVSDYSNVMNLRIVFYAALRQVFERNIEPYIKGGEFKDIESLFLSGKISVRELIKEIGSSSLYRKEFYIPFPNTQVIEFCTKHFLGRAPKNQSEIRYYNQVLAVQGLREMINYMINSKEYLSVFGDDIVPYRRFPTLPAANFPNTQRLYSRQTKQNRNIVVPSFSGLLNTV", "text": "FUNCTION: This protein is postulated to act both as terminal energy acceptor and as a linker polypeptide that stabilizes the phycobilisome architecture. May have intrinsic bilin lyase activity (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the phycobilisome linker protein family."}
{"protein": "MAAIGVHLGCTSACVAVYKDGRAGVVANDAGDRVTPAVVAYSENEEIVGLAAKQSRIRNISNTVMKVKQILGRSSSDPQAQKYIAESKCLVIEKNGKLRYEIDTGEETKFVNPEDVARLIFSKMKETAHSVLGSDANDVVITVPFDFGEKQKNALGEAARAAGFNVLRLIHEPSAALLAYGIGQDSPTGKSNILVFKLGGTSLSLSVMEVNSGIYRVLSTNTDDNIGGAHFTETLAQYLASEFQRSFKHDVRGNARAMMKLTNSAEVAKHSLSTLGSANCFLDSLYEGQDFDCNVSRARFELLCSPLFNKCIEAIRGLLDQNGFTADDINKVVLCGGSSRIPKLQQLIKDLFPAVELLNSIPPDEVIPIGAAIEAGILIGKENLLVEDSLMIECSARDILVKGVDESGASRFTVLFPSGTPLPARRQHTLQAPGSISSVCLELYESDGKNSAKEETKFAQVVLQDLDKKENGLRDILAVLTMKRDGSLHVTCTDQETGKCEAISIEIAS", "text": "FUNCTION: Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding- competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MLWAHCGRFLRYHLLPLLLCRLPFLLLFQRPQWAHGLDIVEEDEWLREIQGATYQLSIVRQAMQHAGFQVRAASVMTRRNAVDLDRPPLWSGSLPHLPVYDVRSPRPLRPPSSQHHAVSPELPSRDGIRWQYQELQYLVEEQRRRNQSRNAIPRPSFPPPDPPSQPAEDARDADAERTESPHSAESTVRHDASENAVRRRHERRRYNALTVRSRDSLLLTRIRFSNQRCFGRGRLRHPAGSGPNTGGPRPGGAGLRQLRQQLTVRWQLFRLRCHGWTQQVSSQIRTRWEESNVVSQTATRVRTWFVERTTFWRRTWVPRQNPAAEAQELAVIPPAPTVLRQNEEPRQQLTGEETRNSTHTQREEVEDVSREGAREGNDGSRASGNDERRNNAGRYDDDHEVQEPQVTYPAGQGELNRRSQEENEEGGPCESPPMTTNTLTVACPPREPPHRALFRLCLGLWVSSYLVRRPMTI", "text": "FUNCTION: Plays an essential role during infection by modulating mitochondrial ultrastructure and thereby increasing bioenergetic potential. Mechanistically, alters cristae architecture by interacting with components of the host mitochondrial contact site and cristae organizing system (MICOS) complex. SUBCELLULAR LOCATION: Host mitochondrion. SIMILARITY: Belongs to the HHV-5 UL13 protein family."}
{"protein": "MNKFWIMLSHTYKNKIMAKSFIISTVITVLLVLVVTNLESIISLFQGDDAKEKIAVVDETNELYPVFSKQLKAVDTDGDLDVKLSKQSEDEVTKQVKDESLDGMLIIKRDEKGTISGTYKALTISDESTYQTLQQALTQTKTAVGTAELGVSQETISSLYAPVTVGQKALKEGAKSEEELGQTVGLVYIMLFVIYFSVIMYASMIAMEVATEKSSRVMEILISSMPPIQQMFAKLLGIGLVGITQLAIIIGAGSLSLKLNQKSETASSVGGFLNLTDVSATTVIYAVIFFLLGYFLYATLAAFLGSVVSRIEDVQQTITPMTLLVVAGFMIAMFGLNAPDAGFITVTSFIPFFTPMIMFLRVGMLDIPFWQAAVGIGITLLTIVILAVIGARIYKGGVLIYGNSSAFKAIKQALRLAKN", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To M.jannaschii MJ1024."}
{"protein": "MFAGRLMVRSIVGRACLATMGRWSKPQAHASQVILPSTPAIAAVAIQCEEFTANRRLFSSQIETESTLDGATYERVCSDTLDALCDYFEELTENASELQGTDVAYSDGVLTVNLGGQHGTYVINRQTPNKQIWLSSPTSGPKRYDFVGTVAAGRWIYKHSGQSLHELLQQEIPGILKSQSVDFLRLPYCS", "text": "FUNCTION: Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways (PubMed:18540637). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+) (PubMed:18540637). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization (PubMed:18540637). Required for ecdysteroidogenesis in the prothoracic gland which is necessary for larval to pupal transition (PubMed:25628335). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the frataxin family."}
{"protein": "MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLSKPIEGPVYGFIFLFKWSEERRSRRKVGPSMEESFVVDEDIVNDMFFAQQLIPNSCATHALLSVLLNCPQISLGSTLTRLKYFTRGMGPESKGWAIGNVPEIARAHNSHARPEPRHLPEKQTGISSVRTAEAFHFVSYVTTNDRLFELDGLKPYPIDHGPWGEKEDWTEKFRRVISERIGNATGGENGHDIRFNLMAVVADRRQQYETKLNTLKTNRQIVLEALQQVGGVNTKKSIQYAEVSHVCLHPPKFVPCSDDCAIWDALRYSSALRCSLIQHGCEHPSIPRSDGSTLVSWPSCVTSVNIVVSGHLKYVLLCFSIILDHKLEKLVPARLDPIKVNEPHLTSLIPSAFGRESHHKSKASSTVTSSSAAASSSAAGTDGVQPAEMKPDEFLHPDASRRVGFLEMPWRSDEARPLSIHTGYSKIPSPAPSNESTDTASEIGSAFNSPVRSANRSALQTIPEGSITKQEGDTKTDANIITVCLKRSLSGEGGGPPAKRLHIGDPDMALQRLGSGDSVEGDPMALQGGSGTGDAQQDQHALQAGGARPNMAHAFAPKDLLALLKNVETEIQICEQHLKDEIEKRKKYKVDDCRRTHNYDDFIRTFLRMLAEQGQLSKLVDQHVLVRRRQGVSVGRLHKQRKPDRRRKRARVSDKYRRKKQ", "text": "FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly nuclear. Binds to chromatin. SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily."}
{"protein": "MKNLVRLLAVIALIIGSFWGKVPAQALNLTSIALPSLPVAVLNAADAKLTTEFGAKIDLNNSDIRDFRDLRGFYPNLAGKIIKNAPYEEVEDVLNIPGLSDTQKERLQANLEKFTVTEPSKEFIEGDDRFNPGVY", "text": "FUNCTION: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Associated with photosystem II at the Lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the PsbU family."}
{"protein": "MDDFDKETAIKFMDFLAEEILNKKLSEDEKELIYSYVGGKPINRNCY", "text": "SIMILARITY: Belongs to the archaeal ATPase family."}
{"protein": "MAAAASNGNGMEVDVAALPSVMAQGVTGSVTVALHPLVILNISDHWIRMRSQEGRPMQVIGALIGKQEGRNIEVMNSFELLSQINDEKITINKEYYYTKEEQFKQVFKDMEFLGWYTTGGTPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVYESVIDIVNGEATMLLAELSYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVRLILEYVRAAEGGEVPFNHEILREASALCHCLPVLSTDKFKTDFYDQCNDVGLMSYLGTITKTCNTMNQFVNKFNILYDRQGIGRRMRGLFF", "text": "FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily."}
{"protein": "MWICPGGGGGGGGGGGGGDREDARPAPLCCGRCWRSGCAARPPRMCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN", "text": "FUNCTION: Human-specific protein that promotes neural progenitor proliferation and evolutionary expansion of the brain neocortex by regulating the Notch signaling pathway (PubMed:29856954, PubMed:29856955, PubMed:29561261). Able to promote neural progenitor self-renewal, possibly by down-regulating neuronal differentiation genes, thereby delaying the differentiation of neuronal progenitors and leading to an overall final increase in neuronal production (PubMed:29856954). Acts by enhancing the Notch signaling pathway via two different mechanisms that probably work in parallel to reach the same effect (PubMed:29856954). Enhances Notch signaling pathway in a non-cell-autonomous manner via direct interaction with NOTCH2 (PubMed:29856954). Also promotes Notch signaling pathway in a cell- autonomous manner through inhibition of cis DLL1-NOTCH2 interactions, which promotes neuronal differentiation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NOTCH family."}
{"protein": "MANVRCLYKLIRLQKLLLPLNATSSRLAPLQPRPLTFLIARSYGKDEKKANLEDFRAREEQRERERDAADQAAEKASQKEAGGGGGLGAKGSESTGPEDDAKQAKVDAIRAKILDAALQHVPQQGWTRQAIILGAEESGYPSVVHGMFPEGGFALVSHFNGKCNAQLVESLQQKTDGGKQEVEDPLDFLVQAVRQRLEMVTPYKTHWPQAMALLAQPQHAPTALAQVLTLVDDICYYSGDRSVDFGWYTRRVGLATIMKMTELYFLQDKSPGHAQTWEFLKSRMDEAVQLQMMLSQTEGMTHTFQRSFNSAFITARNILGLGYNRN", "text": "FUNCTION: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the COQ9 family."}
{"protein": "MSTEQDIKTEEQIPLTYAAVAAPTVQTEGEAVVAPEEPKPKKNWFTFGKKKAAPTDETNIEEGGAPGDEPVKEKKEKKCWWSRCQKGEGEQKEENIAIGVDLVNRDANSMNNHVQLNFEDIFGEADSQHSWDCVWRLNHTVFTAVRLFIYRLVSLLALPFTIIFAIFFGLLASINVFIIVPLGKLLSIPGTLLAKLWNWLIHAIFDPIASAVGLIFSNFNIRKYGINQETTAPCV", "text": "FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein Membrane, caveola; Peripheral membrane protein Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). SIMILARITY: Belongs to the caveolin family."}
{"protein": "MSLVDLGKRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWATEHHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQNQVNANPERANPVTMATPFIFTSGEVVNLASLVSSASTKTTSGDPHASSTVHFSNSTTSVLATLAALAEASAPLSNSHRATANSEEIIEGNSVDSSIQQVVGSGGQRVITIVTDGIPLGNIQTAIPAGGIGQPFIVTVQDGQQVLTVPAGQVAEETVIEEEAEEAEKLPLTKKPRIEEMTNSVEESKEGTERELLQQRLQEANRRAQEYRHQLLKKEQEAEQYRLRLEAMARQQPNGVDFAMVEEVAEVDAVVVTEREMEERETEVTGAVGTAEPHTGVSMETVST", "text": "FUNCTION: May function as transcription factor capable of interacting with purine rich repeats (GA repeats). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MFENFREKLQTVQQDFTSGIKTLSDKSKEAKVKKKQRRDEYLPQYSAGVELLSRYEDTWVALHKRAKESAKSGETVDGEVVMLCAHWEKRRGAVLELQEQLQQIPTFLSDLETITSRIAHLEADFEEMESRLVYLEDLCAQCEHQRFKQFQILQLENYKKKKRKELESCKAELDAEHAQKVLEMEHAQQVKLKERRKYFEEAFQQDMEQYLSTGYLQITDRRDPLGSMSSMEVNVDLLEQMDLTDVSDHEALDVFLSSVGEESSAVSPDAGGPSLEPGSSPSDISLKVPSQSELRHNISSISSSCTDTVSGTTEGPDEEESSSGDSPLVQSDEEEVHADTALMGLPETEALKSSDDSDTQAP", "text": "FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. Plays a role in intracellular vesicle trafficking. Plays a role in synaptic vesicle trafficking and in neurotransmitter release. May be required for normal dopamine homeostasis in the cerebral cortex, hippocampus, and hypothalamus. Plays a role in the regulation of cell surface exposure of DRD2. Contributes to the regulation of dopamine signaling. May play a role in actin cytoskeleton reorganization and neurite outgrowth (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Endosome membrane; Peripheral membrane protein; Cytoplasmic side Melanosome membrane; Peripheral membrane protein; Cytoplasmic side Nucleus Postsynaptic density Endoplasmic reticulum. SIMILARITY: Belongs to the dysbindin family."}
{"protein": "MSAPAQNNAEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGEIKFDVWDTAGQEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVASPALAPPEVQVDEQLMHQYQQEMDQATALPLPDEDDADL", "text": "FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Not essential for cell viability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. Ran family."}
{"protein": "MLDESSSSDESRATELPVSSEDECEEVTDAKVLPNKVLVVFEGESTLFRDQLLDTVFGVQDQGNIVKQLSWDTKYYAVEYDLYVDECVDIHGWLNEVNSDDYEELRDLLTMIIIVRSFDSTQDTKEYNSVLYDFIQGNSVSVISVNTNSARQVKDTYDEFLELDASSIEFINYHDDRVEKETNECKGMARLKEIIDTHPWTDCKVVLKNKESTSDKVNKPDLEYLIDTLKKAKIHYQKLSNGSDGFSEEAEQFALQMATDIANNL", "text": "FUNCTION: Involved in gross chromosomal rearrangements (GCRs) and telomere healing. SIMILARITY: Belongs to the IRC6 family."}
{"protein": "MALQTPVLSPATPTVMAESALYRQRLEVIAEKRRLQEEIGAARRELEEEKLRVERLKRKSLRERWLMDGAAEGPERPEEPASKDPQSPEGQAQARIRNLEDSLFSLQSQLQLLQSASTGAQHRPAGRPAWRREGPRPLSQSAMEAAPTAPTDVDKRTSLPDAPVGMSPESPSDPREESIAVLPASRPSTEAIGTSSEANGPCPGHSPLPEQLSLGVSSVTKAKGDGAVEVVWAGLRATENSATGPTDVELEAKVEEVVLEAIGARQGTSSPELPTWVKEGRGVVEVVWEGLGGRDLDVTGESGRDAEATHTSSRRLQEQFEAETCRKEEGASRDSLEGVGQGGPGVEEGSFIWVERVALSEDWEEILMEGLEAPQGAGSAGEPEALIGAQPRGGEASWEVEKREVEKVEGIEEKGRAEKLGAEREDGVAVLPDETQGREENEAEKVERKDSEGPFPAEIATDEEKWEVKTTEGEESLEVEKGGEAEPVTTEKPLVTEKKPEGSLETERKGSEMPLDQEKDGEGSLDRESKTTEILLDGEIGDKSSLDETKGSKKLLDEKTGGEGSLDEEAEGSKKLLDREADGIEPFSEVDKTSGAKDDVSPEEQGKANEGAEFQAEDASPPGATVCVQDEPRSEEQGQQEPEKQEGLVEGAASKPEPCTEREGPPGDATLLLAETPAPEQPVESQPLLHQEASSTNPGDHPAPTYAPAQQLELAEAKEASGPKQKTCQCCVVM", "text": "FUNCTION: ATP-binding protein, which may act as a adapter in the Toll- like receptor (TLR) signaling. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the paralemmin family."}
{"protein": "MSLREEALHLHKVNQGKLESKSKVEVRNAKDLSLAYSPGVAEPCKDIHEDINKVYDYTMKGNMVAVVTDGTAVLGLGNIGPEAALPVMEGKAVLFKSFAGVDAFPIALNTNDVDKIVETVKLLEPTFGGVNLEDIAAPNCFIIEERLKKETNIPVFHDDQHGTAIVTVAGLVNALKLSGKSMSSIKVVANGAGAAGIAIIKLLHHYGVRDIVMCDSKGAIYEGRPNGMNDVKNEVAKFTNQDRKDGSLKDVIVDADVFIGVSVAGALTKEMVQSMAKDPIIFAMANPNPEIMPEDAREAGASVVGTGRSDFPNQVNNVLAFPGIFRGALDVRATHINEEMKIAAVEAIASLVSEDELSADYVIPAPFDKRVAPAVAKAVAKAAMETGVARITVDPEEVAEKTRKLTIIGE", "text": "FUNCTION: Bifunctional enzyme with both malic and malolactic enzyme activities (PubMed:33824210). In the absence of NADPH, catalyzes the reversible decarboxylation of malate to pyruvate (PubMed:16788182, PubMed:33824210). Can use NAD and NADP, but with a very strong preference for NADP (PubMed:16788182). In the presence of excess NADPH, catalyzes the non-oxidative decarboxylation of malate to lactate (PubMed:33824210). During growth on glucose, contributes to NADPH balancing via oxidation of the NADPH produced in excess by other enzymatic reactions (PubMed:33824210). Can also catalyze the decarboxylation of oxaloacetate (PubMed:16788182). SIMILARITY: Belongs to the malic enzymes family."}
{"protein": "MAGGPGPGEPAAPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSGQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPAPLPSPGTTAPRPSSIPAPAEAEAWSPRKLPSSASTFLSPAFPGSQTHSGPELGLVPSPASLWPPPPSPAPSSTKPGPESSVSLLQGARPFPFCWPLCEISRGTHNFSEELKIGEGGFGCVYRAVMRNTVYAVKRLKENADLEWTAVKQSFLTEVEQLSRFRHPNIVDFAGYCAQNGFYCLVYGFLPNGSLEDRLHCQTQACPPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLTPKLGDFGLARFSRFAGSSPSQSSMVARTQTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVVLETLAGQRAVKTHGARTKYLKDLVEEEAEEAGVALRSTQSTLQAGLAADAWAAPIAMQIYKKHLDPRPGPCPPELGLGLGQLACCCLHRRAKRRPPMTQVYERLEKLQAVVAGVPGHSEAASCIPPSPQENSYVSSTGRAHSGAAPWQPLAAPSGASAQAAEQLQRGPNQPVESDESLGGLSAALRSWHLTPSCPLDPAPLREAGCPQGDTAGESSWGSGPGSRPTAVEGLALGSSASSSSEPPQIIINPARQKMVQKLALYEDGALDSLQLLSSSSLPGLGLEQDRQGPEESDEFQS", "text": "FUNCTION: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3. SUBCELLULAR LOCATION: Cytoplasm Nucleus Lipid droplet Note=Translocates to the nucleus when sumoylated. RSAD2/viperin recruits it to the lipid droplet (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily."}
{"protein": "MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTIYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF", "text": "FUNCTION: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SIMILARITY: Belongs to the actin family."}
{"protein": "MHVKKGDKVMVISGKDKGKQGTILAAFPKKDRVLVEGVNMVKKHSKPTQANPQGGISNQEAPIHVSNVMPLDPKTGEVTRVGYKVEDGKKVRVAKKSGQVLDK", "text": "FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. FUNCTION: Has also been isolated as a basic, heat-shock stable DNA- binding protein from the B.subtilis nucleoid. It binds cooperatively to double-stranded supercoiled DNA which it further compacts into complexes 15-17 nm in diameter. Overexpression of the protein disrupts nucleoid segregation and positioning. FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, nucleoid Note=Is located predominantly at the nucleoid poles during exponential phase, while in stationary phase the protein is more evenly distributed in the whole cell. SIMILARITY: Belongs to the universal ribosomal protein uL24 family. SIMILARITY: Belongs to the universal ribosomal protein uL24 family."}
{"protein": "MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYTQYLCGGVLLDPNWVLTAAHCYDDNYKVWLGKNNLFKDEPSAQHRFVSKAIPHPGFNMSLMRKHIRFLEYDYSNDLMLLRLSKPADITDTVKPITLPTEEPKLGSTCLASGWGSITPTKFQFTDDLYCVNLKLLPNEDCAKAHIEKVTDAMLCAGEMDGGKDTCKGDSGGPLICDGVLQGITSWGHTPCGEPDMPGVYTKLNKFTSWIKDTMAKNP", "text": "FUNCTION: 7S NGF alpha chain stabilizes the 7S complex. The beta dimer promotes neurite growth. The gamma chain is an arginine-specific protease; it may also have plasminogen activator activity, as well as mitogenic activity for chick embryo fibroblasts. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily."}
{"protein": "MGWLPLLLLLVQCSRALGQRSPLNDFQLFRGTELRNLLHTAVPGPWQEDVADAEECARRCGPLLDCRAFHYNMSSHGCQLLPWTQHSLHTQLYHSSLCHLFQKKDYVRTCIMDNGVSYRGTVARTAGGLPCQAWSRRFPNDHKYTPTPKNGLEENFCRNPDGDPRGPWCYTTNRSVRFQSCGIKTCREAVCVLCNGEDYRGEVDVTESGRECQRWDLQHPHSHPFQPEKFLDKDLKDNYCRNPDGSERPWCYTTDPNVEREFCDLPSCGPNLPPTVKGSKSQRRNKGKALNCFRGKGEDYRGTTNTTSAGVPCQRWDAQSPHQHRFVPEKYACKDLRENFCRNPDGSEAPWCFTSRPGLRMAFCHQIPRCTEELVPEGCYHGSGEQYRGSVSKTRKGVQCQHWSSETPHKPQFTPTSAPQAGLEANFCRNPDGDSHGPWCYTLDPDILFDYCALQRCDDDQPPSILDPPDQVVFEKCGKRVDKSNKLRVVGGHPGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSCHEPLTGYEVWLGTINQNPQPGEANLQRVPVAKAVCGPAGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWGESIGTSNNTVLHVASMNVISNQECNTKYRGHIQESEICTQGLVVPVGACEGDYGGPLACYTHDCWVLQGLIIPNRVCARPRWPAIFTRVSVFVDWINKVMQLE", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily."}
{"protein": "MEKEDAGAVQCGTGEGEAVVLNERSEQCSAFASIAGCDEAVAQCFLAENDWDMERAINSFFEPGVESALQNKAAADIADPLKQETMSGTASDSCIDLTGDDLVVTKSEATTSNSSTVKQEDESHFSFLTWNIDGLDESNVAERARGVCSYLALYSPDVVFLQEVIPPYYEYLKKRAVSYTIITGNEDEYFTAMMLKKSRVKLISQEIVPYPSTVMMRNLLVANVNISGNSICLMTSHLESTKDHSKERLKQLDIVLKKMMDAPPLATVIFGGDTNLRDQEVAKIGGMPNNILDVWDFLGKPEHCRYTWDTKVNKNLRAPYICRLRFDRIFFRASQEGSQVIPQSLYLAGTEKLDCGRFPSDHWGLLCDFAIIL", "text": "FUNCTION: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead- end complexes between DNA and the topoisomerase 2 (top2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. SUBCELLULAR LOCATION: Nucleus Nucleus, PML body. SIMILARITY: Belongs to the CCR4/nocturin family. TTRAP/TDP2 subfamily."}
{"protein": "KIPCGESCVWIPCLTSVFNCKCENKVCYHD", "text": "FUNCTION: Probably participates in a plant defense mechanism. Inhibits the cytopathic effects of the human immunodeficiency virus. SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily."}
{"protein": "RGARGETEGRWSREAPGAWACGVERGGCQHECKGSAGASNCLCPADAALQADGRSCGLPAEHPCHQLCEHFCHLHGLGNYTCICEAGYQLAADQHRCEDVDDCAQLPSPCPQRCVNTEGGFQCHCDTGYELVDGECVDPVDPCFDNNCEYQCQPVGRSEHKCICAEGFAPVPGAPHKCQMFCNQTSCPADCDPHYPTICRCPEGYIIDEGSTCTDINECDTNICPGQCHNLPGTYECICGPDSALSGQIGIDCDPTQVNEERGTPEDYGGSGEPPVSPTPGATARPSPAPAGPLHSGVLVGISIASLSLVVALLALLCHLRKKQGASRGELEYKCGVPAKELMLQQVKTERTPQKL", "text": "FUNCTION: Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein."}
{"protein": "MRKRTLVSVLFLFSLLFLLPDQGRKLHANAEESSDDVTDPPKVEEKIGGHGGLSTDSDVVHRESESMSKKTLRSNAEKFEFQAEVSRLMDIIINSLYSNKDIFLRELISNASDALDKIRFLALTDKDVLGEGDTAKLEIQIKLDKAKKILSIRDRGIGMTKEDLIKNLGTIAKSGTSAFVEKMQSSGDLNLIGQFGVGFYSAYLVADYIEVISKHNDDSQYVWESKANGKFAVSEDTWNEPLGRGTEIRLHLRDEAGEYLEESKLKELVKRYSEFINFPISLWASKEVETEVPVEEDESADEETETTSTEEEKEEDAEEEDGEKKQKTKKVKETVYEWELLNDVKAIWLRSPKEVTEEEYTKFYHSLSKDFTDEKPMAWSHFNAEGDVEFKAVLYVPPKAPHDLYESYYNSNKANLKLYVRRVFISDEFDELLPKYLSFLKGLVDSDTLPLNVSREMLQQHSSLKTIKKKLIRKALDMIRKLAEEDPDEIHDDEKKDVEKSGENDEKKGQYTKFWNEFGKSVKLGIIEDAANRNRLAKLLRFETTKSDGKLTSLDQYIKRMKKSQKDIFYITGSSKEQLEKSPFLERLIKKGYEVIFFTDPVDEYLMQYLMDYEDKKFQNVSKEGLKVGKDSKDKELKEAFKELTKWWKGNLASENVDDVKISNRLADTPCVVVTSKFGWSANMERIMQSQTLSDANKQAYMRGKRVLEINPRHPIIKELKDRIASDPEDESVKETAQLMYQTALIESGFILTDPKDFAARIYNSVKSGLNISPDAVADEEIEAAEEPETSEATETKSDDLAGGLNIEAEPVEQQEENTKDEL", "text": "FUNCTION: May have a molecular chaperone role in the processing of secreted materials. Required for shoot apical meristem (SAM), root apical meristem (RAM) and floral meristem (FM) formation, probably by regulating the folding of CLAVATA proteins (CLVs). Also involved in pollen tube elongation (PubMed:11867518). Involved in resistance to tunicamycin- or high calcium-induced ER stresses. Possesses ATPase activity (PubMed:25297550). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the heat shock protein 90 family."}
{"protein": "MKNKLGIILVCNCLFSLFINRGVGAEETINIGDCSFNGHPLYGKIQLVGSFPDLTVQVVSSFPDLKVQLVESFPNQCGQWQIVTSFPDTKVQIVESFPDVKIQYVDSFPGLP", "text": "SIMILARITY: To U.parvum UU089.1."}
{"protein": "MNYIYSATTNSFYPLEMKEDYTQAGSWPDDAVEVDEQVYIEFSGLPPKGKIRIAGENGFPAWSEIPPPTHEEQIAAAELKKQQLINQANDYMNSKQWAGKAAIGRLKGEELAQYNLWLDYLDALELVDTSSAPDIEWPTPPAVQAR", "text": "SIMILARITY: To E.coli YmfS."}
{"protein": "MSQLALQMSSLGVEGEGIWLALGTIGMLLGMLYFIADGLDVQDPRQKEFYVITILIPAIAAASYLSMFFGFGLTEVSLANGRVVDVYWARYADWLFTTPLLLLDIGLLAGASQRDIGALVGIDAFMIVTGLVATLTKVVVARYAFWTISTISMVFLLYYLVAVFGEAVSDADEDTRSTFNALRNIILVTWAIYPVAWLVGTEGLALTGLYGETLLFMVLDLVAKVGFGFILLRSRAIMGGGSEPTPSAQETAAD", "text": "FUNCTION: Light-driven proton pump. The chromophore contains 78% all- trans- and 22% 13-cis-retinal in the dark and 90% all-trans- and 10% 13-cis-retinal upon illumination with >500 nm light. FUNCTION: Light-driven proton pump. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family."}
{"protein": "MAFATRQLVRSLSSSSTAAASAKKILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSSISTSTDAASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTIFASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEVVKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLLVPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIIDGWHEMDSQNPLFQPSPAMNKLVAENKFGKKTGEGFYKYK", "text": "FUNCTION: Mitochondrial fatty acid beta-oxidation enzyme that catalyzes the third step of the beta-oxidation cycle for medium and short-chain 3-hydroxy fatty acyl-CoAs (C4 to C10) (PubMed:9593854, PubMed:2817332). Plays a role in the control of insulin secretion by inhibiting the activation of glutamate dehydrogenase 1 (GLUD1), an enzyme that has an important role in regulating amino acid-induced insulin secretion (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family."}
{"protein": "MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSETQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGSSVVMGCKAAGATRIIGVDVNKEKFKKARELGATECLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGLLPASVQLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAKKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILLL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-V subfamily."}
{"protein": "MAKKRDRIVNTQPFISDDASVASSRKRSKVPKTHQKQEKLIEAGMSEKIMKQALAQQKEVADEENAERNPSSAAFAVAGAATAGEEQKILEEEEDDIDDFDGTFENQSQFDKQEEINEDDEKLFESFLNKNAPPQRTLTDIIIKKLKDKDADLAEEERPDPKMDPAITKLYKGVGKFMSEYTVGKLPKAFKLVTSMEHWEDVLYLTEPEKWSPNALYQATRIFASNLKDRQVQRFYNYVLLPRVREDIRKHKKLHFALYQALKKSLYKPSAFNQGILFPLCKSGTCNLREAVIIGSILEKCSIPMLHSCVALNRLAEMDYCGTTSYFIKVLLEKKYCMPYRVLDALVAHFMRFVDDIRVMPVIWHQSLLTFVQRYKYEILKEDKEHLQTLLQRQKHHLVTPEILRELKDSRNRGEKEDPMVDNFAPVPAKEDRFDIPEVPMEED", "text": "FUNCTION: Essential protein required during embryogenesis and pollen development (PubMed:23382868). Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits (PubMed:23382868). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the bystin family."}
{"protein": "MLTPAFELTQDCDFLTVAIRVPHARASEFDVYFEGVDFKFYAKPYFLRLTLPGRIVENGSEQGTYDADKGIFTIRLPKETPGQHFEGLNMLTALLAPRKSRSAKPLVEEIGASGVAEEGADDEDEEFDWEIEQTPYEEVSESTLQSQCHYGFGNLRAGVVQRLQDELSEVIDIKDPDFTPVTERRQKRLAAELAKFDPDHYLADFFEDEAVEQILKYSPWWNDAHAEMVASLGKNQEQGDSAALVSFSEEEKYQLRKFVNKSYLLDKTAHRQVYYGLVDILLAYCYEVRVTEGEHSVESAWTIRKLSPTLCWFETWTDVHEILVSFGRRVLCYPLYRHFKLVLKAYRDTIKILQLGKSAVLKCLLDVHKVFQENDPAYILNDLYISDYCVWIQKAKSKKLAALTEALKAVSLSKAQLGLELPELEAAALLVQEEEGAGRAAQCNPSHQAPHSSPEPSDSDSTSSSGTEDSASEQEEPAGTQPSLLTSLQAPLLEEDSALIIRESGLCRNMASQGCEVSQGQPLASARAPLIEELGDALKMLRVSTPHGVSAGSHGSVEDAEERGQVPCD", "text": "FUNCTION: Required for the quantitative accumulation of H/ACA ribonucleoproteins (RNPs), including telomerase, probably through the stabilization of DKC1, from the time of its synthesis until its association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus, nucleoplasm Note=May at least partially shuttle between cytosol and nucleoplasm. SIMILARITY: Belongs to the SHQ1 family."}
{"protein": "MSNHEKMSTTDLMENLREELTCFICLDYFSSPVTTECGHSFCLMCLLKSWEEHNTPLSCPECWRTLGAPHFQANERLGRLANIGRQLRSQVLQSEDEQSICGRMPGPSWVFSDDEQSVINVSPPSQGTNKACFSSEAEEQHKEKLQDIINILRKKKKEVQAILNHEKERVMLCKEETKTCKQVVVSEYMKMHQFLKEEEQLQLQLLEREEKANMKKLRENEIQLTQQIRRLGKMIGRIESTCQNLTLESFEEVKGAMDRYESLLFQSPETTITELSLCHITGMREMLRKFSTDITLDPATANAYLLLSEDLKSVRYGGTRQQLPDNPERFDQSATVLGAQIFTCGRHYWEVEVGKKTEWEVGICKDSVNRKGNLPKPPGDLFSLIGLKIGDDYSLWVSSPLKGQHVREPVHKVGVFLDYDSGHIAFYNATDESLIYSFPPTPFHEALRPIFSPCLPNEGTNTDPLIICHI", "text": "FUNCTION: Probable E3 ubiquitin-protein ligase which plays an important role in blastocyst development. Involved in progression of blastocyst stage and subsequent embryo development."}
{"protein": "MLQMPKLNEIPPGRGGPGEPWGEGRWAGPTGPEAARPARGARGQARGARARWDSWEHSRLPTHPGPGWDQCSPSFLCAPSSQKLIMESKDEVSDSDSGIILQSGPDSPVSPMKELTNAVRKQQRALEARLEACLEELRRLCLREAELTGTLPAEYPLKPGEKAPKVRRRIGAAYKLDEWALHREDPLSSLERQLALQLQITEAARRLCAEENLSRQARRQRKHAALQEEKKLRDLQRCLGDRRRNSEPPPTTVPSLGRELSASDDSSLSDGLLLEEEDSQAPKPPPESPAPPSRPLPPQSLEGLQPTGPESGGQERAPIQNSPWKETSLDHPYEKPRKSSELSSESSSPATTPQDQPNPSSLWVLDAASYHVVPIRNVPGQRQGRTSAPATPEMQGRRGQSQSLRVDSFRAGAEGRGRSAFPRRRPTHYTVTVPDSCFTPGKPPLPHPACHSCSEDSGSDVSSISHPTSPGSSSPDISFLRPLCLPEPPRHRGAWGPACGRELAPHYSKLLLPAGYFPTGRYVMVAEGHLPPGEWELCRAAVGAAYDEEGAPLRYQRLVPSHSRIVRTPSLKDSPAGRGLSKAAVSEELKWWHERARLRSSRPHSLDRQGAFRVRSLPPGRESFGRASGPRTQVPPVYVLRRSTDGAPVQVFVPENGEIISQV", "text": "FUNCTION: Expressed in peripheral macrophages and intestinal myeloid- derived cells, is required for optimal PRR (pattern recognition receptor)-induced signaling, cytokine secretion, and bacterial clearance. Upon stimulation of a broad range of PRRs (pattern recognition receptor) such as NOD2 or TLR2, TLR3, TLR4, TLR5, TLR7 and TLR9, associates with YWHAQ/14-3-3T, which in turn leads to the recruitment and activation of MAP kinases and NF-kappa-B signaling complexes that amplifies PRR-induced downstream signals and cytokine secretion (By similarity). In the intestine, regulates adherens junction stability by regulating the degradation of CYTH1 and CYTH2, probably acting as substrate cofactor for SCF E3 ubiquitin-protein ligase complexes. Stabilizes adherens junctions by limiting CYTH1- dependent ARF6 activation (PubMed:29420262). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Translocates to the nucleus upon NOD2 stimulation."}
{"protein": "MKTFLILAMAVALAKAQSTDEITNLVQFGKLVMCLGNIGYTEGLEYDGYGCFCGKGGKGTPVDATDRCCEVHDNCYGQAVEEGKCWSVETYGTTYWYDQSTSGSCSIRCWEEGDYNSLVPRKACKAAICECDRKAAQCFADNRPTFNRKYLNYAKDTC", "text": "FUNCTION: Starfish phospholipase A2 (PLA2) that has hemorrhagic and capillary permeability-increasing activities and hence is considered to be deeply involved in the local inflammation. Shows hemolytic activity only in the presence of phosphatidylcholine (PC). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn- phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily."}
{"protein": "MFVRSSWLLLWGTIVWASAEPVTLHIGGTFPMESGSGGWAGGEACLPAVEMALKDVNSRLDILPGYVLNMTNHNSQCQPGLAMQQLYDFLYKPPTKLMLLTGCSPVTTVIAEAAPVWKLVVLSYGGSSPALSNRNRFPTLFRTHPSANMQNPTRIHIMEKFKWKRFTILMSVEEVFVTTAKDLEAIARKKGIKVDRQSFYGDPTDAMKTLQRQDARIIVGLFYVTEARKVLCQAYHHGLYGRRYVWFFIGWYADTWYIPPPEEHLNCTAEQMTEAAEYHFTTESVMLSRDNIPAISEMTGMQFQQRLTQYFQKDTANVGGFPEAPLAYDAVWALALAFNCTRNNLPSHIRLENFTYDNKVIADTLFQCVKNTSFRGVSGKVMFSDSGDRIARTQIEQMQGGKYKIMGYYDTTSGDLEWYNKEQWLNGKGPPPDSTVIKKHAMTVSNEFYYPTILFAVLGIAACVFIYLFTQKHHERLIIFQSQPECNNILLIGCSLCLFSLFLIGLPSDDISISESLFPLLCHARVTILLFGFTFAYGSMFAKVWIVHRMGATENQQLASRQKDEEENTPWEGIRTLISTMVGRQALMRKSSGQAYGALLEKRNTVLNQPISSSKFYVIVAALTAVDVFVCFVWVLIDPLHLTEQKFPLFTPADSEEDEMIMPVLQQCQSNQQEVWIGIIMGFKCLLLVFGTFLSYETRNLKLRFINDSRFVGLAIYNVAVMTLVTAPVVTLLIHGKVDANFAFISLTVLICTYISVGLIYGPKIRHIIKVPPSADEIQLNGNVGPGVMSKVDQKRYDMLKKENETLQIQIEEKERKIHECKERLEELTKNSETEDMNAQLLCENDKQIADENLTYSTATTLTTTIPLIDLQNGNHPGQIYENDNDDDGSSTSSDEILL", "text": "FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by gbb-1 and gbb-2 (By similarity). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (By similarity). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium- channels and modulates inositol phospholipid hydrolysis (By similarity). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (By similarity). Along with gbb-2, may couple to the G(o)-alpha G-protein goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons (PubMed:18614679). As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior (PubMed:18614679). Acts in neurons to regulate lifespan, and this may be through G-protein-egl-8/PLC-beta signaling to the transcription factor daf-16/FOXO (PubMed:26537867). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family."}
{"protein": "MALLLVSLLAFLGTGSGCHHWLCHCSNRVFLCQDSKVTEIPTDLPRNAIELRFVLTKLRVIPKGSFAGFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPSLRYLLISNTGIKHLPAVHKIQSLQKVLLDIQDNINIHIVARNSFMGLSFESVILWLSKNGIEEIHNCAFNGTQLDELNLSDNNNLEELPNDVFQGASGPVILDISRTKVHSLPNHGLENLKKLRARSTYRLKKLPNLDKFVTLMEASLTYPSHCCAFANLKRQISELHPICNKSILRQDIDDMTQIGDQRVSLIDDEPSYGKGSDMMYNEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILRVLIWFISILAITGNTTVLVVLTTSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIHTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLTAITLERWHTITHAMQLECKVQLRHAASVMVLGWTFAFAAALFPIFGISSYMKVSICLPMDIDSPLSQLYVMALLVLNVLAFVVICGCYTHIYLTVRNPTIVSSSSDTKIAKRMATLIFTDFLCMAPISFFAISASLKVPLITVSKAKILLVLFYPINSCANPFLYAIFTKNFRRDFFILLSKFGCYEMQAQIYRTETSSATHNFHARKSHCSSAPRVTNSYVLVPLNHSSQN", "text": "FUNCTION: G protein-coupled receptor for follitropin, the follicle- stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily."}
{"protein": "MAQCNLFYQYPITPILEGHVRNILICTEKDVEKLQSQSSLRLREKIDQGHRDKLLRMRLKTELDALQKKMQKDSDVLNSHLKAIEDALLFTNDGEVNVETKADAQLIPKSPEKLEKFNQVAITPLDPFIRFTDDFRGEMINTFFNNAQMWNFTFGSWFYKLKRVFYNEPGLRRALKLTNVDSLTISKELLAVTVNALEQATVYPIFGSEMSDLEAALCILAAFYSTYENSQIDERTTLVDVITLLPVIFRLLGSEITALKNVSPSGTYFGFNDPSCMKFFVPMRKGKHYAENTFGNHVLIKMLLGRGVMQKIPGEKISQNFDVEARLHGAIKNDVLVYWTYQLMRPKLGNNVPIFIHDQHYLRSGLVAIESLFLLWRI", "text": "FUNCTION: Plays a role at the late stage in the encapsidation of viral DNA, assuring correct genome cleavage and presumably stabilizing capsids that contain full-lengtht viral genomes. Located on the external vertices of the T=16 icosahedric capsid, may bind together the tegument and the capsid through interaction with large tegument protein U31 (By similarity). SUBCELLULAR LOCATION: Virion. Host nucleus. SIMILARITY: Belongs to the herpesviridae UL25 family."}
{"protein": "MAGSPSRAAGRRLQLPLLSFLQGATAVLFAVFVRYNHKTDAALWHRGNHSNADNEFYFRYPSFQDVHAMVFVGFGFLMVFLQRYGFSSVGFTFLLAAFALQWSTLVQGFLHSFHGGHIHVGVESMINADFCAGAVLISFGAVLGKTGPAQLLLMALLEVVLFGINEFVLLHLLGVRDAGGSMTIHTFGAYFGLVLSQVLYRPQLEKSKHRQGLYHSDLFAMIGTIFLWIFWPSFNAALTSLGAGQHRTALNTYYSLAASTLGTFALSALVGEDGRLDMVHIQNAALAGRVVVGTSSEMMLTPFGALAAGFLAGTVSTLGYKFFTPILESKFKVQDTCGVHNLHGMPGVLGVLLGVLVAGLATHEAYGDGLESVFPLIAEGQRSATSQAMYQLFGLFVTLMFASVGGGLGGLLLKLPFLDSPPDSQCYEDQVHWQAPGATLSPLPTPAFQVPGEHEDKAQRPLRVEEADTQA", "text": "FUNCTION: Ammonium transporter involved in the maintenance of acid-base homeostasis. Transports ammonium and its related derivative methylammonium across the basolateral plasma membrane of epithelial cells likely contributing to renal transepithelial ammonia transport and ammonia metabolism. May transport either NH4(+) or NH3 ammonia species predominantly mediating an electrogenic NH4(+) transport (By similarity). May act as a CO2 channel providing for renal acid secretion (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily."}
{"protein": "MSPSAANTPSYDDFALALEAQSLDSQKGQLVRGKVCEYSTDGAYIDIGGKAPAFLPKREAALHAVLDLEAHLPKDEELEFLVIRDQNEDGQVTVSLRALALEQAWTRVAELQEGGQTVQVKVTGSNKGGVTADLEGLRAFIPRSHLNEKEDLDSLKGKTLTVAFLEVNRADKKLVLSERQAARTALVREIEVGQLINGKVTGLKPFGVFVDLGGATALLPINQISQKFVADVGAIFKIGDPIQALVVAIDNTKGRISLSTKVLENHPGEILENVAELQASAADRAERARKQLESQ", "text": "FUNCTION: Binds mRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family."}
{"protein": "MSSLPRGFEPQTPEDLGQRSLAELREMLKRQERLLRNVKFICKLPDKGKKISDAVTKLKAAIAEREEVRGRSELFYPVSLDCKERQKAIAVVDGDRDKAQNSDQILDTSSPVPGCSSVANITSSQTTSRQQGLAHPTRGGDAEAAEAEHTVSEHPTSSSGAPAPSSSQASEGLPQHCALGQVEDHPGSSDNLFIDRLQRITIADPTEHHSEGNRNPENLAGLWSGPQKKPHYMEVLEMRAKNPMPPPHKFKTNVLPSQPRDSSSACQRRGSPISSEERRRRDRKHLDDITAARLLPLHHLPTQLLSIEESLALQRQQKQSYEEIQAKLAAQKLAERLNIKMQSYNPEGESSRKYREVRDEDDDQSSEDEF", "text": "FUNCTION: Appears to be a stable component of the Pol II(G) complex form of RNA polymerase II (Pol II). Pol II synthesizes mRNA precursors and many functional non-coding RNAs and is the central component of the basal RNA polymerase II transcription machinery. May play a role in Mediator complex-dependent regulation of transcription activation. Acts in vitro as a negative regulator of transcriptional activation; this repression is relieved by the Mediator complex, which restores Pol II(G) activator-dependent transcription to a level equivalent to that of Pol II. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRINL1 family."}
{"protein": "MKRRTDPECTAPLKKQKRIGELARHLSSTSDDEPLSSVSHAAKASTTSLSGSDSETEGKQPCSDGFKDAFKADSLVEGTSSRYSMYNSVSQKLMAKMGFREGEGLGKYSQGRKDIVETSNQKGRRGLGLTLQGFDQELNVDWRDEPEPNACEQVSWFPECTTEIPDSREMSDWMVVGKRKMVIEDETEFCGEELLHSMLKCKSVFDILDGEEMRRARTRANPYEMIRGVFFLNRAAMKMANMDFVFDRMFTNPLDSSGKPLLKESDIDLLYFADVCAGPGGFSEYVLWRRKWHAKGFGMTLKGPNDFKLEDFYSASSELFEPYYGEGGVDGDGDITRPENINAFRNFVLDNTDRKGVHFVMADGGFSVEGQENLQEILSKQLLLCQFLMALSVVRTGGHFVCKTFDLFTPFSVGLIYLLYCCFERVCLFKPVTSRPANSERYVVCKGLKVGIDDVREYLFSVNIQLNQLRNTDSDVNLVVPLSVIKGDHEFNDYMIRSNESYCSLQIKALAKIHAFVQDTTLSEPRQAEIRKECLQLWEIPDRARVAPSPSDPKFKFFELIKDTDINIFSYKPTLLTAKTLEKIRPVLEYRCMVSGSEQKFLLGLGKSQIYTWDGRQSDRWVKLDLKTELPRDTLLCVEIVHELKGEGKAQRKISAIHILDVLVLNGSDVREQHFNQRIQLAEKFVKAVSKPSRPDMNPIRVKEVYRLEEMEKIFVRLEMKLIKGSGGTPKLSYTGRDDRHFVPTGVYIVRTVTEPWTMAFSKGWKKKFFYNKKTGESFFTLPPESIAPFHTCYYTRLFWEWGDGFHMRDSQKPQDPDKLSKEDVLSFIQSHNPLGP", "text": "FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG- capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MADIPDNAPQHCPGTDSTEAGKSSACQGCPNQSICASGAAAGPDPAIEEIKEKMSLVKHKILVLSGKGGVGKSTFSAHLAHGLAQDEGKEVALLDVDICGPSIPKMMGLEGEQVHQSGSGWSPVYVEDNLAVMSVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLSAAGIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMSGFICPKCKNESQIFPPTTGGAEKMCTDLSVSLLGKVPLDPNIGKSCDTGKSFFTEIPDSPATLSYRKIIQRIQDYCEKKK", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nubp1-nubp2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily."}
{"protein": "MMLPQWLLLLFLLFFFLFLLTRGSLSPTKYNLLELKESCIRNQDCETGCCQRAPDNCESHCAEKGSEGSLCQTQVFFGQYRACPCLRNLTCIYSKNEKWLSIAYGRCQKIGRQKLAKKMFF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the colipase family."}
{"protein": "MSSDRPVALVTGANKGIGFAIVRDLCRKFLGDVVLTARDESRGHEAVKQLQTEGLSPRFHQLDIDNPQSIRALRDFLLQEYGGLNVLVNNAGIAFKVVDPTPFHIQAEVTMKTNFFGTQDVCKELLPIIKPQGRVVNVSSSVSLRALKSCSPELQQKFRSETITEEELVGLMNKFIEDAKKGVHAKEGWPNSAYGVTKIGVTVLSRIYARKLNEERREDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPGAEGPHGQFVQDKKVEPW", "text": "FUNCTION: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics (PubMed:8198567, PubMed:7705364). Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol (By similarity). Can convert prostaglandin E to prostaglandin F2-alpha (By similarity). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S- nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b- DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MPKKFQGENTKSAAARARRAEAKAAADAKKQKELEDAYWKDDDKHVMRKEQRKEEKEKRRLDQLERKKETQRLLEEEDSKLKGGKAPRVATSSKVTRAQIEDTLRRDHQLREAPDTAEKAKSHLEVPLEENVNRRVLEEGSVEARTIEDAIAVLSVAEEAADRHPERRMRAAFTAFEEAQLPRLKQENPNMRLSQLKQLLKKEWLRSPDNPMNQRAVPFNAPK", "text": "FUNCTION: Ribosome-binding protein involved in ribosome hibernation: associates with translationally inactive ribosomes and stabilizes the nonrotated conformation of the 80S ribosome, thereby promoting ribosome preservation and storage (PubMed:32687489). Also required for proper progression of late cytokinetic stages (PubMed:23894443). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Midbody Note=Colocalizes with gamma-tubulin at interphase, prophase, metaphase, and anaphase. Relocates from centrosome to midbody at telophase. SIMILARITY: Belongs to the CCDC124 family."}
{"protein": "MDYTISEFGKVFLFLLFGVVFVIGGYVSSRMLRPHRPNDEKLTSYECGEEAVGSAWVQFNIRFYVVALIFIIFDVEVLFLFPWATVFKQLGGFALFEAVIFVTILTLGLVYAWVKGDLDWVRPTPNVPKMPEKRFDNISSGRSQVVKEESVS", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family."}
{"protein": "MQESGACRKKPAMPSRNAGSHLVVMKRIQRNGDGAMKRQKHGRRELREVKRTSRRSAKSEDFSGAEDENNGENETEVAVNNSESGEQEGVDDTGMAYNALLTLLGSEKPEKPTKRRKNDEAGVEEINEDDLEIHLTKSDDESDEENEPEVASDDEESDEKFNAFDFHFNQPSEDYMEKASQSVTSKWNNTTKETIDEYVVSTSTPSCMNKESVKLGISSIKKRVRDVYSEKHPSKISGIDASLLDSMLNYKSVLYPYKHYNNTFYRELYSMHAINHVFKTRDNILKNTEKIKHAQEMALEGKSHEDKEYRDQGFTRPKVLILLPTRNAAYEVVENILKYSGSEQQENKKKFKAQFNSNDVPPETKPQDFRDAFKGNNNDFFCLGMKFTRKSAKLYSSFYSSDIIIASPLGLSMILENPDKKKRQYDFLSSIEVFIVDRATQIEAQNWAHVNLVLKYLNKVPKEFHDADFSRIRMWYINDQAPLVRQTLVFCEYTTPPITSLVSSKSVNIGGRVRYKPIYTSKNCIMNSIGLRLKQIFQRFSSSSPMEDSENRFKFFINSMLPSLLSSTSYSDGILVYIPSYFDYVRIKNYMRNSTKFTFEGIDEYSTQSKLTRYRQQFISGKVKILLYTERLHYFRRFEINGVKTLLMYGVPSNPLFYKELVRCIGKSVFKEVADIDLSFVKVMYSQWDAIALERIVGGDRAPVLCSGTNEMYEFR", "text": "FUNCTION: DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP25 family."}
{"protein": "MRLDKFIAQQLGVSRAIAGREIRGNRVTVDGDIIKNAAFKLLPEHAVAYDGNPLAQQHGPRYFMLNKPQGYVCSTDDPDHPTVLYFLDEPVAYKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAAQFAKGVQLHNEKDLTKPATLEVITPVQVRLTISEGRYHQVKRMFAAVGNRVVELHRERIGAITLDENLAPGEYRPLTEEEIASVG", "text": "FUNCTION: Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family."}
{"protein": "MGSRRFDAEVYARRLALAAAATADAGLAGLVITPGYDLCYLIGSRAETFERLTALVLPAAGAPAVVLPRLELAALKQSAAAELGLRVCDWVDGDDPYGLVSAVLGGAPVATAVTDSMPALHMLPLADALGVLPVLATDVLRRLRMVKEETEIDALRKAGAAIDRVHARVPEFLVPGRTEADVAADIAEAIVAEGHSEVAFVIVGSGPHGADPHHGYSDRELREGDIVVVDIGGTYGPGYHSDSTRTYSIGEPDSDVAQSYSMLQRAQRAAFEAIRPGVTAEQVDAAARDVLAEAGLAEYFVHRTGHGIGLCVHEEPYIVAGNDLVLVPGMAFSIEPGIYFPGRWGARIEDIVIVTEDGAVSVNNCPHELIVVPVS", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MTTIIAFIFVFGLIVFFHELGHFLFAKRAGIMVKDFSIGFGPKIFAYRKKETQYTIRLLPIGGYVRMAGEDGEEIELKPGYRVGLELTPEETVSKIIVNGKDQYVNAQPIEVSLCDLEKELFIEGYEDYDDTKKVRYQVERDALVIDGKIETMITPYDRSFNAKSLGNRAMTIFAGPLFNFILAILIFTALAFVQGGVPSTDNTLGNVLPDGAAAEAGLKKGDEVLSINGKETKSWTDIVQNVSENPGKTLDFKIERDGKTQDIDVKPATQKENGKDVGKIGVETPMDSSFTAKITNGFTQTWNWIVQIFTILGNMFTGGFSLDMLNGPVGIYTSTQQVVQYGFMTVLNWTAVLSINLGIVNLLPLPALDGGRLMFFLYELVRGKPIDPKKEGIIHFAGFALLMVLMILVTWNDIQRAFF", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
{"protein": "MPTITLPRIIYPFPSLINQFVTAAHEQNRQWVADFGFITTPEAMARFDRSRFAWLAARAFPHAGFHELCTIANFNTWLFMLDDQCDEAQLGKKAVYLEHVTDGFMNILKHNTPVDTVLGRSFTDIWERMQALGDTAWQTRFIRSMEEYFTSCHWEAGNRAADIVPTVAEYVTMRPYTGALFADVEAIEIIEKVYLPAHILQHFIVQRLVLACNNIVCWANDIFSCAKEARQGDVHNLVLVLQHERNSTLQEAVNETARMHNEEVKLFTALEKLLPSFGAEMDRELERFMAVLRSWITANYDWSYHDTGRYQVKEVEVVINS", "text": "FUNCTION: Catalyzes the conversion of (2Z,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene (1S,6S,7R)-(-)-gamma-cadinene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP to yield a germacradienyl cation (PubMed:23307484, PubMed:27666571, PubMed:27829890). The only accepted substrate is (2Z,6E)-farnesyl diphosphate (FPP) (PubMed:27829890). SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MASADWGYGSENGPDQWSKLYPIANGNNQSPIDIKTSEANHDSSLKPLSISYNPATAKEIVNVGHSFHVIFDDSSNQSVLKGGPLADSYRLTQFHFHWGNSNDHGSEHTVDGTRYSGELHLVHWNSAKYSSASEAISKADGLAILGVLMKVGPANPSLQKVLDALNSVKTKGKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKDSISLSPEQLAQLRGLLSSAEGEPAVPVLSNHRPPQPLKGRTVRASF", "text": "FUNCTION: Catalyzes the reversible hydration of carbon dioxide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
{"protein": "MNAYPWLEIPRTVRFSDTDAAGVMHFQHLLGWCHQAWEDSLEQFGIPVGAVFPGGRSDQPSVALPIVHCHADFRAPMYVGDAAVIHLLPKRIDPGCFEVVSEISLNTQKVASGCLQHLAIDAVTRQRCSLPEPIERWIEASTLGQIQPL", "text": "FUNCTION: Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a reaction involved in phylloquinone (vitamin K1) biosynthesis. SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family. DHNA-CoA hydrolase subfamily."}
{"protein": "MTLDNYNIFGDEYLFSMPLSPLPKVLGTFDGIQSAPTLTTPTLTPTTLRSIEETFFEMTNDAPYQAGFKPPPLAPLVNNNNNNNNNGNGNGNGNGNQQQQQVFDCGASVMPGSDTEESNGSWADGQMNEDQSISDTSSGATDSTSYQNGHMMGNSGGGNGGGTGGANNFSNVLAAAGRNTNTSNSATPARRGGGRRPNRSANMTPEEEEKRRIRRERNKQAAARCRKRRVDQTNELTEEVELLEKRGENLKKEMELLNETKNQLEYFLQAHRPTCQKVRADMLSVTTCNGLIGPPALLSAGSCGSGSSHHNNNSNSNDSSSGTITGLDATLNSTGRSNSPLDLKPVPIDEDLLLHIKDEPLDGALDSSSSLDQDGPPPHKRFALPNIATLMTPTGPAGSLQTPVSGTAPHGFGSFPTTISNISSIHNGPTLNSLNKMPKERPNTLAFQRPFGGQMQLSVSGRAPTQIQGVPIQTPSTGTFNFDSLMDGGTGLTPVSGPLIPNCTSQNKHPLELPTPTTEPSKLVSL", "text": "FUNCTION: Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with Jra (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Fos subfamily."}
{"protein": "MVSKSDQLLIVVSILEGRHFPKRPKHMLIVEAKFDGEQLATDPVDHTDQPEFATELAWEIDRKALHQHRLQRTPIKLQCFALDPSTSARETIGYIVLDLRTAQETKQAPKWYQLLSNKYTKFKSEIQISIALETDTKAPVDSFKAKGAPPRDGKVPASLSGLDPKDIVAVLNEEGGYHQIGPAGYCTDFFIMSVTIAFATQLEQLIPCTMKLPERQPEFFFYYSLLGNDVTNEPFSDLINPNFEPERASVRIRSSIEILRVYLTLHSKLQIHLCCGDQSLGSTEIPLTGLLKKGSTEINHRPVTVEGAFTLDPPNRAKQKLAPIPVELAPTVGVSVALQREGMDVQSLIELKTQNEHEPHHSKKRVLTPIKENTHTGPQSPSESPVPPHNQSPPTKDDATESEVESLLYDKDTKLNPKAISSSVPALLAKPVTTSIASEAASGQKIAVPATSHHFCFSIDLRSIHDLEVGFPINCILRYSYPFFGSAAPIMTNPPVEVRKNMEVFLPQSYCAFDFATLPHQLQDTFLRIPLLVELWHKDKMSKDLLLGIARIQLSNILSSEKTRFLGSNGEQCWRQTFSESVPIVATQGSNNRIVDLSYTVTLEDYGLVKMREIFVSDSSQGLSAVQQKPSSVPPAPCPSEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYNILEGKLQKTLIDLEKREQQLAIAESELQRERRELKSERERNLQELQDSIRRAKEDCVHQVELERLKMKQLEEDKHRLQQQLNDAENKYKTLEKEFHQFKDQQSSKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYPDSREIASGKMDGPHGSALEEGLDDYLTRLIEERDTLMRTGVYNHEDRIISELDRQIREVLAKNNASN", "text": "FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors and for proper positioning of neurons during brain development. Also implicated in the migration and selfrenewal of neural progenitors. May play a role in centriole duplication during mitosis (By similarity). Required for the recruitment of CEP295 to the proximal end of new-born centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Regulates the localization of TACC3 to the centrosome in neural progenitors in vivo. SIMILARITY: Belongs to the CEP120 family."}
{"protein": "MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGSFPAGPLAVAGGPRKTAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAVLLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD", "text": "FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium- chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. May function as a modulator of the estrogen signaling pathway in the uterus. Induces the expression of PERM1 in the skeletal muscle (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Co-localizes to the cytoplasm only in presence of MAPK15. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily."}
{"protein": "MGFSDLLNPQNPESTPSTPANKSSAPSTPSTGQSNSNMTSVSLLPPLMKGARPANEEPRQDLPRPYKCPLCDRAFHRLEHQTRHIRTHTGEKPHACQFPGCTKRFSRSDELTRHSRIHNNPNSRRNNKAQHLAAAAAAAAANQDNALASNAASMMPPPSKPITRSAPVSQVGSPDISPPHSFSNYAGHMRSNLGPYARNSDRASSGMDINLLATAASQVERDEHYGFHNGPRGHHIFGSRHHNSNRLPSLSAYAISQNMSRSHSHDEDDMYSHRVKRSRPNSPNSTAPSSPTFSHDSLSPTPDHTPLATPAHSPRLRPLGTSELQLPSIRHLSLHHTPALAPMEPQPEGPNYYSPTQPHVGPSISDIMSKPDGTQRKLPVPQVPKVAVQDLLSPGFTSVSSSASNSVAGGDLADRF", "text": "FUNCTION: Transcription regulator component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Represses the transcription of the alcR, alcA and aldA genes by binding to a GC- rich region in their promoter. Also plays a role in response to carbon starvation and the control of extracellular proteases activity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein family."}
{"protein": "MQDLRNADTLRLPNGDGAAANDEVKSPFLIGVAGGTASGKSTVCKKIMEQLGQAEMDHTQRQVVSISQDSFYRELTPAEKAKAQKGLFNFDHPDAFNEELMYSTLQNILKGHKVEIPSYDYRTNSLDFENVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEILATTNSAQHSNTVRVAASSMKRDH", "text": "FUNCTION: (Microbial infection) Required for optimal replication of E.chaffeensis in the immune tissues, hemocytes, and fat body. SIMILARITY: Belongs to the uridine kinase family."}
{"protein": "MDTKMEDVGKTPEPIRFQTTTEPASISTLDGWIENLMACKQLPEVDVLRLCEKAREVLHSESNVQPVKCPVTVCGDIHGQFHDLMELFRIGGPNPDTNYLFMGDYVDRGYYSVETVTLLVALKIRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTNLFDFLPLTALIENQIFCLHGGLSPSIDTLDNIKSLDRIQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEAFNHNNGLTLVARAHQLVMEGYNWSQDRNVVTIFSAPNYCYRCGNQAAIMEIDEHLKYTFLQFDPCPRAGEPMVTRRTPDYFL", "text": "SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily."}
{"protein": "MNTTDRQITFSALSCLLSYPDEEWRAELPDWKALIQEIGNRQIREKLLHFFETSASYSPEALIEHYVYTFDFGKKTNMYVTYFNSGEQRERGIELLHLKNTYEQSGFLPTEKELPDYLPLMLEFAAAAEIEAARSVFEKYLSNVRELASRLEKNDSIYAELLHVLLAALENIGVRESVEGAVQA", "text": "FUNCTION: Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NarJ/NarW family."}
{"protein": "MQNHLSSTRRLGRRALLFPLCLVLYEFATYIGNDMIQPGMLSVVQTFGVDESWVPTSMTAYLAGGMFLQWLLGPLSDRIGRRPVMLIGTLYFAATCLAILLTNSIEQFTLMRFLQGISLCFIGAVGYAAIQESFEESVCIKITALMANVALIAPLLGPLAGAAWVHLFPWEGMFILFAALSLLAFLGLYKAMPETATRRGEKLSLSALGRDYTLVLKNRRFLCGSLACGFASLPLLAWIAQSPVIIISGEGLSSYDYGMLQVPIFGMLILGNLTLARLSGRRPVRRLIQLGAWPMVGGLAIAAASTLYSAHAYLWMTAGLSLYAFGIGLANAGLYRLTLFSSTMSKGTVSAAMGMISMFIYTLGIEVGKYAWLLGGNGAFNLFNLISGLLWLALIARMLRDQLVGRMAGR", "text": "FUNCTION: Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. MdfA family."}
{"protein": "MVHCAGCKRPILDRFLLNVLDRAWHVKCVQCCECKCNLTEKCFSREGKLYCKNDFFRCFGTKCAGCAQGISPSDLVRRARSKVFHLNCFTCMMCNKQLSTGEELYIIDENKFVCKEDYLSNSSVAKENSLHSATTGSDPSLSPDSQDPSQDDAKDSESANVSDKEAGSNENDDQNLGAKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLVDRLEPGELIPNGPFSFYGDYQSEYYGPGGNYDFFPQGPPSSQAQTPVDLPFVPSSGPSGTPLGGLEHPLPGHHPSSEAQRFTDILAHPPGDSPSPEPSLPGPLHSMSAEVFGPSPPFSSLSVNGGASYGNHLSHPPEMNEAAVW", "text": "FUNCTION: Potential transcription factor. May play a role in early mesoderm formation and later in lateral mesoderm differentiation and neurogenesis. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAFIKLLRKTKDEPSRLAKAVRHLQVTLDDPHATYRPRDVLFGQVLLDLKQNVANVRVRLTFIGEVKSKYGTAHKRGGCFMEKSTVLYGDDGDLDTDEMEPTVNGLTKGVHKFPFSIRVPSGKKIHSSIKFERGSVSYHLMAVFESVVEPEGVSAKVRTKVNILVPIDVYRYSDVVVKTILLNSNAKSKSHKINSNDHNGHLNGDVTTLTTSDGSSEGTKKTISESQIINNLSQRQVLQKSKSEGSKSESIQASTGQINQLPETSSQVSYNAVLTNGMNRDADNQTVKIDVRLPHSGFVQGEYIPLTINVSHYREYYHPAGVIATLVRVCKVASGRKEDTKEIYRKDICQSISPLLIESNKLENTISTYLKVPNDIIASMTSLPEHFTFQYFVEVVINLSRKLEIYSHSQKPLSYILEKQKTKKPLTIPRDLKELNLPASVNENGAWEVPRPSLNNEKSNGGIDSSRNDFQSKFGSAFNKSTLFGLKNIDEIHVAEQTIIFDDMVDVERLKRMRNVAGLSIETIIGNKRSSPAIDLAKLEISKLSQGKVMKSNGTSKNTSSSGSIESNSIVRYRYISFEQDTQSSTDSYDEDITKMGNQLNEWLSPANAYEEYYPVPEYSANENVFASEDKQELEYKRLHELESDPPQF", "text": "FUNCTION: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. SIMILARITY: Belongs to the arrestin family. PalF/RIM8 subfamily."}
{"protein": "MVSFVQLVVQIREIFEHKMVDVDEVMKLMGSYKSDINEWRRFAIFDMNKYTRNLVDIGNGKYNLMILCWGPGMASSVHDHTDAHCFVKILDGELTETKYDWPKKKHTPLETIENKTYGLNGVSYMNDELGLHRMENQSHSNGAVSLHLYIPPYSTCNAFDERTGKKTKCTVTFYSKYGEKIDYHGSKEGK", "text": "SIMILARITY: Belongs to the cysteine dioxygenase family."}
{"protein": "MSGPNRTYSFGEGDDSLAHPSSRTHAMHSQYDDVSPISDGARMNPMNGQGMDHGLASVLEDGRQGWGRSPEPSPSLLTGSSATPGMDNLGPGAVGGGISGIALSVANSHDRLSGVEALMGTDGQEANIPAERGLSTTGSDNPYVPEPPEHRYSYGSNIALGAAAAPAGQLTPGQSVSHLSSTNPSQRNLYDIPYQDVGGLNAGPYQRHSAYSSNDLPVDINPDEIVDDGDDGFVPAPNSGSGARKSQAIPAAAGGAAAGGVLGNLGGLFGGKSAADTSYGPVPGAGLEAGEKGRWVKPKPGGGNKKRGWIVGAILAFIIIGAIVGGAVGGTIGHRGNEEPSSASSASSSSTQTATEDTSVNGDLDKNSAEIKALMNNKNLHKVFPGIDYTPWGVQYPLCLKYPPSQNNVTRDMAVLTQLTNNVRLYGTDCNQTEMVLHAIDKLEIKDMKIWLGVWIDSNETTSRRQIDQLYKIIDDAKDISIFNGAIVGNEALYRAGSDKTSAQTTLINYMQEVKDHFKKKNIDLPVATSDLGDNWDATLVQAADVVMANVHPFFGGIPVDQAAAWTWRFWQDHNVALTKGTNKKQIISEVGWPSGGGNDCGQGANCPNDTAGAVAGVDELNKFMEDWVCQALDNGTDYFWFEAFDEPWKIVYNTGKENWEDKWGLMDSARNLKPGLKIPDCGGKTAT", "text": "FUNCTION: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
{"protein": "MGRMHSSGKGISSSALPYSRNAPSWFKLSSDDVVEQIIKYARKGLTPSQIGVILRDAHGVSQAKVVTGNKILRILKSNGLAPEIPEDLYYLIKKAVSVRKHLEKNRKDKDSKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVA", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MESFAYILILTLAIATLFFAIAFRDPPKIGK", "text": "FUNCTION: Seems to play a role in the dimerization of PSII. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbT family."}
{"protein": "MRNLILTAMLAMASLFGMAAQADDYTAGKEYVELSSPVPVSQPGKIEVVELFWYGCPHCYAFEPTIVPWSEKLPADVHFVRLPALFGGIWNVHGQMFLTLESMGVEHDVHNAVFEAIHKEHKKLATPEEMADFLAGKGVDKEKFLSTYNSFAIKGQMEKAKKLAMAYQVTGVPTMVVNGKYRFDIGSAGGPEETLKLADYLIEKERAAAKK", "text": "FUNCTION: Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily."}
{"protein": "MNEAKSLFTTFLILAFLLFLLYAFYEAAF", "text": "FUNCTION: Plays an essential role in the regulation of calcium transport at the sarcoplasmic reticulum (SR), which is secondarily required for regular muscle contraction. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Single-pass membrane protein Note=Colocalizes with SERCA at the sarcoplasmic reticulum and the diad, a structure composed of a single t-tubule paired with a terminal cisterna of the sarcoplasmic reticulum."}
{"protein": "MKATLLPSLLALSLTLCLALGLSSSGVLVRADAFASSQPPVVSDPVLASQHLTQANVALQSGRYQDALSAFDLALQADPSSWLTYYRRATAQLSLGRTSAALQDFQSLLKLNPKFDKAYLQQAKVYLKEGDCDKAKQALKTYDSIRAEKGAANSSPAEANSVRSKLTLVETSIKSLGQLVKELDKAQKADKKGKAKELDSTKVDHCIHLAGEVLKISPSHLETRLVRARCQTMKGRIEDAMADWTRAVHLTPSPFLLRRLSVLSYFVVSEPGSQSRDAGLQHLKACLHSDPDNKSCAKMHRKIKALEKSLKKARNFYNSQSYRAVLSALKGGKVGRATVVDDIKEAIRSATEVQSGDEEPLIPSTYKGDPVQESGLLLELHTMYCKAYTELNDMDKAMPYCELVLAKDPDNVEATLARAELALQREDYDQAVRDLTKAFDASGRTDRAIHQKLQTAQKRLKLSQSKDYYKVLGVKRTDSLATIKKAYRKMARENHPDKGGSQEKMAQINEAWGVLGDEELRKKYDQGDDPNDPMGGQQGGYGNPFAQGGHPFDMFFQQQAGFGGFPGGGFPGGQQFHFKMG", "text": "FUNCTION: Endoplasmic reticulum (ER) protein that functions as a co- chaperone for BIP1 during ER stress (PubMed:26487566). Might be specifically involved in the refolding of N-glycosylated proteins (PubMed:26487566). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "MAVNPELAPFTLSRGIPSFDDQALSTIIQLQDCIQQAIQQLNYSTAEFLAELLYAECSILDKSSVYWSDAVYLYALSLFLNKSYHTAFQISKEFKEYHLGIAYIFGRCALQLSQGVNEAILTLLSIINVFSSNSSNTRINMVLNSNLVHIPDLATLNCLLGNLYMKLDHSKEGAFYHSEALAINPYLWESYEAICKMRATVDLKRVFFDIAGKKSNSHNNNAASSFPSTSLSHFEPRSQPSLYSKTNKNGNNNINNNVNTLFQSSNSPPSTSASSFSSIQHFSRSQQQQANTSIRTCQNKNTQTPKNPAINSKTSSALPNNISMNLVSPSSKQPTISSLAKVYNRNKLLTTPPSKLLNNDRNHQNNNNNNNNNNNNNNNNNNNNNNNNIINKTTFKTPRNLYSSTGRLTTSKKNPRSLIISNSILTSDYSITLPEIMYNFALILRSSSQYNSFKAIRLFESQIPSHIKDTMPWCLVQLGKLHFEIINYDMSLKYFNRLKDLQPARVKDMEIFSTLLWHLHDKVKSSNLANGLMDTMPNKPETWCCIGNLLSLQKDHDAAIKAFEKATQLDPNFAYAYTLQGHEHSSNDSSDSAKTCYRKALACDPQHYNAYYGLGTSAMKLGQYEEALLYFEKARSINPVNVVLICCCGGSLEKLGYKEKALQYYELACHLQPTSSLSKYKMGQLLYSMTRYNVALQTFEELVKLVPDDATAHYLLGQTYRIVGRKKDAIKELTVAMNLDPKGNQVIIDELQKCHMQE", "text": "FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to- anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the APC3/CDC27 family."}
{"protein": "MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDTMRYVLRCNGSEEEKTLYLTPEQEKDKSHFIDKETGQEHELIESMPLLEWFANSYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQGMDYQGVDDEFFDLDDY", "text": "FUNCTION: Component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons (PubMed:7990965). The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (By similarity). ETF1/ERF1 is responsible for stop codon recognition and inducing hydrolysis of peptidyl-tRNA. Following GTP hydrolysis, eRF3 (GSPT1/ERF3A or GSPT2/ERF3B) dissociates, permitting ETF1/eRF1 to accommodate fully in the A-site, followed by hydrolysis of peptidyl-tRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family."}
{"protein": "MPNTQSPYNAFAMLLSSNGHPVTPAELHGLLIGRSCAGAGFDADAWLADAAQLLEIEPGDSVRNALVGLQEMVKGELTSDDMAIVLLLPTDDAALSDRATALGQWCQGFVTGFGLNAGGKDLSDEAKEVLQDLVAISQVQEALEESEDGESDYMEVMEYLRVAPLLLFSELAKPAAPAPKPSLH", "text": "SIMILARITY: Belongs to the UPF0149 family."}
{"protein": "MMFPGLLAPPAGYPSLLRPTPTLTLPQSLQSAFSGHSSFLVEDLIRISRPPTYLPRSIPTASLSPPRQEAPTALADSGTSDLGSPGSGSRRGSSPQTALSPASEPTFLKFGVNAILSSAPRRETSPALLQSPPPKTFAFPYFEGSFQPFIRSSYFPASSSVVPIPGTFSWPLAARGKPRRGMLRRAVFSDVQRKALEKTFQKQKYISKPDRKKLASKLGLKDSQVKIWFQNRRMKWRNSKERELLSSGGCREQTLPTKLNPHPDLSDVGQKGPGDEEEDSPGASLAYHAPPDPRHLLEGPLPASPAHSSSPGKPSDFSDSDEDEEGEEDEEITVS", "text": "FUNCTION: Could have a role in patterning the central nervous system during embryogenesis. Has a key role in regulating the distinct phenotypic features that distinguish two major classes of ventral interneurons, V0 and V1 neurons. Regulates the transcription factor profile, neurotransmitter phenotype, intraspinal migratory path and axonal trajectory of V0 neurons, features that differentiate them from an adjacent set of V1 neurons (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the H2.0 homeobox family."}
{"protein": "MRRFLLLYATQRGQAKAIAEEISEQALSHGFSADLHCVSESEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTDFFAHLWYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQHFYDTGHADDCVGLELVVEPWIDGLWPALTKHFKSLGGQEDMSDSDTLAQASDAPLSMAMKPELLHIQSQVELLSLEDVGKRDSELQEQNETNKNQPSRIEDFDSSLVNSVPPLSQSSLSIPAVSPEYLEVYLQESLGQDENQASVPPSVDPIFQVPISKAVELTTNDAIKTTLLLELDISKVEFSHQPGDSFNVICPNSGSEVEDLLQRLQLADKQAHRVILKIKMDTKKKGASLPQHVPEGSSLQFIFTWCLEIRAVPKKAFLRALSDYTSDATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQPPLNLLLEHLPKLQPRPYSCASSSLLHPDKLHFVFNIVELPSNTTAASLRKGVCTGWLATLVAPFLQPNTEVLTADHSDALAPEILISPRATNSFHLPDDLSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDAAPEEEEEAPAKYVQDNLQHHSQQVARTLLQENGYIYVCGDAKNMAKDVHDALVEIISKEAGVDKLEAMKTLATLKQEKRYLQDIWS", "text": "FUNCTION: Key enzyme in methionine and folate homeostasis responsible for the reactivation of methionine synthase (MTR/MS) activity by catalyzing the reductive methylation of MTR-bound cob(II)alamin. Cobalamin (vitamin B12) forms a complex with MTR to serve as an intermediary in methyl transfer reactions that cycles between MTR-bound methylcob(III)alamin and MTR bound-cob(I)alamin forms, and occasional oxidative escape of the cob(I)alamin intermediate during the catalytic cycle leads to the inactive cob(II)alamin species. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine (By similarity). Also necessary for the utilization of methyl groups from the folate cycle, thereby affecting transgenerational epigenetic inheritance (By similarity). Also acts as a molecular chaperone for methionine synthase by stabilizing apoMTR and incorporating methylcob(III)alamin into apoMTR to form the holoenzyme. Also serves as an aquacob(III)alamin reductase by reducing aquacob(III)alamin to cob(II)alamin; this reduction leads to stimulation of the conversion of apoMTR and aquacob(III)alamin to MTR holoenzyme (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MHMDYHSPYFFGYLLGLIHLLGVVAALHALFTVRTAQGAIAWAMPLFFIPYLTLIPYLIFGARSFYAYIKARRQANQEMHVAMANLNWRPWVEEALTARESESYAALRAMPKLGRMPCLANNQVKLLVNGKATFDAIFAAIEKARDVVLVQFFIIHDDTLGKALQQLLLRKAAEGVQVFVLYDRVGSHALPASYSQQLRNGGVQIHAFATRRGWFNRFQVNFRNHRKIVVVDGLLGFIGGHNVGDEYLGGHPQLSPWRDTHVQISGPVLACLQESFAEDWYWATRQLPPLILPDAYPDNGVLCQALASGPADPQETCSLFFLEAIHSATRRVWITSPYFIPDEAVFAALRLAVLRGVDVRVLIPSRPDHRIVYAASSLFAFEAVRAGVRMFRYQPGFLHQKVVLVDDEVSAIGSANLDNRSFRLNFEITLLTVDRNFADQVEHMLIKDFEQAREITAEDSRDTHRLQQLGMRIARLISPIL", "text": "FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsA sub-subfamily."}
{"protein": "MQFDSLPLPPSSSHDTTSVPPLKRHAACDECRKRKLKCSGEATGCSRCLKQSLPCHYSLQKPMGRPPKKRPREDNDASVYEITDNGMWADIDDGGILTEEAGAEATAASDALRLCPPVYTAPMRMPQAFPNLLSTDDSHNHLWQLESGRSLDPIPATTGPWPDFSSVTAATSSPFTLPSSLTLIDSPSVSSPSSDGGNSSQCTCLSYLYLCLSHLSSLAPFPISQHTLCSLFIAAKTARAVIRCEVCPTSFALGMQNVMFTGTLLNVIADAWLRVSQADAEELGKLAAPPAYVASVTQNSPNPAEAWKDWLRQTVRSAITGGPADPAGQVKCSDSPTLLSLIEEMEARQHRWHRTRTVESPNEPGSCSPVSHEDHREEDMLCFRVIRSARDVIAKFEFAPHEYPEGVVPV", "text": "FUNCTION: Transcription factor that is involved in protection against oxidative stress (PubMed:32667960). Binds to promoter regions of the gliotoxin (GT) biosynthetic genes gliZ, gliF, gliT, gliM, gliA and gtmA (PubMed:32667960). Two related but different DNA motifs (5'-TCGG-3' and 5'-CGGNCGG-3') are specifically enriched among rglT binding sites in GT-inducing conditions (PubMed:32667960). Also indirectly regulates the expression of gliP, gliG, gliH and gliN (PubMed:32667960). Plays a key role in resistance against exogenously-added GT and GT biosynthesis, mainly through the direct regulation of gliT (PubMed:32667960). Furthermore, rglT is important for virulence in chemotherapeutic mice with invasive pulmonary aspergillosis (IPA) (PubMed:32667960). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "YAPSALVLTIGQGATAAESGVQRAVTLTCTPKSSGTHPDAKGACTQLRAAGGDFDKVTRIKSDTVCTKEWNPTVVTAEGVWDGRRISYEHTFANPCMAKAGKGLVFEF", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I16 (SSI) family."}
{"protein": "MASASTSSSNESESQSVLTWEQVSRLNDVLTEAVPVHGRGNFPTLEVRLKDIVQMVRNRLELRGIMVKDVRLNGSTASHVLVQDIGWSYKDLDVIFRVDLPREEEFQLIKDVVLSTLLDFLPEGVNKEKITPMTLKEAYVQKLVKVYTDQDRWSLISLSNNNGRNVELKFVDSIRRQFEFSVDSFQIILDSVLSYYDLSENPMSQHFHPTVVGESMYGDFVEALGHLTNKTIATKRPEEIRGGGLLKYCNLLVREFKPTDPDEFKALERYMCSRFFIDFPDIVEQQRKLEAYLQSHFIGEERNKYNYLMILRRVVNESTVCLMGHERRQTLNLISLTAFRVLAEQNAIPDVSSVTCYYQPAPYVKDLNFNNYYVASCNQSIPTWLPCN", "text": "FUNCTION: Catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group and enhances mRNA stability and gene expression. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the TENT family."}
{"protein": "MAGKAAEERGLPKGATPQDTSGLQDRLFSSESDNSLYFTYSGQPNTLEVRDLNYQVDLASQVPWFEQLAQFKMPWTSPSCQNSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQYFTAIGYPCPRYSNPADFYVDLTSIDRRSREQELATREKAQSLAALFLEKVRDLDDFLWKAETKDLDEDTCVESSVTPLDTNCLPSPTKMPGAVQQFTTLIRRQISNDFRDLPTLLIHGAEACLMSMTIGFLYFGHGSIQLSFMDTAALLFMIGALIPFNVILDVISKCYSERAMLYYELEDGLYTTGPYFFAKILGELPEHCAYIIIYGMPTYWLANLRPGLQPFLLHFLLVWLVVFCCRIMALAAAALLPTFHMASFFSNALYNSFYLAGGFMINLSSLWTVPAWISKVSFLRWCFEGLMKIQFSRRTYKMPLGNLTIAVSGDKILSVMELDSYPLYAIYLIVIGLSGGFMVLYYVSLRFIKQKPSQDW", "text": "FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane. Plays an essential role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile (PubMed:11099417, PubMed:11452359, PubMed:27144356, PubMed:15054092). Required for normal sterol homeostasis (PubMed:11099417, PubMed:11452359, PubMed:15054092). The heterodimer with ABCG5 has ATPase activity (PubMed:16893193, PubMed:20210363, PubMed:27144356). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily."}
{"protein": "MAYLGVDTSRIAGTQPLEMLLVSSGSPDPHSTIIIDPRTGVSSWSYKGSELQGASTGLVEPLGHDGEHVVITTKERPLVHVLAVHPKDRFHQKCVLPGPVSAIVSDNSGHFVFMSIKRQLYCWLLSTGELLSVIDAHYQNITKIVISDDDSMIFTASKDGAVHGYLVTDLVSADRDHTVAPFRKWASHTLSISDLKITNGSNPRVLSAGADHIACLHSISMDSVILKASSDRPLTACAIDPAETRIFIGTEVGNIAQINLFQLAPEERDLLVQAGDEHNTKFRVLNGHSDEISRLAINTDGTLLASGDASGKYCIWEISSHQCLKVSTMRSVINTLRFIPFWKTISGGEHVAKFRPVWDLKREPTKCDRFAIEVSTEFNSDQKHWNDVIEETIDQLLLESGSKSSAQLQWDAEGPARNEAAKAEKAAENTIKNIITLGDDEDDAPEVGNQRRKSGKKNKKNRKNQKKNDFEAAVIEKKQVEPIVIDDEEEVNSSLQKKFDALKAENEKLKEINKQMYEFVAKEIVDSEK", "text": "FUNCTION: Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit (By similarity). Required for processing ITS2 sequences from rRNA intermediates during 26S rRNA maturation (PubMed:16876152). Required in the soma to promote normal proliferation and prevent germline tumor formation (PubMed:14973273). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat IPI3/WDR18 family."}
{"protein": "MTAPILVATLDTRGPAATLGTITRAVRAAEAAGFDAVLIDDRAAAGVQGRFETTTLTAALAAVTEHIGLITAPLPADQAPYHVSRITASLDHLAHGRTGWLASTDTTDPEGRTGELIDVVRGLWDSFDDDAFVHDRADGLYWRLPAVHQLDHQGRHFDVAGPLNVARPPQGHPVVAVTGPALAAAADLVLLDEAADAASVKQQAPHAKILLPLPGPAAELPADSPADGFTVALTGSDDPVLAALAARPGRPDRTAATTLRERLGLARPESRHALTTA", "text": "FUNCTION: Catalyzes the oxidation of the proline residue of pristinamycin IIB (PIIB) to pristinamycin IIA (PIIA)."}
{"protein": "YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY", "text": "FUNCTION: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle. SIMILARITY: Belongs to the NPY family."}
{"protein": "MGRGSGTFERLLDKATSQLLLETDWESILQICDLIRQGDTQAKYAVSSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKDLLKRQVEVNVRNKILYLIQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVMTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCFEQLNKKAEGKAASTTELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLALALSQSEAEEKERMRQKSAYTAYPKAEPTPVASSAPPASSLYSSPVNSSAPLAEDIDPELARYLNRNYWEKKQEEARKSPTPSAPVPLTEPTAQPGEGHAIPANVETSLPETDPQAVTAAGAAFSEQYQNGESEESHAQFLKALQNAVTTFVNRMKSNHVRGRSITNDSAVLSLFQSINTMHPQLLELLNQLDERRLYYEGLQDKLAQIRDARGALSALREEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQEYLEVQRQLAIQRLQEQEKERQMRLEQQKQTIQMRAQMPAFSLPYAQLQAMPAAGGVLYQPSGPASFAGTFSPAGSVEGSPMHTMYMSQPAPAASGPYPSMPAAAADPSMVSAYMYPAGAAGAQAAAQGPAGPTTSPAYSSYQPTPTQGYQTVASQAPQSLPAISQPPQSGTMGYMGSQSVSMGYQPYSMQNLMPTLPGQDAPLPPPQQPYISGQQPVYQQMAPSSGPPQQQPPVAQQPPAQGPPAQGSEAQLISFD", "text": "FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin- coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Early endosome membrane; Peripheral membrane protein; Cytoplasmic side Endosome, multivesicular body membrane; Peripheral membrane protein Note=Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments."}
{"protein": "MALLAIHSWRWAAAAVAFEKHKHSAVLTRSLVSICGSGLRWSSYQSGASGSARLSQTTESLRNSTQQRWEKNNSRQLLDASKVLQAWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKCGAQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKDKAMASPLQITPQTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMWHTQSTRIQNHDNLGWDAKKESLSKEEERKKLQEEIVNSVKGCGNCSC", "text": "FUNCTION: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP- dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (By similarity). Moreover, through a functional complex formed of ABCB7, FECH and ABCB10, also plays a role in the cellular iron homeostasis, mitochondrial function and heme biosynthesis (By similarity). In cardiomyocytes, regulates cellular iron homeostasis and cellular reactive oxygen species (ROS) levels through its interaction with COX4I1 (PubMed:31511561). May also play a role in hematopoiesis (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily."}
{"protein": "MSKITSSGVRENVHKLLEYSTETKKRNFLETVELQVGLKNYDPQRDKRFSGTLKLPQVPRPNMTICIFGDAFDVDRAKSLGVDAMSVDDLKKLNKNKKLIKKLAKKYNAFIASEVLIKQIPRLLGPTLSKAGKFPTPVSHNDDLYSKVTDVKSTIKFQLKKVLCLAVAVGNVDMEEDVLVNQIMMAANFLVSLLKKNWQNVGSLVIKSTMGPSFRIY", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL1 forms part of the L1 stalk, a mobile element that plays a role in evacuating the exit-site tRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL1 family."}
{"protein": "MATITKLDIIEYLSDKYHLSKQDTKNVVENFLEEIRLSLESGQDVKLSGFGNFELRDKSSRPGRNPKTGDVVPVSARRVVTFKPGQKLRARVEKTK", "text": "FUNCTION: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. FUNCTION: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. SIMILARITY: Belongs to the bacterial histone-like protein family. SIMILARITY: Belongs to the bacterial histone-like protein family."}
{"protein": "MKSEVLSVKEKIGYGMGDAASHIIFDNVMLYMMFFYTDIFGIPAGFVGTMFLVARALDAISDPCMGLLADRTRSRWGKFRPWVLFGALPFGIVCVLAYSTPDLSMNGKMIYAAITYTLLTLLYTVVNIPYCALGGVITNDPTQRISLQSWRFVLATAGGMLSTVLMMPLVNLIGGDNKPLGFQGGIAVLSVVAFMMLAFCFFTTKERVEAPPTTTSMREDLRDIWQNDQWRIVGLLTIFNILAVCVRGGAMMYYVTWILGTPEVFVAFLTTYCVGNLIGSALAKPLTDWKCKVTIFWWTNALLAVISLAMFFVPMQASITMFVFIFVIGVLHQLVTPIQWVMMSDTVDYGEWCNGKRLTGISFAGTLFVLKLGLAFGGALIGWMLAYGGYDAAEKAQNSATISIIIALFTIVPAICYLLSAIIAKRYYSLTTHNLKTVMEQLAQGKRRCQQQFTSQEVQN", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:galactoside symporter (TC 2.A.2) family."}
{"protein": "ISLEICXIFHDN", "text": "FUNCTION: Oxygen labile bacteriocin-like. Has antibacterial activity only against strictly anaerobic rumen bacteria. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MVTRTRPVAAMAVRSRSSSRTGTAYLLLVLCEVSWAQIFSFPFRRPETCDFNQYFDISALSCAPCGANQRRDALGTSCVCLPGYHMISNNGGPSIICKKCPENMKGVTKDGWDCISCPSGLTAEGKCHCPTGHILVERNVSGSLLAQATCELCDESENSFTKANALGTRCVRCEPTFVNTSRSCSCSEPHTLTGGLCFSNTGNFHQRVISTARYGELGMSLNSEWFAKYLQATAAACWTHANLTSCQALGNMCVMNMNSYDSTTLDACRLFHYIFESTAGLISVHSVPFWRQNLPWLFYGDQPGLAPQVLSTTPLPTNFSFKGQNQLKFVAASYDIRGNFIKWQPLEGGVLQLCPDTERRLDAAYAFGTTYQQNCEISLSKLLVDFSSPVFYDVYLEYTDEEQHRYLWPIPVLNLNLQHNKLFVNQDSSSSKWLLTRRIFLVDAVSGRENDLGNQPRVIRVATQISLSIRLVPNTKNGNIYTPLLTIAYSDIDIKNAHSQSAKISFSVKYEMNQGDASVHTDIALGVLGGLAVLSSLLKTAGWKRRVGSPMIDLQTVMKFLLYYAGDLANVFFIITVGTGLYWLIFFKAQKSVSVLLPMPVQEERFVTYVGCAFAMKALQFLHKFISQISIDIFFIDWERPKGKVLKAVEGEGGVRSATVPVSIWRTYFVANEWNEIQTVRKINPLFQVLTTLFFLEVVGFKNLALMDSSSSLSRNPSDYTAPYSRILRYAVATAIWLVIGIIQVVFFAAFYERFIEDKIRQFVDLCSMSNVSVFLLSHRCFGYYIHGRSVHGHADTNMEEMNMNLKREAENLCSQRGLVPNTDGQTFQIAVSSQMRQHYDRIHETLTRRNGPARLLSSSGSTFEQSIKAYHAMNKFLGSFIDHVHKEMDYFIKDKLLLERILGMEFMEPMEKSIFYNDEGHSFSSVLYYGNEATLLIFDLLFFCVVDLACQDFVLASFLTYLQQEIFRFIRNTVGQKNLATKTLVDERFLI", "text": "FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Is a key regulator of stereociliary bundle orientation (PubMed:26035863). Required for epithelial cell branching morphology (PubMed:26035863). Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (sftpc). Involved in the negative regulation of canonical Wnt signaling, and activation of the non-canonical cascade stimulated by WNT5A (PubMed:26035863). In non-canonical Wnt signaling, it may act as ROR2 coreceptor (PubMed:26035863). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme."}
{"protein": "MSAEREAAEAATVAAATEAGAETGTGAGEGAPSQPPTVEVASDPQPPPAPEASASASAPPLRCLVLTGFGGYDKVKLQSRPAVPPAPGPGQLTLRVRACGLNFADLMGRQGLYDRLPPLPVTPGMEGAGVVVAVGEGVGDRKAGDRVMVLNRSGMWQEEVTVPSAQTFLMPEAMTFEEAAALLVNYITAYMVLFDFGNLRPGHSVLVHMAAGGVGMAALQLCRTVENVTVFGTASASKHEVLKENGVTHPIDYHTTDYVDEIKKISPKGVDIVMDPLGGSDTAKGYHLLKPMGKVVTYGMANLLTGPKRNLMAMARTWWNQFSVTALQLLQANRAVCGFHLGYLDGEVELVNSVVTRLVALYNQGHIKPRIDSVWPFEKVADAMKQMQEKKNIGKVLLVPGPEKET", "text": "FUNCTION: Plays a part in calcium-regulated keratinocyte activation in epidermal repair mechanisms. Has no effect on cell proliferation (By similarity). Possesses ATPase activity. Negatively regulates mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2) (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane; Peripheral membrane protein. Note=The majority is localized in the cytoplasm a small amount is associated with mitochondria. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily."}
{"protein": "MSEEWVPKTQLGKLVASGQIKTMGEALRSKLPLKEYEIVDYLLPNLKDEVIDIKRAQRMTDSGRRMTYSITVVVGNGDGYVGLGIGRSKEAAPAIRKALINAKLNIMEIRRGCGSWECGCGRAHTLPFLVQGKSGSVRITLKPAPRGVGLAVGDVARTILSIAGIEDAWGFAAGHTKTTVNYALAVYNALKETSKVRINPGIVLSTPIYSGSVVNVSGHKD", "text": "FUNCTION: With S4 and S12 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS5 family."}
{"protein": "MLRIPVRKALVGLSKSPKGCVRTTATAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRKNPPKVLFLLGADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDDIEGANYFQQANELSKLVNQQLLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQAVEEPSIC", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:30879903, PubMed:31557978). Essential for catalysing the entry and efficient transfer of electrons within complex I (PubMed:31557978). Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (PubMed:30879903, PubMed:31557978). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
{"protein": "MTDCVFITGATSGFGRAAAHRFAAAGWSLVLTGRRLERLEALKEELQGRVPVHIIALDVRDSDVVDAAVAALPEGFTRVRTLLNNAGLALAPQSAQHTDRSDWHTMIDTNVTGLVNVTHALLPTLIDVGEGATIVNVGSIAGQWPYPGSHVYGASKAFVKQFSYNLRCDLLGTGVRVTDLAPGIAETEFTLVRTGGDQAASDALYRGTTALTAEDIAEQMFYIATLPPHVNFNRLEVMPTRQAWSAFAIDYDA", "text": "FUNCTION: Catalyzes the formation of isethionate from 2- sulfoacetaldehyde in the deaminative pathway of taurine. The enzyme is specific for NADPH; NADH is not a substrate. Responsible for most of the activity observed in taurine-grown cells. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MYGGDFDGNAAFAGGGFMPSQATTQAHESSSSLKNRDVRTLLPLTLKQLSSASTTGESNFSIDGVDIKTVVIVGRISRMENRITQVDFVVDDGTGWVDCVRWCHARQETEEMEAVKLGMYVRLHGHLKIFQGKRSVNVFSVRPVTDFNEIVHHFTECMYVHMYNTKLRGGSITQDTATPRPQMPYSTMPTPAKPYQTGPSNQFPNQFNDSMHGVKQTVLNYLNQPMHIVSEAGVHCDIIARELRIPLLQVKEALEQLSNDGCIYSTLDETCFKSTANA", "text": "FUNCTION: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions. Required fo cell division in meristems. Involved in the maintenance of transcriptional epigenetic gene silencing (TGS) at specific loci (including some transposons) by regulating histone H3 acetylation, 'Lys-4' and 'Lys-9' methylation (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Redistributes to discrete nuclear foci upon DNA damage. SIMILARITY: Belongs to the replication factor A protein 2 family."}
{"protein": "MSRPGEHRVVHTLRTQAPARRLYELVARVEDWPAVFEPTVHVQVLERGPGTERFRIWARVGGRVKTWTSRRTLDPDTLRVTFRQELTQPPIASMGGSWEFRGDGDGTEVVLTHDFAAVDEAALPGLREALDANSGKELAALVALAERRQPPEELVFTFEDTLRVPSGDDAYAFIERSDLWQERLPHVRKVTLTEEAAGTGPAETRDMTVQDMTMETVTTDGGTHTTRSIRLCVPARSIVYKQLVPPALLSGHCGAWTFGEDTVTARHTVAIDPARVEEVLGKGATVADARTHLREVLGANSRATLRHAAAAAGPAS", "text": "FUNCTION: Is needed for correct cyclization of the oligoketide leading to isochromanequinone formation."}
{"protein": "MEQVRNYYQILGVPRNATAEEIKKSFRKLARQYHPDVNPNDKTAEEKFKDINEAYDVLSDETKRRELDSRLFGRFRRPPTSRFSPNSNGGRSPNGTSVNGQVRTPTGRTGTRQPAQSWQDFSETRRTKVVSPARPVPRDVEANLTLPLEKAYRGGKERIRLEDGRSLEVEMPGGMGDGQRIRLKQQGINGGDLYLKINLSPHPLFTLQGTDIACQVPVTPSEAILGGAIEVMTIDGLVKMTVPAGLKNGQKLRLAKKGFPNNQGDRGDQLVEIRVEIPPEPSPEELELYRRIREKETFNPRQKFFDF", "text": "FUNCTION: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaJ family."}
{"protein": "MASGVKVDPSCKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKLVEDGKECRYAAVDVEVTVQRQGAEGTSTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASLGLESLFQVQASEMSDLDEKSVKSDLMSNQRI", "text": "FUNCTION: Depolymerizes growing actin filaments in muscle cells; required for the assembly of actin filaments into the functional contractile myofilament lattice of muscle. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
{"protein": "MATLSPLLLAALLWVPVGTLTCYGDSGQPVDWFVVYKLPAHSSPGDVAQSGLRYKYLDEESGGWRDGAGSINSSTGALGRSLLPLYRNTSQLAFLLYNDQPPKYRGSQHSSNRGHTKGVLLLDQEGGFWLIHSVPNFPPPSSSAAYSWPPSARTYGQTLICVSFPLTQFLNISRQLTYTYPMVYDYKLEGDFARKFPYLEEVVKGHHVLQEPWNSSVTLTSKAGASFQSFAKCGNFGDDLYSGWLAEALGSNLQVQFWQRSAGILPSNCSGVQHVLDVTQIAFPGPAGPNFNATEDHSKWCVAPERPWTCVGDMNRNKREEHRGGGTLCAQLPALWKAFKPLVKAWEPCEKENRAFSPRSPAKD", "text": "FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the DNase II family."}
{"protein": "MPQPQQLPGPNADIWDWQMRGLCRGVDSSMFFHPDGERGRARAQREMRAKEMCRSCPVIAQCRSHALAVGEPYGIWGGLSESERELLLKRGIRRSA", "text": "FUNCTION: A redox-sensitive transcriptional regulator. Maintains intracellular redox homeostasis by regulating catabolic metabolism and polyketide biosynthesis. Regulates expression of the redox buffer ergothioneine (ERG). In concert with myothiol (MSH), another redox buffer, responds to low pH leading to acid resistance. The apo- but not holo-form probably binds DNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the WhiB family."}
{"protein": "MAIVSSVPLASKSCLHKSLISSIHKLKPFCRTIPTLGMSRPGKYVMPSMSMSSPVSDDGVQRRTGGYHSNLWNDDIIQFLSTPYGEPAYRERGERLIDEVKNMFNSISMEDVEFSPLNDLIQRLWIVDSVERLGIDRHFKNEIKSTLDYVYSYWTQKGIGCGIESVVPDLNSTALGLRTLRLHGYPVSAEVLKHFQNQNGQFACSPSETEGEMRSIVNLYRASLIAFPGEKVMEEAEIFSTKYLKEALQKIPVSSLSREIGDVLEQDWHTNLPRLEARNYIDVFGQDTKDTKLYMKTEKLLELAKLEFNIFQSLQKTELDSLLRWWKDSGFPHITFSRHLHVEYYTLASCIAFEPQHSRFRLGFAKACHVITILDDMYDVFGTIDELELFTAQIKRWDPSATDCLPKYMKRMYMILYDMVNEMSREAETAQGRDTLNYARQAWEDFIDSYMQEAKWIATGYLPTFDEYFENGKVSSGHRVAALQPILTMDIPFPHDILKEVDFPSKLNDLASAILRLRGDTRCYKADRARGEEASCISCYMKDNPGATEEDALSHINAVISDVIKGLNWELLNPNSSVPISSKKHVFDVSRALHYGYKYRDGYSVSNIETKSLVMRTLLESVPF", "text": "FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-beta-phellandrene (PubMed:21385377). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily."}
{"protein": "MLILTRRVGETLIIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQAEKSQPTSY", "text": "FUNCTION: Controls extracellular enzymes, N-(3-oxohexanoyl)-L- homoserine lactone, and pathogenicity. Repressor of virulence factors. FUNCTION: A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family."}
{"protein": "MSSKKGSKTSKTSRSVKQTEEYYDDDAEFQNSEDEYPPSDEDLDNSGGSDDENTQSGGLSDAPDDELGEDSATLDIDPDDEAEYDTDGDEKFNPIDEMGEPEDPDDPSEQEEDEVEDLGSEDVDNVEIEDDAADIEDLDPELVDEARNSKSKQCYMKNLNKDFIALDEDDSGIYSKIEYKKIPDNERETDPILTYYEIVRILGTRAQQFNYGAKPLIKGVEGMHPAKMAFVELTAKMTSFIVRRHLPGKKYEDWRIDELGMIHTITEELFVPDNFNWDSITALHKTMISNQQKNSTTDTETLSTQENASTRVSGSNLRSRSGSKSSKSNNSRSASKSNSRTESKSNSRTGSKSNSRTGSKSNSRTGSKSKKSSNTKSKSKRNSDNSDDSDYSDYSE", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family."}
{"protein": "MILKQAILTLVLVNANLFAQEPPKTYSSTDKETRQGPPKPPMGKRWVLNPDFSDEFNGTELDTTKWLDHHPTWIGRAPGLFMSSQVSVGDGFLKMEGKKLEKDTIVHAYGKDITFNIAGAAVVSKKATKFGYYECRVKAAATTMSTTFWFSSSNNFKGPKDCDRYGLEWDIHESIGREGDFNGSYFASGMHSNAHFWYTDCNGKKYDHRAPQVKFEDAKLTSEDFNVYGGWWRDESTASYYYNNRPPKHQKFYDKVKKKPFDQPMYMRLVNETYPFPWIELPNAEELSDPSKNTVYYDWVRAYRLVDVNDPNSEVEKDPTLKLYHENVTFPSATIEHKRSKSLEIPLSYQANEDREIAFILFDNEGKKIKEAILTAYAGYANLEYTLQLDQKLPLGSPYKLSAHIRPLKGNKKNSLDESTVYIHLTK", "text": "FUNCTION: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6- sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6- sulfate-(1->3)-beta-D-galactose. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the glycosyl hydrolase 16 family."}
{"protein": "MEITNVMEYEKIAKEKLPKMVYDYYASGAEDQWTLQENRNAFSRILFRPRILIDVSKIDVSTTVLGFNISMPIMIAPTAMQKMAHPDGELATARATSAAGTIMTLSSWATCSVEEVASTGPGIRFFQLYVYKDRNVVIQLVKRAEEAGFKAIALTVDTPRLGRRESDIKNRFALPRGLTLKNFEGLDLGKIDKTNDSGLASYVAGQVDQSLSWKDIKWLQSITSLPILVKGVITAEDARIAVEYGAAGIIVSNHGARQLDYVPATIVALEEVVKAVEGRIPVFLDGGVRRGTDVFKALALGASGVFVGRPSLFSLAADGEAGVRKMLQMLRDEFELTMALSGCRSLREISRTHIKTDWDTPHYLSAKL", "text": "FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2. Is a key enzyme in photorespiration in green plants. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
{"protein": "MAERNEQLERLAYEYQLLQAQAQLLAQNLELLTLGRNEFQAVKQTLEELKKVEDEKPEILVPIGAGSFLKGMIVDKNSAIVSVGSGYATEKSLDDAIGYLDARIKEYDEAIRKTQEALAKLEGQLQELAQKAQKLQQEAAMRFSVKE", "text": "FUNCTION: Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin alpha subunit family."}
{"protein": "MTEKLNEIVVRKTKNVEDHVLDVIVLFNQGIDEVILKGTGREISKAVDVYNSLKDRLGDGVQLVNVQTGSEVRDRRRISYILLRLKRVY", "text": "FUNCTION: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Chromosome. SIMILARITY: Belongs to the histone-like Alba family."}
{"protein": "MHKDPSIIVNINLREAKLKKKVREHLQSLGFTRSDSGALQAPGNTKDVIRALHSSQRAERIFANQKFITLRAAKLIKFFASGNEVIPDKISPVLERVKSGTWQGDLFRLAALTWSVPVSSGFGRRLRYLVWDESNGKLIGLIAIGDPVFNLAVRDNLIGWDTHARSSRLVNLMDAYVLGALPPYNALLGGKLIACLLRSRDLYDDFAKVYGDTVGVISQKKKQARLLAITTTSSMGRSSVYNRLKLDGIQYLKSIGYTGGWGHFHIPDSLFIELRDYLRDMDHAYADHYMFGNGPNWRLRTTKAALNVLGFRDNLMKHGIQREVFISQLAENATSILQTGKGEPDLTSLLSAKEIAECAMARWMVPRSIRNPEYRLWKARDLFDFISNDSLKFPPSDEIAKTVV", "text": "FUNCTION: Component of antiviral defense system Druantia type I, composed of DruA, DruB, DruC, DruD and DruE. Expression of Druantia in E.coli (strain MG1655) confers resistance to phage lambda, SECphi18, SECphi27 and T4. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MPDLKTMMLNFGPQHPAAHGVLRLVLEMDGEVIERADPHIGLLHRGTEKLIEHKTYLQALPYFDRLDYVSPMSQEHAYSLCVEKLLQCEIPIRAKYLRVLFCELTRILNHLLNISSQALDVGAMTPLLWLFEEREKILEFYERASGARFHAAYIRPGGLAADIPEGLIEDIAKFIEQFPKYIDDVDELLTENRIWKQRTVGISEISIKQALDWGFSGPMLRAAGLAWDLRKSQPYEIYDQLDFDIPIGQNGDCYDRYLVRMAEIRQSVSLVKQCIEKMPEGPIKTEDRKISPPPRAEMKESMEAMIHHFKLYSEGYHVPEGEAYVAVEAPKGEFGVYIVSDGTNRPYRCRIRAPGFAHLQALDFMAKGHMLADIAAIIGSLDIVFGEIDR", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 49 kDa subunit family."}
{"protein": "MQINTIPVNPTLPRHIAIIMDGNGRWAERRSRPRTTGHRAGVKAAMRTVDFCLEKGIKMLTLFAFSSENWNRPADEVNFLMEMSIKLFGRGIEELHRRGVQVRFIGERKRFDIALVEHMTKAEHLTANNQRLILSLAVSYGGRQDITMAARALAQDVAAGRLKPEQIDEDLLGQHMALADLPPPDMFIRTSGVIRISNFLLWQIAYTELWFTDVMWPEFNSTVLQQALDDYASRERRFGLTNAQIASRGKGSIPA", "text": "FUNCTION: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di- trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. SIMILARITY: Belongs to the UPP synthase family."}
{"protein": "MRRLLLVTSLVVVLLWEAGAVPAPKVPIKMQVKHWPSEQDPEKAWGARVVEPPEKDDQLVVLFPVQKPKLLTTEEKPRGQGRGPILPGTKAWMETEDTLGHVLSPEPDHDSLYHPPPEEDQGEERPRLWVMPNHQVLLGPEEDQDHIYHPQ", "text": "FUNCTION: Lipid-binding protein which promotes lipid absorption by facilitating MTTP-mediated lipid transfer (mainly triglycerides and phospholipids) and MTTP-mediated apoB lipoprotein assembly and secretion (By similarity). Protects the gastrointestinal epithelium from irradiation-induced apoptosis (By similarity). May play an important role in maintaining normal growth homeostasis in epithelial cells (PubMed:14583459). Involved in p53/TP53-dependent cell survival after DNA damage (PubMed:23235459). May down-regulate the expression of MAD1L1 and exert a suppressive role in mitotic spindle assembly checkpoint in hepatocellular carcinomas (PubMed:24374861). SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum."}
{"protein": "MDVMNAFDSQAEDSPLSIGHSLRRRPLARKKLSEMVEEELEQMIRRHEFGEGEQLPSERELMAFFNVGRPSVREALAALKRKGLVQINNGERARVSRPSADTIISELSGMAKDFLSHPGGIAHFEQLRLFFESSLVRYAAEHATDEQIALLTKALEINSQSLDDNALFIRSDVEFHRVLAEIPGNPIFMAIHVALLDWLIAARPGVADRELHEHNNLSYQQHIAIVDAIRQRDPDKADRALQTHLNSVSATWHAFGKKNQKMR", "text": "FUNCTION: Transcriptional repressor that controls expression of the genes required for the catabolism of sialic acids. SIMILARITY: Belongs to the NanR family."}
{"protein": "MSDGPETAEGDTDDAVQDAAVNSRVASESSARSQPRATVVGCLPPTPFAIHTTPAPSEHSKEKNVSRRLPTEKTPSRLATPQFPPTPVSSRGSIAEPSAYPSITQALRSCLPPQKDIEILLSNLSSMSIFCYKSSFKLCSSWPSEMTEEQIPIANLLYSETHPVLLARHMLLFAVGLQHLSPTKAIPGLTRHHRAIMEQLADSAIKLVNTDDVLLGTLEGLENLILESFYHIDGGNIRRAWITMRRAVMTAQLLGLHRPGHYRFKTVNKQNDLDPAVMWACIVSTEQFLCLLLGLPTSTSGASFTIPRATSACVESGNLPVLIPDVVRKIIERNQTHVPQEALDMTQKIDHELLGVVKQWPPAFWRPLQLSGLEVDSADAFWETRRAWDHIFYYSLVNQLHLPYMLNPSHVSQKVYSRIACASASREILIRQIAIRTFNPVTAGCRMGDFVALIAGMTLMLAHILSHCSKGTENLLVHQRVGDRATVERALECMESMSEQHEDILTAKCAALLKNLLDIEAGPAEARSDDGQKDDQNVLVVKVPHVGAIKIARDGISITPFDTEQEQVSHDGVTIGGFGSIHVSTPHDSDRDGDHQADVVTPNDTASQATTQVVRPASARKQWRPVSQRSSGDVFTLPEETFPDASAGMEEWLFQGLDTAFFDVLISGAGEQPLNSTDTEGWNFVMSP", "text": "FUNCTION: Probable transcription factor that regulates expression of the gene cluster that mediates the biosynthesis of Griseofulvin, an important antifungal drug that has been in use for a long time for treating dermatophyte infections (PubMed:20534346). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSAADKKPLIPPSHITIKIKSQDDICVYFRIKRDVELRTMMQAYSDKVGQQMSAFRFHCDGIRIKPNQTPNELDLEDGDEIDAFVDQIAGFSHRH", "text": "FUNCTION: Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily."}
{"protein": "MDAFATSPTTALFETVNCNAHVAPMAGEDSSENRPASNYKPSTWDYEFLQSLATTNNTVGEKHTRMADKLKEEVKSMMKGTMEPVAKLELINIVQRLGLKYRFESEIKEELFSLYKDGTDAWWVGNLHATALRFRLLRENGIFVPQDVFETFKDKSGEFKSQLCKDVRGLLSLYEASYLGWEGEELLDEAKKFSTTNLNNVKESISSNTLGRLVKHALNLPLHWSAARYEARWFIDEYEREENVIPNLLKYAKLDFNVVQSIHQKELGNLARWWVETGLDKLGFVRNTLMQNFMWGCAMAFEPQYGKVRDAAVKLGSLITMVDDVYDVYGTLEELEIFTDIVDRWDINGIDKLPRNISMIVLTMFNTANQISYDLLRDRGFNSIPHIAEAWATLCKTYLKEAKWYHSGYKPTLEEYLENGLVSISFVLSLVTAYLQTERLENLTYESAAYVNSVPPLVRYSGLLNRLYNDLGTSSAEIARGDTLKSIQCYMTQTGATEEVAREHIKGLVHEAWKGMNRCLFEQTPLAEPFVGFNVNTVRGSQFFYQHGDGYAVTESWTKDLSLSVLIHPIPLNEED", "text": "FUNCTION: Produces a mixture of beta-bisabolene and alpha-bisabolol, along with traces of alpha-bisabolene and farnesene isomers from (2E,6E)-farnesyl diphosphate in fragrance biosynthesis. SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily."}
{"protein": "MVPVLHSLSTIILIAEFVWGNLSNGLIVLKNCIDWINKKELSTVDQILIVLAISRISLIWETLIIWVKDQLISSITIEELKIIVFSFILSSHFSLWLATALSIFYLFRIPNCYWQIFLYLKWRIKQLIVHMLLGSLVFLVANMIQITITLEERFYQYGGNTSVNSMETEFSILIELMLFNMTMFSIIPFSLALISFLLLIFSLWKHLQKMPLNSRGDRDPSATAHRNALRILVSFLLLYTIYFLSLLISWVAQKNQSELVHIICMITSLVYPSFHSYILILGNYKLKQTSLWVMRQLGCRMKRQNTPTT", "text": "FUNCTION: Putative taste receptor which may play a role in the perception of bitterness. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor T2R family."}
{"protein": "MNIIRKLKPGTISLVLGPMFAGKTTFLIHCIYMLERLEKKVVFIKSTKNTRDKTIKTHSGIQLRPKQCKIIESTQLSDVGSLTDIHAVVVDEAHFFDDLIKCRTWAEEEKIIILAGLNASFEQKMFPPIVRIFPYCSWVKYIGRTCMKCNQHNACFNVRKNADKTLILAGGSELYVTCCNNCLKNTFIKQLQPIKY", "text": "FUNCTION: Phosphorylates thymidine. ASFV replicates in the cytoplasm of infected cells and contains genes encoding a number of enzymes needed for DNA synthesis, including thymidine kinase. Important for growth in swine macrophages in vitro and is a virus virulence factor in swine (By similarity). SIMILARITY: Belongs to the thymidine kinase family."}
{"protein": "MAATAELIPAGEVIACHTVEDWNNKLKAAKESNKLIVIDFTAVWCPPCRFIAPIFVELAKKHLDVVFFKVDVDELATVAKEFDVQAMPTFVYMKGEEKLDKVVGAAKEEIEAKLLKHSQVAAA", "text": "FUNCTION: Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily."}
{"protein": "MAMSSLWWTAILLLALTVSMCYGVPTYQDFLRTHVDFPKTSFPNIAAYCNVMMVRRGINVHGRCKSLNTFVHTDPRNLNTLCINQPNRALRTTQQQLPVTDCKLIRSHPTCSYTGNQFNHRVRVGCWGGLPVHLDGTFP", "text": "FUNCTION: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen Secreted Nucleus, nucleolus Note=Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (By similarity). SIMILARITY: Belongs to the pancreatic ribonuclease family."}
{"protein": "MGDRERNKKRLLELLQAAGTGNGHCADCGAADPDWASYKLGIFICLHCSGVHRNFPDISKVKSVRLDFWDDSMVEFMTHHGNLNVKAKFEARVPAFYYVPQANDCLVLKEQWIRAKYERQEFTAIDKAVSHPGNREGFLWKRGRDNAQFLRRRFVLLSREGLLKYYTKEEGKAPKAVISIKDLNATFQTEKIGHPHGLQITYRKEGHTRNLFVYHDSGKEIVDWFNALRAARLQYLKLAFPDLPESELVPLITRNYLKQGFMEKTGPKHREPFKKRWFALDPQERRLLYYKNPLDAFELGQVFLGSNEQGYEVWEDLPKGIRGNRWKAGLTVITPERKFIFTCPTEKEQREWLESLRGVLSSPLSPLHLLTTSAETGCGLG", "text": "FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Possesses a stoichiometry of two binding sites for InsP4 with identical affinity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Constitutively associated with the plasma membrane. Excluded from the nucleus (By similarity)."}
{"protein": "MSEPHFKVIIVGGSITGLTLAHSLHKIGVDFTILEKRATVTPQEGASVGILPNGARVLDQLGLYGLVEEATAPLGATHIHFPDGFHFCSLYPKSMLDNFGYPVAFLERRRLLEVLYNALPDKSKVLVNKTVSDIEQCEDGKSAGVKVRTADGDVYEGDIVVGADGVHSRTRSELWRMSSSAGQSEDVRMEKARMSAEYSCVFGISRGPSGLKAGEQIMRMYDGRTLVVIPSKDDVVFWFLSRKLGKKYKYSEAPRFTLEDAAAECAELADAPLGNDVRFGDVWKIRQTFNMVVLEENLLRTWSFGRVLCIGDSIHKMTVNLGQGANCAIEDVAILTNLLSQCLGSKREAKPSGQELDALLRRFNDVHLSRVSHIYDTSWLIARVHARDGFVRKIIGRYVMPYFGHKFESRPFNMIANAAALEFLPLPRSSFPGWEKYKSKEDKSGSWAVVSRSVLLLVGLAILSTWWRRA", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B (PubMed:32286350). The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B (PubMed:32286350). Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A (PubMed:32286350). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
{"protein": "GFIGWGNNIFGHYSGDF", "text": "FUNCTION: Competitive antagonist of atrial natriuretic peptide NPR-A receptors. It binds competitively to atrial natriuretic peptide (ANP) receptors from bovine adrenal cortex and inhibits the ANP-induced intracellular cGMP accumulation in bovine aorta smooth muscle cells. Can also reduce the increase in cGMP produced by ANP or BNP (brain natriuretic peptide) in pregnant guinea pig myometrium, but has no effect on relaxation induced by either peptide. Blocks the ANP-induced human sperm acrosome reaction without affecting the acrosomal exocytosis or sperm motility. Also exhibits major and deleterious nonspecific (and even cytotoxic) effects on human fat cells, as it displays noncompetitive antagonism and exerts an inhibitory action on basal and beta-adrenergic receptor-induced lipolytic response. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MEPTRDNPLFGGAFSATLPPGAIDVSDLRPVPDHQEVFCHRVTDQSLIVELLELQAHVQGEEAARYHFEDVGGVQEARAVQVETVQPLVLEKLALRGCCQEAWILSGQQQVAKENQQVAKYVTLHQALLRLPQYQTDLLLTFNQPPPENRSSLGPENLSIPPWSLGDFEQLVTSLTLHDPNIFGPE", "text": "FUNCTION: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1. Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics. Enhances the expression of SCN5A at the cell membrane in cardiomyocytes. SUBCELLULAR LOCATION: Nucleus Cytoplasm, perinuclear region Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=May shuttle between the nucleus and cytoplasm. SIMILARITY: Belongs to the MOG1 family."}
{"protein": "MAGPQALAFGLLLAVVTATLAAAQRDCVCDNYKLATSCSLNEYGECQCTSYGTQNTVICSKLASKCLAMKAEMTHSKSGRRIKPEGAIQNNDGLYDPDCDEQGLFKAKQCNGTATCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKERESPYDHQSLQTALQEAFTSRYKLNQKFIKNIMYENNVITIDLMQNSSQKTQDDVDIADVAYYFEKDVKGESLFHSSKSMDLRVNGEPLDLDPGQTLIYYVDEKAPEFSMQGLTAGIIAVIVVVSLAVIAGIVVLVISTRKKSAKYEKAEIKEMGEIHRELNA", "text": "FUNCTION: May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity). SUBCELLULAR LOCATION: Lateral cell membrane; Single-pass type I membrane protein Cell junction, tight junction Note=Colocalizes with CLDN7 at the lateral cell membrane and tight junction. SIMILARITY: Belongs to the EPCAM family."}
{"protein": "MRTTSPYSHCSHVEMNAGAFVTMLLVALSVCVAAAVDPDVIQPFPQPKPTTIAQKAAVKYKPLLYTSMVVCVPYAAVDAAGRVTDGLKGRHGNDGCTYARHGSQVYGRVEPYGNLSAIMYAWYFPKRFWLGFPIQRHDWKSVVVWIDNLESKVSAIVAVSMAKSDTKYNTETELDANDFARLQVDNQIVISNTSLRFEFFEFGLRSSYLRLTGYNGQYQNLIMWDQLTDAAREALNDDNNFGSAVVPLSDKQFKAHVKEAYPSKSVR", "text": "FUNCTION: Probable secreted effector that may act as a pathogen- associated molecular pattern (PAMP) recognized by the plant immune system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Necrosis inducing protein (NPP1) family."}
{"protein": "MSGKIPKYFITELLSRTNIIELINTRLELKKYGKNYQTNCPFHHDKTPSFTVSNEKQFYYCFGCNAHGNAIDFLIQYEHLSFIESIEELALIHGVKIPFENTVQNSIYVKKQKLYLLMEKICKLYKKNINVTHLANKYLARRGINQNMIDFFLIGFSSLKWNEFYKKINISKEFEQELLINNIIATDKNGYIYDRFQGRIIFPIQDNHGRIIGFGGRSLNDMSPKYLNSPETDIFYKRKQIYGLYQVIKKCSKPVYLLVVEGYIDVITLTQYNIDYAVSILGTSTTTEHIQLLFKNTDIIICCYDGDDAGKNAAWKTLKKALPYISDKKTLKFILLPNQEDPDTIIRKEGREKFQKRIDNAITMSKFFFKNILKNINLSSDDDKFHLSVHALPLINTISSDTIRIYLRQILARMIGILDDNQFEKFLYEKETKNTQKTYFQIKRTPMRTLIGLLVQNPSLAKLVPVTMKFKNLQIKGLSIFLEILQTCRDNPNIHTGQLLELYRNTTIINVLKILARWDHMIIQKETQNMFLDLLMNIHDKILEKRREYLIAKERKKGLQMNEKKEIWSINKKLSKR", "text": "FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. SIMILARITY: Belongs to the DnaG primase family."}
{"protein": "MATSGVEKSSKKKTEKKLAAREEAKLLAGFMGVMNNMRKQRTLCDVILTVQERKIPAHRVVLAAASHFFNLMFTTNMLESKSFEVELKDAEPDIIEQLVEFAYTARISVNSNNVQSLLDAANQYQIEPVKKMCVDFLKEQVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLSQDTLTVRAEDQVYDAAVRWLKYDEPNRQPFMVDILAKVRFPLISKNFLSKTVQAEPLIQDNPECLKMVISGMRYHLLSPEDREELAGGTRPRRKKHDYRIALFGGSQPQSCRYFNPKDYSWTDIRCPFEKRRDAACVFWDNVVYILGGSQLFPIKRMDCYNVVKDSWYSKLGPPTPRDSLAACAAEGKIYTSGGSEVGNSALYLFECYDTRTESWHTKPSMLTQRCSHGMVEANGLIYVCGGSLGNNVSGRVLSSCEVYDPATETWTELCSMIEPRKNHGLVFVKDKIFAVGGQNGLGGLDNVEYYDIKLNEWKMVSPMPWRGVTVKCAAVGSVIYVLAGFQGVGRLGHILEYNTETDKWIANSKVRAFPVTSCLICVVDTCGANEETLET", "text": "FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL7) complex acts by mediating ubiquitination and subsequent degradation of substrate proteins. Probably mediates 'Lys-48'-linked ubiquitination (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Colocalizes with CUL3 in punctate structures at the perinuclear region of the cytoplasm."}
{"protein": "MKEKSKNAAKTRREKENGEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMRAVFPEGLGDAWGQPSRAGPLDGVAKELGSHLLQTLDGFVFVVASDGKIMYISETASVHLGLSQVELTGNSIYEYIHPSDHDEMTAVLTAHQPLHHHLLQEYEIERSFFLRMKCVLAKRNAGLTCSGYKVIHCSGYLKIRQYMLDMSLYDSCYQIVGLVAVGQSLPPSAITEIKLYSNMFMFRASLDLKLIFLDSRVTEVTGYEPQDLIEKTLYHHVHGCDVFHLRYAHHLLLVKGQVTTKYYRLLSKRGGWVWVQSYATVVHNSRSSRPHCIVSVNYVLTEIEYKELQLSLEQVSTAKSQDSWRTALSTSQETRKLVKPKNTKMKTKLRTNPYPPQQYSSFQMDKLECGQLGNWRASPPASAAAPPELQPHSESSDLLYTPSYSLPFSYHYGHFPLDSHVFSSKKPMLPAKFGQPQGSPCEVARFFLSTLPASGECQWHYANPLVPSSSSPAKNPPEPPANTARHSLVPSYEAPAAAVRRFGEDTAPPSFPSCGHYREEPALGPAKAARQAARDGARLALARAAPECCAPPTPEAPGAPAQLPFVLLNYHRVLARRGPLGGAAPAASGLACAPGGPEAATGALRLRHPSPAATSPPGAPLPHYLGASVIITNGR", "text": "FUNCTION: Transcription factor that may be a master gene of CNS development in cooperation with Arnt. It may have pleiotropic effects in the tissues expressed during development. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAAELKSLLGKDVLFLKDCVGSEVENACANPAAGTVILLENLRFHVEEEGKGKDASGNKVKAEPAKIDAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLYDEEGAKIVKDLMAKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGTESSKKYAEAVARAKQIVWNGPVGVFEWEAFARGTKSLMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNV", "text": "FUNCTION: Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoglycerate kinase family."}
{"protein": "MFPPSGSTGLIPPSHFQARPLSTLPRMAPTWLSDIPLVQPPGHQDVSERRLDTQRPQVTMWERDVSSDRQEPGRRGRSWGLEGSQALSQQAEVIARQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELEALARAEKAGRAEAEGLRAALAGAEVVRKNLEEGSQRELEEVQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLSSLETRRAGEAKELAEAQREAELLRKQLSKTQEDLEAQVTLVENLRKYVGEQVPSEVHSQTWELERQKLLETMQHLQEDRDSLQATVELLQVRVQSLTHILALQEEELTRKVQPSDSLEPEFTRKCQSLLNRWREKVFALMVQLKAQELEHSDSVKQLKGQVASLQEKVTSQSQEQAILQRSLQDKAAEVEVERMGAKGLQLELSRAQEARRRWQQQTASAEEQLRLVVNAVSSSQIWLETTMAKVEEAAAQLPSLNNRLSYAVRKVHTIRGLIARKLALAQLRQESCPLPPPVADVSLELQQLREERNRLDAELQLSARLIQQEVGRAREQGEAERQQLSKVAQQLEQELQQTQESLASLGLQLEVARQGQQESTEEAASLRQELTQQQELYGQALQEKVAEVETRLREQLSDTERRLNEARREHAKAVVSLRQIQRRAAQEKERSQELRRLQEEARKEEGQRLARRLQELERDKNLMLATLQQEGLLSRYKQQRLLTVLPSLLDKKKSVVSSPRPPECSASAPIAAAVPTRESIKGSLSVLLDDLQGLSEAISKEEAVCQGDNLDRCSSSNPQMSS", "text": "FUNCTION: May be a regulator of keratinocyte proliferation or differentiation. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFSP", "text": "FUNCTION: Accepts the ubiquitin-like proteins sumo1, sumo2 and sumo3 from the uble1a-uble1b E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as ranbp2 or cbx4. Essential for nuclear architecture and chromosome segregation (By similarity). Mediates nuclear localization of vsx1. Required for progression through mitosis during organogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MTDTPETLSGTECNGDRPPENGQQPSSQTRQETTDADETQAYYKVEPSLEDLPAKENQEETGNTKGNILPKGPEDEKILNENPEENLFVVHQAIKDLSLQEISAEDMAFREGHPWKKIPPNSSNLEVSRQKERTAQQQLEQRGDASTTEIEWLGFQKSRPVDILHSKCDEEEEEEEEVWNEEINEEDVDECAEEEDEVRVIEFKRKHREGSPLKEESLAREDSPLGSPGSQPGTPDEQPVFGKKGDIARNSYSRYNTISYRKIRKGNTKQRIDEFESMMHL", "text": "FUNCTION: Plays a role in cytoskeletal rearrangements during the late wrapping and/or compaction phases of myelinogenesis as well as in maintenance and stability of myelin sheath in the adult. May play an important role in late-stage oligodendroglia maturation, myelin/Ranvier node formation during CNS development, and in the maintenance and plasticity of related structures in the mature CNS (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton."}
{"protein": "MILLPFHTRRLVSHVYCGLKPASQNKGIALEMTRPSSNLANFREAFAKAKHIAVITGAGVSAESGVPTIIGAGGYWRKWQAQHLATPEAFSRNPSRVWEFYHYRREVMLTKNPNPAHLAIAECETRLRKQGRKVVVITQNIDELHHKAGSRNLFEIHGSLFKTRCTSCGSVKENYKSPICSALAGKGAPESDVQDAKIPVEKLPRCEENGCNGLLRPNVVWFGETLDSNLLGEVEKELEMCDLCVVVGTSSVVYPAAMFAPQVAARGVPVAEFNMENTSATTTFKFHFQGPCGTTLPPALARHETELIS", "text": "FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. SUBCELLULAR LOCATION: Mitochondrion Cytoplasm, cytosol Nucleus Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus. SIMILARITY: Belongs to the sirtuin family. Class III subfamily."}
{"protein": "MIEKRKDRIVKRLNISISEETYETLQRLKAKTGKTMGQLIEEAVKLLEAEE", "text": "FUNCTION: This protein is non-essential for virus function."}
{"protein": "MGIQPSPVLLASLGVGLLTLLGLALGTYLVRRSRRPQVTLQDPDEKYLLRLLDKTTVSHNTRRFRFALPTAHHILGLPVGKHVYLSARIDGSLVIRPYTPVTSDEDQGYVDLVIKVYLKGVHPKFPEGGKMSQYLDSLKIGDMVEFRGPSGLLSYAGKGNFNIQPNKKSPPELRVAKKLGMIAGGTGITPMLQLIRAILKVPEDPTQCFLLFANQTERDIILREDLEELQAQYPNRFKLWFTLDSPPEDWTYSKGFVTADMIQEHLPAPAEDVLLLLCGPPPMVQLACHPNLDKLGYSQKMRFTY", "text": "FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family."}
{"protein": "MATMQLQRTASLSALVFPNKISTEHQSLMFVKRLLAVSVSCITYLRGIFPERAYGTRYLDDLCVKILKEDKNCPGSSQLVKWMLGCYDALQKKYLRMIILAVYTNPGDPQTISECYQFKFKYTKNGPIMDFISKNQNNKSSTTSADTKKASILLIRKIYVLMQNLGPLPNDVCLTMKLFYYDEVTPPDYQPPGFKDGDCEGVIFDGDPTYLNVGEVPTPFHTFRLKVTTEKERMENIDSTILKPKESKTQFEKILMDKDDVEDENHNNFDIKTKMNEQNENSGASEIKEPNLDCKEEETMQFKKSQSPSISHCQVEQLVSKTSELDVSESKTRSGKIFQSKMVNGNNQQGQTSKENRKRSLRQFRKTVLHVLESSQESVLKKRRVSEPKEHT", "text": "FUNCTION: Plays a key role in meiotic progression (PubMed:19686734, PubMed:21079677, PubMed:21478856). Regulates 3 different functions during meiosis: ensures that sufficient numbers of processed DNA double-strand breaks (DSBs) are available for successful homology search by increasing the steady-state numbers of single-stranded DSB ends (PubMed:19686734, PubMed:21079677). Promotes synaptonemal-complex formation independently of its role in homology search (PubMed:19686734, PubMed:21079677). Plays a key role in the male mid- pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes (PubMed:21478856). SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus Chromosome Note=Preferentially localizes to unsynapsed or desynapsed chromosomal regions during the prophase I stage of meiosis (PubMed:19851446, PubMed:19686734, PubMed:27723721). Accumulates on the chromosomes during the leptotene to zygotene stages of meiotic prophase I (PubMed:19851446, PubMed:19686734, PubMed:27723721). As germ cells progress into the pachytene stage, disappears from the synapsed chromosomal regions (PubMed:19851446, PubMed:19686734, PubMed:27723721). Once the chromosomes desynapse during the diplotene stage, it again accumulates on the chromosome axis of the desynapsed homologs (PubMed:19851446, PubMed:19686734, PubMed:27723721). TRIP13 is required for depletion from synapsed chromosomes (PubMed:19851446). The expression of the phosphorylated form at Ser-375 is restricted to unsynapsed chromosomal regions (PubMed:22346761)."}
{"protein": "MLEAECDEVELTSRDVGDYLMFKTRITDNFTGDLTLNINTSNLIKFKTCSFFICYGDDKDRYELGWTSTSTSRSIFQHYKDGKYIRDFRIQDPFPILSGSTFPVVISKIIANRVAFRMSRRLNNVIVDKLKNNIIEFLFVVYLDVDTGKIKPNTILKNLDLSSLFIVFSNNGNNKINLPYEIELQTKDRGIVYTKMGNPISYNLFNKFEDLLDIETKGVDKPEDKPKPVFDDKGKQPTDTVPPVDNGKPDISKPGEKQGDIDIASKFNNIVMAKLKAQSSSDPLTKKQCDQLMLSLIKWFEKFGITKDNARLLIFQFGISFSTSKENLNNITNNIVVENDKGGFVKILKIDYLNKLYGSIPESHTHNLERVLLRHYAQEILILLRSKVLEWPRKLARNKGIFEQYAYMACDFFDTAELELTEAETTALTTVKSWTMNHYKKKRQIVNSSQLE", "text": "FUNCTION: Minor capsid protein that encapsidates the 5'-terminal portion of the viral genome. SUBCELLULAR LOCATION: Virion Note=Integral virion tail component. SIMILARITY: Belongs to the closteroviridae minor capsid protein family."}
{"protein": "MATRVQPSVKVLGASFSQEANPFTAAVELTPMPMLITNPRLPDNPIIFANEAFQNLTGYEADEIIGKNCRFLQGPGTDPKHVEIIHSALEAEQSVEIDILNYKKSGEPFWNRLHISPVKTENGELHHFVSSQLDVTLELGKLVELEKERETLSIEKQRSSDQLQYIVEVANVGFWTRDYTTGEISCSAEYRRIFGLTPDEPVNYDKIIDMVVLEDRITLIQRSQESFATGKSFRVEYRITNRLGQVRWVETRAKALLGKSPALLGIVIDVTERKKAEADKALVTREISHRFKNSMAMVQSIANQTLRNATDPQTANELFSERLRALSQAHDMLLREDWTGTTISQICETALAPFNSTFGHRIRTSGPELVVSDRVTVSLSLGLYELATNAVKYGALSNENGTVQFSWDVLERQGERKFHMRWVEDGGPAVERPTRRGFGQRLLYSVLTGELRAKCDINFAPDGLVIDVLAPMTADVFPQLDSLSDTQAEPV", "text": "FUNCTION: Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light."}
{"protein": "MEANQCPLVVEPSYPDLVINVGEVTLGEENRKKLQKIQRDQEKERVMRAACALLNSGGGVIRMAKKVEHPVEMGLDLEQSLRELIQSSDLQAFFETKQQGRCFYIFVKSWSSGPFPEDRSVKPRLCSLSSSLYRRSETSVRSMDSREAFCFLKTKRKPKILEEGPFHKIHKGVYQELPNSDPADPNSDPADLIFQKDYLEYGEILPFPESQLVEFKQFSTKHFQEYVKRTIPEYVPAFANTGGGYLFIGVDDKSREVLGCAKENVDPDSLRRKIEQAIYKLPCVHFCQPQRPITFTLKIVNVLKRGELYGYACMIRVNPFCCAVFSEAPNSWIVEDKYVCSLTTEKWVGMMTDTDPDLLQLSEDFECQLSLSSGPPLSRPVYSKKGLEHKKELQQLLFSVPPGYLRYTPESLWRDLISEHRGLEELINKQMQPFFRGILIFSRSWAVDLNLQEKPGVICDALLIAQNSTPILYTILREQDAEGQDYCTRTAFTLKQKLVNMGGYTGKVCVRAKVLCLSPESSAEALEAAVSPMDYPASYSLAGTQHMEALLQSLVIVLLGFRSLLSDQLGCEVLNLLTAQQYEIFSRSLRKNRELFVHGLPGSGKTIMAMKIMEKIRNVFHCEAHRILYVCENQPLRNFISDRNICRAETRKTFLRENFEHIQHIVIDEAQNFRTEDGDWYGKAKSITRRAKGGPGILWIFLDYFQTSHLDCSGLPPLSDQYPREELTRIVRNADPIAKYLQKEMQVIRSNPSFNIPTGCLEVFPEAEWSQGVQGTLRIKKYLTVEQIMTCVADTCRRFFDRGYSPKDVAVLVSTAKEVEHYKYELLKAMRKKRVVQLSDACDMLGDHIVLDSVRRFSGLERSIVFGIHPRTADPAILPNVLICLASRAKQHLYIFPWGGH", "text": "FUNCTION: Inhibitor of DNA replication that promotes cell death in response to DNA damage (PubMed:22927417, PubMed:26658330, PubMed:29395061). Acts as a guardian of the genome by killing cells with defective replication (PubMed:29395061). Persistently blocks stressed replication forks by opening chromatin across replication initiation sites at stressed replication forks, possibly leading to unwind DNA ahead of the MCM helicase and block fork progression, ultimately leading to cell death (PubMed:29395061). Acts independently of ATR (PubMed:29395061). Also acts as an interferon (IFN)-induced antiviral protein which acts as an inhibitor of retrovirus protein synthesis (PubMed:23000900). Specifically abrogates the production of retroviruses such as human immunodeficiency virus 1 (HIV-1) by acting as a specific inhibitor of the synthesis of retroviruses encoded proteins in a codon-usage-dependent manner (PubMed:23000900). Binds to tRNAs and exploits the unique viral codon bias towards A/T nucleotides (PubMed:23000900). The exact inhibition mechanism is unclear: may either sequester tRNAs, prevent their maturation via post- transcriptional processing or may accelerate their deacylation (PubMed:23000900). Does not inhibit reverse transcription, integration or production and nuclear export of viral RNA (PubMed:23000900). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Recruited to stressed replication forks carrying extended RPA filaments (PubMed:29395061). Recruited to DNA damage sites via interaction with RPA1 (PubMed:26658330, PubMed:29395061). SIMILARITY: Belongs to the Schlafen family. Subgroup III subfamily."}
{"protein": "MRRSDRLRCAGASLLVVLCGVFRSSFGGRTLPALSDDIPFRLKWPGPDFTLPTAGIPYKEDNYIIMTTADKEKYKCLLPLMANGNEEQDGEYKGPSPGALLEPLFKLSSCSYRIESYWTYEVCHGKYIRQYHEEKETGQKLSIQEYYLGKMMKKSTTEAGENQEEKESAESPKEIYTKNIEGQMTPYYPVEMINGTPCSLKQNQPRSSTVMYICHPESKHEILSVAEVTTCEYEVVILTPLLCNHPKYRFRTSPINDIFCQSMPGSPLRPQSLVKLEHQKEEIKSPLKPNKEEEQQLLREKFSTIHKPVTVGSQQQVTVGTTHISRLTDEQLIKEFLSGSYCFHGGVGWWKYEFCYGKYVHQYHEDKDTGKTTVVVGTWKADEHQEWAKKNLARAYMTTPDGVQTVKTVSHFYGGGDVCEVSEQPRQVIVKLKCKESESPHAVTVYMLEPQTCQYILGVESPVICKILDTADENGLLSIPN", "text": "FUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non- glycosylated proteins and glycoproteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen."}
{"protein": "MAQKEGGRTVPCCSRPKVAALTAGTLLLLTAIGAASWAIVAVLLRSDQEPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGLSCVEMGFLRALTHSELDVRTAGANGTSGFFCVDEGRLPHTQRLLEVISVCDCPRGRFLATICQDCGRRKLPVDRIVGGRDTSLGRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVAQASPHGLQLAVQAVVYHGGYLPFRDPNSEENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKICTVTGWGNTQYYGQQAGVLQEARVPIISNDVCNGADFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISRTPRWRLCGIVSWGTGCALAQKPGVYTKVSDFREWIFQAIKTHSEASGMVTQL", "text": "FUNCTION: Plays an essential role in cell growth and maintenance of cell morphology. May mediate the activating cleavage of HGF and MST1/HGFL. Plays a role in the proteolytic processing of ACE2 (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MSGQPPPPPPQQQPPPPPPPASAAAPATAPPGLAVGPGPAAGVPVPGLAAGSSAAAPFPHGDSALNEQEKELQRRLKRLYPAVDEQETPLPRSWSPKDKFSYIGLSQNNLRVHYKGHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFGQHPFVFDIEDYMREWRTKIQAQIDRFPIGDREGEWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTVLEELASIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGGRSPKSQDSYPVSPRPFSSPSMSPSHGMSIHSLAPGKSSTAHFSGFESCSNGVISNKAHQSYCHSKHQLSSLTVPELNSLNVSRSQQVNNFTSNDVDMETDHYSNGVGETSSNGFLNGSSKHDHEMEDCDTEMEVDCSQLRRQLCGGSQAAIERMIHFGRELQAMSEQLRRECGKNTANKKMLKDAFSLLAYSDPWNSPVGNQLDPIQREPVCSALNSAILETHNLPKQPPLALAMGQATQCLGLMARSGVGSCAFATVEDYLH", "text": "FUNCTION: May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways. Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Nucleus Note=Predominantly cytoplasmic (PubMed:18710924). A phosphorylated form is associated with the plasma membrane (By similarity). Perinuclear in spermatids (PubMed:14648869). SIMILARITY: Belongs to the RANBP9/10 family."}
{"protein": "EVPANAVTESDPTAVALKYHRNAEASERVAAARPGLPPEEQHCENCQFMLPDQGADEWRGCSLFPGKLINLDGWCASWTLRAG", "text": "FUNCTION: Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP) family."}
{"protein": "MSNGAADRARLRHLDHCRQPHCFARDICVFTYFELPEEHPQGPAHGVRITVEKGIDTHLIKFFTKRPLLVEKDQGNTILTLYCICPVPGLHEDFCCHLCAEFNHL", "text": "FUNCTION: Not yet known. SIMILARITY: Belongs to the adenoviridae E3A-2 family."}
{"protein": "MEDFLLSNGYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKVIDKMGGPEEFIQRFLPRELQIVRTLDHKNIIQVYEMLESADGKICLVMELAEGGDVFDCVLNGGPLPESRAKALFRQMVEAIRYCHGCGVAHRDLKCENALLQGFNLKLTDFGFAKVLPKSHRELSQTFCGSTAYAAPEVLQGIPHDSKKGDVWSMGVVLYVMLCASLPFDDTDIPKMLWQQQKGVSFPTHLSISADCQDLLKRLLEPDMILRPSIEEVSWHPWLAST", "text": "FUNCTION: May be involved in a signaling pathway during male germ cell development or mature sperm function. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family."}
{"protein": "MQPDRNLLADLDHIFVDRSLGAVQVPQLLRDAGFRLTTMREHYGETQAQSVSDHKWIAMTAECGWIGFHKDANIRRNAVERRTVLDTGARLFCVPRADILAEQVAARYIASLAAIARAARFPGPFIYTVHPSKIVRVL", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. The cognate antitoxin is VapB45."}
{"protein": "MHINFSYPYIIPSSHINLSLTLISLEEWALITFNGKDAVKYLQDQLACDVTSLKNNEYTFTVHCNTKGKVYSNVYFLHYQDGFALITRKSVYANELNIFKKYAIFYTVNINFHQNKILLGIAGLQVKDILSNIFTTIPNRLCPVIHTMDTTILYLHQPADRFLLITTNNIQNLILKKLTKYKIQTNNSKQWLALDIAAGYPIIDQINSELLLPQALNIEALGGISFNKGCYLGQEAIARTKYHNMNKKELCFLSGKANRIPTASEKLEIKINNNWRYTGIVLAACKLKNNIWIQVVLNRNLAIDSILRVRGDITSVFHLCPLNYL", "text": "FUNCTION: Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the tRNA-modifying YgfZ family."}
{"protein": "MLALSLLSIVSIASAAGVTAIPEGDNPYTIFPSVAKTASINGFADRIYDQLPECAKECVKQSTSSTPCPYWDTGCLCVMPQFAGAVGNCVAKNCKGKEVGSVESLATSICSSAGVWEPYWMIPSSVSDALAKAADAAAETTAESTTAESTAAETTKAEETSAKETTAAETSKAAESSAPAETSKAEETSKAAETTKAEESSVAQSSSSAADVASVSVEAANAGNMPAVAIGGVIAAVAALF", "text": "FUNCTION: GPI-linked hyphal surface heme-binding protein involved in heme-iron utilization (PubMed:15306022, PubMed:17042757, PubMed:18466294, PubMed:21205162, PubMed:25275454, PubMed:27617569). Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and form a cross-cell wall heme-transfer cascade (PubMed:15306022, PubMed:17042757, PubMed:18466294, PubMed:21205162, PubMed:25275454, PubMed:27617569). The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation (PubMed:15306022, PubMed:17042757, PubMed:18466294, PubMed:21205162, PubMed:25275454). SUBCELLULAR LOCATION: Secreted, cell wall Cell membrane; Lipid-anchor, GPI-anchor Note=Found anchored in the cell membrane as well as a covalently-linked GPI- modified cell wall protein (GPI-CWP). SIMILARITY: Belongs to the RBT5 family."}
{"protein": "MTQSPIFLTPVFKEKIWGGTALRDRFGYSIPSESTGECWAISAHPKGPSTVANGPYKGKTLIELWEEHREVFGGVEGDRFPLLTKLLDVKEDTSIKVHPDDYYAGENEEGELGKTECWYIIDCKENAEIIYGHTARSKTELVTMINSGDWEGLLRRIKIKPGDFYYVPSGTLHALCKGALVLETQQNSDATYRVYDYDRLDSNGSPRELHFAKAVNAATVPHVDGYIDESTESRKGITIKTFVQGEYFSVYKWDINGEAEMAQDESFLICSVIEGSGLLKYEDKTCPLKKGDHFILPAQMPDFTIKGTCTLIVSHI", "text": "SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family."}
{"protein": "MEDEMQIDKKEVEIEQKPPRFEIKKWNAVALWQWDIVVDNCAICRNHIMDLCIECQANTDSAAAQECTVAWGTCNHAFHFHCISRWLNTRNVCPLDNREWEFQRYGH", "text": "FUNCTION: Component of E3 ubiquitin ligase SCF complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recruit the E2 ubiquitination enzyme, like UBC3/CDC34, to the complex and brings it into close proximity to the substrate. Component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. SUBCELLULAR LOCATION: Cytoplasm. Nucleus."}
{"protein": "MARVKRAVNAHKKRRSILKASRGYRGQRSRLYRKAKEQQLHSLNYAYRDRRARKGEFRKLWIARINAAARLNDITYNRLIQGLKAAGVEVDRKNLADIAISDPAAFTALVDVARAALPEDVNAPSGEAA", "text": "FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity). FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family."}
{"protein": "MSDMNKILHKWSASLKKGTDFDSWGQLVEAIDEYQILARQLQKEAQSPANSSDFTEDQKKTIGKIATCLGLRSAALQYTQSQEGFTLEDVKKLEPILSSIVTFNKEFPFDVQPVPLRRILAPGEEENLEVDEEEEDGGAGIGSPDLFPARVPGTLLPRLPSEPGMTLLTIKIEKIGLKDAGQCIDPYITVSVKDLNGIDLTPVQDTPMATRKEDTYVHFNVEIEIQKHVEKLTKGAAIFFEFKHYKPKKRFTSTKCFAFMEMDEIKPGQTVIELYKKPTDFKRKKLQLLTKKPLYLHLLQTLLKD", "text": "FUNCTION: Acts as a ventralizing factor during embryogenesis. Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin- independent dorsalization pathway activated by axin/JNK-signaling (By similarity). SIMILARITY: Belongs to the AIDA family."}
{"protein": "MERTPNPNRQAVELNRTSLYLGLLLVAVLGILFSSYFFN", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbL family."}
{"protein": "MSLAVEAVKDFLLKLQDDICEALEAEDGQATFVEDKWTREGGGGGRTRVMVDGAVIEKGGVNFSHVYGKGLPMSSTERHPDIAGCNFEAMGVSLVIHPKNPHVPTSHANVRLFVAEREGKEPVWWFGGGFDLTPYYAVEEDCRDFHQVAQDLCKPFGADVYARFKGWCDEYFFIPYRNEARGIGGLFFDDLNEWPFEKCFEFVQAVGKGYMDAYIPIVNRRKNTPYTEQQVEFQEFRRGRYAEFNLVIDRGTKFGLQSGGRTESILISLPPRARWGYNWQPEPGTPEARLTEYFLTKRQWV", "text": "FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase family."}
{"protein": "MSVCSSDLSYSSRVCLPGSCDSCSDSWQVDDCPESCCEPPCCAPSCCAPAPCLSLVCTPVSRVSSPCCPVTCEPSPCQSGCTSSCTPSCCQQSSCQLACCASSPCQQACCVPVCCKTVCCKPVCCVPVCCGDSSCCQQSSCQSACCTSSPCQQACCVPICCKPVCSGISSSCCQQSSCVSCVSSPCCQAVCEPSPCQSGCISSCTPSCCQQSSCQPACCTSSSCQQACCVPVCCKTVCCKPVCSEDSSSCCQQSSCQPACCTSSPCQQACCVPVCCKPVCCKPVCSVPICSGASSLCCQQSSCQPACCTSSQSQQGCCVPVCCKPVSCVPVCSGASSSCCQQSSCQPACCTTSCCRPSSSVSLLCRPVCRPACCVPVPSCCAPTSSCQPSCCRPASCVSLL", "text": "FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SIMILARITY: Belongs to the KRTAP type 10 family."}
{"protein": "MEAILMIGVITLCVIFLLSGRNNKKIQEARELEDYLEDLNQRIAQRTQILSELNEVITNRSVDKSVNMSACEIAVLDLYEQSNIRIPSDIIEDMVNQRLQTEQDVLNYIETQRTYWKLENQKKLYRGSLK", "text": "FUNCTION: Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells. Required for the redistribution of replicating viral DNA from the initial replication site to membrane- associated sites surrounding the nucleoid. Required for the second pull step of DNA ejection. SUBCELLULAR LOCATION: Host cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the phi29likevirus gp16.7 family."}
{"protein": "MSQPSISKSMTIGESGLAVVFAATAFLCVIAAAKALDAPFAFHAALSAAASVAAVFCIVNRYFERPAALPPAEINGRPNYNMGPIKFSSFMAMFWGIAGFLVGLIIASQLAWPALNFDLPWISFGRLRPLHTSAVIFAFGGNVLIATSFYVVQKSCRVRLAGDLAPWFVVVGYNFFILVAGTGYLLGVTQSKEYAEPEWYADLWLTIVWVVYLLVFLATIIKRKEPHIFVANWFYLAFIVTIAVLHLGNNPALPVSAFGSKSYVAWGGIQDAMFQWWYGHNAVGFFLTAGFLAIMYYFIPKRAERPIYSYRLSIIHFWALIFLYIWAGPHHLHYTALPDWTQTLGMTFSIMLWMPSWGGMINGLMTLSGAWDKLRTDPVLRMLVVSVAFYGMSTFEGPMMSIKVVNSLSHYTDWTIGHVHSGALGWVGFVSFGALYCLVPWAWNRKGLYSLKLVNWHFWVATLGIVLYISAMWVSGILQGLMWRAYTSLGFLEYSFIETVEAMHPFYIIRAAGGGLFLIGALIMAYNLWMTVRVGEAEVQMPVALQPAE", "text": "FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the heme-copper respiratory oxidase family."}
{"protein": "MNIEEFFELSAGKWFSHRTSHHLAFKQSEDGKSDLVIESLAADHPEVIKLCELYEVPASAASCGARVSWNGTMEWDEEKHTGSTVLATVPDVDNPNEGRLLREMGYAEKAPVAGRYKMGDDGALTLTTEYETMWSEERLWFASPNLRMRVSVLKRFGGFSMASFTSEIRMGGSPAAAKAEEAANSASS", "text": "FUNCTION: Catalyzes the site-selective attachment of phycocyanobilin (PCB) to 'Cys-82' in CpcB and 'Cys-83' in PecB. Also able to add PCB to ApcA1, ApcA2, ApcB, ApcD and ApcF, but not PecA. In vitro can be made to add phycoerythrobilin, a non-physiological substrate, to its target proteins (using genes from Fremyella diplosiphon PCC 7601). Binds PCB extremely rapidly, followed by a much slower phase of PCB transfer to the apo-acceptor protein. This suggests that the lyase has a chaperone- like function, and may serve to regulate the manner (possibly the conformation) in which the chromophore is attached to its target rather than to accelerate the rate. SIMILARITY: Belongs to the CpcS/CpeS biliprotein lyase family."}
{"protein": "MKSVILTGLLFVLLCVDHMTASQSVVATQLIPINTALTPAMMEGKVTNPIGIPFAEMSQIVGKQVNTPVAKGQTLMPNMVKTYVAGK", "text": "FUNCTION: Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-III AFP family."}
{"protein": "MAEPDVSDTNTALKKSGEPGMELENNKATSGAVVTEAGFNTRKLWPDLIKLPSNRWVYSCKEIVDRLGTDPKAAQLTKKKMEKCLMYFYMIKKNLRLFDHTYTAACILFFRYWYIYELPQSLQDCIHLSQAILATACKAMENNRPLDMYVKATCEFMMKDLAQQQRGRQNMDKLKWDVRDKLVRYEKQLLCQFGFDLDLQNPKELIEEIFSGFYRFNRDNIMDEEFKKLFPKILAEARNFIIQAGTQPVSLLCDGYTFTALALLFAGLQYKRSTAPNFRFPRHFFQERFPIRITGPMIVNLFTDYRILEDNFFDLKSNKGDKLEVTNEEVQSLIDEEPTDETVPNPYDYELIKDGVCSQEFLDHTESKLKELTEKIISESLKKRPVIDDNTPKDDTKRVKM", "text": "FUNCTION: Component of the BUR kinase complex involved in transcription regulation. This complex phosphorylates the UBC2/RAD6 ubiquitin- conjugating enzyme (E2), leading to monoubiquitination of histone H2B and the silencing of telomeric-associated genes. Also required for histone H3 methylation. Necessary for the recovery from pheromone- induced growth arrest in the cell cycle G1 phase. The kinase activity of the complex requires the presence of BUR2. Overexpression of BUR2 interferes with mitotic chromosome segregation (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MHGHNRNGQAHVPRRKRRNRFVKKNGQCNVYFANLSNKSQRYMADIFTTCVDTRWRYMLMIFSAAFLVSWLFFGLLFWWIAFFHGDLEASPSVPAVGGPGGNGGESPNAPKPCIMHVNGFLGAFLFSVETQTTIGYGFRCVTEECPLAVIAVVVQSIVGCVIDSFMIGTIMAKMARPKKRAQTLLFSHHAVISVRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPYMTQEGEYLPLDQRDLNVGYDIGLDRIFLVSPIIIVHEIDEDSPLYGMGKEELESEDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVVFEEKSHYKVDYSRFHKTYEVAGTPCCSARELQESKITVLPAPPPPPSAFCYENELALMSQEEEEMEEEAAAAAAVAAGLGLEAGSKEEAGIIRMLEFGSHLDLERMQAATLPLDNISYRRESRI", "text": "FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane. Note=TAX1BP3 binding promotes dissociation of KCNJ4 from LIN7 family members and KCNJ4 internalization. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ4 subfamily."}
{"protein": "MKPSVILYKALPDDLLQRLQEHFTVHQVANLSPQTVEQNAAIFAEAEGLLGSNENVNAALLEKMPKLRATSTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTASIGPDWYGTDVHHKTLGIVGMGRIGMALAQRAHFGFNMPILYNARRHHKEAEERFNARYCDLDTLLQESDFVCLILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSMANVVAVPHIGSATHETRYGMAACAVDNLIDALQGKVEKNCVNPHVAD", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2- keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D- fructose and L-sorbose. Activity with NAD is very low. FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily."}
{"protein": "MGCNMCVVQKPEEQYKVMLQVNGKELSKLSQEQTLQALRSSKEPLVIQVLRRSPRLRGDSSCHDLQLVDSGTQTDITFEHIMALGKLRPPTPPMVILEPPPISHEYYDPAEFMEGGPQEADRLDELEYEEVELYKSSHRDKLGLMVCYRTDDEEDLGIYVGEVNPNSIAAKDGRIREGDRIIQINGVDVQNREEAVAILSQEENTNISLLVARPESQLAKRWKDSDRDDFLDDFGSENEGELRARKLKSPPAQQPGNEEEKGAPDAGPGLSNSQELDSGVGRTDESTRNEESSEHDLLGDEPPSSTNTPGSLRKFGLQGDALQSRDFHFSMDSLLAEGAGLGGGDVPGLTDEEYERYRELLEIKCHLENGNQLGLLFPRASGGNSALDVNRNESLGHEMAMLEEELRHLEFKCRNILRAQKMQQLRERCMKAWLLEEESLYDLAASEPKKHELSDISELPEKSDKDSTSAYNTGESCRSTPLLVEPLPESPLRRAMAGNSNLNRTPPGPAVATPAKAAPPPGSPAKFRSLSRDPEAGRRQHAEERGRRNPKTGLTLERVGPESSPYLSRRHRGQGQEGEHYHSCVQLAPTRGLEELGHGPLSLAGGPRVGGVAAAATEAPRMEWKVKVRSDGTRYVAKRPVRDRLLKARALKIREERSGMTTDDDAVSEMKMGRYWSKEERKQHLIRAREQRKRREFMMQSRLECLREQQNGDSKPELNIIALSHRKTMKKRNKKILDNWITIQEMLAHGARSADGKRVYNPLLSVTTV", "text": "SUBCELLULAR LOCATION: Cytoplasm, cell cortex Note=Mainly localized under the plasma membrane."}
{"protein": "MARLRSMVQAGVARVEGFGLAGFSDEELYAIHTSTLEVLEYTGLKIESQEALEIFSEGGARVDFKTKVVKIPQYLVEDAIQSAPSTLVLAGRNPKNDIVLGGKRVGFINFGEGVSIIDPYTKEYRKTTRRDVANITRFCDAMDQMDAVLRPVAPQDIHPSVAVVHNAEVIFNNTSKHVFIGVEGGRNFKKVLKMAAAVAGGEDKLRERPLFSCNICPTSPLQIVNHASEVIIEGARAGIPVNMLSMGMSGATSAITLAGTLVTHNCEVLGAIVLSQLTSKGAPVLYGSSTTIMDMKNMTAPVGSPELGMINAGVAKLAQYYNLPSWVAGGOVDSKIPDAQASHEFTLTGFLTALAGANLIYGAGMLELGITFDYAQMLMDNEMARMIKKAVGGISVTDETLAVDVIKSVGTAGNFISEDHTYAHMRTQSQSKLVDRSMRENWLAAGAKDFTQRAYEEAISILENYTPEPLPEKIAATLRSIVEETEDEYGVARSLI", "text": "FUNCTION: Catalyzes the transfer of a methyl group from trimethylamine to the corrinoid cofactor of MttC. SIMILARITY: Belongs to the trimethylamine methyltransferase family."}
{"protein": "MSERRVAMDLPSGSNASMPLQRHRVSSLRGTRSPSSLDSPPASRTSAVGSLVRAPGVYVGVAPSGGIGGLGARVTRRALGISSVFLQGLRSSGLATAPAPGPERNHATAEDLGGCLVEYMTKVHALEQVSQELETQLRAHLESKAKRSGGWDALRASWASSYQQVGEAVLENARLMLQMETIQAGADDFKERYENEQPFRKAAEEEVSSLYKVIDEANLTKTDLEHQIESLKEELGSLSRSYEEDVKVLYKQLAGSELEQTDVPMGTGLDDVLETIRVQWERDVEKNRAEAGAVLQAKQQTEVVHVSQTQEEKLAAALSVELHDTSRQVQSLQAETESLRALKRGLENTLHDAKHWHDMELQNLGAVVGRLEAELAEIHSETEQQQQERAHLLACKGQLQKDVASYHALLDREESN", "text": "FUNCTION: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Plays a role in maintenance of retinal lens optical clarity (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Cytoplasm, cytoskeleton Cytoplasm, cell cortex Note=Expressed primarily at the plasma membrane in peripheral lens fiber cells, however also localizes to the cytoplasm in mature lens fiber cells. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MSTSSSSRIAIEQNNKCVNSVAAALCPLSNCQFSGVVISAISDEQKLEFNSIYKSSCTLSCSYDSQGVLLRIMLDNDQGHVLKEYMISADTDAAQLGRRCYAVSLESDNLVLRFGSDKDQQLFRKVVENVKHLRPKSVFSQRTEESSASQYFQFYGYLSQQQNMMQDYVRTSTYQRAILGNSIDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAQYAQQLVESNNVQHKISVIPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKWLKPHGKMYPTHGDLHIAPFSDESLYSEQYNKANFWYQSAFHGVDLTTLHKEGMKEYFRQPIVDTFDIRICMAKSVRHVCDFLNDKEDDLHVIDIPLEFHILQTGICHGLAFWFDVEFSGSSQNVWLSTSPTAPLTHWYQVRCLLPMPIFIKQGQTLTGRVLLEANRRQSYDVTIDLHIEGTLISSSNTLDLKNPYFRYTGAPVQAPPGTNTQSPSEQYWTQMDTQGNRNSNSMLNGALTVNGMGDGGMDITHGLMHPH", "text": "FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family."}
{"protein": "MSNSKDEVERIDWLEAELADTIDEDYELELSEPTLSEKIREIYRKAHPPALPRMDYFRALLALQAELIKLQDWVVYHKQKVVVIFEGRDAAGKGGVIKRITQRLNPRIVRTVALPAPSDREKTQWYFQRYVPHLPAGGEIVLFDRSWYNRCGVERVMGFATEEEVEQFFDDVPEFERMLVRSGVRLVKYWFSITDEEQQLRFLTRIHDPLKQWKLSPMDLQSRVRWEAYTKAKEETFARTNIREAPWHIVEANDKKRARLNCIDHLLKQIPYEDVPHEDITLPERIFNPNYERKVLPPELYVPAKY", "text": "FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert ADP to ATP. Can also convert GDP to GTP, with lower efficiency. SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class I subfamily."}
{"protein": "MLKSTLLAFGLFIALSARAENQAIAKLFLRAGVDGTIVIESLTTGQRLVHNDPRAQQRYPAASTFKVLNTLIALEEGAISGENQIFHWNGTQYSIANWNQDQTLDSAFKVSCVWCYQQIALRVGALKYPAYIQQTNYGHLLEPFNGTEFWLDGSLTISAEEQVAFLRQVVERKLPFKASSYDSLKKVMFADENAQYRLYAKTGWATRMTPSVGWYVGYVEAKDDVWLFALNLATRDANDLPLRTQIAKDALKAIGAFPTK", "text": "FUNCTION: This oxacillinase hydrolyzes methicillin. SIMILARITY: Belongs to the class-D beta-lactamase family."}
{"protein": "MANTWRLDIRGLDGSLVLIVLALITIGLVMVLSSSVAVSEVRFGHQWHYFQRQVFALGVGGLFAALVLMVPSQSWLQHRGKWFLLGLVLLALVLIFGREIGGAKRWLPLVVMNFQPAEWMKIATILFLAGYLQRHQDAVKQDSTAVIRLFLPFGIMAGLLLLQPDYGTTVLIAGVLVGMLFIAGAPFRYFVITVLPIGAILAVLLINSPYRMARVMNFMDPWQDPYGVGYQLSQALMAIGSGGITGSGLGASVQKLLYLPDAHTDFMFAVFAEETGWLGVVILLSLYGLLLWRMFAVAQAAWLPQAPFKALVVYGVAIMFAGQLLINVGVNLGVFPTKGLTLPFVSYGGSSLMMALLAIGLVLRIDYETRLIKGHSTEELSANPSFGS", "text": "FUNCTION: Peptidoglycan polymerase that is essential for cell division. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the SEDS family. FtsW subfamily."}
{"protein": "MPFQFGTQPRRFPVEGGDSSIELEPGLSSSAACNGKEMSPTRQLRRCPGSHCLTITDVPVTVYATTRKPPAQSSKEMHPK", "text": "SIMILARITY: Belongs to the FAM229 family."}
{"protein": "MSSKDQILEKDKKETDDNGNKKTTTTTSSSSSSSSSSKPRSNKFDKVIIKSNGVCYITEGVIGNGSFGVVTQAIVADTKEVVAIKKVLQDQRYKNRELQIMKMLNHINIVSLKNSFYTSDNDEVYLNLVLEYVPDTVYRVSRHYSMSKQPVPNIFVKLYIYQLCRSINYIHSLGICHRDIKPQNLLLDTSTSTLKLCDFGSAKILIKGETNVSYICSRHYRAPELIFGSTNYTTTIDVWSLGCVLAELLLGQPLFPGENGIDQLVEIIKVLGTPTKEQIHAMNPYYTSFKFPEIKANPWPRVFKAKDVPAESIDLISKILLYDPSSRLKPVEICAHPFFDELRDPKTCLPDGKPLPPLFNFTIAEQTSIGPKLAKTLIPSHAMNQIELPSPLFPNLAISSSNQSSSSNSNANVSSNLNSHSASPSTTSSSSSTPNSIPVQSPSTTNTTSSTTNNTTTTTTTTTTSNH", "text": "FUNCTION: During cellular differentiation, may mediate an extracellular cyclic AMP stimulated signal transduction pathway that regulates prespore and prestalk B-cell proportions through inhibition of stalk cell formation and induction of prespore cell differentiation. The cAMP receptor carC appears to activate gskA via the tyrosine kinases zakA and zak2, to stimulate prespore differentiation, while carD appears to negatively regulate gskA, to promote prestalk formation. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily."}
{"protein": "CYLSERLMLDARENLKLLDRMNRLSPHSCLQDRKDFGLPQEMVEGDQLQKDQAFPVLYEMLQQSFNLFYTEHSSAAWDTTLLEQLCTGLQQQLDHLDTCRGQVMGEEDSELGNMDPIVTVKKYFEGIYDLLQEKGYSDCAWEIVRVEMMRALTVSTTLQKRLTKMGGDLNSP", "text": "FUNCTION: Paracrine hormone primarily responsible for maternal recognition of pregnancy. Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium. This results in the suppression of the pulsatile endometrial release of the luteolytic hormone prostaglandin F2-alpha, hindering the regression of the corpus luteum (luteolysis) and therefore a return to ovarian cyclicity. This, and a possible direct effect of IFN-tau on prostaglandin synthesis, leads in turn to continued ovarian progesterone secretion, which stimulates the secretion by the endometrium of the nutrients required for the growth of the conceptus. In summary, displays particularly high antiviral and antiproliferative potency concurrently with particular weak cytotoxicity, high antiluteolytic activity and immunomodulatory properties. In contrast with other IFNs, IFN-tau is not virally inducible. SUBCELLULAR LOCATION: Secreted. Note=Secreted into the uterine lumen. SIMILARITY: Belongs to the alpha/beta interferon family. IFN-alphaII subfamily."}
{"protein": "MSRKLFSVLLVGLMLMTSLLVTISSTSAASLPTMPPSGYDQVRNGVPRGQVVNISYFSTATNSTRPARVYLPPGYSKDKKYSVLYLLHGIGGSENDWFEGGGRANVIADNLIAEGKIKPLIIVTPNTNAAGPGIADGYENFTKDLLNSLIPYIESNYSVYTDREHRAIAGLSMGGGQSFNIGLTNLDKFAYIGPISAAPNTYPNERLFPDGGKAAREKLKLLFIACGTNDSLIGFGQRVHEYCVANNINHVYWLIQGGGHDFNVWKPGLWNFLQMADEAGLTRDGNTPVPTPSPKPANTRIEAEDYDGINSSSIEIIGVPPEGGRGIGYITSGDYLVYKSIDFGNGATSFKAKVANANTSNIELRLNGPNGTLIGTLSVKSTGDWNTYEEQTCSISKVTGINDLYLVFKGPVNIDWFTFGVESSSTGLGDLNGDGNINSSDLQALKRHLLGISPLTGEALLRADVNRSGKVDSTDYSVLKRYILRIITEFPGQGDVQTPNPSVTPTQTPIPTISGNALRDYAEARGIKIGTCVNYPFYNNSDPTYNSILQREFSMVVCENEMKFDALQPRQNVFDFSKGDQLLAFAERNGMQMRGHTLIWHNQNPSWLTNGNWNRDSLLAVMKNHITTVMTHYKGKIVEWDVANECMDDSGNGLRSSIWRNVIGQDYLDYAFRYAREADPDALLFYNDYNIEDLGPKSNAVFNMIKSMKERGVPIDGVGFQCHFINGMSPEYLASIDQNIKRYAEIGVIVSFTEIDIRIPQSENPATAFQVQANNYKELMKICLANPNCNTFVMWGFTDKYTWIPGTFPGYGNPLIYDSNYNPKPAYNAIKEALMGY", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family."}
{"protein": "MKNLLVFIFVFSLCMFDHVSGAGIRIGNELKFQKLLWMRCYSKDDVLGPKIIPIGGHFVTYFSVNIWRTTRFMCTLKQGPNYRHYQNFTAFKLFGMEDHGDVWDWRARENEIYLKKKEGGKFIKNPVNMHKVYDWIN", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant self-incompatibility (S1) protein family."}
{"protein": "MQDTAKYLIHADITAAGVVERSDVVGAVFGQTEGLLGDELDLRDLQDSKKVGRIDVEIRSEGGQSFGEITVASGLDRVETAILAAALETIEQVGPCRAEIEVSEIEDVRSAKRREVVERATELLNDFEEKSIQTADIVETVRQQVRVADVTDYEGLPAGPRVADSDAIVVVEGRSDVMQLLKYGIKNAVAVEGTDVPDAIADLTAGRTVTSFLDGDRGGDLILKELAQVGDVDYVAVTPSDKSVEDLSRSEVMSALRDKVPYETVASAKSLDSIREEMSQAGESTTADGGAVAAATSDDAADNQPSPSSQTGSAKVETTDGTTSVVDNSNATAVADATTDEETTENGDGPTIPSLSDHIEAVIQTHSGTARLVDEDATLLAEGDADAVVSLLESTEDVPKTVVIDADCSQKLLDVAAQRGVDVVVAAGHGEYVKQPTAVQVRIES", "text": "FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. SIMILARITY: Belongs to the archaeal DnaG primase family."}
{"protein": "MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ", "text": "FUNCTION: Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11554766, PubMed:11518699, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:20074060, PubMed:12519745). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=In response to stress, recruited by p53/TP53 to specific promoters. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily."}
{"protein": "MPVIEEIDDIDDIDNLEMDLAELDSTMKTPVAPKIVPTVVRSQDQEEEAYSAAISGNAGSGSGFNFVNSTTGQVEKSHSLTKEELDEIKEFQMLYPCYFDTRRTHAQGRRAPKDLCVENPLAKTIADAARSLGIPSIFEGSKTHPQDFGNPGRVRVLIKENGKPFVSGIDNKRVLMKRIGEYLKSHPTTLESVKQLPYGPDFDNVEPKKIPLLKGTAMNDIVPLHSPYLTQHPMTKSLYDAPPPPPPAQQVSAPEKQMKMPKNKFRVVRR", "text": "FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. It must be involved intimately in the translocation of a wide variety of protein substrates (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SRP19 family."}
{"protein": "MEYMQAPPSSSHGNILCCTCGVPIPPNPANMCVSCLRTQVDISEGIPKQVTIHFCRQCERYLQPPGSWVQCALESRELLALCLKKLKASMSKVRLIDAGFLWTEPHSKRIKIKLTIQKEVMNGAILQQVFTVEFVVQGQMCEDCHRVEAKDFWKAVVQVRQKTVHKKTFYYLEQLILKHKLHQNTVRIKEIHEGIDFYYATKQHAQKMVDFLQCTVPCRSKASQRLISHDVHSNTYNYKSTFSVEIVPVCKDNVVCLSPRLAQSLGNMGQVCVCVRVTSSIHLIDPNTLQIAEVDGSTFWRHPFNSLCSPRQLEEFIIMDIDIIRDQRLGAGAGLKSNKHTLAEVWVQKTSEMDSSHQYHCRTFMGHLLNIGDLVLGFDFANANINDEFLNKMNPQHVPDVVLIKKSYDRMKRARKRVWKLKEMDREKDAADTDDERQYTEFLEDLEEDEMLRKNINIFRDASKIPVEESDTDDDGAPRISLAEMLEDLSLSDATGGEGADMMTD", "text": "FUNCTION: Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the nucleus/nucleolus and the cytoplasm in a XPO1/CRM1-dependent manner. SIMILARITY: Belongs to the NMD3 family."}
{"protein": "MKLWKRAAAAIKDRKSLLAVGFSRRNSSYRNADLEAAIIKATSHDDSSVDYSNAHRVYKWIRSSPLNLKTLVYAISSRVNHTRSWIVALKSLMLLHGVLCCKVPSVVGEFRRLPFDLSDFSDGHSCLSKTWGFNVFVRTYFAFLHHYSSFLSDQIHRLRGNNRRSLEKTSDSVIQELERIQKLQSLLDMILQIRPVADNMKKTLILEAMDCLVIESINIYGRICGAVMKVLPLAGKSEAATVLKIVNKTTSQGEDLIVYFEFCKGFGVSNAREIPQFVRIPEEEVEAIEKMIDTVQEKPKLEKDEEKEDEKAMVVLEQPKKLQTIITDKWEIFEDDYRCFDRKDKWEIFEDEYHQNHLPLITMNQPVYITYTMPDLITF", "text": "SUBCELLULAR LOCATION: Membrane, clathrin-coated pit Golgi apparatus Cytoplasmic vesicle, clathrin-coated vesicle Note=Colocalized with clathrin in the Golgi area."}
{"protein": "MSRGQIIHSGHFMCSNPHDDLVQDEDEEDVEVDVVEDDDKSMEASSSVHHKNKALDEKPVTFYKFGVGKTQSIAIDVSLNKLNKCIKVAYNKMTTPKWKDFKGLRLHWKQRVRLNNVIWRAYYIEFRKKQPEKPKKPFCYFAVPDDDTTHQKIEGSIVEGMYWKRKMEGVCAQYKRWRIRSKHNLVTDKGGMVATCSSTSVSSMTGELKRKRKHTVPKETIESKLRSYEPPVKLQRSQTPKHTISDEFAWDFDDLDNVFTDDFLNSLSEPYMFPDPRDVYSGNNADIMQPGLLPLQPTIEDIMMSLGDDMPDSPPFHNDRDTMRTPTNDQPSISAQQIPQMRRSASSSASLHQMQVAQAQAQSISQISQPSQQLQHQIQIQQPVAARPHEFMASSIMMDYRLMPTRQSSAITSQMLMLSQSASTLSSQPQYATSTHYSTNNSFLPIRNTMTNQHHLGHTSQHSPWNKQQQSNFLVSLPHQSHVERILNNQPPLVPPPSRSNLLPTQNDPYLPQFLQSTQPTPQPQSHDPMMAPSRSWWLDSPLTASVQSPLSVATPLPLANQTGPQTPLGQLIGSADNGFLFGGNNTPGGFKMSGTTSGVPTLSQRLEQPPISRTSTIFGNVENKPERIFTSLTSQNTPTPSPLDISSLSRLRTSSLNESWKMSHIVEGSPTYQAFAASVTTKPSILESPSTSGDISGPASVPVQASQHPPKIITPPSASSKRKEQEAAMAPLVNRQQSCDVNLLNGKMAVKVEEKSGRHYLPTTPTELKEVTKEEPLLMSAPSSVKSMRRQAPDSTLHPEERKRILHLHAEQNRRSALKDGFDQLMDIIPDLYSGGVKPTNAVVLAKSADHIRRLQAEKWDKTQKIDEAKAKIEKLNQKITSLQSNLPQSSAPSSSSQVDSKTSLETFFDRYVKEGAKKNWRFWVMSQMLKPICVTQTNSFASSVAGDSSSRNEVAASCSDWLNKNWKATELRPLASTLLVSLATNSSILAEPDTLPDYVMQQLKNPF", "text": "FUNCTION: Transcription factor that binds to the E box motif 5'-CACGTG- 3', probably in a heterodimeric complex with mxl-2 (PubMed:17826759). Involved in modulating longevity in response to TOR signaling, dietary restriction, the decline in protein homeostasis associated with normal aging, germline signaling and the insulin-like signaling pathway (PubMed:24699255, PubMed:27001890). Plays a role in autophagy (PubMed:27001890). Involved in regulating migration of the ray 1 precursor cells in the male tail, acting in concert with Wnt and semaphorin signaling pathways (PubMed:17826759). Regulates transcription of genes encoding extracellular matrix (ECM) components which may contribute to the substratum required for migration of the neighboring ray 1 precursor cells (PubMed:17826759). Involved in repressing infection by the microsporidian pathogen N.parisii, probably acting independently of its canonical partner, mxl-2 (PubMed:27402359). SUBCELLULAR LOCATION: Nucleus Cytoplasm Mitochondrion Note=Nuclear localization is promoted by conditions of dietary restriction or reduced insulin- like/IGF-1 signaling in a pha-4-dependent manner."}
{"protein": "MKYVVVSGGVISGIGKGVLASSTGMLLKTLGLKVTSIKIDPYMNIDAGTMSPLEHGECFVLNDGGETDLDLGNYERYLNVTLTKDHNITTGKIYSHVIAKERKGDYLGKTVQIVPHLTNAIQEWIERVSRIPVDNTGMEPDVCIIELGGTVGDIESAPFVEALRQFQFRVGKENFALIHVSLVPVIHGEQKTKPTQAAIKDLRSLGLVPDMIACRCSETLEKGVIEKIAMFCHVGADQVVNVHDVNSTYHVPLLLLEQKMINYLHQRLQLQEITLSSEDIQRGENLLSKWKSMTGNFDSSMETVKIALVGKYTNLKDSYLSVIKALEHSSMKCRRKLEIMWVEATDLEPETQDTEKAKFHEAWNKVSTADGILVPGGFGSRGTEGMMLASRWARENHIPFLGVCLGLQIATIEFARNVLGVKEGNSAEFFPELDESNQVVVFMPEIDKETMGGSMRLGLRPTYFQQGTEWCAIKKLYGSAESVEERHRHRYEINPNFIERLEEHGLMFVGRDETNKRCEIFEMKDHPFFVATQYHPEYTSKVLDPSKPFLGLVAASSGILDDVIAGKYEFNGDGKSDF", "text": "FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. SIMILARITY: Belongs to the CTP synthase family."}
{"protein": "MDAVTVNNFFLIGAVLVGMSILVSSLSSRLGIPILVIFLAVGMIAGNDGVGGIVFDNYPVAYLVGNLALAVILLDGGLRTRVSSFRVALWPALSLATLGVLVTTGLTGIAAAWLFDLHWMEGLLIGAIVGSTDAAAVFSLLGGKGLNERVTATLEIESGSNDPMAVFLTVTLIEMLASGQTGLSWGFVLHLVQQFGLGALLGLGGGWLLLQLINRMHLAGGLYPLLVISGGLLVFALANAVGGSGILAIYLCGLLLGNRPIRSRHGILHMLDGMAWLAQIGMFLVLGLLVTPHDLWPIALPALALALWMILVARPLSVLIGLIPFRAFHDREKAFIAWVGLRGAVPIILAVFPLMAGLPNAQLFFNVAFFIVLVSLLVQGTSLPWAARLLRVVVPPDPAPISRAGLEIHPTSEWELFVYHLNKEKWCIGAALRELKMPGGTRIAALFRGTELLHPSGSTILEADDILCVIGHEHDLPALGKLFSQAPDRGLGARFFGDFVLEGDAQLSAVASLYGLKLDGIDGEQALGRFIAHEIGGEAVIGDQVEWNGLTWTVAALEGNRIRKVGVKFPEGRPGPGLFL", "text": "FUNCTION: K(+)/H(+) antiporter that extrudes potassium in exchange for external protons and maintains the internal concentration of potassium under toxic levels. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. NhaP2 subfamily."}
{"protein": "MALLCYNRACGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELSELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEEDKKEEDNDEIKIGTSCKNGGCSKTYRGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGRHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEINMRKAEPMQWASLELPAAKKQEKQKDDTTD", "text": "FUNCTION: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (By similarity). Involved in stress response. Prevents tumorigenesis (By similarity)."}
{"protein": "MESGPRVEPGPGAPAAVLARIPQEPRPSPEGDPSPPPPPTPMSALVPDTPPDTPPALKTATNPKQLPLEPGNPTGQISPQPAPPQEECPSSEAKSRGPTPTATGPREAKPSRRSSQPSPTTVPASDSPPAKQDVKKAGERHKLAKERREERAKYLAAKKAVWLEKEEKAKALREKQLQERRRRLEEQRLKAEQRRAALEERQRQKLEKNKERYEAAIQRSVKKTWAEIRQQRWSWAGALHHSSPGRKTSGSRCSVSAVNLPKHVDSIINKRLSKSSATLWNSPSRNRSLQLSAWESSIVDRLMTPTLSFLARSRSAVTLPRNGRDQGRGSGPGRRPTRARAGASLAPGPHPDRTHPSAAVPVCPRSASASPLTPCSAPRSAHRCTPSGERPERRKPGAGGSPALARRRLEATPVQKKEKKDKERENEKEKSALARERNLKKRQSLPASIRPRLSTGSELSPKSKARPSSPSTTWHRPASPCPSPGPGHALPPKPPSPRGTTASPKGRVRRKEEAKESPSPSGPEDKNHRKSRAAEEKEPAAPASPAPSPVPSPTPAQPQKEQSSTQIPAETAVPAVPAAPTAPPTAAPSVTPSKPMAGTTDREEATRLLAEKRRQAREQREREEQERKLQAERDKRMREEQLAREAEARAEREAEARRREEQEAREKAQAEQEEQERLQKQKEEAEARSREEAERQRQEREKHFQKEEQERQERRKRLEEIMKRTRKSEAAETKKQDAKETAANNSGPDPVKAVETRPSGLQKDSMQKEELAPQEPQWSLPSKEMPGSLVNGLQPLPAHQENGFSPKGTAGDKSLGRTAEGLLPFAEAEAFLKKAVVQPPQVTEVL", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. SIMILARITY: Belongs to the MAP7 family."}
{"protein": "MGRNVKTKAKRKNKKKAEASSSEIPSIPTRVWQPGVDTLEDGEELQCDPSAYNSLHGFHVGWPCLSFDILGDKLGLNRTEFPHTLYMVAGTQAEKAAHNSIGLFKITNVSGKRRDVVPKTFGNGEDEDEDDEDDSDSDDDDGDEASKTPNIQVRRVAHHGCVNRIRAMPQNSHICVSWADSGHVQVWDMSSHLNALAESETEGKDGTSPVLNQAPLVNFSGHKDEGYAIDWSPATAGRLLSGDCKSMIHLWEPASGSWAVDPIPFAGHTASVEDLQWSPAEENVFASCSVDGSVAVWDIRLGKSPALSFKAHNADVNVISWNRLASCMLASGSDDGTFSIRDLRLIKGGDAVVAHFEYHKHPITSIEWSAHEASTLAVTSGDNQLTIWDLSLEKDEEEEAEFNAQTKELVNTPQDLPPQLLFVHQGQKDLKELHWHNQIPGMIISTAGDGFNILMPYNIQNTLPSELPA", "text": "FUNCTION: Probable substrate receptor of CRL4 E3 ligase complexes acting as negative regulators of thermotolerance by disturbing the action of HSP90-1 and by preventing the expression of heat-inducible genes (e.g. HSP14.7, HSP21, At2g03020 and WRKY28). SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."}
{"protein": "MTEEVIVIAKWDYTAQQDQELDIKKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKTSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSYNGQIGWFPSNYVLEEVDEAAAESPSFLSLRKGASLSNGQGSRVLHVVQTLYPFSSVTEEELNFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHAPQISYTGPSSSGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDFSVSLKASGKNKHFKVQLVDNVYCIGQRRFHTMDELVEHYKKAPIFTSEHGEKLYLVRALQ", "text": "FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum."}
{"protein": "MSLSTLKREQIKKDLKDQEFDVVIIGGGITGAGIALDASERGMKVALVEMQDFAQGTSSRSTKLVHGGLRYLKQLQVGVVAETGRERAIVYENGPHVTTPERMLLPMHKGGSMGKFTTSIGLAMYDRLAGVKKAERKTMLNAKETLEKEPLVKKAGLKGGGSYVEYRTDDARLTIEVMKRAEEKGAKVINHTKSVHFTYDSNEKVNGIQVEDQISNETYPIKAKKVINASGPWVDEVRSGDYARNNKQLRLTKGVHIVIDQSKFPLGQAVYFDTEKDGRMIFAIPREGKAYVGTTDTFYDNNKTSPLANQEDRDYLIDAINYMFPDVNVADEDIESSWAGVRPLILEEGKDPSEISRKDEVWEGKSGLLTIAGGKLTGYRHMALEIVDLLSKRLKSEFGLKFDKCATKHLTISGGDVGGSANFDKFIEQKVEEAKSYQIDESTARHFASKYGSNAEELFKIAQTAQYQETGLPLDIYTELVYSIQNEMVYRPTDFFIRRTGKLYFKIDDVLNYKEQVIDVMAGLLGYTNIEKEAYTKELQIAIDEAQTGNHQPAVKE", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "METPFYGEEALSGLAAGASSVAGATGAPGGGGFAPPGRAFPGAPPTSSMLKKDALTLSLAEQGAAGLKPGSATAPSALRPDGAPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSTQFLYPKVAASEEQEFAEGFVKALEDLHKQSQLGAATAATSGAPAPPAPADLAATPGATETPVYANLSSFAGGAGPPGGAATVAFAAEPVPFPPPPGALGPPPPPHPPRLAALKDEPQTVPDVPSFGDSPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSHVNSGCQLLPQHQVPAY", "text": "FUNCTION: Transcription factor binding AP-1 sites (By similarity). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing its transcriptional activity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Jun subfamily."}
{"protein": "MAQTKRSRDESEKEEVVVKADVESSDVDHSFKSLNLSQPTMRAIEKMGFSKMTPVQARTIPPLMAGRDVLGAAKTGSGKTLAFLLPTIELLHSLKFKPRNGTGVIIITPTRELALQIFGVVRELMEFHSQTFGIVIGGANRRQEAEKLMKGVNLLVATPGRLLDHLQNTKGFIFKNLKALVIDEADRILEIGFEDEMRQIIKILPNEDRQSMLFSATQTTKVEDLSRISLRPGPLFINVVSEHDSSTADGLEQGYVVCESDKRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTNGKGKSLMFLIPNELGFLRYLKAAKVPLNEYEFPTNKIANVQSQLEKLIKSNYYLHQTAKDGYRSYLQAYASHSLKTVYQIDKLDLAKVAKSYGFPVPPKVNITIGASGKTPTVVKKRKTHKH", "text": "FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily."}
{"protein": "LGVLEKLNTMDLEKTPRIIILSAVGQDKITQQAITLGADYYTVKPFDMEVFTKRIREMFNSAPTIQESSAQSNRVSYPTTSSYILTSEPKSKTPVDLETEITNIIHEIGVPAHIKGYMYLREAITMVVNDMELLSAVTKELYPSIAKKYNTTASRVERAIR", "text": "FUNCTION: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MHTLVFLSTRQVLQCQPAACQALPLLPRELFPLLFKVAFMDKKTVVLRELVHTWPFPLLSFQQLLQECAHCSRALLQERPSTESMQAVILGLTARLHTSEPGASTQPLCRKHALRVLDMTGLLDDGVEQDPGTMSMWDCTAAVARTCIAQQQGGAAEPGPAPIPVEVRVDLRVNRASYAFLREALRSSVGSPLRLCCRDLRAEDLPMRNTVALLQLLDAGCLRRVDLRFNNLGLRGLSVIIPHVARFQHLASLRLHYVHGDSRQPSVDGEDNFRYFLAQMGRFTCLRELSMGSSLLSGRLDQLLSTLQSPLESLELAFCALLPEDLRFLARSPHAAHLKKLDLSGNDLSGSQLAPFQGLLQASAATLLHLELTECQLADTQLLATLPILTQCASLRYLGLYGNPLSMAGLKELLRDSVAQAELRTVVHPFPVDCYEGLPWPPPASVLLEASINEEKFARVEAELHQLLLASGRAHVLWTTDIYGRLAADYFSL", "text": "FUNCTION: Negatively regulates Toll-like receptor-mediated NF-kappa-B signaling by disrupting IKK core complex formation through interaction with IKBKB. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRAME family. LRRC14 subfamily."}
{"protein": "MKLPIIFLTLLIFVSSCTSTLINGSSDEERTYSFSPTTSPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRCSISDIK", "text": "FUNCTION: Pollen tube attractants guiding pollen tubes to the ovular micropyle (PubMed:23271953, PubMed:29109411). Attracts specifically pollen tubes from A.thaliana, but not those from A.lyrata (PubMed:23271953). Triggers endocytosis of MDIS1 in the pollen tube tip (PubMed:26863186). SUBCELLULAR LOCATION: Secreted Note=found at the micropylar end of the female gametophyte, possibly at the filiform apparatus of the synergid cell. Difuses to the surface of the funiculus of the ovule through the micropyle. SIMILARITY: Belongs to the DEFL family."}
{"protein": "MGTGGRGRPTPGLNVYEVFLSLQGEGKFVGEPQAFVRFSGCNLRCAYCDEPASRSSRRRALIRRVSGEVELELPVPCGPEDVVEVLVELEDLEDTFGTVSLTGGEPLVQPWGALKELIERLRERGFRVLLETNASLPDRAPLIDELADVVSADVKLPSHGPNMDDFPDRCLRFLERISAEVYAKVVLVDEECYQHAESALKGLHRLGVEPIYLQPATGSEHDLEDLWELAGLVNADVRVLPQVHKLVDFIPR", "text": "FUNCTION: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7- deazaguanine synthase family."}
{"protein": "MASSSALALRRLLSSSTVAVPRALRAVRPVAASSRLFNTNAARNYEDGVDRNHHSNRHVSRHGGDFFSHILDPFTPTRSLSQMLNFMDQVSEIPLVSATRGMGASGVRRGWNVKEKDDALHLRIDMPGLSREDVKLALEQNTLVIRGEGETEEGEDVSGDGRRFTSRIELPEKVYKTDEIKAEMKNGVLKVVIPKIKEDERNNIRHINVD", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
{"protein": "MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDLFIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTITKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPANSGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCTCCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVTEMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLPEDGLLEVQYFFKILDN", "text": "FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Microtubule inner protein (MIP) part of the dynein- decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the NDK family."}
{"protein": "MEEDKYQLVLHNDDLERMVLYDPNSKSLLVRNSTDMLRQKSKQLVLQQQIESPYSPMPSLRSPSIPTTPTLVGGLSSQSHNNNHPSTLHIMCPYCKRSYNNNNNNNINNNISTNNNNINNNSSNNLNNLNNNINNINNGIFNNNNNNNSNSNNNNISGGNNNTMDINGNSIVSGVIAPFNPSPYYRSPISEPPFISRDYFLLLQDSSKSGVNNNNNNNNNDSTTTNNNNNNNTTPPQQQQQQNSSGLNSEFLNIGYYKKFFKEDIKIGSGGFGSVYLCRHLINGVDLGEFAVKKVPVGENLPWLFRVLREVKALETLTKHRNIINYKHSWLEYDQPADFGPKVPCLYILMEYANNGNLQDYMAEKRDLIPENEIWSFFIDLCHGIGYLHHSGIIHRDIKPPNILIHQSYDSITDREVTHLMISDFGTCDTIGPLESLAPPLYKNNIKRTGNTGTIEYLAPELLQKGVNGEYNSDYDEKCDIWSLGILLYQMAYGTLPYRYSGDPFIDEDPNRNLPSLIDEIAGFSNNRLIFPQIPQRSRDLKDMITILLRAKPHERPTISQILSTHFIQSKTKHYTINPIHLPFTKRNKFKNTSVHNTTASTIKLRRKGSISTTNSTTSSSSSTATSSSLSSTTIATTSSSNAINNTTATTTTNSNLGNNNNNNTNALISSRISPIRKTQLVEENSEDSSNEIANINPNRSLIQPIVLSDTDNDDIIIDDDDDDDDSTNNNDTNNTDNTDDEMNSGDVVGIVNNKKSSYSRSSSIRSPSSSNKLRQRTISNSGGNNGIRKALPSLEAPRSGRFKRAAIVIQRGVRSSAVYQAFYMLQALFQVWLCFDQCSTCPNTFPSPILLYPLLLLSLIPILVVNNNNNSNNMNNNNNNNNINSNGQLAHLNGSGGGGIINNGNRDTKKINTIISIIRFIYYFVISVLLPKEISCKSTSHIIPILPPIADYVVFPLLSLFKNLTLLIINLIFIFYRD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MLAKKLVTAQKRGETRALCLGLGMVACSMMMYFFIGITIVPFYTKSVWTTETICKVLKANIKDKTHCTNSEGSEDEDIFHYPCLQVWVNLTASGQEVMLYHTEDTLERNPKCSYVPGNSENSKEVKARIETIASNFKKYQTFPCYYDPGGMQTNVILSRLYPPKGLLFTFLWPTLMFTGGCLIIVLVKISQYFSVLSARQ", "text": "FUNCTION: Probable regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel that modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca(2+)/voltage sensitivity of the KCNMA1 channel (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB1 subfamily."}
{"protein": "MSFRSVLLTALLSLSFTTTMQAAHHHYHRYTDKLHRQNHKKDLISPKPTEQEACNTSSLSKELIPLSEQRGLLSPICDFISERPCLHGVSVRNLKQALKNSAGTQIALDWSILPQWFNPRVSHAPKLSIRDFGYSAHQTVTEATPPCWQNCFNPSAAVTIYDSSYGKGVFQISYTLVRYWRENAATAGDAMMLAGSINDYPSRQNIFSQFTFSQNFPNERVSLTIGQYSLYAIDGTLYNNDQQLGFISYALSQNPTATYSSGSLGAYLQVAPTASTSLQIGFQDAYNISGSSIKWSNLTKNRYNFHGFASWAPRCCLGSGQYSVLLYVTRQVPEQMEQTMGWSVNASQYISSKLYVFGRYSGVTGHVFPINRTYSFGMASANLFNRNPQDLFGIACAFNNVHLSASPNTKRKYETVIEGFAAIGCGPYLSFAPDFQLYLYPALRPNKQSARVYSVRANLAI", "text": "FUNCTION: Facilitates L-arginine uptake, as part of the AaxABC system. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OprB family."}
{"protein": "MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYESKSLKSIQNVSHLILHMKQHILLLEIFVDVSSSVECLELRDTDLDTFRFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIPRFYLFYDLSTLYSLTERVKRITVENSKVFLVPCLLSQHLKSLEYLDLSENLIVEEYLKNSACEDAWPSLQTLILRQNHLASLEKTGETLLTLKNLTNVDISKNSFHSMPETCQWPEKMKYLNLSSTRIHSVTGCIPKTLEILDVSNNNLNLFSLNLPQLKELYISRNKLMTLPDASLLPMLLVLKISRNAITTFSKEQLDSFHTLKTLEAGGNNFICSCEFLSFTQEQQALAKVLIDWPANYLCDSPSHVRGQQVQDVRLSVSECHRTALVSGMCCALFLLILLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPSRNICYDAFVSYSERDAYWVENLMVQELENFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTVFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIEKKAIPQRFCKLRKIMNTKTYLEWPMDEAQREGFWVNLRAAIKS", "text": "FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein Cytoplasmic vesicle, phagosome membrane; Single-pass type I membrane protein Membrane raft Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. SIMILARITY: Belongs to the Toll-like receptor family."}
{"protein": "MKQFEIVTEPIQTEQYREFTINEYQGAVVVFTGHVREWTKGVKTEYLEYEAYIPMAEKKLAQIGDEINEKWPGTITSIVHRIGPLQISDIAVLIAVSSPHRKDAYRANEYAIERIKEIVPIWKKEIWEDGSKWQGHQKGNYEEAKREE", "text": "FUNCTION: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity). SIMILARITY: Belongs to the MoaE family."}
{"protein": "MSAILHLRAETKPMEARAALTPTTVRTLVSHGFKIYVEESAQSVFEAAEYAAAGAEVVATGSWRGAPRERIIVGLKELPEEDTFPLEHTHIQFAHCYKNQSGWREVLGRFQSGGGLLYDLEFLQDDRGRRVAAFGYYAGFAGAALGLRDWAWKQTHTDAEDLPAVAPYENEQALVSEVAAACEEAYKKGARKPRVLVIGALGRCGSGAVELLRQCGLHDKHIIRWDIAETARGGPFPEIAAADIFINCIYLSQPIAPFINMELLDRPDRKLRTIVDVSADTTNPHNPVPVYNVATVFSSPTVVVPTSQGPKLSVISIDHLPSLLPREASEAFASDLLPSLLQLPERDTAPVWLRAKELFQQHCERLSKEARL", "text": "FUNCTION: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L- lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysin biosynthesis. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the AlaDH/PNT family."}
{"protein": "MTTISLRKSNTRLPPEVNRVLYVRNLPFNITSEEMYDIFGKYGAIRQIRIGCDKATKGTAFVVYEDIYDAKNAVDHLSGFNVANRYLIVLYYQHAKMSKKFDQKKSEDEITKLQEKYGVSTKDK", "text": "FUNCTION: May be necessary for the splicing of pre-mRNA. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MEESLLPVYIHSAEYVELCDNVQSKVPRRASMVHSLIEAYGLLKEMRVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQWQLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGHLKQVV", "text": "FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of non-histone proteins. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones. SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation. SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily."}
{"protein": "MDGVVTDLITVGLKRGSDELLSSGIINGPFTMNSSTPSTANGNDSKKFKRDRPPCSPSRVLHLRKIPCDVTEAEIISLGLPFGKVTNLLMLKGKSQAFLEMASEEAAVTMVNYYTPITPHLRSQPVYIQYSNHRELKTDNLPNQARAQAALQAVSAVQSGSLALSGGPSNEGTVLPGQSPVLRIIIENLFYPVTLEVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVNAHYAKMALDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDFTRLDLPTGDGQPSLEPPMAAAFGAPGIISSPYAGAAGFAPAIGFPQATGLSVPAVPGALGPLTITSSAVTGRMAIPGASGIPGNSVLLVTNLNPDLITPHGLFILFGVYGDVHRVKIMFNKKENALVQMADANQAQLAMNHLSGQRLYGKVLRATLSKHQAVQLPREGQEDQGLTKDFSNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVTVDDLKNLFIEAGCSVKAFKFFQKDRKMALIQLGSVEEAIQALIELHNHDLGENHHLRVSFSKSTI", "text": "FUNCTION: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes FAS exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U)."}
{"protein": "MWSGQPHPDEGHPPPLEAVPVPWKSVGPCKSHRESLGGLPETPAGEEAQGEEGPAATQLDVSRLRSSSMEIREKGSEFLKEELHKAQKELKLKDEECERLSKVREQLEQELEELTASLFEEAHKMVREANMKQAASEKQLKEARGKIDMLQAEVTALKTLVITSTPASPNRELHPQLLSPTKAGPRKGHLRHKSTSSALCPAVCPVAGHILTPDKEGKEVDTTLFAEFQAWRESPTLDKTSPFLERVYREDVGPCLDFTMQELSALVRAAVEDNTLTIEPVASQTLPAVKVAAVDCGHTNGFRAPIDTTCALSGLACACRHRIRLGDSESHYYISPSSRARITAVCNFFTYIRYIQQGLVRQDAEPMFWEITRLRKEMSLAKLGFFPHEA", "text": "FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May also activate RAB8A and RAB8B (By similarity). SIMILARITY: Belongs to the SEC2 family."}
{"protein": "MLTLARQQQRQNIRWLLCLSVLMLLALLLSLCAGEQWILPGDWFSPRGELFVWQIRLPRTLAVLLVGAALAISGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPNWALGLCAIAGALIITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSVDLRQLMYWMMGGFGGVDWRQSWLMVALIPVLLWICCQSRPMNMLALGEISARQLGLPLWFWRNVLVAATGWMVGVSVALAGAIGFIGLVIPHILRLCGLTDHRVLLPGCALAGASALLLADIVARLALAAAELPIGVVTATLGAPVFIWLLLKAGR", "text": "FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily."}
{"protein": "MEARGLACESSNSAVKAPSIEDFVLVKPISRGAFGKVYLARKKCNSKLYAIKVVKKAEMVDKNMTEQMRAERDALALSKSPFIVHLFYSLQTATKVYLVMEYLIGGDVKSLLHIYGYFDEDMSLKYISEVALALDYLHRHSIIHRDLKPDNMLISNEGHIKLTDFGLSKVKLDRELNLMDILTTPSLVKPTKDYFRTPGQVLSLISSLGLNTPVIEGKRHSSTVLGSPMSCGKVKQRNRSLGSPLMKRRAEYMNSPVCTSRALASNSVFSPVLLARSLTPRLLKSGKRLDTMSVGSTHSCMLPSTTDSENCVSPMWEDEQNLHDVENIPQLNGREVDNRKSRNVPLTPVEKRKTLPARAQDHRPVFTPLNNQVTNSRNIKPDLSAKRLQFGATDNSATPLEKTVPHQSVGNGLIKPEPLKELKSSVKRAFEEVEKSPEQAEILFKKNDAAYERSFQIPEKTSRAHTGLTGIFSIVGLDDVKSAPKCQQFNERTGPKQSSPIAVAKNLFCELEDQGEEGGKAEPNSSSSTSPGDERNIRRSLSLESDVSAHEMSLVANTPQKLSDAKQEVLSSSFEELDENEISAVTPMARPTVATPKHSSAKQRRGECERSLLDHPHGLSDSMIKSPGFLKPKNVVAFRSYCSSINRSCTSHLSLASFDAMEMSASASFHNAVTPVQKKRPSLSNSLYQTPQQMVVSHTPYRTPKSVRRGPERVEGAPILGTPDYLAPELLLGKPHDFMVDWWALGVCLFEFLTGVPPFNDETPQLVFQNILNRDIPWPDGEEELTLNSRNAIEILLTMDTLKRAGLKELKDHPFFDGVDWENLHHQTMPFIPQPDNETDTSYFEARNTAQHLTVSGFSL", "text": "FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of arpp19 and ensa at 'Ser- 62' and 'Ser-74', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the ppp2r2d (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). May be involved in megakaryocyte differentiation (PubMed:19460416). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cleavage furrow Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes (By similarity). Upon mitotic exit moves to the cleavage furrow. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family."}
{"protein": "MDQSARYADLSLKEEDLIAGGKHILVAYKMKPKAGHGYLEASAHFAAESSTGTNVEVSTTDDFTKGVDALVYYIDEATEDMRIAYPMDLFDRNVTDGRMMLVSVLTLIIGNNQGMGDIEHAKIHDIYFPERAIQLFDGPSKDISDMWRILGRPIENGGYIAGTIIKPKLGLRPEPFAAAAYQFWLGGDFIKNDEPQGNQVFCPLKKVLPLVYDSMKRAQDETGQAKLFSMNITADDHYEMMARADFGLETFGPDADKLAFLVDGFVGGPGMITTARRQYPNQYLHYHRAGHGMITSPSAKRGYTAFVLAKISRLQGASGIHVGTMGYGKMEGEGDDRNIAYMIERDEAQGPVYFQKWYGMKPTTPIISGGMNALRLPGFFENLGHGNVINTAGGGSYGHIDSPAAGAISLKQAYECWKAGADPIEFAKEHKEFARAFESFPKDADAIFPGWREKLGVHK", "text": "FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuBisCO large chain family. Type II subfamily."}
{"protein": "MSTIKYRAACDHCSATKIKCTQERPQCTRCRALGRDCHYSRSLRAGKPPRSSQGLNRKISNAPVLPRQNTPVSNPTSMSSKPEHWPTMPTSYPTPQAAAPTAEIFHFPDLSSAATSSSSSPANTDWFFDFNSGSADGLGDLTPPLVVTAPHLPPLDHDLKHPVFPTQGIHFGAFADLISLPPASPLLPSPSLADGDRCAKLATETLNSLYDMPANHLHGSGNRHPSVDQTLSTCARAVQAIHELVNCSCQKDLYLPMLIIIVASKIVAWYQAVAYIRDPGTGFADGKQCFREVVVEGPLNIGAYQLDDEVGWTLKNQIVLGQLQRLNEAVNIYDRRYCSDSLGGQMTEGGKLYASMVGFVKSTLQFTIHALEGRIRSGHPR", "text": "FUNCTION: Transcription factor that regulates the expression of the hps1-dma1 gene cluster that probably mediates the biosynthesis a derivative of cyclopiazonic acid (CPA) (Probable). Further studies are required to whether the CPA-like hps1-dma1 cluster is functional or a non-functional relic reflecting evolution of D.septosporum (Probable). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAEEESVPKMVAPEDDIREIHSRLDEIERRLDFVWGEVYQRFGKRIGRDIGILYGLVIGLYLCMLYILLGVAFR", "text": "FUNCTION: Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MtrG family."}
{"protein": "MFIQLLILSYAILLQLIATQVADKQLPNLTKQCEPTSQTIYDFHVPTLDGSEKSLAEYRGKVLLLVNVATYCAYTFQYNDFNPMLENNSNGTLKILAFPCNQFLLQEPAENHELLNGLKYVRPGNGWEPHGNMHIFGKVEVNGDDHHPLYKFLKEHCPQTVPIIGDRHQLMYNPIGTNDIIWNFEKFLIDKKGHPRYRFHPSAWVQGSVIAPFIDELEREI", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glutathione peroxidase family."}
{"protein": "MINSDAQSAQKQVEVEKPDEKYSAPRLLPPIPDSYQPAKAITKIPATSSLEDILAILERDGGVILTDFVSLQELDKIDEELEPYTKSSIADDDSYNNFIGKKTLVIPGLVGKSDTIANILDTNETIDKLLKVILEERYPAVFEQHTEELVVDPLLSICMGFHVGHGSPRQALHRDDMIFSSKHRPDMKINEVDGFSCFLAGTRITRENGGTMVILGSHKWEHDRRGRPDEVSFLEMERGSAFIFLSTLAHGAGYNTIPGEVRKITNLVFCRGTLRTEENQFLCVPRSKVLKMSPKMQTLLGFKKPAGSWLGMVENEDPAKDLEAIYEKMLK", "text": "FUNCTION: Dioxygenase; part of the gene cluster that mediates the biosynthesis of swainsonine (SW), a cytotoxic fungal alkaloid and a potential cancer therapy drug (PubMed:28381497, PubMed:32786262). Swainsonine production occurs via a multibranched pathway and is dispensable for fungal colonization of plants and infection of insect hosts (PubMed:32786262). The first step of swainsonine biosynthesis is the production of the precursor pipecolic acid (PA) via conversion of L-lysine (Lys) to 1-piperideine-6-carboxylate (P6C) by the aminotransferase swnA, the latter being further reduced to PA by the reductase swnR (PubMed:32786262). PA can be converted from lysine by both the SW biosynthetic cluster and the unclustered genes such as lysine cyclodeaminase (PubMed:32786262). The PKS-NRPS hybrid synthetase swnK uptakes and condensates PA and malonyl-CoA with and without skipping of the ketoreductase (KR) domain in order to produce 3 intermediates, 1-oxoindolizidine, (1S)-1-hydroxyindolizin, and (1R)-1- hydroxyindolizine; with the transisomer (1S)-1-hydroxyindolizin being predominant (PubMed:32786262). The terminal thioester reductase (TE) domain of swnK is involved in reduction of the thioester bond to release the intermediate aldehydes (PubMed:32786262). The oxidoreductase swnN could contribute to the reduction of 1- oxoindolizidine to (1S)-1-hydroxyindolizin and (1R)-1- hydroxyindolizine, contributing to the major route of SW production (Probable). The dioxygenase swnH2 would be responsible for the oxidization of (1R)-1-hydroxyindolizine into (1R,2S)-1,2- dihydroxyindolizine and of (1S)-1-hydroxyindolizin to yield both (1R,2S)-1,2-dihydroxyindolizine and (1S,2S)-1,2-dihydroxyindolizine (PubMed:32786262). The dioxygenase swnH1 then performs the conversion of the 1,2-dihydroxyindolizine epimers to SW (PubMed:32786262). SIMILARITY: Belongs to the PhyH family."}
{"protein": "MRCPKCLLCLSALLTLLGLKVYIEWTSESRLSKAYPSPRGTPPSPTPANPEPTLPANLSTRLGQTIPLPFAYWNQQQWRLGSLPSGDSTETGGCQAWGAAAATEIPDFASYPKDLRRFLLSAACRSFPQWLPGGGGSQVSSCSDTDVPYLLLAVKSEPGRFAERQAVRETWGSPAPGIRLLFLLGSPVGEAGPDLDSLVAWESRRYSDLLLWDFLDVPFNQTLKDLLLLAWLGRHCPTVSFVLRAQDDAFVHTPALLAHLRALPPASARSLYLGEVFTQAMPLRKPGGPFYVPESFFEGGYPAYASGGGYVIAGRLAPWLLRAAARVAPFPFEDVYTGLCIRALGLVPQAHPGFLTAWPADRTADHCAFRNLLLVRPLGPQASIRLWKQLQDPRLQC", "text": "FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N- glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family."}
{"protein": "MKIRNACAVLIEVLLFILEGVTGARKISTFSGPGSWPCNPKCDGRTYNPSEECCVHDTILPFKRINLCGPSCTYRPCFELCCPESYSPKKKFIVKLKVHGERSHCSSSPISRNCKSNKIFHGEDIEDNQLSLRKKSGDQP", "text": "FUNCTION: Probable ligand of the IGFLR1 cell membrane receptor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IGFL family."}
{"protein": "QQCVKKDELCIPYYLDCCEPLECKKVNWWDHKCIG", "text": "FUNCTION: Suppresses strongly the sweet taste responses in the rat with high specificity to sucrose, glucose, glycine, and saccharin. This effect is reversible, but complete recovery of the suppressed responses required at least 3h. Gurmarin showed no effect or only a very weak effect on the sweet taste sensation in humans."}
{"protein": "MAQSEVDSVDCVTSDRDGDIGNQSDDSSNSSLFKTQCVPSPTRKQRIPTVKCVPSLASVETDSSSDSSLEPRPLTLKAIFERFKKKKRKKRKKRKYKPKLRRQGRPSGTRNIRRSQIDAKQIKDKGAVFPFLESESGRKTLPWKKILTYEQAVARGFFHHIEKLKYEHHLKECLSQMHAGEDLEKEDFDSRRHKYMDDDGPLSPIEEPSTEDEATDPQSECDIKLVEDSCFIISTEFPRKRNLEQGKIKKESAFSKKSKAKDATQRGNRRSWKGGEHACLHSEVS", "text": "FUNCTION: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKKHLHHKVSGSCDPGDRSPKEKGRSQGIRNLLILISLSIIPYLSCLGGDFVFDDAESIVNNPIVNGKDPLLQIFSRDFWGRSISSSNSHKSYRPVTTFTFWLNYKLHETSTLGYHVVNIICHTVATLVFYKLGKQLEHIFDFFNIAFSASILFAVHPVHTEAVANITGRAELLMTIFSLAALILHVKNREINCKFVLLVILSTLSKEQGLMTIPIAICIDFLAHRSCRSNFVRMICLLVAIGFLRMMVNGFEAAKFTKLDNPTAFLNSKFYRMINYTYIWLYHAYLLVIPVNLCFDYSMGCISSITTMWDLRALSPVLIFTIVIIGVKFQNECRAFTLSSLMGIISFLPASNIFFTVGFSIAERVLYLPSAGFCLLCAIIFKKLSVHFKNADVLSITLILLLISKTYRRSGEWKTELSLYSSGLSVCPTNAKIHYNLGKVLGDNGLTKDAEKNYWNAIKLDPSYEQALNNLGNLLEKSGDSKTAESLLARAVTLRPSFAVAWMNLGISQMNLKKYYEAEKSLKNSLLIRPNSAHCLFNLGVLYQRTNRDEMAMSAWKNATRIDPSHSQSWTNLFVVLDHLSQCSQVIDLSYQALSSVPNESRVHMQIGSCHAKHSNFTAAENHIKSAIDLNPTSVLFHANLGILYQRMSRHKEAESQYRIVLALDSKNIVAKQNLQKLEEHNCYNSTLP", "text": "FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Endoplasmic reticulum. SIMILARITY: Belongs to the TMTC family."}
{"protein": "MKILVTGGAGFIGSAVVRHIINNTQDSVVNVDKLTYAGNLESLADVSDSERYAFEHADICDAVAMSRIFAQHQPDAVMHLAAESHVDRSITGPAAFIETNIVGTYVLLEAARNYWSALNDEKKKSFRFHHISTDEVYGDLPHPDEANNNEALPLFTETTAYAPSSPYSASKASSDHLVRAWKRTYGLPTIVTNCSNNYGPYHFPEKLIPLVILNALEGKALPIYGKGDQIRDWLYVEDHARALYTVVTEGKAGETYNIGGHNEKKNIDVVLTICDLLDEIVPKEKSYREQITYVADRPGHDRRYAIDADKISRELGWKPQETFESGIRKTVEWYLANTNWVENVKSGTYQSWIEQNYEGRQ", "text": "FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6- deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily."}
{"protein": "MENDMEEKFEDWKGKEAIPGKHGGIRAASIVCVVVMMENIVFIANGFNFVKYFMGSMHYTPATAANMVTNFMGTSFLLTLFGGFIADSFVTHFTTFIVFCCIELMGLILLTFQAHNPKLLPEKDKTPSTLQSAILFTGLYAMAIGTGGLKASLPSHGGDQIDRRNPRLISRFFDWLYFSICSGCLLAVTVVLWIEEKKGWIWSFNISVGILATALCIFTVGLPFYRFKRPNGSPLKKIAIVIISAARNRNKSDLDEEMMRGLISIYKNNSHNKLKWIDKATLNKNISETEVEETRTFLGLLPIFGSTIVMSCCVAQLSTFSAQQGMLMNKKLFHSFEIPVPSLTAIPLIFMLLSIPLYEFFGKKISSGNNNRSSSFNLKRIGLGLALSSVSMAVSAIVEAKRKHEVVHNNFRISVLWLVFQYLMLSVSDMLTLGGMLEFFYREAPSNMKSISTALGWCSTALGFFLSTTLVEVTNAVTGRLGHQWLGGEDLNKTRLELFYVLLCVLNTLNLLNYIFWAKRY", "text": "FUNCTION: Involved in abscisic acid transport. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family."}
{"protein": "MDIEAYFERIGYKNSVNKLDLATLTEVLQHQMRAVPFENLSMHCGEAMCLGLEATFDHIVRKKRGGWCLQVNHLLYWALTKMGFETTMLGGYVYITPVNKYSSEMVHLLVQVTISDRNYIVDSAYGSSYQMWEPLELTSGKDQPQVPAIFRLTEENGTWYLDQIRREQDVPNQEFVNSDLLEKSKYRKIYSFTLEPRTIEDFEYVNTYLQTSPASVFVSTSFCSLQTSEGVCCLIGSTLTSRRFSYKDNVDLVEFKSLTEEEIEDVLKTTFGISLEKKFVPKHGELVFTI", "text": "FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Acetylates both arylamines and arylalkylamines. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the arylamine N-acetyltransferase family."}
{"protein": "MPRFRDLSHNCRPSEAPRVMEPKNRDRTVDPAVLEMLVKSKDDKVITAFDRFVAQQPQCKIGYEGICCRFCMAGPCRIKATDGPGSRGICGASAWTIVARNVGLMILTGAAAHCEHGNHIAHALVEMAEGKAPDYSVKDEAKLKEVCRRVGIEVEGKSVLELAQEVGEKALEDFRRLKGEGEATWLMTTINEGRKEKFRTHNVVPFGIHASISELVNQAHMGMDNDPVNLVFSAIRVALADYTGEHIATDFSDILFGTPQPVVSEANMGVLDPDQVNFVLHGHNPLLSEIIVQAAREMEGEAKAAGAKGINLVGICCTGNEVLMRQGIPLVTSFASQELAICTGAIDAMCVDVQCIMPSISAVAECYHTRIITTADNAKIPGAYHIDYQTATAIESAKTAIRMAIEAFKERKESNRPVYIPQIKNRVVAGWSLEALTKLLATQNAQNPIRVLNQAILDGELAGVALICGCNNLKGFQDNSHLTVMKELLKNNVFVVATGCSAQAAGKLGLLDPANVETYCGDGLKGFLKRLGEGANIEIGLPPVFHMGSCVDNSRAVDLLMAMANDLGVDTPKVPFVASAPEAMSGKAAAIGTWWVSLGVPTHVGTMPPVEGSDLIYSILTQIASDVYGGYFIFEMDPQVAARKILDALEYRTWKLGVHKEVAERYETKLCQGY", "text": "FUNCTION: The beta subunit (this protein) generates CO from CO(2), while the alpha subunit combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl- CoA, is transferred to the alpha subunit by a corrinoid iron-sulfur protein."}
{"protein": "MGSCARLLLLWGCTVVAAGLSGVAGVSSRCEKACNPRMGNLALGRKLWADTTCGQNATELYCFYSENTDLTCRQPKCDKCNAAHPHLAHLPSAMADSSFRFPRTWWQSAEDVHREKIQLDLEAEFYFTHLIMMFKSPRPAAMVLDRSQDFGKTWKPYKYFATNCSATFGLEDDVVKKGAICTSKYSSPFPCTGGEVIFKALSPPYDTENPYSAKVQEQLKITNLRVQLLKRQSCPCQRNDLNDEPQHFTHYAIYDFIVKGSCFCNGHADQCIPVHGFRPVKAPGTFHMVHGKCMCKHNTAGSHCQHCAPLYNDQPWEAADGKTGAPNECRTCKCNGHADTCHFDVNVWEASGNRSGGVCDDCQHNTEGQHCQRCKPGFYRDLRRPFSAPDACKPCSCHPVGSAVLPANSVTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYGCRPCDCAGSCDPITGDCISSHTDIDWHHEFPDFRPVHNKSEAAWEWEDAQGFSALLHSGKCECKEQTLGNAKAFCGMKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPESWTDRGCTCPILNPGLEYLVAGHEDVRTGKLIVNMKSFVQHWKPSLGRKVMDILKRECK", "text": "FUNCTION: May play an important role in neural, kidney and vascular development. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix."}
{"protein": "MQLTSFTDYALRTLIYLASLPKDELTNITEVTDLFGVSRNHMVKVINRLGQLGYVHTVRGKNGGIRLMKAPQEITVGGVVRDLEPLDLVNCSVEFCHITPACRLKEKLAKAKLAFLAELDDCTIEELLSDNSELLILLARP", "text": "FUNCTION: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity."}
{"protein": "MTNWLQKRVRLSPKETALVFEGKEETFEEISEAVERLAGKLFALGIRKDEMIALLGKNDRMTFLLIHALQQLGAVTLFLNNRLTKKEIAYQLANAEVKQVIVADTFEDKVGAGISYSELAETDYKEPELLETWDLSRTASIMYTSGTTGKPKGVIQTYENHWWSAVASVLNLGLTEKDSWLCAVPIFHISGLSIMMRSVIYGIPVYLEEHFDEEKITQLLESGKVSTISVVTSMLERLLKIHGGSYHPNVRTILLGGGPASKTVLEICKQRDIPLVQSFGMTETASQIVTLPPKDALNKIGSSGKALFPAEVKIADDGEILLKGPSITPGYLHNKKATEASFVDGWFKTGDIGYLDEEGFLFVVERRSDLIISGGENIYPTEIEHVIGEYVAVKEVAVIGQPDDKWGSVPVAFIVAEETFDEDELQLICQTNLASYKIPKQIIIVEKLPKTASGKIQRNKLKERHSK", "text": "FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. MenE subfamily."}
{"protein": "MFDIKQIFNKTYEYLIIIITLILISIIVIANIFIVGPSEEAIVLRLGKLNRTLDSGIHVKIPLIEEKFIVPVKIVQEIKFGFLISPSDIRENDNANDESRIITGDLNIINIEWLVQYKIRDPYSFKFKVEDPETTIKDIAKSSMNRLIGDNTIFEIINDNRVGITEGVKSSMNEIIDNYNLGIDVVQVQIRNALPPKGKVYEAFEDVNIAIQDKNKYINEGRKEFNQIVPKIKGEALKVIEEARGYKESRINNALADTEIFNAILDAYLKNPDITKERLYNETMKEILENKDNIELIDKNFKNFLPFKEVK", "text": "FUNCTION: HflC and HflK could encode or regulate a protease. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily."}
{"protein": "MDNGHGYEEFELLEDGSLGECSTQVANATFLTISKLICLVVAFKFIKHIPISTTVRVYVHVFASTFTVMWFSRNHLQSAIIYNMFSLISLALAIKQFSGYIILAGNISLLIALQNFCRHYRSEDYFLSIRGILMIHIMRLTTVAFNLEKANSNKFRFVQFSSYVEYIYFPPFIIFGPYLSFEQFFKMRDKKWTGSENELGFIIQSLLAIFNAITLAIISSCHFEFFEPSSQFMEDALTAMSFRFSHYFVCLSTQAFVLMLGSDVVVANPLNIEFSRSTLQTVSEWNKPFHTFLHENIFKRRLFNSTACNVFFTFAVSSLLHGLDFQMTITLLALGFIAYSETVFRKRLSARYSMCVAAKACPVRSNSLSCKHRHSNKTGRALIINLFFLMLSMYHLVFTGMTFTDDYSAIGYPFDHAWKIWGSHYYSSFMISFLFLALSKII", "text": "FUNCTION: Key regulator of the Wnt signaling pathway that mediates lipid modification of Wnt proteins (PubMed:10444600, PubMed:15020416, PubMed:9288750). Acts as a protein-serine O-palmitoleoyltransferase that catalyzes the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins (By similarity). Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors (By similarity). Has a role in cell specification, specifically in blastomere signaling (PubMed:10444600, PubMed:15020416, PubMed:9288750). Involved in cytosketetal polarity (PubMed:10444600, PubMed:15020416, PubMed:9288750). Required for the orientation of mitotic spindle axis (PubMed:9288749, PubMed:10444600, PubMed:15020416, PubMed:9288750). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family. Porcupine subfamily."}
{"protein": "MARNGSLEEFLGVAVDAAKRAGEIIRKGFHETKHVVHKGQVDLVTETDKACEDLIFNHLKQHFPSHKFIGEETSAATGDFDLTDEPTWIVDPVDGTTNFVHGFPSVCVSIGLTIGKIPTVGVVYDPIIDELFTGINGKGAYLNGKPIKVSSQSELVKSLLGTEVGTTRDNLTVETTTRRINNLLFKVRSLRMCGSCALDLCWVACGRLELFYLIGYGGPWDVAGGAVIVKEAGGVLFDPSGSEFDITSQRVAATNPHLKEAFVEALQLSEYVS", "text": "FUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides. SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
{"protein": "MFLFSDGLQSINNNNRRKRIVKNAYIPSRGIRKIPHLSTLLPEFHIYKDGKGAEAVVGWGLRPTTHKARAFATEHQLPFIALEDGFLRSLGLGVSGYPPYSIVYDDIGIYYDTTRPSRLEQLILAADTMPSETLAQARQAMDFILQHHLSKYNHAPELSDDHPLRSPSKSETVLIIDQTFGDMAIQYGGADASTFELMFQTALNENPQADIWVKTHPDVLCGKKQGYLTQLVQQHRVHLLAEDINPISLLQNVDKVYCVTSQMGFEALLCGKPLTTFGLPWYAGWGVSDDRHPKIGSLIQTQRRAPRNLLQLFAAAYLQYSRYLNPNTGEAGSLFDVIDYLATVKRKNDKLRGELYCVGMSLWKRAVAKPFFNVPSCRLKFISSTQKLARVKLSDDARILAWGNGKEAIVRFAEQHHIPLLRMEDGFIRSVGLGSNLVPPLSLVTDDMSIYFNAETPSRLEYILQNQNFDDQDFQTALKLQKMLTENHISKYNVGSSDFTAPSTDKTVILVPGQVEDDASIRYGSPQIYRNLDLLRTVRERNPNAYIIYKPHPDVVSGNRIGHISPDDAARYADQTAEQADILTCLQYADEIHTMTSLTGFEALLRGKKVSCYGLPFYAGWGLTQDLLPIPRRSRRLELWQLVAGTLIYYPDYIHPKTHQAINAETAAQILIRQKNMQKNNNGLHRGCFAKKLGKIKQLYRSFK", "text": "FUNCTION: Involved in the phospholipid modification of the capsular polysaccharide, a strong requirement for its translocation to the cell surface. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MKLHSSSKIQNHAWLSDARMNNPSETSKSPESGDGNTGTQTNGLDFQKQAVPIGAITSAQAQALLGHLHQVQLAGTSLQAAAHSLNVQTKFKEEPGEPMQVVQPSQQPSLQAAIPQTQLMVAGGQIAGLTLTPAQQQMLLQQAQAQLLAAAVQHSASQQHNAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQYVLVHPTTNLQSAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPVQQLPQSQTTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENITSDSTLTNQSVLNSPGHGMEGLNRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGSSSSPIKSLFSSPNPLVASTPSLVTSSPATTLTVNPVLPLTSAAAITSFHIPGTTGTSSANTATVISTAPPVSSVLTSPSLSSSPSATAASSEASTAGETSTTQTTSTPMTSSLNTGQVMVTASGIHTAAATALQGAAQLPTNASLAAMAAAAGLNPGLMAPSQFAAGGALFSLNPGALGSALSPALMSNSTLATIQALASSGSLPITSLDAAGNLVFANAGGTPNIVTAPLFLNPQNLSLFTSNPVSLISAASAGATGPITSLHATTSSIDSIQNALFTMASASGAASTTTSASKAQ", "text": "FUNCTION: Transcription factor that binds to the octamer motif (5'- ATTTGCAT-3') and activates the promoters of the genes of some small nuclear RNAs (snRNA) and histone H2B (PubMed:2017364). In vitro does not bind to variant octamer sequences, such as the H2B octamer 5'- GTTTGCAT-3', although binding has been observed in vivo during early embryogenesis, suggesting that interactions between pou2f1 and other factors might be required for octamer-dependent H2B transcription (PubMed:1990276, PubMed:2017364, PubMed:1406629). Acts downstream of Notch signaling during radial glia formation (PubMed:18241856). May be important for gastrulation, possibly through the regulation of an FGF- type signaling pathway (PubMed:7542467). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Retained in the cytoplasm during early development, then gradually translocates to the nucleus around the mid-blastula transition (MBT). SIMILARITY: Belongs to the POU transcription factor family. Class-2 subfamily."}
{"protein": "MDCPIPQTELDEIYAFATDLARKAGQLLLERVNDRNSEQVYAEKENAVDLVTQTDEDVESLIKTAIQTKYPAHKFLGEESYAKGQSREYLIDEQPTWCVDPLDGTVNFTHAFPMFCVSIGFIVNHYPVIGVIYAPMLNQLFSSCLNRGAWLNEMQQLPLIRKPSIPPLPATAPSKCIFACEWGKDRRDIPDGTLQRKIESFVNMAAERGSRGGKGGMVHGVRSLGSATMDLAYTAMGSVDIWWEGGCWEWDVAAGIAILLEAGGLVTAANPPEDIEGPIEPVKLGSRLYLAIRPAGPSETETGRETQERTVREVWRRVRQLDYERPTRQS", "text": "FUNCTION: Not known. Probably involved in quinate metabolism. SIMILARITY: Belongs to the inositol monophosphatase superfamily."}
{"protein": "MSSYQKELEKYRDIDEDEILKTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDREALLQYLEQQALEVKERDDLVPFTGEKKGKPYIQPKREIPVEEQVTLEPELEEALAHATDAEMCDIAAILGMYTLMSNKQYYDAICSGEICNTEGISSVVQPDKYKPVPDEPPNPTNIEEILKSVRSNDKEVEEVNLNNIQDIPIPMLTELCEAMKTNTHVRSFSLVATRSGDPVANAVADMLRENRSLQSLNIESNFISSTGLMAVLKAVRENATLTELRVDNQRQWPGDAVEMEMATVLEQCPSIVRFGYHFTQQGPRARAAQAMTRNNELRRQQKKR", "text": "FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments. SIMILARITY: Belongs to the tropomodulin family."}
{"protein": "MTLSGSGSASDMSGQTVLSADDADIDVVGEGDEALDKDSECESTAGHTDEVGELGGKEIPRSPSGSGTEAEGKGESQQQQQEGIQNKPKNSLVKPPYSYIALITMSILQSPQKKLTLSGICEFISNRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPQSEDMFDNGSFLRRRKRFKRQQQDSLREQTALMMQSFGAYSLASPYGRHYGLHPAAYTHPAALQYPYIPPVGHMLPPAVPLLPSSELTRKAFSSQLSPSLQLQLSSLSSTAASIIKSEPSSRPSFSIENIIGVSAASSAAPHTFLRPPVTVQSALMSHQPLALSRSTAAIGPILSVPTNLISGQFLPTAAAAVAKWPAQ", "text": "FUNCTION: Transcriptional repressor that is an essential upstream regulator of neural crest determination and mesoderm induction. Functions by recruiting the transcriptional corepressor tle4. Also acts in a negative auto-regulator loop by inhibiting the transcription of its own gene. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "HSQGTFTSDYSKHLDSRYAQEFVQWLMNT", "text": "FUNCTION: Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family."}
{"protein": "MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVNAAMVFEFLYKMCDVMTAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKGQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIDKQGKGGTTDDAGKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEYELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFESKLNYSDHDVIKWVRYIGRSGIYETRC", "text": "FUNCTION: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP50 is a subunit of the plasma membrane adaptor. The complex binds polyphosphoinositide- containing lipids (By similarity). SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. SIMILARITY: Belongs to the adaptor complexes medium subunit family."}
{"protein": "MSSQSLHDCLRGRCLGVLRRMEIIGRFRYYFQHPWSRLLVSYLVTFFNFLIFAEDPVSHSQKEAHMSVVGNCFSFIISKYPAGFWSVLKVLLWVLAIICGLIAGKFIFHRRLFGRVLRLKMFREDHGSWMTMFFSTILSLFIFSHIYNLLLLMSVRMRPYMVTEYMGIRNESFMKMAAVGTWMGDFVTAWMVTDMMLQDTHYPDWGRTARHLWRQGHNRIVLFWTVLICLTSVVVLVISTDWIRWDNLNRGFLPSDEVSRAFLASFILVFDLLIVMQDWEFPHFMGDLDMNLPGLSTTQLKIRLPVCKRIFKEEYHIHITGKWFNYGIIFLVLILDLNMWKNQIFYKPYEYGQYVGPGEKIYTVEDPDTLQDFNRSMLTWEWRSTNIDPRTNQTFNQSNAI", "text": "FUNCTION: May be involved in endoplasmic reticulum (ER) stress-induced cell death pathway. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM117 family."}
{"protein": "MAEPETCDLFVIGGGINGAGVARDAAGRGLKVVLAEKDDLAQGTSSRSGKLVHGGLRYLEYYEFRLVREALIEREVLLNAAPHIIWPMRFVLPHSPQDRPAWLVRLGLFLYDHLGGRKKLPGTRTLDLKRDPEGTPILDQYTKGFEYSDCWVDDARLVALNAVGAAEKGATILTRTPVVSARRENGGWIVETRNSDTGETRTFRARCIVNCAGPWVTDVIHNVAASTSSRNVRLVKGSHIIVPKFWSGANAYLVQNHDKRVIFINPYEGDKALIGTTDIAYEGRAEDVAADEKEIDYLITAVNRYFKEKLRREDVLHSFSGVRPLFDDGKGNPSAVTRDYVFDLDETGGAPLLNVFGGKITTFRELAERGMHRLKHIFPQMGGDWTHDAPLPGGEIANADYETFANTLRDTYPWMPRTLVHHYGRLYGARTKDVVAGAQNLEGLGRHFGGDFHEAEVRYLVAREWAKTAEDILYRRTKHYLHLTEAERAAFVEWFDNANLVA", "text": "FUNCTION: Catalyzes the oxydation of D-erythritol 1-phosphate to D- erythrulose 1-phosphate. SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family."}
{"protein": "MISFCPVCGKSVKVSFKFCPYCGKALPVEEDGGTQSAVTPHVSSVPGSRRDLNSSFETSPKKVKCSHTVTSLPLSRHSDCDSSGSDNTLTSPDRATGTRSRPLTPKGSPLSNRQSPQTLKRTRVTTSLQALATGTELTDQNGKHWTLGALQIRDDQGILYEAEPTSAVPSESRTQKWRFSLKLDSKDGRLFNEQNFFQRVAKPLQVNKWKKQFLLPLLAIPTCIGFGIHQDKYRFLVFPSLGRSLQSALDDNPKHVVSERCVLQVACRLLDALEYLHENEYVHGNLTAENVFVNPEDLSQVTLVGYGFTYRYCPGGKHVAYKEGSRSPHDGDLEFISMDLHKGCGPSRRSDLQTLGYCMLKWLYGSLPWTNCLPNTEKITRQKQKYLDSPERLVGLCGRWNKASETLREYLKVVMALNYEEKPPYATLRNSLEALLQDMRVSPYDPLDLQMVP", "text": "FUNCTION: Inactive kinase that suppresses ERK activity by promoting phosphatase activity of DUSP3 which specifically dephosphorylates and inactivates ERK in the nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. VRK subfamily."}
{"protein": "MAPDSDPFPEGPLLKLLPLDARDRGTQRCRLGPAALHALGARLGSAVKISLPDGGSCLCTAWPRRDGADGFVQLDPLCASPGAAVGASRSRRSLSLNRLLLVPCPPLRRVAVWPVLRERAGAPGARNTAAVLEAAQELLRNRPISLGHVVVAPPGAPGLVAALHIVGGTPSPDPAGLVTPRTRVSLGGEPPSEAQPQPEVPLGGLSEAADSLRELLRLPLRYPRALTALGLAVPRGVLLAGPPGVGKTQLVRAVAREAGAELLAVSAPALQGSRPGETEENVRRVFQRARELASRGPSLLFLDEMDALCPQRGSRAPESRVVAQVLTLLDGASGDREVVVVGATNRPDALDPALRRPGRFDREVVIGTPTLKQRKEILQVITSKMPISSHVDLGLLAEMTVGYVGADLTALCREAAMHALLHSEKNQDNPVIDEIDFLEAFKNIQPSSFRSVIGLMDIKPVDWEEIGGLEDVKLKLKQSIEWPLKFPWEFVRMGLTQPKGVLLYGPPGCAKTTLVRALATSCHCSFVSVSGADLFSPFVGDSEKVLSQIFRQARASTPAILFLDEIDSILGARSASKTGCDVQERVLSVLLNELDGVGLKTIERRGSKSSQQEFQEVFNRSVMIIAATNRPDVLDTALLRPGRLDKIIYIPPPDHKGRLSILKVCTKTMPIGPDVSLENLAAETCFFSGADLRNLCTEAALLALQENGLDATTVKQEHFLKSLKTVKPSLSCKDLALYENLFKKEGFSNVEGI", "text": "FUNCTION: ATP-dependent chaperone, which plays an essential role in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre- ribosomal particles (PubMed:35354024). Acts together with AFG2A, AIRIM and CINP (PubMed:35354024). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, spindle Nucleus. SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily."}
{"protein": "MATSNNPRKFSEKIALHNQKQAEETAAFEEVMKDLSLTRAARLQLQKSQYLQLGPSRGQYYGGSLPNVNQIGSSSMDLSFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTVYLSPPADTSWRRTNSDSALHQSTMTPTQAESFTGGPQDAHQKRVLLLTVPGMEETGSETDKTLSKQSWDSKKAGSRPKSCEVPGINIFPSADQENTAALIPATHNTGGSLPDLSTIHFPSPLPTPLDPEEPPFPALTSSGSTGSLAHLGVGGTGQGMNTPSSSPQRRPAVVSPLSLSTEARRQQAQQVPPTLSPLSPITQAVAMDALSLEQQLPYAFFTQAGSQQPPPQPQPPPPPPPVSQQQPPPPQVSVGLPQGGPLLPSASLTRGPQLPPLAVTVPSTLPQSPTESPGQPPMGIDVTSAPALQYRTGAGSPATQSPTSPVSNQGFSPGSSPQHTSTLGSVFGDAYYEQQMTARQANALSRQLEQFNMMENAISSSSLYNPGSTLNYSQAAMMGLSGSHGGLQDPQQLGYAGHGGIPNIILTVTGESPPSLSKELSSTLAGVSDVSFDSDHQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL", "text": "FUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells (By similarity). In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses. May be required for dendritic growth of developing cortical neurons. In concert with SIK1, regulates the light-induced entrainment of the circadian clock. In response to light stimulus, coactivates the CREB-mediated transcription of PER1 which plays an important role in the photic entrainment of the circadian clock (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Cytoplasmic when phosphorylated by SIK or AMPK and when sequestered by 14-3-3 proteins. Translocated to the nucleus on Ser-151 dephosphorylation, instigated by a number of factors including calcium ion and cAMP levels. Light stimulation triggers a nuclear accumulation in the suprachiasmatic nucleus (SCN) of the brain. SIMILARITY: Belongs to the TORC family."}
{"protein": "MANSSSGVAIHDDCKLKFNELQSKRMHRFITFMMDNKGKEIIVDKIGDRTTSYEDFTSSLPEGDCRFAIYDFDFLTAEDVPKSRIFYILWSPDNAKVRSKMLYASSNERFKKELNGIQLEVQATDAGEISLDALKDRVK", "text": "FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (By similarity). Involved in innate immunity. Required for the expression of defense-related genes PR1A, LOX2 and CHS1 upon biotic stresses. Required for basal resistance to the fungal blast (Magnaporthe grisea), bacterial blight (Xanthomonas oryzae pv. oryzae, Xoo) and the herbivorous insect brown planthopper (Nilaparvata lugens, BPH). Involved in the promotion of seed germination. Required for the expression of alpha-amylase genes during seed germination (PubMed:24033867). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin-binding proteins ADF family."}
{"protein": "MKFLSSLVVLGLSAQALASPYVDHQATKDQRDVNVFKQVLQDINLDVQKFDQDITQYQGGDPTVLLADSDAIIKTTEEGIQRIGPQPPLSVTEALALVGPVQGVNKLIMKAVDHLIEKKGPLVGGGYGPQVKDSLERQAHAASKLSELVSSKVPSPLAPISKQLSDQVAQALQKGIQAFSISARQATKVKREATKVQRDISAFKKVIQNISLAVNKFNVDIERYVGGDASHLLADGNVLIKATLDGVQSLQNEPPLSSMEALALVGPVQDLSNQILLAIQNLIDKKEPLVQAGFGGKVENNLRQQEEAAQKLSELVSTKVPHELADISRQLSDGIAAGIKKGIDAFAGTGPAPTTSSTPEASTAPAPSTPPQTPEDTLVPATSTPAPGPAPTAPDSSMVWPTSTTASPDVQPTITSSGTSVPAAPTGGNSSPAVPAFTGAASANQVSGAVGLAAGLLAVLAF", "text": "FUNCTION: Constitutive protein of the cell wall. Binds fatty acids and may thus serve as a fatty acid transporter between P.marneffei and host cells during infection (PubMed:20053994). Abundant antigen target of host humoral immune response (PubMed:9488383). SUBCELLULAR LOCATION: Secreted, cell wall Note=Associated with the entire thickness of the cell walls of yeast and conidia found in mold form. Localizes on the outer layers of the hyphal cell walls. SIMILARITY: Belongs to the cell wall mannoprotein 1 family."}
{"protein": "MPEFRVWAPKPALVRLDVNGAVHAMTRSADGWWHTTVAAPADARYGYLLDDDPTVLPDPRSARQPDGVHARSQRWEPPGQFGAARTDTGWPGRSVEGAVIYELHIGTFTTAGTFDAAIEKLDYLVDLGIDFVELMPVNSFAGTRGWGYDGVLWYSVHEPYGGPDGLVRFIDACHARRLGVLIDAVFNHLGPSGNYLPRFGPYLSSASNPWGDGINIAGADSDEVRHYIIDCALRWMRDFHADGLRLDAVHALVDTTAVHVLEELANATRWLSGQLGRPLSLIAETDRNDPRLITRPSHGGYGITAQWNDDIHHAIHTAVSGERQGYYADFGSLATLAYTLRNGYFHAGTYSSFRRRRHGRALDTSAIPATRLLAYTCTHDQVGNRALGDRPSQYLTGGQLAIKAALTLGSPYTAMLFMGEEWGASSPFQFFCSHPEPELAHSTVAGRKEEFAEHGWAADDIPDPQDPQTFQRCKLNWAEAGSGEHARLHRFYRDLIALRHNEADLADPWLDHLMVDYDEQQRWVVMRRGQLMIACNLGAEPTCVPVSGELVLAWESPIIGDNSTELAAYSLAILRAAEPA", "text": "FUNCTION: Is involved in the biosynthesis of trehalose but not in that of capsular glucan and glycogen. FUNCTION: Is involved in the biosynthesis of trehalose but not in that of capsular glucan and glycogen. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 13 family."}
{"protein": "MTTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTHIVLAALNSLGVMADASGRNDLVVKTPDGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVANLTELLPGITHEQVCQAVTEAFFAHYGERVDAEVISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGVITRAQVFTDSLNPAPLEALGERLQGCQYRVDVLEQACESLIAEFPAQKGELRELAAWMAQAVR", "text": "FUNCTION: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LplA family."}
{"protein": "MGDYFAWDFANISGSNTSGSLNLNQLNLDNINNGLHNQEDGAGGRNENSERVGSGSPGSVSMQVLSLFSAVNSALATLEKSEEFPSVVKDEQSIFPAVAKASNSLDELAQNIIPAPSPPGFNRKRKTFDEDSSVEMIRRAISDHLDLLNNCCIGIANLNEDSVHKISLTRSGKPSQLVTVSCRHSSVIQKSYGSEKRYLCPPPMVYINGNYSSIFNQSFRTEISIMNDFGQCSQPISEEYTGQGCMIFRSLHISSLVAAKSKNLRLSLDMFSNVNNQLLSHLVTSSISIVSKPSKKGSKLKISNITLRSGSVVSLYNRINSQTVRTKYTSIEAGQFCLRGDRWVPLRINLLLPDENGKLKVCDDVDNPEPIKYGSIVELVDEATGTTSDPLIIRRVEKDHIAEEDGYVNQMHRIVLESAYPISNVRHLKIAEHSSLAYSNNISVRWFLGATSAQNRNASSEAILPIEWEAVGNLSSNEMTRVGDSVCWTIVGISHFDCTMMLPFNQNPVPTVTDYPYIEEPPEYLESSRSLQFKIGGYSVGLQIWLGVHGPLSYSFTAAADTSTMGTVTLGLSQISYDPSCAEQKYPLLFVIPGGIVIIGKCEILLTSSAFGN", "text": "FUNCTION: Transcription factor that behaves as a negative regulator of adhesion. Recognizes specifically the canonical CSL response element GTGA/GGAA. May also play a cbf12-antagonistic role in the regulation of a number of other important processes such as extracellular material production, colony morphogenesis, ploidy maintenance, or meiosis. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the Su(H) family."}
{"protein": "MATSPSSCDCLVGVPTGPTLASTCGGSAFMLFMGLLEVFIRSQCDLEDPCGRASTRFRSEPDYEYDFIVIGGGSAGSVVASRLSEVPQWKVLLIEAGGDEPVGAQIPSMFLNFIGSDIDYRYNTEPERMACLSSMEQRCYWPRGKVLGGTSVMNGMMYIRGNREDYDDWAAQGNPGWSYQDVLPFFKKSEDNLELDAVGTEYHAKGGLLPVGKFPYNPPLSYALLKAGEEMGFSVQDLNGQNSTGFMIAQMTARNGIRYSSARAFLRPARMRNNLHILLNTTVTKVLIHPGTKNVVGVEVSDQFGSMRKILVKKEVIVSGGAVNSPQILLLSGVGPKEDLQKVNVRPVHHLPGVGKNLHNHVAYFTNFFIDDADTAPLNWATAMEYLLFRDGLMSGTGISDVTAKMATRWADRPNLPDLQLYFGGYLASCARTGQVGELLSNNSRAIQIFPAVLNPKSRGYITLRSADPLDPPRIFANYLTDERDVKTLVEGIKFAIRLSQTSPLKQYGMRLDKTVVKGCESHAFASDAYWECAVRQNTGPENHQAGSCKMGPSHDPMAVVNHELRVHGVRGLRVMDTSIMPKVTAGNTHAPAVMIAEKGAYLLKRAWGAKVURVDATWTLHRVI", "text": "SUBCELLULAR LOCATION: Secreted. Note=Secreted as part of the seminal fluid transferred to females. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MSFLLPKLTSKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSADLSKMAAIYLVDVDHTPVYTQYFDISYIPSTVFFFNGQHMKVDYGSPDHTKFVGSFKTKQDFIDLIEVIYRGAMRGKLIVQSPIDPKNVPKYDLLYQDI", "text": "FUNCTION: Essential role in pre-mRNA splicing. Required in cell cycle progression for S/G(2) transition (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DIM1 family."}
{"protein": "MGYGKILVALDRSELAKEVLQQAIALGQKESSQLMVFYCIPVDSQDLSIYPSFYGEAAIGFSQIIKEHLEEQQTEAREWLQSIVQQVQEDGVACEWDVKVGEPGRWIRDMAKNWDADLVVLGRRGLKGLAEVFLGSVSSYVIHHVQCSVLIVQH", "text": "SIMILARITY: Belongs to the universal stress protein A family."}
{"protein": "MVFSSNVFLFLFLPIFLGLYYLSGQRYRNLLLLLASYVFYAWWRVDFLALFAAVTLWNYWIGLKVGAAGVRTKPAQRWLLLGVVVDSINVMMKSAGLEPFILTHVLLPIGISFYIFESISYIIDVYRGDTPATRNLIDFAAFVAIFPHLIAGPVLRFRDLADQFNNRTHTLDKFSEGCTRFMQGFIKKVFIADTLAVVADHCFALQNPTTGDAWLGALAYTAQLYFDFSGYSDMAIGLGLMMGFRFMENFKQPYISQSITEFWRRWHISLSTWLRDYLYITLGGNRKGTLTTYRNLFLTMLLGGLWHGANITYIVWGAWHGMWLAIEKAIGLNTSPRSFNPVRWAFTFLLVVMGWVIFRAENLHVAGRMYGAMFSFGEWSLSELNRANLTGLQVATLVVAYATLAFFGLRDFYTNRPAEKTKPADPSLIKAVPGDNPGSIHEPGFTVGQDAAVQPAYWTADWPRYAMRAAVLLLFVASILKLSAQSFSPFLYFQF", "text": "FUNCTION: Together with AlgJ and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family."}
{"protein": "MEKFSNIAQLKDSGLKVTGPRLKILDLFETHAEEHLSAEDVYRILLEEGVEIGVATIYRVLTQFEQAGILQRHHFETGKAVYELDKGDHHDHIVCVKCGEVTEFHNPEIEALQDKIAEENGYRIVDHALYMYGVCSDCQAKGKR", "text": "FUNCTION: Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of the fbp protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Fur family."}
{"protein": "MSFFRYLSDISSETRTLLLAYGVLGGLYLILVPLALYWWMNRRWYIMGKIERLFVYGLVFLFFPGLILLSPFLNMRLKGQGET", "text": "FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I NdhL subunit family."}
{"protein": "MRRAGAACSAMDRLRLLLLLLLLLGVSFGGAKETCSTGMYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECLGLQSMSAPCVEADDAVCRCSYGYYQDEETGRCEACSVCGVGSGLVFSCQDKQNTVCEECPEGTYSDEANHVDPCLPCTVCEDTERQLRECTPWADAECEEIPGRWITRSTPPEGSDVTTPSTQEPEAPPERDLIASTVADTVTTVMGSSQPVVTRGTADNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQTHTQTASGQALKGDGNLYSSLPLTKREEVEKLLNGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWGAQDSATLDALLAALRRIQRADIVESLCSESTATSPV", "text": "FUNCTION: [Isoform 2]: Does not bind NGF, BDNF, NTF3, and NTF4. FUNCTION: Low affinity neurotrophin receptor which can bind to mature NGF, BDNF, NTF3, and NTF4 (PubMed:11559852, PubMed:1317267). Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF (proNGF), BDNF (proBDNF) and NTF3 (proNT3) with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:22155786, PubMed:24908487, PubMed:27457814). Plays an important role in differentiation and survival of specific neuronal populations during development (PubMed:1317267, PubMed:11559852). Can mediate cell survival as well as cell death of neural cells (PubMed:1317267, PubMed:11559852, PubMed:24908487). The heterodimeric receptor formed with SORCS2 plays a role in proBDNF-dependent synaptic plasticity, in hippocampal long term depression (LTD) and long term potentiation (LTP) (PubMed:27457814). Plays a role in the inactivation of RHOA (By similarity). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (PubMed:22460790). Necessary for the circadian oscillation of the clock genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (PubMed:23785138). FUNCTION: (Microbial infection) Cell surface receptor for rabies virus glycoprotein Gs. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Perikaryon Cell projection, growth cone Cell projection, dendritic spine."}
{"protein": "MKEKREFRDYLSDIFDAIEKIENFTQDISFDAFVEDEMRVFAVVRALEIIGEAAKNVPLEIKENYPSVPWKEMARTRDKLIHSYFGVDLNVVWKTVNKNLPPLKDQISEILKDLGNTSS", "text": "FUNCTION: Probable toxic component of a putative type VII toxin- antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin MA_102. Neutralization may be due to AMPylation by MA_102. SIMILARITY: Belongs to the HepT RNase toxin family."}
{"protein": "MATVSTGSLIFIVKKNSPMMSKLVFFWQNREKEFRDFGGFSEKSVYFCDTIDNRKRLILVVINREVLLMTFDAIDQLAVNTVRTLSMDAIQAANSGHPGLPMGAAPMAYVLWNHFMNINPKTSRNWSNRDRFILSAGHGSAMLYSLLHLAGYDLSVEDLKNFRQWGSKTPGHPEVNHTDGVEATTGPLGQGIANAVGMAMAEAHLAAKFNKPGFDIVDHYTFALNGDGDLMEGVSQEAASMAGHLKLGKLVLLYDSNDISLDGPTSMAFTEDVKGRFEAYGWQHILVKDGNDLEEIAAAIEAAKAETEKPTIIEVKTIIGFGAEKQGTSAVHGAPLGAEGIAFAKKAYQWTHQDFEVPAEVTERFAQGLQARGEKAEQAWNDLFAAYQAEYPELAAEYQKAFANEAAQVELEAHELGSSMASRVSSQQAIQQISEQVASFWGGSADLSASNNTMVKAETDFQPGHYEGRNIWFGVREFAMAAAMNGIALHGGTRVYGGTFFVFSNYLLPAVRMAALQNLPTVYVMTHDSIAVGEDGPTHEPIEQLASVRSMPNLNVIRPADGNETNAAWKRAIAETDRPTMLVLTRQNLPVLEGTKELAEDGLNKGAYILSEAKGDLDGIIIATGSEVKLAMDTQEALEAEGIHVRVVSMPSQNIFDEQSAEYKESILPAAVTKRLAIEAGSSFGWAKYVGLAGKTLTIDTWGASAPGNRIFEEYGFTVANATELYKSL", "text": "FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. SIMILARITY: Belongs to the transketolase family."}
{"protein": "MSGTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVERGPQYGTVEKAWHNLMTEAEKVSELHLEVKNALMNEDFEKIKNWQKEAFHKQMMGGFKETKEADDGFRKAQKPWAKKLKEVEAAKKSYHAACKEEKLATSRETNSKADPAMNPEQLKKLQDKVEKSKQDSQKTKEKYEKSLKDLDGTTPQYMENMEQVFEQCQQFEDKRLSFFREVLLEVEKHLDLSNVESYASIYRELEYAIKSADAMEDLKWFRNNHGPGMSMNWPQFEDWSADLNRTLSRREKKKPTDGVTLTGISQSGEQSSIQNQHSSHLSVQSAQSTNNPFEDEEETVSINETENKKIENVGSYEKTHPAEWSDDESNNPFNPSDTNGDNNPFDEDALTTLEVRVRALYDYDGQELDELSFKAGEELTKIEDEDEQGWCKGRLEGGQVGLYPANYVESVQ", "text": "FUNCTION: Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. SUBCELLULAR LOCATION: Cell membrane Cytoplasmic vesicle Cell projection, ruffle membrane Cytoplasm Cytoplasm, cytoskeleton Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Early endosome Recycling endosome membrane Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection Membrane, caveola Note=Detected at the neck of flask- shaped caveolae. SIMILARITY: Belongs to the PACSIN family."}
{"protein": "MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPYQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQFDKLRKRDAFLEQFRKEDMFKDNFDEMDRSREVVQELIDEYHAATQPDYISWGTQEQ", "text": "FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the tubulin family."}
{"protein": "MNIQNDKERLLNGSIDEIEIITTDNNENDTIRNDDILKNSQLREQQQHQQIQQQIQQQKKESSLSTIASVIAFYFFISISLVFLNKILLSDFKFEYPLFITWYQQIISFVSIYIMTSISKSVPALSFLPEFEFKSATASKVLPVTAVLTGMVIFNNLCLEYVEVSFYQVARSLTICFSLILTYIVLKSKTSYRATMACLVVFLGFVLGSAGEVNFSWLGIIFGLLSSFFVALYSIAVKRVLPAVDGNEWRLSIYNTAISIGLIFPLILVSGEANTILDEPLLYSGTFWFYMTVAGLMGYLISISVFMQIKHTSPLTNTISGTVKACVQTILAVVFWGNPISTQNAVGILLVIGGSFWYSMQRFFEMKK", "text": "FUNCTION: Antiporter specific for GDP-l-fucose and depending on the concomitant reverse transport of GMP. Involved in GDP-fucose import from the cytoplasm into the Golgi lumen. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35C subfamily."}
{"protein": "MSVRNRVVLAPMSGVTDMPFRELAWRFGAGLVVTEMVASRELVNDTAESWSRLKAAGFRPHMVQLAGREAHWMAEAAKIAADHGADIIDINMGCPAKKVIGGYSGSALMRDPDHALGLIEATVKAVDIPVTLKMRLGWDENSINAPDIARRAEASGIQLVTIHGRTRMQFYEGRADWDAIRAVREVISVPLIANGDVETAHDAQEILRRSGADAVMIGRGCQGRPWHAGVLAGAAEPRREDIADIAVEHYRMMLDFYGEAVAIRHARKHLGWYLERFAPALAGTEKAGIMTSRDPREVAARLYHALDAGALDGREAA", "text": "FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. SIMILARITY: Belongs to the Dus family."}
{"protein": "MPVAYTFPVLPSSCLLCGISNRSTSFVVDRPELQISGLLVVRSESGEFFGSGLSLRRFQREGRRRLNAAGGGIHVVDNAPSRTSSLAASTSTIELPVTCYQLIGVSEQAEKDEVVKSVINLKKTDAEEGYTMEAAAARQDLLMDVRDKLLFESEYAGNLKEKIAPKSPLRIPWAWLPGALCLLQEVGQEKLVLDIGRAALRNLDSKPYIHDIFLSMALAECAIAKAAFEVNKVSQGFEALARAQSFLKSKVTLGKLALLTQIEESLEELAPPCTLDLLGLPRTPENAERRRGAIAALRELLRQGLSVEASCQIQDWPCFLSQAISRLLATEIVDLLPWDDLAITRKNKKSLESHNQRVVIDFNCFYMVLLGHIAVGFSGKQNETINKAKTICECLIASEGVDLKFEEAFCSFLLKQGSEAEALEKLKQLESNSDSAVRNSILGKESRSTSATPSLEAWLMESVLANFPDTRGCSPSLANFFRAEKKYPENKKMGSPSIMNHKTNQRPLSTTQFVNSSQHLYTAVEQLTPTDLQSPVVSAKNNDETSASMPSVQLKRNLGVHKNKIWDEWLSQSSLIGRVSVVALLGCTVFFSLKLSGIRSGRLQSMPISVSARPHSESDSFLWKTESGNFRKNLDSVNRNGIVGNIKVLIDMLKMHCGEHPDALYLKSSGQSATSLSHSASELHKRPMDTEEAEELVRQWENVKAEALGPTHQVYSLSEVLDESMLVQWQTLAQTAEAKSCYWRFVLLHLEVLQAHIFEDGIAGEAAEIEALLEEAAELVDESQPKNAKYYSTYKIRYILKKQEDGLWKFCQSDIQIQK", "text": "FUNCTION: Component of the plastid division machinery required for PDV1 localization to constriction sites. Involved in chloroplast division site placement (PubMed:28984364, PubMed:23936263). Required for the proper formation of FtsZ rings at the division site in nongreen plastids (e.g. etioplasts) (PubMed:23936263). Inhibits FtsZ assembly, functioning as an antagonistic regulator of FtsZ dynamics against ARC6, by recruiting ARC3 to the middle of the plastid to facilitates its interaction with FtsZ proteins (PubMed:26527658, PubMed:30824505). Required during stromule biogenesis in the leaf epidermis, especially in non-mesophyll cells plastids (PubMed:28984364). SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Single-pass membrane protein Note=Localizes both to the mid-plastid and to a single spot at one pole."}
{"protein": "MDDSTPYPVPQELYIPQKMKAFMAEPQGCALVAALEGQFQCSIVVINDHLSVISSADGVAVDINQIEKILRDVWRKRDVQIMIREAALNASCTHICHTLLPRAYCAVVLFFSSDLQRRSRCTDIIIDQFTGKVTMFGTEQAVNKAREMMIECLTEHFGLLEMNIPPTQRTTRMGYTNSYNPEIRTHLPPNSFLNSVFPMGEPNAILTSTPPTTSIMDEPLLSASLEKHLLFPSDFSVPPPRLSPVQELPLTPPKTCVVEKIKQWIPTTEVGKILGNRAAVKKHIERQFNCVITVHTEVQSSFGATPVEIVAQNKEQCQEARNAVMSLMQSHQDKPASNPPDSGFSTPGSPFTSDSSSTTPEKRGNSRQYHRGSFRDQPKVMLALTPRKLSPSD", "text": "FUNCTION: RNA-binding protein which binds to its own mRNA and target mRNAs to negatively regulate gene expression to modulate apoptosis and differentiation in the germline (PubMed:30728462). Negatively regulates the expression of the argonaute protein wago-4, and may thus play a role in RNA-mediated gene silencing (RNAi) in the germline (PubMed:30728462). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region."}
{"protein": "MPLLDSFTVDHTRMEAPAVRVAKTMNTPHGDAITVFDLRFCVPNKEVMPERGIHTLEHLFAGFMRNHLNGNGVEIIDISPMGCRTGFYMSLIGTPDEQRVADAWKAAMEDVLKVQDQNQIPELNVYQCGTYQMHSLQEAQDIARSILERDVRINSNEELALPKEKLQELHI", "text": "FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). SIMILARITY: Belongs to the LuxS family. SIMILARITY: Belongs to the LuxS family."}
{"protein": "MLLNISSSPISHRNPHFLSNFNNPISYFPRRSKTHLSKSHFFPKFTPLSNQSLKNRVLFGNKRYPDGERFDFRSRAISGIDLGSFESVLEAIAVLTTIIVVHESGHFLAASLQGIHVSKFAIGFGPILAKFDYNNVEYSLRAFPLGGFVGFPDNDPDSEIPIDDENLLKNRPTLDRSIVVSAGIIANVIFAYAIIFVQVLSVGLPVQEAFPGVLVPEVKTFSAASRDGLLSGDVILAVDGTELSKTGPDAVSKIVDIVKRNPKSNVVFRIERGGEDFDIRVTPDKNFDGTGKIGVQLSPNVRITKVRPRNIPETFRFVGREFMGLSSNVLDGLKQTFFNFSQTASKVAGPVAIIAVGAEVARSNIDGLYQFAALLNINLAVINLLPLPALDGGTLALILLEAVRGGKKLPVEVEQGIMSSGIMLVIFLGLFLIVKDTLSLDFIKEML", "text": "FUNCTION: Metalloprotease essential for chloroplast and plant development. May be involved in regulated intramembrane proteolysis (RIP). SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50A family."}
{"protein": "MMMRFLSAVVIMSSAMAVGLVSAQRCGSQGGGGTCPALWCCSIWGWCGDSEPYCGRTCENKCWSGERSDHRCGAAVGNPPCGQDRCCSVHGWCGGGNDYCSGSKCQYRCSSSVRGPRVALSGNSTANSIGNVVVTEPLFDQMFSHRKDCPSQGFYSYHSFLVAAESFPAFGTIGDVATRKREVAAFLAHISQATSGERSDVENPHAWGLCHINTTTVTENDFCTSSDWPCAAGKKYSPRGPIQLTHNFNYGLAGQAIGEDLIQNPDLVEKDPIISFKTALWFWMSQHDNKPSCHDIVLNANSAANRIPNKGVIGNIISRAFGHDDFAVRSSSIGFYKRYCDMLGVSYGHDLKYWFDNTPSSEFQRIQMRVAA", "text": "FUNCTION: Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin- containing fungi. Possesses also insecticidal activity and superantigenic properties."}
{"protein": "MTLPNKAALVGLAHTLSEQVKRYLVTADETKSPEDHKLCIEGERTPSSTEHAQAWEIVRTCDRIGSLVHGPVPWLLSNALSHLDSACLAAATQLNLQDIIVDGPSPTSLDTIVTATGVSEDLLRRILRGCAQRFIFEEVAPDQYAHTDASKMLRVTGIHALVGFSCDEVMRSAAYFSNFLQQTKGKPPSWNVPSPFSLAFDPTKGLFDYYSTVDEVRGRRFDLGMGGTEATKPLVEEMFDFSSLPEGSTVVDVGGGRGHLSRRVSQKHPHLRFIVQDLPAVIHGVEDTDKVTMMEHDIRRRNPVRGADVYLLRSILHDYPDAACVEILSNIVTAMDPSKSRILLDEMIMPDLLAQDSQRFMNQIDMTVVLTLNGKERSTKEWNSLITMVDNRLETEKIWWRKGEEGSHWGVQQLRLRK", "text": "FUNCTION: Involved in the conversion of sterigmatocystin to O- methylsterigmatocystin (OMST) and dihydrosterigmatocystin to dihydro-o- methylsterigmatocystin in the aflatoxin biosynthesis pathway. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily."}
{"protein": "MSGVWVFKNGVVRLVEKQQATAGTAVAGGRRKALVHTPSGQVVSSYAALEARLTALGWERYYEDPSLFQFHKRGSLDLISLPADFSAFSSVHMYDIVVKNRDSFRVVDA", "text": "FUNCTION: GTP-binding protein that functions in the development of root systems, which are mediated by auxin. Acts as a cell cycle regulator during root development. Proteasome-mediated degradation of the protein is necessary for the transition of metaphase to anaphase in mitosis. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=During mitosis, associates with mitotic spindles. SIMILARITY: Belongs to the FPF1 family."}
{"protein": "MAAGKFASLPRNMPVNHQFPLASSMDLLSSKSPLAERRTDAYQDVSIHGTLPRKKKGPPSIRSCDNAGHSKSPRQSSPLTQDIIQENPLQDRKGENFIFRDPYLLDPTLEYVKFSKERHIMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLWCLEERYGTSPGRGREGSLAEGRPDVVKRLSLTTGSSIQAREHSLPRGNLLRNKEKSGSQPACLDHVQDRKALTLKAHQSESHLPIGCKLPPQSPSMDTSPCPSSPVFRTGSEPTLSPALVRRFSSDARTGEALRGSDSQLCPKPPPKPCKVPFLKTPPSPSPWLTSEANYCELNPAFAVGCDRGAKLPMQAHDSHEMLLTAKQNGPSGPRNSGINYMILDGDDQARHWDPLAVQTDEGQEDKTKFVPPLMETVSSFRPNDFESKLLPPENKPLETAMLKHAKELFTNHDARVIAQHMLSVDCKVARILEVSEDRKRSMGVSSGLELITLPHGRQLRLDIIERHNTMAIGIAVDILGCTGTLENRAGTLNKIIQVAVELKDAMGDLYAFSAIMKALEMPQITRLEKTWTALRHHYTQTAILYEKQLKPFSKILHEGRESTYVPASNVSVPLLMPLVTLMERQAVTFEGTDMWENNDESCEILLNHLATARFMAEASESYRMNAERILADFQPDEEMTEILRTEFQMRLLWGSKGAEVNQNERYDKFNQILTALSRKLEPPSGKQAEL", "text": "FUNCTION: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (PubMed:12517963). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (By similarity). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (PubMed:10896938). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (PubMed:25499443). May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (PubMed:25499443). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (PubMed:19365570). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (PubMed:22801373). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (PubMed:22801373). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (PubMed:10896938). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion Note=Localization to focal adhesions depends on interaction with PTPRA."}
{"protein": "MDQRPELLSSMEYVASPDPKPGVPLRVAENVAPGAEDWLPSASGHLAWATSLETEHQTHLELSEEQRLQISKELVDLQIATHHLREQHEAEVFELRREILRLESRVLELELHGNGACQGHKVQPMANLGQHQVPPLEPPGGQQKLQEELKWLLEHHRARQQALETQVGVLSQQLQGAREEARTTGQQLASQAMVLASCKGQLRQAEAENTQLQLQLKKMNEEYAVRLQHYARETVENASSTNQAALQAFLESTLQDIRAAHRTREQQLAQAARTYRKRLADLNQRQELLLTTCRATFATAINLEPLPMHWATELSHPRENEYGRHRTLLLYPEKGSGETSKENKSQPLALDTASWAQIQQRLQDFSQDTQAELERERAQLMVRATMAEQQLSELQEYVDQHLGRYKQEILKLRKLVNIGDPQGVEAVSSPGSGGARL", "text": "FUNCTION: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, perinuclear region Cell membrane, sarcolemma Sarcoplasmic reticulum Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm (By similarity). SIMILARITY: Belongs to the CCDC78 family."}
{"protein": "MSPLLLWLGLMLCVSGLQAGDEEEHKCFLEGENLTLTCPYNIMLYSLSLKAWQRVRSHGSPETLVLTNTRKADFNVARAGKYLLEDYPTESVVKVTVTGLQRQDVGLYQCVVYLSPDNVIILRQRIRLAWCQGKPVMVIVLTCGFILNKGLVFSVLFVFLCKAGPKVLQPSKTSKVQGVSEKQ", "text": "FUNCTION: Forms a receptor signaling complex with TYROBP/DAP12 which mediates activation of macrophages as part of the innate immune response. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein."}
{"protein": "MIASKFGIGQQVRHSLLGYLGVVVDIDPEYSLDEPSPDELAVNDELRAAPWYHVVMEDDNGQPVHTYLAEAQLRSEMRDEHPEQPSMDELARTIRKQLQAPRLRN", "text": "FUNCTION: Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HspQ family."}
{"protein": "MPGDHRRIRGPEESQPPQLYAADEEEAPGTRDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGPAGAGGEAPAALRGRLLCDFRRAPFAGRRRRAPPGGCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGPAPTWLLDPTRLEEERAAAGLTVALMPVLNQVAGLLGSGEGGLTESWAEAVRLGLEGCQRLYPVLQQSLVRAARRRGAAAQP", "text": "FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus. SIMILARITY: Belongs to the RNase PH family."}
{"protein": "MKSIVFVALFGLALLAVVCSASEDAHKELLKEVVRAMVVDKTDAVQAEERECRWYLGGCSQDGDCCKHLQCHSNYEWCIWDGTFSK", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 17 (Hntx-9) subfamily."}
{"protein": "MDNIYIKQALVLKEVKHVFQKLIGEDPMESMYMVDTIQRLGIEHHFEEEIEAALQKQHLIFSSHLSDFANNHKLCEVALPFRLLRQRGHYVLADVFDNLKSNKKEFREKHGEDVKGLISLYEATQLGIEGEDSLDDAGYLCHQLLHAWLTRHEEHNEAMYVAKTLQHPLHYDLSRFRDDTSILLNDFKTKREWECLEELAEINSSIVRFVNQNEITQVYKWWKDLGLNNEVKFARYQPLKWYMWPMACFTDPRFSEQRIELTKPISLVYIIDDIFDVYGTLDQLTLFTDAIKRWELASTEQLPDFMKMCLRVLYEITNDFAEKIYKKHGFNPIETLKRSWVRLLNAFLEEAHWLNSGHLPRSAEYLNNGIVSTGVHVVLVHSFFLMDYSINNEIVAIVDNVPQIIHSVAKILRLSDDLEGAKSEDQNGLDGSYIDCYMNEHQDVSAEDAQRHVAHLISCEWKRLNREILTQNQLPSSFTNFCLNAARMVPLMYHYRSNPGLSTLQEHVKLLSNNAVAGAERHVVHILCLQFVIE", "text": "FUNCTION: Monoterpene synthase that catalyzes the hydrolysis of neryl diphosphate (NPP) to form nerol and diphosphate (PubMed:24124526). Is specific for NPP and has no hydrolase activity toward geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) (PubMed:24124526). The monoterpene nerol may have an insect repellent effect for the plant leaves (PubMed:24124526). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MGASVLAMAARGGHTHTVKLLLENGAFVDDCEHACVSEGNTNTHCSAGSVQEARALLEVRALLAAAQHGQGAAVALLLDWGSDARVCHTGTGWSALMLAAAGGSLSVCQQLVERGADPDHTNVLGNTALEVALQLRRRDVQKYLDNITSVRPRPDDEKKRPDVFHALKLGNAQLVKEIVEQDAAQVDVCNADGASPLMMAAVSGQLEVVQLLVEKRADVDRQDSVHGWTALMQATYHGNKEVVKFLLSQGADVQLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMLVDKDKSKQRGKSALRRRASAGTPSPPEDKTGLKSWWNRMSNRFRRLKLTHTLRHGLSTNRLAPFPDAADVPLDATMRAEEGGAEVASPTAPPAGAQSTACSRTEDCGLNGTGSGKEDFLITTMLRNGAPLARLPSEQLKAVIPPFLPPSCFEPWSSERCGSLRDARSTHTHSQRPGRSSAGSDTASISRVVNRSIKFPSITKGPSPSNSGSYNSAHSSGGSNGVGGVNRHSDTHNRSGGSAADSVLSQIAAQRKRAAGLMDSRSPAVETPSPAHTPLPDSRPKLELQKRPQSGNSSRSKSTSPTLTPSPSPTPAHTPAPAHTPAHRPTGASADSQGSASTQQRSRSSGGSSSGTITDEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIRTDGPRQQILAAISELNAGKGRERQILQETIINFQSSFGSSASTPRAATHTH", "text": "FUNCTION: Required for renal function. SUBCELLULAR LOCATION: Cell projection, cilium."}
{"protein": "MASFMKQLSLVLSFIALALAGCAVYQNTQTAMKDQLKVTPTWLDNTLKSTNLLSLGLGKPSGGKLGDEACVFSAVKEVVVAAINAEARMGASLIRLFFHDCFVDGCDAGLLLNDTATFTGEQTAAGNNNSVRGFAVIEQAKQNVKTQMPDMSVSCADILSIAARDSFEKFSGSTYTVTLGRKDARTANFTGANTQLVGPNENLTSQLTKFAAKGFNGTEMVALLGSHTIGFARCPLLCISTFINPARVSTLNCNCSGTVNATGLVGLDPTPTTWDQRYFSDVVNDQGLLFSDNELLKGNTTNAAVRRYRDAMGAFLTDFAAAMVKMSNLPPSPGVALEIRDVCSRVNANSVDPCEESRLLASPD", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. FUNCTION: May contribute to protection against cold-induced oxidative stress. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MKNTFLICDECQAVNIRTLQKKLEKLDPDAEIVIGCQSYCGPGRRKTFTFVNNRPLAALTEEELIEKVSQQLKKPRDPEEEERLRKRHEERKRRKVEQDRKLKEKLEKRKAQQ", "text": "SIMILARITY: Belongs to the UPF0741 family."}
{"protein": "MVKFAHVVAFLLLASLFQPLTARDLEINVLQLDVSQSGCPGVTKERWPELLGTPAKFAMQIIQKENPKLTNVQTVLNGTPVTEDLRCNRVRLFVNVLDFVVQTPQVG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine protease inhibitor) family."}
{"protein": "MKFVKIDSSSVDMKKYKLQNNVRRSIKSSSMNYANVAIMTDADHDGLGSIYPSLLGFFSNWPELFEQGRIRFVKTPVIIAQVGKKQEWFYTVAEYESAKDALPKHSIRYIKGLGSLEKSEYREMIQNPVYDVVKLPENWKELFEMLMGDNADLRKEWMSQ", "text": "FUNCTION: Small subunit of the DNA topoisomerase that untwists superhelical DNA. Controls topological states of double-stranded DNA by transient breakage and subsequent rejoining of DNA strands."}
{"protein": "MSESTYPSVKDLTLEEKASLTSGGDAWHLQGVESKGIPGYMITDGPHGLRKSLASSAGETDLDDSVPATCFPPAAGLSSSWNPELIHKVGEAMAEECIQEKVAVILGPGVNIKRNPLGGRCFEYWSEDPYLAGHEAIGIVEGVQSKGVGTSLKHFAANNQESDRLRVDARISPRALREIYFPAFEHIVKKAQPWTIMCSYNRINGVHSAQNHWLLTDVLRDEWGFEGIVMSDWGADHDRGASLNAGLNLEMPPSYTDDQIVYAVRDGRITPAQLDRMAQGMIDLVNKTRAAMSIDNYRFDVDAHDEVAHQAAIESIVMLKNDDAILPLNAGPVANPSAMPQKIAVIGEFARTPRYQGGGSSHITPTKMTSFLDTLAERGIKADFAPGFTLDLEPADPALESEAVETAKNADVVLMFLGLPEAAESEGFDRDTLDMPAKQITLLEQVAAANQNVVVVLSNGSVITVAPWAKNAKGILESWLLGQSGGPALADVIFGQVSPSGKLAQSIPLDINDDPSMTNWPGEEGHVDYGEGVFVGYRYYDTYGKAVDCPFGYGLSYATFEITGVAVAKTGANTATVNATVTNTSDVDAAETVQVYVAPGKADVARPKHELKGFTKVFLKSGESKTVTIDLDERAFAYWSEKYNDWHVESGEYAIEVGTSSRDIAETVTVALEGDGKTQPLTEWSTYGEWEADPFGAKIVAAVAAAGEAGELPKLPDNAMMRMFLNSMPINSLPTLLGEGGKKIAQFMVDEYAKLSK", "text": "FUNCTION: Catalyzes the hydrolysis of a non-reducing terminal alpha-L- arabinopyranosidic linkage in ginsenoside Rb2 (alpha-L- arabinopyranosyl-(1->6)-alpha-D-glucopyranosyl) to release alpha-D- glucopyranosyl (Rd). It is not able to hydrolyze alpha-L- arabinofuranosyl-(1->6)-alpha-D-glucopyranosyl (Rc). SIMILARITY: Belongs to the glycosyl hydrolase 3 family."}
{"protein": "MILLKLYLTLAAILCQSRGTTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNQNEHTPVSGRTIGGCGCAEKIT", "text": "FUNCTION: Blocks ryanodine receptors, and potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MKRRTFTAGLAALPFLGSSLTRAFAQDAAASLPKTYSGQKIRALASTGAAFEAMATVSRDFTEATGIAVEYVNLSYNEQYQKLILDLTSGAASFDVFNFAYQWKFEIEPYCADLANIPKEIQGAPDLALDDYPQRALEIYGRANNKLIGLPTLGDVTLFVWNKEAYKAAGLDPDAAPKTWDEVVERGAKLVSNGQFGYAMPAGKGIQTTVTWIMVFKSMGGEYFDASGAPTFASEAGVKTMKFLVEKLAAVSPPGNLAWDFPEMFNSLSTGQSGQSMMWPGAFGDLLNPKRSQVHDKIGWSPMPQASLLGGWSMGVNDASRSKDAAKLYVAWLTSPDIVRRMGLIGGAPARISALKDPELIKQAPNRPAVLAGLQGDVAEYPPIKEAEQVHIMIYDEVNAAVAKIKTPEQAASDLQGKVESFMRRRGYLKT", "text": "FUNCTION: Probably part of the binding-protein-dependent transport system y4oPQRS. This system probably transports a sugar-like molecule. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family."}
{"protein": "AGNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDSGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDNQANDAGKKWAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTKDGHPELMDKVGHDFSGNDDISDVGKAYKKAGITGHIWQSDGITNSLPRGLSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDVITDVLNEAAYKKKFRVATYDDNPWVTFNK", "text": "FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod phospholipase D family. Class I subfamily."}
{"protein": "MDVRFYPPPAQPAAAPDAPCLGPSPCLDPYYCNKFDGENMYMSMTEPSQDYVPASQSYPGPSLESEDFNIPPITPPSLPDHSLVHLNEVESGYHSLCHPMNHNGLLPFHPQNMDLPEITVSNMLGQDGTLLSNSISVMPDIRNPEGTQYSSHPQMAAMRPRGQPADIRQQPGMMPHGQLTTINQSQLSAQLGLNMGGSNVPHNSPSPPGSKSATPSPSSSVHEDEGDDTSKINGGEKRPASDMGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDGLGEEQKQVYKKKTEAAKKEYLKQLAAYRASLVSKSYSEPVDVKTSQPPQLINSKPSVFHGPSQAHSALYLSSHYHQQPGMNPHLTAMHPSLPRNIAPKPNNQMPVTVSIANMAVSPPPPLQISPPLHQHLNMQQHQPLTMQQPLGNQLPMQVQSALHSPTMQQGFTLQPDYQTIINPTSTAAQVVTQAMEYVRSGCRNPPPQPVDWNNDYCSSGGMQRDKALYLT", "text": "FUNCTION: Transcriptional regulator with a major role in neural stem cell commitment and corticogenesis as well as in lymphoid cell development and lymphoid tissue organogenesis (By similarity). Binds to GC-rich DNA sequences in the proximity of transcription start sites and may alter chromatin structure, modifying access of transcription factors to DNA. During cortical development, controls the neural stem cell pool by inhibiting the switch from proliferative to differentiating progenitors. Beyond progenitor cells, promotes neurite outgrowth in newborn neurons migrating to reach the cortical plate. May activate or repress critical genes for neural stem cell fate such as SOX2, EOMES and ROBO2 (By similarity). Plays an essential role in the development of lymphoid tissue-inducer (LTi) cells, a subset necessary for the formation of secondary lymphoid organs: peripheral lymph nodes and Peyer's patches. Acts as a developmental checkpoint and regulates thymocyte positive selection toward T cell lineage commitment. Required for the development of various T cell subsets, including CD4-positive helper T cells, CD8-positive cytotoxic T cells, regulatory T cells and CD1D-dependent natural killer T (NKT) cells. Required for the differentiation of common lymphoid progenitors (CMP) to innate lymphoid cells (ILC) (By similarity). May regulate the NOTCH-mediated gene program, promoting differentiation of the ILC lineage. Required at the progenitor phase of NK cell development in the bone marrow to specify NK cell lineage commitment (PubMed:21126536) (By similarity). Upon chronic antigen stimulation, diverts T cell development by promoting the generation of exhaustive T cells, while suppressing effector and memory T cell programming. May regulate the expression of genes encoding inhibitory receptors such as PDCD1 and induce the exhaustion program, to prevent the overstimulation of T cells and activation- induced cell death (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the high motility group (HMG) box superfamily."}
{"protein": "MNRLPSSASALACSAHALNLIEKRTLNHEEMKALNREVIDYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRRPFMPLLPGFRHVPFGNIDAMSMAFSEGKKTGDEIAAVILEPIQGEGGVILPPQGYLTEVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDTLLDGFRQLAREYPNLVHDARGKGMLIAIEFVDNETGYRFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIELCEQVLKSARNALAAMQVSVEEV", "text": "FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4- aminobutanal. Also functions as a cadaverine transaminase in a a L- lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily."}
{"protein": "MVLMAPRTLLLLLSGALALTQTWARSHSMRYFYTTMSRPGAGEPRFISVGYVDDTQFVRFDSDDASPREEPRAPWMEREGPKYWDRNTQICKAQAQTERENLRIALRYYNQSEGGSHTMQVMYGCDVGPDGPFLRGYEQHAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAARRAEQRRVYLEGEFVEWLRRYLENGKETLQRADPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWEPSSQPTVPIVGIVAGLVLLVAVVTGAVVAAVMWRKKSSDRKGGSYSQAASSNSAQGSDVSLTA", "text": "FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MHC class I family."}
{"protein": "MTELKFKGVYVEDIGHLTCGTLTLTENSINFIGDKGGKSVYITGTDVDKLKWQKLGNKPGLRVGLSDGGAHRFGGFLDDDLQKIQSFTSSNWSKSINQSNLFINGWNYGQADVKGKNIEFSWENEPIFEIPCTNVSNVIANKNEAILEFHQNEQSKVQLMEMRFHMPVDLENEEDTDKVEEFKKAVLAYAGLEAETEQPICLLTDILCTTPRGRYDIKVYPTSIALHGKTYDYKIPVKTINRLFLVPHKDGRQVYFVLSLNPPIRQGQTHYSYLIFEFGKDEEEDLELSLTDEQLDYFNGNLQREMTGPIYETISILFKSICNLKVTVPGRFLGSSGTPAIQCTHRQNLGLLYPMEKGFLFIQKPVMYIRFEEISSCHFARSDSGTVTRTFDFEIDLKTGSSLTFSAMDKEENNKLFDYLNKKEIKIRNSHRIDNKSAGYGSSDEDDIDPYKSTVKAEGREQDDDSDDESTDEDYDLDKDMKKQKNDKDSSEGSGSEPDDEYDSGSEKDASGTGESDPDEENIEPKKKESKEKKNKREKKEKPVKEKAVKKGKKTKDPNEPKRATTAYIIWFNANRNSMKEDGDTLGDVAKKAGAKWKSMSADDKKEWNDKAAQDKARYEAEMKEYKKNGGGVEKASGPSTKKSSDQSPGKQFKSKEHISDTDDSDDDEPLKAKKDESDAASESSGESD", "text": "FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to double-stranded DNA (By similarity). In embryos, may function redundantly with hmg-4 to promote cell cycle progression and development of the anterior pharynx (PubMed:30336114). In the germline, acts non-redundantly with hmg-4 to play a role in oocyte development (PubMed:30336114). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the SSRP1 family."}
{"protein": "MSPTISHKDSSRQRRSGMFSHALDMKSGPLPPGGWDDSRRDSVGGEGDREVLLGDAGPGDLPKAPRSYRSELSSILLLLFLYVLQGIPLGLAGSIPLILQSKNVSYTDQAFFSFVFWPFSLKLLWAPLVDAVYFKNFGRRKSWLVPTQYTLGIFMIYLSTQVDRLLGNIDGRTPDVVALTVTFFLFEFLAATQDIAVDGWALTMLSRENVGYASTCNSVGQTAGYFLGNVLFLALESADFCNKYLRFQPQPRGIVTLSDFLFFWGTVFLITTTLVALLKKENREASIVKEETQGITDTYKLLFSIIKMPAVLAFCLLILTSKIGFSAADAVTGLKLVEEGVPKEHLALLAVPMVPLQIILPLLISKYTAGPQPLNIFYKAMPYRLLLGLEYALLVWWTPKVEHQGGFPLYYYIIVLLSYALHQVTLYSMYVSIMAFNAKVSDPLIGGTYMTLLNTVSNLGGNWPSTVALWLVDPLTVKECVGASNQNCRTPDAIELCKKLGGSCVTALDGYYVESIICVLIGFGWWFFLGPKFKKLQDEGPSSWKCKRNN", "text": "FUNCTION: Probable acetyl-CoA transporter necessary for O-acetylation of gangliosides (PubMed:10570973). Negatively regulates BMP signaling (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC33A transporter family."}
{"protein": "MSLVRRSNVFDPFADFWDPFDGVFRSLVPATSDRDTAAFANARVDWKETPESHVFKADLPGVKKEEVKVEVEEGNVLVISGQRSKEKEDKNDKWHRVERSSGQFMRRFRLPENAKVDQVKASMENGVLTVTVPKAEVKKPEVKAIEISG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
{"protein": "MDTHDTYLHLHSSPLNSSPSQPPVMSSMVGHPSVISSSRPLPSPMSTLGSSMNGLPSPYSVITPSLSSPSISLPSTPSMGFNTLNSPQMNSLSMNGNEDIKPPPGLAPLGNMSSYQCTSPGSLSKHICAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYTCRDIKECLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKEKSDTEVETTSRFNEDMPVDKILDAELSVEPKTETYTESSPSNSTNDPVTNICHAADKQLFTLVEWAKRIPHFSDLPLDDQVILLRAGWNELLIASFSHRSITVKDGILLGTGLHVHRSSAHSAGVGSIFNRVLTELVSKMKDMQMDKTELGCLRAIVLFNPDAKGLSNSLEVEALREKVYASLETYTKQKYPDQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQIT", "text": "FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for rxrs is 9-cis retinoic acid (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily."}
{"protein": "MALASGVTFAGYTVVRMLGCSAMGEVYLVQHPGFPGWQALKVLSPAMAADDEFRRRFQRETEVAARLFHPHILEVHDRGEFDGQLWIAMDYVDGIDATQHMADRFPAVLPVGEVLAIVTAVAGALDYAHQRGLLHRDVNPANVVLTSQSAGDQRILLADFGIASQPSYPAPELSAGADVDGRADQYALALTAIHLFAGAPPVDRSHTGPLQPPKLSAFRPDLARLDGVLSRALATAPADRFGSCREFADAMNEQAGVAIADQSSGGVDASEVTAAAGEEAYVVDYPAYGWPEAVDCKEPSARAPAPAAPTPQRRGSMLQSAAGVLARRLDNFSTATKAPASPTRRRPRRILVGAVAVLLLAGLFAVGIVIGRKTNTTATEVARPPTSGSAVPSAPTTTVAVTAPVPLDGTYRIEIQRSKQTYDYTPTPQPPDVNTWWAFRTSCTPTECLAAATMLDDNDHTQAKTPPVRPFLMQFGEGQWKSRPETVQFPCVGPNGSPSTQATTQLLALRPQPQGDLVGEMVVTVHSNECGQQGAVIRIPAVASRSGDLPPAVTVPDPATIPDTPDTTSTATLTPPTTTAPGPGR", "text": "FUNCTION: Plays an important role in slowing down the growth of mycobacteria within the infected host. FUNCTION: Plays an important role in slowing down the growth of mycobacteria within the infected host (PubMed:19341393). Activates the peroxidase activity of Rv2159c in a phosphorylation independent manner during oxidative stress conditions and thereby maintains the cellular homeostasis (PubMed:27818650). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Single-pass membrane protein Note=More abundant in the cytosol than in the cell membrane. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MAAKQVLFSDEARAKMLDGVNTLANAVKVTLGPKGRNVVLDKSFGTPTITKDGVSVAKEIELEDKFENMGAQIVKEVASKTADVAGDGTTTATVLAQALLTEGLKAVAAGMNPMDLKRGIDKATARLVEELKALSKPCSDPKSIEQVGTISANSDATVGKLIADAMAKVGKEGVITVEEGKGFEDELDVVEGMQFDRGYLSPYFATNQENMTTDLENPYILIVDKKISNIRDLLPILEGVSKSGRALLIIAEDVESEALATLVVNNMRGVVKVCAVKAPGFGDRRKAMLEDIATLTGATFVSEDLSMKLEETNMEHLGTASRVQVTKDNTTIIDGAGEKEAIAKRINVIKANIAEANSDYDREKLQERLAKLSGGVAVIKVGAVTEAEMKEKKDRVDDALHATRAAVEEGIVAGGGVALIRAQKALDGLTGENDDQNYGIALLRKAIEAPLRQIVSNAGGESSVVVNQVKANQGNYGYNAANDTYGDMVEMGILDPTKVTRSALQHAASIAGLMITTEAMIGEIKEAAPAMPMGGGMGGMPGMM", "text": "FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Note=Released into the host cell cytosol during infection. SIMILARITY: Belongs to the chaperonin (HSP60) family."}
{"protein": "MESSEPEPTEDASMDAFLEKFQSQPYRGGFREDQWEEEFDKIPLFMKKAPSEIDPEEFPDLACLQSMIFDDDRYPEEQAKTYKDEGNDYFKEKDYKKAVLSYSEGLKKKCADPDLNAVLYTNRAAAQYYLGNVRSSLNDVLAAKKLKPGHLKAIIRGALCHLELKHFAEAVNWCDEGLQIDAKEKKLLEIRAKADKLKRMEERDLRKAKLKEKKEQHQNEALLQAIKARNIRLVSESAGEDEDSASNGPAEILLDGLSSENPYGARLSIDDQGRLSWPVLFLYPEYAQSDFISAFHEDTRFIDHLMAMFSEAPSWDSEHKYHPENLEVYFEDEDRAELYQVSPDSTLLQVLQHPRCCVKALTPAFLVCVGSSPFCRNYLQGKKVHR", "text": "FUNCTION: May act as a co-chaperone for HSP90AB1 (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Cytoplasm Note=Predominantly nuclear in the G1 and S phases of cell cycle and is evenly distributed between the nucleus and cytoplasm in the G2 phase (PubMed:19390865). MSL1 can promote its nuclear localization (PubMed:19390865, PubMed:24913909). SIMILARITY: Belongs to the TTC4 family."}
{"protein": "MPNAECRHNAGFWSAAYAEMPISKFTAYAENAVLPKRKMDGISAYADMPKKIFGGICRYAVMPKNSECRTGMIQTQPGTKIVFNAPYDDKHTYHIKVINSSARRIGYGIKTTNMKRLGVDPPCGVLDPKEAVLLAVSCDAFAFGQEDTNNDRITVEWTNTPDGAAKQFRREWFQGDGMVRRKNLPIEYNP", "text": "FUNCTION: Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod. SUBCELLULAR LOCATION: Cell projection, pseudopodium. Cytoplasm, cytoskeleton."}
{"protein": "MKKPPVPLLQGGVRADGRAPDQMREVQISVGVISNADGSAMVSYGATTAVAAVYGPREMHPRHLSLPDRGVMRVRYHMAPFSTKDERKSPTPSRREIEISKVLREALEPAVMLEQYPRSRIDVFIEILQADGSTRVASLTAASLALADAGIYMRDLVIGVSVGLVDGTVVLDLNGLEDQYGEGDLPVGYMPNLRRYTLLQLDGAWGRDKLLEALNLAVKGAEFVYQKARDALKNRYMAIAEEIYGR", "text": "FUNCTION: Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteromeric RNA-tails. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase PH family. Rrp41 subfamily."}
{"protein": "MAINTDTQYEKALGGSGNPLPADSHETEKLLTNASENKEENGMKKSFSVTMSSEKSMGDLEQNGHNLPYKSVSAGQLESAPLSPSRVSLARASSTATTAQEQGRPTDYLVLAIFSCFCPVWPVNIVALVFSIMSRNSLQQGDLDGARRLGRLARLLSVVSILLGLVIIVLCILSLTIFH", "text": "FUNCTION: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Endomembrane system; Single-pass membrane protein Cytoplasm, perinuclear region Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. SIMILARITY: Belongs to the CD225/Dispanin family."}
{"protein": "MVHHSGSIQSFKQQKGMNISKSEITTEASLKPSRRSLPCLAQSYAHSKSLSQSASLFQSTESESQAPTSVTFLSADKPEHVTSEESRKDSTLKCSFADLSDFCLALGKDKDYLDESEHANYDRSRLLNDFVTKDKPASKTKLSKNDMSYIASSGLLFKDGKKRIDYILVYRKTNIQYDKRNTFEKNLRAEGLMLEKEPAIANPDIMFIKIHIPWDTLCKYAERLNIRVPFRKKCYYTDQKNKSKSRVQNYFKRIKKWMSQNPMVLDKSAFPELEESDCYTGPFSRARIHHFIINNKDTFFSNATRSRIVYHMLERTKYENGISKVGIRKLITNGSYIAAFPPHEGAYKSSLPIKTHGPQNNRHLLYERWARWGMWYKHQPLDLIRMYFGEKIGLYFAWLGWYTGMLIPAAVVGLCVFFYGLVTMNESQVSQEICKATEVFMCPLCDKNCSLQRLNDSCIYAKVTYLFDNGGTVFFAIFMAIWATVFLEFWKRRRSILTYTWDLIEWEEEEETLRPQFEAKYYRMEVINPITGKPEPHQPSSDKVTRLLVSVSGIFFMISLVITAVFAVVVYRLVVMEQFASFKWNFVKQHWQFATSGAAVCINFIIIMLLNLAYEKIAYLLTNLEYPRTESEWENSFALKMFLFQFVNLNSSIFYIAFFLGRFVGHPGKYNKLFERWRLEECHPSGCLIDLCLQMGVIMFLKQIWNNFMELGYPLIQNWWSRHKIKRGIQDASIPQWENDWNLQPMNIHGLMDEYLEMVLQFGFTTIFVAAFPLAPLLALLNNIIEIRLDAYKFVTQWRRPLPARATDIGIWLGILEGIGILAVITNAFVIAITSDYIPRFVYEYKYGPCANHVKQNENCLKGYVNNSLSFFDLSELGMGKSGYCRYRDYRGPPWSSKPYEFTLQYWHILAARLAFIIVFEHLVFGIKSFIAYLIPDIPKGLRERIRREKYLVQEMMYEAELEHLQQQRRKSGQPIHHEWP", "text": "FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylcholine and galactosylceramide (PubMed:23532839). Does not exhibit calcium-activated chloride channel (CaCC) activity (PubMed:23532839). Seems to act as potassium channel regulator and may inhibit pain signaling; can facilitate KCNT1/Slack channel activity by promoting its full single-channel conductance at very low sodium concentrations and by increasing its sodium sensitivity (PubMed:23872594). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Shows an intracellular localization. SIMILARITY: Belongs to the anoctamin family."}
{"protein": "MSSIPDYAEQLRTADLRVTRPRVAVLEAVNAHPHADTETIFGAVRFALPDVSRQAVYDVLHALTAAGLVRKIQPSGSVARYESRVGDNHHHIVCRSCGVIADVDCAVGEAPCLTASDHNGFLLDEAEVIYWGLCPDCSISDTSRSHP", "text": "FUNCTION: Represses transcription of the catalase-peroxidase gene katG and its own transcription by binding to the promoter region in a redox- dependent manner. FUNCTION: Represses transcription of the catalase-peroxidase gene katG and its own transcription by binding to the promoter region in a redox- dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Fur family."}
{"protein": "MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNEILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKWLNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPILCAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKKLGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPANAYVKSEVFSHVVKSINIKGSYVGNRADTREALDFFSRGLIKSPIKIVGLSELPKVYDLMEKGKILGRYVVDTSK", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MIFLTTLPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIINTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAESLYLDLEEVTPAEDGIYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTLRGQAQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESPSFSAGDNPHVLYSPEFRISGAPDKYESEKRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK", "text": "FUNCTION: Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid- containing gangliosides and to the glycoproteins RTN4R and RTN4RL2 (PubMed:8995428, PubMed:9298990). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane (By similarity). Negative regulator of neurite outgrowth; in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides (PubMed:17640868). In cerebellar granule cells the inhibition is mediated primarily via binding to neuronal gangliosides (PubMed:17640868). In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides (PubMed:19367338). Inhibits axon longitudinal growth (PubMed:9298990). Inhibits axon outgrowth by binding to RTN4R (By similarity). Preferentially binds to alpha-2,3-linked sialic acid (PubMed:8995428). Binds ganglioside Gt1b (PubMed:8995428). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane raft. SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family."}
{"protein": "MATVEPETTPTTNPPPAEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV", "text": "FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:18805096). This protein recognizes and binds the 7- methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (By similarity). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:18805096, PubMed:25456498). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (PubMed:18805096). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (PubMed:25456498). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (By similarity). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). This protein recognizes and binds the 7-methylguanosine- containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures PubMed:7939721. Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (By similarity). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:8558852). Component of the CYFIP1- EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap. Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (By similarity). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (PubMed:8558852). SUBCELLULAR LOCATION: Cytoplasm, P-body Cytoplasm Cytoplasm, Stress granule Nucleus Note=Interaction with EIF4ENIF1/4E-T is required for localization to processing bodies (P-bodies). Imported in the nucleus via interaction with EIF4ENIF1/4E-T via a piggy-back mechanism. SUBCELLULAR LOCATION: Cytoplasm, P-body Cytoplasm Cytoplasm, Stress granule Nucleus Note=Interaction with EIF4ENIF1/4E-T is required for localization to processing bodies (P-bodies). Imported in the nucleus via interaction with EIF4ENIF1/4E-T via a piggy-back mechanism. SIMILARITY: Belongs to the eukaryotic initiation factor 4E family."}
{"protein": "MRFKGLDLNLLVVLDALMTERNLTAAARSINLSQPAMSAAVARLRTNFRDDLFAMAGREFIPTPRAEGLAPAVRDALLQIQLSIVSWEPFNPAQSDRRFRIVLSDYVTLVFFEKVVARAAQEAPGISFDCLPLADDFEELLRRGDIDFLIMPELFMSMHPHAALFEDKFVCVGCRTNEQLSEPFTFERYMSMGHVAVKFGNTRRPTIEEWYLLEHGLKRRIEVVVQGFSMIPPMLSGTERIGTMPLRLAQHFAKTIPLRIVELPLPIPPLAEAVQWPALHNSDPASLWMRELLLQEASLMVSPRAPVRLSAPGF", "text": "FUNCTION: NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers. SIMILARITY: Belongs to the LysR transcriptional regulatory family."}
{"protein": "MIKNPKVLILTAHYGNGHVQVAKTLEQAFHQKGIEDVIVCDLFGESHPVITDITKYLYLKSYTIGKELYRLFYYGVEKIYDKKIASWYANFGRKRLKALLHTEKPDIVINTFPIIAVPELKKQTGFSIPVYNVLTDFCLHKIWIHREVDRYFVATDHVKQVMIEIGVPAERIVETGIPIRKNFELTMNSELIYNKYQLSREKKILLIVAGAHGVLGNVKDLCASFMSVPNLQVAVVCGKNDALKQELLKLQEQNSEALKVFGYIENIDELFRVTSCMITKPGGITLSEAAALQVPVILYKPVPGQENENAIYFESKGAAVVIREDAEIFEKTKALLEDDRKLLQMKEAMGSIYRPEPAAHIVDVILEENHAQTNHVPMKSPALAQSFT", "text": "FUNCTION: Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta- monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D- glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O- (beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D- glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the glycosyltransferase 28 family. UgtP subfamily."}
{"protein": "MDEINFAVLGTGGIGRRTLEVSTYKDGLTPVAACDRHGVAVNHDGLDVEEILDATEGNIAGDGTGDTEDKRVTDGGAAVKQHGDGAGIVASAQGTSTETPIDEIIAESDEIDAVLLALPNLEHDFIPRIAERFAEAEFEGVLIDVLKRSRVIGMLDDREETLVESGITFVCGAGATPGLLTGAAALAAQSFVEVEEVEIWWGVGLKSGYEDNRGTVREDIAHLDGYDIETAREMDESEIEAVIEEHDGVLEFNDMEHADDVLLERAGICDAEDVTVGGILDIRKDEKPTTTTVRVTGRTFDGKRGTNTFQLDDATSMAANVNGPALGYLKSAVRRNRAGDYGVFGPAELMPGF", "text": "FUNCTION: A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN- carbamic acid using NAD(P)+ (By similarity). Complements a bioA deletion in E.coli (PubMed:32042199). SIMILARITY: Belongs to the BioU family."}
{"protein": "VKSTNLMAFVATKMLERQEDLDTCTEMQVEKMKASTKARLRTESSFAPRTWEDAIKDEILRRSVDTSSLDRWPELKQELENVSDALKADSLWLPMKSLSLYSEVSNQEPSSIPIGEMKHQILTRLKLICSRLEKLDHNLSKAVLGIQNSEDLILIIYNRDICKNTILMIKSLCNSLI", "text": "FUNCTION: Mediates the nuclear export of encapsidated genomic RNAs (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs complexes and the nuclear export machinery of the cell. Possesses no intrinsic RNA-binding activity, but includes a C-terminal M1-binding domain. This domain is believed to allow recognition of RNPs to which the M1 protein is bound. Because the M1 protein is not available in large quantities until the later stages of infection, such an indirect recognition mechanism probably ensures that genomic RNPs are not exported from the nucleus before sufficient quantities of viral mRNA and progeny genomic RNA have been synthesized. Furthermore, the RNPs enters the cytoplasm only when they have associated with the M1 protein that is necessary to guide them to the plasma membrane. May down- regulate viral RNA synthesis when overproduced (By similarity). SUBCELLULAR LOCATION: Virion Host nucleus."}
{"protein": "MLNSPLTSVLFVLLFVLSPIYGAFEYMQLVLQWPTAFCHTTPCKRIPNNFTIHGLWPDNVSTTLNYCAAKENFKNIEDDTKKDDLYKRWPDLTTAETYCKQHQNFWRHEYNKHGKCCSESYNREQYFDLAMALKDKFDLLSSLRNHGIIPGRGMKYTVQKINSTIKKITQGYPNLSCTKGIMELVEIGICFDSMVKNVINCPHPKTCKPTGSNEIKFP", "text": "FUNCTION: Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species of the Solanaceae, self-incompatibility is controlled by the single, multiallelic locus S. This stylar glycoprotein is associated with expression of self-incompatibility in potato. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the RNase T2 family."}
{"protein": "MKSTLMTASVLILVLLSIVDYASVYAEFIDSEISLERQWINACFNVCMKISSDKKYCKYLCGKN", "text": "FUNCTION: Potassium channel inhibitor (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor kappa-KTx family. Kappa-KTx 3 subfamily."}
{"protein": "MLLKNASFYDDEVLKRADIRLKDSLITEIKENLSPINNEEVIECRDLFVLPSFIDLSVTGLEGYENLKQKAFKGGVGLLNVFNCDQSGIKNIMAIKNNQLADIATLKNKGGEILIAPSDAFLELISHYAKSYNLPLLISLENSFEALNSGELAYELGQNFVENAFENTRLVRFMEVSRALQIPVLLDKVNSITTLKLIKAFNDLGAKLQAQTPLSHLVLDESVYEDYEPRFKIAPPLRDKESQNALKEALKNNEIAMLTSLHASKNSNAQLFEESAFGCESIEDAFSVAYTFLVQKKVISFQQLIKVMAINQAKFLKLNAGEVKENQLANLMIVDLNAQTRVSNQNSPFYGLELYGEVQRMILKGQTTFIKENACKKS", "text": "FUNCTION: Non-functional DHOase. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. PyrC' subfamily."}
{"protein": "MKTDGNTTLDTTISMEELERTVKSAYEALAKDQQDDGHWIYELEADVTIPAQFILLEHTLDKIDEELEQKIANYLRRCQSREHWGWPVYYGGEFNISASVQAYFALKMTGEDINAPHMVRAREAILAHGGPEYANVFTRIQLSLFGEASWLATPFMPVEIMLLPRWMYFSIWNMSYWSRTTVAPLLIVADLKPKAINPRNVHIPELFPTPPDKVKTWIHGPFRSKWGHVFKFIDTAIRPFTRFVPSFLHKKAYKAALDFIEPRLNGVDGLGAIYPPMSYSAVMYRALGIPDDDPRAATNWEALKGLLVIKEREAYCQACVSPVWDTALSGHALMEASFGPDGINADRTEKLIDRAAHWLRAHQVLNVVGDWAINNPNLQPGGWAFQYGNDYYPDVDDTAVAAMLLHRQNLPENEEALDRARKWIIGMQSSNGGWGAFDIDNDKQILNDIPFADHGALLDPPTADVSARCISLLAELGHPEDRPVIERGIKYLRKEQEEDGSWFGRWGTNYIYGAWSVLCAFNASGVPHDDPSVLKCVNFLKSVQREDGGWGESCETYEGSAHGVYTESLPSQTAWAVLGLMASGRRTDPAVKRGIVWLIQHQQDNGEWAEEPFNAVGFPRMFYLHYLGYKQFFPLLALARYRHMEKSGTNNVSFAF", "text": "FUNCTION: Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol. SIMILARITY: Belongs to the terpene cyclase/mutase family."}
{"protein": "MGWALKKVCFLGVIFLISACTVKKNGVKNLSYKHESLRAYENAKDYDPTTKKATYKRNFFERHFKHHTDSQGNNTKQPLDNGMRDSNAIQRATMHPYQVGGKWYYPTKVDLGEKFDGIASWYGPNFHAKKTSNGEIYNMYAHTAAHKTLPMNTVVKVINVDNNSSTIVRINDRGPFVSNRIIDLSNAAARDIDMVQKGTASVRLIVLGFGGVISKQYEQSFNANYSKILHKEFKVGESEKSVSGGKFSLQMGAFRNQIGAQTLADKLQAENKNYSVKVAFKDDLYKVLVQGFQSEEEARDFMKKYNQNAVLTRE", "text": "FUNCTION: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the RlpA family."}
{"protein": "MDKEKSDPSCKSSDLKISNISIQVVSVPGKLPGRRPPRKPIGKPRPRKQPKKRAPFWNVQNKIILFTVFLFILAVTAWTLLWLYISKTESKDAFYFVGMFRITNIEFLPEYRQKESREFLSMAKTVQQVVNLVYTTSAFSKFYKQSVVADVSSNNKGGLLVHFWIVFVMPHAKGHIFCEECVAAILKDSIQTSIINRTSVGSLQGLAVDMDSVVLNAGLRSDYSSAVGSDNGCSRYLYADHLTLRYPLEISATSGQLMCHFKLVAIVGYLIRLSIESIQLEADNCITDSLTVYDSLLPIRSAILYRICEPTRTLMSFVSTNNLMLVILKSPYVRRLAGIRAYFEVIPEQKCESTILVKEINSFEGKISSPYYPSYYPPKCKCTWTFQTSLSTLGIALKFYNYSITKKSAKGCEHGWWEINEHMYCGSYMDHETIFRVPSPLVHIQLQCSSRLSDKPLLVEYGGYNISQPCPAGSFRCSSGLCVPQAQRCDGVNDCFDESDELFCVTVKPACNSSSFRQHGPLVCDGFRDCEDGQDEQNCTRSIPCTSRTFKCGNDICFRKQNAQCDGIVDCPDGSDEEGCGCSRSSSFLHRIVGGSDSQEGTWPWQVSLHFVGSAYCGASVISREWLLSAAHCFHGNRLSDPTPWTAHLGMYVQGNAKFISPVRRIVVHEYYNSQTFDYDIALLQLSIAWPETLKQLIQPICIPPAGQKVRSGEKCWVTGWGRRHEADSKGSPVLQQAEVELIDQTVCVSTYGIITSRMLCAGVMSGKSDACKGDSGGPLSCRRKSDGKWILTGIVSWGHGCGRPNFPGVYTRVSSFVPWIHKYVPSLL", "text": "FUNCTION: Serine protease which preferentially hydrolyzes peptides with Arg at the P1 position. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MSIPLLYYPLSTQNQRVESFEILSNEEQSKIYTTDTLPSASEMDELIWAAYRQIFSEHQILKFTRQRFLESQLRFNQIKVREFIRGLAISDSFRKLNYDVNNNYRFVELCVQRILGRDVYNEKEKIAWSIVICNKGVIGFIDCLINSQEYLENFGDNIVPYQRRRIIFQRVNGETPFNLKTPRYGIEFRDKLVKPQFIWQGAIRRFRPQEQRPRAGDPVLFLNMVYDLNITPKFNRYPGLVNR", "text": "FUNCTION: Rod-core linker protein required for attachment of phycocyanin to allophycocyanin in cores of phycobilisomes. FUNCTION: Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the phycobilisome linker protein family."}
{"protein": "MKKMNVVAFVTLIISFLLLSQVLAELSSSSNNETSSVSQTNDENQTAAFKRTYHHRPRINCGHACARRCSKTSRKKVCHRACGSCCAKCQCVPPGTSGNTASCPCYASIRTHGNKLKCP", "text": "FUNCTION: Gibberellin-regulated protein that may function in hormonal controlled steps of development such as seed germination, flowering and seed maturation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the GASA family."}
{"protein": "MLSQVRVAVTQAEPVWLDLEATVKKTCDLIAEAAANGAQLVTFPECWIPGYPAWIWARPVDMRLSSIYIQNSLKIDSPQMASIQQCAAENKIVVVLGFSENLHNSLYISQAIIASDGKILTTRKKIKPTHMERTIFGDSFGDCLQSVVDTSAGRVGALSCWEHIQPLLKYHTYAQREQIHVAAWPPLFPHSEDGSLFSMSTEGTSSIARTYAIESQSFVLHTTTVIGQSGIDRMATSTGALMSTPGGGCSAIFGPDGRQLSQPIPSAEEGIIYADLDFEHIYHSKAFVDVCGHYSRPDLLWLGVEGGVKRHVRDNATTATPQVEQQEE", "text": "FUNCTION: Nitrilase that hydrolyzes preferentially phenylacetonitrile, (R,S)-mandelonitrile, and 3-indolylacetonitrile. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family."}
{"protein": "MFLVLLRACLLTLSLCSPAEDDGLVQEKLFLSSMGLWSRPKPSHHAAVPSQMWKIFKQASKQTVNDPCVVSEYGVRGNIVRFMQDQGSLISAPAVHSFNCVRKHLFFNMSVLEEVEQLSLAQLEMKFKQDLLLLGPHVFSVDLYRVLKTTLKGVTHESSRKLLQSQTLSPGAHASVLVNLTNLAQSWRKPEKNFGMQLELQVMHLNNMLHDHAYVQIPDIHATLVVVSLNPLQCRSRRKRSASYYLPVTPSNVCKPRRLYIDFKDVGWQDWIIAPQGYLANYCHGECPFPLSESLNGTNHAILQTLVHSFDPKGTPQPCCVPIKLSPISMLYYDNNDNVVLRHYEDMVVDECGCR", "text": "FUNCTION: Serves to facilitate the differentiation of either mesoderm or endoderm either as a cofactor in an instructive signal or by providing permissive environment. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MKIIHTADWHLGRILNGKSLLEDQAYILDKFIEAMKLEQPDVIVIAGDLYDTSYPNKDAIQLLEQTIDILNLEMSIPLIMINGNHDSKERLNYGSKWFEKSHMYIRTDLNDMNKPVTIGNVDFYTMPFATINEMQYFFDDKAIETHQQALNRVLAYMHEVIDENKVNIFVGHLTVQGGIRSESERPLTIGTVESVDENLFNQFDRVMLGHLHHPFSIESNFINYSGSLLQYSFSETKQPKGYKIVEIKNQKITDKFIPLKPLRQLEVIEGNYEDAIQEKLEVKHKENYLHFKLKHMSHVSDPMMHLKQIYPNTLALTNQTFDFNTSIHHENIEIQKLDDETIIDNFYNSITGEHLTTNQSKKIEKIMTALLEEGSK", "text": "FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity (By similarity). SIMILARITY: Belongs to the SbcD family."}
{"protein": "MGRPPCCDKSNVKKGLWTEEEDAKILAYVAIHGVGNWSLIPKKAGLNRCGKSCRLRWTNYLRPDLKHDSFSTQEEELIIECHRAIGSRWSSIARKLPGRTDNDVKNHWNTKLKKKLMKMGIDPVTHKPVSQLLAEFRNISGHGNASFKTEPSNNSILTQSNSAWEMMRNTTTNHESYYTNSPMMFTNSSEYQTTPFHFYSHPNHLLNGTTSSCSSSSSSTSITQPNQVPQTPVTNFYWSDFLLSDPVPQVVGSSATSDLTFTQNEHHFNIEAEYISQNIDSKASGTCHSASSFVDEILDKDQEMLSQFPQLLNDFDY", "text": "FUNCTION: Required for anther development and early tapetal function during microspore maturation (PubMed:18397379, PubMed:21957980). Regulates callose dissolution required for microspores release from the tetrads (PubMed:18397379). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MANRPLDILNNALDTPVIVRLKGAREFRGELKGYDIHMNLVLDNAEELRDGEVVSKFSSVVIRGDNVVYVSP", "text": "SIMILARITY: Belongs to the snRNP Sm proteins family."}
{"protein": "MNDLRYPIGQFTYKRPITEEMIDTWIQEIEDLPNELTKAIKDLDQKQLDTPYRVGGWTVRQVVHHVVDSHMNSYIRFKLALTEKNPTIKPYKEEKWAELPDSKLPVDVSLVMLDSLHKRWVNLLYSLELEDLEKTFNHPDTGETKLAAAIGLYAWHGRHHTAHITSLRKRLNW", "text": "FUNCTION: Possible metal-dependent hydrolase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metal hydrolase YfiT family."}
{"protein": "METLSFPRYNIAEIVVHIRNKLLTGADGKNLSKSDFLPNPKPEVLYMIYMRALQLVYGVRLEHFYMMPVNIEVMYPHIMEGFLPVSNLFFHLDSFMPICRVNDFEIADILYPKANRTSRFLSGIINFIHFRETCLEKYEEFLLQNKSSVDKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQDFRQKTTLLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEVMEKYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAINQDIHKIKSGIQQLRDAEKREKLKSQEILVDLKSALEKYHEGIEKTTEECCTRIGGKTAELKRRMFKMPP", "text": "FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Note=Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore (By similarity). SIMILARITY: Belongs to the NUF2 family."}
{"protein": "MLHPRARTMLLLSLPAVAIGIASSLILIVVMKIASVLQNLLWQRLPGTLGIAQDSPLWIIGVLTLTGIAVGLVIRFSQGHAGPDPACEPLIGAPVPPSALPGLIVALILGLAGGVSLGPEHPIMTVNIALAVAIGARLLPRVNRMEWTILASAGTIGALFGTPVAAALIFSQTLNGSSEVPLWDRLFAPLMAAAAGALTTGLFFHPHFSLPIAHYGQMEMTDILSGAIVAAIAIAAGMVAVWCLPRLHAMMHQMKNPVLVLGIGGFILGILGVIGGPVSLFKGLDEMQQMVANQAFSTSDYFLLAVIKLAALVVAAASGFRGGRIFPAVFVGVALGLMLHEHVPAVPAAITVSCAILGIVLVVTRDGWLSLFMAAVVVPNTTLLPLLCIVMLPAWLLLAGKPMMMVNRPKQQPPHDNV", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family."}
{"protein": "MPRVSAPLVLLPAWLVMVACSPHSLRIAAILDDPMECSRGERLSITLAKNRINRAPERLGKAKVEVDIFELLRDSEYETAETMCQILPKGVVAVLGPSSSPASSSIISNICGEKEVPHFKVAPEEFVKFQFQRFTTLNLHPSNTDISVAVAGILNFFNCTTACLICAKAECLLNLEKLLRQFLISKDTLSVRMLDDTRDPTPLLKEIRDDKTATIIIHANASMSHTILLKAAELGMVSAYYTYIFTNLEFSLQRMDSLVDDRVNILGFSIFNQSHAFFQEFAQSLNQSWQENCDHVPFTGPALSSALLFDAVYAVVTAVQELNRSQEIGVKPLSCGSAQIWQHGTSLMNYLRMVELEGLTGHIEFNSKGQRSNYALKILQFTRNGFRQIGQWHVAEGLSMDSHLYASNISDTLFNTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMDVPIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWEGGKCPKEEDHRAKGLGMENIGGIFVVLICGLIVAIFMAMLEFLWTLRHSEATEVSVCQEMVTELRSIILCQDSIHPRRRRAAVPPPRPPIPEERRPRGTATLSNGKLCGAGEPDQLAQRLAQEAALVARGCTHIRVCPECRRFQGLRARPSPARSEESLEWEKTTNSSEPE", "text": "FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK4 subfamily."}
{"protein": "MKTQIVILIVAVLFLQLVSQSDAFLKGIIDTVSKLFGKRGLKNLDQYNDLFDGEISDADIKYLQDLMR", "text": "FUNCTION: Amphipathic peptide that shows no antibacterial activity even at 50 uM but shows a low hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Forms a helical membrane channel in the prey. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short antimicrobial peptide (group 4) family."}
{"protein": "MSIMKKRSSRAADPDELLCCCEYIDRHGSRSHMVACCCDCEDLDEACDRWMNKEPQNPDSVSRALATINDRLRVPWISGARQIDVSLIPPLILLPVFLHIAALHYLLGIIMLTAMPITVLWYYFFTHRKKGRTLFFLGLALFSLFYMFYLFLTQVVPRGEVTELQLAVVTAGVALTVIFLMLTKRGPGLVRPRPSETHSTVTYHSTPPDVDGVYLNGARHQVVIGSRVASSEHTGEPGTEEEEEGVQKRNWCAVCKVVRPQRAGHCRICGVCVLRLDHHCVWINSCVGLANHRTFLLTLLFFLLTSIYGISLVLASVCPDQRVLTALFYCPDVYSQYSSALCFTCAWYSSIVTGGLLHLLLLQILNISLNVTEREARLALREKSAQRRLWGLIVHTGHYSRGFWSNWTEFLTMTEDTQPAGHKTEDLV", "text": "FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MMCTAKKCGIRFQPPAIILIYENEIKGKSRQRIMPVRNFSKYSDCSRAAEQLKNNPRHKGYLEQVSLKQLEKLFSFLRGNLWGQSLAETMEQIQRETTIDPEEDLNKLDDKELAKRKSIMDELFEKNQKKKDDPNFVYDIEVEFPQDEQLQSCGWDTESAEEF", "text": "FUNCTION: Required for ciliation. Recruits the RABL2B GTPase to the ciliary base to initiate ciliation. After specifically capturing the activated GTP-bound RABL2B, the CEP19-RABL2B complex binds intraflagellar transport (IFT) complex B from the large pool pre-docked at the base of the cilium and thus triggers its entry into the cilia. Involved in the early steps in cilia formation by recruiting the ciliary vesicles (CVs) to the distal end of the mother centriole where they fuse to initiate cilium assembly. Involved in microtubule (MT) anchoring at centrosomes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, cilium basal body Note=Associates with the mother centriole in early interphase. Localizes to spindle poles during mitosis, and to distinct foci oriented towards the midbody at telophase. Localizes slightly apical to the subdistal appendage on the mother centriole, but below the distal appendage. SIMILARITY: Belongs to the CEP19 family."}
{"protein": "MTQYLPPNLLALFAAREPIPFMPPVDKLPHEKKSRGYLGVAKFMADFEDPKDTPLPKTVETRQERLERRRREKAEQVAYKLEREIALWDPTEIKNATEDPFRTLFIARINYDTSESKLRREFEFYGPIKKIVLIHDQESGKPKGYAFIEYEHERDMHAAYKHADGKKIDSKRVLVDVERARTVKGWLPRRLGGGLGGTRRGGNDVNIKHSGREDNERERERYRLEREREDREGPGRGGGSNGLDARPGRGFGAERRRSRSRERRDRERDRGRGAVASNGRSRSRSRERRKRRAGSRERYDEFDRRDRRDRERERDRDREREKKKKRSKSRERESSRERRERKRERRDRERGTGSGGDVKERKPDFRDMDVIKIKEEPVDDGYPTFDYQNATIKREIDDEDEEKYRPPPAHHNMFSVPPPPILGRGNASTNPNPDNGQQSSGDPSWWRQ", "text": "FUNCTION: Mediates the splicing of pre-mRNA by binding to the stem loop I region of U1-snRNA (PubMed:15611175). Required during oogenesis for nurse cell chromatin dispersal (PubMed:24244416). SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleoplasm."}
{"protein": "MRGELWLLVLVLREAARALSPQPGAGHDEGPGSGWAAKGTVRGWNRRARESPGHVSEPDRTQLSQDLGGGTLAMDTLPDNRTRVVEDNHSYYVSRLYGPSEPHSRELWVDVAEANRSQVKIHTILSNTHRQASRVVLSFDFPFYGHPLRQITIATGGFIFMGDVIHRMLTATQYVAPLMANFNPGYSDNSTVVYFDNGTVFVVQWDHVYLQGWEDKGSFTFQAALHHDGRIVFAYKEIPMSVPEISSSQHPVKTGLSDAFMILNPSPDVPESRRRSIFEYHRIELDPSKVTSMSAVEFTPLPTCLQHRSCDACMSSDLTFNCSWCHVLQRCSSGFDRYRQEWMDYGCAQEAEGRMCEDFQDEDHDSASPDTSFSPYDGDLTTTSSSLFIDSLTTEDDTKLNPYAGGDGLQNNLSPKTKGTPVHLGTIVGIVLAVLLVAAIILAGIYINGHPTSNAALFFIERRPHHWPAMKFRSHPDHSTYAEVEPSGHEKEGFMEAEQC", "text": "FUNCTION: Plays a critical role in endothelial cell capillary morphogenesis. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Cell junction, tight junction. Note=Localized predominantly at the tight junctions of vascular endothelial cells and to a lesser extent at the luminal surface of vascular endothelial cells. SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: [Isoform 3]: Secreted. SUBCELLULAR LOCATION: [Isoform 2]: Secreted. SIMILARITY: Belongs to the plexin family."}
{"protein": "MRPWTGSWRWIMLILFAWGTLLFYIGGHLVRDNDRPDHSSRELSKILAKLERLKQQNEDLRRMAESLRIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNELQRHADEFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATGGWETVFRPVSETCTDRSGISTGHWSGEVKDKNVQVVELPIVDSLHPRPPYLPLAVPEDLADRLVRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATRKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVDKKRVYLATDDPSLLKEAKTKYPNYFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLHPDASANFHSLDDIYYFGGQNAHNQIAIYAHQPRTADEIPMEPGDIIGVAGNHWDGYSKGVNRKLGRTGLYPSYKVREKIETVKYPTYPEAEK", "text": "FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein Note=Membrane-bound form in trans cisternae of Golgi. SIMILARITY: Belongs to the glycosyltransferase 23 family."}
{"protein": "MDAQKDVQPPKQQPMIYICGECHTENEIKSRDPIRCRECGYRIMYKKRTKRLVVFDAR", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity). FUNCTION: Factor that activates expression from a metal response element of the mouse metallothionein-I gene. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family."}
{"protein": "MRNSNRGPAFLILFATLMAAAGDGVSIVAFPWLVLQREGSAGQASIVASATMLPLLFATLVAGTAVDYFGRRRVSMVADALSGAAVAGVPLVAWGYGGDAVNVLVLAVLAALAAAFGPAGMTARDSMLPEAAARAGWSLDRINGAYEAILNLAFIVGPAIGGLMIATVGGITTMWITATAFGLSILAIAALQLEGAGKPHHTSRPQGLVSGIAEGLRFVWNLRVLRTLGMIDLTVTALYLPMESVLFPKYFTDHQQPVQLGWALMAIAGGGLVGALGYAVLAIRVPRRVTMSTAVLTLGLASMVIAFLPPLPVIMVLCAVVGLVYGPIQPIYNYVIQTRAAQHLRGRVVGVMTSLAYAAGPLGLLLAGPLTDAAGLHATFLALALPIVCTGLVAIRLPALRELDLAPQADIDRPVGSAQ", "text": "FUNCTION: Efflux pump that contributes to intrinsic antibiotic resistance (PubMed:9811639, PubMed:12520088, PubMed:20525733, PubMed:30837962). The pump uses the electrochemical gradient as a source of energy (By similarity). Confers resistance to rifampicin (PubMed:20525733). Confers low-level resistance to tetracycline and to several aminoglycosides, including streptomycin, gentamicin, 2'-N- ethylnetilmicin and 6'-N-ethylnetilmicin (PubMed:9811639, PubMed:12520088). FUNCTION: Efflux pump that contributes to intrinsic antibiotic resistance. The pump uses the electrochemical gradient as a source of energy. FUNCTION: Efflux pump that contributes to intrinsic antibiotic resistance. The pump uses the electrochemical gradient as a source of energy. Confers resistance to various antibiotics, including tetracycline, acriflavine, spectinomycin and p-aminosalicylate. May be involved in export of toxic by-products that accumulate during stationary phase when nutrients are limited. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Drug:H(+) antiporter-3 (DHA3) (TC 2.A.1.21) family."}
{"protein": "MFESQDHSIRTITELKVRTFEEEMDPVRSWVRNVGVIDANIAAQSGVALSRAHFEKQPPSNLRKSNFFHFVLALYDRNGQPVEVERTSFVDFVEQDKTGEKTNNGTHYKLQLLYSNGVRTEQDLYARLIDSVTKQPISYEGQNKNPEMCRVLLTHEVMCSRCCEKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKTAGNPRDMRRFQVVLSTTVCVDGPVLAISDNMFVHNNSKHGRRSRRMDPNETVENNMEYATPCIKAISPSEGWTTGGAMVIVIGENFFDGLQVVFGSMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFIYTALNEPTIDYGFQRLQKLIPRHPGDPDKLAKEMLLKRAADVVESLYGNTTSNQDMLLKRAADIAEALYSVPRPHSQLQAMPSSPVHGSVMGLSSYPTQLGVSIGEPGQTSGQGYTRNSSSLSPRGYPSSSTPQQSAYGSNGGMSYGAVPMSSLGVSGSPGFNSASPNSSPYAIMPSSPPGSSSSSSLLPFSSFPSSTKQKSAFAPVLRPQGFPHHPSAKTSGGTSFRAMTGLVVPPM", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the COE family."}
{"protein": "MTKKDKKPKVATITTKSGETLKVFEDLAQFEDFLKHETEDDDDFDNVHCQLKYYPPFVLHEAHDDPEKIKDTANSHSKKYVRHLHQHVEKHLLKEIKEALQLPDLKFKDKSKDEDFEKIVWNYGDTGEFHDRKFRISISVTCKHDDAMVDLDYKTVPLTEESVI", "text": "FUNCTION: Involved in the control of energetic metabolism and significantly contribute to cell fitness, especially under respiratory growth conditions. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the RGI1 family."}
{"protein": "MSSELLDALTILEKEKGISKEIIIEAIEAALISAYKRNFNQAQNVRVDLNRETGSIRVFARKDVVDEVYDQRLEISIEEAQGIHPEYMVGDVVEIEVTPKDFGRIAAQTAKQVVTQRVREAERGVIYSEFIDREEDIMTGIVQRLDNKFIYVSLGKIEALLPVNEQMPNESYKPHDRIKVYITKVEKTTKGPQIYVSRTHPGLLKRLFEIEVPEIYDGTVELKSVAREAGDRSKISVRTDDPDVDPVGSCVGPKGQRVQAIVNELKGEKIDIVNWSSDPVEFVANALSPSKVLDVIVNEEEKATTVIVPDYQLSLAIGKRGQNARLAAKLTGWKIDIKSETDARELGIYPRELEEDDEPLFTEPETAESDE", "text": "FUNCTION: Participates in both transcription termination and antitermination. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NusA family."}
{"protein": "MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSVVFDKGGVLEQICEGKGYIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYLGQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDMRLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAVKFSRE", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate to glycolate as well as succinic semialdehyde (SSA) to gamma- hydroxybutyrate in vitro. May function in redox homeostasis and play a role in oxidative stress tolerance by detoxifying glyoxylate and SSA generated in glycolate metabolism and GABA metabolism, respectively. SUBCELLULAR LOCATION: Cytoplasm, cytosol Note=According to PubMed:22309191, GLYR1 does not localize in the peroxisome as initially described in PubMed:18495639. SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily."}
{"protein": "MGKEVMGKKENEMAQEKERPAGSQSLFRGLMLIEILSNYPNGCPLAHLSELAGLNKSTVHRLLQGLQSCGYVTTAPAAGSYRLTTKFIAVGQKALSSLNIIHIAAPHLEALNIATGETINFSSREDDHAILIYKLEPTTGMLRTRAYIGQHMPLYCSAMGKIYMAFGHPDYVKSYWESHQHEIQPLTRNTITELPAMFDELAHIRESGAAMDREENELGVSCIAVPVFDIHGRVPYAVSISLSTSRLKQVGEKNLLKPLRETAQAISNELGFTVRDDLGAIT", "text": "FUNCTION: Negatively controls the transcription of the yiaKLMNOPQRS operon, which may be involved in the utilization of 2,3-diketo-L- gulonate."}
{"protein": "MPSFNPVRFLELPIDIRKEVYFHLDGNFCGAHPYPIDILYKSNDVELPGKPSYKRSKRSKKLLRYMYPVFATYLNIFEYSPQLIEKWLEYAFWLRYDCLVLDCFKVNHLYDGTLIDALEWTYLDNELRLAYFNKASMLEVWYTFKEYKKWVIDSVAFDELDLLNVSNIQFNIDNLTPQLVDKCLSILEQKDLFATIGEVQFGQDEEVGEEKDVDVSGANSDENSSPSSTIKNKKRSASKRSHSDNGNVGATHNQLTSISVIRTIRSMESMKSLRKITVRGEKLYELLINFHGFRDNPGKTISYIVKRRINEIRLSRMNQISRTGLADFTRWDNLQKLVLSRVAYIDLNSIVFPKNFKSLTMKRVSKIKWWNIEENILKELKVDKRTFKSLYIKEDDSKFTKFFNLRHTRIKELDKSEINQITYLRCQAIVWLSFRTLNHIKLQNVSEVFNNIIVPRALFDSKRVEIYRCEKISQVLVI", "text": "FUNCTION: Acts as central component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere."}
{"protein": "MALSRVCWARAALWGSAVPPGLYVVRRLQFVRSGLTWGAPRSSKLHLSPKADVKSLISYVVTKTKVINGKYHRFLGRHFPRFYVPYTIFMKGLQMLWADGKKARRIKTNMWKHNIKFHQLPYREMEHLRQFRRDVTKCLFLGILSIPPFANYLVFLLMYLFPRQLLIRHFWTPKQQIDFLDIYHALRKQSHPEILCYLEKVVPLISDAGLQWHMTELCTKMQRGTHPAVHDILALRECFANHPLGMDQLRALQMKALCRAMLLTPYLPSVLLRHRLKTHTTVIHQLDKALAKLGVGQLTAQEVKSACYLRGLNSTHIAEERCRTWLGEWLQISCSLKETELSLLLHNVVLLSINYVGSRR", "text": "FUNCTION: Plays an essential role for mitochondrial structure and function, as well as thermogenesis of brown adipocytes. In brown adipose tissue also localizes in the nucleus where it interacts with the chromatin remodeler SMARCA4 to regulate thermogenic genes expression, such as UCP1 (By similarity). May regulate phagocytosis and inflammatory responses to lipopolysaccharide in macrophages (By similarity). Involved in tumorigenesis and may function as a negative regulator of the p53/TP53 (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Nucleus Mitochondrion inner membrane; Single- pass membrane protein."}
{"protein": "MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPSPLASIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILNSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSPVQEGNQSENKKRVEVIDLTIESSSDEEDLPPTKKHCPVTSAAIPALPGSKGALTSGHQPSSVLRSPAMGTLGSDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYSPSVITSLDEQDTLGHFFQFRGTPPHFLGPLAPTLGSSHRSATPAPAPGRVSSIVAPGSSLREGHGGPLPSGPSLTGCRSDVISLD", "text": "FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1. Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus speckle Note=Colocalizes with MITF in the nucleus. Colocalizes with GFI1 in nuclear dots. Colocalizes with SUMO1 in nuclear granules. SIMILARITY: Belongs to the PIAS family."}
{"protein": "MISTSSILILVFLLACFMATSAQWGYGGYGRGYGGYGGYGRGMYGGYGRGMYGGYGRGMYGGWGK", "text": "FUNCTION: May have antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the YARP (YGGW-amide related peptide) family."}
{"protein": "MDKELLQSTVRKVLDEMRQRPIPLGVSNRHIHLSAQDYERLFPGHPISEKKALLQPGQYAAEQTVTLVGPKGQLKNVRLLGPLRSVSQVEISRTDARTLGIAAPLRMSGNLKGTPGIRLVSPFAELELPSGVIVAQRHIHMSPLDALILRVSHGDMVSVAIEGDDRGLIFNNVAIRVSPDMRLEMHIDTDEANAAGADNPHAFARLVGPR", "text": "FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. FUNCTION: Involved in 1,2-propanediol (1,2-PD) utilization in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. Also able to catalyze the reverse reaction. Also has phosphate acetyltransferase activity to a lesser extent (PubMed:17158662). Required for optimal growth on 1,2-PD when the BMC is intact. CoA is regenerated within the BMC (for use by PduP) via this enzyme, although there must also be cofactor transport across the BMC. Directly targeted to the BMC (PubMed:25962918). SUBCELLULAR LOCATION: Bacterial microcompartment Note=Probably located inside the BMC shell. SIMILARITY: Belongs to the PduL family."}
{"protein": "MLKRQLLLAHRGYSDIAPENTQLAFELAFQYRFDGVELDVHLTKDGELVIIHDETTTRTALVDKTIELETLASLKQDDHSAFFKFKTQPQPIMTLKEFFDQYLDKFQLINVEIKTDQKEYPGIEAKIDALAQQYGKKVIEKVVFSSFNFASLQRLYDINPNYQIAFLFWTKKQFQAVDALKIKQVCQYLHPWTNIYEKFPDMVLSLQLPLGLWTLNSEVKFHQFRQDRMVYAQIANKKFEV", "text": "SIMILARITY: To M.genitalium MG385. SIMILARITY: To glycerophosphoryl diester phosphodiesterases (EC 3.1.4.46)."}
{"protein": "MYYGLDIGGTKIELAVFNEELEKLYSERVPTPKTDYEEWLNTIVDLVNRADEKFGEVGTVGLGVPGFVNQQTGLAEITNIRVADNKPILRDLSVRLGREVRAENDANCFALSEAWDTENQQYPTVLGLILGTGFGGGFVLNGKVHSGQVGMAGELGHLQLNYHALKLLGWDNAPIYQCGCGNKACLDNYLSGRGFEMLYRDLKGETLSAREIIDLFYQGNESAVDFVNLFVELAAISIGNIITAFDPHMIVLGGGLSNFDYLYEALPKALPPHLMRTAKVPPIKKAKHGDSGGVRGAAALFLTK", "text": "FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily."}
{"protein": "MAYSSCLNRSLKPNKLLLRRIDGAIQVRSHVDRTFYSLVGSGRSGGGPPGLLSSRESIHPLSVYGELSLEHRLRFVLNGKMEHLTTHLHRPRTTRSPLSFWGDGGIVPFEPFFHAFPGGLEKAVINRTSLILPS", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf68 family."}
{"protein": "MAAKLLLLLCLFSGLHARSRRVEEDDSEDSPSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDAHACPLTFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTTLGITTVLTMTTLSTIARKSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTIRKKKTSLLHPDSTRWIPDRISLQAPSNYSLLDMRPPPPVMITLNNSMYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRRGRIHIDVSELDSYSRVFFPTSFLLFNLVYWVGYLYL", "text": "FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRG3 sub- subfamily."}
{"protein": "MTQEPFREELAYDRMPTLERGRQDPASYAPDAKPSDLQLSKRLPPCFSHKTWVFSVLMGSCLLVTSGFSLYLGNVFPAEMDYLRCAAGSCIPSAIVSFTVSRRNANVIPNFQILFVSTFAVTTTCLIWFGCKLVLNPSAININFNLILLLLLELLMAATVIIAARSSEEDCKKKKGSMSDSANILDEVPFPARVLKSYSVVEVIAGISAVLGGIIALNVDDSVSGPHLSVTFFWILVACFPSAIASHVAAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSIMRIVEMFKDYPPAIKPSYDVLLLLLLLVLLLQAGLNTGTAIQCVRFKVSARLQGASWDTQNGPQERLAGEVARSPLKEFDKEKAWRAVVVQMAQ", "text": "FUNCTION: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Cell membrane Cytoplasm, perinuclear region Endoplasmic reticulum."}
{"protein": "MGTTNGTDYGAYTYKELEREQYWPSENLKISITGAGGFIASHIARRLKHEGHYVIASDWKKNEHMTEDMFCDEFHLVDLRVMENCLKVTEGVDHVFNLAADMGGMGFIQSNHSVIMYNNTMISFNMIEAARINGIKRFFYASSACIYPEFKQLETTNVSLKESDAWPAEPQDAYGLEKLATEELCKHYNKDFGIECRIGRFHNIYGPFGTWKGGREKAPAAFCRKAQTSTDRFEMWGDGLQTRSFTFIDECVEGVLRLTKSDFREPVNIGSDEMVSMNEMAEMVLSFEEKKLPIHHIPGPEGVRGRNSDNNLIKEKLGWAPNMRLKEGLRITYFWIKEQIEKEKAKGSDVSLYGSSKVVGTQAPVQLGSLRAADGKE", "text": "FUNCTION: Catalyzes a reversible epimerization of GDP-D-mannose that precedes the committed step in the biosynthesis of vitamin C (L- ascorbate), resulting in the hydrolysis of the highly energetic glycosyl-pyrophosphoryl linkage. Able to catalyze 2 distinct epimerization reactions and can release both GDP-L-galactose and GDP-L- gulose from GDP-mannose. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MRERVTFIHNDYSLDPEALDNQDAGLLGPQIETVRQDKLTIPFGELPSELTDILQEYEALHIRWASPVKSETMDPFTSRISPGLHVYATPVLPSSCNPTKLCSWLQRFGPLDCSKPEAFTEFQQSTSTSPSFSFYEALEDLHSFITTSSQEFCPELDSVCNARLRSLLTASGLDLSFDKAANALVVSALWPLRPQTVAVPASSARRVEVGIFINDRSQPNMKENELGVAGVLSVLGDQKKPSPTIFTFPARHRRDGSVFTSKFLTPTGLHPTLQLSFNSNKLPSADGECAPYAFLTLPKTIFADRYQLGDELFLASKNLTALRYTTLPVDLEAPAYTTETWGSSILLGLAPPDPGTEKPWSVEIPLHLRYLKPSATGQVEIEIPYPAVFWACSSEEGTLESPFDRLHVGYDYLFPRDTVFWHANPQPENGSRLMNRVTVPVLDDDGVGSIRSGTAIAVAIGFAWVMWKLVSVMLKSDRAPAGVTKETKQKKSH", "text": "FUNCTION: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase GPI14 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the PIGX family."}
{"protein": "MEDSGIQRGIWDGDAKAVQQCLTDIFTSVYTTCDIPENAIFGPCVLSHTSLYDSIAFVALKSTDKRTVPYIFRVDTSAANGSSEGLMWLRLVQSARDKEEQNLEAYIKNGQLFYRSLRRIAKDEELLVWYGKELTELLLLCPSRAHKMNGSSPYTCLECSQRFQFEFPYVAHLRFRCPKRLHSTDANPQDEQGGGLGTKDHGGGGGGKEQQQQQQQQQQEAPLIPGPKFCKAGPIHHYPASSPEASNPPGSAGAGSAKPSTDFHNLARELENSRGSSSCVAAPGVGSGGSGHQEAELSPDGVATGGCKGKRRFPEEAAAEGGGAGLAGGRARFSERPLATSKEELVCTPQQYRAAGSYFGLEENGRLFAPPSPETGEAKRSAFVEVKKAGRAVGLQEEAAATDGAGGTAEDPDAGGGVAGGGSNGSSTPAAGSPGAPEKLLAPRPGGSLPGRLEGGSPARGSAFTSVSQLGGGGGAGTAGTAGGSGGGQTAASDERKSAFSQPARSFSQLSPLVLGQKLGALEPCHPGDGVGPTRLYPAAADPLAVKLQGAADLNGACGPLASGGGGGLPKQSPFLYATAFWPKSSAAAAAAAAAAAGPLQLQLPSALTLLPPSFTSLCLPAQNWCAKCNASFRMTSDLVYHMRSHHKKEYAMEPLVKRRREEKLKCPICNESFRERHHLSRHMTSHN", "text": "FUNCTION: Probable histone methyltransferase, preferentially acting on 'Lys-9' of histone H3 (PubMed:19646955). Histone methyltransferase activity has not been confirmed in other species. Involved in the control of steroidogenesis through transcriptional repression of steroidogenesis marker genes such as CYP17A1 and LHCGR (PubMed:19646955). Forms with BHLHE22 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation (PubMed:22284184). In the retina, it is required for rod bipolar and type 2 OFF-cone bipolar cell survival (PubMed:26023183). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily."}
{"protein": "MSTVLCCVLVLLISVALCMDFEERPSSSWRSEQTMFLKSHKSRNLLSLRDLQQPDHGKMKRSEESAQNQCESLHGYQSTLQNDTHTHNFNDLSGSVSLAWVGDGTGVLLVLTTFQVPLFIMRFGQSKLYRSEDYGKTFQDITDLINNTFIQTEFGIAIGPDNSGKVILTGDLAEGKVTKIFRSVDFGKSFVTSELPFHPLMQITYNPKDSNILMVYSINYDLWLSKDFGANWKKIHESVCLVKWGIDDTIFLTTNPNGSCSDRGTLELRKSLDYGKTFKTIGNRIYSFGLGGRFVFASIMTDSGSTRMIHVSVDQGETWDMAQLPTVGHEQFYSILAANNDMVFMHVDEPGDSGIGTIYISDDRGIVFSKSLERHLYTTTGGDTDFTNITSLRGVYITSVLAEDGSVQTVITFNQGGEWRPLMKPWNGVCDSTAKHPSECSLHIHASYSISMKLNVPMQPLSETNAVGLVLAHGSVGGAVSVLSPDVYVSDDGGYTWFQALKGPHHYAILDSGGLLVAVEHNPTHPISQIKFSTDEGQCWHAHNFTDDPIYFTGLASEPGARSMNVSLWGYRDTILNQYWVSVTVDFRQLLSRDCQENDYIQWLAHSSDINSPTDGCVLGYKERFLRLRRDSVCWNGRDYKVTKEPTTCPCTLTDFHDFGFYHEENSSVCVEQPDLIGHSLEFCLHGRKEQLQTSGYRKIPGDHCEEGITPERKEIDLSKKCVSNLLRTEQLTKEHSFNSAPIIAVVIIVLLISAVAGVIFIKKYVCGGRFLVHRYSVLQQHAEANGIDGLDDLDTLEGGKTHYHDDSDEDLLE", "text": "FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. May also mediate transport from the endoplasmic reticulum to the Golgi. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein Endosome membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Nucleus membrane; Single-pass type I membrane protein Cell membrane; Single-pass type I membrane protein; Extracellular side Lysosome membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the VPS10-related sortilin family. SORT1 subfamily."}
{"protein": "MASNESGGGNLMDEFEEAFQSCLLTLTKQEPNSGTNKEEIDLEVQKTTNRFIDVARQMEAFFLQKRFLVSTLKPYMLIKDENQDLSIEIQRKEALLQKHYNRLEEWKACLSDIQQGVHSRPTPPIGSGMLQGPGGGMPPMGGTPPRPGMMPGMPPGAMQPGGPMQPSPHMLQAQQMQQLRMISRQMPPK", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 28 family."}
{"protein": "MSEYMKNEILEFLNRHNGGKTAEIAEALAVTDYQARYYLLLLEKEGMVQRSPLRRGMATYWFLKGEMQAGQNCSSTT", "text": "FUNCTION: Plays a role in the inhibition of methylation at the GATC1028 site located in the regulatory region upstream of the pabA promoter. May, in conjunction with the Mbf (methylation blocking factor), inhibits deoxyadenosine methylase from methylating the GATC1028 site. SIMILARITY: To E.coli AfaF and DaaF."}
{"protein": "MILTVTLNPAIDVSYPLDELKCDTVNRVVDVTKTPGDKGLNVCRVLNDFGETVKATGCIGGESGDFIINHLPDSILSRFYKISGDTRTCIAILHEGNQTEILEKGPLLSVEEIDGFTHHFKYLLNDVDVVTLSGSLPAGMPDDYYQKLIGIANLNGKKTVLDCSGNALEAVLKGDSKPTVIKPNLEELSQLLGKEMTKDFEALKEVLQDELFEGIEWIIVSLGADGVFAKHNDTFYNVDIPKIEIVSAVGSGDSTVAGIASGLANDEDDRALLTKANVLGMLNAQEKTTGHVNMANYDKLYQSIKVKEV", "text": "SIMILARITY: Belongs to the carbohydrate kinase PfkB family. LacC subfamily."}
{"protein": "MKWDKLLNDKRRRESGVTRSKNTDVRSAFENDFQRIVMSASFRRLQDKTQVFPLEKSDFVRTRLTHSMEVSTIAKSMGNMVTHTIQEEKLDQDFTKDHADKIPEILACAGLLHDMGNPPFGHFGEESIREWFRDNLATITYKNKSLAEILTPQMKEDFYYFEGNAQVLRVVSKLHYLFDQYGLNLTFATLNAVIKYPVSSLKVNKKQIKSKKLGYFYADESLFNEITTATEALDNRHPLTYLLEVADDIAYLNADLEDGVKKGIVNITQILKGFEEVEEHNKVTAACYNELKKKSERYEGQEESFIVQQWLASNVRGQLINRSLEVFYENYDAIMAGTFNDSLIDASSAEQLVQILQSLSFTYIYQDKGIVESEIAGNEIISKLLETFIPAVIYYDSETPERQTAKDKRLLTLISDNYLGCYRKNAEGESETMKLYLRLLLVTDFICGMTDSYAKDLYQRLNGLS", "text": "SIMILARITY: Belongs to the dGTPase family. Type 3 subfamily."}
{"protein": "MENILLGIVQGLTEFLPVSSSGHLAIFTAIFNKTPDVGYFAFLHLATFLAVVIFVKKEIFEIINGVFKKDEKYITLSLKLFVSMIPAAIVGIFFEDFIKSIFSETFFIGVFLAITGVFMLLSDKMDKNLKTITKIPYLDAFIIGIFQAFSVLPGISRSGSTLFAALLLGVKKEDAVKYSFLMSLPVIFGAGVLEMQKTVITKEYVYGFIVAFLTGILGLHLLKKMVIAGKLKFFGYYCFLASLFVIFYI", "text": "FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family."}
{"protein": "MSEQKVKLMEEEMNVYRVQGFTCANCAGKFEKNVKKIPGVQDAKVNFGASKIDVYGNASVEELEKAGAFENLKVSPEKLANQTIQRVKDDTKAHKEEKTPFYKKHSTLLFATLLIAFGYLSHFVNGEDNLVTSMLFVGSIVIGGYSLFKVGFQNLIRFDFDMKTLMTVAVIGATIIGKWAEASIVVILFAISEALERFSMDRSRQSIRSLMDIAPKEALVRRNGQEIIIHVDDIAVGDIMIVKPGEKIAMDGIIVNGLSAVNQAAITGESVPVSKAVDDEVFAGTLNEEGLIEVKITKYVEDTTITKIIHLVEEAQGERAPAQAFVDKFAKYYTPIIMVIAALVAVVPPLFFGGSWDTWVYQGLAVLVVGCPCALVISTPISIVSAIGNAAKKGVLVKGGVYLEKLGAIKTVAFDKTGTLTKGVPVVTDFEVLNDQVEEKELFSIITALEYRSQHPLASAIMKKAEQDNIPYSNVQVEEFTSITGRGIKGIVNGTTYYIGSPKLFKELNVSDFSLGFENNVKILQNQGKTAMIIGTEKTILGVIAVADEVRETSKNVIQKLHQLGIKQTIMLTGDNQGTANAIGTHVGVSDIQSELMPQDKLDYIKKMQSEYDNVAMIGDGVNDAPALAASTVGIAMGGAGTDTAIETADIALMGDDLSKLPFAVRLSRKTLNIIKANITFAIGIKIIALLLVIPGWLTLWIAILSDMGATILVALNSLRLMRVKDK", "text": "FUNCTION: Couples the hydrolysis of ATP with the export of cadmium (PubMed:1530844). Involved in cadmium resistance (PubMed:2524829, PubMed:1530844). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily."}
{"protein": "MDSKTPVTLAKVIKVLGRTGSRGGVTQVRVEFLEDTSRTIVRNVKGPVRENDILVLMESEREARRLR", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 family."}
{"protein": "MITLITEQLQKQTLDELKCTRFSISLPLPDHADISNCGNSFQLVSEGASWRGLPHCSCAEFQDSLNFSYHPSGLSLHLRPPSRGNSPKEQPFSQVLRPEPPDPEKLPVPPAPPSKRHCRSLSVPVDLSRWQPVWRPAPSKLWTPIKHRGSGGGGGPQVPHQSPPKRVSSLRFLQAPSASSQCAPAHRPYSPPFFSLALAQDSSRPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPASSPELPWRPRGLRNLPRSRSQPCDLDARKTGVKRRHEEDPRRLRPSLDFDKMNQKPYSGGLCLQETAREGSSISPPWFMACSPPPLSASCSPTGGSSQVLSESEEEEEGAVRWGRQALSKRTLCQRDFGDLDLNLIEEN", "text": "SIMILARITY: Belongs to the FAM53 family."}
{"protein": "MGRAPCCEKIGLKRGRWTAEEDEILTKYIQTNGEGSWRSLPKKAGLLRCGKSCRLRWINYLRRDLKRGNITSDEEEIIVKLHSLLGNRWSLIATHLPGRTDNEIKNYWNSHLSRKIYAFTAVSGDGHNLLVNDVVLKKSCSSSSGAKNNNKTKKKKKGRTSRSSMKKHKQMVTASQCFSQPKELESDFSEGGQNGNFEGESLGPYEWLDGELERLLSSCVWECTSEEAVIGVNDEKVCESGDNSSCCVNLFEEEQGSETKIGHVGITEVDHDMTVEREREGSFLSSNSNENNDKDWWVGLCNSSEVGFGVDEELLDWEFQGNVTCQSDDLWDLSDIGEITLE", "text": "FUNCTION: Flavonol-specific transcription activator involved in the regulation of several genes of flavonoid biosynthesis. Activates the expression of CHS, CHI, F3H and FLS1. Controls flavonol biosynthesis primarily in cotyledons and leaves (PubMed:17419845, PubMed:20731781). Confers tolerance to UV-B (PubMed:19895401). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSPSESFNSFSLFSTLSMFKFLTQITFSRPFVYSALNKGCPDFLITSNCIHGNSWPHLSNLFEVKNFLMPSEDPPQLQNCKVIFLHGNTNAPTPLRPMEFRAIAFTTISPYIRVCVST", "text": "FUNCTION: Essential for the functional mitochondria and respiratory growth. SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MKKRKQYCGYIAIVGKPNVGKSTLINEIIENEISITSKKKNTTQKNILGIKTKQLHQFIYVDTPGIYLNNEKDDSFKIIKSSILILFIVDRTVWKTDDEIVLNKIKKNKIPIICVINKIDKILDKSIILPHINFLLKKINPIEIIPISAKKRENIVLLENLIYPYLPNNNHIFPKKYITTHSLSFSISEIIRQKLIFFLRDELPSIITVKIESIEEKFKKKLYIRAAIYVKHERQKKIIIGKKAEGIKKISIASRLDIEKKINMKIYLIIWVKVKIKK", "text": "FUNCTION: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family."}
{"protein": "MTDQPAQNGLIPPPTSEPSKAAASAETKPKKRICCACPDTKKLRDECIVEHGESACTKWIEAHKICLRAEGFNV", "text": "FUNCTION: Copper chaperone for cytochrome c oxidase (COX). Binds 2 copper ions and delivers them to the Cu(A) site of COX (By similarity). Can complement the yeast mutant cox17. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the COX17 family."}
{"protein": "MTSPVAQCASVPDSGLLCLVMLARYHGLAADPEQLRHEFAEQAFCSETIQLAARRVGLKVRRHRPAPARLPRAPLPAIALDRQGGYFVLARFEPGADQAVLIQRPGQAPARLGQAEFEALWAGELLLCACAASPTQALARFDFSWFIPALVKHRHLIGEVLLISLVLQFISLLTPLFFQVVMDKVLVNNAMETLNVIAVGFLAAILFEALLTGIRTYLFAHTSSKLDVELGARLYAHLLRLPLAYFQARRVGDSVARVRELEHIRAFLTGNAVTVLLDVVFSVVFIAVMFFYSVKLTLVVLAALPCYFLLSLVLTPVLRRRLDVKFNRGAENQAFLVETVSGIDTVKSLAVEPQWQRNWDRQLAGYVAAGLSVANVAMLANTGVTLISRLVALGVLWVGATEVVAQRMTVGELVAFNMLSGHVTQPVIRLAQLWNDFQQTGVSMQRLGDILNCRTEVAGDKAQLPALRGSIELDRVSFRYRPDAADALRNVSLRIAPGEVVGVVGRSGSGKSTLTRLIQRMFVADRGRVLIDGHDIGIVDSASLRRQLGVVLQESTLFNRSVRDNIALTRPGASMHEVVAAARLAGAHEFICQLPEGYDTMLGENGVGLSGGQRQRIGIARALIHRPRVLILDEATSALDYESEHIIQRNMRDICDGRTVIIIAHRLSAVRCADRIVVMEGGEVAECGSHETLLAAGGLYARLQALQAGEAG", "text": "FUNCTION: Involved in the export of calmodulin-sensitive adenylate cyclase-hemolysin (cyclolysin). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Cyclolysin exporter (TC 3.A.1.109.2) family."}
{"protein": "MQQPMNYPCPQIFWVDSSATSSWAPPGSVFPCPSCGPRGPDQRRPPPPPPPVSPLPPPSQPLPLPPLTPLKKKDHNTNLWLPVVFFMVLVALVGMGLGMYQLFHLQKELAELREFTNQSLKVSSFEKQIANPSTPSEKKEPRSVAHLTGNPHSRSIPLEWEDTYGTALISGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNQPLNHKVYMRNSKYPEDLVLMEEKRLNYCTTGQIWAHSSYLGAVFNLTSADHLYVNISQLSLINFEESKTFFGLYKL", "text": "FUNCTION: [FasL intracellular domain]: Cytoplasmic form induces gene transcription inhibition. FUNCTION: Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells (PubMed:7511063). Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development (PubMed:19794494, PubMed:7532682). Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses (PubMed:19794494). TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance (PubMed:10779162). Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis (By similarity). FUNCTION: [Tumor necrosis factor ligand superfamily member 6, soluble form]: Induces FAS-mediated activation of NF-kappa-B, initiating non- apoptotic signaling pathways (PubMed:19794494). Can induce apoptosis but does not appear to be essential for this process (By similarity). SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 6, soluble form]: Secreted Note=May be released into the extracellular fluid by cleavage from the cell surface. SUBCELLULAR LOCATION: [Isoform FasL]: Cell membrane; Single-pass type II membrane protein Cytoplasmic vesicle lumen Lysosome lumen Note=Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination. Colocalizes with the SPPL2A protease at the cell membrane. SUBCELLULAR LOCATION: [FasL intracellular domain]: Nucleus Note=The FasL ICD cytoplasmic form is translocated into the nucleus. SIMILARITY: Belongs to the tumor necrosis factor family."}
{"protein": "MGTGAADGSRGARRWLPWLGLFFWAAGAAAARGADGSEILPDSIPSAPGTLPHFIEEPEDAYIIKSNPIALRCKARPAMQIFFKCNGEWVHQNEHVSEESLDESSGLKVREVFINVTRQQVEDFHGPEDYWCQCVAWSHLGTSKSRKASVRIAYLRKNFEQDPQGREVPIEGMIVLHCRPPEGVPAAEVEWLKNEEPIDSEQDENIDTRADHNLIIRQARLSDSGNYTCMAANIVAKRRSLSATVVVYVNGGWSSWTEWSACNVRCGRGWQKRSRTCTNPAPLNGGAFCEGMSVQKITCTALCPVDGSWEVWSEWSVCSPECEHLRIRECTAPPPRNGGKFCEGLSQESENCTDGLCILDKKPLHEIKPQRWSRRGIENASDIALYSGLGAAVVAVAVLVIGVTLYRRSHSDYGVDVIDSSALTGGFQTFNFKTVRQGNSLLLNPAMQPDLTVSRTYSGPICLQDPLDKELMTESSLFNPLSDIKVKVQSSFMVSLGVSERAEYHGKNHSGTFPHGNNRGFSTIHPRNKTPYIQNLSSLPTRTELRTTGVFGHLGGRLVMPNTGVSLLIPHGAIPEENSWEIYMSINQGEPSLQSDGSEVLLSPEVTCGPPDMLVTTPFALTIPHCADVSSEHWNIHLKKRTQQGKWEEVMSVEDESTSCYCLLDPFACHVLLDSFGTYALTGEPITDCAVKQLKVAVFGCMSCNSLDYNLRVYCVDNTPCAFQEVISDERHQGGQLLEEPKLLHFKGNTFSLQVSVLDIPPFLWRIKPFTACQEVPFSRVWSSNRQPLHCAFSLERYTPTTTQLSCKICIRQLKGHEQILQVQTSILESERETITFFAQEDSTFPAQTGPKAFKIPYSIRQRICATFDTPNAKGKDWQMLAQKNSINRNLSYFATQSSPSAVILNLWEARHQQDGDLDSLACALEEIGRTHTKLSNITEPQIDDADFNYSRQNGL", "text": "FUNCTION: Receptor for the netrin NTN4 that promotes neuronal cell survival (PubMed:21216843). Plays a role in cell-cell adhesion and cell guidance. Receptor for netrin involved in cell migration (By similarity). Plays a role in the regulation of neuronal cell migration in the developing brain via its interaction with FLRT2 (PubMed:21673655). Plays a role in axon guidance by mediating axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (PubMed:21673655). May play a role in apoptosis in response to DNA damage. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). Mediates cell-cell adhesion via its interaction with FLRT3 on an adjacent cell (PubMed:26235030). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the unc-5 family."}
{"protein": "MANKQVEISMAEWDVMNIIWGKKSVSANEIVVEIQKYKEVSDKTIRTLITRLYKKEIIKRYKSENIYFYSSNIKEDDIKMKTAKTFLNKLYGGDMKSLVLNFAKNEELNNKEIEELRDILNDISKK", "text": "FUNCTION: Transcriptional repressor that constitutively blocks expression of beta-lactamase. Binds DNA as a dimer (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the BlaI transcriptional regulatory family."}
{"protein": "MNAMLETPELPAVFDGVKLAAVAAVLYVIVRCLNLKSPTAPPDLYFQDSGLSRFLLKSCPLLTKEYIPPLIWGKSGHIQTALYGKMGRVRSPHPYGHRKFITMSDGATSTFDLFEPLAEHCVGDDITMVICPGIANHSEKQYIRTFVDYAQKNGYRCAVLNHLGALPNIELTSPRMFTYGCTWEFGAMVNYIKRTYPQTQLVVVGFSLGGNIVCKYLGETQANQEKVLCCVSVCQGYSALRAQETFMQWDQCRRFYNFLMADNMKKIILSHRQALFGDHVKKPQSLEDTDLSRLYTATSLMQIDDNVMRKFHGYNSLKEYYEEESCMRYLHRIYVPLMLVNAADDPLVHESLLTIPKSLSEKRENVMFVLPLHGGHLGFFEGSVLFPEPLTWMDKLVVEYANAICQWERNKSQCSDTEQMEAELE", "text": "FUNCTION: Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane. Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1- arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA). Also displays an ester hydrolase activity against acetyl ester, butanoate ester and hexadecanoate ester. Plays a key role in sperm capacitation in response to progesterone by mediating degradation of 2AG, an inhibitor of the sperm calcium channel CatSper, leading to calcium influx via CatSper and sperm activation (By similarity). Involved in acrosomal reaction (Probable). May also play a role in smooth muscle cells migration (PubMed:15721306). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Cytoplasmic vesicle, secretory vesicle, acrosome membrane Note=Absent from the sperm flagellum. SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4 family."}
{"protein": "MSNISTKDIRKSKPKRGSGFDLLEVTESLGYQTHRKNGRNSWSKDDDNMLRSLVNESAKELGYENGLEDVKTIQQSNHLSKCIAWDVLATRFKHTVRTSKDVRKRWTGSLDPNLKKGKWTQEEDEQLLKAYEEHGPHWLSISMDIPGRTEDQCAKRYIEVLGPGSKGRLREWTLEEDLNLISKVKAYGTKWRKISSEMEFRPSLTCRNRWRKIITMVVRGQASEVITKAIKENKNIDMTDGKLRQHPIADSDIRSDSTPNKEEQLQLSQQNNPSLIKQDILNVKENESSKLPRLKDNDGPILNDSKPQALPPLKEISAPPPIRMTQVGQTHTSGSIRSKVSLPIEGLSQMNKQSPGGISDSPQTSLPPAFNPASLDEHMMNSNSISDSPKHAYSTVKTREPNSSSTQWKFTLKDGQGLSISNGTIDSTKLVKELVDQAKKYSLKISIHQHIHNHYVTSTDHPVSSNTGLSNIGNINGNPLLMDSFPHMGRQLGNGLPGLNSNSDTFNPEYRTSLDNMDSDFLSRTPNYNAFSLEATSHNPADNANELGSQSNRETNSPSVFYPQANTLIPTNSTATNNEIIQGNVSANSMSPNFNGTNGKAPSSTASYTTSGSEMPPDVGPNRIAHFNYLPPTIRPHLGSSDATRGADLNKLLNPSPNSVRSNGSKTKKKEKRKSESSQHHSSSSVTTNKFNHIDQSEISRTTSRSDTPLRDEDGLDFWETLRSLATTNPNPPVEKSAENDGAKPQVVHQGIGSHTEDSSLGSHSGGYDFFNELLDKKADTLHNEAKKTSEHDMTSGGSTDNGSVLPLNPS", "text": "FUNCTION: Activates HIS4 transcription only in combination with PHO2/BAS2. BAS1 is also involved in the regulation of the purine biosynthesis pathway. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSQPGARPGSKXREEALEQWVEERKKKRIAEKELRRINKKIKKLEDENPWLGNIVGLLRRKKDEEGGPPAKRPRREDMEIDSTPGRKSKTRGFTDQERRDHRRRKALENKKKQLAGGGKNLSREEEEELRRLARDDDERERRVAGPRPGGVNPMDGPPRGAPGGGFVPSLQGVPESPFSRTGEGIDIRGTQQFPWYGFTPPPPGYYWVPGCTQQ", "text": "FUNCTION: Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. Needs co- infection with hepatitis B virus to provide surface proteins, otherwise there is no packaging or budding. Packages the HDV ribonucleoprotein in hepatitis B virus empty particles. Interacts with both HDV genomic RNA and cytoplasmic tail of HBsAg. May inhibit viral RNA replication (By similarity). SUBCELLULAR LOCATION: Virion. Host nucleus, host nucleolus. Note=isoprenylated in the cytoplasm, and translocates in the nucleus possibly after phosphorylation. Translocates after to nuclear speckle, then to the ER membrane where interaction with Hepatitis B virus antigene takes place (By similarity). SIMILARITY: Belongs to the hepatitis delta antigen family."}
{"protein": "MSNKLAEIGNNIDSRYTAASGIRRQINKVFPTHWSFMLGEIALYSFIILLLTGVYLTLFFDPSITKVIYDGAYLPLNGVEMSRAYETALNLSFEVRGGLFIRQMHHWAALTFMVSMTVHMLRIFFTGAFRRPREANWIIGCVLLFLGMAEGFMGYSLPDDLLSGVGLRIMSAIILALPIIGTWLHWLIFGGDFPSDLMLDRFYIAHVLIIPGIILGLIAAHLALVWYQKHTQFPGAGRTENNVVGVRILPVFILETSSFGLVTFGVLALLAGLTSINAIWNLGPYNPSQVSAGSQPDIYMLWTDGAARVMPAWELYIGSYTIPGAFWVALLCGVLVGLLVGYPFIEKKITGDDAHHNLLQRPRDVPVRTSLGVMAIVFYFLLTLSGGNDLFAYHFEVSLNAMTWVGRIGLIVLPPLAYFITYRICLGLQRSDREVLEHGIETGVIKIMPNGAFVEVHQPLGPVDEHGHPVPLPYAGAPVPKQLNDLGFGGEPGRGGYFTPDNDSLAAKYAEIEHENHLEEMAMYKNLQKNNRAQDGVEED", "text": "FUNCTION: Cytochrome b subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family."}
{"protein": "MDIFIVKDNKYPKVDNDDNEVFILLGNHNDFIRLKLTKLKEHVFFSEYIVTPDTYGSLCVELNGSSFQHGGRYIEVEEFIDAGRQVRWCSTSNHISKDIPEDMHTDKFVIYDIYTFEAFKNKRLVFVQVPPSLGDDSHLTNPLLSPYYRNSVARQMVNNMIFNQDSFLKYLLEHLIRSHYRVSKHITIVRYKDTEELNLTRICYNRDKFKAFVFAWFNGVSENEKVLDTYKKVSNLI", "text": "FUNCTION: Late protein which is part of a large complex required for early virion morphogenesis. This complex participates in the formation of virosomes and the incorporation of virosomal contents into nascent immature virions. SUBCELLULAR LOCATION: Virion Note=Localizes to the virion core. SIMILARITY: Belongs to the orthopoxvirus OPG115 family."}
{"protein": "MTRSANSPFEVAIVGGGITGLALAVGLLKRNVSFTIYERAENFGELGVGITFTPNAQRAMEALDPCVLQSFTNVASAPSGGTINFVDGVREQGSEDPRTSTAALLFQLHVKGGYKACRRCDFVDQIVQHIPKDCVQYRKWLDSIETDHESGRAVLKFRDGEIAHADVVIGCDGIRSQVRASMFGTDELCPRAQYSHQLGYRGMVPLAQATAVLGPEKTSSAVLHTGPGAFVLTIPLAEVHAMHIEAFIMDKEEWPEVQTSSDSKRYVLPATRNEATKAFAEFGPTVRSAVSMFPEKLEKWAVFDMLEAPVPTFAKGRVCLAGDAAHASTPNQGGGAGFGIEDALVLAEVLAVLAEAPNVSGIVASEALAVYSEVRYERSQWLVRSSRRTGELCTWKDRDWGLAAEELSRDIISRSHQLWDHDTAGMVSDALAILGERVRGADTAF", "text": "FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of sorbicillinoids, a diverse group of yellow secondary metabolites that restrict growth of competing pathogenic fungi but not of bacteria (PubMed:25580210, PubMed:28618182). Sorbicillinoids biosynthesis requires the action of two PKSs (PubMed:25580210). SorA iteratively combines three acetyl units and the growing chain is modified by the ketoacyl reductase subunit, and optional by the enoyl reductase subunit in the second cycle (PubMed:25580210). The polyketide is then handed over to the PKS SorB, which adds three more acetyl units, and two methyl groups (PubMed:25580210). SorB releases an aldehyde, which undergoes spontaneous cyclization resulting in the formation of sorbicillin or 2',3'-dihydrosorbicillin (PubMed:25580210). The monooxygenase sorC oxidizes sorbicillin and 2',3'-dihydrosorbicillin to 2',3'- dihydrosorbicillinol and sorbicillinol, respectively (PubMed:28618182). The oxidoreductase sorD further converts sorbicillinol into oxosorbicillinol (PubMed:28618182). Sorbicillinol is the building block for the other sorbicillinoids such as disorbicillinol, bisvertinolon, and dihydrobisvertinolone (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family."}
{"protein": "MIKHVLLFFVFISFSVSANDFFRADSRTPDEIRRAGGLLPRGQQEAYERGTPININLYEHARGTVTGNTRYNDGYVSTTVTLRQAHLIGQNILGSYNEYYIYVVAPAPNLFDVNGVLGRYSPYPSENEFAALGGIPLSQIIGWYRVSFGAIEGGMQRNRDYRGDLFRGLTVAPNEDGYQLAGFPSNFPAWREMPWSTFAPEQCVPNNKEFKGGVCISATNVLSKYDLMNFKKLLKRRLALTFFMSEDDFIGVHGERDEL", "text": "FUNCTION: The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. SIMILARITY: Belongs to the enterotoxin A family."}
{"protein": "MREIVSADDALRKLLEKACKFNESVDVAVHFFSKDSVKIGCVFKYPFYFGRVLVFCGEPQMAQVIDENVTYGGEELIERIKAKKNFVKGYKYSLASPPMMSKLSKIARILGPRGLMPDSKYGLVTHDIAAAVTAILGGKALFKTNKAGVMHSKIGNLGMGFDKLRENFQIFCESVFATRPKNVSLQSYVRSISVSSTMGDGCFVDFLAL", "text": "FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. SIMILARITY: Belongs to the universal ribosomal protein uL1 family."}
{"protein": "MSVHSPNPGLILQSKRFNGLRNILEREGPFCKDGFAASSENLEFLQTKCQVLIIGAGGLGCELLKDLALMGFGNLHVIDMDTIELSNLNRQFLFRRTDIGASKAECAARFINARVPTCRVTPHFKKIQDFDESFYQQFHLVVCGLDSIVARRWINGMLLSMLRYEEDGTIDTSSIVPMIDGGTEGFKGNARVILPGFTACIECTLDLFPPQVNYPLCTIANTPRLPEHCIEYVKIIQWEKQNPFGVPLDGDDPQHIGWIYERALERSNEFNITGVTYRLVQGVVKHIIPAVASTNAAIAAACALEVFKLATSCYDSMANYLNFNDLDGIYTYTYEAEKSENCLACSNTPQPLPIEDPNTTTLEDVIKLLCDSPRFQLKSPALTTVMKDGKRRTLYMSGVKSIEEATRKNLTQSLGELGLHDGQQLTVTDATSPSAMTLQLKYQSNEVEMV", "text": "FUNCTION: Catalytic subunit of the dimeric Uba3-APP-BP1 E1 enzyme. E1 activates Nedd8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a Nedd8-Uba3 thioester and free AMP. E1 finally transfers Nedd8 to the catalytic cysteine of UbcE2M. Required for Cul1 and Cul3 neddylation. Negatively regulates full-length ci stability and hedgehog signaling. SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3 subfamily."}
{"protein": "MLLAQINRDSQAMAEFPGGGGEAQHVTLCLTEAVADGESMDTMEGMSLQAVTLADGSTAYIQHNTKDGKLMEGQVIQLEDGSAAYVQHVPKGDDLSLEDGQAVQLEDGTTAYIHHSSKDSYDQSSVQAVQLEDGTTAYIHHAVQVPQSDTILAIQADGTVAGLHTGEASIDPDTISALEQYAAKVSIEGGEGAGSNALINESESEKKMQIVLSHGSRIPAKPPQTNEKAFRCDYEGCGKLYTTAHHLKVHERSHTGDRPYQCDHGGCRKAFATGYGLKSHVRTHTGEKPYRCSEENCTKSFKTSGDLQKHVRTHTGERPFKCPFEGCGRSFTTSNIRKVHIRTHTGERPYYCSEPGCGRAFASATNYKNHVRIHTGEKPYVCTVPGCDKRFTEYSSLYKHHVVHTHSKPYNCNHCGKTYKQISTLAMHKRTAHNDTEPIEEEQESFFVPQPPDEVIKGSQITYVTGVDGEDGIQTTQSGQQLALIAQDGTSHVAIVAQDLSAFHTSATESGPQHSHNLGGSESRPVTLLATSNGRQIAVQIGEQQSLEEAIRIASRIQQGESPGIED", "text": "FUNCTION: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the activator element (AE) motif of the selenocysteine tRNA gene promoter (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family."}
{"protein": "MAEAAGRSGGRRRRAAEGSKTQDKKVASGQSNTGTKPDHPPILKVDDRQRLARERREEREKQLAARETVWLEREERARQHYEKHLEERKKKLEEQRLKEEGRRAAVEEKRRQRIEEDKERHEAVVRRTIERSQKPKQKQNRWSWGGALHSRINNSDPDRRSVSTMNLSKHVDPVINKRLSSSSATLLNSSDRARRLQLSPWESSIVSRLLTPTHSFLARSKSTAALSGDAASCSPISPLSYKTMSCRNSADRAKLFASTDAVGRRRTHLAGTDKKEKERDHLSSNFSANLKGGHFSSNPKARSPAPSPVWHASKSLPSLAGTLKQITSPPGSSKVPSTQARPPSPGNIRPVKKDTKPENEKKRAEKEAEKANEERTEGSKETSAGTGESANQEELAVQAEDAQAASPSLPPAPPALSPPPAPMKTSAGTTDPEEATRLLSEKRRLAREQREREEQERREREELERQKKEELSQRIAEERARREEEEARRQEAERKRKDAEEEREKEERLRRQAEEREQKEREEMERIQKQKEEEARLREEAERIRLEREKHFQREEQERLERKKRLEEIMKRTRRVEAVDKKPNDQQNGHISKANNTGEAVITSPAPPMEPSGGPQLQHATQSPHSGKPVTCTHTIVSHQPPMNMDSNLNPEKNTEENGMSMQNDNFEEIINLPIGSKPSRLDALNNDGSDSPGIPLNPILAFEDKGTLLPQVDSVQTHQTAEVI", "text": "FUNCTION: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the MAP7 family."}
{"protein": "MPDAYVESLGKMIAILVNYKPGSITLENITRLCQTMGLESFVDQVSANISRLSIASKIIVIDIDYEVTDGKVIDVKLVLASNFDKFDYFNGEANILHRSLTTYSDLHEFHHNLKFLTLLDACSSIDIESNVSQFDLFEYYSMLPQYMQSYLDDNGAQLTVQTNLNDRFGIYLLDHSEKKVAKLTFAATQDPNQRYYEYKYSSETKEWINQSAESYTTGITLVFELLGDPPTYLPKDSLPPEHPDEGFTSASASELQRRFAFKCQNPRVTLVNDFTVDVYPASTFQLLNDNICLCFDILRRQKWWHTVLYPISQLLLHQGQDSAVGDAPAPAAQPPLHRRRSSNKGCRRASAAESATLGDENMHQLTLTEIMNKSVIPEDDAMMDDRIELYVNENYVYLGTQEGCSFYNDPIERWEAFVESLRQMLT", "text": "FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 1 family."}
{"protein": "MGWHDGCIRCMVGVPFASVIATVLCFAGVALFCGCGHEALSGTEKLIETYFSKNYQEYEYLIHVINAFQYVIYGIAIFFFLYGILLLAEGFYTTTAIKHILGEFKPPAMKGGLISTVTGGPPKGRSTRGRQPVHTIELICRCLGKWLGHPDKFVGVTYVITILWILIFACSAVPVYIYFNTWVTCQSIAFPGKTTTSVSTLCLDARMYGVLPWNAFPGKVCGTSLLAICKTSEFQMTFHLFIAAFVGAAATLVALLTYMVGASFNYAVLRVTGRSDRSKF", "text": "FUNCTION: This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the myelin proteolipid protein family."}
{"protein": "MGNITADNTSMNCDIDHTIHQTLAPVVYVMVLVVGFPANCLSLYYGYLQIKARNELGVYLCNLTVADLFYICSLPFWLQYVLQHDHWSHDDLSCQVCGILLYENIYISVGFLCCISIDRYLAVAHPFRFHQFRTLKAAMGVSALIWVKELLTSIYFLMHEEVVEDADRHRVCFEHYPLEPRQRGINYYRFLVGFLFPICLLLASYRGILRAVRRSHGTQKSRKDQIQRLVLSTVVIFLACFLPYHVLLLVRSLWESSCDFAKGIFNAYHFSLLLTSFNCVADPVLYCFVSETTHRDLARLRGACLAFLTCARTGRAREAYPLGAPEASGKSEDPEVLTRLHPAFQTPHPPGMGGSPAGGLS", "text": "FUNCTION: Proton-sensing receptor involved in pH homeostasis. May represents an osteoblastic pH sensor regulating cell-mediated responses to acidosis in bone. Mediates its action by association with G proteins that stimulates inositol phosphate (IP) production or Ca(2+) mobilization. The receptor is almost silent at pH 7.8 but fully activated at pH 6.8 (By similarity). Also functions as a metastasis suppressor gene in prostate cancer (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MLATRNLVPIIRASIKWRIKLSALHYCMSDAETSEALLEDNSAYINNEKHNLFLEKIFSDYQPFKHDNRTQVSCSQHMRDYRPLLTLSSATRSVLFSLLASDMSIILSISPNTGILLCIGHLLASDIEDVVIVLSRGSPLVDLASTRIFKLAQNGTLRFAIKRTTFQELRFLRKSKDENVMEAATRGIITIRQLYYENKVLPLRFTGNVATHIEENLEFEEQITWRTHVDSSIFPNTRCAYPSGYGPSAKIPCLSHKPNDILAYTGSTLVGRVVSKLAPEQVMKKVTLESGGKSTMAVFIQHDVTWAVENTQFGVFDRQGQCCIAQSGYTVHRSTLSQIVENNLEKDPSYVLHVDTESDIRGPFILKIHFESIPRRINSAKAENSKVLCGGPRENSVYLYPTLSATLTDECRIMKEEVFAPIITILCVKTVDEAIQRGNNSKFGLAAYVTKENVHGIILSTALKTVKLFIICVHLASYQIPFGGNKNSGMGAELGKRALENYTEGNHVLPVSLVKETLAPNTETASPARWPIH", "text": "SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aldehyde dehydrogenase family."}
{"protein": "MELTNLIEKCTKLSKDFATEVEKLWNDELSSESGLSRKTRNVIRNILRDITKSLTTDKKSKCFCILERSTINGEQIKDVYKTIFNNGVDVESRINTTGKYVLFTVMTYAAAELRLIKSDEIFALLSRFFNMICDIHRKYGCGNMFVGIPAALIVLLEIDHINKLFSVFSTRYDAKAYLYTEYFLFLNINHYLLSGSDLFINVAYCAVSFSSPIRVPDYIMEALTFKACDHIMKSGDLKYTYAFTKKVKDLFNTKSDSIYQYVRLHEMSYDGVSEDTDDDDEVFAILNLSIDSSVDRYRNRVLLLTPEVASLRKEYSEAEPDYKYLMDEEVSAYDKHLPKPITNTGIEEPHATGGDKEDQPIKVVYPPNNDKDDAIKPHNPLEDPNYVPTITRTDIGIADYQLVINKLIEWLDKCEEECGNGGEFKTELEEAKRKLTELNAELSDKLSKIMSLERDSVHKTERIDRLTKEIKELRDIQNGTDDGSDSSEIDKKIIRELRESLDREREMRSKLEKELDTIRDGKVEGSCQRELELRRMWLKQRDDDLRAEIDKRRNVEWELSRLRRDIKECDKYKEDLDKAKATISNYVSRISTLESEIAKYQQDRDTLSVVRRELEEERRRVKDLESRLDECTRNQEDTQEVDALRSRIRELENKLTDCIESGGGNLTEISRLQSRISDLERQLNECRGNVTEISRLESRISDLERQLNDCRRNNETNAETERDATS", "text": "FUNCTION: Structural protein that forms a matrix surrounding the mature virion (MV) through interaction with protein A26. Presence of protein A25 in the virion structurally prevents direct virus-cell fusion mechanism (By similarity). SUBCELLULAR LOCATION: Virion. Note=Present above the membrane of mature virions (MV). SIMILARITY: Belongs to the poxviridae A25 protein family."}
{"protein": "MIRGKIDILVVDDDVSHCTILQALLRGWGYNVALAYSGHDALAQVREKVFDLVLCDVRMAEMDGIATLKEIKALNPAIPILIMTAFSSVETAVEALKAGALDYLIKPLDFDRLQETLEKALAHTRETGAELPSASAAQFGMIGSSPAMQHLLNEIAMVAPSDATVLIHGDSGTGKELVARALHACSARSDKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISPLMQVRLLRAIQEREVQRVGSNQTISVDVWLIAATHRDLAEEVSAGRFRQDLYYRLNVVAIEMPSLRQRREDIPLLADHFLRRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAIERAVVLLTGEYISERELPLAIAATPIKAENSAEIQPLVDVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR", "text": "FUNCTION: Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MSDKIQSRESKTTKPTKTEKISDKSGNLSQVKSSKNLSKSQSIYLEIDSLSKKFLEEGRQYIYKWIRDEYGLSKNEATALDISIYNTTIARMINIYKFDETLAAFLPFKFGKEIISPRQDFYGFATTCGTILYYQSFGDTLGYYNGNWEFNYGNDNRPDYVNDLISEFIHLGGINDISMVNWLASDDTILYLITARVVLEYFFQGDNAEISYFGTRLRQEYLKAKPLIQNRHPGQTTMDSLDIMSNIEWDKLPYNSRAIGAGAAMRSGSIGIFYPGRQNRKKLVALAVECSRITHNSATAILGSVTSALFTAFSLEKISVNLWPHYLLEILRSNIIDEYIEQSRPNEYSLFSRDKVIFQGQWEKYVSSRFSGVNPRDLRYMHNPVERYRYLTENFSKGCDMPGGCGDDCVIMAYDSLLQSNGVLEKVVVYSILHPGDSDTVGSVALSWFGAYYSTKKNLDILSPRFDELEYSNEINNLIWNTEDFVLGLTKVFYKFIYIDIATDLVEQSMKLK", "text": "SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family."}
{"protein": "MTLKQRYQQAGKEASWALSLSILYVIGWCLCAYLPKETQGPIGFPLWFELSCIYLPILFIVIGHWIIKIIFQDISLEINDQGNQK", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To E.coli YhdT."}
{"protein": "MATPVEPPNGIRTPGKHYYSMWQSLFEIDTKYVPIKPIGRGAYGIVCSSVNRETNEKVAIKKINNAFENRIDALRTLRELKLLRHLRHENVIALKDVMMPIQRRSFKDVYLVYELMDTDLHQIIKSSQTLSNDHCQYFLFQLLRGLKYLHSANILHRDLKPGNLLINANCDLKICDFGLARTSSGKDQFMTEYVVTRWYRAPELLLCCDNYGTSIDVWSVGCIFADVLGRKPVFPGTECLNQLKLIINILGSQREEDIEFIDNPKARKYIKSLPYSPGTPFSRLYPNAHPLAIDLLQRMLVFDPSKRISVMEALQHPYMSPLYDPNTDPPAQVPINLDIDEDLVEETIREMMWEEILHYHPEAAVALLWKLFYELLLVPSRHRP", "text": "SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily."}
{"protein": "MATVEVATELGTVVTAVGPKAKDEEEEEEEEESLPPCETVRWAPVGAVAEAGPGAATFSEAAAAEEPGAAPGSPSDATVRTLRRLEAERRQLDSALLALSSHFAQVQFRLRQVVRGAPAEQQRLLRELEDFAFRGCPHVLGYEGLADPCGGDESDVLPGDRPRVRGEDQSEQEKRERLETQREKQKELILQLKTQLDDLETFAYQEGSYDSLPQSVVLERQRVIIDELIKKLDMNLNEDISSLSTEELRQRVDAAVAQIVNPVRVKEQLVEQLKTQIRDLEMFISFIQDEVGSPLQTGGHCECQASGKVGIGSTRVGGSTLPPGPGKAKAEDAKRARETGLHLMRRALAVLQIFTVSQLGCATGQIPQTLWQRSQADRDYSHLLKRLEVSVDRVKQLALRHQPHDHVITSANLQDLSLGGKDELTTVVRKELTVAVRDLLAHGLYASSSGMSLVMAPLACLLPVFSSAPETMHPWELFVKYYHAKNGRAYVESPARKLSQSFALPIMGDTAVTPKQSLLTAIHLVLTEHDPFKRSADSELKALVCMALNEQRLVSWVNLICKSGSLIEPHYQPWSYMAHTGFESALNLLSRLSSLKFSLPVDLAVRQLKNIKDAF", "text": "FUNCTION: May play a role as p53/TP53 inhibitor and thus may have oncogenic activity."}
{"protein": "MKFKSLPMFALLMLGGCSLIPDYQQPAAPMQAQWPTGQAYGGQGDQRSIATALPKAKEFFKDPALVRLLDAALENNRDLRIAAKNVESYRALYRIQRAERFPTLDGQASGNRTRLPDDLSPTGDSRIDSQYQVGLVTAYELDLFGRIRSLSNQALEKYLATEEAQRSVQIALIGDVATTYFLWRTDQALLELTEATLTSYVESLAMIESSAWAGTSSELDVRQARTLVNQAQAQQALYTRRIAQDVNALELLLGSKIPTDLPKNSPLAMSALGKVPAGLPADLLLNRPDIRSAEHQLMAANANIGAARAAFFPRISLTASAGSASSDLDGLFNSGSDSWSFAPQISVPIFNAGKLRANLDYAELQKDVGVATYEKSIQTAFREVADGLAARGTYGKQLSAQSELVDNYKAYFSLAQQRYDQGVDSYLTVLDAQRELFSSQQKLLNDQLDQINSEVQLYKALGGGWSVSQN", "text": "FUNCTION: The outer membrane component of an organic solvent efflux pump. Involved in export of a number of low log POW compounds including hexane (log POW 3.5), toluene (log POW 2.5) and dimethylphthalate (log POW 2.3). The solvent resistance phenotype has been postulated to depend on the operon expression level. FUNCTION: The outer membrane component of an organic solvent efflux pump. Involved in export of a number of organic solvents, including toluene and styrene. This is the most important solvent efflux pump in this strain, although it can export AMP and some antibiotics. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family."}
{"protein": "MTMTTMPESLNSPVSGKAVFMEFGPPNQQMSPSPMSHGHYSMHCLHSAGHSQPDGAYSSASSFSRPLGYPYVNSVSSHASSPYISSVQSYPGSASLAQSRLEDPGADSEKSTVVEGGEVRFNGKGKKIRKPRTIYSSLQLQALNRRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKRSKFKKLMKQGGAALEGSALANGRALSAGSPPVPPGWNPNSSSGKGSGGNAGSYIPSYTSWYPSAHQEAMQQPQLM", "text": "FUNCTION: Plays a role as a transcriptional activator or repressor (PubMed:14671321). Inhibits several cytokine signaling pathways, such as TGFB1, activin-A/INHBA and BMP4 by interfering with the transcriptional stimulatory activity of transcription factors, such as MSX2, FAST2, SMAD2 and SMAD3 during hematopoietic cell differentiation (PubMed:14671321). Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina (By similarity). Likely to play a regulatory role in the development of the ventral forebrain (By similarity). May play a role in craniofacial patterning and morphogenesis and may be involved in the early development of diencephalic subdivisions (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the distal-less homeobox family."}
{"protein": "MSNNEFHQRRLSATPRGVGVMCNFFAQSAENATLKDVEGNEYIDFAAGIAVLNTGHRHPDLVAAVEQQLQQFTHTAYQIVPYESYVTLAEKINALAPVSGQAKTAFFTTGAEAVENAVKIARAHTGRPGVIAFSGGFHGRTYMTMALTGKVAPYKIGFGPFPGSVYHVPYPSDLHGISTQDSLDAIERLFKSDIEAKQVAAIIFEPVQGEGGFNVAPKELVAAIRRLCDEHGIVMIADEVQSGFARTGKLFAMDHYADKPDLMTMAKSLAGGMPLSGVVGNANIMDAPAPGGLGGTYAGNPLAVAAAHAVLNIIDKESLCERANQLGQRLKNTLIDAKESVPAIAAVRGLGSMIAVEFNDPQTGEPSAAIAQKIQQRALAQGLLLLTCGAYGNVIRFLYPLTIPDAQFDAAMKILQDALSD", "text": "FUNCTION: Catalyzes the transfer of the amino group from gamma- aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). PuuE is important for utilization of putrescine as the sole nitrogen or carbon source. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MAQKLVAQGGETGDVWDDGVYDNVTKVYVGQGQYGIAFVKFEYANGSEVVVGDEHGEKTELGVEEFEIDSDDYIVYVEGYREKVSDMTSEMITFLSFKTSKGKTSQPIVKKPGVKFVLHGGKIVGFHGRSTDVLHSLGAYVSLPSTPKLLGNWIKVEQNGEGPGLRCSHGIAQVGNKIYSFGGELIPNQPIDKHLYVFDLETRTWSIAPATGDVPHLSCLGVRMVSVGSTLYTFGGRDFSRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVGAMDRIKTLDSYNIVDKTWFHCSNPGDSFSIRGGAGLEVVQGKVWIVYGFNGCEVDDVHFYDPAEDKWTQVETFGVKPNERSVFASAAIGKHIVIFGGEIAMDPRAHVGPGQLIDGTFALDTETLQWERLDKFEGTPSSRGWTASTTGTIDGKKGLVMHGGKAPTNDRFDDLFFYGIDSV", "text": "FUNCTION: Promotes simple nitriles, but not epithionitrile or thiocyanate formation (PubMed:18987211, PubMed:19224919). Converts allylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase (PubMed:18987211, PubMed:19224919). Triggers the production 3-butenylnitrile (PubMed:19224919). SIMILARITY: Belongs to the jacalin lectin family."}
{"protein": "MEKIKLLNVKTPNHYTIIFKVVAYYSALQPNQNELRKKELFIKNDGKALSFPYDWKLATHVICDDFSSPNVQEGSKRSLRLAKTNWIRDCVDKNTLLNYSFYSCNPYLLFKGICASSCQIDSYQSSLIDDALETFGGRFSKGLMKSMTHLFTYSGMGAKCKKVLDKPSLSIKLIHPQWLLDCLQFGQLIDQDPYLFPNPSYKKNDSSISKAEPTSLFRNVLHGKRIYFSNDLNLPTNFRHSLQKFSVGIGAKIAESINDCDIFIGLKRDTIEFNLASNKNTTIGTISWLLNLFVLGSWKSPLLNALHYPFPSVGFLKDQMVAVTNYTDAARIYLEKLLLACGATYTKDLKPTNTLLIAASSYGQKYGAAKVWNIPTVHHSWLYSSFKNLSSQAFTDFPVPLDDSYMDFIFPCPLNVEKGSFEDTLKSSLTKGNSEVLLDDLSDPSVSSIKGNKTNEELEKEFKSTSDNFGKHIILTSSFSNQSADKGSSLAAEDDRNDEGSTITGVNRELQDEGRLEIDAKSSKTNTPPSPLLVGTPSKESLKEASSDDELPVLATKLVDNVIKEKSPLSLTPKVVVPSHKETYTDEKKLIDELDRVNPLNSSQLLRSKRKSAATALSMLQNVIMPDVLAFEREKKRRQTHRSVSSGEVSRESSESRNTNAKASKRVYITFTGYDKKPSIDNLKKLDMSITSNPSKCTHLIAPRILRTSKFLCSIPYGPCVVTMDWINSCLKTHEIVDEEPYLLNDPEKELELGCTLESALKRARAQGPSLLEDYVVYLTSKTVAPENVPAVISIVKSNGGVCSTLNVYNKRLARHLEDGNVVLITCNEDSHIWTNFLDNASQNKTIFLQNYDWLIKTVLRQEIDVNDRIADEFARAV", "text": "FUNCTION: Required for mitotic fidelity, specifically in the G2 phase of the cell cycle. Plays a role in chromatin organization."}
{"protein": "MFQISNLLLAADFSSEVANNSAVGMIGSFIAAALLIVIPATAFLIFVSQKDSLNRTSTGRR", "text": "FUNCTION: Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbX family. Type 2 subfamily."}
{"protein": "MAPREAAPAERGSVMEGIRAILLGPPGAGKGTQAPKLAEKYCVCHLATGDMLRAMVASGSELGMRLKATMDAGKLVSDEMVVELIEKNLDTPPCKKGFLLDGFPRTVKQAEMLDELLEKRQEKLDSVIEFKVDDSLLVRRICGRLIHASSGRSYHEEFNPPKEAMKDDVTGEPLMRRSDDNETTLKSRLEAYHTMTSPLVEYYQRHGIHTAVDAAQSPDVVFASILAAFSKARCKDLVLFV", "text": "FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily."}
{"protein": "MESYLEENFGGVKAKNSSEEALRRWRKLCGVVKNPKRRFRFTANLDKRGEAQAIKHANHEKLRVAVLVSKAALQFIQGLSLRSEYVVPEEVKAAGFQICADELGSIVEGHDSKKLITHGGVTGIADKLATSPADGLSTAEESIKRRQDVYGLNKFTESEVRSFWVFVWEALQDTTLIILAVCAFVSLVVGIAMEGWPKGAHDGLGIVASILLVVFVTATSDYRQSLQFKDLDKEKKKIQVQVTRNGFRQRLSIYDLLPGDVVHLAIGDQVPADGLFISGFSLLINESSLTGESEPVVVNEDNPFLLSGTKVQDGSCKMLITTVGMRTQWGKLMATLSEGGDDETPLQVKLNGVATIIGKIGLFFAVITFIVLSQGLISKKYHEGLLLSWSGDDALEMLEHFAIAVTIVVVAVPEGLPLAVTLSLAFAMKKMMNDKALVRHLAACETMGSATTICSDKTGTLTTNHMTVVKACICGNIKEVNNPKNASDLCSELPETVVKTLLESIFNNTGGEVVIDQDGKYQILGTPTETALLEFALSLGGNFKAKRDETKIVKMEPFNSTKKRMCVVLKLPGGGCRAHCKGASEIVLAACDKFMDETGAVVPLDKTTADKLNGIIESFANEALRTLCLGYREMEEGFSVEEQIPLQGYTCIGIVGIKDPVRPGVRESVATCRSAGIMVRMVTGDNINTAKAIARECGILTEDGLAIEGPEFREKSLDELLKLIPKIQVMARSSPLDKHTLVKHLRTTFNEVVAVTGDGTNDAPALHEADIGLAMGIAGTEVAKESADVIILDDNFSTIVTVAKWGRSVYVNIQKFVQFQLTVNVVALLVNFSSACFTGNAPLTAVQLLWVNMIMDTLGALALATEPPNDDLMKREPVGRTGKFITNVMWRNILGQSFYQFIVMWYLQTQGKSMFGLDGPDAEVVLNTIIFNSFVFCQVFNEISSREMEKINVLRGILKNYVFLGVLTSTVVFQFIMVQFLGEFANTIPLTRLQWIASVLLGLIGMPISAIIKLLPVGSS", "text": "FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell, into the endoplasmic reticulum, or into organelles. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily."}
{"protein": "MAGIGPITQDWEPVVIRKKPANAAAKRDEKTVNAARRSGADIETVRKFNAGTNKAASSGTSLNTKMLDDDTENLTHERVPTELKKAIMQARTDKKLTQSQLAQIINEKPQVIQEYESGKAIPNQQILSKLERALGAKLRGKK", "text": "FUNCTION: Transcriptional coactivator that stimulates transcriptional activity by bridging regulatory proteins and TBP, thereby recruiting TBP to promoters occupied by DNA-binding regulators. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the MBF1 family."}
{"protein": "MLQIGEDVDYLLIPREVRLAGGVWRVISKPATKEAVFRERLIQFLQEEGRTLEDVARIIEKSTPHPPQPPKKAKVPRVRRVPQMVTPPLRLVVGTYDSSNGSDSELSDFDTSKVKGNRGSGKTRKVRKMPVSYLGSKFLGSDESEDDQELVEAFLRRGEKKPSAPPPRRRVNLPVPMFENNLGPQPSKGDRWREYVSQVSWGKLKQRVRGWAPRSGSEVGQAQQSSIAERAGEMRHSHTSPDLDDSSRNTGDLSDQTLITRRWKPKIKWVSLRRCRKEQVPPLAHGTAEEPPEAAENQGAGAAAEHGVEAAASQRPEAAASPRAEAAANPRAEATANPRAEAAANPRAEAAASPRAEAAANPRAEAAANPRAEATANPRAEAAANPRAEATANPRAEAAVNPRTEAAVNPRTEAAANPRAEAAVNPRAEATASPRAEAEVNQKTEATASPRAETAASPRVEAAASLRVEAAASPRAEATVSPRAEAVATPRAETAASARVEAAANLRAGVLPDQRAEAIDSQRAEGPVNQSTGATENQRVEVLADQRAGVLHDQREEAGPQAILEASADSGSRARKQVKTVRFQTPGRFSWFHMRRKAFWHTPRLPTLPKRGPRAGAGEARSLRVLRADTRADMEHREQEEQL", "text": "FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Required for localization of CUL7 to the centrosome. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome."}
{"protein": "MNKTFFLVVIMATVLVLAFDATDAQTNVRCTNTRDCFSFCSQFTNVHPACLGDYCECLRWEGGISI", "text": "FUNCTION: inhibits Kv1.3/KCNA3 channel. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 30 subfamily."}
{"protein": "MNPNKERLIEIFRSNVKGRIPDISGRNIRHDGRWGHWLEERFGISANADNHADILGYELKNEATSGKTTFGDWSANEYIFKTPPYNSLFSGSTASEKQNAFCRMFGKPNEAKNGRFSWSGSPIPKIWQYNSFGQIMVIEENLDIVIYYSFSQDLRYNKFEIIPPQLQHDEIQIARWYGVANPLLSRRGKTLKDKLEDKFNDLGWFTCTTDSIGAYDKICFGRPITFENWINLVDSGIVYFDSGMYEGNKRPYSQWRADNSYWNSLITDCHQ", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-CCNGG-3' and cleaves after C-2."}
{"protein": "MTDNTTAPLYSLRGLQLIGWRDMQHALNYLFADGQMKQGTLVAINAEKMLTAEDDPEVRALIDAAEFKYADGISVVRSVRKKFPQAQVSRVAGADLWEELMARAGKEGTPVFLVGGKPEVLAQTEAKLRAQWNVNIVGSQDGYFKPEQRQALFERIHASGAKIVTVAMGSPKQEILMRDCRVIHPQALYMGVGGTYDVFTGHVKRAPKMWQTLGLEWLYRLLSQPSRITRQLRLLRYLRWHYTGNL", "text": "FUNCTION: Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis. SIMILARITY: Belongs to the glycosyltransferase 26 family."}
{"protein": "MKAIVVLLILALILCLYAMTTVEGACQFWSCNSSCISRGYRQGYCWGIQYKYCQCQ", "text": "FUNCTION: Antibacterial protein involved in the immune response to septic injury. When combined with 14.026 kDa and 14.059 kDa hemolymph antimicrobial peptides, it has a strong cooperative activity against the Gram-positive bacteria B.subtilis and S.aureus, and against the Gram-negative bacteria E.coli DH5-alpha and K.pneumoniae ATCC 138833. Does not show detectable antibacterial activity when present alone. Has no hemolytic activity in human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the invertebrate defensin family."}
{"protein": "MKNKSVIEEADDVRRAVEMVQLGARMQMLEVETRLSREKLLRIYKEVRGASPPKGMLPFSTDWFMTWQPNVHSSLFMNLYRYFTGPAGVHGLDAILKSYHLYLDHIETGVIEPALSLTRAWTLVRFFDADLLQMAACTRCGGEFVAHAHDPVHDYVCGLCNMPSRAGSARRKTTTRKAVAPTHKTTAASRKAVVA", "text": "FUNCTION: Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FlhC family."}
{"protein": "MRIDVISLFPEFIAQCAAFGVVGRAQERGLLELKGWNPRDHAQGNYRRVDDRPFGGGPGMVMLIEPLRACLEVAQAADARPAPVIYLSPQGRPLTQPLARELAQLPRMVLLCGRYEGVDERFLDQAVDMEISIGDYVLSGGELGAAVLVDVVTRLQDGVLNDAESAAQDSFEGPQGLLDCPHYSHPSSHAWGDVPEVLRSGNHGAIARWRRQQSLGRTWLRRPELLDEATLDKQDRRLLEEFRRELAPGDEK", "text": "FUNCTION: Specifically methylates guanosine-37 in various tRNAs. FUNCTION: Specifically methylates guanosine-37 in various tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase TrmD family. SIMILARITY: Belongs to the RNA methyltransferase TrmD family."}
{"protein": "MAFSHDNRVRFKDEGKPLSSEYGYGRKARPSLDRVFKNVKWGFKKPLSFPSHKDPDHKETSSVTRKNIINPQDSFLQNWNKIFLFACVVALAIDPLFFYIPIVDSARHCLTLDSKLEIAASLLRTLIDAFYIIHIVFQFRTAYIAPSSRVFGRGELVDDAKAIALKYLSSYFIIDLLSILPLPQIVVLAVIPSVNQPVSLLTKDYLKFSIIAQYVPRILRMYPLYTEVTRTSGIVTETAWAGAAWNLSLYMLASHVFGALWYLISVEREDRCWQEACEKTKGCNMKFLYCENDRNVSNNFLTTSCPFLDPGDITNSTIFNFGIFTDALKSGVVESHDFWKKFFYCFWWGLRNLSALGQNLQTSKFVGEIIFAISICISGLVLFALLIGNMQKYLESTTVREEEMRVRKRDAEQWMSHRMLPEDLRKRIRRYEQYRWQETRGVEEETLLRNLPKDLRRDIKRHLCLDLLKKVPLFEIMDEQLLDAVCDRLRPVLYTENSYVIREGDPVGEMLFVMRGRLVSATTNGGRSGFFNAVNLKASDFCGEDLLPWALDPQSSSHFPISTRTVQALTEVEAFALTAEDLKSVASQFRRLHSKQLQHTFRFYSVQWRTWSVSFIQAAWRRYCRRKLAKSLRDEEDRLREALASQDKEHNAATVSSSLSLGGALYASRFASNALHNLRHNISNLPPRYTLPLLPQKPTEPDFTANHTTDP", "text": "FUNCTION: Probable cyclic nucleotide-gated ion channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family."}
{"protein": "MLYHVEMFTIILLFGFSLADYCGSDQVPYGMEVHHSGVVRLMCSKPNCYDKNYSDCPERAESRHGCQKSNQWVGGFEKNIEGDLYTMCCEFEGLEKYAKVRYSDVRIRRGEFFEGEEKENDDGDVVKFDVIKDIRMHKDDEGQAYYNLTVLSFNCESIPDVKPAWYQKSQWPYFQFAKN", "text": "FUNCTION: Intercellular signal essential for a variety of patterning events during development. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MYWRRAALVGTRLIPVRSSSAGRLEGPAGISGSGMGNSTSSSLGNAATAPVNQIQETISNNCVVIFSKTSCSYCTMAKNLFHDMNVNYKVVELDMLEYGSQFQDALHKMTGERTVPRIFVNGTFIGGATDTHRLHKEGKLLPLVHQCHLKNSKREEL", "text": "FUNCTION: Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the glutaredoxin family."}
{"protein": "MALLEIIHYPSKILRTISKEVVSFDSKLHQQLDDMHETMIASEGIGLAAIQVGLPLRMLIINLPQEDGVQHKEDCLEIINPKFIETGGSMMYREGCLSVPGFYEEVERFEKVKIEYQNRFAEVKVLEASELLAVAIQHEIDHLNGVLFVDKLSILKRKKFEKELKELQKKQKHE", "text": "FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). SIMILARITY: Belongs to the polypeptide deformylase family."}
{"protein": "MLIDFRQVCGAGAAALALASPALADTTNLRVCASTKDAPFSDAQGAGFENKIAQVLADEMGATLDLVMLEKDAIYLVRDGIEKDLCDVLVGVDAGDERLLTTRPYYRSGYAFVTRQDRNFEGDKWQDVDQEGFDTFSYRLHSPAETILKYTGRYEYNLIYQASLTNFEDRRNKYTQVEASRVITEVADGGADLAIVFAPEAARYVRDSREPLRMTLITNEIERSDGVIIPLQYSQSVGVSKTHPELLGPIEQALQSGKARIDAILTEEGIPLLPSS", "text": "FUNCTION: May be involved in the assemblage of active methanol dehydrogenase and/or its cofactor PQQ in the periplasm. SUBCELLULAR LOCATION: Periplasm."}
{"protein": "MVSVEGRAMSFQSIIHLSLDSPVHAVCVLGTEICLDLSGCAPQKCQCFTIHGSGRVLIDVANTVISEKEDATIWWPLSDPTYATVKMTSPSPSVDADKVSVTYYGPNEDAPVGTAVLYLTGIEVSLEVDIYRNGQVEMSSDKQAKKKWIWGPSGWGAILLVNCNPADVGQQLEDKKTKKVIFSEEITNLSQMTLNVQGPSCILKKYRLVLHTSKEESKKARVYWPQKDNSSTFELVLGPDQHAYTLALLGNHLKETFYVEAIAFPSAEFSGLISYSVSLVEESQDPSIPETVLYKDTVVFRVAPCVFIPCTQVPLEVYLCRELQLQGFVDTVTKLSEKSNSQVASVYEDPNRLGRWLQDEMAFCYTQAPHKTTSLILDTPQAADLDEFPMKYSLSPGIGYMIQDTEDHKVASMDSIGNLMVSPPVKVQGKEYPLGRVLIGSSFYPSAEGRAMSKTLRDFLYAQQVQAPVELYSDWLMTGHVDEFMCFIPTDDKNEGKKGFLLLLASPSACYKLFREKQKEGYGDALLFDELRADQLLSNGREAKTIDQLLADESLKKQNEYVEKCIHLNRDILKTELGLVEQDIIEIPQLFCLEKLTNIPSDQQPKRSFARPYFPDLLRMIVMGKNLGIPKPFGPQIKGTCCLEEKICCLLEPLGFKCTFINDFDCYLTEVGDICACANIRRVPFAFKWWKMVP", "text": "FUNCTION: Catalyzes the deimination of arginine residues of proteins (By similarity). In oocytes, is released during cortical reaction and plays a role in preimplantation cleavage and early embryonic development (By similarity). May be involved in cytoskeletal reorganization in the egg and early embryo (PubMed:27545678). FUNCTION: Catalyzes the deimination of arginine residues of proteins (By similarity). May be involved in cytoskeletal reorganization in the egg and early embryo (PubMed:27545678). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasmic vesicle, secretory vesicle, Cortical granule Note=Predominantly cytoplasmic (oocyte cytoplasmic sheets), also nuclear. Released extracellularly during the cortical reaction, and remains associated with the blastomeres surfaces as a peripheral membrane protein until the blastocyst stage of development. SIMILARITY: Belongs to the protein arginine deiminase family."}
{"protein": "MATEEHQRLASIVKSCHESLRQLTKEYGATAAWQEHTSPRNAKQLAEYAKAMKQLAAIWETNDGKVELQARSRIKWAIDYITKYFFTEGIYLQKRQREQRLLESYRAEGKLGEVQCRLMEEPPDRLHVLDVGSCFNPFSSAPHLEVTALDLCPATEDVLQADFLKVEVVPGIREPELEEGSVRRLPASHYECVIFSLLLEYMPSAEQRLQCCLQAYDLLLPEGILVLITPDSQHVGKNAHLMKNWRYSLARIGLLRVRFEKLPHISCMVFRKAISRELSQHWASIHREEGMCEEIRIPQDDS", "text": "FUNCTION: S-adenosyl-L-methionine-binding protein that acts as an inhibitor of mTORC1 signaling (PubMed:29123071). Acts as a sensor of S- adenosyl-L-methionine to signal methionine sufficiency to mTORC1 (PubMed:29123071). Probably also acts as a S-adenosyl-L-methionine- dependent methyltransferase. SIMILARITY: Belongs to the BMT2 family."}
{"protein": "MTGGLRDGEKEEEFLHSPFIRKQGNIYKPYNKDMDYDILNEKSMEDVHTKEIDLVNRDPTHLNDDVVKVDFEDVIAEPAGTYSFDGVWKASFTTFTVTKYWCYRLLTALVGIPLALIWGIFFAILSFIHIWAVVPCVKSYLIEIHCISRVYSICVHTFCDPLFEAMGKCLGGVRIRTSKEV", "text": "FUNCTION: May act as a positive regulator of T-cell coactivation. May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein Membrane, caveola; Peripheral membrane protein Membrane raft Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). SIMILARITY: Belongs to the caveolin family."}
{"protein": "MEKYENLGLVGEGSYGMVMKCRNKDSGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLKLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDIWAIGCLVIEMLMGQPLFPGESDIDQLHHIMTCLGNLIPRHQELFYKNPVFAGVRLPEIKDIEAEPLESRYPKLPEVVISLAKKCLHIDPDKRPLCADLLHHDFFQMDGFAERFSQELQLKIEKDARNNSLPKKFQIRKKEKDDALGEERKTLVVQDTNADPKTKDSKVLKVKGSKIDVEKTEKGTRASNGSCLHDNGTSHKGLSSTSLRDCSNVTIDHPRNPGTAIPPLTHNLSAVAPGINAAMGTIPGVQNYRVDEKTKKYCNPFVKPSQPSPSGIYNMNVSASVSNCPLPRKSKHSPPLDLAVSMGARRVKLYLETESET", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily."}
{"protein": "MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV", "text": "FUNCTION: Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha- chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins (PubMed:7360115, PubMed:17320177). Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces (PubMed:2141838, PubMed:9605165, PubMed:12055245). The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization (PubMed:28671664). SUBCELLULAR LOCATION: Secreted, extracellular space. Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MAKSSRENGPREPAAGGSLSGTRESLAQGPDAATADELSSLGSDSEANGFAERRIDKFGFIVGSQGAEGALEEVPLEVLRQRESKWLDMLNNWDKWMAKKHKKIRLRCQKGIPPSLRGRAWQYLSGGKVKLQQNPGKFDELDMSPGDPKWLDVIERDLHRQFPFHEMFVSRGGHGQQDLFRVLKAYTLYRPEEGYCQAQAPIAAVLLMHMPAEQAFWCLVQVCEKYLPGYYSEKLEAIQLDGEILFSLLQKVSPVAHKHLSRQKIDPLLYMTEWFMCAFARTLPWSSVLRVWDMFFCEGVKIIFRVGLVLLKHALGSPEKLKACQGQYETIEQLRSLSPKIMQEAFLVQEVIELPVTERQIEREHLIQLRRWQETRGELECRSLPRMHGAKAILDAEPGPRPALQPSPSIRLPPDAALLSSKAKPHKQAQKEQKRTKTSAQLDKSPGLSQATVVTAAGDACPPQGVSPKDPVPQDPTPQNLACHHSQESLTSQESEDTYL", "text": "FUNCTION: Acts as GTPase-activating protein for RAB27A. SUBCELLULAR LOCATION: Cell projection, microvillus Note=Localizes to the microvilli-rich region of the syncytiotrophoblast."}
{"protein": "MIKRVKTGIPGMDEILHGGIPERNVVLLSGGPGTGKSIFSQQFLWNGLQMGEPGIYVALEEHPVQVRQNMAQFGWDVRKYEEEGLFAMVDAFTAGIGKSKEYEKYIVHDLTDIREFIDVLRTAVKDIGAKRLVVDSVTTLYINKPAMARSIVMQLKRVLAGLGVTSIFVSQISVGERGFGGPGVEHGVDGIIRLDLDEIDGELKRSLIVWKMRGTSHSMRRHPFDITDKGIIVYPDKVLKRKAVIELE", "text": "SIMILARITY: Belongs to the UPF0273 family."}
{"protein": "MMYKLGVLLIICLLLFPLTAVPQDGDQPADRPAERMQDDISFEHDRFFDPVKRCCKYGWTCWLGCSPCCG", "text": "FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
{"protein": "NYCVAKRCRPGGRQCCSGKPCACVGKVCKCPRDNS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family. 07 subfamily."}
{"protein": "MPITRMRMRPWLEMQINSNQIPGLSWINKEEMIFQIPWKHAALHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDTKSKTKRKLCGDSSPDTLSDGLSSSTLPDDHSSYTAQGYLGQDLDMDRDITPALSPCVVSSSLSEWHMQMDIMPDSTTDLYNLQVSPMPSTSEAATDEDEEGKLPEDIMKLFEQSEWQPTHVDGKGYLLNEPGAQLSTVYGDFSCKEEPEIDSPGGDIEIGIQRVFTEMKNMDPVMWMDTLLGNSTRPPSIQAIPCAP", "text": "FUNCTION: Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses (By similarity). Regulates transcription of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage (By similarity). Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters (By similarity). Binds to a consensus sequence in gene promoters (By similarity). Its target genes for transcriptional activation activity include: genes involved in anti- viral response, such as IFN-alpha/beta, RIGI, TNFSF10/TRAIL, ZBP1, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as GBP2, GBP5 and NOS2/INOS; anti-proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA; metabolic enzymes, such as ACOD1/IRG1 (By similarity). Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4 (By similarity). Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53 (By similarity). Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells (By similarity). Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development (By similarity). Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1. SIMILARITY: Belongs to the IRF family."}
{"protein": "MVTTVEMLTTWNPVTVSLVSPVIIYWVASAFFGFLHYIELPVFEKYRIHPPEEIARRNRVPQMAVVKAVLFQQLCEVVVGIALAMFEGYPEPIDEAKQMLRYEAFFSKNLPALLQVAPFAPKLAYNFIVPAFQYFFAFFIIDSWQYFWHRYLHYNKKLYNMIHAHHHRLQVPYAMGALYNHPFEGLILDTFGAGVAYLAAGLSPQQAVIFFTLSTLKTVDDHCGYVFPYDPLQMFFANNARYHDLHHQPYGFQKNFSQPFFTFWDHVLGTYMPPKSETPYEKKQKAKNAKKVN", "text": "FUNCTION: Required for hydroxylation of C-4 in the sphingoid moiety of ceramide. Involved in the response to syringomycin (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family."}
{"protein": "MGCAESKDGEGEAQNNRPKYRSCTDTCWLAIYIIFWLFLIVIAIFSFVYGNPLRIINGYDSFGNTCGVKYNEKFQGFPLSGMNTLDKPELFYFDVKELKKSLKICVKSCPAKTMTKGSELLEYYSQTGTQLCKYDYNMQQLTTAGNDAKTFNFLGPCPSFPVHESSPVLHRCVPKGTGEKVQNYYDMLNNWDVAQQFVGDIYSTWHIIAMVCGLALLISIALVTMMHWLSRIVSWIICVLVIVASVALTVALWYAYYNIRNKSGVNTQYSMLEEFVRNQQAVLTLAVLATITMIILIVVIYFLKNKLAGLSALFEEAGQCMMNLPGLLIAPLLAFLVLIAFLSFWVAVIICLATASSPGQSPIAPFDNSKAHQQPLPANALFVSNSTDVNDLRPNARVEYADAGVLRSMFWIYVVGLIWTVEFIFACQQFALAAAVAFWYFQKPTSTPTFYAIGKLVKYHLGTVAKGSFVITIFKIPRLILTYLYAKLKKGEDKGSECAACCLKCCICGFWLLEKFIRFLNHNAYTVVAIESINFCPAAGIAWNAMATNVLQVATINSVGDFILFLGKVVVAALSGLIGIVLLKDKPGLNFYMAPVIIIIIFSFFIAHIILSLFEMVVDTLFLCVCEDKTLNGRSGRWAQSNLAKLVGEEPLQPGEEPPIEVVQMMPINKQPFSITRLPQSDPEVAPMSAD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CTL (choline transporter-like) family."}
{"protein": "AQCGAQGGGATCPGGLCCSQWGWCGSTPKYCGAGCQSNCR", "text": "FUNCTION: Antimicrobial peptide active against plant pathogenic fungi and Gram-negative and -positive bacteria."}
{"protein": "MRKQWLGICIAAGMLAACTSDDGQQQTVSVPQPAVCNGPIVEISGADPRFEPLNATANQDYQRDGKSYKIVQDPSRFSQAGLAAIYDAEPGSNLTASGEAFDPTQLTAAHPTLPIPSYARITNLANGRMIVVRINDRGPYGNDRVISLSRAAADRLNTSNNTKVRIDPIIVAQDGSLSGPGMACTTVAKQTYALPAPPDLSGGAGTSSVSGPQGDILPVSNSTLKSEDPTGAPVTSSGFLGAPTTLAPGVLEGSEPTPAPQPVVTAPSTTPATSPAMVTPQAVSQSASGNFMVQVGAVSDQARAQQYQQQLGQKFGVPGRVTQNGAVWRIQLGPFASKAEASTLQQRLQTEAQLQSFITTAQ", "text": "FUNCTION: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Note=Localizes at the septal ring. Is also associated with some other structures/complexes along the cell cylinder. SIMILARITY: Belongs to the RlpA family."}
{"protein": "MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMREMYSASKPLKGARIAGCLHMTVETAVLIETLVALGAEVRWSSCNIFSTQDHAAAAIAKAGIPVFAWKGETDEEYLWCIEQTLHFKDGPLNMILDDGGDLTNLIHTKYPQLLSGIRGISEETTTGVHNLYKMMSNGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACKEGNIFVTTTGCVDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYWLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMPINGPFKPDHYRY", "text": "FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form adenosine and homocysteine (PubMed:7657650). Binds copper ions (PubMed:7657650). SUBCELLULAR LOCATION: Cytoplasm Melanosome Nucleus Endoplasmic reticulum. SIMILARITY: Belongs to the adenosylhomocysteinase family."}
{"protein": "MATIHVDGKEYEVNGADNLLEACLSLGLDIPYFCWHPALGSVGACRQCAVKQYQNAEDTRGRLVMSCMTPASDGTFISIDDEEAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSFRRYRFTKRTHRNQDLGPFISHEMNRCIACYRCVRYYKDYADGTDLGVYGAHDNVYFGRPEDGTLESEFSGNLVEICPTGVFTDKTHSERYNRKWDMQFAPSICQQCSIGCNISPGERYGELRRIENRYNGTVNHYFLCDRGRFGYGYVNLKDRPRQPVQRRGDDFITLNAEQAMQGAADILRQSKKVIGIGSPRASVESNFALRELVGEENFYTGIAHGEQERLQLALKVLREGGIYTPALREIESYDAVLVLGEDVTQTGARVALAVRQAVKGKAREMAAAQKVADWQIAAILNIGQRAKHPLFVTNVDDTRLDDIAAWTYRAPVEDQARLGFAIAHALDNSAPAVDGIEPELQSKIDVIVQALAGAKKPLIISGTNAGSLEVIQAAANVAKALKGRGADVGITMIARSVNSMGLGIMGGGSLEEALTELETGRADAVVVLENDLHRHASATRVNAALAKAPLVMVVDHQRTAIMENAHLVLSAASFAESDGTVINNEGRAQRFFQVYDPAYYDSKTVMLESWRWLHSLHSTLLSREVDWTQLDHVIDAVVAKIPELAGIKDAAPDATFRIRGQKLAREPHRYSGRTAMRANISVHEPRQPQDIDTMFTFSMEGNNQPTAHRSQVPFAWAPGWNSPQAWNKFQDEVGGKLRFGDPGVRLFETSENGLDYFTSVPARFQPQDGKWRIAPYYHLFGSDELSQRAPVFQCRMPQPYIKLNPADAAKLGVNAGTRVSFSYDGNTVTLPVEIAEGLTAGQVGLPMGMSGIAPVLAGAHLEDLKEAQQ", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
{"protein": "MPVVNHEDSEFHLSHTEEDKLNEFQVITNFPPEDLPDVVRLLRNHGWQLEPALSRYFDGEWKGEPDQMGEPTQTSTPMAETLVPPALGPRPLLFTASLPVVRPLPANFRNDFRTIGLNGRSNTVWSMFESFSYDGNPFLFILLLIPRIINRLSATIFTFFCTLLSLHSISGGGNSGKPKISKVPKAPTRETHIPLAEILGDTKDKDAFCELKSFKPDISFNEALRIAKEEFKFMLLILVGDTYDTDTDTVDVNSKLLLEKILLNKKTLQYLRKIDNDLIIYLKCVHELEPWLVARQLGVRNTPEIFLIANVANKASHSETLPSQRLSILGKLKVNSLNRFLQSLTNVVEKYTPELVVNKTEMHELRMSREIKKLQEDAYKKSLEMDRIKAIEKEKSLKHAQDLKLNSTARQLKWLKACIDEIQPFETTGKQATLQFRTSSGKRFVKKFPSMTTLYQIYQSIGCHIYLAVYSSDPAEWSNALQDKIRQLSADDDMLCFKEGQLETATATTIEELGHIINNELTSFDLERGKLEFDFELVSPFPKYTVHPNEHMSVDQVPQLWPNGSLLVEALDEEDEEDEENEEQ", "text": "FUNCTION: Integral endoplasmic reticulum membrane protein that coordinates the assembly of the ER-associated protein degradation (ERAD) machinery at the ER membrane. Mediates binding of CDC48 to the E3 ubiquitin ligases SSM4/DOA10 and HRD1, and to ERAD substrates. Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin- conjugating enzymes UBC6 and UBC7-CUE1. Also a component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER- membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48- NPL4-UFD1 ATPase complex and targeted to the proteasome. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein."}
{"protein": "MSERAPLVIIGTGLAGYNLAREWRKLDGETPLLMITADDGRSYSKPMLSTGFSKNKDADGLAMAEPGAMAEQLNARILTHTRVTGIDPGHQRIWIGEEEVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRRVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVVSAVGLRPRTELAFAAGLAVNRGIVVDRSLRTSHANIYALGDCAEVDGLNLLYVMPLMACARALAQTLAGNPSQVAYGPMPVTVKTPACPLVVSPPPRGMDGQWLVEGSGTDLKVLCRDTAGRVIGYALTGAAVNEKLALNKELPGLMA", "text": "FUNCTION: Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAD-dependent oxidoreductase family."}
{"protein": "MQGDWVLLLLLGLRIHLSFGVIPVEEENPVFWNQKAKEALDVAKKLQPIQTSAKNLILFLGDGMGVPTVTATRILKGQLGGHLGPETPLAMDHFPFTALSKTYNVDRQVPDSAGTATAYLCGVKANYKTIGVSAAARFNQCNSTFGNEVFSVMHRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRDWYSDADMPSSALQEGCKDIATQLISNMDIDVILGGGRKFMFPKGTPDPEYPGDSDQSGVRLDSRNLVEEWLAKYQGTRYVWNREQLMQASQDPAVTRLMGLFEPTEMKYDVNRNASADPSLAEMTEVAVRLLSRNPQGFYLFVEGGRIDQGHHAGTAYLALTEAVMFDSAIEKASQLTNEKDTLTLITADHSHVFAFGGYTLRGTSIFGLAPLNAQDGKSYTSILYGNGPGYVLNSGNRPNVTDAESGDVNYKQQAAVPLSSETHGGEDVAIFARGPQAHLVHGVQEQNYIAHVMAFAGCLEPYTDCGLAPPADENRPTTPVQNSAITMNNVLLSLQLLVSMLLLVGTALVVS", "text": "FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate compounds. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the alkaline phosphatase family."}
{"protein": "MSDRFEATYLIETPHDVASVAQELAGEQSTATSSRMPGETDALIRDFGARVEHIEALPPAEAPSLPVAHTLGQRVHRARLTLSWPLHNIGDSLPMLLTTLLGNQTGMRRLSGIRLERVAMPQSFIAAQPRPAFGIAGTRRLTGVQGRPLIGSIVKPNIGLAPEQTAAMARQLAEGGVDFIKDDELLANPPYSPVARRAALVLRALDEAAQRTGRRTMYAVNITDGLDEMRRHHDAVVQAGGTCIMVNLNSVGLSALLALRRHSQLPIHGHRAGWAMMTRCPALGMEFQPYQMLHRLAGVDHLHVSGLGGKFWEHADSVLQAAHECLTPLDTQAGAADDRALPVFSGGSTIFDVAPTYQGIGTADLIFASGGGIFGHPDGLAAGCASLRQAWEAAIAGQELRAYAQSRPELAAALARGKPVRKA", "text": "FUNCTION: May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity (By similarity). SIMILARITY: Belongs to the RuBisCO large chain family. Type IV subfamily."}
{"protein": "MSVPRFQKINFGAYDNYVPVSELSKKSWNQQHFALVFPKPPRPGKRRRSKPSLLQENTSPKYDAEKLRGDRKQPLWMHRSLMRISERPSVYLAARSRHPQKETPPSQEDAKQAAKPSSPKVKKSKEDKDKSDSEAESIVSKEKPRKLSKAKEEKPDEKKDLKKERKDSKKGKESATESEDEKAGAEKGAKKDRKGSKKGKETPSDSGSEKGDAKKDSKKSKKDSKGKESATESEGEKGDAKKDDKKGKKGSKKGKESATESEGEKGDAKKDDKKGKKGSKKGKESATESEGEKGDAKKDDKKGKKGSKKGKESATESEGEKGDAKKDDKKGKKGSKKGKESATESEGEKGDAKKDDKKGKKGSKKGKESDSKAEGDKGDAKKDDKKDKKGSKKGKESATESEGEKKDSKKDKAGKKDPTKAGEKGDESKDKKDAKKKDSKKEKKDEKKPGEAESEPKDSAKKDAKKDAKKDAKKDAKKDAKKDAKKGK", "text": "FUNCTION: Possible architectural role during spermatogenesis. May be involved in spermatid differentiation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca, calyx. Note=Sperm head cytoskeletal structure."}
{"protein": "MSNPRMFQSRGKRVVSDSLPIANSTHTLEDTLKLRPDWTIALSQHETETRSTRTSCSTTTESTIAMRSKQKAIISVLEEFRDSEAAYVHDLHVAQRYYADRLSDRVKKSEWKDVFEIFLVLCKQASLFEIEMHKSLNDEINYILDDQDACLKPKPSVAQLFLSWLPKLSAVYGRYCVIQENIGKKVEKWMKNSSISEYLQECDSMAKIESNSWNLDSFLVKPVQRFLKYPLLLNQLYRSASLGIISDYVLLGEACHKSEIASQRMNELKRRRDIIITALDSVSNSQEVLLLSTDSIDKKIAKLQNSTNIFYVPEHEPILAFVHQLSSSYTNLLNLRSAICDWLKFSRYHYLKFFTFVEAYSVFCKDTKSADKWALISVALDNIAKGAVLRLTEQCQTSVLRPISNGILFFRNPLCVTDVWIKKATAFSKRRQSQVFEEDLESFPLLSNCLLEELPLFLEMARNVTDECILAFAQIQATFYDTIQKVLEPVVAKFNLTDHQDIPSIESIMDFTSLRSSMESSPKSK", "text": "FUNCTION: Has a role in the control of cell polarity and cytokinesis. Involved in bipolar growth and septum formation. SUBCELLULAR LOCATION: Cytoplasm Note=Septum."}
{"protein": "MSEILSSLRSLMASHSPPLDALVVPSEDYHQSEYVSARDKRREFVSGFSGSAGLALITKKEARLWTDGRYFLQALQQLSDEWTLMRMGEDPLVEVWMSDNLPEEANIGVDSWCVSVDTANRWGKSFAKKNQKLITTTTDLVDEVWKSRPPSEMSPVVVHPLEFAGRSVSHKFEDLRAKLKQEGARGLVIAALDEVAWLYNIRGTDVAYCPVVHAFAILTTDSAFLYVDKKKVSDEANSYFNGLGVEVREYTDVISDVALLASDRLISSFASKTVQHEAAKDMEIDSDQPDRLWVDPASCCYALYSKLDAEKVLLQPSPISLSKALKNPVELEGIKNAHVRDGAAVVQYLVWLDNQMQELYGASGYFLEAEASKKKPSETSKLTEVTVSDKLESLRASKEHFRGLSFPTISSVGSNAAVIHYSPEPEACAEMDPDKIYLCDSGAQYLDGTTDITRTVHFGKPSAHEKECYTAVFKGHVALGNARFPKGTNGYTLDILARAPLWKYGLDYRHGTGHGVGSYLCVHEGPHQVSFRPSARNVPLQATMTVTDEPGYYEDGNFGIRLENVLVVNDAETEFNFGDKGYLQFEHITWAPYQVKLIDLDELTREEIDWLNTYHSKCKDILAPFMNQTEMEWLKKATEPVSVSA", "text": "FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity). Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins (PubMed:11891249). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the peptidase M24B family."}
{"protein": "MLEACESKLDIIKNFVPSWFAAVMGTGILAVDSLLYSSYLPILKDVAVGLFYFNVLLFFIFLVPWVLRWIMFKDNALADLKHPVLSAFYPTIAVSCLVLGADFINIGHNMFWGGVFWTLGAIGMFLFSLIVPFYMFKSESIKLDHVNPGWYIPPVGLIVIPIAGSLIMPHLTGVWHELTVLINYFGWGAGFFLYLALLAVVIYRFILHHPLPSAMAPTVWINLGPIGAGIVALINMVNNSPFITIKEPFYIFSFIFWGFGLWWSLMAIIMTLYYVKKLKLPYAMSWWAFIFPLGAYVASSHLVYKIFKFSIIDYIGFGLYWLLFFFWAITLIKTTNKVYTGEVFKGH", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family."}
{"protein": "MVRKLNKTYAPSTRNGTIKGQVKSARGKNLIYGKHRCGKGRNARGIITARHRGGGHKRLYRKIDFRRNKKNIYGRIITIEYDPNRNAHICLIHYRNGEKGYILHPRGTIIGDTIVSGTEVSIKIGNALPLTEMPLGTAIHNLEITRGKGGQLARAAGAVAKLIAKEGKSATLKLPSGEVRLISKNCSATVGQVGNVGVNQKSLGRAGAQRWLGKRPVVRGVVMNPVDHPHGGGEGRAPIGRKKPTTPWGYPALGRKTRKGNKYSDKFILRHRRKQQRI", "text": "SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uL2 family."}
{"protein": "MLEEPRPRPPPSGLAGLLFLALCSRALSNEILGLKLPGEPPLTANTVCLTLSGLSKRQLGLCLRNPDVTASALQGLHIAVHECQHQLRDQRWNCSALEGGGRLPHHSAILKRGFRESAFSFSMLAAGVMHAVATACSLGKLVSCGCGWKGSGEQDRLRAKLLQLQALSRGKSFPHSLPSPGPGSSPSPGPQDTWEWGGCNHDMDFGEKFSRDFLDSREAPRDIQARMRIHNNRVGRQVVTENLKRKCKCHGTSGSCQFKTCWRAAPEFRAVGAALRERLGRAIFIDTHNRNSGAFQPRLRPRRLSGELVYFEKSPDFCERDPTMGSPGTRGRACNKTSRLLDGCGSLCCGRGHNVLRQTRVERCHCRFHWCCYVLCDECKVTEWVNVCK", "text": "FUNCTION: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Acts in the immune system, mammary gland, adipose tissue, bone and skin. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family."}
{"protein": "MPGLFAAKKLKDNRQNFRWKDTQYKRKTLGLNIKADPLEGSPQARGIVIEKVGIEAKQPNSAIRKCVRVQLIKNGKQITAFAPGDGAIGFIDEHDEVMIEGIGGPSGRSMGDIPGVRWKVTKVNNVALSEMVSGKIEKPVR", "text": "FUNCTION: With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits. SIMILARITY: Belongs to the universal ribosomal protein uS12 family."}
{"protein": "MSRRNQKKPQAPIGNETNLDFVLQNLEVYKSQIEHYKTQQQQIKEEDLKLLKFKNQDQDGNSGNDDDDEENNSNKQQELLRRVNQIKQQVQLIKKVGSKVEKDLNLNEDENKKNGLSEQQVKEEQLRTITEEQVKYQNLVFNMDYQLDLNESGGHRRHRRETDYDTEKWFEISHDQKNYVSIYANQKTSYCWWLKDYFNKNNYDHLNVSINRLETEAEFYAFDDFSQTIKLTNNSYQTVNIDVNFDNNLCILALLRFLLSLERFNILNIRSSYTRNQYNFEKIGELLETIFAVVFSHRHLQGIHLQVPCEAFQYLVNSSSQISVKDSQLQVYSFSTDLKLVDTNKVQDYFKFLQEFPRLTHVSQQAIPVSATNAVENLNVLLKKVKHANLNLVSIPTQFNFDFYFVNLQHLKLEFGLEPNILTKQKLENLLLSIKQSKNLKFLRLNFYTYVAQETSRKQILKQATTIKNLKNNKNQEETPETKDETPSESTSGMKFFDHLSELTELEDFSVNLQATQEIYDSLHKLLIRSTNLKKFKLSYKYEMEKSKMDTFIDLKNIYETLNNLKRCSVNISNPHGNISYELTNKDSTFYKFKLTLNQELQHAKYTFKQNEFQFNNVKSAKIESSSLESLEDIDSLCKSIASCKNLQNVNIIASLLYPNNIQKNPFNKPNLLFFKQFEQLKNLENVSINCILDQHILNSISEFLEKNKKIKAFILKRYYLLQYYLDYTKLFKTLQQLPELNQVYINQQLEELTVSEVHKQVWENHKQKAFYEPLCEFIKESSQTLQLIDFDQNTVSDDSIKKILESISESKYHHYLRLNPSQSSSLIKSENEEIQELLKACDEKGVLVKAYYKFPLCLPTGTYYDYNSDRW", "text": "FUNCTION: Ribonucleoprotein DNA polymerase that catalyzes the de novo synthesis of telomeric simple sequence repeats. Subunit p95 contains some or all of the template-independent primer DNA-binding site termed the anchor site. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere."}
{"protein": "MWLAAAVPSLARRLLLLGPPPPPLLLLLSRSSRRRRRLHSLGLAAMPEKRPFERLPAEVSPINYSLCLKPDLLDFTFEGKLEAAAQVRQATNQIVMNCADIDIITASYAPEGDEEIHATGFNYQNEDEKVTLSFPSTLQTGTGTLKIDFVGELNDKMKGFYRSRYTTPAGEVRYAAVTQFEATDARRAFPCWDEPAIKATFDISLVVPKDRVALSNMNVIDRKPYPDDENLVEVKFARTPVMSTYLVAFVVGEYDFVETRSKDGVCVRVYTPVGKAEQGKFALEVAAKTLPFYKDYFNVPYPLPKIDLIAIADFAAGAMENWGLVTYRETALLIDPKNSCSSSRQWVALVVGHELAHQWFGNLVTMEWWTHLWLNEGFASWIEYLCVDHCFPEYDIWTQFVSADYTRAQELDALDNSHPIEVSVGHPSEVDEIFDAISYSKGASVIRMLHDYIGDKDFKKGMNMYLTKFQQKNAATEDLWESLESASGKPIAAVMNTWTKQMGFPLIYVEAEQVEDDRVLKLSQKKFCASGPYGGEDCPQWMVPITISTSEDPNQAKLKILMDKPEMSVVLKNVKPDQWVKLNLGTVGFYRTQYSSAMLESLLPGIRDLSLPPVDRLGLQNDLFSLARAGIISTVEVLKVMEAFVNEPNYTVWSDLSCNLGILSTLLSHTDFYEEIQEFVKDVFSPIGERLGWDPKPGEGHLDALLRGLVLGKLGKAGHKATLEEARRRFKEHVEGKQILSADLRSPVYLTVLKHGDGATLDIMLKLHKQADMQEEKNRIERVLGATLSPELIQKVLTFALSEEVRPQDTVSVIGGVAGGSKHGRKAAWKFIKDNWEELHNRYQGGFLISRLIKLSVEGFAVDKMAGEVKAFFESHPAPSAERTIQQCCENILLNAAWLKRDADSIHQYLLQRKTSPPSV", "text": "FUNCTION: Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the peptidase M1 family."}
{"protein": "MGSAGARPALAAALLCLARLALGSPCPAVCQCPAAAPQCAPGVGLVPDGCGCCKVCAKQLNEDCSRTQPCDHTKGLECNFGASPAATNGICRAQSEGRPCEYNSKIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPSPRLVKVPGQCCEEWVCDESKDALEELEGFFSKEFGLDASEGELTRNNELIAIVKGGLKMLPVFGSEPQSRAFENPKCIVQTTSWSQCSKTCGTGISTRVTNDNPDCKLIKETRICEVRPCGQPSYASLKKGKKCTKTKKSPSPVRFTYAGCSSVKKYRPKYCGSCVDGRCCTPQQTRTVKIRFRCDDGETFTKSVMMIQSCRCNYNCPHANEAYPFYRLVNDIHKFRD", "text": "FUNCTION: Probable secreted regulatory protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CCN family."}
{"protein": "MHPRYSPAPPPQQHQGPQMGGPHPHQGGVSGGGGGGIGNMRGSGNMQQLPPQIPRSQNYSTGSSSSAAAAPPTPRSAFPGAPLTASAVALKGALPQRPPAMTSPAAAAAGAALAAGAPYRGAASWTPQGYAPAAAAAAAAVAQQAAYRYTAPLPQPAYAAYTPHTATTPATTTYGQRVPTAASPSNTNSSSSSNTGSQSGTLSTSLSNTTNTNTNMGPNGTAQNQNQQGGEQLSKTNLYIRGLQQGTTDKDLVNMCAQYGTIISTKAILDKTTNKCYGFVDFEQPAFAECAVKGLQGKGVQAQMAKVGIWVLHRPAIQQEQDPTNLYIANLPPHYKETDLEAMLSKYGQVVSTRILRDQQMNSKGVGFARMESREKCEQIIQMFNGNTIPGGKDPLLVKFADGGPKKKNLFKTPDPNARAWRDVSAEGIPVAYDPTLQQNGVSVNVGTPIGVPYSRFSAPQVGGYPVAGSQWIPGYMMTQPITQVDDQYMQMAAAPQLGVTSYKPEAVNQVQPRGISMMVSGDTAVPYGTMMPQLATLQIGNSNFSPSLQYISPTYPYYAPPPTIIPTMPMTDSEQASTAASPDEAYTQYPHQAAPK", "text": "FUNCTION: Has a role in the perception of gravity."}
{"protein": "MSNNKIKRKDASPEQEAIESFTSLTKCDPKVSRKYLQRNHWNINYALNDYYDKEIGTFTDEVSTVAHPPVYPKELTQVFEHYINNNLFDIDSLVKFIEELGYNLEDLATLCLAHLLGYKKLEEPLKREDFLSTWFMQGCSTISDMQECIKTLDVKLHEDLQYFTQIYNYAFNLILDPNRKDIDTDEGIQYWKLFFQPEYPVRMEPDLLEAWFRFLRDEGKTTISKDTWRMLLLFFKRYPTIQKIISDYDETAAWPFIIDEFYECLQDQQ", "text": "FUNCTION: Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the cullin component of SCF-type complexes."}
{"protein": "MAIGPKPESIIGSCDHPPQAEAQTGARLAAINGNNSPVSRLKDFTTDPWLTSTDQPQPGSTTNVPYSPPDSTKHARILIVGAGYGGLLFAVRLLQSGFTLEDILLVDSAGGFGGTWYWNRYPGLMCDIESYIYMPLLEETKNIPSQKYVSGEELRTHAERIAEKWKLGARTLFRTTVSDLTWDDNKLQWIATASCSSNERKQAGCTYTINADFAILANGTLSKPKVPDLPGIDDYTGRIFHTARWDYDYTGGSPAIPAMDQLRTKKVGVIGTGSTAVQVIPQLARWAGELTVFQRTPGAVGLQINRETDHAWWRDNVQLAGPEWQRKRCENFNAFITNPYRASLDAEDLVKDGWTKHPSFSVALGGARNLQADFLDLAKKIDKERREIGQQHINSTVRDPATAEALFNPTYGWCKRPCFHQGYFETYNRENVRLVSTPGQGITKLTRNGIMWGHQEFELDLIVLATGYELGSLCPANRARLSIHGRGRVSMSQKWASGPATLHGVMTRGFPNLFFPGTSQAGVTANQSYMFDRAAEHIAYIIQNARPRTAASAVNPKVRIEPSLEAEELWAMETVSRAKAFAATKTCSAGSYTISARLGESVDESQMARHMPWGEGMASYVKILEEWRKKRDMHGLEVVYD", "text": "FUNCTION: FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture (PubMed:27602587). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B (PubMed:27602587). The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK (PubMed:27602587). Finally, prhA leads to berkeleydione via the berkeleyone B intermediate (PubMed:27602587, PubMed:29317628). PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione (PubMed:27602587, PubMed:29317628). Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable). SIMILARITY: Belongs to the FAD-binding monooxygenase family."}
{"protein": "MSKSHAAYIDYALRRTTNMPVEMMGTDVVRLKDYQHFVARVFLGLDSMHSLLLFHETGVGKTMTTVYILKHLKDIYTNWAIILLVKKALIEDPWMNTILRYAPEITKDCIFINYDDQNFRNKFFTNIKTINSKSRICVIIDECHNFISKSLIKEDGKIRPTRSVYNFLSKTIALKNHKMICLSATPIVNSVQEFTMLVNLLRPGSLQHQSLFENKRLVDEKELVSKLGGLCSYIVNNEFSIFDDVEGSASFAKKTVLMRYVNMSKKQEEIYQKAKLAEIKTGISSFRILRRMATTFTFDSFPERQNRDPGEYAQEIATLYNDFKNSLRDREFSKSALDTFKKGELLKGDASAADISLFTELKEKSVKFIDVCLGILASHGKCLVFEPFVNQSGIEILLLYFKVFGISNIEFSSRTKDTRIKAVAEFNQESNTNGECIKTCVFSSSGGEGISFFSINDIFILDMTWNEASLRQIVGRAIRLNSHVLTPPERRYVNVHFIMARLSNGMPTVDEDLFEIIQSKSKEFVQLFRVFKHTSLEWIHANEKDFSPIDNESGWKTLVSRAIDLSSKKNITNKLIEGTNIWYSNSNRLMSINRGFKGVDGRVYDVDGNYLHDMPDNPVIKIHDGKLIYIF", "text": "FUNCTION: Serves two roles in transcription; it acts in concert with viral termination factor/capping enzyme to catalyze release of UUUUUNU- containing nascent RNA from the elongation complex, and it acts by itself as a polymerase elongation factor to facilitate readthrough of intrinsic pause sites. SIMILARITY: Belongs to the helicase family. NPH I subfamily."}
{"protein": "MYVVTNRIDVKKGFAEKMAPKFTQGGKIQELEGFQKVEVWLIDDEADYDQMYINTWWDSEDDFKGWLKSDAFKEAHEGKSKTKSDDSPILGNKVVKANVISELS", "text": "FUNCTION: Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the oxo-bilirubin chromophore staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo- beta-bilirubin) in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily."}
{"protein": "MNPNNRSEHDTIKATENNEVSNNHAQYPLADTPTLEELNYKEFLRRTTDNNVEALDSSTTKDAIQKGISIIGDLLGVVGFPYGGALVSFYTNLLNTIWPGEDPLKAFMQQVEALIDQKIADYAKDKATAELQGLKNVFKDYVSALDSWDKTPLTLRDGRSQGRIRELFSQAESHFRRSMPSFAVSGYEVLFLPTYAQAANTHLLLLKDAQIYGTDWGYSTDDLNEFHTKQKDLTIEYTNHCAKWYKAGLDKLRGSTYEEWVKFNRYRREMTLTVLDLITLFPLYDVRTYTKGVKTELTRDVLTDPIVAVNNMNGYGTTFSNIENYIRKPHLFDYLHAIQFHSRLQPGYFGTDSFNYWSGNYVSTRSSIGSDEIIRSPFYGNKSTLDVQNLEFNGEKVFRAVANGNLAVWPVGTGGTKIHSGVTKVQFSQYNDRKDEVRTQTYDSKRNVGGIVFDSIDQLPPITTDESLEKAYSHQLNYVRCFLLQGGRGIIPVFTWTHKSVDFYNTLDSEKITQIPFVKAFILVNSTSVVAGPGFTGGDIIKCTNGSGLTLYVTPAPDLTYSKTYKIRIRYASTSQVRFGIDLGSYTHSISYFDKTMDKGNTLTYNSFNLSSVSRPIEISGGNKIGVSVGGIGSGDEVYIDKIEFIPMD", "text": "FUNCTION: Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. SIMILARITY: Belongs to the delta endotoxin family."}
{"protein": "MKGPWLVLAALCLSLANLGPRGEDGLDFPEYDGEDRVIHISLKNYKAALKKYEVLALLYHEPIGDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEDDAAVAKKLGLDEEDSIYVFKDDEMIEYDGEFSADTLVEFLLDVLEDPVEFIDGSHELAAFENLDDEPKLIGYFKNEDSEHYKAYEDAAEEFHPYIPFFATFDAKVAKTLTLKLNEIDYYEPFHDEPITIPSKPNSEKEIVDFLHQHKRPTLRKLRPDSMYETWEDDLNGIHIVAFAEEDDPDGYEFLQIIKEVAEDNTDNPDLSIIWIDPEDFPLLIPYWEEKFGIDLSRPHIGVVNVTDADSVWMDMDDEEDLPTVDELEDWIEDVLEGEVNTEDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDD", "text": "FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium- binding protein and thus acts as an internal calcium store in muscle (PubMed:1375450). Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum Sarcoplasmic reticulum Sarcoplasmic reticulum lumen Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side Mitochondrion matrix Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells. Preferentially forms linear and round aggregates in the endoplasmic reticulum (ER) of resting cells. In a minority of cells, homogeneously detected in the ER lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a depletion of intracellular calcium. SIMILARITY: Belongs to the calsequestrin family."}
{"protein": "MPDEKLPQYNEVWNDLEKGCLHSCPSYSVNNHVNNPIVKQNSTLTQPSLRKKNTMAAPARLRKRSENVRLTQARYAIFHIFLPFILTLLLYHNFYNYFDQALADLNSVVKYVIETIVLIFTYVMTVIIVYFSFSLIKLAFEEAYVYAPSVAKANEGLAKHVAKTIAGLVKYVAKAIQGLAHIILSLLLFILGLEVIEQDEETGDVEMSSMRGQAITTEPASDNTMAEGTDCNTSKDVESGSS", "text": "SUBCELLULAR LOCATION: Cytoplasm Membrane; Multi-pass membrane protein."}
{"protein": "MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQHVS", "text": "FUNCTION: Part of the binding-protein-dependent transport system for glutamine. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MSTAMNKFTQTISKPATILNISDSEESGDEAGVGKVSRTTQSSERWLDLLIEKFQPSLQNITRYINWNFIRICNDRLKKEKMGYIEAKQYVEDMAWMVIASEADSIEWKCIRRQEKVTGVKYPKFFFVQHKEDWIECTGCIPYPGHDLIYDEDDDD", "text": "FUNCTION: Plays a major role in antagonizing the type I IFN-mediated antiviral response. May also inhibit viral transcription and RNA replication (By similarity). SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the pneumovirus non-structural protein 2 family."}
{"protein": "MVDAITVLTAIGITVLMLLMVISGAAMIVKELNPNDIFTMQSLKFNRAVTIFKYIGLFIYIPGTIILYATYVKSLLMKS", "text": "FUNCTION: Envelope protein. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Note=Probably localizes to the membrane of mature virions (MV). SIMILARITY: Belongs to the orthopoxvirus OPG081 family."}
{"protein": "MAEESNKLAFPSVVDRYFTRWYKPDIKGKPCEDHCILQHSNRICIITLAECHPLLQNEKTIKSISYQISANCSRLQNKVSGKSKRGAQFLTELAPLCRISSTDGEEYTIYSCIRGRLLEVNENILQNPGLLKEKPSTEGYIAVVLPKFEESKTITEGLLSQREYEEIVQSRAALRSETVQAVY", "text": "FUNCTION: May regulate actin polymerization, filopodia dynamics and arborization of neurons. SUBCELLULAR LOCATION: Nucleus speckle Cell projection, lamellipodium Nucleus Cell projection, growth cone Cell projection, dendrite Note=Localizes to somata and dendrites in cortical neurons. SIMILARITY: Belongs to the ABITRAM family."}
{"protein": "MGKSLLTDEMIERANRGEKISGPPLLDDNEETKILPTSSSRFGYANPKDHGFSQETLKIQVEPSIHKSRRIENTKRNVFNSKLNKILFAVIFLLILLVLAMKLL", "text": "FUNCTION: Required for the in vivo function of penicillin-binding protein 2a (PBP2a), which is involved in the biosynthesis of cross- linked peptidoglycan (PG) of the cell wall. SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein Note=Localizes to sites of new peptidoglycan (PG) synthesis at midcell independently of PBP2a."}
{"protein": "MERAENARIIQKPMTRRTVDYGSGLSKYIVNRHLRSNRYHIHVPRPNPNQIINLYPPYEYKYNNTSSLCTKYIHTSANKARHVINVVRWTPDGRRLLTGSSTGEFTLWNGLTFNFELINQSHDYAVRCAEWSTDGRWLISGDGGGMVKYFEPNLNNVKIVQAHEMEVRDVAFSPNDSKFVTASDDGSLKVWNFHMSTEELKLTGHGWDVKTVDWHPSKGLLASGSKDNLVKFWDPRTGTCIATLHGHKNTIMQASFQKNFGSNYLATVSRDSTCRVFDLRAMKDVRVLRGHEKDVNCVTWHPLYPNLLTTGGSDGSVNHYSLDEPPLLSQQKYHEKHPNVTLSASSYLLYPTAEIPFAHDLGIWSMQYHPLGHLLCTGSNDKTTRFWSRSRPDDKESTMDRHHLGEEQSEAMLSQRKAAIEEDDNYEPDENPLTETLANAHNPQFSGVLNLPGLGTMPSFPSPYQHGQPQIPGMLHASLSNSYAEPSTQNSFIPGLTSKSQDGYPQNYR", "text": "FUNCTION: Required for 3'-end cleavage and polyadenylation of pre- mRNAs. Also involved in chromosome segregation where it has a role in chromosome attachment to the mitotic spindle. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MMCKALVFAVLLLAVPLERADSRALRTPVDAIQFVEQFLEHYNDLLNIDDLENQTGDQLESPQPLSSGLKVAEYPKWVDVPSQNDNTWFRLLRGALANRKRALPDRAKRGWNRGCFGLKLDRIGSLSGLGC", "text": "FUNCTION: Hormone which plays a role in endochondral ossification through regulation of cartilaginous growth plate chondrocytes proliferation and differentiation. May also be vasoactive and natriuretic. May be important for freshwater adaptation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family."}
{"protein": "MESDCQFLVAPPQPHMYYDTAAAAVDEAQFLRQMVAAADHHAAAAGRGGGDGDGGGGGGGGGGERKRRFTEEQVRSLETTFHARRAKLEPREKAELARELGLQPRQVAIWFQNKRARWRSKQIEHDYAALRAQYDALHARVESLRQEKLALAAQVDELRGKLNERQDQSGSCDGGGAEGDDDDKRNSVMNASSSGLVEEDYVSCLAVPVVDVSEDGSAACGGSSYEYDHHLDYLGGGQLPDPFCGMPDLWETWPMVEWNAVA", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class I subfamily."}
{"protein": "MALLWGLLVLSWSCLQGPCSVFSPVSAMEPLGRQLTSGPNQEQVSPLTLLKLGNQEPGGQTALKSPPGVCSRDPTPEQTHRLARAMMAFTADLFSLVAQTSTCPNLILSPLSVALALSHLALGAQNHTLQRLQQVLHAGSGPCLPHLLSRLCQDLGPGAFRLAARMYLQKGFPIKEDFLEQSEQLFGAKPVSLTGKQEDDLANINQWVKEATEGKIQEFLSGLPEDTVLLLLNAIHFQGFWRNKFDPSLTQRDSFHLDEQFTVPVEMMQARTYPLRWFLLEQPEIQVAHFPFKNNMSFVVLVPTHFEWNVSQVLANLSWDTLHPPLVWERPTKVRLPKLYLKHQMDLVATLSQLGLQELFQAPDLRGISEQSLVVSGVQHQSTLELSEVGVEAAAATSIAMSRMSLSSFSVNRPFLFFIFEDTTGLPLFVGSVRNPNPSAPRELKEQQDSPGNKDFLQSLKGFPRGDKLFGPDLKLVPPMEEDYPQFGSPK", "text": "FUNCTION: Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase- 3/TMPRSS7 and chymotrypsin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family."}
{"protein": "MISSQDVGKRVRLSRILPDGRSVIFAFDHGIEHGPGEIPEERLDPRLLIREVVEAGVDAIMTTPGIARLTWDIWANRVAMIIKVSGKTSIRPQDDQFLQSAISSVDEVVALGGDGVAATVYWGSQFEDKMLERWTRIRLRAEKLGLPALQLAYPRGPHIKNRYAVDIVAYGARAAMETGADLIKTYYTGSTESFRRVVSAAGGVPVLMSGGARTPSPQEFLHKVYSVMEAGGGGVVVGRNIFQAGDIRAMVKAIRAIVHEGFDPEKASKLLG", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DeoC/FbaB aldolase family."}
{"protein": "MASALEQFVNSVRQLSSQGQMTQLCELINKSGELLAKNLSHLDTVLGALDVQEHSLGVLAVLFVKFSMPSIPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGICVIRQAIDKMQMNANQLTSIHGDLCQLSLLAKCFKPALAYLDVDMMDICKENGAYDAKPFLCYYYYGGMIYTGLKNFERAMYFYEQAITTPAMAVSHIMLEAYKKYILVSLILHGKVQQLPKYTSQVVGRFIKPLSNAYHELAQVYSTNNPAELRNLVSKHNETFTRDNNMGLVKQCLSSLYKKNIQRLTKTFLTLSLQDMASRVQLSGAQEAEKYVLYMIEDGEIFASINQKDGMVCFHDSPEKYNNPAMLHNIDQEMLRCIDLDDRLKAMDQEITVNPQFVQKSMGSQEDDSGSKPSSYS", "text": "FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CSN3 family."}
{"protein": "ASMFKHDHYMDNGVRYPNGDGICEQLNETKCDAGFSYDRSICEGPHYWHTISKCFIACGIGQRQSPINIVSYDAKFRQRLPKLKFKPHMEKLKTEVTNHQNRAPEFEPEDGENLYVKLNNLVDGHYKFHNLHVHNGRTRRKGSEHSVNGRFTPMEAHLVFHHDEQTHFEPTRTKLGGAFPGHNDFVVVGVFLEVGDDGFGDEPDDEECKHILKGHHPDNNENGNGDNGNNGYNGDNGNNGDNGNNGYNGDNGNNGVNGNNGYNGDNGNNGDNGNNGENGNNGENGNNGENGHKHGCRVKKAKHLSRILECAYRNDKVREFKKVGEEEGLDVHLTPEMPLPPLKYRHYYTYEGSLTTPPCTESVLWVVQKCHVQVSRRVLHALRNVEGYKDGTTLRKYGTRRPTQKNKVTVYKSFK", "text": "FUNCTION: Acts as a negative regulator for calcification in the shells of mollusks. May function both as a calcium concentrator and as a carbonic anhydrase required for production of carbonate ions, which are assembled to CaCO(3) at mineralization sites. Is important for shell formation in both the calcitic prismatic layer and the aragonitic nacreous layer (By similarity). Shows inhibitory activity of crystal formation when present in free state but, when attached to the insoluble matrix, may regulate the form and size of aragonite crystal. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the alpha-carbonic anhydrase family."}
{"protein": "MDSDDESEAVHSVFNTVSQEGGKIFEQREILQIDYVPSENRIVGRDEQIEKVAGEIGPIVVGQPPNSIIIYGKTGCGKSLVAKHVSKIAREEAENRGVKLATGYVNCQQAKGNSDALSKYGRAINPPESGVKFPTRGISENEYFERVWSVLNEFYDAAIIVLDEVDKLNNDDLLMALSRAGEDGSVDVPIGVIAVSNKINYRDKMSERTKSSFGHNEFIFEPYDADQIREILQNRTDAFADGVLDDGVIPRAAALSAKEHGDARKAMRLLRYAGDQANKENAERVKESHLTDARASAEVDRLLELISGLPPHSKHVLLALANLTKNHPDREWFRTVRVREIYLEVCDRSGADPLSAERTRQLLNELCFLEVAGSRRGTGEGKGHYSQYTLLWDADIVLTLGN", "text": "FUNCTION: Involved in regulation of DNA replication. SIMILARITY: Belongs to the CDC6/cdc18 family."}
{"protein": "MLLPCALLAALLAAGHAANPCCSLPCQNRGVCMTTGFDRYECDCTRTGYYGENCTTPEFFTWLKLILKPTPNTVHYILTHFKGVWNIINNISFLRDTIMRYVLTSRSHLIDSPPTYNSDYSYKSWEAYSNLSYYTRSLPPVGHDCPTPMGVKGKKELPDSKLIVEKFLLRRKFIPDPQGTNVMFTFFAQHFTHQFFKTDHKKGPGFTKAYGHGVDLNHIYGETLERQLKLRLRKDGKLKYQMIDGEMYPPTVKDTQAEMIYPPHVPEHLQFSVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTTRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQRFQYQNRIAAEFNTLYHWHPLLPDTFQIHNQEYTFQQFLYNNSIMLEHGLSHMVKSFSKQSAGRVAGGKNVPAAVQKVAKASIDQSRQMRYQSLNEYRKRFMLKPFKSFEELTGEKEMAAELEELYGDIDAMELYPGLLVEKPRPGAIFGETMVEIGAPFSLKGLMGNTICSPEYWKPSTFGGKVGFEIINTASLQKLICNNVKGCPFTAFHVLNPEPTEATINVSTSNTAMEDINPTLLLKEQSAEL", "text": "FUNCTION: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S- stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy- (10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)- octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. SIMILARITY: Belongs to the prostaglandin G/H synthase family."}
{"protein": "MSIVGRNAILNLRISLCPLFMGKRSFVSSPVSNSAKAVKFLKAQRRKQKNEAKQATLKASTDKVDPVLGRADTPFITRIMAELKEPLVLSKGYNIEEVDKFLAAIESAKRERAELSGLNTEVVGIEDIEKLEDRREAILRILSMRNSENKNAIKMAVELARKEFERFPGDTGSSEVQAACMTVRIQNMANHIKEHRKDFANTRNLRILVQQRQAILRYLKRDNPEKYYWTIQKLGLNDAAITDEFNMDRRYMQDYEFFGDKILIRDSKKVANQKRKEIRKQKRATF", "text": "FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the universal ribosomal protein uS15 family."}
{"protein": "MTLKEEFATRNFSIYGQWLGVLSMILCFALGIANIFTFRLLLIIFSVICLVSSFVILFIEVPLLLRICPTSSTFDDAIRKVSTNYMRAAAYLVMGVVQWLSLLGGASSLIAAAVFLTLTAICYALAGVKGQAFVGSKTLGGSGVAQMIV", "text": "FUNCTION: Golgi membrane protein involved in vesicular trafficking. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the TVP18 family."}
{"protein": "MEAENIRADAFEPAKRATKRGASGGGQQDVEMQVDEATGIEGQVLGSSRASAPPKAKRARSELRKVSVPPHRYSSLKEHWMKIFTPVVEHMKLQIRFNMKARQVELRVGPETPDIANLQRGADFVRAFLCGFEVDDALALLRLEDLFVESFEIKDVKTLRGDHQSRAIGRLAGKGGRTKFTIENVTKTRIVLADSKIHILGSYQNIQLARRAVCNLILGSPPSKVYGNLRAVASRLSERM", "text": "SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the PNO1 family."}
{"protein": "MRWKRTIQLLDVHAEGEIGRVAIGGVPKIPGETIAAQLHWLNTDPKGDELRRFLCLEPRGAPIGSVNLLLPARHPDADAAFIILQPDQAHASSGSNSICVTTALLESGIVEMQEPETIVTLETAAGLVKATATCRDGRCEKVKLTMVPSFVHELDVEIDTPHWGKIKADLCYGGIFYALVDVGQINLTIEKANAAGLVQAGMILKELINRDIKVVHPEIPAISGVAYVMFRDTEADGTVRTCTTMWPGRADRSPCGTGNSANLATLHARGKAKVGDVFTSKSIIGSEFEVGLQAVTEVAGRPAVIPTITGRGFTFGLTQVALDPFDPHPGGFALTDVWGPSAGEI", "text": "FUNCTION: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro, albeit with 2-fold lower efficiency. Displays no proline racemase activity. SIMILARITY: Belongs to the proline racemase family."}
{"protein": "MAAPVLYGGAGGTATGPGDMRRSLMHEKKQVFAELRREAQALRVAKEARGKMSVWDPSTREGARGYREKVVRFGRQIASLLQYFENMHSPALDIIACDKFLLKYQIYGDIDRDPAFGENTMTAEVPVVWDKCEVEVKLYAGPLQKLMSRAKLVGAAREGIPNRNDVAKSTGWNQDQVQKFPDNRMDSLISLLEQMQTGQSKLTRLVKGFLILLEMAERKEVDFHVGNHIHVTYAIAPVCDSYDLPGRCYVFNSKPTSEAHAAVLLAMCREYPPPQFASHVSVPADAEDVCIVSQGRQIQPGSAVTLNPGLVYSSILTYAMDTSCTDLLQEAQIIACSLQENRYFSRIGLPTVVSLYDLMVPAFIAQNSALEGARLSGDLSKAVGRVHQMLGMVAAKDIISATHMQSRTGFDPSHGIRQYLNSNSRLVTQMASKLTGIGLFDATPQMRIFSEMDTADYADMLHLTIFEGLWLVQDASVCTDNGPISFLVNGEKLLSADRAGYDVLVEELTLANIRIEHHKMPTGAFTTRWVAAKRDSALRLTPRSRTAHRVDMVRECDFNPTMNLKAAGPKARLRGSGVKSRRRVSEVPLAHVFRSPPRRESTTTTDDSPRWLTREGPQLTRRVPIIDEPPAYESGRSSSPVTSSISEGTSQHEEEMGLFDAEELPMQQTVIATEARRRLGRGTLERIQEAALEGQVAQGEVTAEKNRRIEAMLSARDPQFTGREQITKMLSDGGLGVREREEWLELVDKTVGVKGLKEVRSIDGIRRHLEEYGEREGFAVVRTLLSGNSKHVRRINQLIRESNPSAFETEASRMRRLRADWDGDAGSAPVNALHFVGNSPGWKRWLENNNIPSDIQVAGKKRMCSYLAEVLSHGNLKLSDATKLGRLVEGTSLDLFPPQLSSEEFSTCSEATLAWRNAPSSLGVRPFAQEDSRWLVMAATCGGGSFGIGKLKSLCKEFSVPKELRDALRVKYGLFGGKDSLE", "text": "FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 35-40 nm in diameter. SUBCELLULAR LOCATION: Virion."}
{"protein": "MSTVEPLSDEGVAAGPRRIEVPRPPSIEEFTIVKPISRGAFGKVYLGRKAGRLYAVKVMKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEAALALDYLHRHGIIHRDLKPDNMLISNQGHIKLTDFGLSRVTLNREINMIDILTTPSMAKPKHDYSRTPGQLLSLISSLGFYTPVGMKMPINPNSGGASDSLHEVISPLSMIEKENTPLSTKLFKTGLDTSPLTPVMPVRSLTPALLQSRERFGASTASSQSCMYLSSMESECCSSPRLEKDVKQTEDEMCSTGTSNSRPPLPSSREVLNSKDPKVLKKELESAISPISSNDCGSRQKLGTERSEITDTPVTTLDTKGIVRKCLSENKIWEEKLVARREMTNEMLETASSQQSPLFLKDPVQPVKEEEIFEKPGVKRSFELVDTSPCQELNYVKKTNAEYKRGCWISELSASKSTGLTTEIQSLMLSGEICESKEIMRCIDRQQTEKPLVPTVAKNLLCDLDADHEKDKEYMNSSLLCADDEKPLGALSADSDLSFPETSVSESHLEKQLVDLDKGVKDLSFEEPKAEDLLTMSPNCQEASRNGVEADVVQNCTMLCCEQDNHQKHTEETDTISSPSEKMTETVHLFRKNNVVFRSYNSPINVSNVSDPCSMASLDIMDLSPACSGSYPTAITPLQKTPRQGDAGTPYRTPKSVRRGAAPVEGERILGTPDYLAPELLLTKPHGSAVDWWALGVCLFEFLTGIPPFNDETPAQVFQNILKRDIPWPEGEEKLSDNAQNAIDILLTFDSTKRAGLKELKHHPLFHGVDWDNLQNQPMPFIPQPDDETDTSYFEARNNAQHLTVSGFSL", "text": "FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser- 62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family."}
{"protein": "MPDDASDLADRVQAGDLRLYELDDETDADTAAAARRAVLERETDADTDALGAFAFDADQAADTAVENLTGGAQLPLGVAGPVALSGGAADGEYYLPMATTEGALVASVNRGCSAITAAGGANARVTKTGMTRAPVFRVADVTEGAEVAQWADDNTDALAAAAESTTSHGELTDVTPYVVGDNVYLRFRYDTKDAMGMNMATIATEAASELVEDETPAELVAVSGNLCTDKKPAAINAVEGRGRTVTADVTIPQDVVEERFDTTPAAIEEANTRKNLIGSAKAGSLGFNAHAANVVAAVFLATGQDAAQVVEGANAITTVEARDDALYASVNLASLEVGTVGGGTTLPTQREALDVLGVRGGGDPAGANADALAEIIAVGALAGEINLLAALASRRLSAAHADLGR", "text": "FUNCTION: Catalyzes the NADPH-dependent reductive deacylation of (S)-3- hydroxy-3-methylglutaryl-CoA (HMG-CoA) to (R)-mevalonate. Cannot use NADH instead of NADPH. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HMG-CoA reductase family."}
{"protein": "MALRLATRRFAPIAFRRGMATTIEHTKEPISATAEALSASRPPIKETKTSTVKEPQMDADAKTKTFHIYRWNPDQPTDKPRMQSYTLDLNKTGPMMLDALIRIKNEVDPTLTFRRSCREGICGSCAMNIDGVNTLACLCRIPTDTAKETRIYPLPHTYVVKDLVPDMTQFYKQYKSIKPYLQRDTAPPDGKENRQSVADRKKLDGLYECILCACCSTSCPSYWWNSEEYLGPAVLLQSYRWINDSRDEKTAQRKDALNNSMSLYRCHTILNCSRTCPKGLNPALAIAEIKKSMAFTG", "text": "FUNCTION: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family."}
{"protein": "MKMVAPWTRFYSNSCCLCCHVRTGTILLGVWYLILNAVVLLILLSALADPDHYHFSSSELGGDFEFMDDANMCIAIAISVLMILICAMATYGAYKQRAAWIIPFFCYQIFDFALNTLVAVTVLVYPNSIQEYIRQLPPDFPYKDDIMSVNPTCLVLIILLFISIILAFKGYLISCVWNCYRYINGRNSSDVLVYVTSNDSTVLLPPYDDATVNSATKEPPPPYVSA", "text": "FUNCTION: Required for optimal lysosomal function. Blocks EGF- stimulated EGFR intraluminal sorting and degradation. Conversely by binding with the phosphatidylinositol 4,5-bisphosphate, regulates its PIP5K1C interaction, inhibits HGS ubiquitination and relieves LAPTM4B inhibition of EGFR degradation. Recruits SLC3A2 and SLC7A5 (the Leu transporter) to the lysosome, promoting entry of leucine and other essential amino acid (EAA) into the lysosome, stimulating activation of proton-transporting vacuolar (V)-ATPase protein pump (V-ATPase) and hence mTORC1 activation. Plays a role as negative regulator of TGFB1 production in regulatory T cells. Binds ceramide and facilitates its exit from late endosome in order to control cell death pathways. SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Late endosome membrane Cell membrane Cell projection Lysosome membrane Endosome membrane Endosome, multivesicular body membrane Endosome, multivesicular body lumen. SIMILARITY: Belongs to the LAPTM4/LAPTM5 transporter family."}
{"protein": "MSTLLGWLGRLWFGSLGTARPDPSTAVAAAGSTDVTSTQDAWAVLSLVNEWVKHSEAKLGVVLAFVGVMAAGLITIAADIPCPSLVILCIEGAAAVLILASAVLASLGLLPRFKGQSEEAQMNPLFYGDVANHFKGKSEEYVTALSGVIGSQDALIRQIARQVHANADVASRKYLWANRSILVGMLGLVCLFVLAAGVALGW", "text": "FUNCTION: Pycsar (pyrimidine cyclase system for antiphage resistance) provides immunity against bacteriophage. The pyrimidine cyclase (PycC) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate the adjacent effector, leading to bacterial cell death and abortive phage infection. A clade D Pycsar system. FUNCTION: The effector gene of a two-gene Pycsar system. Expression of this and adjacent uridylate cyclase PtPycC (AC A0A4V2JTK3) probably confers resistance to bacteriophage. The genes are probably only expressed in response to bacteriophage infection. Probably only responds to cUMP (produced by its cognate NTP cyclase), acts by impairing membrane integrity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MVKIFIDPGHGGSDTGASANGLQEKQLTLQTALALRNMLLNEYQNVSVLLSRTSDQTVSLTQRTNAANSWGADYFLSIHMNAGGGTGFEDYIYPGVGAPTTTYRDIMHEEILKVVDFRDRGKKTANFHVLRETAMPALLTENGFVDNTNDAEKLKSSAFIQSIARGHANGLARAFNLSKNAAALYKVQIAAFRTKANADSLAAQAEAKGFDALVIYRDSLYKVQIGAFSSKENAEALVQQAKNAEFDTFIYQE", "text": "FUNCTION: Hydrolyzes the cell wall of M.luteus more efficiently than that of B.licheniformis and B.subtilis. The C-terminal region, including the repeats, determines substrate specificity. SUBCELLULAR LOCATION: Secreted Note=Accumulates in cells as inclusion bodies. May be secreted by a mechanism different from the normal export system. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family."}
{"protein": "MSDEEIDISTALNNKTTPKKKSLKRNSNSQEGYESPEEREIVYPSVFGAIGTPMAKSDNAKEWDEWKEKERKKDKAEWKRYLRSKWDMTQGHLPLVSDSEFLKGRKEHKEYNSKARMDILDGLDEVNEGFFNCGKGAAMNIRYNDKNVSKKGAKKFVATVETAMKKAGNPTMEQMMTDDLDEDEARAEAEWERQREQRKLASRAYDAAMDEREDDAKYVPWDEYCQEMEELGKELKIGEKHYKKWLEKKMDENKVTHKFNAYQLDLKCLDEDAFSNKKSLKSVVRNVQKFYRKMREPKK", "text": "FUNCTION: Paternally sperm-supplied factor required for embryogenesis (PubMed:8565851, PubMed:20971008). Plays a role in preventing polyspermy possibly by promoting the formation of a continuous and cohesive eggshell chitin layer (PubMed:20971008). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Note=Localized to the perinuclear region of sperm."}
{"protein": "MKLSLSPPPYADAPVVVLISGLGGSGSYWLPQLAVLEQEYQVVCYDQRGTGNNPDTLAEDYSIAQMAAELHQALVAAGIEHYAVVGHALGALVGMQLALDYPASVTVLISVNGWLRINAHTRRCFQVRERLLYSGGAQAWVEAQPLFLYPADWMAARAPRLEAEDALALAHFQGKNNLLRRLNALKRADFSHHADRIRCPVQIICASDDLLVPTACSSELHAALPDSQKMVMPYGGHACNVTDPETFNALLLNGLASLLHHREAAL", "text": "FUNCTION: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously. FUNCTION: Involved in pyrimidine catabolism (PubMed:16540542). May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously (Probable). SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD family. SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD family."}
{"protein": "MAADEVAGGARKATKSKLFEFLVHGVRPGMPSGARMPHQGAPMGPPGSPYMGSPAVRPGLAPAGMEPARKRAAPPPGQSQAQGQGQPVPTAPARSRSAKRRKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRVDIQEALKRPMKQKRKLRLYISNTFNPAKPDAEDSDGSIASWELRVEGKLLDDPSKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTPTTQETDGFQVKRPGDLSVRCTLLLMLDYQPPQFKLDPRLARLLGLHTQSRSAIVQALWQYVKTNRLQDSHDKEYINGDKYFQQIFDCPRLKFSEIPQRLTALLLPPDPIVINHVISVDPSDQKKTACYDIDVEVEEPLKGQMSSFLLSTANQQEISALDSKIHETIESINQLKIQRDFMLSFSRDPKGYVQDLLRSQSRDLKVMTDVAGNPEEERRAEFYHQPWSQEAVSRYFYCKIQQRRQELEQSLVVRNT", "text": "FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:22952240, PubMed:26601204). Stimulates nuclear receptor mediated transcription. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SMARCD family."}
{"protein": "MESLFPNKGEIIRELLKDPLILKNDSKRSNGSELELDSSDLLQREAILANELNILDNLKTFLNLIKEVKTNLNILELENCYYSLQSLRKKMRNNAAYLKQSFNFQQSISTYVDTLHLELVSTLYKILTNGFWKITENSIQFTPTVEWGKDKVHIEYDTFMDFVAQQYFPKGSLDNQAWFILDMTSADSQEQVRAKLNTIMKEYMNLSRIVSMIKNSIFISGKEISYENEKNILVFSKSSSHGQHCVSTVLTSFEAVCDFMLDGLAFRDRKTLSYELGPLFNTEFTKFVKNNASIILESLDSPLKNLVSVINNKLTRLVAKSEVTNWTHSGKEIQDLLMNKQLYYNLLLDKVLESHISEIRSIFEDPKKSWQNLEVVELTTSNTNTMSEKIGKNDSDVQNEKELHNAVSKDDDWNWEVEDDDADAWGDEIDVNIDDEEEKTNQEKEKEPEEEENAWDEAWAIDENIDDASLENGKEHLKAHDVGSLDKDHIEVTQLPKLFLAISQNFKSSFADSHVDEQYFAYKYNLLQTSYMAMCTANFSHNWCQLYVDMRYLIERDEKLYRIKELTRNLLETKLNMKYRIVCQLIRHQLTEFRENERNPSWDATIEKLLPYILKEIVRPLQKIRGEEGSRYLLSFLNFLYNDCVTKEILKWQIISEVNSENLGELVSLLVNNTDIQLLAKEPSYKKMREKFATMGKFLPLHLKEIMEMFYNGDFYLFATDELIQWIELLFADTPLRRNAIDDIYEIRGTALDD", "text": "FUNCTION: Required for protein transport between the Golgi and the endoplasmic reticulum. May tether coatomer-coated retrograde transport vesicles to the ER membrane through interaction with coatomer as well as the SNARE complex. May contribute to the stabilization of the SNARE complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein."}
{"protein": "MAETDPKTMQDITLVVETLLQQMQDKFQIMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELDPENKIPTAQKS", "text": "FUNCTION: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HSBP1 family."}
{"protein": "MSPSPTALFCLGLCLGRVPAQSGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAMKRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGPAVSSGGDVTLQCQTRYGFDQFALYKEGDPAPYKNPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTGTSVTPSRLPTEPPSPVAEFSEATAELTVSFTNEVFTTETSRSITASPKESDSPAGPARQYYTKGNLVRICLGAVILIILAGFLAEDWHSRRKRLRHRGRAVQRPLPPLPPLPLTRKSNGGQDGGRQDVHSRGLCS", "text": "FUNCTION: Collagen receptor involved in collagen-induced platelet adhesion and activation. Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma-chain, the Src kinases (likely FYN or LYN) and SYK, the adapter protein LAT and leads to the activation of PLCG2. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass membrane protein."}
{"protein": "MSFRDLRNFTEMMRALGYPRHISMENFRTPNFGLVSEVLLWLVKRYEPQTDIPPDVDTEQDRVFFIKAIAQFMATKAHIKLNTKKLYQADGYAVKELLKITSVLYNAMKTKGMEGSEIVEEDVNKFKFDLGSKIADLKAARQLASEITSKGASLYDLLGMEVELREMRTEAIARPLEINETEKVMRIAIKEILTQVQKTKDLLNNVASDEANLEAKIEKRKLELERNRKRLETLQSVRPCFMDEYEKTEEELQKQYDTYLEKFQNLTYLEQQLEDHHRMEQERFEEAKNTLCLIQNKLKEEEKRLLKSGSNDDSDIDIQEDDESDSELEERRLPKPQTAMEMLMQGRPGKRIVGTMQGGDSDDNEDSEESEIDMEDDDDEDDDLEDESISLSPTKPNRRVRKSEPLDESDNDF", "text": "FUNCTION: Required for cilia biogenesis. Appears to function within the multiple intraflagellar transport complex B (IFT-B). Key regulator of hedgehog signaling. SUBCELLULAR LOCATION: Cell projection, cilium Nucleus. SIMILARITY: Belongs to the CLUAP1 family."}
{"protein": "MMLITTSHRPTRRTRSFGHDLERVFPNSLYMTRGKKTIQELLMEAYDRGYERLLIINVWKGNPLKMTFIKVHPDDWGYLGYLYLHGVKLQREMGFRGLNPIREDMPLVVTTAKRVGLDHLAFAQVFSELTTGKFVPRGDKSLLSIADKYNTDVLAVIERHPRGIVVNFYRLDVTKERAVGPLINVKIWIMEDGRRWDYKEAFGIKVKPRRKEGEAEEGARKDSH", "text": "FUNCTION: Probably involved in the biogenesis of the ribosome."}
{"protein": "MDSLTIPPVDLRLLAPLLVVVTWATVLLLVDVFFIPDGRKKLTGYLAIGGLVVAGLVGLPLWGVTGTTFGGMLRLDPFALTLTWIFLLIGILSITMSLDYLPGQGIEQGEYYPLIMFAVSGMILLAQGTDLIVLFLGIETLSITLYILTGFAYPRLTSEEAAMKYLVLGAFAAGFFVYGIALIFGATGSTRLGEIGAYAASRGIGDLNLTLLLGGAAMVLIAFSFKVALAPFHMWTPDVYEGSPTPVAAFMSVGTKGGALAALVRLLFEGLPTLNEYWLPVLAGLTALTMVVGNLGAVAQTNVKRMLAYSSIGHAGYVMLGVMVAGEQRGPEAFLFYMLVYALSNLGAFAVLIALEHQGENAWRLDDFAGLYQRQPLLAVAMAIFMFSLAGVPPMAGFMAKFYALTAAWEGGLPWLALVGVVTSAIAAFFYLRVIIRMFMTEPEGEPTPTLNRGLTVDIALAAIGTIAIGLIPAPVFALVERSLVVLGG", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."}
{"protein": "MRLSIVTTMYMSEPYVLEFYRRARAAADKITPDVEIIFVDDGSPDAALQQAVSLLDSDPCVRVIQLSRNFGHHKAMMTGLAHATGDLVFLIDSDLEEDPALLEPFYEKLISTGADVVFGCHARRPGGWLRNFGPKIHYRASALLCDPPLHENTLTVRLMTADYVRSLVQHQERELSIAGLWQITGFYQVPMSVNKAWKGTTTYTFRRKVATLVDNVTSFSNKPLVFIFYLGAAIFIISSSAAGYLIIDRIFFRALQAGWASVIVSIWMLGGVTIFCIGLVGIYVSKVFIETKQRPYTIIRRIYGSDLTTREPSSLKTAFPAAHLSNGKRVTSEPEGLATGNR", "text": "FUNCTION: May play only a redundant role in maintaining cell wall viability and bacterial virulence. FUNCTION: May play only a redundant role in maintaining cell wall viability and bacterial virulence. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family."}
{"protein": "MSSFSTHNFVAIATFVCWFCCLATAAPLTSKAAYLLKRNSLIEEDASRKLGAKIVLTNEEKVLDDFILAEKRKLIDDSRLNQTEYMPAASFYRSKDFIDTTFAYKIIQDMPKGGALHLHDLAIASLDWVVKNATYRDNVYMCMDKDNDVNLRVLQLIPPDPFCVWKLVATERANSGDVEAFDDWLKKNISYLSTDPVTQYATVDSVWVRFNKYFAQVIGLLFYAPIMRDYYRQALEEFRADNVQYIELRSQLFGFFELDGTVHDAEFGLNLYKSVTEEFQREYPDFIGAKIILSGLRFKSQEEILNEVKIAMDLHKKYPDFFLGYDLVGQEDPNFSLLHYLDALLYPSIQNPPYRLPYFFHAAETNWQETEVDYNLADALLLNTTRVGHGFALIKHPRFTELAKENGVAVEVNPISNQILGLVRDVRNHALVPLIADDYPIVISSDDPGAWEASPLSHDFYVALMDLCGRDTALTFLKQLALNSIRYSAMSDTEKVAAKAKWTTQWDKFVKTSVEGLKPHINDRS", "text": "FUNCTION: Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. May play a role in the regulation of cell proliferation. SUBCELLULAR LOCATION: Secreted. Note=Dense core vesicles (DCV). SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. ADGF subfamily."}
{"protein": "MASQSEPGYLAAAQSDPGSNSERSTDSPVAGSEDDLVAAAPLLHSPEWSEERFRVDRKKLEAMLQAAAEGKGRSGEDFFQKIMEETNTQIAWPSKLKIGAKSKKDPHIKVSGKKEDVKEAKEMIMSVLDTKSNRVTLKMDVSHTEHSHVIGKGGNNIKKVMEDTGCHIHFPDSNRNNQAEKSNQVSIAGQPAGVESARARIRELLPLVLMFELPIAGILQPVPDPNTPSIQHISQTYSVSVSFKQRSRMYGATVTVRGSQNNTNAVKEGTAMLLEHLAGSLASAIPVSTQLDIAAQHHLFMMGRNGSNVKHIMQRTGAQIHFPDPSNPQKKSTVYLQGTIESVCLARQYLMGCLPLVLMFDMKEDIEVDPQVIAQLMEQLDVFISIKPKPKQPSKSVIVKSVERNALNMYEARKCLLGLESSGVSIATSLSPASCPAGLACPSLDILASAGLGLTGLGLLGPTTLSLNTSATPNSLLNALNTSVSPLQSSSSGTPSPTLWAPPIANTASATGFSTIPHLMLPSTAQATLTNILLSGVPTYGHTAPSPPPGLTPVDVHINSMQTEGKNISASINGHVQPANMKYGPLSTSSLGEKVLSSNHGDPSMQTAGPEQASPKSNSVEGCNDAFVEVGMPRSPSHSGNAGDLKQMLGASKVSCAKRQTVELLQGTKNSHLHGTDRLLSDPELSATESPLADKKAPGSERAAERAAAAQQKSERARLASQPTYVHMQAFDYEQKKLLATKAMLKKPVVTEVRTPTNTWSGLGFSKSMPAETIKELRRANHVSYKPTMTTAYEGSSLSLSRSSSREHLASGSESDNWRDRNGIGPMGHSEFSAPIGSPKRKQNKSREHYLSSSNYMDCISSLTGSNGCNLNSCFKGSDLPELFSKLGLGKYTDVFQQQEIDLQTFLTLTDQDLKELGITTFGARRKMLLAISELSKNRRKLFEPPNASCTSFLEGGASGRLPRQYHSDIASVSGRW", "text": "FUNCTION: Putative RNA-binding protein. May be involved in regulating gene expression during embryonic development. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the BicC family."}
{"protein": "MGKTKLKPVEDVNSEVVDEVEKAEEVEEQRNDREQEEEQKEEEAPKSFEELGLDSRLIRALTKKGIEKPTLIQQSAIPYILEGKDVVARAKTGSGKTLAYLLPLLQKLFSADSVSKKKLAPSAFILVPSRELCQQVYTEVSSLIELCRVQLKAVQLTSSMSASDMRNALAGLPEILVSTPACIPKCFAAGVLEPTAVSESLSILVLDEADLLLSYGYEDNLRSVTSIIPRRCQCLLMSATTSSDVEKLKKLILHNPIVLTLTEDNDKEEAVPSNVQQFWISCSAQDKLLHILALLKLEVVQKKILIFINTIDMGFRLKLFLEKFGIKSAILNGELPQNSRLHILEQFNAGLFDYLIATDDNSQTKKQKEEAKGEANKENKKNNKRSKPKLDAEFGVVRGIDFKKVHTVINFDMPQSVTGYIHRIGRTGRAYSSGSSVSLISPDEMEGFEDIKSFLASDKNKDIDIITPFPLLTENAVESLRYRAEDVAKSVTKIAVRESRAQDLRNEIINSEKLKAHFEANPRDLDLLRHDKPLSKTAPAPHLKDIPEYLVDAKTQEASKMVKLARAAMGNTRRSGGGGGRNNKNKKRSRKGSDPLKTFNPNGSKRGAVGQKDGKDSSSTKKQKTV", "text": "SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9 subfamily."}
{"protein": "MSAQINNIRPEFDREIVDIVDYVMNYEISSKVAYDTAHYCLLDTLGCGLEALEYPACKKLLGPIVPGTVVPNGVRVPGTQFQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRNAVASGKAPLTMKQVLTAMIKAHEIQGCIALENSFNRVGLDHVLLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAKTGEMGYPSALTAPVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAAMTLYEQMQAAGKTAADIEKVTIRTHEACIRIIDKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEKRAIANAITLEFTDGTRFEEVVVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRARLEQMPVNEYLDLYVI", "text": "FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2- methyl-aconitate. It is also able to catalyze the dehydration of citrate and the hydration of cis-aconitate at a lower rate. Due to its broad substrate specificity, it seems to be responsible for the residual aconitase activity of the acnAB-null mutant. SIMILARITY: Belongs to the PrpD family."}
{"protein": "MAEEQKTSKVDVESPAVLAPAKEPTPAPVEVADEKIHNPPPVESKALAVVEKPIEEHTPKKASSGSADRDVILADLEKEKKTSFIKAWEESEKSKAENRAQKKISDVHAWENSKKAAVEAQLRKIEEKLEKKKAQYGEKMKNKVAAIHKLAEEKRAMVEAKKGEELLKAEEMGAKYRATGVVPKATCGCF", "text": "FUNCTION: Exhibits a non sequence-specific DNA-binding activity. SIMILARITY: Belongs to the remorin family."}
{"protein": "MEASLHFPIDASLRAAVAVISAGAFYLLNLVIYRLFLSPLAKFPGPKLAAVTSWYELYYDLVHKGKYLFEIEKMHDKYGPIVRINPFELSIRDSEYYDELYVAGSVRPTDRYEAFVEGIVDFKGSHIATIEHDLHRKRRKPLDPYFSRLGVSRLEPMLGELTEKLIVNRFESFKRTGKVVRLDHAFTAYSGDVINRLCMDDPPDVLVDDPEFSPWWYNMFHNGIATLPLFMGLPWLIHVVRLIPVSILAKLDPGTQTFNKFKMMCDDHLRVAKREKAAQGSKDTSMMDARPTIFRHLLNSDLPPSELTDDLLSKEAQVLIGTGTITTAGSLCFICYHIVVNPAIKKRLQEDLKLIMANYPAKKPTWAELETATYLQAVIKEGLRLSFGTMHRRTRVSPKQPLQFRQWTIPAGVPVGMSAYYAHRDPSVFPRPDEFLPERWLSNVTPEMSRNYVPFSRGSRRCLGMNLAYAEINHVIATLFRPGGPDFKLYETSEKDVKPAHDLIVPLPSLESKGFRVIFR", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities (PubMed:23324037, PubMed:27116000). The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively (PubMed:23324037). Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA (PubMed:23324037). It is expected that ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and ophiobolin B intermediates by the combined action of the cytochrome P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC (Probable). Although oblB catalyzes multistep oxygenations at C5 and C21/C7 in a relatively efficient manner, it is unable to convert ophiobolin F to ophiobolin C and produces instead several unexpected derivatives (PubMed:27116000). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MSGLAASWSLKPLGPHGVTQALCAVLLAVLVTMNVVLGDTLLDIPSQSPPLNQYLHCYRCLLETEELGCLLGSDTCLTPLGSTCVTLHIKNSSGFNVMVSDCRNKEQMVDCSYTRASPVFGFWIFYQCCFLDFCNNPKNRKNTMH", "text": "FUNCTION: May have a role in hematopoietic cell differentiation. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MGVKKEKGRKRFRKRKTFGNQILPLELLIEKNKREIINSAELMEEIYMKIDEKHTQCVTK", "text": "FUNCTION: Regulates the expression of extracellular-protein genes of Bacillus natto. SIMILARITY: To B.subtilis SenS."}
{"protein": "MNGAKRRKVAQDTPRNTKPVAQEKPARAEPKPSSDEESEEESATLEEPSAEETAVDAPKKTFKDLGVNDALCEACEKLNYKYPTPIQEKSIPVALQGRDIIGLAETGSGKTAAFALPVLQALLDKPQPLFGLVLAPTRELATQIGQAFEALGSLISLRCAVIVGGLDMVPQAIALGKKPHIVVATPGRLVDHLEKTKGFSLRTLKYLIMDEADRLLDMDFGPSIDKILKFVPRERRTYLFSATISSKIESLQRASLRDPVKVSISSNKYQTVSTLLQNYLFIPHPQKDVHLIYLINEHAGQSTIVFTRTVWETQRVSILLRTLGFGAIPLHGQLSQSSRLGALNKFRSGTRDILVATDVAARGLDIPSVDVVLNYDLPQDSKTYIHRVGRTARAGKSGVAISLVTQYDLEIYLRIEAALGKKLAEYPTEKEEVMAFQSRVEEAQRIARIEMKSFTEERGKKGSTLKGGRGKKGGKRGRDDMDREEG", "text": "FUNCTION: ATP-dependent rRNA helicase required for pre-ribosomal RNA processing. Involved in the maturation of the 35S-pre-rRNA and to its cleavage to mature 18S rRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily."}
{"protein": "MVLPLILTLVIVAPIFLWMYSWYISAIPKHYVKPGTKLQKKVHSNLRILEQKYHPSWWCPFGTTQTVVRQIFRDCPSLPFTREIVEFDDGGAAGIDWLIPEGADDTTPIVVFLPGITGSTHDSSYVLHPVKEARDKGWKCVVVNPRGLGGVKLRTTRTYNAATPHDFAFIAKMINERYPDAKKLGCGFSMGGMILWNYLAMTGENADLDGGMIVSSPWDPLVASDSIECFIPQLIFNSFIAKNLVDMVRPYRELFKDMVDFDEVCRCNTVRGFDRSFVIPMYGFKSCDDYYRQATLATKVDKIKIPCVTLNSVDDYFSPVECIPTLDIMESDYVCGIITNHGGHTAFMESADPNARGMVEKLLSQWGNMIFHDYS", "text": "SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4 family."}
{"protein": "MAGVKYPGQDPVDLDIYQSSHMVDYQPYRKHKYSRVTPQEQAKLDAQLRDKEFYRPIPNPNPKLTDGYPAFKRPHMTAKDLGLPGFFPSQEHEATREDERKFTSTCHFTYPASHDLHLAQGDPNQVLQSADFPCLVDPKHQPAAEMAKGYLLLPGCPCLHCHIVKVPILNRWGPLMPFYQ", "text": "SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Present in the germ cell lineage at all stages (PubMed:26168773)."}
{"protein": "MTSSVLTPSLKLLAMTNSSSSTLFCIPSIFNISSSESHRFNFSLSSRPVNLTLSLKSKTLRNSSPVVTFVSQTSNWAEEEEGEDGSIGGTSVTVDESFESEDGVGFPEPPEEAKLFVGNLPYDVDSQALAMLFEQAGTVEISEVIYNRDTDQSRGFGFVTMSTVEEAEKAVEKFNSFEVNGRRLTVNRAAPRGSRPERQPRVYDAAFRIYVGNLPWDVDSGRLERLFSEHGKVVDARVVSDRETGRSRGFGFVQMSNENEVNVAIAALDGQNLEGRAIKVNVAEERTRR", "text": "FUNCTION: Required for specific RNA editing events in chloroplasts and stabilizes specific chloroplast mRNAs (PubMed:19297624). SUBCELLULAR LOCATION: Plastid, chloroplast."}
{"protein": "MNSSSHLTLLDLTLNASEDNILGQNVNNKSSACEDMGIAVEVFLTLGLVSLLENILVIGAIVKNKNLHSPMYFFVGSLAVADMLVSMSNAWETITIYLINNKHVVIADTFVRHIDNVFDSMICISVVASMCSLLAIAVDRYITIFYALRYHHIMTARRSGVIIACIWTFCISCGIVFIIYYESKYVIVCLISMFFTMLFFMVSLYIHMFLLARNHVKRIAASPRYNSVRQRASMKGAITLTMLLGIFIVCWSPFFLHLILMISCPQNVYCACFMSYFNMYLILIMCNSVIDPLIYALRSQEMRRTFKEIICCHGFRRTCTLLGRY", "text": "FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. This receptor is a possible mediator of the immunomodulation properties of melanocortins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSTGISSDLHLHPRALNFSKTSKSGLSNRKVSFSSVGYAQNRKLSCSVSSTENVAPKDDDRGKDRPLVKMCGITSARDAAMAVEAGADFIGMIIWPHSKRSISLSVAKDISQVAREGGAKPVGVFVEDDENTILRAADSSDLELVQLHGNSSRAAFSRLVRERKVIYVLNANEDGKLLNVVPEEDGHLADWILVDSATGGRYLDQLLSFFALSHCNVFLRGTSYTITLVHETVCLSQVTEISRV", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TrpF family."}
{"protein": "MSDDEFIDTGLFAEPEGFTPPPPPPHFAKYQRKNKTDPAELNLRLVGKSPLWGHLLWNAGVFTADYLDKHADELVTGKDVLELGAAAGLPSLICGINKCNRVVCTDYPDPDLISNIQHNFDHCQGLDLSKTVVKGFIWGADAKPLMDDSEKEIQNEDKFDLVILSDLVFNHTEHLKLLKTCRDTVKKNGKCLVVFSPHRPKLLENDLEFFRTCEDFQFKAEKIDLVTWKPMFEEDDESIDIRARVYSFFLVPQW", "text": "FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM7 family."}
{"protein": "MADLVQNAANNVLNDGMDTSRHTSSTAAPPSRNEVELNGQPPTAPPPQVVTDSEEDEDEELTLKYGAKHVIMLFIPVTLCMVVVVATIKSVSFYTQKDGQQLIYTPFREDTETVGQRALHSMLNAIIMISVIVVMTLVLVVLYKYRCYKVIQAWLFFSNLLLLFFFSLIYLGEVFKTYNVAMDYFTLALIIWNFGVVGMICIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAAISVYDLLAVLCPKGPLRILVETAQERNEAIFPALIYSSTMVWLFNMADSAETRNNSSHPVPQQENQVVAMAPTAQAEDDGGFTPAWVDHQQHQLGPMQSTEESRRQIQEMPSARPPPPADDDEERGVKLGLGDFIFYSMLVGKASATASGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDNLVRPFMDQLAVHQFYI", "text": "FUNCTION: Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid- beta precursor protein) (PubMed:10521267). Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic granule Cell membrane Cell projection, axon Synapse Cell projection, neuron projection. SIMILARITY: Belongs to the peptidase A22A family."}
{"protein": "MSRQVVRSSKFRHVFGQPAKADQCYEDVRVSQTTWDSGFCAVNPKFVALICEASGGGAFLVLPLGKTGRVDKNAPTVCGHTAPVLDIAWCPHNDNVIASGSEDCTVMVWEIPDGGLMLPLREPVVTLEGHTKRVGIVAWHTTAQNVLLSAGCDNVIMVWDVGTGAAMLTLGPEVHPDTIYSVDWSRDGGLICTSCRDKRVRIIEPRKGTVVAEKDRPHEGTRPVRAVFVSEGKILTTGFSRMSERQVALWDTKHLEEPLSLQELDTSSGVLLPFFDPDTNIVYLCGKGDSSIRYFEITSEAPFLHYLSMFSSKESQRGMGYMPKRGLEVNKCEIARFYKLHERRCEPIAMTVPRKSDLFQEDLYPPTAGPDPALTAEEWLGGRDAGPLLISLKDGYVPPKSRELRVNRGLDTGRRRAAPEASGTPSSDAVSRLEEEMRKLQATVQELQKRLDRLEETVQAK", "text": "FUNCTION: May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cell cortex Cytoplasmic vesicle, phagosome membrane Note=In non-infected macrophages, associated with the cortical microtubule network. In mycobacteria-infected macrophages, becomes progressively relocalized and retained around the mycobacterial phagosomes. Retention on the phagosomal membrane is strictly dependent on mycobacterial viability and not due to impaired acidification (By similarity). SIMILARITY: Belongs to the WD repeat coronin family."}
{"protein": "DLAGEIHGLSNVK", "text": "SUBCELLULAR LOCATION: Cytoplasm, cytosol."}
{"protein": "MASEFKKKAFWRAVIAEFLAMILFVFISIGAALGFNFPIEEKANQTVGRSQDIVKVSLAFGISIATMAQSVGHVSGAHLNPAVTLGCLLSCQISILKAVMYIIAQCLGAVVATAILSGITSGLENNSLGLNGLSPGVSAGQGLGVEILVTFQLVLCVVAVTDRRRHDVSGSVPLAIGLSVALGHLIAIDYTGCGMNPARSFGSAVLTKNFTYHWIFWVGPMIGGAAAAIIYDFILAPRTSDLTDRMKVWTNGQVEEYELDGDDNTRVEMKPK", "text": "FUNCTION: Forms a water-specific channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family."}
{"protein": "MSVEIVPLPLRINENESFLSYDDRLNRVVFKTSSGFGVVLLDDPEANRRYYSSDKPIIDAKFSPDLKYSAIQFSDYDIEILHLENGTRYIQTCKYKSSKATILGYYWTTKENILLVTNASLELYAMGLDGSCKLVKESKIKITNCVYSFNCNFGVLFLHSGGTSIQPYFFRTNSFDKLPKFNIEGNGNGFNIKNLYVTKLHEKFFCVYGDQEYIYLYEMTLETIYKIKPIKILLSGPNSIHFVDNLIIVHSELNISIVYDLKTIQRDRERGQTNKKEPEFPISAIPMTLSTINSNNLLYLMNNATKTHSTTSTPIINSINNNNNNNNNPSSSSSPSSSNNSQSSSPTMISSYEQRQIDQHKEQQLQKPNVTLYSKNWRFICPNYIFDPDSGIWYEVTLNFEKISNFLQFDSHKTIPFLQERTLLSAKFALLSIIKTIIEFKTDTLDGIGKIYDDLNKVLFRTTNRQLTESLHKSINQPNNNNNNNNNNNNNNNNNTAQTLNSTGNLSNSISIGGMNTSTDNLTTTTTTSSSISSSPSNSFIGNSKTNVNNLSYLNYKKQQQQQMEKQQHMPNDDEDSFSLIGDGGSGGSGGSFYNTNTNTTSTTNTTTSPSGKSNSNLKLSQSLNNTPNQSPNSRSSLNNSSNNINNNNNNNNNNNNNNNNNNHVVQNRQSRSNQYILINSHDMYDFVFNPIYEKLLIESQKEKEKENDNNNNNTNNNTNNNNNNNIEELNSNEKLELDSKYLIAVVIQYIKSLSFNHCTGISDKLYNLLISLLIDNNMFSRLHQFLQYYVITDSLSIAYKLLSIGEQYPPVLQLSLDMFKRLSMPNIIIETLLERGQVIQAIRLLRSTKETNEQAYQELLTPTYPIQFLASSSNQSNDTLFFSVFKFFETNNLIIPSHPSFDKYIKLFIEKFTEKSLSPLLLDILSNLNNNSTSGGDITPKKNVGGSFLNQSLNNSSPTLRSSNSLNSSPRLQYSNN", "text": "FUNCTION: May have a role in autophagy. SUBCELLULAR LOCATION: Lysosome membrane Late endosome membrane. SIMILARITY: Belongs to the RMC1 family."}
{"protein": "MKLIIYLTILAGTALVTHSSVQKEDHAPYLAYLKSNFNPCVGVLIKASWVLAPSHCYLPNLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLMLIKLAKPATFNHKVQVLPIATTNVRPGTVCTLSGLDWSQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSSHRNSLCVRFVKVFSRIFGEVAVATVICKNKLQGIEVGHFMGGDVGIYTNIYSYVPWIEKTTKEKMT", "text": "FUNCTION: Plays a role in male fertility (PubMed:23553430). May have a role in sperm migration or binding to zona-intact eggs (PubMed:23553430). Involved in the activation of the proacrosin/acrosin system (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKNKIAAPFKQAEFQILYGEGINFYGELVDLGVKEKLIEKAGAWYSYKGEKIGQGKANATAWLKDNPETAKEIEKKVRELLLSNPNSTPDFSVDDSEGVAETNEDF", "text": "FUNCTION: Mutations in this gene were selected in directed evolution experiments for resistance to intense ionizing radiation (3000 Gy). FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. FUNCTION: Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single- stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in response to DNA damaging agents that is mediated by RecA and LexA (PubMed:22412352). FUNCTION: Plays a role in recovery after DNA ADP-ribosylation. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecA family."}
{"protein": "MELAELEQALRRVPGSRGGWELEQLRPEGRGPTTADTPSWSSLGGPKHQEMSFLEQGESRSWPSRAVTTSSERSHGDQGNKASRWTRQEDVEEGGPPGPREGPQSRPVAESTGQEATFPKATPLAQAAPLAEVDNPPTERDILPSDCAASASDSNTDHLDLGIEFSASAASGDELGLVEEKPAPCPSPEVLLPRLGWDDELQKPGAQVYMHFMQEHTCYDAMATSSKLVIFDTMLEIKKAFFALVANGVRAAPLWDSKKQSFVGMLTITDFILVLHRYYRSPLVQIYEIEEHKIETWREIYLQGCFKPLVSISPNDSLFEAVYALIKNRIHRLPVLDPVSGAVLHILTHKRLLKFLHIFGTLLPRPSFLYRTIQDLGIGTFRDLAVVLETAPILTALDIFVDRRVSALPVVNETGQVVGLYSRFDVIHLAAQQTYNHLDMNVGEALRQRTLCLEGVLSCQPHETLGEVIDRIVREQVHRLVLVDETQHLLGVVSLSDILQALVLSPAGIDALGA", "text": "FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. AMPK also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. The AMPK gamma3 subunit is a non-catalytic subunit with a regulatory role in muscle energy metabolism. It mediates binding to AMP, ADP and ATP, leading to AMPK activation or inhibition: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma subunit family."}
{"protein": "MAEELVLETCDLQCERNGREHRTEEMGSQQLVVRRGQPFTITLNFAGRGYEEGVDKLAFDVETGPCPVETSGTRSHFTLTDCPEEGTWSAVLQQQDGATLCVSLCSPSIARVGRYRLTLEASTGYQGSSFHLGDFVLLFNAWHPEDAVYLKEEDERREYVLSQQGLIYMGSRDYITSTPWNFGQFEDEILAICLEMLDINPKFLRDQNLDCSRRNDPVYIGRVVSAMVNCNDEDHGVLLGRWDNHYEDGMSPMAWIGSVDILKRWRRLGCQPVKYGQCWVFAAVACTVMRCLGVPSRVVTNYNSAHDTNGNLVIDRYLSETGMEERRSTDMIWNFHCWVECWMTRPDLAPGYDGWQALDPTPQEKSEGVYCCGPAPVKAIKEGDLQVQYDIPFVFAEVNADVVYWIVQSDGEKKKSTHSSVVGKNISTKSVGRDSREDITHTYKYPEGSEKEREVFSKAEHEKSSLGEQEEGLHMRIKLSEGANNGSDFDVFAFISNDTDKERECRLRLCARTASYNGEVGPQCGFKDLLNLSLQPHMEQSVPLRILYEQYGPNLTQDNMIKVVALLTEYETGDSVVAIRDVYIQNPEIKIRILGEPMQERKLVAEIRLVNPLAEPLNNCIFVVEGAGLTEGQRIEELEDPVEPQAEAKFRMEFVPRQAGLHKLMVDFESDKLTGVKGYRNVIIAPLPK", "text": "FUNCTION: Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively. Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis. Acts as a protein-glutamine gamma-glutamyltransferase by mediating the cross- linking of proteins: under physiological conditions, the protein cross- linking activity is inhibited by GTP; inhibition is relieved by Ca(2+) in response to various stresses. When secreted, catalyzes cross-linking of proteins of the extracellular matrix, resulting in the formation of scaffolds. Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components. In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively (By similarity). Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases (By similarity). Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3. Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription. Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln- 5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system (By similarity). Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate. May also act as an isopeptidase cleaving the previously formed cross-links. Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Chromosome Secreted, extracellular space, extracellular matrix Cell membrane Mitochondrion Note=Mainly localizes to the cytosol. Present at much lower level in the nucleus and chromatin. Also secreted via a non-classical secretion pathway to the extracellular matrix. SIMILARITY: Belongs to the transglutaminase superfamily. Transglutaminase family."}
{"protein": "MASILRTALLGLLLFTTAQAQFQFFEQMFGGGQQHQESSGQGGNVPSDSAWYQNTYNGAQCSNYLCPGTLACVAVPHHCPCAHPKVEEKFELGEGSAICASKGGFKAGETARKIELARKGLL", "text": "FUNCTION: Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway. SIMILARITY: Belongs to the LCL2 family."}
{"protein": "MTSKKERLDVLLVERGLAETREKAKRAIMAGIVYSNENRLDKPGEKIDRDLPLTVKGNPLRYVSRGGLKLEKALKEFPVSVKDKIMIDIGSSTGGFTDCALQNGAKQSYAVDVGYNQLAWKLRQDERVVVMERTNFRYATPADFTKGMPEFATIDVSFISLRLILPVLRTLLVPGSDCMALVKPQFEAGRESVGKKGIVRDPKVHADVLKRMISFSAAEGYICKGLSFSPITGGDGNIEFLLHLHWPGEGQEGQELPEEEIMRVVEEAHKTLKEKKADVPE", "text": "SIMILARITY: Belongs to the TlyA family."}
{"protein": "MGHKPLYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYVKEERVNYDIFQLTSFDEKLSDRHVDTHSEVLIFEVIPADDFLQQQLQITPQDRVWHVKRVRYRKQKPMALEETWMPLALFPDLTWQVMENSKYHFIEEVKKMVIDRSEQEIIPLMPTEEMSRLLNISQTKPILEKVSRGYLVDGRVFEYSRNAFNTDDYKFTLIAQRKSSR", "text": "FUNCTION: Represses mngA and mngB. Regulates its own expression."}
{"protein": "MTNITLQKQHRTLWHFIPGLALSAVITGVALWGGSIPAVAGAGFSALTLAILLGMVLGNTIYPHIWKSCDGGVLFAKQYLLRLGIILYGFRLTFSQIADVGISGIIIDVLTLSSTFLLACFLGQKVFGLDKHTSWLIGAGSSICGAAAVLATEPVVKAEASKVTVAVATVVIFGTVAIFLYPAIYPLMSQWFSPETFGIYIGSTVHEVAQVVAAGHAISPDAENAAVISKMLRVMMLAPFLILLAARVKQLSGANSGEKSKITIPWFAILFIVVAIFNSFHLLPQSVVNMLVTLDTFLLAMAMAALGLTTHVSALKKAGAKPLLMALVLFAWLIVGGGAINYVIQSVIA", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0324 family."}
{"protein": "MLSFFRRTLGRRSMRKHAEKERLREAQRAATHIPAAGDSKSIITCRVSLLDGTDVSVDLPKKAKGQELFDQIMYHLDLIESDYFGLRFMDSAQVAHWLDGTKSIKKQVKIGSPYCLHLRVKFYSSEPNNLREELTRYLFVLQLKQDILSGKLDCPFDTAVQLAAYNLQAELGDYDLAEHSPELVSEFRFVPIQTEEMELAIFEKWKEYRGQTPAQAETNYLNKAKWLEMYGVDMHVVKARDGNDYSLGLTPTGVLVFEGDTKIGLFFWPKITRLDFKKNKLTLVVVEDDDQGKEQEHTFVFRLDHPKACKHLWKCAVEHHAFFRLRGPVQKSSHRSGFIRLGSRFRYSGKTEYQTTKTNKARRSTSFERRPSKRYSRRTLQMKACATKPEELSVHNNVSTQSNGSQQAWGMRSALPVSPSISSAPVPVEIENLPQSPGTDQHDRKCIPLNIDLLNSPDLLEATIGDVIGASDTMETSQALNDVNVATRLPGLGEPEVEYETLKDTSEKLKQLEMENSPLLSPRSNIDVNINSQEEVVKLTEKCLNNVIESPGLNVMRVPPDFKSNILKAQVEAVHKVTKEDSLLSHKNANVQDAATNSAVLNENNVPLPKESLETLMLITPADSGSVLKEATDELDALLASLTENLIDHTVAPQVSSTSMITPRWIVPQSGAMSNGLAGCEMLLTGKEGHGNKDGISLISPPAPFLVDAVTSSGPILAEEAVLKQKCLLTTEL", "text": "FUNCTION: Plays a role in the formation and organization of tight junctions during the establishment of polarity in epithelial cells. SUBCELLULAR LOCATION: Cytoplasm Cell junction, adherens junction Cell membrane; Peripheral membrane protein Photoreceptor inner segment."}
{"protein": "MAALNGLVLLLLTISAMFISECYSSGESQSIQRKGQCEEVICHRKLNHLGERVTSGCPTGCLCVIREPDNVDNANGTCYALMSSTTTTTTTPDGTTTSEEEE", "text": "FUNCTION: Complement inhibitor (PubMed:27018802). Prevents complement- mediated C5 activation by binding to C5 (PubMed:27018802). Binds C5 at a different binding site than the other tick complement inbibitors OmCI and CirpT1, and the drug eculizumab (PubMed:27018802, PubMed:31871188). Inhibits complement in human and guinea pig but not in other species tested (rabbit, rat, mouse, and pig) (PubMed:27018802). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the RaCI family."}
{"protein": "MVKIIGKGGANYVLAFGNDNDDLYRICVRGRSLRENNRSTVDNYHYALEVVKPQLGEFVCRMELVDLPVCDSLRQVLKSKIEVWDATTVTCLKMPNLVPAGSLSHTVDHFTKIHIGERAIVWEFKPKWLSGNDKYCRNCTLNLLRGQTSISYCHAQLLNPGQAGPILKSLFAGLNVPPAFIEDMEAYIAQPCSVLQRLRVAQEQVDASLGPLDQPDTAASPERCLSMTLKDVSCFVSWHKDASPVAVVVDLDMKPAAKSAHWTALQEQLDRFQPQVRH", "text": "FUNCTION: Has kinase activity and phosphorylates inositol-1,3,4,5,6- pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6- hexakisphosphate (InsP6), also known as phytate. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IPK1 type 1 family."}
{"protein": "MNRIRIHVLPTNRGRITPVPRSQEPLSCSFTHRPCSQPRLEGQEFCLKHILEDKNAPFKQCSYISTKNGKRCPSAAPKPEKKDGVSFCAEHARRNALALHAQMKKSNPGPMGETLLCQLSSYAKTELGSQTPESSRSEASRILDEDSWSDGDQEPITVDQTWRGDPDSEADSIDSDQEDPLKHAGVYTAEEVALIMREKLIRLQSLYIDQFKRLQHLLKEKKRRYLHNRKVEHEALGSSLLTGPEGLLAKERENLKRLKCLRRYRQRYGVEALLHRQLKERRMLATEGAAQQAHTTRSSQRCLAFVDDVRCSNQSLPMTRHCLTHICQDTNQVLFKCCQGSEEVPCNKPVPVSLSEDPCCPLHFQLPPQMYKPEQVLSVPDGLEAGPMDLYLSAAELQPTESLPLELSDDLDVVGDGMPCPPSPLLFDPSLTLEDHSVTEIAGGPGQIQVAGDGCRSQGPHNVEKTCAPFPQRGLATANGKPEPTSIS", "text": "FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MSDSKEPSVQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGALVLQLLSFTLLAGLLIQVSKFPSSISQEQSKQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKQQEIYQELTQLKAAVGELPEKSKQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSQQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCRPCPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFAWMGLSDLNQEGTWQWVDGSPLSPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA", "text": "FUNCTION: Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. Probably recognizes in a calcium- dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens (By similarity). FUNCTION: On DCs it is a high affinity receptor for ICAM2 and ICAM3 by binding to mannose-like carbohydrates. May act as a DC rolling receptor that mediates transendothelial migration of DC presursors from blood to tissues by binding endothelial ICAM2. Seems to regulate DC-induced T- cell proliferation by binding to ICAM3 on T-cells in the immunological synapse formed between DC and T-cells (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein."}
{"protein": "MEGLEENGGVVQVGELLPCKICGRTFFPVALKKHGPICKKTATKKRKTFDSSRQRAEGTDIPTVKPLKPRPEPPKKPSNWRRKHEEFIATIRAAKGLDQALKEGGKLPPPPPPSYDPDYIQCPYCQRRFNENAADRHINFCKEQAARISNKGKFSTDTKGKPTSRTQYKPPALKKSNSPGTASSGSSRLPQPSGAGKTVVGVPSGKVSSSSSSLGNKLQTLSPSHKGIAAPHAVANVKPRNSTPPSLARNPAPGVLTNKRKTYTESYIYRPDGDSASSLNGGNIKGIEGNSPGNLSKFCHECGTKYPVEWAKFCCECGIRRMIL", "text": "SIMILARITY: Belongs to the ZC2HC1 family."}
{"protein": "MAKIYKDEDISLEPIKNKTIAILGYGSQGRAWALNLRDSGLNVVVGLERQGDSWRRAIDDGFKPMYTKDAVAIADIIVFLVPDMVQKSLWLNSVKDFMKKGADLVFAHGFNIHFKIIEPPKDSDVYMIAPKSPGPIVRRSYEMGGGVPALVAVYQNVSGEALQKALAIAKGIGCARAGVIESTFKEETETDLFGEQVILVGGIMELIKASFETLVEEGYQPEVAYFETVNELKLIVDLIYEKGLTGMLRAVSDTAKYGGITVGKFIIDKSVRDKMKIVLERIRSGEFAREWIKEYERGMPTVFKELSELEGSTIETVGRKLREMMFRGMKQISSH", "text": "FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate. SIMILARITY: Belongs to the ketol-acid reductoisomerase family."}
{"protein": "MPRLEEHCWSCSCSTSVKTKDLSSAGWIVCKTGEMMSIITSVLSHAYGSLHSLQSANLIRRGLVLFIVGVVLALVLNLLQIQRNVTLFPEEVLDTLFSSAWWIPLCCGTAAAVVGLLYPCLDHHLGEPHKFKREWASVMRCIAVFVGINHASAKLDFANNVQLSLTLAALSLGLWWTFDRSRSGFGLGLTTALLATLIAQLLVYNGIYQYTSPDFLYVRSWLPCIFFSGGVTVGNIGRQLAMGSTEKIHND", "text": "FUNCTION: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of scap and degradation of hmgcr. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs). Binds oxysterol, including 25-hydroxycholesterol, regulating interaction with scap and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with scap, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing scap from escorting SREBPs to the Golgi. Sterol deprivation reduces oxysterol-binding, disrupting the interaction between insig1 and scap, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBPs. Also regulates cholesterol synthesis by regulating degradation of hmgcr. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the INSIG family."}
{"protein": "XIGAGATSKLVY", "text": "SIMILARITY: Belongs to the phospholipase A2 family."}
{"protein": "MLGRSLLTWVLAAAVTCAQAQQVPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELLAHKAPVLRTLVNSISNLVNAFVPSGKIMQMVDEKLPGLIGSIPGPFGEEMRGIADVTGIPLGEIISFNIFYELFTMCTSIITEDGKGHLLHGRNMDFGIFLGWNINNNTWVVTEELKPLTVNLDFQRNNKTVFKATSFAGYVGMLTGFKPGLLSLTLNERFSLNGGYLGILEWMFGKKNAQWVGFITRSVLENSTSYEEAKNILTKTKITAPAYFILGGNQSGEGCVITRERKESLDVYELDPKHGRWYVVQTNYDRWKNTLFLDDRRTPAKKCLNHTTQKNLSFATIYDVLSTKPVLNKLTVFTTLIDVTKDQFESHLRDCPDPCIGW", "text": "FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1- phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (By similarity). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (By similarity). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (By similarity). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro- dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (By similarity). Has also an N-acylethanolamine hydrolase activity (By similarity). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (By similarity). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (By similarity). SUBCELLULAR LOCATION: Lysosome Secreted Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. SIMILARITY: Belongs to the acid ceramidase family."}
{"protein": "MAAAAELKLLEKSLGLRPGNKYSAQGERQIPVLQTNNGPSLTGLATIATHLVKQASKEHLLGSTAEEKALVQQWLEYRITQVDGHSSKEDTHTLLKDLNSYLEDKVYLAGYNITLADILLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPDIRQHLSSVVFIKNRLYANSH", "text": "FUNCTION: Positive modulator of ATM response to DNA damage. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes at S phase and following DNA damage."}
{"protein": "MRPRATTICSLFFLLRVLAEPAKNSDFYLPGDYLLGGLFTLHANMKGIVHLDYLQVPMCKEYETKVIGYNLMQAMRFAVEEINNDSSLLPDVLLGYEMVDVCYVSNNVQPVLYFLAQEDDLLPIQENYSNYVSRVVAVIGPDNSDAVMTVANFLSLFLLPQITYSAISDELRDKVRFPALLRTAPSADHHIEAMVQLMLHFRWNWIIVLVSGDTYGRDNGQLLGDRLARGDICIAFQETLPTVQPNQNMTSEERQRLVTIVDKLQQSTARVVVVFSPDLTLYNFFNEVLRQNFTGAVWIASESWAIDPVLHNLTELRHMGTFLGITIQSVPIPGFSEFRVRDPQAGPPPLSRTSQRSTCNQECDSCLNGTLSFNNVLRLSGERVVYSVYSAVYAVAHALHSLLGCDHGTCTKTEVYPWQLLKEIWKVNFTLLDHQISFDPQGDMALHLEIVQWQWDLSQNPFQSVASYYPLQRQLKTIQDISWHTINNTIPVSMCSKRCQSGQKKKPVGIHICCFECIDCLPGTFLNQTEDEYECQACPSNEWSHQSEASCFKRRLAFLEWHEAPTIVVALLAALGFLSTLAILVIFWRHFQTPMVRSAGGPMCFLMLTLLLVAYMVVPVYVGPPKVSTCFCRQALFPLCFTICISCIAVRSFQIVCVFKMASRFPRAYSYWVRYQGPYVSMAFITVLKMVTVVIGMLATGLNPTTRIDPDDPKIMIVSCNPNYRNSLFFNTGLDLLLSVVGFSFAYMGKELPTNYNEAKFITLSMTFYFTSSVSLCTFMSAYNGVLVTIMDLLVTVLNLLAISLGYFGPKCYMILFYPERNTPAYFNSMIQGYTMRRD", "text": "FUNCTION: Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family. TAS1R subfamily."}
{"protein": "MADAQAAAAGKKKYKNKKNSAEKNPNHNPNSSGQVEAQTPSNGHVQHQEEEATEDQEPAQELRGLLKKMHLCNGHGHKEQEARPLGEVVNGHAHGHSNNNHIRCTSGSSNNNNSTHNNNSVDSSNNNRKQRREGGDGGGSDSNSLKPEEKPITATSKTTANIHPTTTTDPKPKVSEDVAVEQGVHVATGSGHSREQERKQPPSDYAEGATPTITAQLQLPEPAISADEIVYKEYEAEHQMHDIMRLIQAELSEPYSIYTYRYFIYNWPKLCFLASHDNQYVGAIVCKLDMHMNVRRGYIAMLAVRKEYRKLKIGTTLVTKAIEAMLADNADEVVLETEMRNQPALRLYENLGFVRDKRLFRYYLNGVDALRLKLWFR", "text": "FUNCTION: Probable catalytic component of a complex displaying alpha (N-terminal) acetyltransferase activity. SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily."}
{"protein": "MSTSKSSKVRIRNFIGRIFSPSDKDKDRDDEMKPSSSAMDISQPYNTVHRVHVGYDGQKFSGLPQPWMDILLRDISLADQKKDPNAVVTALKFYAQSMKENEKTKFMTTNSVFTNSDDDDVDVQLTGQVTEHLRNLQCSNGSATSPSTSVSASSSSARPLTNGNNHLSTASSTDTSLSLSERNNVPSPAPVPYSESAPQLKTFTGETPKLHPRSPFPPQPPVLPQRSKTASAVATTTTNPTTSNGAPPPVPGSKGPPVPPKPSHLKIASSTVSSGCSSPQQYSSARSVGNSLSNGSVVSTTSSDGDVQLSNKENSNDKSVGDKNGNTTTNKTTVEPPPPEEPPVRVRASHREKLSDSEVLNQLREIVNPSNPLGKYEMKKQIGVGASGTVFVANVAGSTDVVAVKRMAFKTQPKKEMLLTEIKVMKQYRHPNLVNYIESYLVDADDLWVVMDYLEGGNLTDVVVKTELDEGQIAAVLQECLKALHFLHRHSIVHRDIKSDNVLLGMNGEVKLTDMGFCAQIQPGSKRDTVVGTPYWMSPEILNKKQYNYKVDIWSLGIMALEMIDGEPPYLRETPLKAIYLIAQNGKPEIKQRDRLSSEFNNFLDKCLVVDPDQRADTTELLAHPFLKKAKPLSSLIPYIRAVREK", "text": "FUNCTION: Serine/threonine-protein kinase, which phosphorylates mlk-1. Involved in the stress response to heavy metals by activating the mlk- 1/mek-1/kgb-1 pathway (PubMed:20008556). In ventral cord commissural motoneurons, required for dorsal axon guidance downstream of unc- 6/netrin repulsion receptor unc-5 and probably of Rho GTPases ced-10 and mig-2. Plays a redundant role with mig-10 in orientating axonal growth of HSN neurons (PubMed:18499456). Plays a redundant role with pak-1 in P neuroblast migration and in distal tip cell (DTC)-mediated guidance of gonad elongation probably downstream of Rho GTPases (PubMed:17050621, PubMed:19023419, PubMed:23390595). In association with pak-2, plays a role in embryogenesis. In association with pak-1, may be involved in spermatogenesis (PubMed:23390595). SUBCELLULAR LOCATION: Perikaryon Cell projection, dendrite Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily."}
{"protein": "MARNAEKAMTALARWRRMKEEEERGPIARRPHDVKDCRNLSDAERFRREIVRDASKKITAIQNPGLGEFKLRDLNDEVNRLIKLKHAWEQRIRELGGTDYRKYAQKELDAIGRETGNSRGYKYFGAAKDLPGVRELFEKSTEGEEQRRHRADLLRNIDAHYFGYLDDEDGRLIPLEKLIEEKNIERINKEFAEKQAQKQQTASDAAPENIYKVEEDDDDDLETQESTVIGEDGRPMTIRHVLLPTQQDIEEMLLEQKKQELMAKYLD", "text": "FUNCTION: Regulates the processing of the mir-60 microRNA (miRNA), which in turn negatively regulates the expression of the transcription factor zip-10 (PubMed:29664006). Does not affect the splicing of zip-10 (PubMed:29664006). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ISY1 family."}
{"protein": "MVHCAGCKRPILDRFLLNVLDRAWHVKCVQCCECKCNLTEKCFSREGKLYCKNDFFRCFGTKCAGCAQGISPSDLVRRARSKVFHLNCFTCMMCNKQLSTGEELYIIDENKFVCKEDYLSNSSVAKENSLHSATTGSDPSLSPDSQDPSQDDAKDSESANVSDKEGGSNENDDQNLGAKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLVDRLEPGELIPNGPFSFYGDYQSEYYGPGGNYDFFPQGPPSSQAQTPVDLPFVPSSGPSGTPLGGLEHPLPGHHPSSEAQRFTDILAHPPGDSPSPEPSLPGPLHSMSAEVFGPSPPFSSLSVNGGASYGNHLSHPPEMNEAAVW", "text": "FUNCTION: Potential transcription factor. May play a role in early mesoderm formation and later in lateral mesoderm differentiation and neurogenesis (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MASGRRAPRTGLLELRAGTGAGAGGERWQRVLVSLAEDALTVSPADGEPGPEPGAVREPEPAQINGAAEPGAAPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQALKKTGKEVVLEVKYMKEVSPYFKNSAGGTSVGWDSPPASPLQRQPSSPGPQTRNLSEAKHVPLKMAYVSRRCTPSDPEHRYLEICSADGQDTIFLRAKDEASARSWAGAIQAQINALLPWVKDELQALLAASSPAGSQDIKQIGWLTEQLPSGGTAPTLALLTEKELLLYGGLPQTREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCHRAAEGVQEVSTACTWNGRPCNLSVHIDKGFTLWAAEPGAARAVLLRQPFEKLQMSSDDGASLLFLDFGGAEGEIQLDLHSCPKTMVFIIHSFLSAKVTRLGLLA", "text": "FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate (By similarity). SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side Cell junction Cytoplasm, cytoskeleton Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. SIMILARITY: Belongs to the syntrophin family."}
{"protein": "MKRWSIITGIVIIFCILTCKGQVENKKVDFRTEKGKFVPLNLVPGDVVEYSCPYSLNNDIRNMNGVEREHFDNKKFCFDYIFVGSKLTFLKEYVRGSYNVVHKEEGNLYTSQFSVPPVVLTHRNFDCFCYMEENNVVVKKVLRIHISNGVLRKIPGCDFNADYKESTAITTFSNMSPRRVKVCDVYPKSGDFISLMCPSDYSIKPDGCFSNVYVKRYPNEEVKEEDRFNLNRKWDASKYNVVSIETVLKMNMITQGDKYSIFSKLPDVKDQVDFTCICQSNDEQDNLMMNVYINNTSYLTNNTRSIGVNKHSFSNSEIFERIEREEISFAFSSYLSITLILLYLFFLNF", "text": "SUBCELLULAR LOCATION: Cell surface Cell membrane; Lipid-anchor, GPI-anchor Note=Present on the surface of merozoite."}
{"protein": "MPQLKVLINGGGIAGNAIAFWLTKLGHDVTVLERFPALRTTGLQLDLRGHGIEVLKRMGLDDAMKAKVIKEDGAQFVDTNGKVVAYFPAVDTSKGGVQAFTSEYEIMRGDICRVFYAATKDRATYKFGTSVESFEDLGDSIKVQLTDHTVDHYDLLIGADGVTSSIRKMMLGPGVPDKFIQFQNLYASYFTIPAPIKPDEKYMANIFIAPGSKLLMTRRDNPERLQVYMGGKAPGARLENARRGDTAEEKLGIEEFMQGCGWRTSEMIDELRKADDFYLERLGMVKLDSWHRGRVALVGEAAWCSSVLTGMGTTSCLVGAYCLAGEIAKHCGRGDQGEAKDDPMMVQKNLANALAGYEEKFMPFMHQVQDGLSAKTGTRTYMPSSQWGVTILNWVIKIIALLRLNMAGDWVIREAVRNWKLPDYPELLKE", "text": "FUNCTION: Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:29773797). The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1 (PubMed:17912413, PubMed:29773797, PubMed:20552126). The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3- methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione (PubMed:29773797). The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite (PubMed:29773797). The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal (PubMed:29773797). In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP) (PubMed:29773797). The putative Diels- Alderase asR5 probably catalyzes the formation of the tropolone- humulene skeleton by linking humulene and the polyketide moiety (PubMed:29773797). Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A (PubMed:29773797). SIMILARITY: Belongs to the aromatic-ring hydroxylase family."}
{"protein": "MNPLIFKEDRPLDLIAVGRLCVDLNANETQRPMEETKTFTKYVGGSPANIAIGASRLGLQTGFIGKVSDDQMGRFITGYLKDNKINTDQIHIDCTGAVTGLAFTEIKSPEDCSILMYRDNVADLNLDPTEVSEDYIKQSKALLISGTALAKSPSREAVFLALEYAHKHDVVVFFDVDYRPYTWQSEAETAVYYNLAAEKSDVIIGTREEFDMMEKLLNYEQSNDQVTAERWFSHYAKIVVIKHGGDGSIAYTRDGQSHRGGIFKTKVLKTFGAGDSYASAFIYGLMQGLEIPQAMRLGGASASIVISKHSCSDAMPTRAEISAFMETAEELV", "text": "FUNCTION: Catalyzes the phosphorylation of 5-dehydro-2-deoxy-D- gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2- deoxy-D-gluconate (DKGP). SIMILARITY: Belongs to the carbohydrate kinase PfkB family."}
{"protein": "MRKQLLLGLGLVSALLVSVQASAQKFEQLAKTPQMGWNSWNTFGCNVDEKMIRAMADAMVTSGMKAAGYEYINIDDCWHGERDKNGFIQADKKHFPSGMKALADYVHAKGLKLGIYSDAGNTTCAGRPGSRGHEYQDALTYASWGIDYVKYDWCDTQDINPKSAYATMRDAIHKAGRPMLFSICEWGDNQPWEWAQDVGHSWRTTGDIYPCWNCEHNHGSWSSFGVLPILDKQAGLRKYAGPGHWNDMDMMEVGNGMTEEEDRAHFSLWAFMASPLIAGNDLRNMSDTTRAILTHKETIAINQDKLGIQAMKWIDEGDLEIYIKPLEKGHYAVLFLNRADDAMDYRFDWSFHYMKDDISKHEIFFDKQAFNWRNIWNGETGSTKEVLNIKVPAHGVVVLRLSPR", "text": "FUNCTION: Hydrolyzes galactomannan found in plant cell wall, by cleaving alpha-1,6-D-galactose side-chains from the mannan backbone. Appears to act in synergy with mannanase (ManA) to elicit hydrolysis of galactomannan. Has greater activity against galactomannans with decreased degree of polymerisation values. To a lesser extent, is also able to degrade other galactosides containing alpha-1,6-linked D- galactose, such as melibiose and stachyose. SIMILARITY: Belongs to the glycosyl hydrolase 27 family."}
{"protein": "MSQVKLKPKKKYGHIDGCVRCGRKRGIVRRYGLHLCRQCFRETARQLGFEKYS", "text": "FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles. SIMILARITY: Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily."}
{"protein": "MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSKRRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVRVEFEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQPLKILTSPEEIEKYVAEIEKEKEENEKKKQKKTS", "text": "FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP- dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin- independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1A family."}
{"protein": "MSNYNNKHHDDGNPFYNEPINTSPTQQQQQQQQNLFPNTNIDYNDYTQNRGQQQQQQPAYQPDLQFQSFSHDVDVNSNTSPNNNNNNNSNNNNSNKIGGNSSNNKFSDNVPLNTNEDGTEKKYSFYEVPYYRFLFNVDTKEVGLRLIRSMLPIKFSFFNLIRENPDLYGPFWVLTSLVFIVAVTSNLNEYFHSSDHKSWEVDIQKIVYSAITIYGYSFVIPLILWGIFKWMNLGLRLLDMLCIYGYTLFIFVPASILCVIPLQLVQWIIVAIASIVSGLFLVTNIFTPLKEDFTKRGLIICAVIGALHIGLALVLKLYFFANSTENFTISDSSSTPTPTPTNTTKLL", "text": "SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane Late endosome membrane Note=Mainly localizes within medial-/trans-Golgi and trans-Golgi network (TGN), while less so within cis-Golgi. SIMILARITY: Belongs to the YIP1 family."}
{"protein": "MSTVTLSSGYEMPVIGLGLWRLEKDELKEVILNAIKIGYRHFDCAAHYKSEADVGEALAEAFKTGLVKREELFITTKIWNSDHGHVVEACKNSLEKLQIDYLDLYLVHYPMPTKHNAIGKTASLLGEDKVLDIDVTISLQQTWEGMEKTVSLGLVRSIGLSNYELFLTRDCLAYSKIKPAVSQFETHPYFQRDSLVKFCMKHGVLPTAHTPLGGAAANKDMFGSVSPLDDPVLNDVAKKYGKSVAQICLRWGIQRKTAVIPKSSKIQRLKENLEVLEFQLSDEDMQLIYSIDRKYRTSLPSKTWGLDVYA", "text": "FUNCTION: Synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. SIMILARITY: Belongs to the aldo/keto reductase family."}
{"protein": "MEVADSLLGNGSDVPPPCELGLENETLVCLEQPRAAKEWQPAVQILLYSLIFLLSVLGNTLVITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFMGTSVSVSTFNLVAISLERYGAICKPLQSRVWQTKSHALKVIATTWCLSFTIMTPYPIYSNLVPFTKTNNQTANMCRFLLPNDVMQQSWHTFLLLILFLIPGIVMMVAYGLISLELYQGIKFDAIQKKSARDRNPSTGSSGRYEDGDGCYLQKARPRRRLELRQLSTPGSGRLNRIRSTSSTANLMAKKRVIRMLMVIVVLFFLCWMPIFSANAWRAYDTASAERRLSGTPISFILLLSYTSSCVNPIIYCFMNKRFRLGFLATFPCCPHPGPPGPRGEVGEEEEGRTTGASLSRYSYSHMSASAPGP", "text": "FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MYNMMETELKPPGPQQTSGGGGGGGGNSTAAAAGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGAGVNQRMDSYAHMNGWSNGSYSMMQDQLGYPQHPGLNAHGAAQMQPMHRYDVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMSQHYQSGPVPGTAINGTLPLSHM", "text": "FUNCTION: Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (By similarity). Binds to the proximal enhancer region of NANOG (By similarity). Critical for early embryogenesis and for embryonic stem cell pluripotency (By similarity). Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). May function as a switch in neuronal development (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MGKNKNYNKNQFKKSKTNNDTTVAQQQQTIEEKPDFKIDGSILEGGGQILRNSVALASLFNKAISIEKIRYNRDQPGLKNQHKAGIDLMSRLFKAHLTGCSVGSCKLYYQPTQKTIQDDGVIEADTKTAGSICLMIQVSLPCLIFAPHSTKMVLGGGTNCDFAPAADYIQNVFLPIATTMGFKCEMSIDKRGFYPKGGGAVTLTTQPLTQPLSPITIVNKGEVNRIVIKSYFTSPRISPLVAERMNNTAKKLIKKDFKKVDVETELIDVSKFSFGDGTFIEIRAYTDQGCIFGATGNGAIGVPAEKVAEDAANSLLKDLQDGGCMDEYLQDQLIIFMALAKGKSQIKTGPISLHTQTSIHITSLMTGAIFTITPLTNNTQSGEETNLITCEGISYFPSDLNNNNNNSNSNTTTTTTTTTISTTTIDNQNSEEK", "text": "FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily."}
{"protein": "MVATAVTSAFFPVTSSPDSSDSKNKKLGSIKSKPSVSSGSLQVKANAQAPPKINGTVASTTPVEGSKNDDGASSPPPRTFINQLPDWSMLLAAITTIFLAAEKQWMMLDWKPRRPDMVIDPFGIGKIVQDGLVFSQNFSIRSYEIGADQTASIETLMNHLQETAINHCRSAGLLGEGFGATPEMCKKNLIWVVTRMQVVVDRYPTWGDVVQVDTWVSASGKNGMRRDWLVSNSETGEILTRATSVWVMMNKLTRRLSKIPEEVRGEIEPFFMNSDPVLAEDSQKLVKLDDSTAEHVCKGLTPKWSDLDVNQHVNNVKYIGWILESAPLPILESHELSALTLEYRRECGRDSVLQSLTTVSDSNTENAVNVGEFNCQHLLRLDDGAEIVRGRTRWRPKHAKSSANMDQITAKRA", "text": "FUNCTION: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for palmitoyl-ACP versus other acyl-ACPs. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the acyl-ACP thioesterase family."}
{"protein": "MFTLKKSLLLLFFLGTINLSLCEQERNAEEERRDDSDKRDVEVEKRFLSTLLNVASNVVPTLICKITKKC", "text": "FUNCTION: Antimicrobial peptide active against a variety of Gram- positive and some Gram-negative bacterial strains. Has antifungal activity against a slime mold isolate. Has hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "AGDASSGFFRAVADGCPITHTSCSAPHRRLTKVSVIGAGNVGMAIAQTILTQNLADEIALVDALPDKLRGEALDLQHAAAFLPRVRIVSGTDAAVTKNSDLIVVTAGARQIPGETRLNLLQRNVALYRKIVPPVAEHSPDALLLVVSNPVDVLTYVAWKLSGFPASRVIGSGTNLDSSRFRFLVAEHLDVSAQDVQAYMVGEHGDSSVAIWSSISVGGMPALKSLRDSHRSFDEAALEGIRRAVVGGAYEVIGLKGYTSWAIGYSVASLATSLLRDQRRVHPVSVLAAGFHGISDGHEVFLSLPARLGRAGVLGVAEMDLTEAEAAQLRRSAKTLWENCQLLGL", "text": "SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family."}
{"protein": "MVYISNGQVLDSRNQSPWRLSFITDFFWGIAEFVVFFFKTLLQQDVKKRRGYGGSSDSRYDDGRGPPGNPPRRMGRISHLRGPSPPPMAGGUGR", "text": "FUNCTION: Required for Ca(2+) flux in immune cells and plays a role in T-cell proliferation and in T-cell and neutrophil migration (By similarity). Involved in endoplasmic reticulum-associated degradation (ERAD) of soluble glycosylated proteins (By similarity). Required for palmitoylation and cell surface expression of CD36 and involved in macrophage uptake of low-density lipoprotein and in foam cell formation (By similarity). Together with ZDHHC6, required for palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1 stability and function. Plays a role in protection of cells from ER stress-induced apoptosis. Protects cells from oxidative stress when overexpressed in cardiomyocytes (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Cell membrane; Single- pass membrane protein Note=Probably mainly localized in the ER. SIMILARITY: Belongs to the selenoprotein K family."}
{"protein": "MTRLSILLLLISLVYSTPYPQTQISKKIGDDATLSCSRNNINDYVVMSAWYKEPNSIILLAAKSDVLYFDNYTKDKISYDSPYDDLVTTITIKSLTAKDAGTYVCAFFMTSTTNDTDKVDYEEYSTELIVNTDSESTIDIILSGSSHSPETSSEKPDYINNFNCSLVFEIATPGPITDNVENHTDTVTYTSDIINTVSTSSRESTTVKTSGPITNKEDHTVTDTVSYTTVSTSSEIVTTKSTANDAHNDNEPSTVSPTTVKNITKSIGKYSTKDYVKVFGIAALIILSAVAIFCITYYICNKRSRKYKTENKV", "text": "FUNCTION: Prevents cell to cell fusion by interacting with and directing the viral OPG040 protein on the host plasma membrane. The OPG185-OPG040 complex associates with components of the entry fusion complex (EFC) presumably to avoid superinfection and syncytium formation. Via its interaction with C3/VCP protein, protects the infected cell and probably also the extracellular enveloped virus from complement attack. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host membrane; Single-pass type I membrane protein Note=Component of extracellular enveloped virus (EEV) but not intracellular mature virus (IMV). Component of the outermost membrane of EEV. SIMILARITY: Belongs to the orthopoxvirus OPG185 family."}
{"protein": "MERRARRPRGRFYAFRRGRWNHLKRLRRRYKFRHRRRQRYRRRAFRKAFHNPRPGTYSVRLPNPQSTMTIRFQGVIFLTEGLILPKNSTAGGYADHMYGARVAKISVNLKEFLLASMNLTYVSKLGGPIAGELIADGSKSEAAENWPNCCVPLDNNVPSATPSAWWRWALMMMQPTDSCRFFNHPKQMTLQDMGRMFGGWHLFRHIETRFQLLATKNEGSFSPVASLLSQGEYLTRRDDVKYSSDHQNRWRKGGQPMTGGIAYATGKMRPDEQQYPAMPPDPPIITSTTAQGTQVRCMNSTQAWWSWDTYMSFATLTALGAQWSFPPGQRSVSRRSFNHHKARGAGDPKGQRWHTLVPLGTETITDSYMGAPASELDTNFFTLYVAQGTNKSQQYKFGTATYALKEPVMKSDSWAVVRVQSVWQLGNRQRPYPWDVNWANSTMYWGTQP", "text": "FUNCTION: Self-assembles to form the virion icosahedral capsid with a T=1 symmetry. This very small capsid (25 nm in diameter) allows the virus to be very stable in the environment and resistant to some disinfectants, including detergents. Essential for the initial attachment to host receptors. After attachment, the virus is endocytosed and traffics to the nucleus. The capsid protein binds and transports the viral genome and Rep across the nuclear envelope (By similarity). SUBCELLULAR LOCATION: Host nucleus Virion. SIMILARITY: Belongs to the gyrovirus capsid protein family."}
{"protein": "MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRFIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC", "text": "FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm Nucleus Mitochondrion outer membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ubiquitin family."}
{"protein": "MANFTPVNGSSANQSVRLVTTAHNHLETVEMVFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLACADLIIGAFSMNLYTLYIIKGYWPLGAVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQFVVGKRTVPDNQCFIQFLSNPAVTFGTAIAAFYLPVVIMTVLYIHISLASRSRVHKHRPEGPKEKKAKTLAFLKSPLMKPSIKKPPPGGASREELRNGKLEEAPPPALPPPPRPVADKDTSNESSSGSATQNTKERPPTELSTTEAATTPALPAPTLQPRTLNPASKWSKIQIVTKQTGSECVTAIEIVPATPAGMRPAANVARKFASIARNQVRKKRQMAARERKVTRTIFAILLAFILTWTPYNVMVLVNTFCQSCIPERVWSIGYWLCYVNSTINPACYALCNATFKKTFRHLLLCQYRNIGTAR", "text": "FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is inhibition of adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM4 sub-subfamily."}
{"protein": "MESTMRSPLPYGNACATCARAKCRCVPRNGGRGRCERCHHLNKECRAPQGRRKIQPKTLSRSVQLERKMDGLMSLLTSFGGRTDLPTPVQRQSEVQGMWRTEVESGTEDEETSASEEEYLRAFRTQRLQFLPLIHIPATTTVGDLKLQSPFLWQCISAVESKNTARQATLCVKIRELAGKRLLVDCDKSLDLLQGVLVYLAWITLHSQPHKSSLCMYSQMAIGLVFELGLNKPAPPDLSMTVSNSNAVGHMPGLEASISTRRTMHERRAVLSCFVLTSIIAQFLGRMGPLQWTSHMKQCLDILAESEESPGDRVLVQLTRTRLLVDQISHGPWSEGLYGLNSAQTLATFHLKALQSQLETIRAEIPIQLADNKPILFHLFDTELSLYEAALVKPLADEDFSSQRLDHLYACLRVVKQFFDLFFTIPPAGYTSLALPYIAQVSHCLVILFRLSTLDYPGWDKSTVKNTADILCIAEQISTRMAQVGDAIGMRSEGAYGDPFSKWGMMMQKLRSEWAIRLPDCSEVVVDRSSAESSCPSIEMGDLDCFVNWSELGWVMEGAGAGGFIQ", "text": "FUNCTION: Transcription factor; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKTELRSCAACGEPISDRFFLEVGGCSWHAHCLRCCMCMCPLDRQQSCFIRERQVYCKADYSKNFGAKCSKCCRGISASDWVRRARELVFHLACFACDQCGRQLSTGEQFALMDDRVLCKAHYLETVEGGTTSSDEGCDGDGYHKSKTKRVRTTFTEEQLQVLQANFQIDSNPDGQDLERIASVTGLSKRVTQVWFQNSRARQKKHIHAGKNKIREPEGSSFARHINLQLTYSFQNNAQNPMHLNGSKAGLYPTHESSMDELSQDSSVHCMPSEV", "text": "FUNCTION: Probable transcription factor. Required for the establishment of a subset of imaginal tissues: the abdominal histoblasts and the salivary gland imaginal rings. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLDLEVVPERSLGNEQWEFTLGMPLAQAVAILQKHCRIIKNVQVLYSEQSPLSHDLILNLTQDGIKLLFDAFNQRLKVIEVYDLTKVKLKYCGVHFNSQAIAPTIEQIDQSFGATHPGVYNSAEQLFHLNFRGLSFSFQLDSWTEAPKYEPNFAHGLASLQIPHGATVKRMYIYSGNSLQDTKAPMMPLSCFLGNVYAESVDVIRDGTGPSGLRLRLLAAGCGPGVLADAKMRVFERAVYFGDSCQDVLSMLGSPHKVFYKSEDKMKIHSPSPHKQVPSKCNDYFFNYFTLGVDILFDANTHKVKKFVLHTNYPGHYNFNIYHRCEFKIPLAIKKENAGGQTEICTTYSKWDSIQELLGHPVEKPVVLHRSSSPNNTNPFGSTFCFGLQRMIFEVMQNNHIASVTLYGPPRPGAHLRTAELP", "text": "FUNCTION: Plays a regulatory role in autophagic activity. In complex with BCAS3, associates with the autophagosome formation site during both non-selective and selective autophagy. SUBCELLULAR LOCATION: Cytoplasm Preautophagosomal structure Note=The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner. SIMILARITY: Belongs to the PHAF1 family."}
{"protein": "MTNAKKVRARRKIRRTAAGAMALAVGLTGAGILVNAVTPDAQVATAQQDEQALIQEGKDLYDVACITCHGANLQGVKDRGPSLIGVGSGATYFQVHSGRMPMLRNEAQAKRKTPRYSEAQTLAIAAYVEANGGGPSIVYNKDGSVAMESLRGANYKDGIDPADVARGSDLFRLNCASCHNFTGRGGALSSGKYAPVLDPANEQEIYQAMLTGPQNMPKFSDRQLSADEKKDIIAYIKSAKETPSQGGWNLGGLGPVTEGMMMWLVGIVVLVAAAMWIGSRS", "text": "FUNCTION: Cytochrome c1 subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MDGATYQRFPKIKIRELKDDYAKFELRETDVSMANALRRVMISEVPTVAIDLVEIEVNSSVLNDEFIAHRLGLIPLTSERAMSMRFSRDCDACDGDGQCEFCSVEFRLSSKCVTDQTLDVTSRDLYSADPTVTPVDFTIDSSVSDSSEHKGIIIVKLRRGQELKLRAIARKGIGKDHAKWSPAATVTFMYEPDIIINEDMMDTLSDEEKIDLIESSPTKVFGMDPVTRQVVVVDPEAYTYDEEVIKKAEAMGKPGLIEISPKDDSFIFTVESTGAVKASQLVLNAIDLLKQKLDAVRLSDDTVEADDQFGELGAHMRGG", "text": "FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. NRPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family."}
{"protein": "MTTEKENVTTAVAVKDGGEKSKEVSDKGVKKRKNVTKALAVNDGGEKSKEVRYRGVRRRPWGRYAAEIRDPVKKKRVWLGSFNTGEEAARAYDSAAIRFRGSKATTNFPLIGYYGISSATPVNNNLSETVSDGNANLPLVGDDGNALASPVNNTLSETARDGTLPSDCHDMLSPGVAEAVAGFFLDLPEVIALKEELDRVCPDQFESIDMGLTIGPQTAVEEPETSSAVDCKLRMEPDLDLNASP", "text": "FUNCTION: Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. Transcription factor that binds to the GCC-box pathogenesis-related promoter element. Acts as a transcriptional inhibitor and may regulate other AtERFs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
{"protein": "MFVRIGFVVAASIAAVTVKRLNVKPSKPSKPSDNGEGGDKEQSVDPDYNLNDKNLQEEEEEEEEEVKLINSVINQTRGSFSDYLDDDILPEFEDLLSGEIEYPLPDDDNNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEELVYLRWVNACLRYELRNYQTPAGKISARDLSKNLSPKSQAKAKRLMLEYAGSERGQGDTDLESNYSQPSSPGSDDFDNASMDSSTSRFSSFSKKPGLIQKLKKWGKSKDDSSVQSSPSRSFYGGSPGRLSSSMNKQRGPLESLMIRNAGESVAITTFGQVDQESPGTPETPNLPRIRTQQQASSPGEGLNSVAASFHVMSKSVDNVLDEKYPAYKDRHKLAVEREKHIKHKADQARAERFGGNVALPPKLAQLKEKRVVVPSVITATGDQSNESNESNEGKASENAATVTKMKLVDIEKRPPRVPRPPPRSAGGGKSTNLPSARPPLPGGGPPPPPPPPGGGPPPPPGGGPPPPPPPPGALGRGAGGGNKVHRAPELVEFYQSLMKRESKKEGAPSLISSGTGNSSAARNNMIGEIENRSTFLLAVKADVETQGDFVQSLATEVRASSFTDIEDLLAFVSWLDEELSFLVDERAVLKHFDWPEGKADALREAAFEYQDLMKLEKQVTSFVDDPNLSCEPALKKMYKLLEKVEQSVYALLRTRDMAISRYKEFGIPVDWLSDTGVVGKIKLSSVQLAKKYMKRVAYELDSVSGSDKDPNREFLLLQGVRFAFRVHQFAGGFDAESMKAFEELRSRAKTESGDNNNNNNNNSNEEESVN", "text": "FUNCTION: Required for the positioning and movement of chloroplasts. Interacts with profilin and actin independent of its polymerization status. Regulates chloroplast localization by anchoring chloroplasts to the plasma membrane and forming a bridge to the actin cytoskeleton. SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MASALCRTASRLRSVQLFRRIRVSSDLLSASSPSPACISDALRHGDFSLPRSFFSLNCGIEMLKMDQRCLLSTSASDTTSKHDSGKPETKSSEKNEKSGGSESSDGGSDHKNERASGKDVRGGPVSWMSFFLLFATGAGLVYYYDTQKKRHIEDINKNSIAVKEGPSAGKAAIGGPFSLIRDDGKRVTEKNLMGKWTILYFGFTHCPDICPDELIKLAAAIDKIKENSGVDVVPVFISVDPERDTVQQVHEYVKEFHPKLIGLTGSPEEIKSVARSYRVYYMKTEEEDSDYLVDHSIVMYLMSPEMNFVKFYGKNHDVDSLTDGVVKEIRQYRK", "text": "FUNCTION: Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. Plays an essential role in embryo development. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SCO1/2 family."}
{"protein": "MSGCGLFLRTTAAARACRGLVVSTANRRLLRTSPPVRAFAKELFLGKIKKKEVFPFPEVSQDELNEINQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLGRTVDLGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKKVSQQILEKRAYICAHPLDRTC", "text": "FUNCTION: As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation (PubMed:20816094, PubMed:24158852, PubMed:32320651). This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs (PubMed:12359260, PubMed:16020546, PubMed:21237683, PubMed:24158852). However, in vivo, it does not seem to play a primary role in fatty acid oxidation (PubMed:20816094, PubMed:24158852). In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein (PubMed:24158852). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=Essentially associated with membranes. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MTNKSSLKNNRKGVASNTLSGAEQANIGSSAMPDTNSTGPFSSVSSLDTPVVRKSTSPTGSQTKSIMNASGTSGAVVSNTPEPGLKRIPTVTFSDPKLGSLRSDVEQTPPNQVARQSSEKKATSVHIAAEGANQGRNLKDINTKVPKDGEASASSFSTPTSILSNADMGNNISSLLAKKLSFTGGTDSILNSDNSSDSPRKEHPHFYVEDPLHTPSVRSRSNSTSPRPSVVVNTFNPINIEREGSISKTGEPTLLESVLEEAMSPNAVSNPLKRENIMTNMDPRLPQDDGKLHVLFGATGSLSVFKLKHMIRKLEEIYGRDKICIQVILTNSATKFFAMKYMRKNKKQHNSIDTSFNSTNSNAGNITGNKKKVASLEKFSIQKTSSNSAASQTNNKQEEEKQMASTTGFPSTLGGSRTYSNSSNVVSQHPQIELPAHIQFWTDQDEWDVWRQRTDPVLHIELRRWADILVVAPLTANTLAKIALGLCDNLLTSVIRAWNPTFPIFLAPSMGSGTFNSIMTKKHFRIIQEEMPWVTVFKPSEKVMGINGDIGLSGMMDANEIVGKIVVKLGGYPDVSAGKEEEEDEDNDEEDDNKKNDTGGKDEDNDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDEDDEDEDEDDEGKKKEDKGGLQRS", "text": "FUNCTION: Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory subunit of protein phosphatase PPZ1, which is involved in many cellular processes such as G1-S transition or salt tolerance. SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys decarboxylase) superfamily."}
{"protein": "MDAPRRSSRLAAKIANVLDSKGTIIPEAAPVMLKKPAKDESVDSTIQVGDVIPDITLPDEDGTSIRLRDITANKGLVIFAYPKASTPGCTKQGCGFRDNYPKIQASDYEVLGLSFDTSKAQKAFKDKQNFPYHLLSDPKGELIKKLGAEKPGGGKLFRSHWIFEKGTGKCIVKEIDISPLVSVDKAFAVITDSEP", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (By similarity). Acts as a scavenger of H(2)O(2) (PubMed:20356456). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily."}
{"protein": "MSGTLSSNNNGIDTKNDNENVSGNVNGNENQTENQNQNQNENENGTGNESSNEPPMKKIKTESGLDDSNPTFDFGITTDSSSQNIENSKSTPSEFTSDSTSAFDSAVKNSDGLSLPKSVAPSTDLKKDAIPTSNSGLALPKKNEKKGKTTGGKNVNKKESGKPGAKGSQSQTDASKMSDVLFSAGVDIREEEALLTSSVAASKTQSQPAAVNIPEHPPFLHPDQVAAFMKKASKEQNFNQNFAKQGEILQMISSSCENYMRDIITNTIVISRHRRKAVKVNSGRRSEVAIALKSIAIQQKKDEERRVKKRIALGLEKEDTENKIDSEETLHRASNATAGLRAGSKKQYGWLTSSTNKPLAATGKGAGNIAAAIAARGDTGLRFREAREEPGIVMRDLLNALENRRIGSHNIITKGYARIRD", "text": "FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF4 family."}
{"protein": "MNSFVSTVLLLSVTIALVSGYPSQLQTTCVTKAKSCTMFFLNGVYCTECTYSGTLELKIGSTCTFSIYEKKVASQPNENSQNEVAQCKQSSCYSNQYVPVDCAAAFGNEYITYIENQ", "text": "FUNCTION: Negatively regulates the egg-laying rate by promoting retention of fertilized eggs. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the UPF0375 family."}
{"protein": "MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATPKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK", "text": "FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division. SUBCELLULAR LOCATION: Nucleus Chromosome Note=The RNA edited version has been localized to nuclear speckles. During mitosis, it appears in the vicinity of condensed chromosomes. SIMILARITY: Belongs to the histone H1/H5 family."}
{"protein": "MGFTAQQEALVGSSYETFKKNLPTNSVLFYTVILEIAPTAKDMFSFLKESGPKHSPQLQAHAEKVFALTRDAATQLVAKGEVTLADASLGAVHVQKAVTDPHFVVVKEALLQTVKEAVGADEWSDDLSTAWEGAYDGLATAIKKAMG", "text": "FUNCTION: Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation (By similarity). SIMILARITY: Belongs to the plant globin family."}
{"protein": "MVKLAKAGKTHGEAKKMAPPPKEVEEDSEDEEMSEDEDDSSGEEEVVIPQKKGKKATTTPAKKVVVSQTKKAAVPTPAKKAAVTPGKKAVATPAKKNITPAKVIPTPGKKGAAQAKALVPTPGKKGAATPAKGAKNGKNAKKEDSDEDEDEEDEDDSDEDEDDEEEDEFEPPIVKGVKPAKAAPAAPASEDEEDDEDEDDEEDDDEEEEDDSEEEVMEITTAKGKKTPAKVVPMKAKSVAEEEDDEEEDEDDEDEDDEEEDDEDDDEEEEEEEPVKAAPGKRKKEMTKQKEAPEAKKQKVEGSEPTTPFNLFIGNLNPNKSVNELKFAISELFAKNDLAVVDVRTGTNRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGRDSKKVRAARTLLAKNLSFNITEDELKEVFEDAMEIRLVSQDGKSKGIAYIEFKSEADAEKNLEEKQGAEIDGRSVSLYYTGEKGQRQERTGKTSTWSGESKTLVLSNLSYSATKETLEEVFEKATFIKVPQNPHGKPKGYAFIEFASFEDAKEALNSCNKMEIEGRTIRLELQGSNSRSQPSKTLFVKGLSEDTTEETLKESFEGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDFKPQGKKTKFE", "text": "FUNCTION: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG- 3' repeats more tightly than the telomeric single-stranded DNA 5'- TTAGGG-3' repeats (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs."}
{"protein": "MHLTGPTLLSLLAALLVSLGLLLWYPTKTRTKDKLLKDLNTLKINTVNLLNQVLKTDTTKLVDFHIANVHCDGIIDRLLSPDELAQLYHKDYPLYKRLVGCGYTKTVGLLHGFALWASETKTRDVSSLKYFIDCISTLDWKEPNLFAGFHTTESKVKKCIV", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the IIV-6 203L/325L family."}
{"protein": "MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA", "text": "FUNCTION: Along with MDM2, contributes to TP53 regulation (PubMed:32300648). Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MDM2/MDM4 family."}
{"protein": "MGDYVTPGEEPPQPGIYRSEQMCLAQLYLQSDASYQCVAELGELGLVQFRDLNPDVSSFQRKYVNEVRRCDEMERKLRYLEREIKKDQIPMLDTGENPDAPLPREMIDLEATFEKLENELREVNKNEETLKKNFSELTELKHILRKTQTFFEEVDHDRWRILEGGSGRRGRSTEREETRPLIDIGDMDDDSAARMSAQAAMLRLGFVAGVIQRERLPAFERLLWRACRGNVFLRTSEIDDVLNDTVTGDPVNKCVFIIFFQGDHLKTKVKKICEGFRATLYPCPDTPQERREMSIGVMTRIEDLKTVLGQTQDHRHRVLVAASKNVRMWLTKVRKIKSIYHTLNLFNIDVTQKCLIAEVWCPIAELDRIKMALKRGTDESGSQVPSILNRMETNEAPPTYNKTNKFTKGFQNIVDAYGIATYREINPAPYTMISFPFLFAVMFGDMGHGAIMLLAALFFILKEKQLEAARIKDEIFQTFFGGRYVIFLMGAFSIYTGFMYNDVFSKSINTFGSSWQNTIPESVIDYYLDDEKRSESQLILPPETAFDGNPYPIGVDPVWNLAEGNKLSFLNSMKMKMSVLFGIAQMTFGVLLSYQNFIYFKSDLDIKYMFIPQMIFLSSIFIYLCIQILSKWLFFGAVGGTVLGYKYPGSNCAPSLLIGLINMFMMKSRNAGFVDDSGETYPQCYLSTWYPGQATIEIILVVLALVQVPIMLFAKPYFLYRRDKQQSRYSTLTAESNQHQSVRADINQDDAEVVHAPEQTPKPSGHGHGHGDGPLEMGDVMVYQAIHTIEFVLGCVSHTASYLRLWALSLAHAQLSDVLWTMVFRNAFVLDGYTGAIATYILFFIFGSLSVFILVLMEGLSAFLHALRLHWVEFQSKFYGGLGYEFAPFSFEKILAEEREAEENL", "text": "FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Required for assembly and activity of the vacuolar ATPase (By similarity). Regulates the size of gut granules during embryonic development (PubMed:20148972). In neurons, required for necrotic cell death by promoting intracellular acidification (PubMed:16005300). Required for cell death induced by hypoxia (PubMed:16005300). Required for acidification of synaptic vesicles and the release of neurotransmitters from adult neurons (PubMed:22426883). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family."}
{"protein": "MFKIKKKKLFIPIIILVLTAFLALIGYISIIFLGHYVIDEKKLILHASSKIVDQNGDEVASLYTENREPVSINEIPKQVREAFIAVEDKRFYEHHGIDAKSVGRAVYRDILAGGKVEGGSTITQQLAKNIFLTHDKTFLRKTKEVIIAINLERDYSKDKLLEMYLNQLYFGHGVYGIQAASHYYFNKEVKDLTVSEGAVLAAIPKAPSTYSPILHPDKNKERRDTILGMMNDQGYISAKEAVTAQGRTLGLHVKKQSETPWFDSYIDLVIKEAEDKYSISGEQLLQGGYTIKVPLDSKLQKTAYQVMKEGSYYPGTDQNAEGSAVFINNKTGGVEAAIGGRDYTSKGYNRVTAVRQPGSTFKPLAVYGPAMQEKKFKPYSLLKDELQSYGDYTPKNYDSRYEGEVTMSDAITYSKNAPAVWTLNEIGVETGKSYLKANGIDIPDEGLALALGGLEKGVSPLQLAGAFHTFAANGTYTEPFFISSIIDEDGETIADHKEEGKRVFSKQTSWNMTRMLQQVVKKGTATSGTYHGDLAGKTGSTSYTGVSGATKDAWFAGYTPKITGAVWMGYDKTDQNHYLKAGSSYPTRLFKDILTQAGETGHVFTKPKNVKELESPIELKPVKTLTADYTFKAAGLFTIELKWDAQEDDRAVYRIYVNKDGEETLLDSVEGKGSYEIPYANLFSGASYKIVPYNTQTKREGEGTDYVQPKLFSS", "text": "FUNCTION: Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family."}
{"protein": "MNNTYYITTPIYYVNDIPHIGHAYTSVASDVIARFMRLRGFDVMFLTGTDEHGQKVEKAAINKNIDPQKFTDQTSESFRHLMTAMHISNDDFIRTTEHRHKKAVAVFWQKLLDNGTIYEGFYEGWYAVRDEAFFDESELTRDGLAPTGAPVEWVKEPSYFFNLSKWQDKLLEFYEANPDFIRPISRRNEVISFVKSGLKDLSVSRTTFNWGIKVPNNEKHVIYVWLDALANYISALGYLDEQSNYNKFWPADLHVVGKDILRFHAVYWPAFLMAAEVPLPKTIMAHGWWTNEGQKISKSLGNTIDPIKLIDEFGVDQVRYFLMREVTFGADGNFARSNLITRINSELSNKIGNLLQRTTSFVYKNNDAKVPLLTQGVIDKIYELPILKTASKFVEQNILLMDKTEINKILENIINLAEEANIYIDSEAPWNLKKTDPDKMLEVLYALLEVLRYIAIMLLPFIPSSANKMLDQLGVNKEERLFKHLIRDYTLTAGSNILEPTIIFPKFE", "text": "FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily."}
{"protein": "MVAEGDPGNLVRTIHLLVLSASWGMQCWTTFVAGFVLIRGVPRHTFGLVQSKLFPFYNHIVLCCSFISLAIYAAYHPRELLSPSESVQITLFFVCLLAAALHARWFSPVTTKTMFKMHIIEREHSLGQGVGLSANREAYQRLQEKDPKYKALRQRFMRYHGISSLCNLLCLLCNGANLVYMALLMPTL", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM205 family."}
{"protein": "MAGGSKTRIHASLVSTLLLLLPLASAIHRSDFPASFLFGTATSSYQIEGAYLEGNKSLSNWDVFTHLPGNIKDGSNGDIADDHYHRYEEDVELMNSLGVNAYRFSISWSRILPKGRFGGVNPAGIDFYNKLIDSILLKGIQPFVTLTHYDIPQELEDRYGAWLNAEIQSDFGHFADVCFGAFGDRVKYWTTFNEPNVAVRHGYMLGTYPPSRCSPPFGHCARGGDSHAEPYVAAHNVILSHATAIEIYKRKYQSKQRGMIGMVLYSTWYEPLRDVPEDRLATERALAFETPWFLDPLVYGDYPPEMRQILGGRLPSFSPEDRRKLRYKLDFIGVNHYTTLYARDCMFSDCPQGQETQHALAAVTGESNGLPIGTPTAMPTFYVVPDGIEKMVKYFMRRYNNLPMFITENGYAQGGDSYTDAEDWIDDEDRIEYLEGYLTKLAKVIRDGADVRGYFAWSVVDNFEWLFGYTLRFGLYYIDYRTQERSPKLSALWYKEFLQNLHENQ", "text": "FUNCTION: Hydrolyzes glycosides and monolignol glucosides (PubMed:25219312). Can hydrolyze para-nitrophenyl beta-D- glucopyranoside (pNPGlc) in vitro (PubMed:23811195, PubMed:25219312). Hydrolyzes para-nitrophenyl beta-D-fucopyranoside, para-nitrophenyl beta-D-galactopyranoside and para-nitrophenyl beta-D-xylopyranoside in vitro (PubMed:25219312). Hydrolyzes the monolignol glucosides coniferin and syringin with high catalytic efficiencies (PubMed:25219312). SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MKEYVLLLFLALCSAKPFFSPSHIALKNMMLKDMEDTDDDDDDDDDDDDDDEDNSLFPTREPRSHFFPFDLFPMCPFGCQCYSRVVHCSDLGLTSVPTNIPFDTRMLDLQNNKIKEIKENDFKGLTSLYGLILNNNKLTKIHPKAFLTTKKLRRLYLSHNQLSEIPLNLPKSLAELRIHENKVKKIQKDTFKGMNALHVLEMSANPLDNNGIEPGAFEGVTVFHIRIAEAKLTSVPKGLPPTLLELHLDYNKISTVELEDFKRYKELQRLGLGNNKITDIENGSLANIPRVREIHLENNKLKKIPSGLPELKYLQIIFLHSNSIARVGVNDFCPTVPKMKKSLYSAISLFNNPVKYWEMQPATFRCVLSRMSVQLGNFGM", "text": "FUNCTION: Negatively regulates periodontal ligament (PDL) differentiation and mineralization to ensure that the PDL is not ossified and to maintain homeostasis of the tooth-supporting system. Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of BMP-dependent activation of SMAD proteins (By similarity). Critical regulator of TGF-beta in articular cartilage and plays an essential role in cartilage homeostasis and osteoarthritis (OA) pathogenesis. Negatively regulates chondrogenesis in the articular cartilage by blocking the TGF-beta/receptor interaction on the cell surface and inhibiting the canonical TGF-beta/Smad signal. Binds calcium and plays a role in osteoblast-driven collagen biomineralization activity. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily."}
{"protein": "MWSYVWLPLVALSLFKDSIIMAKAATILLPSQTGFDISRSPVCSAPDPNLNYRPVIGILSHPGDGASGRLSNATDASSIAASYVKLAESGGARVIPLIFNEPEEILFQKLELVNGVILTGGWAKEGLYFEIVKKIFNKVLERNDAGEHFPIYAICLGFELLTMIISQNRDIFEKMDARNSASSLQFVENVNIQGTIFQRFPPELLKKLGTDCLVMQNHRFGISPQSFEGNIALSNFFKIVTTCVDDNGKVYVSTVQSTKYPVTGFQWHPEKNAFEWGSSKIPHSEDAIQVTQHAANHLVSEARKSLNRPESKKVLSNLIYNYKPTYCGYAGIGYDEVYIFTQQRSLL", "text": "FUNCTION: Cleaves the polyglutamate sidechains of folate polyglutamates in the vacuole. Is important for polyglutamyl tail length determination before vacuolar exit. Plays a role on folate stability and intracellular folate content. Has endopeptidase activity against 4- amino-10-methylpteroyl penta-, tetra-, tri- and di-gamma-L-glutamate substrates and is responsible for the production of folic acid, also called pteroylglutamic acid (PteGlu) from teroylpolyglutamates. SUBCELLULAR LOCATION: Vacuole Secreted, extracellular space Secreted, cell wall Note=Extracellular or cell-wall bound. SIMILARITY: Belongs to the peptidase C26 family."}
{"protein": "MLAARRLLGGSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGAQSRGDWYKTKEILLKGPDWILGEVKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREIIRHDPHKLVEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGAWFASFGRERNSGTKLFNISGHVNNPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALIQAQTGLGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEERMQQFAQQHQARQAAF", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I 51 kDa subunit family."}
{"protein": "MMDKLQGWWRSISAREQRLVAVGGSCLLIGFCYWIVWQPIANRIAERERQVLSQQQTLAWLKEKGEEVLAMQGGQGRQIDTSGTLEGVVNRTAFNQKIKIARLQPQGQELQVWIDTVQFDDLLIWLASLADQHGVQVQVIEVARENLAPGLVKVRRLQLSRPQ", "text": "FUNCTION: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits ExeL resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing ExeE protein in the cytoplasm and the rest of the T2SS machinery. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP M family."}
{"protein": "MFAIFTKIKDRVEAFLNEKNIVTDCLNKIEEKTGIKKRYLAYGAAGVTGAFLLLGYGASLICNLIGFVYPAYFSIKAIESPGKEDDTQWLTYWVIYGFFSVGEFFSDIFLHWFPFYYVCKCLFLLWCMAPVSWNGSQVLYRHVVRPFFLKHEAAVDGMVSNISVKAMSAAENVTREVLHTLVRNRTVGPAESEPRSLPSSAHTEPTVD", "text": "FUNCTION: Required correct function and survival of retinal photoreceptors (PubMed:24691551). Required for retinal development (By similarity). In rod photoreceptors, facilitates stability and/or trafficking of guanylate cyclases and is required to maintain endoplasmic reticulum and mitochondrial homeostasis (By similarity). May play a role in clathrin-coated intracellular vesicle trafficking of proteins from the endoplasmic reticulum to the retinal rod plasma membrane (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DP1 family."}
{"protein": "MNTIVKHTVGFIASIVLTILAVFVTLYTSMALNAKITIIFGFAFIQAAVQLLMFMHLTESKDGNLQTFKVLFAIIITLITVIGTYWVMQGGHSSHL", "text": "FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase bacterial subunit 4 family."}
{"protein": "MATTAMRMIISIIFISTYVTHITLCQNITEEFYQSTCSAVSRGYLSALRTGWYTSVVTIELSKIQKNVCNSTDSNVKLIKQELERYNNAVVELQSLMQNEPASSSRAKRGIPELIHYKRNSTKKFYGLMGKKRKRRFLGFLLGIGSAIASGVAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKELLPKVNNHDCKISNIATVIEFQQKNNRLLEIAREFSVNAGITTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSVVKEEVMAYVVQLPIYGVIDTPCWKLHTSPLCTTDNKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPTDVNLCNTDIFNAKYDCKIMTSKTDISSSVITSIGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNRGVDTVSVGNTLYYVNKLEGKALYIKGEPIINYYDPLVFPSDEFDASIAQVNAKINQSLAFIRRSDELLHSVDVGKSTTNVVITTIIIVIVVVILMLIAVGLLFYSKTRSTPIMLGKDQLSGINNLSFSK", "text": "FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. FUNCTION: [Fusion glycoprotein F2]: Major determinant of the species specificity of RSV infection. The trimer of F1-F2 (F protein) also facilitates the attachment and entry into the host cell. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post- fusion hairpin state. During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs at the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also facilitates the attachment and entry into the host cell. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass membrane protein Note=Localized at the host apical membrane. SUBCELLULAR LOCATION: [Fusion glycoprotein F2]: Virion membrane Host cell membrane Note=Localized at the host apical membrane. SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family."}
{"protein": "MDDAGGLGGSGGFRPGVDSLDEPPNSRIFLVISKHTSELVLRERFSPFGDIQDIWVVRDKHTKESKGVAFVKFARSSQACRAMEEMHGQCLGPSDTKPIKVFIAQSRSSGSHRDVEDEELTRIFVMIPKSYTEEDLREKFKVYGDIEYCSIIKNKVTGESKGLGYVRYLKPSQAAQAIENCDRSFRALLAEPKNKVSGSPEQDDYSSGRQEALGQEPRANLFPFVGEQQSEFSTFDKNDSRGQEAVSKRLSVVSRVPFTEEQLFSIFDIVPGLEYCEVPRDPYSNYGHGVVQYFNVASAIYAKYKLHGFQYPPGNRIVVSFLDDGSNMTELIRKMATQMVAAQLASMVWSTTSQQQFLQYGGNAASQAPQIQTDVVLPSCKKKAPPETPVKERLFVVFNPHPLPLDVLEDIFCRFGNLIEVYLVSGKNVGYVKYADRKSANEAITTLHGKILNGVRLKVMLADSPREESKKRQRTY", "text": "FUNCTION: RNA-binding protein with binding specificity for poly(C). May play an important role in neural development (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. May shuttle between cytoplasm and nucleus."}
{"protein": "MPLPWISVIWFAYLIVIFVLIVVASVFIHVYQTPRDRSSFVTFICVFSIAALLATVMLLPVDVALVSSTISSALGQREEWATQEEVDKITYSLTIIYYSLYFLDALLCFVGIPFAYFWHEEYDEVAFEAGDQTACKRFWAATKYTLTFIAVVIALVLVGFFAPMMESQPGHDLGYWRGYLIENQGEHAFTFLLGFVTIIGSCLYAFYTPSGLAMLPALFLRKSSSFATQTLGGSTAMELNFNRERQRQLEGRCGGNSALLSAKDRRELDTLVREERTLIRRQRLIEGRQEEDQSWPVTVYSKLKTILRPFRLLGGFCLFLVGLSTWISLLMTVVDKLINSPCKHHCGYVLSRTNFNPISWIFIQSSRAFPTDYIIFALIVFFFFWGSVVGVVAVGIRFLWIRIFQIRKGHTSPQAMLLATAVLTLITLGLNYSIVMMLVPGYATFGPQTFCDLAPTSSEEQSDCSNHRHLVKPCSEKADSTAADKTCTPSVASTILNRVALNFPLFGALLLWAHFLFLAGGGRRRGRGRESVSKHQKKRQSYMRGCPIASREPATSNYERLFKEGFFIFKRR", "text": "FUNCTION: Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily."}
{"protein": "MLCPWKCQNAQRGLWNVFKLWVWIMLCCDFFAHHGTDCWTYHYSKRPMPWEKARAFCRENYTDLVAIQNKGEIEYLNKTLPFSRTYYWIGIRKVEGVWTWVGTNKSLTEEAKNWGAGEPNNRKSKEDCVEIYIKRNKDSGKWNDDACHKAKTALCYTASCKPWSCSGHGQCVEVINNYTCNCDLGYYGPECQFVTQCVPLEAPKLGTMACTHPLGNFSFMSQCAFNCSKGTDMIGVEETTCAPFGNWSSPEPTCRVIQCEPLTEPDLGTMDCNHPLVDFGFSSTCTFSCSEEAELTGEKKTICGLSGNWSSPSPRCQKINRTISINEESDYNPLFIPVAVMVTAFSGLAFIIWLARRLKRKSKKVSEKHG", "text": "FUNCTION: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the selectin/LECAM family."}
{"protein": "MVSFSSLLLAVSAVSGALAAPGDSTLVELAKRAITSSETGTNNGYYYSFWTNGGGDVEYTNGNGGQYSVKWTNCDNFVAGKGWNPGSAKTVTYSGEWESNSNSYVSLYGWTQNPLVEYYIVDKYGDYDPSTGATELGTVESDGGTYKIYKTTRENAPSIEGTSTFNQYWSVRQSGRVGGTITAQNHFDAWANVGLQLGTHNYMILATEGYKSSGSATITVE", "text": "FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MASPKSPTRPTQQNPQPNFHDFLPTMAGNLGGEGLIGELCNGFELLMDREKGVITFESLRRNAAAVLGLGDLTDEDVRCMIKEGDFDCDGALNQMEFCVLMFRLSPDLMEASRCLVTEVIEEEFGFTRRH", "text": "FUNCTION: Potential calcium sensor that binds calcium in vitro."}
{"protein": "MKRIPIKELIVEHPGKVLILDGGQGTELENRGININSPVWSAAPFTSESFWEPSSQERKVVEEMYRDFMIAGANILMTITYQANFQSISENTSIKTLAAYKRFLDKIVSFTREFIGEERYLIGSIGPWAAHVSCEYTGDYGPHPENIDYYGFFKPQLENFNQNRDIDLIGFETIPNFHELKAILSWDEDIISKPFYIGLSVDDNSLLRDGTTLEEISVHIKGLGNKINKNLLLMGVNCVSFNQSALILKMLHEHLPGMPLLVYPNSGEIYNPKEKTWHRPTNKLDDWETTVKKFVDNGARIIGGCCRTSPKDIAEIASAVDKYS", "text": "FUNCTION: Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Also converts S-methylmethionine (SMM) to methionine. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGRWAWVPSPWPPPGLGPFLLLLLLLLLLPRGFQPQPGGNRTESPEPNATATPAIPTILVTSVTSETPATSAPEAEGPQSGGLPPPPRAVPSSSSPQAQALTEDGRPCRFPFRYGGRMLHACTSEGSAHRKWCATTHNYDRDRAWGYCVEATPPPGGPAALDPCASGPCLNGGSCSNTQDPQSYHCSCPRAFTGKDCGTEKCFDETRYEYLEGGDRWARVRQGHVEQCECFGGRTWCEGTRHTACLSSPCLNGGTCHLIVATGTTVCACPPGFAGRLCNIEPDERCFLGNGTGYRGVASTSASGLSCLAWNSDLLYQELHVDSVGAAALLGLGPHAYCRNPDNDERPWCYVVKDSALSWEYCRLEACESLTRVQLSPDLLATLPEPASPGRQACGRRHKKRTFLRPRIIGGSSSLPGSHPWLAAIYIGDSFCAGSLVHTCWVVSAAHCFSHSPPRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPYTLYSVFNPSDHDLVLIRLKKKGDRCATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVADHKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWINDRIRPPRRLVAPS", "text": "FUNCTION: Activates hepatocyte growth factor (HGF) by converting it from a single chain to a heterodimeric form. SUBCELLULAR LOCATION: Secreted. Note=Secreted as an inactive single- chain precursor and is then activated to a heterodimeric form. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MNVSFSTPVQNSTASRLALIQQAAARSGALPPAGQYRGSKLSPFDVSQMSGVSISMVERAKINGPEFVEELEWLRQQTTSRCFLDAEMWTNEILAHLPDKWCAPNTLNLYNQVSELVLDNTRSPMASPASNSLYAPGEDQMPTVKRNHTSRFAQSLIKNKEFRRAAFFLEKTMNGNKLDHFLHFRCLFLAYYQEHLENDAEGIERKTSFAEERSPFSLLYQRMEDKKLRENEDVWFEYLMGLLEVELGLKDLAEKSFRNVVIREPRIWPAWEALSRLIADIEDADKFVTSAEVKSLWMGDWFMTLVLQRFHQHSMAIQKAEQLVTRGMTGLPMIITKIAACSNARHDHDQAISNFEDVRKADPYRLGDLHLLSDSLYIRNDQKKLSTLAIEVYKVHKFRWETCCIVANYHAIRRDSEHAIKFFQRALRLNPGLAALWVLIGHEFMEMKNNAAACVSYRRAIEIDPADHRGWYGLGQMYDIMKMPAYALFYYQEAQKCKPHDSRLLVALGDIYSKLNRIEDAEKCFTGAYLFGDVEGNALWSLAKLHERYSDDNKAAQAFEVFLVVYELVTSAEEKIIYAIAFLANHFFKIEDFDKASEYATKCLAFETLCQEGNRLFREIAKIQARESRLPVEEAPGPSNASAAGGQEAMDTEEAPQEGGEEEMSEGEDDFSF", "text": "FUNCTION: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:11861581, PubMed:15238519). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (PubMed:11861581). Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells (PubMed:11134076, PubMed:11861581, PubMed:15238519). Required for embryonic anterior-posterior axis formation (PubMed:11832245). Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion (PubMed:15556870). Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons (PubMed:24321454). SIMILARITY: Belongs to the APC8/CDC23 family."}
{"protein": "MEFPDHSRHLLQCLSEQRHQGFLCDCTVLVGDAQFRAHRAVLASCSMYFHLFYKDQLDKRDIVHLNSDIVTAPAFALLLEFMYEGKLQFKDLPIEDVLAAASYLHMYDIVKVCKKKLKEKATTEADSTKKEEDASSCSDKVESLSDGSSHMAGDLPSDEDEGEDEKLNILPSKRDLAAEPGNMWMRLPSDSAGIPQAGGEAEPHATAAGKTVASPCSSTESLSQRSVTSVRDSADVDCVLDLSVKSSLSGVENLNSSYFSSQDVLRSNLVQVKVEKEASCDESDVGTNDYDMEHSTVKESVSTNNRVQYEPAHLAPLREDSVLRELEREDKASDDEMMTPESERVQVEGGMESSLLPYVSNILSPAGQIFMCPLCNKVFPSPHILQIHLSTHFREQDGLRSKPAADVNVPTCSLCGKTFSCMYTLKRHERTHSGEKPYTCTQCGKSFQYSHNLSRHAVVHTREKPHACKWCERRFTQSGDLYRHIRKFHCELVNSLSVKSEALSLPAVRDWTLEDSSQELWK", "text": "FUNCTION: Transcriptional repressor that plays a role in various developmental processes such as myogenesis and brain development. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes. Plays a key role in myogenesis by directly repressing the expression of ID2 and ID3, 2 inhibitors of skeletal myogenesis. Also involved in controlling cell division of progenitor cells and regulating the survival of postmitotic cortical neurons. May also play a role in the organization of chromosomes in the nucleus (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Associates with condensed chromatin. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family. ZBTB18 subfamily."}
{"protein": "MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPVRDNSSGTFIVLIRRLDCNFDEKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKDEFTYEKGGHIILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVCAICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVSEHTPLLRPLASASTQSFGALSESRSHQNMTESSDYEEDDNDTDSSDAENEINEHSVVVQLQPNGERDYNIANTV", "text": "FUNCTION: E3 ubiquitin-protein ligase that regulates cell proliferation. Involved in apoptosis regulation. Mediates ER stress- induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA. Also involved in protein trafficking and localization. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Late endosome membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Nucleus inner membrane; Single-pass type I membrane protein Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane."}
{"protein": "MAALLGRRFGMAAAALIALAALGSAASGTASKSSFVKSTVKAHDVVIFSKSYCPYCRRAKAVFKELELKKEPYVVELDQREDGWEIQDALSDMVGRRTVPQVFVHGKHLGGSDDTVEAYESGKLAKLLNIDVKEDL", "text": "FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily."}
{"protein": "MSLPYLFLDSEVTPPISLSLAFIIFMFLVKFILKTHNKNSVPVVPLPPGPSPWPIVGSLPEMWRNRPAHRWIHSLMKKLNTDIACIRLGNVHVIPVTSPEIAREFLKKNDAVFASRPVTMATKTLSSGYLTTVVGPWGDQWRKMRRVLVAEAFNPSRVHWLLGKRNEEADNLVKFLYNQCSANQNGAVVNVRIAAQFYSGSIMRKMIFNRTYFGKGREDGGPGVEEEEHVSALLTLLTYAYAFCVSDYLPWLRVFDIDGHEKKVRKAMNIVKKHQEPIVNERLQEWRDGKRNEPDDLLDVFISLKDANGQPLLSDEEIKAQTTELQLSTVDSPFNIAEWALTEMLNQPEMLKKAEEELDRVVGKKTLVQESHVPHLPYIRACAKEVMRLHPVGPFNLPHVSIADAEVAGYFIPKGSNVILSRLELGRNPRVWEEPLRFNPERHLNIAVDQQVDLEENDLRFVSFSTGRRGCMGVGLGSTIVVMLLARLLQGFSWSLPPDVDKIDFTEDQIYLKKASPLLAQAKPRLPASVYPI", "text": "FUNCTION: Catalyzes with low efficiency E and Z isomers of indole-3- acetaldoxime from tryptophan (Trp). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MELNNKEDSPRHTVPFVRQITEDGKAKLEIYRPTTNPIYIYTQILAAIAVSMGSMVVGFASAYTSPALVSMQNTTITSFKVTEQEASWVGGIMPLAGLAGGIAGGPFIEYLGRKNTILATAVPFIVAWLLIAFANSIWMVLAGRALSGFCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILICFVAGKYVNWSGLAFIGSILPIPFMVLTLLIPETPRWFVTRGREERARKALQWLRGKKADVEPELKGIVKSHCEAERHASQNAIFDLMKRSNLKPLLIALGLMFFQQLSGINAVIFYTVSIFKDAGSTIDENLCTIIVGVVNFGATFFATVLIDRLGRKILLYISEVAMVITLLTLGTFFYYKNSGNDVSNIGWLPLASFVIYVIGFSSGVGPIPWLMLGEILPGKIRGSAASVATGFNWTCTFIVTKTFADIVAAIGNHGAFWFFGVICLIGLFFVIFFVPETQGKSLEEIERKMMGRVRRMSSVANMKPLSFNM", "text": "FUNCTION: High-capacity facilitative transporter for trehalose, required to induce anhydrobiosis. Anhydrobiotic larvae can survive almost complete dehydration. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Trehalose transporter subfamily."}
{"protein": "MLQMIPARPSRALASLSEAYEECRQITARYAKTFYLGTLLMPEAKRQAIWAIYVWCRRTDELVDGPQAAQTNFATLDAWERRLERLFAGEPEDDCDVALVDTLARYPLDIQPFRDMIEGQRMDLLQNRYSTFEDLYTYCYRVAGTVGLMSQPVMGIESTNSRAPWDPTTPPDPTQEALALGIANQLTNILRDVGEDARRGRIYLPQEELAQFNYSEQDLFNGVIDDRWRAFMQFQLDRARDYFEQAERGIRQLSHDARWPVWASLMLYREILDVIEQNNYDVFRKRAYVPTWRKLCSLPVAMLRATVL", "text": "FUNCTION: Involved in the biosynthesis of carotenoids. Catalyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to give prephytoene diphosphate (PPPP) and the subsequent rearrangement of the cyclopropylcarbinyl intermediate to yield 15-cis-phytoene. SIMILARITY: Belongs to the phytoene/squalene synthase family."}
{"protein": "ADFSDDRITECQEAFELFDRSAEGKVFLGQVGDILRALGQNPTNGDVTKVLGNPPKEELATKQVSFSEFLPMLAQIERQTEHGSYEDFVEGLRVFDKENNGKIMGAELRHVLSTLGEKMSEEEVEESLLQGQQDPNGCIHYEEFSKYLLEG", "text": "FUNCTION: In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity."}
{"protein": "MESMLNKLKSTVTKVTADVTSAVMGNPVTREFDVGRHIASGGNGLAWKIFNGTKKSTKQEVAVFVFDKKLIDKYQKFEKDQIIDSLKRGVQQLTRLRHPRLLTVQHPLEESRDCLAFCTEPVFASLANVLGNWENLPSPISPDIKDYKLYDVETKYGLLQVSEGLSFLHSSVKMVHGNITPENIILNKSGAWKIMGFDFCVSSTNPSEQEPKFPCKEWDPNLPSLCLPNPEYLAPEYILSVSCETASDMYSLGTVMYAVFNKGKPIFEVNKQDIYKSFSRQLDQLSRLGSSSLTNIPEEVREHVKLLLNVTPTVRPDADQMTKIPFFDDVGAVTLQYFDTLFQRDNLQKSQFFKGLPKVLPKLPKRVIVQRILPCLTSEFVNPDMVPFVLPNVLLIAEECTKEEYVKLILPELGPVFKQQEPIQILLIFLQKMDLLLTKTPPDEIKNSVLPMVYRALEAPSIQIQELCLNIIPTFANLIDYPSMKNALIPRIKNACLQTSSLAVRVNSLVCLGKILEYLDKWFVLDDILPFLQQIPSKEPAVLMGILGIYKCTFTHKKLGITKEQLAGKVLPHLIPLSIENNLNLNQFNSFISVIKEMLNRLESEHKTKLEQLHIMQEQQKSLDIGNQMNVSEEMKVTNIGNQQIDKVFNNIGADLLTGSESENKEDGLQNKHKRASLTLEEKQKLAKEQEQAQKLKSQQPLKPQVHTPVATVKQTKDLTDTLMDNMSSLTSLSVSTPKSSASSTFTSVPSMGIGMMFSTPTDNTKRNLTNGLNANMGFQTSGFNMPVNTNQNFYSSPSTVGVTKMTLGTPPTLPNFNALSVPPAGAKQTQQRPTDMSALNNLFGPQKPKVSMNQLSQQKPNQWLNQFVPPQGSPTMGSSVMGTQMNVIGQSAFGMQGNPFFNPQNFAQPPTTMTNSSSASNDLKDLFG", "text": "FUNCTION: Component of the AP2-containing clathrin coat that may regulate clathrin-dependent trafficking at plasma membrane, TGN and endosomal system (Probable). A possible serine/threonine-protein kinase toward the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L-lysine has not been confirmed (PubMed:15809293, PubMed:16914521). By regulating the expression of excitatory receptors at synapses, plays an essential role in neuronal function and signaling and in brain development (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle Golgi apparatus, trans-Golgi network membrane Endosome membrane Note=Colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes. SIMILARITY: Belongs to the protein kinase superfamily."}
{"protein": "MMLYISAKKAQVAFILYIVLVLRIISGNNDFCKPSSLNSEISGFIGYKCNFSNEGVHNLKPDMRERRSIFCTIHSYFIYDKIRLIIPKKSSSPEFKILPEKCFQKVYTDYENRVETDISELGLIEYEIEENDTNPNYNERTITISPFSPKDIEFFCFCDNTEKVISSIEGRSAMVHVRVLKYPHNILFTNLTNDLFTYLPKTYNESNFVSNVLEVELNDGELFVLACELINKKCFQEGKEKALYKSNKIIYHKNLTIFKAPFYVTSKDVNTECTCKFKNNNYKIVLKPKYEKKVIHGCNFSSNVSSKHTFTDSLDISLVDDSAHISCNVHLSEPKYNHLVGLNCPGDIIPDCFFQVYQPESEELEPSNIVYLDSQINIGDIEYYEDAEGDDKIKLFGIVGSIPKTTSFTCICKKDKKSAYMTVTIDSAYYGFLAKTFIFLIVAILLYI", "text": "FUNCTION: Gametocyte surface protein required for male fertility. SUBCELLULAR LOCATION: Cell surface Cell membrane; Lipid-anchor, GPI-anchor Note=Present on the surface of male and female gametocytes."}
{"protein": "MKRMLINATQQEELRVALVDGQRLYDLDIEHSGSEQKKSNIYKGKITRIEPSLEAAFVDYGEEKNGFLPLKEISKNYFPENHIETLGFNIKNVLQEGQEVIVQISKEERGTKGAALTTFISLAGSYLVLMPNSPKSGGISRRIEGNDRIALKELLTLLELPEEMSLIIRTAGAGKSIESLRWDLSLRLQHWKTIQIIAKSRTAPFLIHQESNIIVRAFRDYLRQDIGEILIDNPKILDLARKHITFLGRPDFVNKIKLYSGEVPLFSYFQIETQINSAFQRKVRLPSGGSIMVDSTEALTAIDINSSRSTSGTDIASTAFNTNLEAVDEISRQLRLRDLGGLIVIDFIDMSAISHQRAIENRLREIARDDRARIQIGQISRFGLLEMSRQRLSSSLGESSHHICPRCTGTGTIRDNESLSLSILRLIEEEALKENTYEVRAIVPVEIACYLLNEKRDAVHAIEKRQAGGKTIIVPSKKMKTPHYSVSRIRKSESKNYTRYGLSNIRQSKITSFLKKNLLKKKQKEILDVANFNFYDNCYNKIQEAQENILKKNNYNNILLKVLSNNRNFIFKMITWFKNSFFIKNMLITSDIFKKNTLKNTNNIFFKKKYSSLNKKNNNQKKRVILSKLFEANIENIPLKNKKLDTSSANYLYDNIERKKNITKKNDLIQKNIHENSYLKHVLMNRYNVINIINNNYIFYKIFNRTKIFKNQNTNNSFLKFSSVTSPIFIFSSVFSLELALGKVWIKYPIAILDETKKQKKLNRKQILHISSISETNTIVNKNNYSGIKKIKHETYSFKKYVKNNIQNQEVTQSQLIKRTKKRNVFILDKKNFLYKRTCNRKNKIHQSSAPITKISKQSDLNKKEKEFHYNLSMMKSSLRGKNSAGVHSATNFSNSPVSKLK", "text": "FUNCTION: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. SUBCELLULAR LOCATION: Cytoplasm Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily."}
{"protein": "MTIELLDSMGVVDTSNAYIRKAVAAPASDVLGRIANLETRLARSAAEIDAAQAVRYRVFVEEMKAQVAPEAGRRKRDIDSWDAICDHLLVLDTSIEGDAEEQIVGTYRLLRQDVAERTGGFYSASEFAIGELLSRHPGKRFMELGRSCVLPEYRTKRTVELLWQGNWAYALKHGIDAMFGCGSFPGVVPEEHALALSFLHHNVRVRDEWAVSARPELYRTMDLMPPEAINPKKALAALPPLIKGYMRLGAMVGDGAVVDQAFRTTDVLIVLPIGKISGRYLNYYGADAGRFSSPVS", "text": "FUNCTION: Catalyzes the first step in the biosynthesis of ornithine lipids, which are phosphorus-free membrane lipids. Catalyzes the 3- hydroxyacyl-acyl carrier protein-dependent acylation of ornithine to form lyso-ornithine lipid (LOL). SIMILARITY: Belongs to the acetyltransferase family. OlsB subfamily."}
{"protein": "MAGFGAAPDFNEGSKINASKNQQDEGKMFIGGLSWDTSKKDLTEYLSRFGEVLDCTIKTDPVTGRSRGFGFVLFKDAVSVDKVLETNEHKLDGKLIDPKRAKALKGKEPPKKVFVGGLSPETTEEQIKQYFGGFGEIENIELPIDTKTNERRGFCFVTYTGEEPVKKLLESRFHQIGTGKCEIKAAQPKEVYRQQQQKQQRGGRGAVTGRGGTRGRGRGQGWNQGYNNYYDQNYGGYGNNGSYGDQDYNSYSGYDYSGYSYGYNPGYTEYSGQQSTYGKARGGGNHQNNYQPY", "text": "FUNCTION: Acts as a transcriptional regulator. Binds DNA and RNA (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MSLKAISAKDAASLDKDLMEMGGWSLDQLMELAGLSVSQAGMWSIYRLHPPSAGKNVLVVCGPGNNGGDGLVAARHLAQYGYTPSVYYPKEGKNELYQRLKTQLHNLSVPFVPDFTEALKSADFLVDAIFGFSFGGPLREPFPSIISQIESSSVPVLSVDAPSSWDIQSGPPKEGPGSKFMPKALISLTAPKPCVKYYRGRHFVGGRFLTKSIVEKYGLNCPDYPGIDQIVEVGVDAEGRL", "text": "FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the NnrE/AIBP family."}
{"protein": "MMMTMAADYGSSEGHYDTPWEFLARPNSVRFSTADVRLSTSAAGDAKVSPHGSPSLCSSSSFVNQLVQIGNSAVDARRKVPRDESKRRRPSDSEIYMEQNMNRVEAEKRLENRNLGDYLLRSRGEGSAALSLRATKGVVHIKIEWNGEKWVIGEGPLFRSISSAISFYRRHPLPIRGADHLVLKNQLKPV", "text": "FUNCTION: Functions downstream of migratory protein mig-13 and may play a role in the control of Q neuroblast migration during larval development."}
{"protein": "MTTIAAAGLNVATPRVVVRPVARVLGPVRLNYPWKFGSMKRMVVVKATSEGEISEKVEKSIQEAKETCADDPVSGECVAAWDEVEELSAAASHARDKKKAGGSDPLEEYCNDNPETDECRTYDN", "text": "FUNCTION: Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the CP12 family."}
{"protein": "MEPRVGNKFRLGRKIGSGSFGEIYLGTNIHTNEELAIKLENVKTKHPQLLYESKLYRILQGGTGVPNVKWFGVEGDYNVLVMDLLGPSLEDLFNFCSRKLSLKSVLMLADQMINRVEFFHSKSFLHRDLKPDNFLMGLGRRANQVYIIDFGLAKKYRDSTTHQHIPYRENKNLTGTARYASMNTHLGIEQSRRDDLESLGYILMYFLKGSLPWQGLKAGTKKQKYERISEKKVSTSIEALCRGYPSEFASYFHYCRSLRFDDKPDYAYLKRIFRDLFIREGFQFDYVFDWTILKYQQSQLTAPPSRALNPAVGTSAALPPGISNIDRYTGEEEGRPHMESSRRRVSGALDNSGNISNQPTSSSARDSMIPSSSLFAQSAGSSRRVTAVSGSRDNFPGSEELLQRSRTGDVSRGVIPRNSPGEAGKSTRRHYESVVKGIDNLQVSDEHHPH", "text": "FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. SUBCELLULAR LOCATION: Cytoplasm Cell junction, plasmodesma Note=Present in punctate particles with granular structure. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily."}
{"protein": "MFGGSFFSSDDDGFSMMSQLRSAFHNNVNQRFDTRYRCYPVAMIPGEERPNVNYGGKVILPPSALEKLSRLNVSYPMLFDFENEAAEKKTHGGVLEFIAEEGRVYLPYWMMTTLSLEPGDLVRVINTDIAQGSYVKLQPQSVNFLDITDHRAVLENALRNFSTLTKSDIFEILYNDQVYQIKVIDVQPDDSRHVVSVVETDLVVDFDPPIGYEESLQKNKQQNIAGVQGTMVTKIGYDELVRQGDSNLMKGTGTKLNGKEVAEVPKINLLDVEKQECPAPLILPLGTYFFGYPYKAPSIEEDSKKDPNLFKFEGAGTSLRASRKTNGTMGKGSSDDPIDIDA", "text": "FUNCTION: Functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway. It is required for vegetative growth (By similarity). SIMILARITY: Belongs to the UFD1 family."}
{"protein": "MQTFRLTSTGRNILRPDELAFQPREEIPYKSFHPDLQIDEPLEILEGDHTQYAGLRDSLVTYKSENSYVLKALLNAKIENVKPVGVQTENINPQEKKFGYKTAKQLDWSPDEYFKFVAIHPYSKTSFPVSYDLDELDTMWLTYYNEFQLSSNSEWENVSKEFLEIVLTIIEREWLYLEAWMPKIEPVRVEDELDGRCVICNEAECENSNAIVFCDNCNTSVHQNCYGIPFVPEGQWFCKKCLLAPHEVICCAFCPDRDGAFCTTLDGRWCHTICAIAIPEISFHDTSRLDLVRNIASIPKSRWKLVCCICKLRWGTCVQCSDKNCYAAYHITCARRAGFFYKIYSHSASYDSVDMETYCDKHTPPDYLNGLMKRLFPLAELYYKRMATDVPLNFQATKAPDFVPEGPWKSHPLPAFIVDKVTKVLLSYNVKRQDLPSIVTDICKFYHMKRRSRKDAPLLKSQLLMDSLENLPVRASKDRVRSLEVAKALQDQYQSLLTLVESTAKRQLLKCQLSNLRKKFLNLNYFPAQRLLQDTLVKIIDLDVDGLFNMPLDNGWIGWVELKRQVFSYQIGSISSLEKKLEPIWDVDGVIQCIDDMEQLTAMVQFAQKTEGEVKKLFIKAKIYFESLSLDERGNLKVPSLGINGLEYDNWPGLNELEMSQLDIPSQGNLKSLHDFIEGLDLNEKIGKFPISMFQNQVAQFSTIEIPKMSGRANGMHNFHSEDVTGQSNHALPNSVTKKNGTKQPYTKNSLPFNERITRSKAKKNYS", "text": "FUNCTION: Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MNDAVITLNGLEKRFPGMDKPAVAPLDCTIHAGYVTGLVGPDGAGKTTLMRMLAGLLKPDSGSATVIGFDPIKNDGALHAVLGYMPQKFGLYEDLTVMENLNLYADLRSVTGEARKQTFARLLEFTSLGPFTGRLAGKLSGGMKQKLGLACTLVGEPKVLLLDEPGVGVDPISRRELWQMVHELAGEGMLILWSTSYLDEAEQCRDVLLMNEGELLYQGEPKALTQTMAGRSFLMTSPHEGNRKLLQRALKLPQVSDGMIQGKSVRLILKKEATPDDIRHADGMPEININETTPRFEDAFIDLLGGAGTSESPLGAILHTVEGTPGETVIEAKELTKKFGDFAATDHVNFAVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGQALVLGMDLKESSGKARQHLGYMAQKFSLYGNLTVEQNLRFFSGVYGLRGRAQNEKISRMSEAFGLKSIASHATDELPLGFKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVEKGVTVMVTTHFMDEAEYCDRIGLVYRGKLIASGTPDDLKAQSANDEQPDPTMEQAFIQLIHDWDKEHSNE", "text": "FUNCTION: Part of the ABC transporter complex YbhFSR that could be involved in efflux of cefoperazone. Probably responsible for energy coupling to the transport system. FUNCTION: Part of the ABC transporter complex YbhFSR that could be involved in efflux of cefoperazone. Probably responsible for energy coupling to the transport system. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI", "text": "FUNCTION: Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:9635433, PubMed:14993212, PubMed:20129055, PubMed:24064211). It is degraded during the mitotic phase of the cell cycle (PubMed:9635433, PubMed:14993212, PubMed:24064211). Its destruction at the metaphase- anaphase transition permits replication in the succeeding cell cycle (PubMed:9635433, PubMed:14993212, PubMed:24064211). Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (PubMed:22615398). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly cytoplasmic but can be relocalized to the nucleus. SIMILARITY: Belongs to the geminin family."}
{"protein": "METLSFEFPAGQPPRGRALVGCVGSGDLEVLIEPGLAGRLTINVQTSVNGAEQRWQHLFARMFDGTTPPAMAIDIHDFGATPGVVRLRLEQGFEEIGHD", "text": "FUNCTION: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MdcC family."}
{"protein": "MNYLFVFLALSAAVTFANAECNKIQCRMFCKFGFQQDENGCDICKCAERPEKKCSNRYCKMLCPEGFQVDANGCQICRCKRSALEAPEKKCDGLKQCKMHCENGFVRDENGCPKCECSKCKQFQCLIFCPHGNEVDENGCKTCKCKAAPEKKKCDDLKQCRMFCENGFVRDENGCKKCECNKCKNFICQIFCEYGNVVDENGCKTCKCNSKPLKLSLHCR", "text": "FUNCTION: This highly disulfide-bonded protein is a potent inhibitor of factor Xa. Facilitates digestion of tissues and may also protect the gastric tissues from its own digestive enzymes. May have therapeutic utility as an anticoagulant. Also exhibits a strong metastatic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family."}
{"protein": "MATPQQPLLTKTHKQNSIISFKILTFVVTLFVALFLVVFLVAPYQFEIKHSNLCKTAQDSQLCLSYVSDLMSNEIVTTDSDGLSILMKFLVNYVHQMNNAIPVVSKMKNQINDIRQEGALTDCLELLDQSVDLVSDSIAAIDKRTHSEHANAQSWLSGVLTNHVTCLDELDSFTKAMINGTNLDELISRAKVALAMLASVTTPNDDVLRPGLGKMPSWVSSRDRKLMESSGKDIGANAVVAKDGTGKYRTLAEAVAAAPDKSKTRYVIYVKRGIYKENVEVSSRKMKLMIVGDGMHATIITGNLNVVDGSTTFHSATLAAVGKGFILQDICIQNTAGPAKHQAVALRVGADKSVINRCRIDAYQDTLYAHSQRQFYRDSYVTGTIDFIFGNAAVVFQKCKLVARKPGKYQQNMVTAQGRTDPNQATGTSIQFCNIIASSDLEPVLKEFPTYLGRPWKKYSRTVVMESYLGGLINPAGWAEWDGDFALKTLYYGEFMNNGPGAGTSKRVKWPGYHCITDPAEAMPFTVAKLIQGGSWLRSTGVAYVDGLYD", "text": "FUNCTION: Pectinesterase may play a role in cell wall metabolism during fruit growth and development prior to ripening and may be required for preparing cell walls for softening by polygalacturonase during fruit ripening. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: In the C-terminal section; belongs to the pectinesterase family. SIMILARITY: In the N-terminal section; belongs to the PMEI family."}
{"protein": "MSTIAGESSSSSKMPENSQPTTTEKGSEYLEQLANEAEELRKKLDQERHKLNDIPIQQAAERLDVMGALGVKQRRILKGHVGKVLCMDWSLDKRHIVSSSQDGKVIVWDGFTTNKEHALTMPTTWVMACAFSPSSQMIACGGLDNKCSVVPLSFEDDIIQKKRQVATHTSYMSCCTFLRSDNLILTGSGDSTCAIWDVESGQLIQNFHGHTGDVFAIDVPKCDTGNTFISAGADKHSLVWDIRSGQCVQSFEGHEADINTVRFHPNGDAFATGSDDATCRLFDLRADRQVCVYEKESILFPVNGVDFSLSGRILFAGYGDYRVGVWDSLKCARHSVLYGHENRISCLRTSPDGTAVCSASWDCTIRIWA", "text": "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Plays a role in regulating dopamine-mediated locomotion behavior (PubMed:15378064). SIMILARITY: Belongs to the WD repeat G protein beta family."}
{"protein": "MYPENYEKFEKIIERLREFKGVIIVEGKRDEDSLRKLGVQTEILRLSRSSLADVALLASEHEEVMILTDFDETGEKLAKRLYDLLVGLTKVDMETRRELQFIASKDAKGIEDLYDLWESLRLRFWAPKEGD", "text": "SIMILARITY: Belongs to the UPF0292 family."}
{"protein": "MASPRTRKVLKEVRAQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLSFVRSVTMDKWKDIELEKMKAGGNAKFREFLETQDDYEPSWSLQDKYSSRAAALFRDKVATLAEGKEWSLESSPAQNWTPPQPKTLQFTAHRASGQPQSAAASGDKAFEDWLNDDLGSYQGAQENRYVGFGNTVPPQKREDDFLNNAMSSLYSGWSSFTTGASKFASAAKEGATKFGSQASQKASELGHSLNENVLKPAQEKVKEGRIFDDVSSGVSQLASKVQGVGSKGWRDVTTFFSGKAEDSSDRPLEGHSYQNSSGDNSQNSNIDQSFWETFGSAEPPKAKSPSSDSWTCADASTGRRSSDSWDVWGSGSASNNKNSNSDGWESWEGASGEGRAKATKKAAPSTADEGWDNQNW", "text": "FUNCTION: GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus Note=Associates with the Golgi complex."}
{"protein": "MDSNELPVLAYKDGENSVAPIPAHEQQLPTVTAEPWLEISKQGLQLEGLCFDRQGNLLLCEVFGGTIFHVNLPDKKVTELFKSHKQNPAAVKIHKDGRLFVCYLGDFESTGGIFMVDADGNDAQDIVSDIGTEYCIDDPVFDSKGGFYFTDFRGYSTNLKGGVYYVSPDFKSITPVIQNLAVANGVALSTDEKTLWVTETNANRLHRIDLLEDGVTIAPFGASIPYYFTGHEGPDSCCIDSDDNLYVAMYGQGKVLVFNKKGSPIGQILMPGRDQGHMLRSTHPAFIPGTDQLIICANDIENDGGSWIYTVKAFAKGHQSYQFH", "text": "FUNCTION: Exhibits lactonase activity. Acts in cells with perturbed membrane integrity and is possibly related to the membrane homeostasis (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SMP-30/CGR1 family."}
{"protein": "MKVKMLSRNPDNYVRETKLDLQRVPRNYDPTLHPFEVPREYVRALNATKLERVFAKPFLASLDGHRDGVNCLAKHPKNLATVLSGACDGEVRIWNLTQRNCIRTIQAHEGFVRGICTRFCGTSFFTVGDDKTVKQWKMDGPGYGDEEEPLHTILGKTVYTGIDHHWKEAVFATCGQQVDIWDEQRTNPVCSMTWGFDSISSVKFNPIETFLLGSCASDRNIVLYDMRQATPLKKVILDMRTNTICWNPMEAFIFTAANEDYNLYTFDMSALDTPVMVHMDHVSAVLDVDYSPTGKEFVSASFDKSIRIFPVDKSRSREVYHTKRMQHVICVKWTSDSKYIMCGSDEMNIRLWKANASEKLGVLTSREKAAKDYNQKLKEKFQHYPHIKRIARHRHLPKSIYSQIQEQRIMKEARRRKEVNRIKHSKPGSVPIVSEKKKHVVAVVK", "text": "FUNCTION: Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre- rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre- ribosomal RNA by the RNA exosome. Participates in the 18S rRNA processing in growing oocytes, being essential for oocyte nonsurrounded nucleolus (NSN) to surrounded nucleolus (SN) transition. FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex that plays a key role in embryo preimplantation and is required for normal meiotic cycle progression in oocytes (By similarity). Acts as a maternal factor that regulates oocyte and zygotic chromatin tightness during maternal to zygotic transition (By similarity). Also involved in the transformation of the endometrium into the decidua, known as decidualization, providing a solid foundation for implantation of blastocysts. Recognizes the histone methyltransferases SUV39H1 and SUV39H2 and directs them to polyubiquitination and proteasomal degradation, which facilitates the H3K9me3 removal and early zygotic gene expression, essential steps for progressive genome reprogramming and the establishment of pluripotency during preimplantation embryonic development. Supports the spindle assembly and chromosome condensation during oocyte meiotic division by targeting the polyubiquitination and degradation of PTEN, a lipid phosphatase that inhibits PI3K pathway as well as oocyte growth and maturation (By similarity). Targets PMP22 for polyubiquitination and proteasomal degradation (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Note=In the nucleolus, localizes predominantly in the granular component, but also detected in the fibrillar center and dense fibrillar component. SIMILARITY: Belongs to the WD repeat DCAF13/WDSOF1 family."}
{"protein": "MEPSPASGGSETTRLVSPRDRSSAGGGLRLKSLFTEPSEPLPEGPKLEGMAFHHCHKNRVSQSGLSPERAQARRQLYAACVVCFIFMAGEVVGGYLAHSLAIMTDAAHLLADIGSMMASLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWIVTGILLYLAFLRLLHSDYHIEAGAMLLTASIAVCANMIMAFVLHQTGAPHSHGPRGAEYAPLEEGHGHPLSLGNTSVRAAFVHVLGDLLQSLGVLAASILIYFKPQYKVADPISTFLFSICALGSTAPTLRDVLLVLMEGAPRSVEFEPVRDTLLSVPGVRATHDLHLWALTLTYHVASAHLAIDSTADPEAILAEASSRLYSRFGFSSCTLQVEKYRSEMAHCLRCREPPKA", "text": "FUNCTION: Probable proton-coupled zinc ion antiporter mediating the import of zinc from cytoplasm into synaptic vesicles and participating to cellular zinc ion homeostasis in the brain. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Synapse, synaptosome Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily."}
{"protein": "MPKRKVTFQGVGDEDGEDEISVPKKKLVDPVAAAGGPGSRFKGKHSLDSDEEDDDEEGSSKYDILASEDVEGQEAATLPSEGGVRITPFNLQEEMEEGHFDADGNYFLNQDAQIRDSWLDNIDWVRIKERPPDKHQVSDSEEEDSLGQTPMSAQALLEGLLELLLPRETVAGALRRLGARGGGKGSNSKGTGRPNSPQRLDRLSGLADQMVARGNLGVYQETRERLAMRLKGLGCRAQGSHDPTPPPSLDMFAEEVAEGELETPTPTQREEAESAGDGLMDVMWEYKWENTGDAELYGPFTSAQMQTWVSEGYFPDGVYCRKLDPPGGQFYNSKRIDFELYT", "text": "FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly nuclear."}
{"protein": "MDAALRDICQLSDPCDPRSFEPPIKDFFCIYPMYRSRYEAKAIQGSNEFLDGWNKAIEKDGLRNDGRPFLGCNTIYGNYVAWAYPECLPERAAHVAAYCDWGFFWDDATDAMSMEKNHEATKDLILTIMSTVGIGQKHEPLLAVNKLVVPFVLNKLAGTDGDLGLNHMKAWKAHLDGQARSSHANMSWEELKQHRLVEGGPEWAIRLGAWGAGIRCTAEEIESVREIIDIGGIAGVLANDYYSFNKEFDEHSRAGTIERMQNGVALLMREYGYSEEEAREILKKEINKMEQQFMDMYLTWLNGPVQKSRGLIQYLTMVLCLYSGTMFWMAHGARYHRTDLITTAEDRATIIGKCQGDAFRVMEGYPPPKGLKRTASSPESAPKRRASKANNINQSNGRGGDPMVAFSGPFVKAPSHICDAPYEYIDSLQSKNMRDKFINILNSWLNVPSDSLQIIKNIVQMLHNSSLMLDDIEDASPLRRGQPATHIFYGASQTINSANFSYVKTVIEATHLKNPQCLQIFLEEVSDLHRGQSLDLHWRHHGRCPTTDEYIMMVDNKTGGLFRLMARLMEAESPSPITTPHLSRLLTLIGRYYQIRDDYMNLTSADYTTKKGYCEDLDEGKFSLPLIHLLLHTSCPDRITSALYNRVPSTGLQDEVKTYILDAMQSARTFEYVREVLSHLHGEIMKTLDEAEKTLGINNGVRMLLVGLGL", "text": "FUNCTION: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of aspergiltriene A, aspergildienes A-D and aspergilols A-D (PubMed:33480256). The bifunctional terpene synthase AuAS converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into sesterterpenes (PubMed:33480256). The C- terminal prenyltransferase (PT) domain of AuAS catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into 5 distinct sesterterpenes: aspergiltriene A, aspergildiene A, aspergildiene B, aspergildiene C and aspergildiene D (PubMed:33480256). The cytochrome P450 monooxygenase AP450 then hydroxylates the aspergildienes A, B, C and D to yield the corresponding sesterterpene alcohols, aspergilols A-D (PubMed:33480256). SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase family. SIMILARITY: In the N-terminal section; belongs to the terpene synthase family."}
{"protein": "MINSFSLFAHITPIIRSSLHSRYSVISSRKAMSSLAAAPYRHVMMPFSPAQDAQVHGNSALTKLTDAIPDLKIYTRSSPHYESLRGVYNKLITAQPLAICRPTSVAQVQAIVKTVSGLGIPLGVRGGGHDVFGRGCIADSVTIDMRELDTQELSQDKKTVKVGGGITSKNLVGFLGSHNLCTSNGFAGEAGWTSWASWGGYGPLGDYVGLGVDNIVGAKIVTASGDVVDAKGDSELLWALRGGGGNFGVIAETDVRVYPMSTIQAGFIVYPWPETADVLLRLQALLDSGVPDKLCLQAGFTKGEWGLGMAITYIWPEAETIGPESEEWLQKLKGLGTCIVDTVAETTFEAFQASISSAISNPVNVTSRHISISKFTSDTLNQLIGACESMPAEADCSITCTILHGKAAQANVLSAFGTRRPHIMLHINAVTEEAAHEHVAIAWADRLVDGVEATGDSIGSTYVSFMESDKDPKGCYGENWERLKAVKKEVDPNDVFRFVHGRIPAA", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin (PubMed:15811992, PubMed:15809006, PubMed:16879655). The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488). The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction (PubMed:21296881). The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin (PubMed:21296881). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "MKIITCFKLVPEEQDIVVTPEYTLNFDNADAKISQFDLNAIEAASQLATDDDEIAALTVGGSLLQNSKVRKDVLSRGPHSLYLVQDAQLEHALPLDTAKALAAAIEKIGFDLLIFGEGSGDLYAQQVGLLVGEILQLPVINAVSAIQRQGNTLVIERTLEDDVEVIELSVPAVLCVTSDINVPRIPSMKAILGAGKKPVNQWQASDIDWSQSAPLAELVGIRVPPQTERKHIIIDNDSPEAIAELAEHLKKALN", "text": "FUNCTION: May play a role in a redox process. SIMILARITY: Belongs to the ETF beta-subunit/FixA family."}
{"protein": "MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAARYVEEARKFGVATVIAGGGDGTINEVSTALIQCEGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGDAIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGSVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLKSDEDNPNIIEGASSWFDIQAPHDITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR", "text": "FUNCTION: Probably phosphorylates lipids; the in vivo substrate is unknown. FUNCTION: In vitro phosphorylates phosphatidylglycerol but not diacylglycerol; the in vivo substrate is unknown. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS lipid kinase subfamily. SIMILARITY: Belongs to the diacylglycerol/lipid kinase family. YegS lipid kinase subfamily."}
{"protein": "MADARDMELIKPYNGDPFTGHLSTPISDSDFTRTFIGNLPAYRKGLSPILRGLEIGMAHGYFLIGPWVKLGPLRDSDVANLGGLISGIALILIATACLAAYGIVSFQKEEAAANPLNTAEGWSQFTAGFFVGATGGAFVAFTLLEKFDVVDGIMTGLFN", "text": "SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaL family."}
{"protein": "MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEATALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS", "text": "FUNCTION: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane (PubMed:12730355). Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:11149946, PubMed:14622179, PubMed:15571673, PubMed:15777781, PubMed:23332758, PubMed:9425306, PubMed:9603192). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (PubMed:25678561). Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (PubMed:26792191). SUBCELLULAR LOCATION: Nucleus inner membrane Nucleus outer membrane Nucleus envelope Cytoplasmic vesicle Endoplasmic reticulum membrane Membrane; Single-pass membrane protein Lipid droplet Cell junction Cell membrane Cell projection, growth cone Postsynaptic density membrane Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:12730355). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (PubMed:20167253). SIMILARITY: Belongs to the ERG2 family."}
{"protein": "MAPALPFALPSLAGKVYLVTGGNTGVGFHTVDELAKHGARVYMGARSPGKAEAAIKTIRAETPTADVHFLQMDLMDLHSVVAAAKSFKEKETKLHGLVNNAGIMATPYALSGDGFEAQWQTNYLSHWVLTWHLLDVLVRTLQAEGGAAGSVRVVDVTSDGHNFAPKVGIDFKDINLEKAGVFARYGQSKVGNILHAKQLNKLYGPSGSETAKKGIWTAAVHPGHLDTNLNKQTAFPKFVNTLLRAVGAYSPPRDGAFNSVFAVASPEFKVADSGEYFVPGQKKKQPSKVARDMELAGRLWKWTEEELRKRELLD", "text": "FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes (PubMed:34468074). The pathway begins with the synthesis of the backbone drimenol by the terpene cyclase drtB using farnesyl pyrophosphate (FPP) as substrate (PubMed:34468074). The cytochrome P450 monooxygenase drtD is then responsible for the hydroxylations at C-6, C-9 and C-12, as well as the oxidation of hydroxyl groups at C-6 and C-11 to a ketone and an aldehyde, respectively (PubMed:34468074). Then, the biosynthesis can go in two directions, either the hydroxylated drimenol is further hydroxylated at C-2 and C-3 by an enzyme(s) not associated with the drt cluster, or the FAD-binding oxidoreductase drtC further oxidizes C-11 or C-12 to form the butyrolactone ring (PubMed:34468074). DrtB, drtD and drtC are solely responsible for the formation of the different drimane structures observed during drimane sesquiterpenes biosynthesis (PubMed:34468074). The polyketide synthase drtA synthesizes different lengths (C6 and C8) of PKS chains, which are then oxidized to varying degrees by the short-chain dehydrogenase drtF (PubMed:34468074). Finally, these PKS chains are transferred onto drimane sesquiterpenes by the acyltransferase drtE, forming the sesquiterpene esters (PubMed:34468074). In addition to the different fatty acyl-CoA chains produced by drtA, drtE is also able to use cinnamoyl-CoA as a substrate (PubMed:34468074). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSASTRNKHSKIHGNEKLDISNDEFDRIRDALKNEEFRKLFFDYVDEIQDPENRKIYEEEITQLEKERGVDVTFIHPQPGFVIKTSIDGELKCFINIASCKVVERPNNEVSVNSQTGQKGLSWSIPLAQIPPRDDLDANNKLCKVYDVVFHPDALHLAKRNAQFRQCLIDTALDGVEREYHVNLDRANLKFPKLDYKGMARPSVLRTLSKNPTAEEKEPHPLEHMYPKKPEADAGQSKVLPMKTKVTAVPKFAVPKYCIKHSHDVDMAEYTDELDAKLQVTVPRALVVEIELPLLSSTADCHLDVTEKSVYLLSEKQGAKYKLKVDLPYTVNDKAGNARFDTDHRCLRITLPVVRSTPREERNLHDTVRNLSREDSGVELNSNGESPVEDEELVVELSEHNQENDSNAFPPTAVVSPRSFLKSNLHYLLPAQFNCNILDNVIVFVLHVTNVQPDSVQTLQQARSLHLQFASMGTGYYPTHYAFLMQLPDGVQPELRIDQVEVDTGDENVVLRLTMNEHCMLLPSYLAGTDSNDLKEYPVFGHQNNNNEKETEVEVAEMEKCDLVSEKSLQINMDHNDVEHALEVTIEPQENEAPLDSLELLHEHQQELQQLHHQKKLNKKQRKRNKKQRSLSESACEDLKLAQEHHEQPMDTLKLPHRKQRSYSECNESSLGSSCVQRGILKRFSRYGPHPSISDSCSSIDDCSSTYSCSVDAAGTGFSQSFGSIPEERGGDEAGLSESCKKTVRFNDHIMKQVFRLDSSILGQRKKNQKRRDCKLRAQQRRLSEGDSADYVEVDSTHGSGDQPAHKTAANAQYFKQHNNNHPHVKDNKKQSLHDSGLDLTNGSINNKNNHSNENATKRNEADAKNTMMFEMDDVDEEAQDAANI", "text": "FUNCTION: Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily."}
{"protein": "MEATDIWGEIERSESYLVCSMYEEAESLSSSILKRIFGNIDVLSDEASQGDHQFHDMLESAGMVLVQSLHGIGRTVEIVNELRDVFGEVAAIPVQVLLTGVCLQISNGSYLGVRDILEEFFRIWVYKDNHYILNDAGVSTKGFHAKNCLDIDEYMEVVELYTFGVLAKFSNDMGLAISWVEKAALPEERRQGILRRLHSLLSLKTASSFEENSKDSSYAVVNNKKSLGNEKNDEIDSFLKLSKQHEPWSLWSSHPLSLKVGNTQFSMSRGKVAVSLVGLIICYALKRKRAALIRIIRRQMESTRKAIVDFWKLAFSYQVNPLAAIQSIPSTTT", "text": "FUNCTION: Involved in peroxisome biogenesis and matrix protein import (PubMed:24510720). Required for pollen maturation and in vivo germination via its role in peroxisomal function, which partially involves jasmonic acid biosynthesis (PubMed:24510720). Transported to peroxisomes via the interaction with PEX19-1 (PubMed:21487094). Required for peroxisomal protein import by acting as an anchoring protein for the AAA ATPase complex, which consists of PEX1 and PEX6 (PubMed:21487094). SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein."}
{"protein": "MGSAGSKKRSERQQGLREKLLRVPERPYGRLSGERREQSSRSPGESDKDLNSPSCEGQNARGAEGGGQQDADESDEDDEVGAICKTPIVPLRPMTYKLAVDMSHFIKEQGGLEGMYYSERRHRILDTYFENEEGIVSGWQNYTHGPGIRYPKYFGWLWKLVPVEVPAATREEEETHCLMHPAQISSWDDIHGETLIWQFDSLLAYDYVAFNRFPEEFGYQSGLPEEEWKARLKARGIPTD", "text": "FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike (By similarity). FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates cell surface expression of CD4, CD28, CD3, and MHC-I or MHC-II molecules. FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. FUNCTION: Interferes with TCR signaling from the cell membrane. Interacts with CD247/TCRZ (TCR zeta chain) and exert potent down- regulation of cell surface TCR/CD3 complexes. FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). SUBCELLULAR LOCATION: Host cell membrane; Lipid-anchor; Cytoplasmic side Note=Associates with the inner plasma membrane through its N-terminal domain. SIMILARITY: Belongs to the lentivirus primate group Nef protein family."}
{"protein": "MIVVQVSDTHIKSKGKLAYNKVDIHKALYNCILHINNLKPKPDLVIFTGDITDNGTNEEYKLFKETVKLLDVPFYVIPGNHDNAENLKREFEEYDWFEENNHLSLVIEDFPIRIIGLDSSIKGKSYGGLSEERLLWLEKQLNKFPDKKVLLFIHHPPVKIGIEHMDVQNLQIGRERLADLLGKYEQVLALACGHVHRVSTTLWNKIIVLTAASPSHQVALDLRKDAKAEFVMEPPSVQLHYWTEEQGLTTHTSYIGKFEGPYPFYNEKGELID", "text": "FUNCTION: Catalyzes the hydrolysis of the 3'-5' phosphodiester bond of glycerophosphodiesters such as glycerophosphorylethanolamine (GPE), a typical phospholipid metabolite. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class- III family."}
{"protein": "MNWLEERMPGIGRIAKDIAEHPVPSHTLNIFYCLGGLTLLCFIIQCLTGVFLAFYYKPTPEAAFASVQMITNEVRFGSVIRSMHHWSCQLMILLVFLHMLRVYYTGAFKKPRELNWVAGCFLLVLSLGLAFTGYLLPYEQLSYWASVIGAETANTLPVIGPTLKIMMQGGIKVTAEMLSRFYVLHVMILPAITIGFLVAHFIMIRVQGISDPM", "text": "FUNCTION: Component of the cytochrome bc complex which donates electrons to the photosynthetic reaction center. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family. PetB subfamily."}
{"protein": "MLSKEALIKILSQNEGGNDMKIADEVVPMIQKYLDIFIDEAVLRSLQSHKDINGERGDKSPLELSHQDLERIVGLLLMDM", "text": "FUNCTION: DNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance (PubMed:20347428). FANCM-MHF promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (By similarity). Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere- associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:22561346). SIMILARITY: Belongs to the CENP-X/MHF2 family."}
{"protein": "MTAPWAALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEPGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGCSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNSSTSDCLVSLVTSVTNVDLLPKESSI", "text": "FUNCTION: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin- A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily."}
{"protein": "MKKILIVLYSIFLSFTASSYEFNNKKEYEIEKRNISNVPKVMHFFSFFCPYCYELEKIYNIQSLIKNKIDKKIKIQTYHVNFLGGEFSKILTKIWIIAQKMKVEEKIMMPIFKEIQENNTISHTSNIKNIFLQKTGINKDQYNKFWNSFTIKMLIKKNDNDINKIKLNHVPTMIVNGKYVIDYYKLEKIFKTNFSKKYIKLIKFLLSKK", "text": "FUNCTION: Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins (By similarity). SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily."}
{"protein": "MHPPPPDAGVAMDFGQNSLFGYMEDLQELTIIERPVRRSLKTPEEIERLTVDEDLSDIDRAVYLLSAGQDVQGASVIANLPFLMRQNPTETLRRVLPKVREVLHVASVEMQLTAAVSFLTILQEESMSVHTCAHSFLQVILLHLEHRDTGVSNAWLETLLSAVELLPKETLRHEILNPLVSKAQLSQTVQSRLVSCKILGKITNKFDAHSIKREILPLVKSLCQDVEYEVRSCMCRQLENIAQGIGAELTKNVVLPELIELSRDESGSVRLAAFETLVNMLDMFDTDDRSQTILPLVKSFCEKSFKADESILISLSFHLGKLCHGLYGIFTPDQHLRFLEFYKKLCTLGLQQENGHNESQIPSQIVEQEKKYTSVRKNCAYNFPAMIVFVDPKNFHMELYSTFFCLCHDPEVPVRHTIAICFYEVSKLLNSGVHLIHKELITLLQDESLEVLDALINHLPEILELMSTGGENSVQENKFSSVPDLIPALTAAEQRAAASLKWRTHEKLLQKYTCLPHIISSDQIYYRFLQRMFTIMMTNNVLPVQRAAARTLCIFLRYNRKQEQRHEVIQKLIEQLGQGKSYWNRLRFLDTCEFIIEIFSRSFFCKYFFLPVIELTHDPVANVRMKLCYLLPKVKSALKIPADMHLLQQLEMCVRKLLCQEKDKDVLAIVKKTVLELDRMEMSMDMFQKKNYEKDLLDQEKEREELLFLEMEQLEKEKHQSDGRLASDKSFEKKRRDSRTSTQSLSKNLPISVPGPSSSTASTSKEIKKSKLTRSQSFNNQAFHAKYGTLDKCASKSSTLAHTSSVSGLVRTAMLSLTDDSFRTRNASSVPASFSPNPVMPSTSRGPGNTADPKSSGSKDAQPRKATLKSRKSNP", "text": "FUNCTION: Putative regulatory subunit of serine/threonine-protein phosphatase 4. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MIIEIEGIKLKLHPEVYEPAEDSILLLKNLVDVKNKDVLEIGVGTGLISIACAKKGAKKIVGVDINPYAVKLAKENAKLNNVNISFFESDLFENVTGKFDVILFNPPYLPTSEDEKIDSYLNFAFDGGKDGREILDRFIYELPNYLKKGGVVQILQSSLTGEKETINKLKPLGFKVEISARLKVPFEELMVINAWRL", "text": "FUNCTION: Putative protein methyltransferase using S-adenosyl-L- methionine as the methyl donor. May methylate a Gln residue in target proteins (By similarity). SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related family."}
{"protein": "MEPIWRNYPYPTYPGHHNFQFDPLLSDGSHTGVNQLGGVFVNGRPLADTVRAQIVEMSQHGTRPCDISRQLKVSHGCVSKILGRYYSTGSVRPGVIGGSKPKVATPRVVECIAGYKRANPTMFAWEIRQKLIEDQICGEENVPSVSSINRIVRNKSFMAQLAAPTSVTSSAARPSSATSHHQRSPPRGVQQHMQQSTSVQQLQQLQLTSAATVNSLMTPPAFAMPGTAYSINGLLGTLPQPSLLDDKFTNLSTQSADMSLVYSTGLVGEHDWTMRTPMVILPQNYCGQL", "text": "FUNCTION: Transcription factor (PubMed:17021039). Binds to specific DNA sequence motifs in regulatory elements, for example in the genes encoding transcription factor lin-48, apoptosis regulator ced-9 and neuropeptide-like protein nlp-2 (PubMed:17021039, PubMed:15923112, PubMed:11532910, PubMed:31398431). Specifies cell fate, playing an essential role in embryonic and larval development (PubMed:9374390, PubMed:10511553, PubMed:31398431, PubMed:17020758). Involved in morphogenesis of the vulva and uterus in hermaphrodites and of the rectal epithelium of the tail in males (PubMed:9374390, PubMed:15923112, PubMed:31398431, PubMed:17020758). Plays multiple roles in the development of the egg-laying system, acting in both lin- 3/EGF-pathway-dependent and -independent processes (PubMed:31398431, PubMed:17020758). Positively regulates expression of neuropeptide-like proteins nlp-2 and nlp-7 in uvl cells in an EGF-pathway-dependent manner (PubMed:31398431). Involved in negatively modulating apoptosis in germline and somatic cells, acting in partial redundancy with transcription factor pax-2, probably by directly regulating transcription of ced-9 (PubMed:17021039). Positively regulates transcription of lin-48 in hindgut cells and functions in the development of the hindgut (PubMed:11532910, PubMed:15923112, PubMed:10511553). SUBCELLULAR LOCATION: Nucleus Chromosome."}
{"protein": "MHCHAELRLSSPGQLKAARRRYKTFMIDEILSKETCDYFEKLSLYSVCPSLVVRPKPLHSCTGSPSLRAYPLLSVITRQPTVISHLVPTGSGLTPVLTRHPVAAAEAAAAAAETPGGEALASSESETEQPTPRQKKPRRSRTIFTELQLMGLEKKFQKQKYLSTPDRLDLAQSLGLTQLQVKTWYQNRRMKWKKMVLKGGQEAPTKPKGRPKKNSIPTSEEIEAEEKMNSQAQSQELLESSERQEEPCDTQEPKACLVPLEVAEPIHQPQELSEASSEPPPLS", "text": "FUNCTION: Transcription factor. Binds optimally to the DNA consensus sequence 5'-YYTAATGRTTTTY-3'. May control the expression of neural adhesion molecules such as L1 or Ng-CAM during embryonic development of both the central and peripherical nervous system. May be involved in controlling adhesive processes in keratinizing epithelia. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BAR homeobox family."}
{"protein": "MEEDRNWIVVPTWRVPGRMEKWHALVKYLKYRTKDLEEVRYVPHHKVGWAWWTCSRVIFPLQGKSHLEIQAYWNLTPEKGWLSSHAVRLTWYTEKFWTDVTPDCADILIHSTYFSCFTAGEVRRAIRGEKLLSCCNYPQAHKAQVPSLQYLALVVVQQNDRPQRKGTARKQWRRDHWRGLRVAREDHRSLKQGGSEPSAPRAHFPGVAKVLEILA", "text": "FUNCTION: Counteracts the innate antiviral activity of APOBEC3G. Forms a complex with host APOBEC3G thus preventing the entry of this lethally hypermutating enzyme into progeny virions. Functions as an adapter molecule, recruiting APOBEC3G to the ubiquitin-proteasome machinery. Targets APOBEC3G for degradation through the assembly with elongin BC complex, CUL5 and RBX1. Binds viral RNA and affects the stability of viral nucleoprotein core. May play a role in viral morphology (By similarity). SUBCELLULAR LOCATION: Host cytoplasm Host cell membrane; Peripheral membrane protein; Cytoplasmic side Virion Note=In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor (By similarity). SIMILARITY: Belongs to the primate lentivirus group Vif protein family."}
{"protein": "MATAKNKGKSIRVLGTSEAEKKDEMELEEEFQFSSGKYKDSGPGSDMWLGDASSTSPRSLRKTRTFDRHNPYLVSSYATPQPPTTTTCSVSFPFYLPPAIQNQQRFLHPNDPSGQRQQQMISFDPQQQVQPYVAQQQQQQQHLLQYWRDILKLSPSGRMMMMNMLRQESDLPLTRPPVQPFSATKLYRGVRQRHWGKWVAEIRKPRNRTRLWLGTFDTAEEAAMAYDREAFKLRGETARLNFPELFLNKQEPTPVHQKQCETGTTSEDSSRRGEDDSSTALAVGGVSEETGWAEAWFNAIPEEWGPGSPLWDDYHFPISNHKDDLDATQNSSSDTI", "text": "FUNCTION: Transcriptional activator involved in abiotic stress tolerance. Can directly regulate stress-related gene expression by binding to the DNA sequence 5'-[AG]CCGAC-3' (DRE element) of their promoter region. Involved in the regulation of stomatal closure movement under drought stress (PubMed:23625358). Acts as a positive regulator of drought stress response (PubMed:22095047). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily."}
{"protein": "MSYIEEEDQRYWDEVAAVKNWWKDSRWRYTKRPFTAEQIVAKRGNLKIEYPSNVQAKKLWGILERNFKNKEASFTYGCLDPTMVTQMAKYLDTVYVSGWQSSSTASSTDEPSPDLADYPMNTVPNKVNHLWMAQLFHDRKQREERMTTPKDQRHKVANVDYLRPIIADADTGHGGLTAVMKLTKLFVERGAAGIHIEDQAPGTKKCGHMAGKVLVPISEHINRLVAIRAQADIMGTDLLAIARTDSEAATLITSTIDHRDHPFIIGSTNPDIQPLNDLMVMAEQAGKNGAELQAIEDEWLAKAGLKLFNDAVVDAINNSPLPNKKAAIEKYLTQSKGKSNLEARAIAKEIAGTDIYFDWEAPRTREGYYRYQGGTQCAINRAVAYAPFADLIWMESKLPDYKQAKEFADGVHAVWPEQKLAYNLSPSFNWKKAMPRDEQETYIKRLGALGYAWQFITLAGLHTTALISDTFAKAYAKQGMRAYGELVQEPEMANGVDVVTHQKWSGANYVDNMLKMITGGVSSTAAMGKGVTEDQFKS", "text": "FUNCTION: Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2- methylisocitrate. SUBCELLULAR LOCATION: Glyoxysome. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family."}
{"protein": "MWRPAQGARWHVPAVLGYGGIPRRASWSNVESVANSRRRPVHPGQEVELDFAREWVEFYDPDNPEHLIAADLTWLLSRWACVFGTPACQGTVAGRPNDGCCSHGAFLSDDDDRTRLADAVHKLTDDDWQFRAKGLRRKGYLELDEHDGQPQHRTRKHKGACIFLNRPGFAGGAGCALHSKALKLGVPPLTMKPDVCWQLPIRRSQEWVTRPDGTEILKTTLTEYDRRGWGSGGADLHWYCTGDPAAHVGTKQVWQSLADELTELLGEKAYGELAAMCKRRSQLGLIAVHPATRAAQ", "text": "SIMILARITY: To M.leprae ML2435 and S.coelicolor SCO3349."}
{"protein": "MIPQLNRNYAWAIALGLVARSSLVSAGPCDIYASGGTPCVAAHGTTRALHDSYTGPLYQVKRGSDGATTDIAPRHAGGVANATHQDTFCAGTTCLITIIYDQSGHGNHLSQAPPGHFIGPDSQGYDNLASAIGAPVTLNGQKAYGVFISPGTGYRNNAAKNTATGDEAEGLYAVLDGTHYNNGCCFDYGNAEVSGDDTGNGHMEAIYFGDLTAYGTGSGSGPWIMADLENGLFSGFNAKNNAEDPSLSYRFISAAVKGGPNKWAIRGGNAASGPLSTFYNGSRPNARGYNPMSKEGAIILGIGGHNSKLTVGSSISLRATTLCCTTRYVAHNGSTVNTQVVSSSSSAALKQQASWRVRTGLANSECFSFESVDTPNSFLMHNNFVLLLKSNDGTKALHEAATFCPQLGLNGKGNSIRSWSYPTRYFRHYDNVLYAASNGGVHKFDNPASFNDDVSWVVSASFA", "text": "FUNCTION: Secreted alpha-L-arabinofuranosidase that actively hydrolyzes p-NP-alpha-L-arabinofuranoside and is specific for furanose configuration of the carbohydrate ring. Exhibits also significant activity against polymeric arabinose-containing substrates such as arabinan and arabinoxylan, a major component of plant hemicellulose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 54 family."}
{"protein": "MDTIKRMLWPKKEIFVGTFATGVERDTSVDIFQLVCRVVLRYMRTGKIENNTDSLGNFIVELLKTDCAAKWEWFMKRRRVGDYAKSLAIASIPVIPLLSYATMKKTVALRAFGNELSFNIRVPRPSVPKKGLLLRLAAGLALAPICALAMYATLPREKLSVFKLRTEARAHMEDEREATDCLVVEPARELKGKDGEDLLTGSRMTKVIASTGRPRRRPYAAKIAQVARAKVGYLKNTPENRLIYQRVMIEIMDKDCVRYVDRDVILPLAIGCCFVYPDGVEESAALWGSDESLGVKXGGLVRLPGVVTQTNRDIPSGVLLPQEVLEVRAGPPNAKDRNIFMVAGCPSQARFLVHNHCLKNLKRGLVERVFCVERNGQLTRTPQPTKGAFGRLSPFRKAVCEKVGVAHRLGYDGFLSYYSGAKLRTYTRAVESLHITPVSERDSHLTTFVKAEKISTAKGDPAPRVIQPRNPRYNVELGRYLRHMESKLMKAVDGVFGETTCIKGYTADEVGQIFRDKWDRFNKPVAIGLDASRFDQHCSVEALQFEHGFYRAMYPGNKLLSKLLDWQLHNKGKGYVPDGTITYRKEGCRMSGDINTSLGNYLLMCAMIYGYMRHLGINEYSLANCGDDCVLIVERRNLKQIQGTLPEYFLNLGYTMKVEPPVFQLEEVEFCQAHPVQFQGGWKMVRNVRTAMSKDVHCVNNIRDLATRRAWSNAQHHGGVALTSGIPVVEKFYSRFTLYEVPKKHQRIDTVTNVHKWRGSGGDYVVTPEARASFWAAFGLTGDEQLALEDRLDRWEMDLFGEEGVDAHEPSILDSAVA", "text": "FUNCTION: RNA-dependent RNA polymerase that plays an essential role in the virus replication. SIMILARITY: Belongs to the tombusviridae RNA polymerase family."}
{"protein": "MKIFQNTKNVIVSIAWAAALCTSAVSAQTLTSNSTGTNNGFYYTFWKDSGDASMTLLSGGRYQSSWNSSTNNWVGGKGWNPGSSSRVISYSGYYGVDSSQNSYLALYGWTRSPLIEYYVIESYGSYNPASCSGGTDYGSFQSDGATYNVRRCQRVNQPSIDGNQTFYQYFSVRNPKKGFGNISGTITFANHANFWATKGLNLGNHNYQVLATEGYQSRGSSDITVSQGGSSGGGNSSSSSSASGGGSKIIVVRARGTAGGESITLRVGNTNVATWTLTTTMTNYTATTSASGGSLVQYTNDSGNRDVQVDYISVNGSIRQSEDQTYNTGVYQNGSCGGGNGRSEWLHCNGAIGYGDI", "text": "FUNCTION: Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze glucuronoxylan and the arabinoxylan from wheat. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MPGAAEALPTVTVTLVAGAVPPASGALTAHCIGGFWREVGVASDQSLVLTAPKRVEGLFLTLSGSNLTVKVAYNSSGSCEIEKIVGSEIDSTGKFAFPGHREIHVLDTDYEGYAILRVSLMWRGRNFRVLKYFTRSLEDKDRLGFWKFRELTADTGLYLAARPGRCAELLKEELI", "text": "FUNCTION: May play a role in male fertility. May act as a retinoid carrier protein within the epididymis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MLTEQFDPSTFYSPKTVAIAGLILGCVLIYVYNDYPTNVNVPVIGVGVRYTKWLAAVRNVFYARDSVAEGYKKANFAFQIPTLNRMEIFICDRKMTREYQNLDSDRMSLDAVVVEEFEFDLLSPGHGHGHRRGPDSVPIPVVAKALAWQRRRTANTNDPFFQEFMAEVSYGFQQEVQRLSQDPRSSTTTPVFTVPCFSFALQVVGRITTFALFGRPMCRDRAFLDLCGKYSDGLPRGAMLLRPWPKWMRPFIAKHMEAPQVLAKLKEIIGAEIERRKASDGESPMENIMDYFVDWAYKGRDTVPADADDTVAHVLANLIFASFHTTSQLLTDCLFEIAMRPEYVEPLREEIKDCFEKHGRETRAVLDSLFKMDSFIKETHRWNPLDASALARIAMQDFTFSNGLHIPKGSFIFTPNAPIFQDERHYSNPKIFDGFRFAKMRDDPKLKLTCDLATVGEYSLNFGLGRHACPGRYLASDEVKLSLIHLLQNFDITVDPSELPLKRVRYGKFSLADMSAKVSLRRLRSEVKG", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals (PubMed:23468653, PubMed:29457197, PubMed:32077051). The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline (PubMed:32077051). The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively (PubMed:32077051). The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MNRRQQVKRRVGKYEVGRTIGEGTFAKVKFARNSETGEPVALKILDKEKVLKHKMAEQIRREIATMKLIKHPNVVQLYEVMASKTKIFIILEYVTGGELFDKIVNDGRMKEDEARRYFQQLIHAVDYCHSRGVYHRDLKPENLLLDSYGNLKISDFGLSALSQQVRDDGLLHTSCGTPNYVAPEVLNDRGYDGATADMWSCGVVLYVLLAGYLPFDDSNLMNLYKKISSGEFNCPPWLSLGAMKLITRILDPNPMTRVTPQEVFEDEWFKKDYKPPVFEERDDSNMDDIDAVFKDSEEHLVTEKREEQPAAINAFEIISMSRGLNLENLFDPEQEFKRETRITLRGGANEIIEKIEEAAKPLGFDVQKKNYKMRLENVKAGRKGNLNVATEIFQVAPSLHMVQVSKSKGDTLEFHKFYKKLSNSLEQVVWTNNEVKKETAK", "text": "FUNCTION: Involved in the resistance to some abiotic stresses (e.g. high salt, hyperosmotic stress) in young seedlings, by regulating the expression of several stress-inducible genes (cold- and salt-induced genes but not drought-responsive genes). Required for the ABA response during germination. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium- dependent manner. The CBL9/CIPK3 complex acts in the regulation of abscisic acid response in seed germination. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily."}
{"protein": "MQLIEVSAKTGYVWFRQGIWLFRRNPLAFVTLFFTYLLAMMLVSLVPVIGAALPLLLIPGIAVGFMAACRDTIAGKQVLPTILIDGFRSYGPIVTQRLLTLGGLYIVSMAAVFACSALGDGGTLLKIMFGLGAENLGPDALESPGFKIAALIAAALYAPVAMMFWFAPVLTAWHDVPPVKALFFSVVSCWRNKGAFTVYGLLWFALALGVSFGLAALMQALGASAYALMVMMPASIVITAMLYCSFYATYRGCFGVQEPGAPKLPNTSDR", "text": "FUNCTION: (Microbial infection) Probably transports the toxic C- terminal region of CdiA-2 from B.pseudomallei strain 1026b across the inner membrane to the cytoplasm, where CdiA has a toxic effect. Expression in E.coli makes the bacteria sensitive to the tRNase domain of B.pseudomallei strain 1026b CdiA-2. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein."}
{"protein": "MTKIKADPDGPEAQADACCGERTYHELLVNLNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFINKGEKGIMVLAGDTLPIEVYCHLPVMCEDRNLPYVYIPSKTDLGAAAGSKRPTCVIMVKPHEEYQEAYDECLEEVQALPPPM", "text": "FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, Cajal body Note=Also localized to Cajal bodies (coiled bodies). SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family."}
{"protein": "MAEPEGRSLDDFFAKRDKKKKKDKGGPVSAAGSRGATRPPDGAPSSFSSSASSMSGAGKGIKKEKSGKSENPDQLQEKEDDEWKEFEQKEVDYSGLRIQSLQISNEKDDDEYEKKEEQGADWEDIGGCGTDKSSGPWNKTAQAQAPISAVIEAPEPVHTGGVYRPPAARASVATRKPQGPPEIFSDTQFPSLQATAKHIESRRDKEMEKTFEVVKHKNRARDEAAKNQALRLQLDNQYAVLGEQ", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CDV3 family."}
{"protein": "MSRTIILIPVSTGVGLTSISLGLIHSLEQKGTKVAFMKPVSQPSTGEDKLDRTTSIIRTSTSLETAEPFMLSVAESLIGQNQSDVLLEKIVANHQQLTKNNDIVVVEGLIPTRKHGYANSINYEIAQALDAEIVLVAAPATETPTELKDRVEAAASLFGGKNNPNLLGVVVNKFNAPVDESGRTRPDLAEIFDSFQHNHISETEVNKLFAGSAIKLLACVPWNANLIATRAIDLVKHLGASIINEGEINRRIRGITFCARSLPNMVEHFRAGSLLVASADRPDVLVAAALAASNGIEIGGILLTGGYKIDAQINKLCRPTFEKAKLPIFRIEGNTWQTALSLQSFNLEVPVDDKERIENIKQYISQHFNADFINNLVADSSRLPRLSPPAFRFQLTELARAAKKRIVLPEGDEPRTIKAAVLCAERGIAECVLLADPASVQRVAEAQGVKLGKGITIINPADVRENYVDRLVELRKAKGMTETAAREQLEDTVVLGTMMLEANEVDGLVSGAVHTTANTIRPPMQIIKTAPGSSIVSSIFFMLLPDQVLVYGDCAVNPDPTAEQLAEIAIQSADSAKAFGIDPKVAMISYSTGTSGSGADVEKVKEATRIAKEKRPDLLIDGPLQYDAAVMEDVARSKAPNSPVAGKATVFVFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTIALTAIQATQ", "text": "FUNCTION: Involved in acetate metabolism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family. SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family."}
{"protein": "MATISPSPDLFTLVNVFGVAPEKQRELRDHLVQVTEDLIRHMPGFVSATFHLSRDGEQVVNYAQWRSEADFRAMHADPRLQPHFDYCRSVSRPKPIFCEVTHSFGATSPEGA", "text": "FUNCTION: Oxygenase required for conversion of tetracenomycin F1 to tetracenomycin D3."}
{"protein": "MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGPEDGENTAQWRSQENEEDGEEDPDRYICSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVAMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEVFEPPLTGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGSGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI", "text": "FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid- beta precursor protein). Requires the other members of the gamma- secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis. Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A22A family."}
{"protein": "MTSKTKNIDDIPPEIKEEMIQLYHDLPGIENEYKLIDKIGEGTFSSVYKAKDITGKITKKFASHFWNYGSNYVALKKIYVTSSPQRIYNELNLLYIMTGSSRVAPLCDAKRVRDQVIAVLPYYPHEEFRTFYRDLPIKGIKKYIWELLRALKFVHSKGIIHRDIKPTNFLFNLELGRGVLVDFGLAEAQMDYKSMISSQNDYDNYANTNHDGGYSMRNHEQFCPCIMRNQYSPNSHNQTPPMVTIQNGKVVHLNNVNGVDLTKGYPKNETRRIKRANRAGTRGFRAPEVLMKCGAQSTKIDIWSVGVILLSLLGRRFPMFQSLDDADSLLELCTIFGWKELRKCAALHGLGFEASGLIWDKPNGYSNGLKEFVYDLLNKECTIGTFPEYSVAFETFGFLQQELHDRMSIEPQLPDPKTNMDAVDAYELKKYQEEIWSDHYWCFQVLEQCFEMDPQKRSSAEDLLKTPFFNELNENTYLLDGESTDEDDVVSSSEADLLDKDVLLISE", "text": "FUNCTION: Serine/threonine-protein kinase. Needed for the initiation of DNA synthesis during mitosis as well as for synaptonemal complex formation and commitment to recombination during meiosis. Required for HTA1-HTB1 locus transcription repression. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily."}
{"protein": "MPRVSAPLVLLPAWLLMVACSPHSLRIAAILDDPMECSRGERLSITLAKNRINRAPERLGKAKVEVDIFELLRDSEYETAETMCQILPKGVVAVLGPSSSPASSSIISNICGEKEVPHFKVAPEEFVRFQLQRFTTLNLHPSNTDISVAVAGILNFFNCTTACLICAKAECLLNLEKLLRQFLISKDTLSVRMLDDTRDPTPLLKEIRDDKTATIIIHANASMSHTILLKAAELGMVSAYYTYIFTNLEFSLQRMDSLVDDRVNILGFSIFNQSHAFFQEFSQSLNQSWQENCDHVPFTGPALSSALLFDAVYAVVTAVQELNRSQEIGVKPLSCGSAQIWQHGTSLMNYLRMVELEGLTGHIEFNSKGQRSNYALKILQFTRNGFRQIGQWHVAEGLSMDSRLYASNISDSLFNTTLVVTTILENPYLMLKGNHQDMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRRPGYFSSLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWEGGKCPKEEDHRAKGLGMENIGGIFVVLICGLIVAIFMAMLEFLWTLRHSEASEVSVCQEMMTELRSIILCQDNIHPRRRRSGGLPPQPPVLEERRPRGTATLSNGKLCGAGEPDQLAQRLAQEAALVARGCTHIRVCPECRRFQGLRARPSPARSEESLEWDKTTNSSEPE", "text": "FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK4 subfamily."}
{"protein": "MYFQSLSADPLDSVNTTTDFNQLAQLLLMLTNSSSKETIATHVVTNSVPSAFQFDWSSHFKEEYDLVEKLNSPQYTNLTSISPSSSTDSNNLILRQIQIPKIEPALLNQCCLCTFAIVDKEISVVDGKYYHNNCLRCQMCDIPFEYSDKCYVRDGVFLCRADHAKRYQKCCRKCEIPLNREDMVMKAKEMIFHHACFVCFICGIKLNPGDYYTMSPQGHLYCHAHYNAVRSTVLCEEAAVATVPAVVAPPPPPPTTTTAPPPAAPEQPPREASTEAEASTDEDGNGSGSQRSKRMRTSFKHHQLRAMKTYFALNHNPDAKDLKQLAAKTNLTKRVLQVWFQNARAKYRRELHDGGRSSSPLCVSAPLASMDMNPPLSSSSSGHSTDGYQLNTPPLSSEIYSPNSNYTHL", "text": "FUNCTION: Transcription factor (PubMed:15177025, PubMed:19386265). Binds to a sequence motif, 5'-TTATTGGCTTCGTTAA-3', which may be involved in AIY interneuron function, in the regulatory elements of target genes; binding is more efficient, in vitro, together with homeobox protein ceh-10 (PubMed:15177025). Required for specification of the AIA and AIY interneurons and the NSM neurons (PubMed:11493519, PubMed:24353061). Positively regulates the expression of a number of genes including ceh-10, ceh-23, kal-1, hen-1, ser-2, unc-17 and sra-11 in AIY neurons, and cat-4, flp-4, bas-1, ptps-1 and mgl-1 in NSM neurons (PubMed:11493519, PubMed:24353061, PubMed:19386265, PubMed:15177025). In concert with WNT/beta-catenin signaling, initiates expression of homeobox ceh-10 in AIY, but not in the sister cells, SMDD motor neurons (PubMed:19386265). Also acts in an autoregulatory feedback loop to maintain its own expression (PubMed:9292724, PubMed:19386265). Plays a role in the thermotactic response, olfactory imprinting, regulation of longevity, control of dauer formation and axon outgrowth and pathfinding (PubMed:9292724, PubMed:16051801, PubMed:21055415, PubMed:24353061). Not required for normal chemosensory behavior (PubMed:9292724). SUBCELLULAR LOCATION: Nucleus Perikaryon Cell projection, axon."}
{"protein": "MAASRSELLRPAFGEPSPSLGPFVVNPHTCSYRWWQKFLIVLVLYTAWASPFELAMEKSASAALAVTELVVDAFFAVDIAVSFFVAYRDASTGLLVTDRKKIATRHLARPCLALDVASTIPLQMIYRIVSGKRQALYGLLNLLRLWRLRRVSKLFARLEKDIRFSYLWTRLIKLLYVTLFAVHFASCIYLWMAFHHKAKELTWIGSQFHGFEDRSVWFCYTCAVYWSITTLATVGYGDLHAANTGEMLFSIAFMLFNMGLTSYIIGNITNLVVHETTNTFKMRDMVQRTSVFGRTNRLPVAMREQMMESLQLRFRAEEQLQQEMLSELPKAVRSGIAQHMFRGAVQSCYLFQGVSDKLVLPLVAEMKAESFPPKADIILENEASTDCYIIVSGEVEVLTTLEDGTEKQVMRIGPRGMAGEIGVMFNIPQPFTIRSRKLTQLVRISHSHMVSTIRPNTADGVVVFSNFVLYLESLKVKAKETAFVRDHLRNGYSTVLGSATMFDVDESKESAHKMLPCKEPKRVSIHEHLLNGTGTALNGSSGKLVILPDSMQDLMKLSEKKFGKAARGILTVGGAEVEDIEVIRDGDHLFFSW", "text": "FUNCTION: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4) subfamily."}
{"protein": "MAFSDLTSRTVRFYDNWIKDADPRVENWLLMSSPLPQTIILGLYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGTGYSFRCDIVDYSQSPRAMRMVHTCWLYYFSKFIELFDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYFYYGLCAMGPAYQKYLWWKKHLTSLQLVQFVLVTVHIGQIFFMEDCNYQYPVFLYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTMENGNCKSKHH", "text": "FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ELO family. ELOVL7 subfamily."}
{"protein": "MAMGNPGLWTHFSRSPRELRIPNDLELPNGLLVVCGLPGLLLLFFVTAILLYPFRNKSDLPLINPGKGRIGILRGYRARKTFAAELPRLVTEGLSKASAFRIAAPDGVNIVLAPRYAHEIAEHPDLNPGPIAGDEFNCHIDGFEVFAQLGTSDVIAESVRTRLTRQLTKLTPLLTTETPLLLQSQWKDAPTWVEVSPHETALFILSRLSSLVFVGDDLGRNPDWVHILTSYNTEAFAAAQELNLWPQILRPLVARLKPSCRQLRRYIRDARALLVPVIEQRRHAQSHGDRREYNDAIEWLDQTSRSAGQPYDPLLSQMLLAIGSFHTSSDLLGQVLLDLCSRRDWEVLARELRKEIISSLQGAGWDKIALNNLKLMDSVLKESQRLKPASTVTMGRYASREIRLSDGTAIPKGSTVFIANVAMRDPKIYPEPDAFIPDRFTTRREKGDSSAYLVSASPEHIGFGLGRHACPGRFFAANEVKIVLSHMLLKYDIKFPDNGAAAPSTSGIFLETNPDARICVRRRKEEIVI", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:28233494). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (By similarity). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (By similarity). Acid-catalyzed keto- rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By similarity). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (By similarity). The cytochrome P450 monooxygenase ausG modifies austinolide to austinol (By similarity). Austinol is further acetylated to austin by the O-acetyltransferase ausP, which spontaneously changes to dehydroaustin (PubMed:28233494). The cytochrome P450 monooxygenase ausR then converts dehydroaustin is into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation catalyzed by ausR permits the O-acetyltransferase ausQ to add an additional acetyl group to the molecule, leading to the formation of acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase ausT catalyzes the reduction of the double bond present between carbon atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7- hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an acetylation reaction but also the addition of the PKS ausV diketide product to 1,2-dihydro-7-hydroxydehydroaustin, forming precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha- ketoglutarate-dependent dioxygenase converts precalidodehydroaustin into calidodehydroaustin (PubMed:28233494). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MLSKQIPLGIYEKALPAGECWLERLQLAKTLGFDFVEMSVDETDDRLSRLNWSREQRLALVNAIVETGVRVPSMCLSAHRRFPLGSEDDAVRAQGLEIMRKAIQFAQDVGIRVIQLAGYDVYYQEANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMSSISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGIGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFETLKQSGYCGPYLIEMWSETAEDPAAEVAKARDWVKARMAKAGMVEAA", "text": "FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to L- ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization. FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to L- ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization. SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase family."}
{"protein": "METGGLSAAALANGDLGSQRERTLVPERLQKREHERQLEVERRKQKRQDQEVEEEKSDFFAAAFARERSAVEELLESGESVERLEEAAARLQGLQKLINDSVLFLAAYDLRQAQEVLARLQAALAKRRQELQPKKRFAFKTRKKDAASATQVASAPDAPAAEGSLTSPPPLKEEGDFDSSWICGFSNLQSQVLEKRAEELHQQDVLLTQLRNCTIKLYGNPNTLRLTKAQGCTLLCGPVSTSVFLEDCSDCVLAVACQQLRVHTTKDTRIFLQVTSRAIMEDCTGIQFAPYTWSYPGIDKDFEGSGLDKNKNNWNDVDDFNWLARDVASPNWNVLPEEERRIQWD", "text": "FUNCTION: Tubulin-folding protein; involved in the final step of the tubulin folding pathway. SUBCELLULAR LOCATION: Cytoplasm Note=Detected predominantly in the photoreceptor connecting cilium. SIMILARITY: Belongs to the TBCC family."}
{"protein": "MYGHLSLSTLSLLAVVAAAPFHESWLQPRDSDVSQLFRRGAPDPKASDYLSYYPSPGSTPNVSTIPQAWLDKLATVQLPNVSVATANDGRPTYPNNENDGDSEICSFTDQCYVEDDLYSPPGEKVWALSFDDGPTDVSPALYDYLAQNNISSSATHFMIGGNIITSPQSVLIAIEAGGHLAVHTWSHPYMTTLTNEQVVAELGWTMQALSDLNGGRIPLYWRPPYGDVDNRVRAIAKGVFGLVTVLWDSDTNDWAISDQPDQYSVASVEAYFDTLVTGNRTQGLLLLEHELDNNTVEVFETEYPKAVANGWSVKNVADAFSMKWYLNSGKGNDDVVTTMSVAGTLTTAKPTHTSTSVASATATSSASVTDSAGVSIASAASSQESSSWPIANRPSLFVIACGLALAAIMV", "text": "FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (By similarity). Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis (By similarity). Chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the polysaccharide deacetylase family."}
{"protein": "MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVALAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA", "text": "FUNCTION: AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis (PubMed:11882383, PubMed:21620960, PubMed:21432781). This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates (PubMed:11882383, PubMed:21620960, PubMed:21432781). Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported (PubMed:11882383, PubMed:21620960, PubMed:21432781). AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (PubMed:9632753, PubMed:10400692). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (By similarity). Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport (By similarity). AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (By similarity). AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating the TORC1 signaling pathway, and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Also regulates the TORC1 signaling pathway by catalyzing phosphorylation of CASTOR1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF- kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1 (By similarity). AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis (PubMed:12107176). Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis (By similarity). Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity (PubMed:15546921). The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth (By similarity). AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I) (By similarity). AKT mediates the antiapoptotic effects of IGF-I (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (By similarity). May be involved in the regulation of the placental development (By similarity). Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr- 384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility. Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation. Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation (By similarity). Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor (By similarity). Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity (By similarity). Acts as a negative regulator of the cGAS- STING pathway by mediating phosphorylation of CGAS during mitosis, leading to its inhibition (By similarity). Acts as an inhibitor of tRNA methylation by mediating phosphorylation of the N-terminus of METTL1, thereby inhibiting METTL1 methyltransferase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A (By similarity). Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus. Colocalizes with WDFY2 in intracellular vesicles (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily."}
{"protein": "MAGELYFSGVTGAYDWGSVLDNIMAVKSIPIQKLQQKKQLINQKLQILGEFSQKLSDLKNLIENFNLESALKTKKADVSDSDVISVSVSENAPEISFSVNVLNTASKEILVYDAGFNSLDETIGSDGSFTLRYYTSPTDYVEYTIDYSLIDTLKDIVNKINETQDYVKASIYYDGNKYKLMLAETSEENSTVETAPDLSTKAIHLLGTLPHQFGNNVLIQQAKNARIQIGSGDVIESAGNTFENVIEGVSISAKRAGTSEVSISQDFSKIREFLNNFVKSYNEVVSQVKSLTLGENAPFRGENTIMNVKYGLSDTLTPLMELGLIEYKEDGTISLSGNLESVINEKPDEFKLKMTQFLESAKAVAKVNYEAFEDFKEYLNDQAERIDENIRLLSQRLVQEEQILKRQFAQLEDFMNYANQIRERLKQFMVSISEMNGGNNK", "text": "FUNCTION: Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity). SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the FliD family."}
{"protein": "MEYEAKKGKKGFVSPIRRLVFPKAARQAAFRSSVSRRPLHSMPLYPPDYLIDPHILLCDYLEKEVKFLGHLTWVTSSLNPSSRDELLQLLDTARQLKELPLKTTPEQDSILSLSARCLLLTWRDNEELILRIPTHEIAAASYLQDDALHLLVLKTGLGVDPVPAGMDGSPGGSGRDPGPPGAAPEKRRVGTAERRHTICSLDWRVAWGGGAGAEARAAGGGGSLERQRAGARASGSWERRQTFSGSWERRHAGGGAGKPGGSWERRQASGGVGGSWERRHPGPNPLDPQNHSPDAYCNLVILAVANRDAAEESCALICQVFQIIYGDQSIECVDRAGYHYRSTPKRPWLSSCTMAPRTHLKRATVAHPHRLSTAPTAAVSTTAAGPSSSYRITWSRCGVSWVLLRSSSLHCCYETIVWGCLSRTTVQVCRNSMGTDGSSFSLECGPSSQIRTSATSRASWRVWVSARAESSLTALAASSAA", "text": "SIMILARITY: Belongs to the CCM2 family."}
{"protein": "MAAAAGAEGRRAALEAVAAPERGGGSCVLCCGDLEATALGRCDHPVCYRCSTKMRVLCEQRYCAVCREELRQVVFGKKLPAFALIPIHQLQHEKKYDIYFADGKVFALYRQLLQHECPRCPHLPPFSLFGDLEQHMRKQHELFCCKLCLKHLKIFTYERKWYSRKDLARHRMQGDPDDTSHRGHPLCKFCDERYLDNDELLKHLRRDHYFCHFCDSDGAQDYYSDYAYLREHFREKHFLCEEGRCSTEQFTHAFRTEIDLKAHKTACHSRSRAEARQNRQIDLQFSFAPRHSRRSEGVVSGEDYEEVDRYNRQGRAGRASGRGAQQNRRGSWRYKREEEDREVAAAIRASVAAQQQEETQRVEDREEGSRPKKEEAAARVPEEPRGHRRLPRAQGEGSGSKEASANGPVSQEAFPATGPGPVVALSNTLPPPSPELKEEDFPSLCASTSSCCTAVTPGSVGLALAYPGPPRGKNTFQEEDFPALVSSAPKPSSAPSSLISAWNSGCSKKGNLPTPGSQAVVGGSQPPRKAGKGSRGGRKGGPAPVDEEDSGGLTVQGLRSVPTTVAVSSLLAPATNQSSAKVGKKKKVGSEKPGATSSPLLPPDHTPKPSGAEQVLEAPLSKAEVPVTIVVNGHSEGSALVRSAPKEPPGLPRPLGPLPCPIPQEDFPALGGPCPPRMPPPPGFSTVVLLKGTPPPPPPPPGLVPPISKPPPGFSSLLPSSHSACAPSPTTTTTTTTTTKTPGLAPTPQAYLVPENFRERNLQLIQSIKDFLQSDEACFSKFKSHSGEFRQGMISAAQYYKSCRDLLGESFQKIFSELLALLPDTAKQQELLSAHTDFCSREKPPNSRSKRNKKNVWQTSTQQLGLDCCVCPTCQQVLAHGDVSSHQALHAARDDDFPSLQAIARIIT", "text": "FUNCTION: E3 ubiquitin-protein ligase that plays a key role in the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, leading to degradation of nascent peptide chains. ZNF598 is activated when ribosomes are stalled within an mRNA following translation of prematurely polyadenylated mRNAs. Acts as a ribosome collision sensor: specifically recognizes and binds collided di-ribosome, which arises when a trailing ribosome encounters a slower leading ribosome, leading to terminally arrest translation. Following binding to colliding ribosomes, mediates monoubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS3/uS3, and 'Lys-63'-linked polyubiquitination of RPS20/uS10. Polyubiquitination of RPS20/uS10 promotes recruitment of the RQT (ribosome quality control trigger) complex, which drives the disassembly of stalled ribosomes, followed by degradation of nascent peptides. E3 ubiquitin-protein ligase activity is dependent on the E2 ubiquitin-conjugating enzyme UBE2D3. Also acts as an adapter that recruits the 4EHP-GYF2 complex to mRNAs. Independently of its role in RQC, may also act as a negative regulator of interferon-stimulated gene (ISG) expression. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the ZNF598/HEL2 family."}
{"protein": "MYSAKNRFVQSVQRLQDFRNMYDYEARLATFADWPFTENCKCTPENMAKAGFVHCPTENEPDVACCFFCLKELEGWEPDDDPWNEHSKRSVNCGFLSLTKCVNDLTMEGFLRLEGDRIKSFYRKFSTVVLQYVEEEMTAATKRLLEYFSNQHQCSIDLDH", "text": "FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Stimulates the mitotic kinase activity of aurkb/aurora-B in the CPC. Does not appear to exhibit anti-apoptotic activity (By similarity). CPC. Does not appear to exhibit anti-apoptotic activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, centromere Cytoplasm, cytoskeleton, spindle Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. SIMILARITY: Belongs to the IAP family."}
{"protein": "MSRQKNQNSKGHGVSKGKEREQRTLIRFKTTLMNTLMDVLRHRPGWVEVKDEGEWDFYWCDVSWLRENFDHTYMDEHVRISHFRNHYELTRKNYMVKNLKRFRKYLERESGKTEAAKCDFFPKTFEMPCEYHLFVEEFRKNPGITWIMKPVARSQGKGIFLFRRLKDIMDWRKGTSGKKPTGVETQPARANMNPSGSHDTRSSDDQKDDLPVENYVAQRYVENPYLIGGRKFDLRVYVLVMSYIPLRAWLYRDGFARFSNTRFTLNSIDDHYVHLTNVAVQKTSPDYHLKKGCKWMLQRFRQYLASKHGPKAVETLFSDMDNIFIKSLQSVQKVIISDKHCFELYGYDILIDQDLKPWLLEVNASPSLTASSQEDYELKTCLLEDTLHVVDMEARLTGKEKRVGGFDLMWNDGPVSREDGPSDLSGMGNFVTNTHLGCVNDRKEQLRQLFRSLQAQRKAPS", "text": "FUNCTION: Probable tubulin polyglutamylase that generates side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of target proteins (PubMed:27257088). Similar to TTLL1, may acquire enzymatic activity only in complex with other proteins as it is most likely lacking domains important for autonomous activity (Probable). Mediates tubulin polyglutamylation which induces establishment of microtubule heterogeneity in sperm flagella, thereby playing a role in normal motile flagella axoneme structure and sperm flagella beating pattern (PubMed:27257088). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the tubulin--tyrosine ligase family."}
{"protein": "MMAIQNREEFLLQLSEKLGRKRPEAVEKPKWSFSPQWNVFDGLAQDELVLQLMEHCEVIHTEVKRTTKENLVETLGSLIKEWNIKSAMYSNDERFNEYGLTSCFNNEGTTHFRAWGLGDKEEDIKFAKAADLGITFSDMTLAESGTVVLFNDGLKGRHVSLLPESYIAIVPKSTIVPRLTQATKLIHNQSKAGENLPACVNFVSGPSNSADIEMNLVVGVHGPIRTAYIIVDDQ", "text": "FUNCTION: Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. SIMILARITY: Belongs to the LutC/YkgG family."}
{"protein": "MTTRQPLYKSLYFQVIVAIAIGILLGHFYPQTGVALKPLGDGFIKLIKMVIAPIIFCTVVSGIAGMQNMKSVGKTGGYALLYFEIVSTIALLIGLVVVNVVQPGNGMHIDVSTLDASKVAAYVTAGKDQSIVGFILNVIPNTIVGAFANGDILQVLMFSVIFGFALHRLGAYGKPVLDFIDRFAHVMFNIINMIMKLAPIGALGAMAFTIGAYGVGSLVQLGQLMICFYITCVLFVLVVLGAICRAHGFSVLKLIRYIREELLIVLGTSSSESALPRMLIKMERLGAKKSVVGLVIPTGYSFNLDGTSIYLTMAAVFIAQATDTHMDITHQITLLLVLLLSSKGAAGVTGSGFIVLAATLSAVGHLPVAGLALILGIDRFMSEARALTNLVGNAVATVVVAKWVKELDEDQLQAELASGGRAISDTREEDDLGVAEGPTPTTVK", "text": "FUNCTION: Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the inner membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family."}
{"protein": "MAVVAVAGGTGGKGVPGAANEPRRYAVDYDNVEEMRNVLKENNVEVVVSALLLSDESVAKSQINLIRAAAESGTVTKFIPSEYYIDFHSPIPGSDLFTNFQIEAEEELMRHPQLTWTLIRVGIFLDHLTMPFNPKPTYITPYWVFVDIEHEECVFPGDGSQPLVLSHSTDLAAYIECLVGLPSNEWPRESLVASNKIQVKDLQDLIKKTTGTLCGHLGICIRTFLILAIGREFKVTYDSVESIQKGQITPLTSNRPVFDDPQKGKLFQEVEVQVMLSMLSNAHDLPGKNLAELFPEVHVTNIEDFLRAGWEMKQGLKP", "text": "FUNCTION: Aminotransferase; part of the gene cluster that mediates the biosynthesis of swainsonine (SW), a cytotoxic fungal alkaloid and a potential cancer therapy drug (PubMed:28381497). Swainsonine production occurs via a multibranched pathway and is dispensable for fungal colonization of plants and infection of insect hosts (By similarity). The first step of swainsonine biosynthesis is the production of the precursor pipecolic acid (PA) via conversion of L-lysine (Lys) to 1- piperideine-6-carboxylate (P6C) by the aminotransferase swnA, the latter being further reduced to PA by the reductase swnR (By similarity). The PKS-NRPS hybrid synthetase swnK uptakes and condensates PA and malonyl-CoA with and without skipping of the ketoreductase (KR) domain in order to produce 3 intermediates, 1- oxoindolizidine, (1S)-1-hydroxyindolizin, and (1R)-1-hydroxyindolizine; with the transisomer (1S)-1-hydroxyindolizin being predominant (By similarity). The terminal thioester reductase (TE) domain of swnK is involved in reduction of the thioester bond to release the intermediate aldehydes (By similarity). The oxidoreductase swnN could contribute to the reduction of 1-oxoindolizidine to (1S)-1-hydroxyindolizin and (1R)- 1-hydroxyindolizine, contributing to the major route of SW production (By similarity). The dioxygenase swnH2 would be responsible for the oxidization of (1R)-1-hydroxyindolizine into (1R,2S)-1,2- dihydroxyindolizine and of (1S)-1-hydroxyindolizin to yield both (1R,2S)-1,2-dihydroxyindolizine and (1S,2S)-1,2-dihydroxyindolizine (By similarity). The dioxygenase swnH1 then performs the conversion of the 1,2-dihydroxyindolizine epimers to SW (By similarity). SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily."}
{"protein": "MYKKLYLIGILLLGLISGLTFNLIFFTVPYQLSEAKYTTDIVGSISLAAFPYCLKVIWSPFIDKYSIPFLGVKFGHRRGWALVSQIFLILTMMWFLKRSPCNNLCITAIILFIIAFCSSTQDIVLDAYRIERTTSKKELSIAFTFSSIGFRLGMLLGSVGALYSSIIFGWNTVYKFALFITMVGPIVILCIKEPELKTKRNTTNNLIDLQQYFEVIKKSIISFKNEQKYLLLIILFVFLYKAADSIPMAMSIPLFLDLSFTTHEIAVIYKAYGLLIMIVGGTLGGILAAKIGIFHSVLIGGVIQLLSPIMFMILATIGYDIKTFIITITIQNFCSGFAGTIISIYFASLCNSEFVATQYSISSSFSSLSRIILASLGGICAKHLTWPVFFLCNTLFSMLFIPIFYIYRKKLHFINYSKKI", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily."}
{"protein": "MAGPERWGPLLLCLLQAAPGRPRLAPPQNVTLLSQNFSVYLTWLPGLGNPQDVTYFVAYQSSPTRRRWREVEECAGTKELLCSMMCLKKQDLYNKFKGRVRTVSPSSKSPWVESEYLDYLFEVEPAPPVLVLTQTEEILSANATYQLPPCMPPLDLKYEVAFWKEGAGNKTLFPVTPHGQPVQITLQPAASEHHCLSARTIYTFSVPKYSKFSKPTCFLLEVPEANWAFLVLPSLLILLLVIAAGGVIWKTLMGNPWFQRAKMPRALDFSGHTHPVATFQPSRPESVNDLFLCPQKELTRGVRPTPRVRAPATQQTRWKKDLAEDEEEEDEEDTEDGVSFQPYIEPPSFLGQEHQAPGHSEAGGVDSGRPRAPLVPSEGSSAWDSSDRSWASTVDSSWDRAGSSGYLAEKGPGQGPGGDGHQESLPPPEFSKDSGFLEELPEDNLSSWATWGTLPPEPNLVPGGPPVSLQTLTFCWESSPEEEEEARESEIEDSDAGSWGAESTQRTEDRGRTLGHYMAR", "text": "FUNCTION: The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)- induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type II cytokine receptor family."}
{"protein": "MAESFTTTNRYFDNKHYPRGFSRHGDFTIKEAQLLERHGYAFNELDLGKREPVTEEEKLFVAVCRGEREPVTEAERVWSKYMTRIKRPKRFHTLSGGKPQVEGAEDYTDSDD", "text": "SIMILARITY: Belongs to the UPF0438 family."}
{"protein": "MTIRSLPAALSPLSMAVQAVLLVSSLALAPAANAKPVTWEDIANDHLNTQNVLQYGMGTNAQRWSPLAMVNDKNVFKLTPAWSYSFGDERQRGQESQAIINDGVIYVTGSYSRVFALDAKTGRRLWTYNHRLPDNIRPCCDVVNRGAAIFGDKIYFGTLDARVIALNKDTGKVVWNKKFGDHSAGYTMTGAPTLIKDQKSGKVLLIHGSSGDEFGVVGQLYARDPETGEEVWMRPFVEGHMGRLNGKDSTPTGDVKAPSWPDDPTTETGKVESWSHGGGAPWQSASFDPETNTIIVGAGNPGPWNTWARTSKDGNPHDFDSLYTSGQVGVDPTTGEVKWFYQHTPNDAWDFSGNNELVLFDYKDKDGKQYKATAHADRNGFFYVVDRTNGKLKNAFPFVDNITWASHIDLKTGRPVENEGQRPAKPLPGETKGKPVEVSPPFLGGKNWNPMAYSQDTGLFYVPANHWKEEYWTEEVNYKKGSAYLGIGFRIKRMYEDHVGSLRAMDPTTGKVVWEHNERLPLWAGVLATKGNLVFTGTGDGYFKAFNAKTGEELWKFQTGSGIVSPPITWEQDGEQYIGVTVGYGGAVPLWGGDMAELTKPVAQGGSFWVFKIPAWDTKTAKR", "text": "FUNCTION: Catalyzes the oxidation of ethanol and other primary alcohols to the corresponding aldehydes, except methanol, which is not a substrate (PubMed:7730276). Uses a specific inducible cytochrome c550, encoded by the adjacent gene in the locus, as electron acceptor (By similarity). Is a key enzyme of the carbon and energy metabolism during growth of P.putida on ethanol as the sole carbon and energy source (PubMed:18218017). Displays lower activity on secondary alcohols, aldehydes and diols. Is not active with sugar alcohols such as glycerol and D-sorbitol (PubMed:7730276). In vitro, reacts well with phenazine methosulfate (PMS) as an electron acceptor but not with NAD(P), potassium ferricyanide, or molecular oxygen (PubMed:7730276). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family."}
{"protein": "MEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILARGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIILILIILFATGTIPT", "text": "FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t- SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Also plays a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (PubMed:12737809). Involved in the homotypic fusion of early and late endosomes (PubMed:10982406, PubMed:11029036). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type IV membrane protein Late endosome membrane; Single-pass type IV membrane protein Early endosome membrane; Single-pass type IV membrane protein Midbody Cell membrane; Single-pass type IV membrane protein Zymogen granule membrane; Single-pass type IV membrane protein Note=Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi (PubMed:9614193). Sub-tight junctional domain in retinal pigment epithelium cells (PubMed:11029036). Midbody region during cytokinesis (PubMed:12414999). Lumenal oriented, apical membranes of nephric tubular cell (PubMed:11208143). Cycles through the apical but not through the basolateral plasma membrane (By similarity). Apical region of acinar cells; in zymogen granule membranes (By similarity). SIMILARITY: Belongs to the synaptobrevin family."}
{"protein": "MAMAGLYRRLLPSPPAVDFASSQGKQLFLEAVQNGTMESFYRLVSYFQTQSEPAFCGLASLSMVLNALAIDPGRKWKGPWRWFDESMLDCCEPLDKIKARGISFGKLVCLAHCAGAKVEAFHASHSSIDHFRKYVMKCSTSDDCHVISSYHREALKQTGTGHFSPIGGYHAGKDMALILDVARFKYPPHWIPLTHLWEGMNYVDESTGKTRGFMLISRPHREPGMLYTLSCKHESWNSIAKFLIDDIPFLLTSEDVKDICKVLSVIVTSLPSNFEEFIKWVAEIRRGEDGSPSLSVEEKARLSVKEEILKQVQRTGLFKHVASFLSHSCSGHTPTSGDRDTFPVIAASVCCQGAEILGGKISSSAEYCCRETCMKCWKAEDDKPIRMVCGTVVNGNTEQGVDVLIPSSCGKLSCTCSSTTKSIRKHPASTDVLTVLLLSLPTSTWAGIADEKLLSEIHDLVSIENLPALLQEEVLHLRRQLHILKRCQEGKVDEDLGVPLS", "text": "FUNCTION: Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. SIMILARITY: Belongs to the phytochelatin synthase family."}
{"protein": "MTNGYIGSYTKKNGKGIYRFELNENQSRIDLLETGFELEASTYLVRNNEVLYGINKEGEQCGVASLKIDDNGELHLLNKCLSSKAGTGCYVSISEDKRYLFEAVYGDGIIRMYELNTHTGEIIRLIQELAHDFPTGTHERQDHPHAHYINQTPDGKYVAVTDLGADRIVTYKFDDNGFEFYKESLFKDSDGTRHIEFHDNGKFAYVVHELSNTVSVAEYNDGKFEELERHLTIPESFDGDTKLAAVRLSHDQQFLYVSNRGHDSIAIFKVLDNGQHLELVTITESGGQFPRDFNIASSDDLLVCAHEQGDSVVTVFERNKETGKITLCDNTRVASEGVCVIF", "text": "SIMILARITY: Belongs to the cycloisomerase 2 family."}
{"protein": "MQWQTKLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEQSIPAIVDAYGDKALIGAGTVLKPEQVDALARMGCQLIVTPNIHSEVIRRAVGYGMTVCPGCATATEAFTALEAGAQALKIFPSSAFGPQYIKALKAVLPSDIAVFAVGGVTPENLAQWIDAGCAGAGLGSDLYRAGQSVERTAQQAAAFVKAYREAVQ", "text": "FUNCTION: Involved in the degradation of galactose via the DeLey- Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with re- facial selectivity. It can use a limited number of aldehyde substrates, including D-glyceraldehyde-3-phosphate (natural substrate), D- glyceraldehyde, glycolaldehyde, 2-pyridinecarboxaldehyde, D-ribose, D- erythrose and D-threose. It efficiently catalyzes aldol addition only using pyruvate as the nucleophilic component and accepts both stereochemical configurations at C2 of the electrophile. SIMILARITY: Belongs to the KHG/KDPG aldolase family."}
{"protein": "MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKAAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKKKRGVDYNAEIPFEKKPALGFYDTSEENYQTLDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEIARQTAEESGITNSASSTLLSEYNVTNNSIALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSHGSEGLTPRSGTTPKPVINSTPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREIDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKTVGFGTNNAEHIAYLEHNPYEKFSKEELKKAQDVLVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPGQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLMKQLNDLWDQIEQAYLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQHRYADLLLEKETLKAKF", "text": "FUNCTION: DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=May shuttle between cytoplasm and nucleus. SIMILARITY: Belongs to the CEF1 family."}
{"protein": "MDLSNSSPVITDPVAISQQLLGGLPSNLMQFSVMPGGYSSSGMNVGVSRLKIEEVLVNGLLDAMKSSSPRRRLNVAFGEDNSSEEEDPAYSAWMAKCPSALASFKQIVASAQGKKIAVFLDYDGTLSPIVDDPDKAVMSPVMRAAVRNVAKYFPTAIVSGRSRNKVFEFVKLKELYYAGSHGMDIMAPSANHEHSAEKSKQANLFQPAHDFLPMIDEVTKSLLQVVSGIEGATVENNKFCVSVHYRNVAEKDWKLVARLVNEVLEAFPRLKVTNGRMVLEVRPVIDWDKGKAVEFLLQSLGLNDSENVIPIYIGDDRTDEDAFKVLRQRNCGYGILVSQVPKETEAFYSLRDPSEVMEFLNFLVRWKKHSV", "text": "FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant improves abiotic stress tolerance. SIMILARITY: Belongs to the trehalose phosphatase family."}
{"protein": "MTYLLKKNPFVANNLLKKINKLNRKAQKEIIITWSRGSTIIPIMIGHTIAIHNGKEHLPIYIMDDMVGHKLGEFAATLNFRGHEKGDNKSRR", "text": "FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS19 family."}
{"protein": "MNVPMADEWFDCAIRLDSETIAVHEIFNSDLSKLLNLHSKTVYMSDLCAFISGCVNRNVGKLTIYWHVYGDIIYALTGILHCVKITIECGERIADGRYRLYEIPKLFLMRGQSTPLELKWKHAVGIATTNKPLLTHVLTDVLETSPFTLPDTLLSVQELSIFRERLSYIYYVLGLDVDIVARTEREIFQKCAELARLQQVFLIQGNIMENFVLVQACLFQLGADGLWEEMSGSVRPRPELMSSAFIQHRVMVNNCYCLAVIFNAIYKHKVSLPTVERSHEIVHRVVQEYYKSYVNAPLSVLVCATKVLTLFTEEYNFQSALVFVSQFFQVDVEASRADVIRLFLACLKGD", "text": "SIMILARITY: Belongs to the herpesviridae U59/UL88 family."}
{"protein": "MALPFQKELEKYKNIDEDELLGKLSEEELKQLENVLDDLDPESAMLPAGFRQKDQTQKAATGPFDREHLLMYLEKEALEQKDREDFVPFTGEKKGRVFIPKEKPIETRKEEKVTLDPELEEALASASDTELYDLAAVLGVHNLLNNPKFDEETANNKGGKGPVRNVVKGEKVKPVFEEPPNPTNVEISLQQMKANDPSLQEVNLNNIKNIPIPTLREFAKALETNTHVKKFSLAATRSNDPVAIAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIKIDNQRQQLGTAVEMEIAQMLEENSRILKFGYQFTKQGPRTRVAAAITKNNDLVRKKRVEADRR", "text": "FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the tropomodulin family."}
{"protein": "MDNLGESPTDKGGEPGESEETRATPGALVAADTEGIPEETDRDGDADLKEAAAEESELKSQDVSDVTAAERENSSLLTPAAKKLKLDIKDKKEKKQKVDEDEIQKMQILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGETPPLQPKHMREAVRRLKSKGQIPNSKHKKITFF", "text": "FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF11, together with TAF13 and TBP, play key roles during promoter binding by the TFIID and TFIIA transcription factor complexes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF11 family."}
{"protein": "MNFKLSLVYTALFAGISVSALAETRHKANTETIEQINVQDTGIKQNGYQTTGTSVVSKAEVPVFDTPNTVNILSTKLLEDRKPESLIDALYNVSGVSQANTLGGMFDAIQKRGFGRNRDNSIMRNGLQAGPAKNFSATTETVEVLKGPASVLYGIQDPGGVELISLLKNHNKRHVMSLVEP", "text": "SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family."}
{"protein": "MEEREGTNINNNITSSFGLKQQHEAAASDGGYSMDPPPRPENPNPFLVPPTTVPAAATVAAAVTENAATPFSLTMPTENTSAEQLKKKRGRPRKYNPDGTLVVTLSPMPISSSVPLTSEFPPRKRGRGRGKSNRWLKKSQMFQFDRSPVDTNLAGVGTADFVGANFTPHVLIVNAGEDVTMKIMTFSQQGSRAICILSANGPISNVTLRQSMTSGGTLTYEGRFEILSLTGSFMQNDSGGTRSRAGGMSVCLAGPDGRVFGGGLAGLFLAAGPVQVMVGTFIAGQEQSQLELAKERRLRFGAQPSSISFNISAEERKARFERLNKSVAIPAPTTSYTHVNTTNAVHSYYTNSVNHVKDPFSSIPVGGGGGGEVGEEEGEEDDDELEGEDEEFGGDSQSDNEIPS", "text": "FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Acts redundantly with AHL4 to regulate the formation of tissue boundary between the xylem and procambium in the root meristem (PubMed:23335615). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MATTNKVYFIAGGNRGIGLSLVKELSSREGTTVFASARKPEAATELQEWSKSHPNVKTVELDVTSQQSANEAAQSVAKAVDGIDVLWLNSGICQSYYTVMEAPEEVWNAHYQTNVLGPIHVFKAFYPLLTKKKTRQVIFTSSECGSMGDFRATGFSAYGQSKAAINFTMKELSVELADEHFTFISIHPGVVKTDMNADAIKKFTETSPEMLTYLKKVTIIPEESVSSMLKVVDNLKPENNGSFYRYDGTIIPF", "text": "SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MEEWDLLNENRELTGKTHIRGEKLAPGELHLVIHVCIFNEKGQLLIQKRQKDKEGWPNYWDLSAAGSALKGETSQQAAEREVQEELGIMIDLSGTRAKFSYHFEEGFDDYWFITKDVQLSDLTLQKEEVADARFVTKEELEALRSSGEFIPYFFLNQLFNLKNATTIHF", "text": "SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MSRAHGSPRSFFPVGNPFRVMFPGGAHLSRKLQELLASYEDALALSLRKLKPEAASDVLTLSWMRLAVDCLSELHTNIANLITDLELPVSDWDDKWVDIYLNSSVKLLDICIALSSELSRLDQGQLLLQYALHVLGSESGVPSQEQLKRAEPSLREWMELVGVRCPRLVSCSATLQELAGNLSLMKVKNSVKGKVLMRALYGIESVTVFVCSIFVAVLSGSPKPLVELHVPEKFGWSQAFNDLHTAVSEELTRQLAGGSVAAVKELEEVEACAKRLHVLASTSQLEEEAANLANAVSHTEEEVMSDSIVQEGDHHCGLKLADDTTRECEVVISESIAEEGTHEAEMKKDISYEKGVAMVERISYEEHQDSNVKQANGSSDESALVVPERTSVQESKEELLNCISSMSKSAEGLRHGLDSLSKRVGDFFQIVLTGRDALLCNLRISDAASKVAEVSS", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ROH1 family."}
{"protein": "MSGIIATYLIHDDSHNLEKKAEQIALGLTIGSWTHLPHLLQEQLKQHKGNVIHVEELAEHEHTNSYLRKKVKRGIIKIEYPLLNFSPDLPAILTTTFGKLSLDGEVKLIDLTFSDELKKHFPGPKFGIDGIRNLLQVHDRPLLMSIFKGMIGRNIGYLKTQLRDQAIGGVDIVKDDEILFENALTPLTKRIVSGKEVLQSVYETYGHKTLYAVNLTGRTFDLKENAKRAVQAGADILLFNVFAYGLDVLQSLAEDDEIPVPIMAHPAVSGAYSASKLYGVSSPLLLGKLLRYAGADFSLFPSPYGSVALEKEEALAISKYLTEDDASFKKSFSVPSAGIHPGFVPFIVRDFGKDVVINAGGGIHGHPNGAQGGGKAFRTAIDATLQNKPLHEVDDINLHSALQIWGNPSYEVKL", "text": "FUNCTION: Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1- phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1- phosphate (HK-MTPenyl-1-P). SIMILARITY: Belongs to the RuBisCO large chain family. Type IV subfamily."}
{"protein": "MPSVTQRLRDPDINPCLSESDASTRCLDENNYDRERCSTYFLRYKNCRRFWNSIVMQRRKNGVKPFMPTAAERDEILRAVGNMPY", "text": "SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the CHCHD7 family."}
{"protein": "MAKDNIHPNWYPEAKVYCDGQLIMTIGSTKPELHVDIWSGNHPFFTGSQRIIDTEGRVERFMRKYKINKN", "text": "FUNCTION: Binds the 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily."}
{"protein": "MFEARLLQASLLKKILESIKDLVESANFDCSPEGISLQAMDGTHVTLINLVLRNEGFETYNCDRSLSLGLSLVSLSKILKCAGNDDTLTIRARDNESDTVTFVFESPKNDRVSDFEIKLIDIKNEQYSIRKSDYSAVIKMPSAELQRICRDLSIIGEIVTISANKEGVKFSVSGDSGSGNITIKPTSDSDVPAEQATVIESKEPVVLNFALKFLSNFTKATPLSPMVTLSMSEGIPVVVEYKIDDLGFLGFFLAPKIE", "text": "FUNCTION: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PCNA family."}
{"protein": "MALLAVRMLVLGLCVGGQAAAAGEGQSTPATCSPLCRCDEDGGADCSGRGLTSVPTGLSAFTYYLDISMNNITELPANVFRNLPYLEELRLAGNDLAFIHPEALSGLHQLKVLMLQNNQLKTVPSAALKNLNALQSLRLDANHITSVPEDSFEGLQQLRHLWLDDNSLTEVPISPLQHQSNLQALTLALNRITHIPDNAFANLSSLVVLHLHNNRIQEIGKNCFNGLDNLETLDLNFNNLKIFPEAIQMLPKLKELGFHSNNIASIPEGAFCRNSLLRTIHLFDNPLSFVGTTAFQNLSDLHSLMLRGASMMQDFPSLTGTINLESLTLTGTKIRSIPADLCEDLTVLRTVDLSYNDIEDLPSFQGCVRLQDINLQHNQIKQIDRGTFQGMTSLRVLDLSRNQIKFIHRDAFLSLSALTNLDLSLNSLASVPTAGLSALNQLKLTGNMELRNGLMSKTLPKLRSITVPYAYQCCAFVAYDSAVNPAEDDERRNAFGGEEDMERIPMVMHCSPLPGAFKPCEHLLGSWMIRLTVWFICLVALLFNCLVLAATFSPRTSSLSPSRFLVALLASANLLTGVYVAALTLLDTVTWGSFAEYGVWWETGAGCQVVGFLAVFSSEWAVLLLALAAVERCLAVRALMGKAGALRSRGERRERRRRFAIAALLLGLVSVAAACLSLYHGSAMGSPLCLPFSEGSSPGLGFTVALVLMNTLAYLLSAVVYTRLYCRLGRAQLADPEQAGSVRHIAWLIFTNCIFFCPVAAFSFAPLLAGTSNAVGGPEMAKSVTLIFFPLSACLNPVLYVCFSPSFRYDWLHLRGRGRTGGCGRLVAKTVTKGTVAGGSPVSDDGEGLSSDCGMYTKLHGDSRGMCEHCDAALHIRTSSSSGSSSSSACRHLVKSHSCPALMGNVPQCLSSEGYWPDTGTLSAQSEYGDEGDSFVSDSSEQVQACGRACFCQSRGLPLVHYSYNIPRMTD", "text": "FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May play a role in regulating the circadian rhythms of plasma lipids. Required for proper development of GnRH neurons (gonadotropin- releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland (PubMed:32493844). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MELQYISYFQPTSSVVALLLALVSILSSVVVLRKTFLNNYSSSPASSTKTAVLSHQRQQSCALPISGLLHIFMNKNGLIHVTLGNMADKYGPIFSFPTGSHRTLVVSSWEMVKECFTGNNDTAFSNRPIPLAFKTIFYACGGIDSYGLSSVPYGKYWRELRKVCVHNLLSNQQLLKFRHLIISQVDTSFNKLYELCKNSEDNHGNYTTTTTTAAGMVRIDDWLAELSFNVIGRIVCGFQSGPKTGAPSRVEQFKEAINEASYFMSTSPVSDNVPMLGWIDQLTGLTRNMKHCGKKLDLVVESIINDHRQKRRFSRTKGGDEKDDEQDDFIDICLSIMEQPQLPGNNNPSQIPIKSIVLDMIGGGTDTTKLTTIWTLSLLLNNPHVLDKAKQEVDAHFRTKRRSTNDAAAAVVDFDDIRNLVYIQAIIKESMRLYPASPVVERLSGEDCVVGGFHVPAGTRLWANVWKMQRDPKVWDDPLVFRPDRFLSDEQKMVDVRGQNYELLPFGAGRRVCPGVSFSLDLMQLVLTRLILEFEMKSPSGKVDMTATPGLMSYKVIPLDILLTHRRIKPCVQSAASERDMESSGVPVITLGSGKVMPVLGMGTFEKVGKGSERERLAILKAIEVGYRYFDTAAAYETEEVLGEAIAEALQLGLVKSRDELFISSMLWCTDAHADRVLLALQNSLRNLKLEYVDLYMLPFPASLKPGKITMDIPEEDICRMDYRSVWAAMEECQNLGFTKSIGVSNFSCKKLQELMATANIPPAVNQVEMSPAFQQKKLREYCNANNILVSAISVLGSNGTPWGSNAVLGSEVLKKIAMAKGKSVAQVSMRWVYEQGASLVVKSFSEERLRENLNIFDWELTKEDHEKIGEIPQCRILSAYFLVSPNGPFKSQEELWDDEA", "text": "FUNCTION: Bifunctional protein involved in the biosynthesis of morphinan-type benzylisoquinoline alkaloids. Required for the isomerization of (S)- to (R)-reticuline. The cytochrome P450 module is responsible for the conversion of (S)-reticuline to 1,2- dehydroreticuline while the oxidoreductase module converts 1,2- dehydroreticuline to (R)-reticuline. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: In the C-terminal section; belongs to the aldo/keto reductase family. SIMILARITY: In the N-terminal section; belongs to the cytochrome P450 family."}
{"protein": "MQGPSLSQLVLVLMGALLEAGTPREEVSSTPALPREPRTGTEGLIFHWDWNWPPPGAWPPGGPQDPLCLVTLNGTPGNGSSPFLWVVGTLSSYEQAFLEAVRHARWGPQDLANFGLCPPSLRQAALPLLQQLQAWLGEPRGQRLVVLHLEEVSWEPTPLLKFQEPLPGEASPLELALLVLYPGPGPEVTVTGAGLPGAQSLCPTRDSGFLALAVDRPERAWRGSGLALTLRRRGNGASLSTAQLQALLFGADSRCFTRMTPALLLLPPQGPVPMPAHGRVDSMPFPQPRLSPEPEEPLPSTDPFLETLTRLVRALRGPPARIPPPSLALDPGALAGFPQGQVNLSDPAALERLLNSEEPLLLLLPPPTAVTAGVPAPLQGPVTEMWASSLARRVATEFQSAAAELRGFPGLPPTATLLLARLLALCPGDRGDPGGPLRAVLLLKALQGLRTEWRWRERSGPARAQRSAGTAVSNGPCALRELSVDLRAERSVLIPETYQANNCQGTCGWPQSDRNPRYGNHVVLLLKMQARGAALARPPCCVPTAYAGKLLISLSEERISAHHVPNMVATECGCR", "text": "FUNCTION: Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation and plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles. AMH signals by binding to a specific type-II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family."}
{"protein": "MKRFLLATCLVAVLLWEAGAIPAHQVPVKTKGKHVFPEQETEKAWGTRAMEPLEKDDQLRALLPVPKQKLAATEEKHSDTMTWVETKDILSRFRNPLQGPELDLDSIYHPMSEDVQNEEVPQSRPILYRQVLHGPEEDLDHISHSLEDSGEP", "text": "FUNCTION: Lipid-binding protein which promotes lipid absorption by facilitating MTTP-mediated lipid transfer (mainly triglycerides and phospholipids) and MTTP-mediated apoB lipoprotein assembly and secretion (By similarity). Protects the gastrointestinal epithelium from irradiation-induced apoptosis (By similarity). May play an important role in maintaining normal growth homeostasis in epithelial cells (By similarity). Involved in p53/TP53-dependent cell survival after DNA damage (By similarity). SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum."}
{"protein": "MVEKSVHEINKKIEDGSVNVVTAEEMVGIVENLGVEGAAREVDVVTTGTFGAMCSSGLMLNLGHSEPPIKIQKLWFNNVEAYSGLAAVDAYLGAAQISDTRGIQYGGAHVIEDLLRGKELDVHATSYGTDCYPRKVLDTRITLDDLNEAVLLNPRNAYQKYAAATNSSKRILNTYMGELLPNFGNVTYSGAGVLSPLSNDPDYETIGMGTRIFMGGAQGYIIGNGTQHSPSSSFGTLMLKGNLKEMSSDYLRAASFAGYGTTLYMGIGIPIPILNEKIAASTAVRDEDIFTDILDYAVGSRDKPVIKQVNYAELRSGSIELEGKNTPTSSLSSFKNARKIANELKEWVKHGKFFVSMPVEKLSREGSAKSMKQTQAVPLVKDVMADFIVTIKKNQTVQDAAKKIWENSFNHLAVVSDTGELVGILTAWDISKAVAENIFDSVESVMTKKVLTCAPNEPVDLAARRLDRYGVSAMPVIDTQRKVLGIITSDNISKLLARRY", "text": "FUNCTION: Required for O-acetylhomoserine sulfhydrylase (OAHS)- independent homocysteine (Hcy) biosynthesis (PubMed:25315403, PubMed:25938369). Together with MA_1822, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine (Probable). Likely functions through persulfide intermediate (PubMed:28165724). SIMILARITY: Belongs to the L-aspartate semialdehyde sulfurtransferase family."}
{"protein": "MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIAERENQQ", "text": "FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). FUNCTION: Phosphorylation of GltX by HipA prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to multidrug resistance and persistence (PubMed:24095282, PubMed:24343429). Overexpression of GltX prevents HipA-induced growth arrest, persister formation and increases in (p)ppGpp levels (PubMed:24343429, PubMed:28430938). FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily."}
{"protein": "MSHLAELVASAKAAISQASDVAALDNVRVEYLGKKGHLTLQMTTLRELPPEERPAAGAVINEAKEQVQQALNARKAELESAALNARLAAETIDVSLPGRRIENGGLHPVTRTIDRIESFFGELGFTVATGPEIEDDYHNFDALNIPGHHPARADHDTFWFDTTRLLRTQTSGVQIRTMKAQQPPIRIIAPGRVYRNDYDQTHTPMFHQMEGLIVDTNISFTNLKGTLHDFLRNFFEEDLQIRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPEVYSGFAFGMGMERLTMLRYGVTDLRSFFENDLRFLKQFK", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily."}
{"protein": "MADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI", "text": "FUNCTION: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes. SUBCELLULAR LOCATION: Cytoplasm Nucleus. Secreted Note=Secreted by a non- classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum- Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059)."}
{"protein": "MLRLKCASQRYDWGKVGVNSIVYKLQVASENPDISHVDLPYAELWMGTHPSGSSCLWDNPHVTLAAHIQENPASLGKPSLIYFGRRLPFLFKVLSVAKALSIQAHPDKKMAVRLHAEQPDLYKDGSHKPEMAIALTDFEALLGFRPLNQILAFIQAFPELAELTTLELPSPEEKRDVQPPSIKQLYSNLMRSSPEKVESTIKSLLNRFTTGSKSVCDPPLSILGVDLQEEDVQALVDLFLRLTQAFPGDVGCLSIFFLNYIRLKSGEAIFLKANTPHAYLSGDCVECMANSDNVVRAGLTPKFKDVERLLEMLDYTPLTDSLRLGATQPIPTPEGISMKSFIPPVSEFAVDVIQFDAESRGFSLPSVPTASILLFLHGQGTITCPSTGEACSQETKFGPGFVYFVPADMIVNLVSKEDRKGSLHAFRAYVNRK", "text": "FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol- phosphate-mannose required for a number of critical mannosyl transfer reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family."}
{"protein": "MKNRIPVVLLACGSFNPITNMHLRLFEVARDHLHQTGRYQVIEGIISPVNDSYGKKDLVASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELLRSSAQMDGPDPSKTPSASAALPELKLLCGADVLKTFQTPNLWKDTHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNEISATYVRKALGQGQSVKYLLPEAVITYIRDQGLYINDGSWKGKGKTG", "text": "FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Protects against axonal degeneration following injury. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family."}
{"protein": "MARPVSDRTPAPLLLGGPAGTPPGGGALLGLRSLLQGTSKPKEPASCLLKEKERKAALPAATTPGPGLETAGPADAPAGAVVGGGSPRGRPGPVPAPGLLAPLLWERTLPFGDVEYVDLDAFLLEHGLPPSPPPPGGPSPEPSPARTPAPSPGPGSCGSASPRSSPGHAPARAALGTASGHRAGLTSRDTPSPVDPDTVEVLMTFEPDPADLALSSIPGHETFDPRRHRFSEEELKPQPIMKKARKIQVPEEQKDEKYWSRRYKNNEAAKRSRDARRLKENQISVRAAFLEKENALLRQEVVAVRQELSHYRAVLSRYQAQHGAL", "text": "FUNCTION: This transcriptional activator recognizes and binds to the sequence 5'-RTTAYGTAAY-3' found in the promoter of genes such as albumin, CYP2A4 and CYP2A5. It is not essential for circadian rhythm generation, but modulates important clock output genes. May be a direct target for regulation by the circadian pacemaker component clock. May affect circadian period and sleep regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. PAR subfamily."}
{"protein": "MQDLCEMWRHAVARVLSQLQGPAVEPVEGAQLVMEEPPEPGMGDIAFPLFLFAKRVRRSPAQLAQQLCTLLEEDTSMCAYGTPQARGPYLNVFLNKECVAAHTLDAIFAQGERYGHTQYLQGKRIMVEFSSPNTNKPLHVGHLRNNAIGESLSRIIAFCGADVFKVNIINDRGVHICKSMCAYQKFAHGKTPAHTGIKSDRFVGDWYVQFNRYAQQYPEEAEHDVRDLLQRWESADPHVRALWRTMNEWALRGIKQTYERTGISFDKLYFESETYTKGREEVRRGLACGVFYQMEDNSIWVDLSSLGLDKKALLRSDGTTMYITQDIGTAIFRAQDWPFDQLLYVVGNEQNYHFKVLFFVLRLLGYPWAQQLHHVSYGMVNLPHGRMKSREGTVVDADDILDRLHSAAEEEIAKKGRENALKHAQCIAENVAIAALHYFLLQVSPQKDMVFHPEESLSFNGNTGPYLQYMGARISSLLKKVQEDVEQKGPREVRCDPALLTHEAEWELVKALARFPACVTRAAQGHDPSVITGYLYTLSKSFSRFYHDCPILCEARPDYACARLELVRAVRIVLRTAMRLVLIPFLEEM", "text": "SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family."}
{"protein": "MKIGIADTTFSRINMGKIAIDELRKISSIPYERYTVPGIKDLPIAAKKLLEEKGCDIVITLGWVGGTQKDMLSYIVLSMGLVIVQLMTNKHVIDVTIHEDEAEDEKTLMMVAENRVREHVRNAVDLLVNPKRLQKLAGTGQRQGYPDVGPILK", "text": "SIMILARITY: Belongs to the DMRL synthase family."}
{"protein": "MATPMVSSAGGLLAMLNEPHPVLKLHALSNLNNLVDQFWPEISTSVPIIESLYEDEEFDLHQRQLAALLVSKVFYYLGELNDSLSYALGAGPLFDVSEDSDYVHTLLAKAIDEYASLRSKAVESNEMVDIDPRLEAIVERMLGKCISDGKYQQAMGIAIECRRLDKLEEAIIKSDNVQGTLSYCINVSHSFVNRREYRHEVLSLLVKVYQKLPSPDYLSICQCLMFLDEPQGVASILEKLLRSENKDDALLALQIAFDLVENEHQAFLLSVRDRLPAPKTRAVEATQAVETTIAPNENPSGDVQMADETPAQTIVHETDPVDATYAERLTKIKGILSGETSIQLTLQFLYSHNKSDLLILKTIKQSVEMRNSVCHSATIYANAIMHAGTTVDTFLRENLDWLSRATNWAKFSATAGLGVIHRGHLQQGRSLMAPYLPQGGAGGGGSPYSEGGALYALGLIHANHGEGIKQFLRDSLRSTNVEVIQHGACLGLGLSALGTADEEIYDDVKSVLYTDSAVAGEAAGISMGLLLVGTATEKASEMLAYAHETQHEKIIRGLALGIALTVYGREEGADTLIEQMTRDQDPIIRYGGMYALALAYSGTANNKAIRQLLHFAVSDVSDDVRRTAVLALGFVLYSDPEQTPRIVSLLSESYNPHVRYGAALAVGISCAGTGLSEAISLLEPLTSDVVDFVRQGALIAMAMVMVQISEASDSRVGVFRRQLEKIILDKHEDTMSKMGAILASGILDAGGRNVTIRLLSKTKHDKVTAVIGLAVFSQFWYWYPLIYFISLAFSPTAFIGLNYDLKVPKFEFMSHAKPSLFEYPKPTTVPTANTAVKLPTAVLSTSVKAKARAKKEAEQKAIAEKTSGPEKPVNESGSGKGKASTEKEGDSMQVDSPAAVEKKAPEPEPAFEILVNPARVVPAQEKYIKLLDDSRYVPVKLAPSGFVLLKDLREHEPEVLSLTDAPTSTASPATGTAAAAQGTPASAMAVDDEPQPPQAFEYAS", "text": "FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. SIMILARITY: Belongs to the proteasome subunit S1 family."}
{"protein": "MSTDSLPRSLMEQKAMELQQQLQALLDEIDQNKQESENISRESEYLCQYIGSMMAFQNRQTVPKK", "text": "SIMILARITY: Belongs to the SLO1 family."}
{"protein": "MAEEFVQQRLANNKVTIFVKYTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGGYSDLLEIDNMDALGDILSSIGVLRTC", "text": "FUNCTION: Displays thioltransferase and dehydroascorbate reductase activities. FUNCTION: Has thioltransferase and dehydroascorbate reductase activities. FUNCTION: Has thioltransferase and dehydroascorbate reductase activities. FUNCTION: Displays thioltransferase and dehydroascorbate reductase activities. SUBCELLULAR LOCATION: Virion Note=Localizes to the virion core. SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core. SUBCELLULAR LOCATION: Virion Note=Localizes to the virion core. SIMILARITY: Belongs to the glutaredoxin family."}
{"protein": "MAKESIRRRLAAILAADAVGYSRLMERDEKSTHTLLMARWKEVLEPLVGIHQGRVFKRTGDGVLVEFGSAVNAVECAAALQQAMAAANRDLPEDRAIVLRVGVNLGDIMVEDSDLFGDGVNVAARIEALADPGGVAISDGIHEYVHGRTDIDFVDSGYHEVKNIERPVHIWTWSPKDRAREPPNIAAEPPPQLPAKPSIAVLPFDNMSGDPEQGYFADGITEDIITDLSKVSGLFVIARNSSFAYKGKTPDIRKVSRELGVRYVLEGSVRRAANRIRINAQMIDGTTGGHLWAERYDRGLEDIFAVQDEVTRTIVNALRVKLTAGEEERRESRGKVDPEAYDLLVRSRQAILQFNALSSMEARRMLHRVLEIDPGMAAAHASLSIIALTDFINQWNGATPDNLTQALGLAQEAIDTDGSEPQGHYTLALALSWMRRLDEAEHAAERAIELDPNSANAYTALGTIRDFQGRHEEALALYTRAHRLDPQFDLSLHFQGRALLNLGRFDEAEVAFKRRLLLAPRSDMTRFYLACLYGRTGRHEEARGYWREVLGVNPSFSVDHLRRSLPYQDPHLMDRLVEGLREAGVSI", "text": "SIMILARITY: Belongs to the adenylyl cyclase class-3 family."}
{"protein": "MRFDNKVVVITGAGNGMGEAAARRFSAEGAIVVLADWAKEAVDKVAASLPKGRAMAVHIDVSDHVAVEKMMNEVAEKLGRIDVLLNNAGVHVAGSVLETSIDDWRRIAGVDIDGVVFCSKFALPHLLKTKGCIVNTASVSGLGGDWGAAYYCAAKGAVVNLTRAMALDHGGDGVRINSVCPSLVKTNMTNGWPQEIRDKFNERIALGRAAEPEEVAAVMAFLASDDASFINGANIPVDGGATASDGQPKIV", "text": "FUNCTION: Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency (PubMed:23666479). Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity (PubMed:23666479). Cannot use (2R,3R)-2,3- butanediol (PubMed:23666479). In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin (PubMed:23666479). No activity is detected with NADPH/NADP(+) (PubMed:23666479). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MARQKFERKKPHVNIGTIGHVDHGKTTLTAAITMAMAARGGGKGKKYDDIDSAPEEKQRGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNVVVFLNKEDQVDDAELLELVELEVRETLDNYEFPGDEIPIVPGSALLALQALSENPEITPGQNPWVDKIFKLMDTVDAYIPTPERDTEKPFLMAVEDVFSITGRGTVATGRVERGSVKVGETIEIVGLRETRTTTVTGLEMFQKTLEESVAGDNVGVLLRGIQKIDIQRGMVLAKPGSITPHTKFTAQVYILTRDEGGRHTPFFAGYRPQFYVRTTDVTGKIETFRTDDDQPTQMVMPGDRIKMEVELIQPIAIEKGMRFAIREGGRTVGAGVVSAIVL", "text": "FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily."}
{"protein": "MLKVLVVDDEMLARDELKYLLERTKEVEIIGEADCVEDALEELMQSRPDIVFLDIQLSDDNGFEIANILKKMKNPPAIVFATAYDQYALQAFEVDALDYILKPFDEERIVQTLKKYKKQKQSQIETKHEIKGTDVTVEMHKLALPIEESIVLVNIEDIVYVGLVDGKVTVKTMRETYVTHDTLVILEKKLPQVSFMRVHRSFIANINHITEIQPWFNSTYNLIMKEGSKVPVSRTYAKELKKLLRI", "text": "FUNCTION: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MALSLIFLALLVLCPSSGHSQRSPSPGYYPSSRVPTSPFDREFRTLWGSQHQRREQDVVTLWLDKSTGSGFKSLRPYRSGYFGASIKLQPGFTAGVDTSLYLSNNQEHPGDHDEVDIEFLGTTPGKPYSLQTNVFVRGSGDRNVIGREMKFTLWFDPTQDFHHYAILWNPNQIVFFVDDVPIRTYNRKNEAIFPTRPMWVYGSIWDASDWATENGRIKADYRYQPFVAKYKNFKLAGCTADSSSSCRPPSPAPMRNRGLSRQQMAALTWAQRNFLVYNYCHDPKRDHTQTPEC", "text": "FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. Involved in the accumulation of hemicelluloses. Has a high XEH activity and only a slight XET activity in vitro, but the main in planta activity seems to be XET, thus controlling aluminum sensitivity (PubMed:23204407, PubMed:23104861, PubMed:25446234). Acceptor preferences are XXXGol = XXFGol > XXLGol > XLLGol = XLFGol (PubMed:25446234). SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast Cell membrane. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 3 subfamily."}
{"protein": "MNIMDYENSKRFRRNKLEEDNISDDEMENEEWDEGFGAEEFISFDEELPEYDENNPTPTCFSRWFDTQKYHYHRKIPLPIQLPKEDKKQPKQHPLKWAKFTDETEIESTMVVIGKIPLTRKRNVTNENVSFQGVANEIVVSKNIEGTKKKRNYAFTTYKNKNKKITKPIQNQLCFSITKGIECPHYSCTYIHNYSQIEHCQYNNQCRFALQVDDELYLQNNNGKCLKRHMYESIESYLLRLEIPIYNCTSLVLQVNPHVHSDCNILRRVLQNAKNCRVAPLIWQKKKVLELKTSDDSDSENNDEDDDWKIDLF", "text": "SIMILARITY: Belongs to the IIV-6 077L family."}
{"protein": "MWLKIQVFLLAITLITLGIQAEPNSSPNNPLIEEEARACAGLYKKCGKGASPCCEDRPCKCDLAMGNCICKKKFIEFFGGGK", "text": "FUNCTION: Antagonist of L-type calcium channels (Cav1/CACNA1). Induces immediate clockwise gyration and flaccid paralysis after 6 hours at dose levels of 5 ug per mouse. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family."}
{"protein": "MGDTSPRTSVSTDGDTDHNNLMFDEGHLGIGASDSSDRSKSKMDQKTLRRLAQNREAARKSRLRKKAYVQQLENSRLKLTQLEQELQRARQQGVFISSSGDQAHSTAGDGAMAFDVEYRRWQEDKNRQMKELSSAIDSHATDSELRIIVDGVIAHYEELYRIKGNAAKSDVFHLLSGMWKTPAERCFLWLGGFRSSELLKLIASQLEPLTEQQSLDINNLQQSSQQAEDALSQGMDNLQQSLADTLSSGTLGSSSSGNVASYMGQMAMAMGKLGTLEGFIRQADNLRLQTYQQMVRLLTTRQSARALLAVHNYTLRLRALSSLWLARPRE", "text": "FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-TGACG-3'. Recognizes ocs elements like the as-1 motif of the cauliflower mosaic virus 35S promoter. Binding to the as-1-like cis elements mediate auxin- and salicylic acid-inducible transcription. May be involved in the induction of the systemic acquired resistance (SAR) via its interaction with NPR1. Could also bind to the Hex-motif (5'- TGACGTGG-3') another cis-acting element found in plant histone promoters. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family."}
{"protein": "MEGVFLKMSVVGVSPMIPVGPSSFICAIGGSVEEKSTAASLPRWVSLRRLRPLEFLRIGGKREEKGTVRDDDAVLLERRDRNRNENDNGNWVLKILEVGSIWKGKRQRSGGGGGGEEDEEEEVAEPKKKEDLCEECDFCRIDDDDEDEEKEKTVFEFSEMLSKIPVEDAQMFAKLSFLGNLAYSIPKIKPENLLKYQKLRFVTSSIEKRMSLKVEENNNGEEDEEKKKLINPAVAYRIAASAASRLFSHSKSVLPFGSSKRQDNEEASLLATADSVTAVVAAKEEVKQAVADDLKSNRSPPCEWFVCDDDKSGTRFFFIQGSDSLASWQANLLFEPVPFEDLDVLVHRGIYEAAKGIYEQMLPEVHAHLNSRGKNRAFLRFSGHSLGGSLSLLVNLMLLIRGQVPASSLLPVITFGSPCIMCGGDRLLQKLGLPKSHLLGISMHRDIVPRAFSCNYPNRAAKLLKALNGNFRNHPCLNNQNVLYSPMGKLLILQPSERFSPPHPLLPPGSGLYLLASKNTDETEKSLRAAKILFFNSPHPLEILSDRRSYGSEGKIKRNHDMSSYLKALRHVIRKELKQMKAERDQWLRKFFIINILFSGRDSLKLITRFVASRSSQLVIIFFLPIRLLIMSVYSVVFHHSQAHFSFFK", "text": "FUNCTION: Sn-1-specific phospholipase A1 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis. Hydrolyzes polyunsaturated acyl groups preferentially from chloroplastic phosphatidylglycerol (PG). May function downstream of abscisic acid (ABA), and provide a link between ABA-mediated abiotic stress responses and oxylipin and JA signalings. In vitro, possesses broad substrate specificity. Can hydrolyze the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), the sulfolipid sulfoquinovosyldiacylglycerol (SQDG), and the phoshpolipids phosphatidylcholine (PC), and phosphatidylglycerol (PG). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral membrane protein. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MNKPTLGIDLDTTLNTLDREWVKRYNEIYKDKLLPSDIKGWDIENYVKPECGKKIYDILKEPHFFRNLGVQPFAETALEELTSIFNIYIVSATHYKVCEDKGNWIKEKFPFISYQNIIFCHNKGLVHLDILIDDNPLNLENFKGNKILFDAHHNKSENRFVRARDWYEAKALCESLKDFL", "text": "FUNCTION: Dephosphorylates nucleoside monophosphates such as the 5' and 2'(3')-phosphates of deoxyribonucleotides in vitro. SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family."}
{"protein": "MSRLSRLQRQVLSLYRELLRAGRGKPGAEARVRAEFRQHASLPRSDVLRIEYLYRRGRRQLQLLRSGHATAMGTFVRPRGPTEEPVDATAPGNRLDDSDALKNPCEGTGARETRSDGR", "text": "FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit Sdhb of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF3. Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family. SDHAF1 subfamily."}
{"protein": "MTLPSGDSSITNNTNQTLNEDEKRRLRREKLAALRQKKLAEAQNGEGNKRQEGNGNGTGQGTGNVAADLTTKRNEKQKVENSFAKLNSTSIDHSSTETQATSLEEKQRLLLKRQGQRIEDWKKNRSADTASHFPQRAKENLSHTRIAITKKSTFKLPKIKRNNNKRVFGFVNEDKEGGGGKEEEDEEEEFTKKKILKIANDDARDYLNYGEKFRKPVLEEAEDDLDQFIESISKSESFVDNNNGGKQVQEQNVEEEKQQQQQQQLEQEQEQEQEQLEKLPRYLAVNNNNNEDTDEVYRYEEDFDDEFDEDDEDDINKRLSAKLNKLQNTAKELKEIDHTSIEYPKFRKHFYQVPFEMSTMDNRELDMLRLELDNVRARGKNVPPPFLTWGQLLMPESVMSVIQNDLGFAKPSPIQCQAIPIVLSGRDMIGVAKTGSGKTLSYVLPMVRHIQDQLFPKPGEGPIGLVLSPTRELALQIEKEILKFSSTMDLKVCCCYGGSNIENQISELKRGVNVIVATPGRLIDLLAANGGRITTLRRTTFVVLDEADRMFDMGFEPQIQKIFTQIRPDKQTVLFSATFPRKLEQLAKKVLHNPIEIIVGGVSVVASEISQEIILFEDTDQLMNHKIQKLEDILSRFFDLGKNTGKVLVFVEKQTDADKLVSVLLKKAIPCIAIHGGKDQIDRKHAIREFSDDQSGINVLIATSIAARGLDVRNLDLVVNFEPPSHLEDYVHRVGRTGRAGKHGEAITFVDNTQEKEISILVKALKMSSRAVDSKLQEIADKFMKKIESGEEKRSSGFGGKGLEKLQNVRETNMQLQKKMFGNFKKEDGKKSHRDLSEQVDYFGSSSSSSSFPSSSNTTTTTTTTSTASAIEIPTFEIIEGNSPETSGPDKCKFYCRVTINDLPQKVRWGIVQRESLSKIIEASKTSITTRGQFYPPQSKQTPTNDQPKLYLLIEGLTRKAVEEAAVLIRDKMLQGVEAMRLDNHSAPTGRYVV", "text": "FUNCTION: ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. Catalyzes an ATP-dependent conformational change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5 subfamily."}
{"protein": "MVMTNSPQNIGIKGIEVYIPGQAVNQSDLEKFDGIPQGKYTIGLGQTNMAFVNDREDIYSISLTVLSRLIKNYSIDTNKIGRLEVGTETLLDKSKSVKSVLMQLFPGNNDIEGIDTVNACYGGTSSVINAINWIESSSWDGRDAIVVAGDIAIYDKGAARPTGGVGAIALLIGPDAPIVFDSIRGSFMEHAYDFYKPDFTSEYPVVDGHFSLSCYVKAVDNCYKNYSKKITGDANKTVGVYDHFDFSAFHVPTCKLVTKSYARLLYNDYVSNPSKFADLIDETTRKHIDGLTYDESLTDKILEKTFVGLAKDETKKRVQPALQVPTNTGNMYTASAWVSLASLLYYVGSDNLKNKRISIFSYGSGLASTLLSVTVKGDVSAITKVLDFDYKLGDGRKIQSPEDYLAAIELREKAHLQKSFKPQGSTDNLSQGTYYLTEIDDKFRRAYAIKE", "text": "FUNCTION: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The 3-hydroxy-3-methylglutaryl- coenzyme A (HMG-CoA) reductase HMG1 finally reduces HMG-CoA to produce mevalonate (Probable). SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family."}
{"protein": "MSHPSPQAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGPTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDKEGLLSMANAGSNTNGSQFFITTVPTPHLDGKHVVFGQVIKGMGVAKILENVEVKGEKPAKLCVIAECGELKEGDDWGIFPKDGSGDSHPDFPEDADVDLKDVDKILLISEDLKNIGNTFFKSQNWEMAIKKYTKVLRYVEGSRAAAEDADGAKLQPVALSCVLNIGACKLKMSDWQGAVDSCLEALEIDPSNTKALYRRAQGWQGLKEYDQALADLKKAQEIAPEDKAIQAELLKVKQKIKAQKDKEKAAYAKMFA", "text": "FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D subfamily."}
{"protein": "MGEGHGDTFEGVSTDRLKLELLEEIHMKDVVQLSTLEIRHKIAELEANLNGDLAGSEWKTRYETQLELNDQLEKQIVSLKEKMEKMRGNPSDRLSSIRVYEKMPVESLNVLLKQLEKEKRSLESQVKEYAFRLEQESKAYHRTNNERRSYIAEMTQVSGSNQVSKRQQMDPLPRMKESPVKTGRHNSMNQKTTNAKKGPVKKVPRSNHLPKLNP", "text": "SIMILARITY: Belongs to the CCDC169 family."}
{"protein": "MKTAIFTVVLALAVFAVLSFGWEANEKALSEEFTELIHEKEAASEAEARECRYFWGECHDHMPCCDWLVCRYKWPITYNICVWNRTFPEK", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 13 (Hntx-13) subfamily."}
{"protein": "MRQPTVAGKFYPLSTKALRKEIVKCFHGLEIMSEDVIGAVVPHAGYVYSGPVAAHAFARLPKADTYVIFGPNHTGYGSPVAMSQDVWNTPFGDVETDRELGKLLAGTIIDMDEVAHRYEHSVEVQIPFLQYLFGSDFKVLPICMGMQDEDTAVEVGLEVARAVKESGKKVVFIASSDLSHYVPQEKAEKSDNYLIDAILDMDVPEIYRRKYEKDITACGYGPITAMLTAAKECGAKNTELVKYGTSGDVTGDPMVVGYAAIIVK", "text": "SIMILARITY: Belongs to the MEMO1 family."}
{"protein": "MQLLKQLFKKKFVKEEHDKKTGQEGMTLLEVIIVLGIMGVVSAGVVTLAQRAIDSQIMTKAAQSLNSIQVALTQTYRGLGNYPATADATAASKLTSGLVSLGKISSDEAKNPFNGTNMNIFSFPRNAAANKAFAISVDGLTQAQCKTLITSVGDMFPYIAIKAGGAVALADLGDFENSAAAAETGVGVIKSIAPASKNLDLTNITHVEKLCKGTAPFGVAFGNS", "text": "FUNCTION: Major component of the toxin co-regulated pilus (tcp) which is a type IV pilus essential for bacterial aggregation and subsequent colonization in the host small intestine. SUBCELLULAR LOCATION: Fimbrium. Membrane; Single-pass membrane protein."}
{"protein": "MALCARAALLLGALQVLALPGAVAQETYAQGSPSGNHSVPLLTANVNVTENTTMQVVSNQTSQISTVKPSSVLPKNVTAATVRPATIKVSTPGVSPHVTPSASKSTPKTSASPNSTQTSASMTTTAHSSLLTSVTVSATTHPTKGKGSKFDAGSFVGGIVLTLGVLSILYIGCKMYYSRRGIRYRSIDEHDAII", "text": "FUNCTION: Implicated in oncotic cell death, characterized by cell swelling, organelle swelling, vacuolization and increased membrane permeability. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the CD164 family."}
{"protein": "MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQETEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKFVEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDSLRKKSPAKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSDEIYSNGGVVLPHKEIKSNILKPEIVM", "text": "FUNCTION: Essential protein during embryogenesis (PubMed:15266054). Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. Plays an essential role in plant growth and development and cell-wall architecture. Provides GDP- mannose, used for cell wall carbohydrate biosynthesis, protein N- glycosylation, as well as for the biosynthesis of the antioxidant ascorbate. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the transferase hexapeptide repeat family."}
{"protein": "MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLNGIFGRKTGQAPGFTYTDANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE", "text": "FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. SIMILARITY: Belongs to the cytochrome c family."}
{"protein": "MEKNHSSGEWEKMKNEINELMIEGRDYAHQFGSASSQETREHLAKKILQSYHKSLTIMNYSGELDQVSQGGGSPKSDDSDQEPLVIKSSKKSMPRWSSKVRIAPGAGVDRTLDDGFSWRKYGQKDILGAKFPRGYYRCTYRKSQGCEATKQVQRSDENQMLLEISYRGIHSCSQAANVGTTMPIQNLEPNQTQEHGNLDMVKESVDNYNHQAHLHHNLHYPLSSTPNLENNNAYMLQMRDQNIEYFGSTSFSSDLGTSINYNFPASGSASHSASNSPSTVPLESPFESYDPNHPYGGFGGFYS", "text": "FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis- acting element. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group III family."}
{"protein": "MTSDVTVGPAPGQYQLSHLRLLEAEAIHVIREVAAEFERPVLLFSGGKDSIVMLHLALKAFRPGRLPFPVMHVDTGHNFDEVIATRDELVAAAGVRLVVASVQDDIDAGRVVETIPSRNPIQTVTLLRAIRENQFDAAFGGARRDEEKARAKERVFSFRDEFGQWDPKAQRPELWNLYNGRHHKGEHIRVFPLSNWTEFDIWSYIGAEQVRLPSIYFAHRRKVFQRDGMLLAVHRHMQPRADEPVFEATVRFRTVGDVTCTGCVESSASTVAEVIAETAVARLTERGATRADDRISEAGMEDRKRQGYF", "text": "FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric- sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily. SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily."}
{"protein": "MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDDEQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH", "text": "FUNCTION: Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co- chaperone of HSP70 (PubMed:18373498). Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Also reduces cellular toxicity and caspase- 3 activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Nucleus Cytoplasm, myofibril, sarcomere, Z line."}
{"protein": "MMSVVKGRLLGLGVGPGDPELITLKALRLLRAAPVVGYFVAKGKKGNAFGIIEAHLDQAQVRLPLVYPVTTEKLEPPLCYETIISDFYDTAAEQLAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLATRYESEVVPGVCSMLGGAAVLGAPLVYRNQSLSVLSGVLPEEELRRRLADADAAVVMKLGRNFDKVRRVLVELGLERRALYVERATMANQRIVPLERVEPMASPYFSLIVVPGDKWQGGAGGE", "text": "FUNCTION: Methylates precorrin-2 at the C-20 position to produce precorrin-3A. SIMILARITY: Belongs to the precorrin methyltransferase family."}
{"protein": "QEQGTNPSQEQNVPLPRNYKQALETNTPTKTSWPELVGVTAEQAETKIKEEMVDVQIQVSPHDSFVTADYNPKRVRLYVDESNKVTRTPSIG", "text": "FUNCTION: Inhibitor of subtilisin. SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine protease inhibitor) family."}
{"protein": "FAIGAIIKKFGKKLVEYAVKHKDLYAPYIKKHLCEKL", "text": "SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the ectatomin family. Ectatomin-Eq subfamily."}
{"protein": "MSIVFQIALAALVLFSFVMVVGVPVAYASPQNWDRSKPLLYLGSGIWAILVIVVALLNFLVV", "text": "FUNCTION: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbZ family."}
{"protein": "MMINTQEDKLVSAHDAEEFLRFFNCHDSALQQEATTLLTREAHLLDIQAYRTWLEHCVGSEVQYQVISRELRAASERRYKLNEAMNVYNENFQQLKVRVEHQLDSQNWSNSPKLRFTRFITNVQAAMDVNDEDLLHVRSNVVLHRARRGNQVDVFYAA", "text": "FUNCTION: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2- dihydronaphthalene. The beta subunit seems to have a structural role in the holoenzyme. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family."}
{"protein": "MSESFKVCFCCSRSFKEKTRQPPVSIKRLFEAYSRNGKMSFDELLRFVSEVQGERHAGLDYVQDIFHSVKHHNVFHHHGLVHLNAFYRYLFSDTNSPLPMSGQVHHDMKAPLSHYFVYTGHNSYLTGNQVNSRSSVEPIVQALRKGVKVIELDLWPNPSGNAAEVRHGRTLTSHEDLQKCLTAIKDNAFHVSDYPVIITLEDHLPPKLQAQVAKMLTKTYRGMLFRRVSESFKHFPSPEELKGKILISTKPPKEYLESKTVHTTRTPTVKETSWNRVANKILEEYKDMESEAVGYRDLIAIHAANCKDPSKDCLSDDPEKPIRVSMDEQWLDTMVRTRGTDLVRFTQRNLVRIYPKGTRVDSSNYDPHVGWTHGAQMVAFNMQGHGKQLWIMQGMFRGNGGCGYVKKPRILLDEHTLFDPCKRFPIKTTLKVKIYTGEGWDLDFHHTHFDQYSPPDFFVKIGIAGVPRDTVSYRTETAVDQWFPIWGNDEFLFQLSVPELALLWFKVQDYDNDTQNDFAGQTCLPLPELKSGVRAVRLHDRTGKAYKNTRLLVSFALDPPYTFR", "text": "FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein."}
{"protein": "MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTSPIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM", "text": "FUNCTION: (Microbial infection) Promotes transcriptional activation of early and late herpes simplex virus 1/HHV-1 promoters. FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy- terminal domain) of the large subunit of RNA polymerase II (RNAP II) (PubMed:9499409, PubMed:15563843). The activity of this complex is regulated by binding with 7SK snRNA (PubMed:11713533). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (By similarity). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (PubMed:16331689). Involved in early embryo development (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Nucleus Note=Nucleus in differentiating cells. SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily."}
{"protein": "MARISHQGAAKPFTAWTTIFYLLLVFIAPLAFFGTAHAQDETSPQESYGTVIGIDLGTTYSCVGVMQNGKVEILVNDQGNRITPSYVAFTDEERLVGDAAKNQYAANPRRTIFDIKRLIGRKFDDKDVQKDAKHFPYKVVNKDGKPHVKVDVNQTPKTLTPEEVSAMVLGKMKEIAEGYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRVVNEPTAAAIAYGLDKTGDERQVIVYDLGGGTFDVSLLSIDNGVFEVLATAGDTHLGGEDFDQRVMDHFVKLYNKKNNVDVTKDLKAMGKLKREVEKAKRTLSSQMSTRIEIEAFHNGEDFSETLTRAKFEELNMDLFKKTLKPVEQVLKDAKVKKSEVDDIVLVGGSTRIPKVQALLEEFFGGKKASKGINPDEAVAFGAAVQGGVLSGEEGTGDVVLMDVNPLTLGIETTGGVMTKLIPRNTVIPTRKSQIFSTAADNQPTVLIQVYEGERSLTKDNNLLGKFELTGIPPAPRGVPQIEVSFDLDANGILKVHASDKGTGKAESITITNDKGRLSQEEIDRMVAEAEEFAEEDKAIKAKIEARNTLENYAFSLKNQVNDENGLGGQIDEDDKQTILDAVKEVTEWLEDNAATATTEDFEEQKEQLSNVAYPITSKLYGSAPADEDDEPSGHDEL", "text": "FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the heat shock protein 70 family. SIMILARITY: Belongs to the heat shock protein 70 family."}
{"protein": "MAGGAREVLTLQLGHFAGFVGAHWWNQQDAALGQATDSKEPLGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLSSLKEEGGLYRDKQLDAAIAWQGKLTTHKEELYPKNPYLQDFLSAEGVLSSDGVWRVKSIPNGKGSPPLTTATTPKPLIPTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEECDYLQGFQILCDLHDGFSGVGAKAAELLQDEYSGRGIITWGLLPGPYHRGEAQRNIYRLLNTAFGLVHLTAHSSLVCPLSLGGSLGLRPEPPVNFPYLHYDATLPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSLPDSLMQFGGATPWTPLSACGEPSGTRCFAQSVVLRGIDRACHTSQLTPGTPPPSALHACTTGEEVLAQYLQQQQPGVMSSSRLLLTPCRVAPPYPHLFSSCGPPGMVLDGSPKGAAVESIPVFGALCSSSSLHQTLEALARDLTKLDLRRWASFMDAGVEHDDIAELLQELQSLAQCYQDGDSLVD", "text": "FUNCTION: Involved in the regulation of mitochondrial distribution and morphology. Required for mitochondrial fusion and mitochondrial network formation. SUBCELLULAR LOCATION: Mitochondrion outer membrane Cytoplasm. SIMILARITY: Belongs to the misato family."}
{"protein": "MSLLMITENVKLAREYALLGNYDSAMVYYQGVLDQINKYLYSVKDTHLHQKWQQVWQEINVEAKHVKEIMKTLESFKLDSTSLKAAQHELPSSEGEVWSLPVPVERRPLPGPRKRQSTQHSDPKPHSNRPGAVVRAHRPSAQSLHSDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDSTGYDKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSREEMHMPTTMEDFEMALKKVSKSVSAADIERYEKWIVEFGSC", "text": "FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. SUBCELLULAR LOCATION: Cytoplasm. Midbody Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, spindle Note=Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of CAMSAP-decorated microtubule stretches (By similarity). SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily."}
{"protein": "MKDVKRIDYFSYEELTILGGSKLPLVNFELFDPSNFEEAKAALIEKELVTENDKLTDAGFKVATLVREYISAIVNIRINDMYFAPFSYEKDEYILLSRFKNNGFQIRIINKDIAWWSIVQSYPLLMRQEKSNDWDFKQIDDETLENLNNESIDTIGRVLEIEIYNHQGDPQQSLYNIYEQNDLLFIRYPLKDKVLNVHIGVINTFIRELFGFDTDENHINKAEE", "text": "FUNCTION: Component of the type VII secretion system (Ess). Plays a role in Esx protein secretion. Plays an essential role in the processing and secretion of EssD. FUNCTION: Component of the type VII secretion system (Ess). Plays a role in Esx protein secretion. Plays an essential role in the processing and secretion of EssD. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MKMTGWKKKLCRGHHLWALGCYSLLAVVALRLSLRLKCDVDSLDLESRDFQSQRCRDVLYKNLKLPAKRSINCSGITRGDQEAVVQALLDNLEVKKKRLPFTDTYYLNITRDCEQFKAQRKFIQFPLSKEELDFPIAYSMVVHEKIENFERLLRAVYAPQNIYCVHVDVKSPETFKEAVKAIISCFPNVFMASKLVPVVYASWSRVQADLNCMEDLLQSSVPWKYLLNTCGTDFPIKTNAEMVLALKMLNGKNSMESEIPSEYKKNRWKYRYEVTDRLYLTSKMKDPPPDNLPMFTGNAYFVASRAFVQHVLENPKSQRLIEWVKDTYSPDEHLWATLQRAPWMPGSVPYHPKYHISDMTAIARLVKWQGHEGDVSMGAPYAPCSGIHQRAICIYGAGDLHWILQNHHLLANKFDPRVDDNVLQCLEEYLRHKAIYGTEL", "text": "FUNCTION: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I- branching enzyme activity by converting linear into branched poly-N- acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 14 family."}
{"protein": "MQAVVLAAGKGTRLRPLTEDKPKGMVEVDGKPILTHCFDQLVDLGAEKLVVVVGYKKEIIIQHYDDEYRGVPITYAHQREQKGLAHALLTVEDHIDEDFMLMLGDNIFNANLGDVVKRQREDRADAAFLVEEVDWDEASRYGVCVTNDYGEITEVIEKPEEPPSNLVMTGFYTFTPAIFHACHLVQPSNRGEYEISEAIDLLIRSGRTIDAIRIDGWRLDIGYPEDRDEAEQRLQEETTQATE", "text": "FUNCTION: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Involved in the biosynthesis of the hexuronic acid found at position 3 of the pentasaccharide. SIMILARITY: Belongs to the UDPGP type 2 family."}
{"protein": "MLPLLAALLAAACPLPPARGGATDAPGLSGTPPNASANASFTGEHSTPRLLASAASAPPERAGPEEAPAAPCNISVQRQMLSSLLVRWGRPRGLQCDLLLFSTNAHGRAFFAAAFHRVGPPLLIEHLGLAAGGAQQDLRLCVGCGWVRGRLRAPAGAPTALPAYPAAEPGPLWLQGEPRHFCCLDFSLEELQGEPGWRLNRKPIESTLVACFMTLVIVVWSVAALIWPVPIIAGFLPNGMEQRRTTAGAPAAAPAAVPAGTTAAAAAAAAAAAAAAAVTSGVAPK", "text": "FUNCTION: Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM158 family."}
{"protein": "MASCMRSLFSDQGRYVESFRRFLNNSTEHQCMQEFMDKKLPGIIARIGEAKAEIKILSVGGGAGEVDLQILSKVQAQYPGICINNEVVEPSAEQIVKYKELVAKTSNMENIKFSWHKETSSEYQKRMLEEEEEPPKWDFIHMIQMLYYVKDIPATLKFFHGLLAASAKILIILVSGTSGWEKLWKKYGSRLPRDDLCQYVTSSDLAQILDDLGIKYECYDLVSTMDITDCFIDGNENGDLLWDFLTETCNFSKTAPLDLKAEIMKDLQEPEFSVKKEGKVLFNNNLSFIVVEANV", "text": "FUNCTION: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. HNMT family."}
{"protein": "MVTQILGAMESQVGGGPAGPALPNGPLLGTNGATDDSKTNLIVNYLPQNMTQDEFKSLFGSIGDIESCKLVRDKITGQSLGYGFVNYSDPNDADKAINTLNGLKLQTKTIKVSYARPSSASIRDANLYVSGLPKTMSQKEMEQLFSQYGRIITSRILLDQATGVSRGVGFIRFDKRIEAEEAIKGLNGQKPLGAAEPITVKFANNPSQKTGQALLTHLYQSSARRYAGPLHHQTQRFRLDNLLNMAYGVKSPLSLIARFSPIAIDGMSGLAGVGLSGGAAGAGWCIFVYNLSPEADESVLWQLFGPFGAVTNVKVIRDFTTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGERVLQVSFKTSKQHKA", "text": "FUNCTION: RNA-binding protein that binds to AU-rich element (ARE) sequences of target mRNAs, including VEGF mRNA (PubMed:10734193, PubMed:9016658). May also bind poly-A tracts via RRM 3 (PubMed:9016658). May be involved in neuronal differentiation and maintenance (PubMed:9016658). Plays a role in the stabilization of GAP43 mRNA and in spatial learning (PubMed:11573004). SIMILARITY: Belongs to the RRM elav family."}
{"protein": "MMYQPDREPGEDSCLVLSSSSVQRCTGSQRGCMPCTWAASKAFVGIGLQACVLTSSILHIDLLTRNSTCLILMIISMYVLSLIRVPISKMETIVTVCRSIQALATLVAASVWVAGSAVKKEHLLIVVTVCILFVFIAGTQISLFYVICSANGTGTHFRASLLAIIGGCVLGVSVKLVELKDVPIGIGIAIAIIASCQDFGLALRDTCHYRIGRYACMRTFTDLGRGINYRWVTDVEAVPKIEEVAEEKVSLFKFFKEMPGVIFSPAVGTHATPIIWIVLRLVYGISNVWQTPAYVVFCLTVGHVSAMLLEQLVIRVNYTAEASSGIHSTAHAVCMVLAAFGYGVAAPLSLAFTVSGGILGALYLRKRATGARRLAATHISRWLIVCVYVAAGLCYATIITH", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the alphaherpesvirinae HHV-1 UL43 family."}
{"protein": "MVEAIYRCAKCGREVKIDLSVTRDLRCPYCGSKILYKPRPKVPRRVKAI", "text": "FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family."}
{"protein": "MAKFASIITLLFAALVVFAAFEAPTMVEAKLCERSSGTWSGVCGNNNACKNQCIRLEGAQHGSCNYVFPAHKCICYFPC", "text": "FUNCTION: Possesses antifungal activity sensitive to inorganic cations. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family."}
{"protein": "MGSLESERTVTGYAARDSSGHLSPYTYTLRNKGPEDVIVRVIYCGICHSDLVQMHNEMGMSNYPMVPGHEVVGVVTEIGSEVKKFKVGEHVGVGCIVGSCRSCSNCNGSMEQYCSKRIWTYNDVNHDGTPTQGGFASSMVVDQMFVVRIPENLPLEQAAPLLCAGVTVYSPMKHFGMTEPGKKCGILGLGGVGHMGVKIAKAFGLHVTVISSSDKKKEEALEVLGADAYLVSKDAEKMQEAAESLDYIMDTIPVAHPLEPYLALLKTNGKLVMLGVVPEPLHFVTPLLILGRRSIAGSFIGSMEETQETLDFCAEKKVSSMIEVVGLDYINTAMERLVKNDVRYRFVVDVAASNLDK", "text": "FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH- dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MTSSMSPAPAPAYAQVMEDMEKGKELAAQLQGLLRDSPEAGRFVDQILHTFSRAMRALDKAAVSAAGGEGSEVQSEVTCGGGASAGGKRKAPAANRKANCRRRTQQSSGNTVVVKNLDDGQAWRKYGQKEIQNSKHPKAYFRCTHKYDQMCTAQRQVQRCDDDPASYRVTYIGEHTCRDPATAPIIAAHVIHQVAAGDDDDGCGGLHAGSRLISFVAAPAAPVDAAAAPTTSTITTVTAPGPLLQPLKVEGGIGSSDQEEVLSSLTPGSSAARGGGVAGPFGPDQGDVTSSLHWSYDAVAGMEFFKNDEVVFDLDDIMGLSF", "text": "FUNCTION: Transcriptional activator involved in defense responses against pathogens (PubMed:19700558). Acts as positive regulator of defense responses against the rice blast fungus Magnaporthe oryzae (PubMed:19700558). Acts as positive regulator of defense responses against the bacterial blight Xanthomonas oryzae pv oryzae (Xoo) and the bacterial streak Xanthomonas oryzae pv oryzicola (Xoc) (PubMed:19700558). Acts as positive regulator of abscisic acid (ABA) signaling that suppresses growth of seedlings (PubMed:21725029). Acts as negative regulator of salt stress response (PubMed:21725029). Acts as negative regulator of cold stress response (PubMed:21725029). Acts as negative regulator of drought stress response (PubMed:21725029). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group III family."}
{"protein": "MKDSLVLLGRVPAHPDSRCWFLAWNPAGTLLASCGGDRRIRIWGTEGDSWICKSVLSEGHQRTVRKVAWSPCGNYLASASFDATTCIWKKNQDDFECVTTLEGHENEVKSVAWAPSGNLLATCSRDKSVWVWEVDEEDEYECVSVLNSHTQDVKHVVWHPSQELLASASYDDTVKLYREEEDDWVCCATLEGHESTVWSLAFDPSGQRLASCSDDRTVRIWRQYLPGNEQGVACSGSDPSWKCICTLSGFHSRTIYDIAWCQLTGALATACGDDAIRVFQEDPNSDPQQPTFSLTAHLHQAHSQDVNCVAWNPKEPGLLASCSDDGEVAFWKYQRPEGL", "text": "FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins (PubMed:17937914, PubMed:23891004). As a CIA complex component, interacts specifically with CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur protein assembly, depending of its interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004). Seems to specifically modulate the transactivation activity of WT1 (PubMed:9556563). As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (PubMed:20797633). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the WD repeat CIA1 family."}
{"protein": "MSAWTMGAQGLDKRGSFFKLIDTIASEIGELKREMVQTDISRENGLEPSETHSMVRHKDGGYSEDKDGKTCPRDSGYDSLSNRLSILDRLLHTHPIWLQLSLSEEEAAEVLQAQPPGIFLVRKSSKMQKKVLSLRLPCEFGAPLKEFTIKESTYTFSLEGSGISFADLFRLIAFYCISRDVLPFTLKLPYAISTAKTESQLEELAQLGLNFWSSSADNKPLNSPPPHRPLPSAGICPASLRQLCLINGVHSIKTRTPSELECSQTNGALCFINPLFLKVHSQDLSTGPKRPSTRTPNANGTERPRSPPPRPPPPAINSLHTSPGLSRTEPQTSMPETVNHSKHGNVALLGTKPTPIPPPRLKKQASFLEAESSAKTLTARRPSRRSEPEPELELELEMGTAGHAGGAPPRDAPGDCTRAPPPGSESQPPPCHGARQRLSDMSLSTSSSDSLEFDRSMPLYGYEADTTSSLEDYEGESDQETMAPPIKSKKKRNSSFVLPKLVKSQLRKMSGVFSSFMTPEKRMVRRIAELSRDKCTYFGCLVQDYVSFLKENKECHVSSTDMLQTIRQFMTQVKNYLSQSSELDPPIESLIPEDQIDVVLEKAMHKCILKPLKGHVEAMLKDFHTADGSWKQLKENLQLVRQRNPQELGVFAPTPDLMELEKIKLKFMTMQKMYSPEKKVMLLLRVCKLIYTVMENNSGRMYGADDFLPVLTYVIAQCDMLELDTEIEYMMELLDPSLLHGEGGYYLTSAYGALSLIKNFQEEQAARLLSSEARDTLRQWHKRRTTNRTIPSVDDFQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQLCAEKFKVEDPEEYSLFLFVDETWQQLAEDTYPQKIKAELHSRPQPHIFHFVYKRIKSDPYGVIFQNGEDLTPS", "text": "FUNCTION: Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RIN (Ras interaction/interference) family."}
{"protein": "MLQPQETFSNPALRDEDKHLGNLWASKKSLYKNPAHLAQQQDPWSRLSSTPTATSRSRDTFFDSKIPKDDLDFRLATLYNHHTGAFKNKTEILLHQETIEDIQGTKIQFPGECFHAPSAPITSRTTIRHWINPKKESIHSIQGSIVSPHTAATNGGYSRKNDGGFFST", "text": "FUNCTION: May play an important role for the maintenance of myelin-axon integrity (PubMed:31199454). May affect intracellular Ca(2+) homeostasis. FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). May play an important role for the maintenance of myelin-axon integrity (PubMed:31199454). May affect intracellular Ca(2+) homeostasis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm Cytoplasm, cytoskeleton."}
{"protein": "MGCIKSKENKSPAIKYTPENLTEPVSPSASHYGVEHATVAPTSSTKGASVNFNSLSMTPFGGSSGVTPFGGASSSFSVVSSSYPTGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKSGYIPSNYVVPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEVRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL", "text": "FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis (By similarity). Catalyzes phosphorylation of organic cation transporter OCT2 which induces its transport activity (PubMed:26979622). SUBCELLULAR LOCATION: Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytosol Note=Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily."}
{"protein": "MGTAELKIILEFSAGAELLFGNIKRRQLALDGTKKWNIANLLKWMHANILTERPELFLQGDTVRPGILVLINDTDWELLGELDYELQPNDNVLFISTLHGG", "text": "FUNCTION: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as Jafrac1, Ciao1, Eip71CD and GILT1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the URM1 family."}
{"protein": "MRRIVCPPVLFLSASLLTGCDFSGIFASIQSEVPLKIPSIRGVVTGLVKCNNKLYACAGQLWEKDASKSEGKWTAVNFLPGKKITSIVSKGACVYACVSGEGVYTYTSNGAGRTGGTTTPSTVLGKTNGAIRIGGSDNPFLQMPCELSSGSSGGGGGGSGSSSDGGIKNGSDENVLGSGTGYVVTTKAVYTKSNSSGTSCTYTKDGTFTATTSPILGCTSDGKGCFYVLDGTDVHCRTVQASGGGNGAHCAVASGSATSCKVAHTVTNPLCIAHVKNGQTEFLLIGGSQGYKEIKLETGSGSGTGCLKAENVRGPEQWGEDSVTPKDRVSQYEGTIGRFAISDIYTVESTSGAGGTNGGTNKPDVYVVVGDSQDGYTGLWRFDAQKKEWNRE", "text": "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the TP013X lipoprotein family."}
{"protein": "MTASVVRIEDKLYQNRYLVDAGRPHIKVRQHQSPSPNLLALTVVCPAKCYEVNEDGQVEVIADGCMECGTCRVLCEESGDIDWSYPRGGFGVLFKFG", "text": "FUNCTION: Could be a 3Fe-4S cluster-containing protein. SIMILARITY: To ferredoxins from P.putida and C.tartarivorum, ferredoxin I from A.vinelandii, ferredoxin II from D.desulfuricans."}
{"protein": "MAFLMHLLVCVFGMGSWVTINGLWVELPLLVMELPEGWYLPSYLTVVIQLANIGPLLVTLLHHFRPSCLSEVPIIFTLLGVGTVTCIIFAFLWNMTSWVLDGHHSIAFLVLTFFLALVDCTSSVTFLPFMSRLPTYYLTTFFVGEGLSGLLPALVALAQGSGLTTCVNVTEISDSVPSPVPTRETDIAQGVPRALVSALPGMEAPLSHLESRYLPAHFSPLVFFLLLSIMMACCLVAFFVLQRQPRCWEASVEDLLNDQVTLHSIRPREENDLGPAGTVDSSQGQGYLEEKAAPCCPAHLAFIYTLVAFVNALTNGMLPSVQTYSCLSYGPVAYHLAATLSIVANPLASLVSMFLPNRSLLFLGVLSVLGTCFGGYNMAMAVMSPCPLLQGHWGGEVLIVASWVLFSGCLSYVKVMLGVVLRDLSRSALLWCGAAVQLGSLLGALLMFPLVNVLRLFSSADFCNLHCPA", "text": "FUNCTION: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism (PubMed:20463145, PubMed:22273710, PubMed:24264046, PubMed:27702554). Humans are unable to synthesize vitamin B2/riboflavin and must obtain it via intestinal absorption (PubMed:20463145). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cell membrane. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Multi-pass membrane protein Nucleus membrane; Multi- pass membrane protein. Cytoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SIMILARITY: Belongs to the riboflavin transporter family."}
{"protein": "MEGWQRAFVLHSRPWSETSLMLDVFTEESGRVRLVAKGARSKRSTLKGALQPFTPLLLRFGGRGEVKTLRSAEAVSLALPLSGITLYSGLYINELLSRVLEYETRFSELFFDYLHCIQSLAGVTGTPEPALRRFELALLGHLGYGVNFTHCAGSGEPVDDTMTYRYREEKGFIASVVIDNKTFTGRQLKALNAREFPDADTLRAAKRFTRMALKPYLGGKPLKSRELFRQFMPKRTVKTHYE", "text": "FUNCTION: Involved in DNA repair and RecF pathway recombination. FUNCTION: Involved in DNA repair and RecF pathway recombination. FUNCTION: Involved in DNA repair and RecF pathway recombination. SIMILARITY: Belongs to the RecO family. SIMILARITY: Belongs to the RecO family."}
{"protein": "MDVGADEFEQSLPLLQELVAGADFVGLDIEFTGLRSNLSRPQQISLFDLPSEWYLKTRQSVQQFTICQIGLSMFSSIEGESNKYVAHSCNFFLFPTTFGILDSEFSFQASSVQFLNQYGFDYNKFLKNGIPYMNEEQEKKIKHSILRGNWRVRSSLDKDQIKVVIDKVTQWLDLAEEGDQMTLPGIAGFQAFEVQLVLRQALPNIWTVLKEEWVIVKKVSQPQRWYLEHASCDQVSCWKEQILLSARGFSVFFQMLVKAQKPLVGHNMMMDLLHLHEKFFRPLPESYDQFKQNIHSLFPVLIDTKNVTKDIWKELRFPRVSNLLEVYEVLSSNLNPTKDSGPVIIHARQCKKYAETKCPHEAAYDAFLCGSVLLKVAHLLLQRVHGNGAVHEPAFPQYLDVLAPYVNQVNLIRAGVPKINFSGPDYPSIRPPVLILTVKRWPGVSEQQVYREFQNLCKFDVRRFTRSQFLLLTNKFKDARSVLKEYRNHPTLQVSLYRSWRHSPNITCLLQVCSIVTTWAMIAFLLGRPMP", "text": "FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails (PubMed:27515512). Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development (PubMed:27515512). May act as a regulator of multipotency in embryonic stem cells (PubMed:27515512). Is a critical factor for proper spermatogenesis, involved in pre-piRNAs processing to generate mature piRNAs (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Note=Localizes mainly in the endoplasmic reticulum. SIMILARITY: Belongs to the CAF1 family."}
{"protein": "MDFVKELKSSQDYMNNELTYGAHNYDPIPVVLKRGKGVFVYDIEDRRYYDFLSAYSSVNQGHCHPDILNAMINQAKKLTICSRAFFSDSLGVCERYLTNLFGYDKVLMMNTGAEASETAYKLCRKWGYEVKKIPENSAKIIVCNNNFSGRTLGCVSASTDKKCKNNFGPFVPNFLKVPYDDLEALEKELQDPNVCAFIVEPVQGEAGVIVPSDSYFPGVASLCKKYNVLFVADEVQTGLGRTGKLLCTHHYGVKPDVILLGKALSGGHYPISAILANDDVMLVLKPGEHGSTYGGNPLAAAICVEALKVLINEKLCENADKLGAPFLQNLKEQLKDSKVVREVRGKGLLCAIEFKNDLVNVWDICLKFKENGLITRSVHDKTVRLTPPLCITKEQLDECTEIIVKTVKFFDDNL", "text": "FUNCTION: The enzyme has a very narrow substrate specificity and can only catalyze the transamination of alpha-ketoglutarate with ornithine or N-acetylornithine and, to a lesser extent, of glutamate-5- semialdehyde with glutamate and alanine. FUNCTION: The enzyme has a very narrow substrate specificity and can only catalyze the transamination of alpha-ketoglutarate with ornithine or N-acetylornithine and, to a lesser extent, of glutamate-5- semialdehyde with glutamate and alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family."}
{"protein": "MRKIGLAWQIFIGLILGIIVGAIFYGNPKVATYLQPIGDIFLRLIKMIVIPIVISSLVVGVASVGDLKKLGKLGGKTIIYFEIITTIAIVVGLLAANIFQPGTGVNMKSLEKTDIQSYVDTTNEVQHHSMVETFVNIVPKNIFESLTKGDMLPIIFFSVMFGLGVAAIGEKGKPVLQFFQGTAEAMFYVTNQIMKFAPFGVFALIGVTVSKFGVESLIPLSKLVIVVYATMVFFIFVVLGGVAKLFGINIFHIIKILKDELILAYSTASSETVLPKIMEKMENFGCPKAITSFVIPTGYSFNLDGSTLYQALAAIFIAQLYGIDMPISQQISLLLVLMVTSKGIAGVPGVSFVVLLATLGTVGIPIEGLAFIAGIDRILDMARTAVNVIGNSLAAIIMSKWEGQYNEEKGKQYIAQLQQSA", "text": "FUNCTION: This carrier protein is part of the Na(+)-dependent, binding- protein-independent glutamate-aspartate transport system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family."}
{"protein": "MADKSHVNNVPMQGNGAYSSHAALQHEAMLKALPLFRAAAEAISKVDSTRVAIVEYGSAHGNNSLEPMEAILKSIHARSLELLFSDRPENDFCTLSKTVTEWADGLVENQLLHPLFISMIPRSFYQQVIPPKSAHLGFSLAALHHLDHVPQPTEDGQDESKLLQRQAHVDLATFLKLRSKEIVSGGSLILSFVGQASAGYENYGGPVDACRNAMIQMVQQDKIPVSVAQAFRVPTYNRTLSDVKKLMDEFTQIWKVHDLFEDDVMHPAFYELKIQSNPSQEASHKYAEIVIDWMMAVCSGYFTKALQVGSQGGYTKEEEESLLQDWVTRTKELFIRDHKDEEVICSFIYIRLERL", "text": "FUNCTION: Methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:17121404, PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The roles of the other FUS members are yet undetermined (By similarity). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl- coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure (PubMed:17121404). The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20- hydroxy-prefusarin (By similarity). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (By similarity). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (By similarity). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (By similarity). SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family."}
{"protein": "MLARMLNTTLSACFLSLLAFSSACYFQNCPRGGKRAISDMELRQCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAVGICCSDESCVAEPECHDGFFRLTRAREPSNATQLDGPARALLLRLVQLAGTRESVDSAKPRVY", "text": "FUNCTION: Neurophysin 2 specifically binds vasopressin. FUNCTION: Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the vasopressin/oxytocin family."}
{"protein": "MSVPLILTLLAGAATFIGAILGVIGQKPSNRVLAFSLGFAAGIMLLISLMEMLPAALRTDGMSPVMGYGMFVVGLLGYFALDKMLPHAHPQDLMQKNAKPTRGNIKRTAILLTLGISLHNFPEGVATYVTASNNLELGFGIALAVALHNIPEGLAVAGPVYAATGSKRTAILWAGISGLAEILGGVLTWLILGSMISPVVMAAIMAAVAGIMVALSVDELMPLAKEIDPNNNPSYGVLCGMSVMGLSLVLLQTAGFG", "text": "FUNCTION: Mediates zinc uptake. May also transport other divalent cations. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. ZupT subfamily."}
{"protein": "GIFLDKLKNFAKGVAQSLLNKASCKLSGQC", "text": "FUNCTION: Shows antibacterial activity against representative Gram- negative and Gram-positive bacterial species, and hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily."}
{"protein": "MATQMVNQSTGNSLFCTSTYSNISLDNDMYGLHDLSKADMAAPRLIMLANVALTGELSSGCCDYTPEGERQMAELTTVNDNSFSDSEGDRLEDSPSMDIQSHNFIMEMEPAECSKEGTSENDGTLLSNTLEVEVQKDKRTPSPTDDKYKCVKSKPFRCKPCQYKAESEEEFVHHIKIHSAKIYVDNDSNKKAQGNEADSSISEESDVSKGPIQCDRCGYNTNRFDHYLAHLKHHNKAGENERVYKCTICTYTTVSEYHWKKHLRNHYPRILYTCSQCSYFSDRKNNYIQHIRTHTGERPYQCILCPYSSSQKTHLTRHMRTHSGEKPFKCEQCSYVASNQHEVTRHARQVHNGPKPLTCPHCDYKTADRSNFKKHVELHVNPRQFLCPVCDYAASKKCNLQYHIKSRHSGCTNITMDVSKVKLRTKKGDIGVADVDANKQTENGNIIDKSVEETVKAEKRESCGKAKKSIVNLVDGQVAKKRRLSSTQKKIKTSDARPEKILDKSRKSSCVKRKSDLLENSNDTQTSTV", "text": "FUNCTION: Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells (By similarity). Plays a role in the early development of the nervous system and is required for proper patterning of the neuroectoderm during gastrulation. This involves the correct speciation of the neuroepithelial domain and adequate development of the non-neural ectoderm (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm."}
{"protein": "MDSLNQTRVTEFVFLGLTDNRVLEMLFFMAFSAIYMLTLSGNILIIIATVFTPSLHTPMYFFLSNLSFIDICHSSVTVPKMLEGLLLERKTISFDNCITQLFFLHLFACAEIFLLIIVAYDRYVAICTPLHYPNVMNMRVCIQLVFALWLGGTVHSLGQTFLTIRLPYCGPNIIDSYFCDVPLVIKLACTDTYLTGILIVTNSGTISLSCFLAVVTSYMVILVSLRKHSAEGRQKALSTCSAHFMVVALFFGPCIFIYTRPDTSFSIDKVVSVFYTVVTPLLNPFIYTLRNEEVKSAMKQLRQRQVFFTKSYT", "text": "FUNCTION: Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanethiol (MTMT) and bis(methylthiomethyl) disulfide (By similarity). Also binds odorants cis-cyclooctene and tert-butyl mercaptan (By similarity). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MSLQKCQEEWSEIEKEFQQLQETHKVYKQKLEELNSLQNLCSSCINKHKRRLTEFKGNLHGLKRTSNLEEKELVQQIDGTIKERRNAFFDMEAYLPKKNGLYLNLVLGNVNVTLLSTQAKFAYKDEYEKFKLYLTIILLLGAITCRFVLNYRVTDEVFNFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPDGLMYQIFRNQFLAFSIFQSCVQFLQYYYQSGCLYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLYNAITLFGLSRHDACKEWQVFVLALTFLLLFLGNFLTTLKVVHTKFQKNKLKKP", "text": "FUNCTION: Necessary for efficient adipogenesis. Does not show ion channel activity. SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM120 family."}
{"protein": "MVPHLLLLCLLPLVRATEPHEGRADEQSAEAALAVPNASHFFSWNNYTFSDWQNFVGRRRYGAESQNPTVKALLIVAYSFIIVFSLFGNVLVCHVIFKNQRMHSATSLFIVNLAVADIMITLLNTPFTLVRFVNSTWIFGKGMCHVSRFAQYCSLHVSALTLTAIAVDRHQVIMHPLKPRISITKGVIYIAVIWTMATFFSLPHAICQKLFTFKYSEDIVRSLCLPDFPEPADLFWKYLDLATFILLYILPLLIISVAYARVAKKLWLCNMIGDVTTEQYFALRRKKKKTIKMLMLVVVLFALCWFPLNCYVLLLSSKVIRTNNALYFAFHWFAMSSTCYNPFIYCWLNENFRIELKALLSMCQRPPKPQEDRPPSPVPSFRVAWTEKNDGQRAPLANNLLPTSQLQSGKTDLSSVEPIVTMS", "text": "FUNCTION: G-protein coupled receptor for PEN, a neuropeptide produced from the precursor protein, proSAAS (encoded by PCSK1N). Acts through a G(i)- and G(q)-alpha-alpha-mediated pathway in response to PEN (PubMed:27117253). Plays a role in food intake and body weight regulation. May contribute to the regulation of anxiety-related behaviors (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Colocalizes with GPR171 in the paraventricular nucleus. Colocalizes with the ghrelin receptor GHSR1A in the hypothalamus. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MASSSEKTPLIPSDEKNDTKEESKSTTKPESGSGAPPSPSPTDPGLDFNAFDFSGMAGILNDPSIKELAEQIAKDPSFNQLAEQLQRSVPTGSHEGGLPNFDPQQYMQTMQQVMENPEFRTMAERLGNALVQDPQMSPFLEALGNPAASEQFAERMAQMKEDPELKPILAEIDAGGPSAMMKYWNDKDVLAKLGEAMGIAVGADQTVAAEPEEAEEGEEEESIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGEVRCAQVLLDAGANANAIDKNKNTPLHYAAGYGRKECVSLLLENGAAVTQQNMDNKNPIDVARLNNQLDVVKLLEKDAFL", "text": "FUNCTION: Exhibits chaperone activity toward chloroplast outer envelope membrane, mitochondrion outer membrane, endoplasmic reticulum membrane and peroxisomal proteins, by recruiting specific proteins containing a single transmembrane associated with an AKR2A-binding sequence (ABS) and subsequently binding glycolipids (e.g. monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG)) present in the membrane of the target organelle. SUBCELLULAR LOCATION: Cytoplasm Nucleus Plastid, chloroplast outer membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "DDCGGLFSGCDSNADCCEGYVCRLWCKYKL", "text": "FUNCTION: Inhibitor of voltage-gated potassium channels of the Kv4/KCND family (By similarity). Blocks calcium channels (Cav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 19 (HpTX2) subfamily."}
{"protein": "MDGDSSTTDASQLGIAGDYIGGSHYVIQPHDDTEDSMNDHEDTNGSKESFREQDIYLPIANVARIMKNAIPQTGKIAKDAKECVQECVSEFISFITSEASERCHQEKRKTINGEDILFAMSTLGFDSYVEPLKLYLQKFREAMKGEKGIGGTVTTGDGLSEELTEEAFTNQLPAGLITTDGQQQNVMVYTTSYQQISGVQQIQFS", "text": "FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NFYB/HAP3 subunit family."}
{"protein": "MSLNLVSEQLLAANGLKHQDLFAILGQLAERRLDYGDLYFQSSYHESWVLEDRIIKDGSYNIDQGVGVRAISGEKTGFAYADQISLLALEQSAQAARTIVRDSGDGKVQTLGAVEHSPLYTSVDPLQSMSREEKLDILRRVDKVAREADKRVQEVTASLSGVYELILVAATDGTLAADVRPLVRLSVSVLVEEDGKRERGASGGGGRFGYEFFLADLDGEVRADAWAKEAVRMALVNLSAVAAPAGTMPVVLGAGWPGVLLHEAVGHGLEGDFNRRGTSVFSGQVGELVASELCTVVDDGTMVDRRGSVAIDDEGTPGQYNVLIENGILKGYMQDKLNARLMGMTPTGNGRRESYAHLPMPRMTNTYMLPGKSTPQEIIESVEYGIYAPNFGGGQVDITSGKFVFSTSEAYLIENGKVTKPVKGATLIGSGIETMQQISMVGNDLKLDNGVGVCGKEGQSLPVGVGQPTLKVDNLTVGGTA", "text": "FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA) (By similarity). FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA). SIMILARITY: Belongs to the peptidase U62 family."}
{"protein": "MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHTDDSRNPDCKIKIAHGTTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG", "text": "FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib. FUNCTION: This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the peptidase T1B family."}
{"protein": "MSLATIAENYMMHNETQRAIVPYVPPPYAYANAPTLGGQAGEMESMSLGILNQAMSSTTGASGALKDEKAAFGAMAEALRDPEPIRQIKKHVGLRTLKHLKIELASMRRRYAILRVVILMSGCVTMATSMAGGLTIIDKDIYQDLNGDGWLSKTIHGLNLLCTTMLLAAGKISDKIQEEISRTKRDIAKIESYVSAASMSWSGDTSVPLKEVKYGDS", "text": "FUNCTION: May play a role in the release of virions from infected cells. SIMILARITY: Belongs to the orbivirus NS3 family."}
{"protein": "MHLARFPRRFIAHLPTPLERLDRLSAELGGPEIWIKRDDCTGLSTGGNKTRKLEFLMAEAELQGAEIVMTQGATQSNHARQTAAFAAKLGMKCHILLEDRTGSNEANYNHNGNVLLDHLHGATTEKRPGGGDMNAEMEKLADEWRADGKKVYTIPGGGSNPTGALGYVNCAFELLAQANDGGLKIDHIVHATGSAGTQAGLITGLKAMNAQIPLLGIGVRAPKPKQEENVYNLACATAEKLGCPGVVAREDVVANTDYVGQGYGIPTESGMEAIKMFAELESILLDPVYSAKGAAGFIDLIRKGHFKKGERVVFLHTGGAAALFGYDGAFDFSSRWVG", "text": "FUNCTION: Catalyzes the desulfonation and deamination of L-cysteate, yielding pyruvate, sulphite and ammonium. Involved in sulfolactate degradation. SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase family."}
{"protein": "MSERKVLNKYIPPDYDPSIRPPKKKKKFQGPNGGKLTVRLMTPFSMRCHTCGEYIYKGKKFNARKEKTGEKYFSIDILRFYIRCTRCAAEITFITDPKHADYAAESGASRNYEPWHEKRLQEYEENELAERNDIPEEDEMEKLEQKTLDTKRQMQISDALDELREKSARRSRVNIDDAIALLKEDAYGSIEEEESKKRKFEEEEIDREAKSLFSSQDGEIIRRLNAETTVEKELPKPIDLVSEKLATSNIPNFQPPKYAKRKMEKKKVLV", "text": "FUNCTION: Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily."}
{"protein": "MSIPFSNTHYRIPQGFGNLLEGLTREILREQPDNIPAFAAAYFESLLEKREKTNFDPAEWGSKVEDRFYNNHAFEEQEPPEKSDPKQEESQIPGKEEEASVTILDSSEEDKEKEEVAAVKIQAAFRGHVAREEVKKMKTDSLQNEEKEENK", "text": "FUNCTION: Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates (By similarity). SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein."}
{"protein": "MSSHTATKYDVFLSFRGHDTRHNFISFLYKELVRRSIRTFKDDKELENGQRFSPELKSPIEVSRFAVVVVSENYAASSWCLDELVTIMDFEKKGSITVMPIFYGVEPNHVRWQTGVLAEQFKKHASREDPEKVLKWRQALTNFAQLSGDCSGDDDSKLVDKIANEISNKKTIYATI", "text": "FUNCTION: Disease resistance protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via a direct or indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth (By similarity). SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MDSGSGFDPDTGNNKGNGSGGGNGYGERKFGAFFKRVEPFLPKKDLNPRDLRSWAKKTGFVSDYSGETSTSTRTKFGESSDFDLPKGRDQVVTGSSHKTEIDPILGRNRPEIEHVTGSEPVSREEEERRLNRNEATPETENEGGKINKDLENGFYYPGGGGESSEDGQWPKPILMKFGLRDNPGFVPLIYYGLQHYLSLVGSLVFIPLVIVPAMDGSDKDTASVISTMLLLTGVTTILHCYFGTRLPLVQGSSFVYLAPVLVVINSEEFRNLTEHKFRDTMRELQGAIIVGSLFQCILGFSGLMSLLLRFINPVVVAPTVAAVGLAFFSYGFPQAGTCVEISVPLILLLLIFTLYLRGVSLFGHRLFRIYAVPLSALLIWTYAFFLTVGGAYDYRGCNADIPSSNILIDECKKHVYTMKHCRTDASNAWRTASWVRIPYPFQWGFPNFHMRTSIIMIFVSLVASVDSVGTYHSASMIVNAKRPTRGIVSRGIALEGFCSLLAGIWGSGTGSTTLTENIHTINITKVASRRALVIGAMFLIVLSFLGKLGAILASIPQALAASVLCFIWALTVSLGLSNLRYTQTASFRNITIVGVSLFLGLSIPAYFQQYQPLSSLILPSYYIPFGAASSGPFQTGIEQLDFAMNAVLSLNMVVTFLLAFILDNTVPGSKEERGVYVWTRAEDMQMDPEMRADYSLPRKFAQIFGCRCC", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family."}
{"protein": "MLYAKALSIGDEIGFFSPSSPATAFAPNRFQRAKAYLKAQGFELVEGSLTGKSDYYRSGSIRERAEELNQLIRDPNVRCIMPTIGGNNSNSLLPYIDYEALRNDPKIIIGYSDVTALLLGIYAQTGLITFYGPALVASFGEYPPLVDETFHSFIDLLCSETNQYQYTMPSSWTDIKHDWETQHSAKPVYPNEWQFIGKGKVTGRIIGGNLNTMAGIWGSRYMPEIKVGDILLIEDSLKGIENVERSFAHLAACGVFERVSAIILGKHELFDNKGTGRTPLDVLIEVLADKNVPIFYGFDSCHTHPMLVTPLGVRGTIDFDNHTFKLEDRWVKAK", "text": "SIMILARITY: Belongs to the peptidase S66 family."}
{"protein": "MESSRVVVGGGLPLANRRNSSFAKPKIQQGTFLPLSRINNVSAPQKCSLHTNPNPMFPFVTRRKSQTNPDCGVVKLGEEDDSCSSLDKLPEVNGVHTGVARPVDIKRELVMLSLPAIAGQAIDPLTLLMETAYIGRLGSVELGSAGVSMAIFNTISKLFNIPLLSVATSFVAEDIAKIAAQDLASEDSQSDIPSQGLPERKQLSSVSTALVLAIGIGIFEALALSLASGPFLRLMGIQSMSEMFIPARQFLVLRALGAPAYVVSLALQGIFRGFKDTKTPVYCLGIGNFLAVFLFPLFIYKFRMGVAGAAISSVISQYTVAILMLILLNKRVILLPPKIGSLKFGDYLKSGGFVLGRTLSVLVTMTVATSMAARQGVFAMAAHQICMQVWLAVSLLTDALASSGQALIASSASKRDFEGVKEVTTFVLKIGVVTGIALAIVLGMSFSSIAGLFSKDPEVLRIVRKGVLFVAATQPITALAFIFDGLHYGMSDFPYAACSMMVVGGISSAFMLYAPAGLGLSGVWVGLSMFMGLRMVAGFSRLMWRKGPWWFMHTSDKRLA", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MSLRIILKRDFSQCIRVLESGSKSPTIANRFQAQYGNKNNNMKRNTANNGTGNGNRFHNKYNNESRRPYPKTKYQQQQQQQQQQRKPQQHQQYIIDPRKIKFDNGTESARNAIEEIFNRVNQLQRNYQIQLITDSGLKKCHLSEILQKLDLSINGLQLIDKSTTTTTTTTTTTTTTTNTSDEDLPLIKIITVRDMINQYSTYLNNLKQLELIKLGSSKTLKTLDIKLKLEQKKSTTKEILMKWSINNNDFKLQKTNEIKKLINNNGGNGKSFLINMVYNKRNTNKPINTIFKRRSNTEEDEQELIEIELKRRQLLIENLQSLLTELNCKWTIEGDINTKMTFNVTPKGQPTTIEPSTTTNIVDEEIEDYNNNNNNDDGDCDEKKMNRTERKKRKSEQQKQKQKQKQQSKTNTNSNTAKEEDLDALYSFKIED", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM23 family."}
{"protein": "IACAPRFSLCNSDKECCKGLRCQSRIANMWPTFCSQ", "text": "FUNCTION: Neurotoxin. Causes spastic paralysis and death in mice. Moderate inhibitor of L-type calcium channels (Cav1/CACNA1). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 53 (PNTx27C4) subfamily."}
{"protein": "MKSLLVVAAVLAVGALAQGDDAKGPKVTDKVYFDMEIGGKPIGRIVIGLFGKTVPKTATNFIELAKKPKGEGYPGSKFHRVIADFMIQGGDFTRGDGTGGRSIYGEKFADENFKLKHYGAGWLSMANAGADTNGSQFFITTVKTPWLDGRHVVFGKILEGMDVVRKIEQTEKLPGDRPKQDVIIAASGHIAVDTPFSVEREAVV", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
{"protein": "MTTGKIYFATTNLKKLNEVKEFLKTDIDHMRISMTEIQGPSEKIVEHKLDQAAPFINPKDAVIVDDTSFSLEALGGFPGVYVKDFLEIGTRKIWEIVEKIGNKSATAVCSLGIAHYENGEIVKKVFSGKLKGSITEPEKDCKTEFGYIFIPDGFNGVLKNMPTDEKNRISHRGIASRSLAAYMASKGIIKTHGP", "text": "FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HAM1 NTPase family."}
{"protein": "MIKQLCKNITICTLALSTTFTVLPATSFAKINSEIKQVSEKNLDGDTKMYTRTATTSDSQKNITQSLQFNFLTEPNYDKETVFIKAKGTIGSGLRILDPNGYWNSTLRWPGSYSVSIQNVDDNNNTNVTDFAPKNQDESREVKYTYGYKTGGDFSINRGGLTGNITKESNYSETISYQQPSYRTLLDQSTSHKGVGWKVEAHLINNMGHDHTRQLTNDSDNRTKSEIFSLTRNGNLWAKDNFTPKDKMPVTVSEGFNPEFLAVMSHDKKDKGKSQFVVHYKRSMDEFKIDWNRHGFWGYWSGENHVDKKEEKLSALYEVDWKTHNVKFVKVLNDNEKK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the aerolysin family."}
{"protein": "MWGSRAQQSGPDRGRTCLLAVLLLSFSLFQLHAQDYKPSQTPPPTSDALLKPMGRVQKEICGKTKFQGKIYGGSIAKAERWPWQASLIFRGRHICGAVLIDKNWVASAAHCFKRSLKPSDYRILLGYNELSNPSNYSRQMTLSKVIVHEDYNKLHSQEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGMVTDDKFLQAPFPLLDSEVFLMNDQECEAFFQTPQISITEYDAIKDDMICAGDITNQKSTCRGDSGGPLVCLLDSYWYLVGLASWSGACLEPIHSPSIFTRVSHFSDWIEKKKADTPDVDPSLAPLEETAPSLIGWRNYSAGTTLEPRICTTLLSSQVLLLQSIWLRIL", "text": "FUNCTION: May play an important role in the sperm/egg interaction; released during the acrosome reaction. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome. Secreted. SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MDYRQLHRWDLPPEEAIKVQNELRKKIKLTPYEGEPEYVAGVDLSFPGKEEGLAVIVVLEYPSFKILEVVSERGEITFPYIPGLLAFREGPLFLKAWEKLRTKPDVVVFDGQGLAHPRKLGIASHMGLFIEIPTIGVAKSRLYGTFKMPEDKRCSWSYLYDGEEIIGCVIRTKEGSAPIFVSPGHLMDVESSKRLIKAFTLPGRRIPEPTRLAHIYTQRLKKGLF", "text": "FUNCTION: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endonuclease V family."}
{"protein": "MIKKILTTCFGLFFGFCVFGVGLVAIAILVTYPKLPSLDSLQHYQPKMPLTIYSADGEVIGMYGEQRREFTKIGDFPEVLRNAVIAAEDKRFYRHWGVDVWGVARAAVGNVVSGSVQSGASTITQQVAKNFYLSSEKTFTRKFNEVLLAYKIEQSLSKDKILELYFNQIYLGQRAYGFASAAQIYFNKNVRDLTLAEAAMLAGLPKAPSAYNPIVNPERAKLRQKYILNNMLEEKMITVQQRDQALNEELHYERFVRKIDQSALYVAEMVRRELYEKYGEDAYTQGFKVYTTVRTDHQKAATEALRKALRNFDRGSSYRGAENYIDLSKSEDVEETVSQYLSGLYTVDKMVPAVVLDVTKKKNVVIQLPGGRRVALDRRALGFAARAVDNEKMGEDRIRRGAVIRVKNNGGRWAVVQEPLLQGALVSLDAKTGAVRALVGGYDFHSKTFNRAVQAMRQPGSTFKPFVYSAALSKGMTASTVVNDAPISLPGKGPNGSVWTPKNSDGRYSGYITLRQALTASKNMVSIRILMSIGVGYAQQYIRRFGFRPSELPASLSMALGTGETTPLKVAEAYSVFANGGYRVSSHVIDKIYDRDGRLRAQMQPLVAGQNAPQAIDPRNAYIMYKIMQDVVRVGTARGAAALGRTDIAGKTGTTNDNKDAWFVGFNPDVVTAVYIGFDKPKSMGRAGYGGTIAVPVWVDYMRFALKGKQGKGMKMPEGVVSSNGEYYMKERMVTDPGLMLDNSGIAPQPSRRAKEDDEAAVENEQQGRSDETRQDVQETPVLPSNTDSKQQQLDSLF", "text": "FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). Essential for cell wall synthesis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family."}
{"protein": "MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERSEPERSPHRPIERADAVDTGDRPGLRTTRMSWPSSFHGTGTGGGSSRRLEAENGPTPSPGRSPLDSQASPGLMLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVASEAHGEDLIVTPFAQVLASLRNVRSNFSLLTNVPIPSNKRSPLGGPPSVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQHEVEIPSPTPRQRPFQQPPPAAVQQAQPMSQITGLKKLVHTGSLNINVPRFGVKTDQEDLLAQELENLSKWGLNIFCVSEYAGGRSLSCIMYTIFQERDLLKKFHIPVDTMMTYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEENCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNRDWYHSAIRQSPSPTLEEEPGVLSDPALPDKFQFELTLEEEDEEDSLEVPGLPCTEETLLAPHDTRAQAMEQSKVKGQSPAVVEVAESLKQETASAHGAPEESAEAVGHSFSLETSILPDLRTLSPSEEAQGLLGLPSMAAEVEAPRDHLAAMRACSACSGTSGDNSAVISAPGRWGSGGDPA", "text": "FUNCTION: [Isoform 2]: Efficiently hydrolyzes cAMP. FUNCTION: Hydrolyzes the second messenger 3',5'-cyclic AMP (cAMP), which is a key regulator of many important physiological processes. SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily."}
{"protein": "MAAPAFPPFRLRFATAATLLGMLGLAGCQTGGYQDSVPPTSGVQPLKGLAQNVSVRRNAMGAPLIESSSFHDALFSLGYVHAGDRIEQMVAMRLLAQGRLAELAGSEALDIDRLMRAANLKQSAAQQYADASPRLKRFFEVYARGVNAYLFRYRDKLPAGLASSGYRPEYWKPEDSALIFCLYAFSQSVNLQEELSALTLAQKAGSDKLAWLLPGAPDEPLAEMEVDKLKGLNLASQLPGLPALAAASQKLADLDLLGSPGSANLALGPQRSRSGKSLLASDSRAAWALSPVQINTSKYQVAGLSLPGLPIVLAGYNGKLAWSSSAVMADNQDLFLEQLRRQGSQLSYLADGKWLPARARSETYFVRGQRPVREVMYDTRHGTLLAQPENASLGLALNLPQFKGDRSLDALFDLTRAKNVERAFDSTREVTAAAVNFVFAEPEHIGWQVSGRYPNRREGQGLLPSPGWDGRYDWDGYADPMLHPYDQDPPAGWIGHANQRSLPRGYGMQLSSTWYYPERAERLAQLAGNGRHDSRSLMALQNDQVTLLANKLKQMFDAPGMAQPLKQAIDALPAGQRDKARDTLARLKAFDGRLSPVSADAALYELFLQEVARQTFLDDLGPESGPAWQAFVGNARLSFSAQADHLLGRDDSPFWDDRNTPQKEDKPAILARSLAGAMEAGIAQLGADRRTWQWGKLHQYRWPAPAYHGLGDAISRSPLAAGGDFTTLALTPFAWGSDFDTHLPASARMIVDFGQAEPLQILTSSGQSGNPASAHYRDGLDAWFKGRFMSLPLQQQNFGRAYGNQRLTLVPGR", "text": "FUNCTION: Catalyzes the deacylation of acyl-homoserine lactone (AHL or acyl-HSL), releasing homoserine lactone (HSL) and the corresponding fatty acid. Possesses a specificity for the degradation of long-chain acyl-HSLs (side chains of seven or more carbons in length) (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the peptidase S45 family."}
{"protein": "MEAPICLVENWKNQLTVNLEAIRILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLDTEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLIRAKSSPREDKVKDSSEFVGFFPDFIWAVRDFALELKLNGRPITEDEYLENALKLIQGDNLKVQQSNMTRECIRYFFPVRKCFVFDRPTSDKRLLLQIENVPENQLERNFQVESEKFCSYIFTNGKTKTLRGGVIVTGNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKEAIAVFMEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLREEMERTRRKPSLFGQILDTIGNAFIMILPGAGKLFGVGLKFLGSLSS", "text": "FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:24739961, PubMed:24715728). Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product (PubMed:9659399). Following infection, recruited to the pathogen- containing vacuoles or vacuole-escaped bacteria and acts as a positive regulator of inflammasome assembly by promoting the release of inflammasome ligands from bacteria (PubMed:24739961, PubMed:24715728). Acts by promoting lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol (PubMed:24739961, PubMed:24715728). Following pathogen release in the cytosol, promotes recruitment of proteins that mediate bacterial cytolysis, such as Gm12250/Irgb10: this liberates ligands that are detected by inflammasomes, such as lipopolysaccharide (LPS) that activates the non-canonical CASP4/CASP11 inflammasome or double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed:24739961, PubMed:24715728). May play a role in erythroid differentiation (PubMed:9659399). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Golgi apparatus membrane Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP5, at the Golgi apparatus. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. GB1 subfamily."}
{"protein": "MEPIVKQENPVTTSTLSTWKPAARNKTIPPPESVIELSSSNEGSELGENLDEIAEIQSVDRTGGDDVSGTKRARSDSIASPAKRLAVMIPDDDEEFLLSTTSGQAILALPATPCNVVAAPSSWGSCKQFWKAGDYEGTSGGDWEVSAGGFDHVRVHPKFLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMIQNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLADTIGQYGNGFKTSTMRLGADVIVFSRCLGKDGKSSTQSIGLLSYTFLKSTGKEDIVVPMLDYERRDSEWCPITRSSVSDWEKNVETVVQWSPYATEEELLCQFNLMKKHGTRIIIYNLWEDDEGMLELDFDTDPHDIQLRGVNRDDKNIVMASQFPNSRHYLTYKHSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADVSQLSAVVTIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYWRSKCHKIGYAKRQGRKSAKDTEKDTEDRESSPEFDPKGSASSRKRTVPSSFKTPTAAPRFNTPTAASEKFNPRSNVNGGGKGSVKVSKDIGYKSSEKGGKLGNSFSKSNKRAKPQGARAVEVTNSDDDYDCDSSPERNVTELPGKSSELPKPQSGPRTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENLRIKLEEASNTIQKLIDGKARGR", "text": "FUNCTION: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC7, acts to suppress a wide set of non- methylated protein-coding genes, especially involved in pathogen response. Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa) (PubMed:27171361). SUBCELLULAR LOCATION: Nucleus Note=Accumulates in discrete nuclear bodies adjacent to chromocenters. SIMILARITY: Belongs to the MORC ATPase protein family."}
{"protein": "MSEMSYLEKLLDGVEVEWLPLGEITKYEQPTKYLVKAKDYHDTYTIPVLTAGKTFILGYTNETHGIYQASKAPVIIFDDFTTANKWVDFDFKAKSSAMKMVTSCDDNKTLLKYVYYWLNTLPSEFAEGDHKRQWISNYSQKKIPIPCPDNPEKSLAIQSEIVRILDKFTALTAELTAELNMRKKQYNYYRDQLLSFKEGEVEWKTLGEIGKWYGGGTPSKNKIEFWENGSIPWISPKDMGRTLVDSSEDYITEEAVLHSSTKLIPANSIAIVVRSSILDKVLPSALIKVPATLNQDMKAVIPHENILVKYIYHMIGSRGSDILRAAKKTGGSVASIDSKKLFSFKIPVPNINEQQRIVEILDKFDTLTNSITEGLPREIELRQKQYEYYRDLLFSFPKPETVSN", "text": "FUNCTION: The specificity (S) subunit of a type I restriction enzyme; this subunit dictates DNA sequence specificity. The M and S subunits together form a methyltransferase (MTase) that methylates A-3 on the top and bottom strand of the sequence 5'-GAAN(7)RTCG-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated (PubMed:32483229, PubMed:12654995). After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage (Probable). SIMILARITY: Belongs to the type-I restriction system S methylase family."}
{"protein": "MNSNDNQRVIVIGAGLGGLSAAISLATAGFSVQLIEKNDKVGGKLNIMTKDGFTFDLGPSILTMPHIFEALFTGAGKNMADYVQIQKVEPHWRNFFEDGSVIDLCEDAETQRRELDKLGPGTYAQFQRFLDYSKNLCTETEAGYFAKGLDGFWDLLKFYGPLRSLLSFDVFRSMDQGVRRFISDPKLVEILNYFIKYVGSSPYDAPALMNLLPYIQYHYGLWYVKGGMYGMAQAMEKLAVELGVEIRLDAEVSEIQKQDGRACAVKLANGDVLPADIVVSNMEVIPAMEKLLRSPASELKKMQRFEPSCSGLVLHLGVDRLYPQLAHHNFFYSDHPREHFDAVFKSHRLSDDPTIYLVAPCKTDPAQAPAGCEIIKILPHIPHLDPDKLLTAEDYSALRERVLVKLERMGLTDLRQHIVTEEYWTPLDIQAKYYSNQGSIYGVVADRFKNLGFKAPQRSSELSNLYFVGGSVNPGGGMPMVTLSGQLVRDKIVADLQ", "text": "FUNCTION: Involved in the biosynthesis of C30 carotenoids. Catalyzes the oxidation of the terminal methyl side groups of 4,4'-diapolycopene to yield 4,4'-diapolycopen-4,4'-dial via the aldehyde intermediate 4,4'-diapolycopen-al. Also able to catalyze the oxidation of the terminal methyl side group of 4,4'-diaponeurosporene to form 4,4'- diaponeurosporen-4-al. It has moderate to low activity on the C40 substrates neurosporene and lycopene, and has no detectable activity on zeta-carotene or beta-carotene. SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family."}
{"protein": "MAEAVFRAPKRKRRVYESYESPLPIPFGQDQGPRKEFRIFQAEMISNNVVVRGTEDMEQLYGKGYFGKGILSRSRPNFTIANPTLAARWKGVQTDMPIITSEKYQHRVEWARDFLRRQGHDESTVQKILTDYTEPLELPCREEKEETPQHEPLSSKADSSLEGRVEKDELPVTPGGAGQSDDLPGLGTHSDCLQEGPGHATLAAASPSSHNGHVAEDPEVLPQETLVPQGGLWPEASSQAAGEKRAAHEYVLIEEELCGAQEEEAAAASDEKLLKRKKLVCRRNPYRIFEYLQLSLEEAFFLAYALGCLSIYYEKEPLTIVKLWQAFTAVQPTFRTTYMAYHYFRSKGWVPKVGLKYGTDLLLYRKGPPFYHASYSVIIELLDDNYEGSLRRPFSWKSLAALSRVSGNVSKELMLCYLIKPSTMTAEDMETPECMKRIQVQEVILSRWVSSRERSDQDEL", "text": "FUNCTION: Constitutes one of the two catalytic subunit of the tRNA- splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. Probably carries the active site for 5'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Note=May be transiently localized in the nucleolus. SIMILARITY: Belongs to the tRNA-intron endonuclease family."}
{"protein": "MEPAAGFLSPRPFPRAAAPSSPPAGPGPPASASPRSEPGVLAGPQTPDASRLITDPRSGRTYIKGRLLGKGGFARCYEATDTETSIAYAVKVIPQSRVAKPHQREKIINEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITDNMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIEQILRHDFFTKGYTPDRLPVSSCVTVPDLTPPNPARSLFAKVTKSLFGRRKSKNKNHSEEQDNVSCLVSGLMRTSIGHPDVRPEAPAASALAPVSLVETAAEDSSPRGTLASSGDGFEEGLTVTTVVESALCALRNCVAFMPPAEQNPAPLAQPEPLVWVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSVGSVPRALQPQLGILRYFASYMEQHLMKGGDLPSVEEVEVPAPPLLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDRSPA", "text": "FUNCTION: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1 (By similarity). SUBCELLULAR LOCATION: Cell projection, dendrite Cytoplasm Nucleus Nucleus, nucleolus Golgi apparatus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase (By similarity). When induced, it translocates into the dendrites of activated neurons. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily."}
{"protein": "MSELTEAEKRRLLRERRQKKFSNGGASSRLNKITGQASSHLNAESPLDAPSAAKTTPPASVHSATPDIKEDSNVAPQLDLLKQLAAMQGQGTGKSTPQDSSTPDLLSLLSSMNTGMPSAEGTPSFGQAAPAAPINQAALDYHDYLLNRLKAWTILVKWVFFLLPYLYLITRPNSSVWPAYAFTQSAWFAPLRNPSNFTRIFATFEFLSISIYYQLLKNVEHKSKIKNLQDTNKLVKLVSLVPEGVIPVANLKGKLITLLQYWDLLSMLITDISFVLIVLGLLTYL", "text": "FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP- dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in DNA replication and DNA damage response and also in cell wall function. FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP- dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in DNA replication and DNA damage response and also in cell wall function. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GET2 family."}
{"protein": "MTERLAGKTALVTGAAQGIGKAIAARLAADGATVIVSDINAEGAKAAAASIGKKARAIAADISDPGSVKALFAEIQALTGGIDILVNNASIVPFVAWDDVDLDHWRKIIDVNLTGTFIVTRAGTDQMRAAGKAGRVISIASNTFFAGTPNMAAYVAAKGGVIGFTRALATELGKYNITANAVTPGLIESDGVKASPHNEAFGFVEMLQAMKGKGQPEHIADVVSFLASDDARWITGQTLNVDAGMVRH", "text": "FUNCTION: Involved in the degradation of pyridoxine or pyridoxamine (free, phosphate-unbound, forms of vitamin B6). Oxidizes pyridoxal to 4-pyridoxolactone, but does not have activity toward pyridoxal 5'- phosphate, pyridoxine, pyridoxamine, pyridoxamine 5'-phosphate, 4- phthalaldehyde, 2-nitrobenzaldehyde, pyridine, formaldehyde, 2- carboxybenzaldehyde or sugars. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MVVHIENLNAFSAALKNAGDKLVVVDFTATWCGPCQKIGPIFETLSKSEDYQNVVFLKVDVDDAADVSSHCDIKCMPTFHFYKNGQKIDEFSGANEQTLKQKINDHK", "text": "FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Secreted Note=Shuttles between the nucleus and nucleolus. SIMILARITY: Belongs to the thioredoxin family."}
{"protein": "MSEGDSIGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWIVTLGLSFIYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTRQNEEFRPFIRRLPEFKFWHSATKGILVAMACTFFEAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRKYKGKEDVGKTFAS", "text": "FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the RER1 family."}
{"protein": "MTTSLQDGQSAAGRAGAQDSPLAVQVCRVAQGKGDAQDPAQVPGLHALSPASDATLRGAIDRRKMKDLDVLEKPPIPNPFPELCCSPLTSVLSAGLFPRANSRKKQVIKVYSEDETSRALEVPSDITARDVCQLLILKNHYVDDNSWTLFEHLSHIGLERTVEDHELPTEVLSHWGVEEDNKLYLRKNYAKYEFFKNPMYFFPEHMVSFAAEMNGDRSPTQILQVFLSSSTYPEIHGFLHAKEQGKKSWKKAYFFLRRSGLYFSTKGTSKEPRHLQLFSEFSTSHVYMSLAGKKKHGAPTPYGFCLKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKDGMQLYQNYMHPYQGRSACNSQSMSPMRSVSENSLVAMDFSGEKSRVIDNPTEALSVAVEEGLAWRKKGCLRLGNHGSPSAPSQSSAVNMALHRSQPWFHHRISRDEAQRLIIRQGPVDGVFLVRDSQSNPRTFVLSMSHGQKIKHYQIIPVEDDGELFHTLDDGHTKFTDLIQLVEFYQLNRGVLPCKLKHYCARMAV", "text": "FUNCTION: Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endosome membrane; Peripheral membrane protein Note=Upon insulin stimulation, translocates to the plasma membrane. SIMILARITY: Belongs to the GRB7/10/14 family."}
{"protein": "MKYLFVCVSLALFAYISANPAYGGNRGGYGGGYGNDRVEYEQILVPSYGRSRGGYGGYDRPQILRSAPSGSRASAAAASAAAAIAPGSYSQYAIPRYEIDGSYNGPSHGHGGYGHGGRGGY", "text": "FUNCTION: Chorion membrane (egg shell) protein; plays a role in protecting the egg from the environment. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the chorion protein S15/S18 family."}
{"protein": "MGIEMRCQDRRILLPSLLLLILMIGGVQATMKLCGRKLPETLSKLCVYGFNAMTKRTLDPVNFNQIDGFEDRSLLERLLSDSSVQMLKTRRLRDGVFDECCLKSCTMDEVLRYCAAKPRT", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family."}
{"protein": "MDHYLEIRVLPDPEFSSEMLMAALFAKLHRVLGARGQGDIGVSFPDVNVMPGARLRLHGSAQALQALEASTWRKGLTDYCQCSPVTPVPEIKGWRVVSRVQVKSNPQRLLRRSVKKGWLTEEQAIERLATQAEQRTDLPFLNMKSLSSQQLFKLFIRHGDLLKEPVKGEFSSYGLSATATIPWF", "text": "FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Processes pre-crRNA into individual crRNA units (By similarity). FUNCTION: Complements a csy4 disruption in Pseudomonas aeruginosa PA14, restoring inhibition of biofilm formation and generation of crRNA. SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas6 family. Cas6f/Csy4, subtype I-F/Ypest subfamily."}
{"protein": "MPAPHGGVLQDLVARDASKRDSLLSESQQLSQWTLTARQICDIELILNGGFSPLTGFLAQEDYNGVVHNSRLSDGTLWTMPITLDVPEQFANSVKPNQRIALLQDGTIPVAILTVKDIYKPDKSVEAEKVFRGDPEHPAINYLFNTAGDYYIGGALDAIQLPQHYDYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMHRAHRELTVRAARETNAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPNGIAFLSLLPLAMRMGGDREAVWHAIIRKNYGASHFIVGRDHAGPGSNSKGVDFYGPYDAQELVESYKNELDIDVVPFRMVTYLPDEDRYAPIDEIDTSKTRTLNISGTELRKRLRDGGEIPEWFSYPEVVKILRESNPPRPKQGFALVFNDDIKVDRDQLSIALLSTFLQFGGGRHYKIYDHNDKPEFLELISDFVQAGSGLIIPSTWSASNKVNSANVYTIGHAKDADIKLASTEETIFHIVQKVVLFLEDNHFIQF", "text": "FUNCTION: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfate adenylyltransferase family."}
{"protein": "MTITFQDFNLSSDLMKAINRMGFEEATPIQAQTIPLGLSNKDVIGQAQTGTGKTAAFGIPLVEKINPESPNIQAIVIAPTRELAIQVSEELYKIGQDKRAKVLPIYGGQDIGRQIRALKKNPNIIVGTPGRLLDHINRRTIRLNNVNTVVMDEADEMLNMGFIDDIESILSNVPSEHQTLLFSATMPAPIKRIAERFMTEPEHVKVKAKEMTVSNIQQFYLEVQERKKFDTLTRLLDIQSPELAIVFGRTKRRVDELAEALNLRGYAAEGIHGDLTQAKRMVALRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAGKTGMAMTFITPREKSMLRAIEQTTKRKMDRMKEPTLDEALEGQQQVTVERLRTTISENNLNFYMTAAAELLEDHDAVTVVAAAIKMATKEPDDTPVRLTDEAPMVSKRYKNQRSSKRRDGQGGGYRGGKGKSNNRSSYDKKRSNDRRSSGDRRQKKSY", "text": "FUNCTION: The most abundant DEAD-box RNA helicase. An ATP-dependent RNA helicase with RNA-dependent ATPase activity. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. In vitro, unwinds dsRNA in both 5'- and 3'- directions. Plays a role in ribosomal 50S subunit assembly. Its deletion leads to changes in mRNA levels for over 200 transcripts. SUBCELLULAR LOCATION: Cytoplasm, nucleoid. Cell membrane. Note=Shows transcription-dependent localization at subcellular sites surrounding the nucleoid (PubMed:16352840). Associated with free 50S ribosomal subunit, 70S ribosome and polysomes (PubMed:16861794). Cell membrane association shown in (PubMed:20572937). SIMILARITY: Belongs to the DEAD box helicase family. CshA subfamily."}
{"protein": "MITLFLSPSCTSCRKAKAWLEKHKVPFVEHNIMTSPLTRKELQHILSLTENGTDDIISTRSKIFQKLNIDVESISVSELLHLIEQYPSLLRRPIIIDAKRMQIGFNEDEIRAFLPRSYRKQELKEARMRAGIS", "text": "FUNCTION: Global transcriptional regulator that plays a key role in stress response and exerts either positive or negative regulation of genes. Acts by interacting with the C-terminal domain of the alpha subunit of the RNA polymerase (RNAP). This interaction can enhance binding of RNAP to the promoter region of target genes and stimulate their transcription, or block interaction of RNAP with activator. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArsC family. Spx subfamily."}
{"protein": "MTQAVGLVGWRGMVGSVLMQRMRDENDFALIEPVFFSTSNAGGAAPAWAEGAGSLQNAYDIDALKKLPIIVTAQGGDYTSEVYPKLRGAGWQGIWIDAASTLRMADDAIIVLDPVNRPVIDAALKRGVRNFVGGNCTVSCMLMGLAGLFNNDLVEWMSSMTYQAASGGGAQHMRELLTQFGLLNQAVKPLLDDPAAAILDIDRGVLARQQDPSLPQEHFGVPLGGNLIPWIDKDLGDGMSREEWKAEAETNKILGRGAAFGTPATPIDGLCVRIGAMRCHSQALTIKLKRDVPLDEIEDLIAAGTQWAKVVPNTKEDTVKALTPVAVTGTLDIPVGRLRKLSMGLQYLGAFTVGDQLLWGAAEPLRRMLRIALAEA", "text": "FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate. SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family."}
{"protein": "MLGMIKNSLLSTVETWPYRVLSKGEKEQLSYEERECEGGQFAVVEVTGKPFDEASKEAALKLLKYVGGSNDKGAGMGMTAPVSITAFPAEDGSLQQKVKVYLRIPNQFQASPPCPSDESIKIEERQGMTIYSTQFGGYAKEVDYVNYAAKLKTALGSEAAYRKDFYFCNGYDPPMKPYGRRNEVWFVKE", "text": "FUNCTION: May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HEBP family."}
{"protein": "MEAERRHRALYKGTTPPWKETYRKRCVERLKRNRSKLLDKFRQVGERIHGGVGGSFLVQEVMEEEWKAMQSENGSFPSMWKKEAFSQALNIMRDPDELATLEEIKQELLLEEKAMIEEFENILQFEEQCLDSVVELSTGDQIVCPVCNRNYLTVTSCFIVCQCGVYINTQSQGMSIEKLHSLLESSLTSHGYHCTKLPVFSVATELGGAASLFMSCQECDAMVVIL", "text": "FUNCTION: Mediates the import of RPA complex into the nucleus, via its interaction with importin beta. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MIRRIRTLTPLLVLACAGSGAWASKKAFNIQDDLLAYPQFQVFFPDEYILDARARELLQNQQESSSASADKTFSEGNDAQVYLGSRKDQSEDVNKETIEGSGFTYEEMLLEGQRYLCSIPQVDNGNRDQTNGAESTSKEDEQREIARATDRGLELLREMEGKCMYYISGWWSYSFCYKKQIKQFHALPSGPGVPNYPPIEDSTTHSFVLGRFPNSGDDEDLEGDAEHKKTTTDVAELQTKGGSRYLVQRLGGGTKCDLTGKDRKIEVQFHCHPQSTDRIGWIKELTTCSYLMVIYTPRLCNDVAFLPPQQDEAHAIECREILSEEEVSDWEANREYHLAQQLVESAITPEFPVVGDIEVGAHKWVGSEGKQIEKGRVASIGEEKIEVVAKRQNGEITRLSKEELKKYGLDPEKIETLKSRLEELAKGKDWTLEIVESNGERGLVGTVDSNDDEKEDHAAQGSISQPAQGTTADKGESNAETGEEKKKADEKIDHYEPEKSGPTTDDADDGSEEIFFKDEL", "text": "FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the OS-9 family."}
{"protein": "MSGAARAGPARLAALALLTCSLWPTRADNASQEYYTALINVTVQEPGRGTPLTFRIDRGRYGLDSPKAEVRGQVLAPLPIHGVADHLGCDPQTRFFVPPNIKQWIALLQRGNCTFKEKISRAAFHNAVAVVIYNNKSKEEPVTMTHPGTGDIIAVMITELRGKDILSYLEKNISVQMTIAVGTRMPPKNFSRGSLVFVSISFIVLMIISSAWLIFYFIQKIRYTNARDRNQRRLGDAAKKAISKLTTRTVKKGDKETDPDFDHCAVCIESYKQNDVVRVLPCKHVFHKSCVDPWLSEHCTCPMCKLNILKALGIVPNLPCTDNVAFDMERLTRTQAVNRRAALGDLAGDSSLGLEPLRTSGISPLPQDGELTPRTGEINIAVTKEWFIIASFGLLSALTLCYMIIRATASLNANEVEWF", "text": "FUNCTION: Acts as an E3 ubiquitin-protein ligase (By similarity). May have a role during the programmed cell death of hematopoietic cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Cytoplasm."}
{"protein": "MEGMAQHPVPRTVEEVFSDYKGRRAGLIKALTTDVEKFYQLVDPEKENLCLYGFPNETWEVNLPVEEVPPELPEPALGINFARDGMQEKDWLSLVAVHSDSWLLAVAFYFGARFGFGKNDRKRLFQMINDLPTVFELATGTAKQSKDQLTAHNNGSNSKYKSSGKSRQSESQTKGVKMSAPVKEEVDSGEEEEEDDDEQGATCGACGDNYGTDEFWICCDMCEKWFHGKCVKITPAKAEHIKQYKCPGCSIKKPRIG", "text": "FUNCTION: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes (By similarity). Transcriptional regulator that binds specifically to DNA sequences 5'- GNGGTG-3' or 5'-GTGGNG-3', including promoter elements of the salt- inducible PRP2 gene. Plays a role in salinity tolerance. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Alfin family."}
{"protein": "MKLTCVVIVAVLLLTACQLITADDSRGTQRHRALRSDTKLSMSTRCKGKGASCRRTSYDCCTGSCRSGKCG", "text": "FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
{"protein": "MTTAILQRLSTLSVSGQHLRRLPKILEDGLPKMPGTVPETDVPQLFREPYIRAGYRPIGHEWRYYFFSLFQKHNEVVNVWTHLLAALAVLLRFWAFVETEGLPWTSAHTLPLLLYVLSSITYLTFSLLAHLLQSKSELSHYTFYFVDYVGVSVYQYGSALVHFFYASDQAWYERFWLFFLPAAAFCGWLSCTGCCYAKYRYRRPYPVMRKVCQVVPAGLAFILDISPVAHRVALCHLSGCQEQAAWYHTLQIVFFLVSAYFFSCPVPEKYFPGSCDIVGHGHQIFHAFLSICTLSQLEAILLDYKGRQEIFLHRHSPLSIYAACLSFFFLVACSGATAALLREKIKARLSKKDS", "text": "FUNCTION: Steroid membrane receptor. Binds progesterone. May be involved in oocyte maturation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADIPOR family."}
{"protein": "MKNISFKVNDFQYTINNKLTLIQACLKNKVDISRFCFHEKLSIAGNCRMCLVEDLKQVKPLASCAINVSNSMNIYTNTLKVKKARESVLEFLLANHPLDCPICDQGGECDLQDQSVVFGSDRGRFYEFKRSVEDKDCGPLIKTIMNRCIHCTRCVRFSNEVAGVNILGVTGRGSKMEIGFYIENLMRSELSGNVIDLCPVGALTSKPFAFTSRPWELKSYNSIDVLDSLHSNIRVDIRGTKIMRILPRVNSELNEDWITDKIRFSYDSFRRQRLYDPMVKISGSFLKIGWKKAMLFIKKFFCNFLGFNHSSFIPLRGYIGDYLDLETIYTFKKFLLLNGSNFFLPSSSYNDLTALYSFNTPLTRLDEGDFCILLDVNLRVELPIVNSRIKQLVSKKMLPVFVLGFYSNFNYFVKHISNSSKTLLHVLEGSHWLSAKISKKFSSKPIFLIGDSSSLLKGSLIVPLFNFTNVICDNWNGLNIISNDSSYLSTKEFNLSSSHSQNSHLLNFPINFVLNYDKAVLVDSSAFQIYQGHHGDTNAINSNLIFPSTSFIEKNSFYSNSLAIVQKTKKILFSPGNSRDDWKILNALIDNFGFSYFKVRNSFDLVSFLSESTPFILYKRSFSFKCFGFYEQLVYHFFNYFSVNNNYYIYDSITRNSKIMSLCFNKFKMKGYNFF", "text": "FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane Note=Matrix and cytoplasmic side of the mitochondrial inner membrane. SIMILARITY: Belongs to the complex I 75 kDa subunit family."}
{"protein": "MAPFEPLASGILLLLWLIAPSRACTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLRTRIA", "text": "FUNCTION: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family."}
{"protein": "MQDSSYKEQVTQAFDQSSSTYDRLGVEFFTPMGRPLVEISEPVTGERVLDIGCGRGACLFPAAEKVGPQGRVHGIDIAPGMIEEARKEAAERGLRNIALDVMDAETPELPARSFDLVMGSYSVIFLPDAVGALARYAGILDHGGRIAFTSPVFRAGTFPFLPPEFTPLIPQALLEHLPEQWRPEALVRRFNSWLERAEDLLRTLERCGYTSVAVTDEPVRMTALSSEAWVDWSHTQGMRLLWQNLPQAQRTELRARLVEGLDKLSDATGALAIDVPVRFVTARVAH", "text": "FUNCTION: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the methyl esterification of aklanonic acid to yield aklanonic acid methyl ester. SIMILARITY: Belongs to the methyltransferase superfamily. DnrC family."}
{"protein": "MTRSLKTTLILLASSVISMSALAEFKQAPLPYATNALQPAIDQQTMEIHYGKHHKAYVDNLNAQIKTYPELDKTDLIQLQKQISKYNTAVRNNGGGHFNHTFFWESLAATNKTGQPSPALVKQITQDFGSLDAFKQKFNEAASGRFGSGWAWLIVTPNGKLAVTSTPNQDNPLMDLSETKGTPLLGLDVWEHAYYLKYQNRRADYIKAFWSVVNWNKVNERYNEAIKK", "text": "FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family."}
{"protein": "MSFADTLRQLSSAEDFFSALHVDYDPQILNVARLHILRKMRLYLEADKGDLADESLQKQQYQHYLAQAYNDFVHSSPIKERLFKVHQEAVKPVKLPMVKLTSLTMPPE", "text": "FUNCTION: May protect the nitrogenase Fe-Mo protein from oxidative damage. SIMILARITY: Belongs to the NifW family."}
{"protein": "MEPVASNIQVLLQAAEFLERREREAEHGYASLCPHHSPGTVCRRRKAPLQAPGALNSGRHVHNELEKRRRAQLKRCLEQLRQQMPLGVDHTRYTTLSLLRGARMHIQKLEEQEQQAQRLKEKLRSRQQSLQQQLEQLQGLLGVRERDRLRADSLDSSGLSSERFDSDQEDLEVDVESLVFGTETELLQSFSAGQEHSYSHSTGTWL", "text": "FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence- specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "TITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR", "text": "FUNCTION: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored- polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin family."}
{"protein": "MLNLFILLLERVGLIILLAYILMNINHFKTMMSERDKWRSKFQLIIIFGIFSMISNFTGIEIENGHIVSGDIYYHLSKDASMANTRVLTIGVSGLIGGPWVAIIVGIISGLCRLYIGGADAYTYLISSIVIAIISGYFGHQTIKQNTYPSIKKGAIIGAITEIIQMGCILLFTNNLHHAITLVSFIALPMIIINSLGTAIFLTIILSTIKQEEQMRAVQTHDVLQLANETLPYFRSGLNEKSAQQAAEIILKLMQVSAVAITNKKDILTHIGAGSDHHVARKEIITDLSKEVIQSGKLKVAHTREGIGCHHPNCPLEGAIVVPLYIHNEVAGTLKFYFTDNNIISTSDQQLAKGLANIFSSQLELGQAEMQGQLLKDAEIKSLQAQVNPHFFFNAINTISALVRIDSEKARRLLIQLSQFFRSNLNGARNNTITLQKELQQVAAYLSLEQARYPNRFNIHYRIDDQCQDALIPPFIIQILVENSIKHAFKNRKKNNHIDVDVSMKQDYLSISVQDNGQGIPADQLDTIGYTTVTSTTGTGNALVNLNKRLTGLFGTTSALNIQSSQSGTTVSCLIPYKSSKEEHFNESVNR", "text": "FUNCTION: Member of the two-component regulatory system LytR/LytS that probably regulates genes involved in cell wall metabolism. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MTNGSFRQIINQLDMRWRRRVPVIHQTETAECGLACLAMICGHFGKNIDLISLRRKFNLSARGANLAGINGIAEQLGMVTRALSLELDELGALKMPCILHWDFSHFVVLVSVKRNRYVLHDPARGRRYLGREEMSRYFTGIALEVWPGSEFLAETQQIRISLRSLINSIYGIKRTLAKIFCLSVVIEAINLVMPVGTQLVMDHAIPAGDRGLLTLISAGLMFFILLRAAVSMLRAWSSLVMSTLINIQWQSGLFNHLLRLPLAFFERRKLGDIQSRFGSLDTLRATFTTCVVGAIMDSIMVVGVFVMMLLYGGYLTWIVLGFTMVYVLIRLVTYGYYRQISEETLVRGARASSYFMESLYGIATVKIQGMAGIRGTHWLNLKIDAINSGIKLTKMDLLFGGINTFVAACDQVAILWLGASLVIDNQMTIGMFVAFGSFRGQFSDRVASLTSFLLQLRIMSLHNERIADIALHEKEEKKPEIEIVADMSPVSLETTDLSYRYDSQSAQVFSGLNLSVAPGESVAITGASGAGKTTLMKVLCGLFEPDSGKVLVNGTDIRQLGINNYHRMIACVMQDDRLFSGSIRENICGFAEETDDEWMTECARASHIHDVIMKMPMGYETLIGELGEGLSGGQKQRIFIARALYRKPGILFMDEATSSLDTESERFVNAAIKKMNITRVIIAHRETTLRTVDRIISI", "text": "FUNCTION: Probably involved, in conjunction with MchE, in the secretion of microcin H47. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily."}
{"protein": "MQGPWLMMALALIFVLTGIPKSCALLEAAQEEGAVTPDLPGLEKVQVRPERRFLRKDLQRVRGDLGAALDSWITKRQHPGKREEKEEDVEAEERGDLGEVGAWRPHKRQHPGRRANQDKDSWSDEGDSDWLPPSWLPDFFLDSWFSDAPQVKRQHPGRRSFPWMESDVTKRQHPGRRFIDPELQRSWEETEGEEGGLMPEKRQHPGKRAVGHPCGPQGICGQTGLLQLLGDLSRGQETLAKQTPQLEAWVREPLEE", "text": "FUNCTION: Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TRH family."}
{"protein": "MSLITRLLTGNITLRRRAMESLGKAGYSSHAKFSEHKPIERIRNIGISAHIDSGKTTLTERILFYTGRIAEMHEVRGKDNVGATMDSMELERQRGITIQSAATYTLWKDTNINIIDTPGHVDFTVEVERALRVLDGAVLVLCAVGGVQSQTLTVNRQMKRYNVPCLAFINKLDRLGSNPYRVLSQMRSKMNHNAAFIQLPIGVESNCKGIVDLVREKAIYFEGEHGMDIRLDEIPQDMRVESLERRQELIEHLSNADETLGELFLEEKPFTEDDIKAALRRTCINRTFTPVLVGTALKNKGVQPLLDAVLDYLPNPGEVENLGFIEKEGQDPEKVVLNPARDGKDPFVGLAFKLEAGRFGQLTYLRCYQGVLRKGDNIFNARTNKKVRIARLVRLHSNQMEDVNEVYAGDIFALFGVDCASGDTFTTNPKNNLSMESIFVPEPVVSMAIKPNNTKDRDNFSKAIARFTKEDPTFHFFFDNDVKETLVSGMGELHLEIYAQRMEREYGCPVTLGKPKVAFRETLVGPCEFDYLHKKQSGGSGQYARIIGVMEPLPPTQNTLLEFVDETVGTNVPKQFVPGVEKGYREMAEKGMLSGHKLSGIRFRLQDGGHHIVDSSELAFMLASHGAIKEVFQNGSWQILEPIMLVEVTAPEEFQGAVMGHLSKRHGIITGTEGTEGWFTVYAEVPLNDMFGYAGELRSSTQGKGEFTMEYSRYSPCLPDVQDQIVRQYQESQGLAQPDKKKKKN", "text": "FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Essential during development as it acts as a retrograde signal from mitochondria to the nucleus to slow down cell proliferation if mitochondrial energy output is low (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily."}
{"protein": "MKYLLISLALWLGMVGIHGTELELSETQRRGLQVALEEFHKHPPVQWAFQEIGVDNANDMVFSAGTFVRLEFKLQQTSCFKKDWKNPECKIKANGRKRKCLACIKLDPRGKVLGRMVHCPILKQGLQQELQESQCNRITQAGEDPRSHFFPGQFAFSRALKHK", "text": "FUNCTION: Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Acts also as a ligand for CMKLR2. Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a lower affinity than it does to CMKLR1 or CMKLR2. Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a pro-inflammatory adipokine, causing an increase in secretion of pro-inflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Its dual role in inflammation and metabolism might provide a link Exhibits an antimicrobial function in the skin (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "AYTGQTGAPWGLA", "text": "FUNCTION: Serine protease. Degrades fibrinogen. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family."}
{"protein": "MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYAGPNPAFQPGYTPGTPYKVSCSPTSGTVPPYSSSPNPYQTAVYPVRSAYPQQNPYAQQGAYYTQPLYAAPPHVIHHTTVVQPNGMPATMYPAPIPQPRGNGVAMGMVAGTTMAMSAGTLLTSHYPTPVAPHQVTMPTYRPPGTPTYSYVPPQW", "text": "FUNCTION: Inhibitor of neuronal axonal outgrowth. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Cell membrane; Multi-pass membrane protein Cell projection, axon. SIMILARITY: Belongs to the FAM168 family."}
{"protein": "MSAQDVRSILSLPPSTPLPTLSSSKKVPVPRKPDGITRELYALIGDNAPSLADAQASLAAVKYREKPALKGKKVHWEWTKFTPAARRDNPVRLGHWARITDSDPNDSVEYFGKFNLHGPSVMEYSQFEYDQHLVDPNWTLQETEYLFELLKEYDLRFIVAADRYAYVSPEGEKRKRSVEDMKDRYYTICRRLIRTRTASDPVHQQHLIQAYAFDKAREIKRKQYASDLFHLTPAEIAEEEALYVEITRMQQNERRFRADRDELMRSVMGLDSGLVEVDQSAMENAIGVDKNKKKRKAEDESAAPSPAPTPKKPAPNAGFDNSRCIYHLPTPSNANSLTSHLSQKHPPHQQAFLRGSRLPLPKPTAAGRITDLLAELGLSANRLVMPTRQNMEVFEGLLNAAAALVEMRRQVNRVEQELRVVRMQKEGLMPVTTNPSARVKGEAGVVTGGSEATVKAVTPVKEC", "text": "FUNCTION: Component of the SWR1 complex which mediates the ATP- dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SWC4 family."}
{"protein": "MGDKLRLSIGILGNGASLLLYTAPIVTFSRVFKKKSTEEFSCFPYVMTLFNCLIYTWYGLPIVSHLWENLPLVTINGVGILLESIFIFIYFYYASPKEKIKVGVTFVPVIVGFGLTTAISALVFDDHRHRKSFVGSVGLVASISMYGSPLVVMKKVIETRSVEYMPFYLSFFSFLASSLWLAYGLLSHDLFLASPNMVATPLGILQLILYFKYKNKKDLAPTTMVITKRNDHDDKNKATLEFVVDVDRNSDTNEKNSNNASSI", "text": "FUNCTION: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SWEET sugar transporter family."}
{"protein": "MNEDLIAEIQALSAIGSEEKFSEIIRLLKNSTLELRGKKNPDLQLSASALVFKKHKLFFIEHPYQKELLLPAGHVELGEKPLETAIREFHEETGFSASESGKLVDVNLINIPYNKIKNEKEHQHIDFRFLLELKEKEAGLAELPFFLLDRTEAPDEFKKYYQYKR", "text": "FUNCTION: Probably mediates the removal of pyrophosphate from dihydroneopterin triphosphate (DHNTP), a possible step in the pterin branch of the folate synthesis pathway. SIMILARITY: Belongs to the Nudix hydrolase family."}
{"protein": "MVCAWQLWLSPRPKRSVIASGSHIYSNDDAALFEFLKEDDGRWVVRETHYINNPLVKNGLSGPPLHIHWKQAEYFKVEQGVIGIHKNGKQLRVTKDDGVIEVPAGTRHKFWSHPSNQEDLVFKVWAEPQGLDHSFDEKFIRNLIGYQRDCKMANMAPSVFQLMLICYDCATLATPPFWVPLWLLTSIQYVLAYWIGGHLLGYKPSYSEYYREPGDKKTM", "text": "FUNCTION: Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of virensols and trichoxide, fungal natural products that contain or are derived from a salicylaldehyde core (PubMed:31790246). The pathway begins with the synthesis of the reduced chain in virensol C by the highly reducing polyketide synthase virA via condensation of one acetate and 8 malonate units (PubMed:31790246). VirA has interesting programming rules since the first 2 ketides are fully reduced, the 3 following ketides undergo beta-dehydration, and the last 3 ketides are only reduced to beta-hydroxys to yield the trihydroxy portion (PubMed:31790246). The production of aldehyde virensol C by virA alone is surprising, since virA does not contain a reductase (R) domain that is typically associated with reductive product release in HRPKS (PubMed:31790246). The cupin-domain enzyme virC is involved in enhancing virA product turnover (PubMed:31790246). The short-chain dehydrogenase virB then oxidizes the C-7 alcohol of virensol C to a ketone, yielding virensol D (PubMed:31790246). Virensol D is further transformed to salicylaldehyde 5-deoxyaurocitrin by the short-chain dehydrogenase virD (PubMed:31790246). VirD catalyzes the dehydrogenation of C-3 to form the beta-ketone aldehyde, which is followed by the generation of the nucleophilic C-2 that is required for the intramolecular aldol condensation between C-2 and C-7, itself followed by dehydration and aromatization which leads to salicylaldehyde 5-deoxyaurocitrin (PubMed:31790246). While the dehydrogenation of virensol D is definitely catalyzed by virD, the aldol condensation and dehydration may be uncatalyzed or assisted by virD (PubMed:31790246). The short chain dehydrogenase virG then converts salicylaldehyde 5-deoxyaurocitrin into virensol B which is further hydroxylated by the cytochrome P450 monooxygenase virE to yield the hydroquinone virensol A (PubMed:31790246). VirI then may oxidize virensol A to form the quinone, while virH performs the epoxidation (PubMed:31790246). Finally, the two remaining short-chain dehydrogenases, virK and virL, are probably responsible for reducing the ketones to the corresponding alcohols to furnish the epoxycyclohexanol structure in trichoxide (PubMed:31790246). SIMILARITY: Belongs to the oxidoreductase OpS7 family."}
{"protein": "MVETTGISDQTKKVLIGVAAAATVAGVGYLVYKSFGGSDLERDLEEIKALGNLKFKEKQYDSALEAFTKGVEKAGPNSSDQIVAMLYQNRAACREKVGHSPFDILNDCMAALKVDKKYTKAYLRAAKALNDVGKKQDALAYLLAAFTLDSSLNKTNFEFFGKLLAIEPMSDCHIGKPLKIEDVKPQPVALFRIQQWCDTWDILDLFKTDLTRFEPEVLSEDQKQYQLALEKFKKGKYEELIDLLTEENSYPPAMILRGKMLSYSTDPNEATRYIDKVGAKINELIGSEEDEERKKLMRDAFDILKIELMYTMADLDKFLESVPKDDKERLFKLYSFASIFVVIRLNHFYSLKIWFQYNGCVLDTAVTNHEQQMMADTNNANRLLTEAEKNGTLTPHLSMIVTFLKLCTSEDYADVHRRIREMEELAESRSTHFNLVLMSKVYMMTNNEESSKKLLEEAARITTRYLVPSRHLQTADLHVHKPEAERLRLTTESANAAIAVDPFNFSAHVLHLLGTNGPEPMIKKENYERAMESIRNAALFAPPRELLMLKRMIPLMNAKKRAAEMLDMY", "text": "FUNCTION: Receptor that accelerates the import of all mitochondrial precursor proteins. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Tom70 family."}
{"protein": "MNSKGQYPTQPTYPVQPPGNPVYPQTLHLPQAPPYTDAPPAYSELYRPSFVHPGAATVPTMSAAFPGASLYLPMAQSVAVGPLGSTIPMAYYPVGPIYPPGSTVLVEGGYDAGARFGAGATAGNIPPPPPGCPPNAAQLAVMQGANVLVTQRKGNFFMGGSDGGYTIW", "text": "FUNCTION: In unstressed cells, promotes SIAH1-mediated polyubiquitination and degradation of the serine/threonine-protein kinase HIPK2, probably by acting as a loading factor that potentiates complex formation between HIPK2 and ubiquitin ligase SIAH1 (By similarity). In response to DNA damage, localizes to the nucleus following phosphorylation by HIPK2 and modulates the expression of a subset of TP53/p53 target genes by binding to TP53 at target gene promoters (By similarity). This limits the expression of a number of cell death-mediating TP53 target genes, reducing DNA damage-induced cell death (By similarity). Enhances the binding of transcription factor TCF7L2/TCF4, a Wnt signaling pathway effector, to the promoters of target genes (By similarity). Plays a role in stress granule formation (By similarity). FUNCTION: In unstressed cells, promotes SIAH1-mediated polyubiquitination and degradation of the serine/threonine-protein kinase HIPK2, probably by acting as a loading factor that potentiates complex formation between HIPK2 and ubiquitin ligase SIAH1 (PubMed:33591310). In response to DNA damage, localizes to the nucleus following phosphorylation by HIPK2 and modulates the expression of a subset of TP53/p53 target genes by binding to TP53 at target gene promoters (PubMed:33591310). This limits the expression of a number of cell death-mediating TP53 target genes, reducing DNA damage-induced cell death (PubMed:33591310). Enhances the binding of transcription factor TCF7L2/TCF4, a Wnt signaling pathway effector, to the promoters of target genes (By similarity). Plays a role in stress granule formation (PubMed:17984221). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus speckle Nucleus, nuclear body Cytoplasm, Stress granule Note=Predominantly nuclear in macrophages, stimulation of IL17RB with its ligand IL17E induces accumulation in the cytoplasm (PubMed:22070932). Predominantly cytoplasmic when unphosphorylated and localizes to the nucleus following phosphorylation by HIPK2 (PubMed:33591310). Localizes to stress granules under cellular stress conditions (PubMed:17984221). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus speckle Nucleus, nuclear body Cytoplasm, Stress granule Note=Predominantly nuclear in macrophages, stimulation of IL17RB with its ligand IL17E induces accumulation in the cytoplasm (By similarity). Predominantly cytoplasmic when unphosphorylated and localizes to the nucleus following phosphorylation by HIPK2 (By similarity). Localizes to stress granules under cellular stress conditions (By similarity)."}
{"protein": "GVDKAGCRYMFGGCSVNDDCCPRLGCHSLFSYCAWDLTFSD", "text": "FUNCTION: Toxin that blocks vertebrate P/Q-type (Cav2.1/CACNA1A) and R- type (Cav2.3/CACNA1E) voltage-gated calcium channels. Also inhibits sodium channels (Nav) in bovine chromaffin cells by delaying sodium channel inactivation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 56 (SNX-482) subfamily."}
{"protein": "MGFISYFSSFLPDIPWHFWGSVDSLLQGLVGACAVSVLYNLTRVHLYIMCLNDPDKQKEAAQLRAQSLLMDFLHVSLLTLIYSLLGPRVGALVVLEFSLRAVSMVLSVSKGAGSSQLFLLCQFSLGCGVSCSLDYLHEGAPHRTWNLLLAVGLSWLILWQSRRMCRHVGIMYQLHSRERYCGVCLSLLASWHDIPPFLRRALKVAFLVSDLAAVAVINRDFLSTSEAMRFWTPLTICYTLLVIYMQEEQQQNPSEQMVYQTVFVRMGGLLILMMTVGRWADILHIFISLTGEIWCLIHAGVMLRICREQDFADRISSPRKAPISRGSIYTRDGRTLQRETSLEE", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM82 family."}
{"protein": "MLSSIKCVLVGDSAVGKTSLLVRFTSETFPEAYKPTVYENTGVDVLMDGIQISLGLWDTAGNDAFRSIRPLSYQQADVVLMCYSVANHNSFLNLKNKWIGEVRSNLPCTPVLVVATQTDQREVGPHRASCVNAIEGKRLAQDVRAKGYLECSALSNRGVQQVFECAVRTAVNQARRRNRRRFFSINECKIL", "text": "FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. Inhibits the activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38 by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively regulates leukotriene production in neutrophils. Negative regulator of hematopoietic progenitor cell proliferation, survival and migration. Critical regulator of thymocyte development and T-cell antigen receptor (TCR) signaling by mediating recruitment and activation of ZAP70. Required for phosphorylation of CD3Z, membrane translocation of ZAP70 and subsequent activation of the ZAP70-mediated pathways. Essential for efficient beta-selection and positive selection by promoting the ZAP70- dependent phosphorylation of the LAT signalosome during pre-TCR and TCR signaling. Crucial for thymocyte maturation during DN3 to DN4 transition and during positive selection. Plays critical roles in mast cell function by facilitating phosphorylation of SYK in Fc epsilon RI- mediated signal transduction. Essential for the phosphorylation of LAT, LCP2, PLCG1 and PLCG2 and for Ca(2+) mobilization in mast cells. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor; Cytoplasmic side Note=Colocalizes together with ZAP70 in the immunological synapse. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."}
{"protein": "MECIQHESCFDVDDREDAQQIKEQEGTEMVSITQAAKLHNVTRQAIYVAIKQKKLKASKTTRWEIDLKDLEDYKRNRYSRKKSLYQGELLFDNEKGCYSVNQVADMLGIPVQKVYYATRTGTMRGERKGAAWVISQSEIDRYKSEYLNKQTAKKAKGVTVVEHAIAKPEETVSSETLLFENN", "text": "SIMILARITY: Belongs to the EUO family."}
{"protein": "MTSFTVSPPPHIKKKIFIKNLIWSRIVALLPISAAAVYFFGFAALGNIIASILGAVGIEFVIQKAFNKKLTIMDGNAIYLGLLLALICPPTLPAWMIFIGGAFAVGVGKHAFGGIGSYTFHPSLAAWVFLSLAWAQDMLPGTIPILSSFSDLILENGAGFLTDVSPILVLLAGVILILVKYIEWRIPLSYLLTTVILALVLGDPLAYVVSGTFLLGVFFIATETVTSPVTQNGRIVYGILCGFLTVIYGYFSGNYVWGTLYALLLSNAVAPFIELKTLPKPMGGVANE", "text": "FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Catalyzes Na(+) transport, most probably coupled to electron transfer from reduced ferredoxin to methanophenazine and heterodisulfide reductase. Involved in heterodisulfide reduction during methanogenesis from acetate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrB/RnfD family."}
{"protein": "MARSCVTDPRWRELVALYRYDWIAAADVLFGKTPTWQQDEIIESTQQDGSWTSVTSGHGTGKSDMTSIIAILFIMFFPGARVILVANKRQQVLDGIFKYIKSNWATAVSRFPWLSKYFILTETSFFEVTGKGVWTILIKSCRPGNEEALAGEHADHLLYIIDEASGVSDKAFSVITGALTGKDNRILLLSQPTRPSGYFYDSHHRLAIRPGNPDGLFTAIILNSEESPLVDAKFIRAKLAEYGGRDNPMYMIKVRGEFPKSQDGFLLGRDEVERATRRKVKIAKGWGWVACVDVAGGTGRDKSVINIMMVSGQRNKRRVINYRMLEYTDVTETQLAAKIFAECNPERFPNITIAIDGDGLGKSTADLMYERYGITVQRIRWGKKMHSREDKSLYFDMRAFANIQAAEAVKSGRMRLDKGAATIEEASKIPVGINSAGQWKVMSKEDMKKKLNLHSPDHWDTYCFAMLANYVPQDEVLSVEDEAQVDEALAWLNE", "text": "FUNCTION: Component of the molecular motor that translocates genomic DNA in empty capsid during DNA packaging. Heterooligomerize with small terminase protein to be docked on capsid portal protein. Forms a ring- like structure through which genomic DNA is translocated into the capsid. May have or induce an endonuclease activity to cleave the genome concatemer after encapsidation. FUNCTION: Component of the molecular motor that translocates genomic DNA in empty capsid during DNA packaging. Heterooligomerize with small terminase protein to be docked on capsid portal protein. Forms a ring- like structure through which genomic DNA is translocated into the capsid. May have or induce an endonuclease activity to cleave the genome concatemer after encapsidation. SIMILARITY: Belongs to the punalikevirus large terminase family."}
{"protein": "MSSGAPQKSSPMASGAEETPGFLDTLLQDFPALLNPEDPLPWKAPGTVLSQEEVEGELAELAMGFLGSRKAPPPLAAALAHEAVSQLLQTDLSEFRKLPREEEEEEEDDDEEEKAPVTLLDAQSLAQSFFNRLWEVAGQWQKQVPLAARASQRQWLVSIHAIRNTRRKMEDRHVSLPSFNQLFGLSDPVNRAYFAVFDGHGGVDAARYAAVHVHTNAARQPELPTDPEGALREAFRRTDQMFLRKAKRERLQSGTTGVCALIAGATLHVAWLGDSQVILVQQGQVVKLMEPHRPERQDEKARIEALGGFVSHMDCWRVNGTLAVSRAIGDVFQKPYVSGEADAASRALTGSEDYLLLACDGFFDVVPHQEVVGLVQSHLTRQQGSGLRVAEELVAAARERGSHDNITVMVVFLRDPQELLEGGNQGEGDPQAEGRRQDLPSSLPEPETQAPPRS", "text": "FUNCTION: Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis. SIMILARITY: Belongs to the PP2C family."}
{"protein": "MERYTKKNERFKAEEGKGSKKSRTFLTERERRALFNDRFFDLKNLIPNPTKGGEASIVQDGIVYINELQRLVSELKYLVEKKKCGARHNNIEVDNKNTIYGTSKIEHPFSKNKNTFNCLIRTLRFVHHF", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bHLH protein family."}
{"protein": "MASVSSSPSYSSQAAVLLLLHQPPHQHGHGGACLRYRGSQSQGRGNAVATSLGLSAAGRGGAGGLLLLPPLPALRAAEGKDGRAVTKDEEEEAAAAAVEEEGEVEVRREEDKPGDDGSREAAARGSGSGRFSADYISLGIREPVYEVIEVKSNGRMSTKKISRRQLLKSSGLRLRDTRSVDPSLWLMNSMPSLLVREQAILVNLGSLRAIAMHERVLIFNYNSPGGKAFLDSLLPRLNPRNINGGPAMPFQLEVVEAALLSRIQRLERRLMRIEPRVGALLEVLPNRLTADVLEQLRLSKQALVELGSRAGDLKQMLIDLLDDPHEIRRICIMGRNCTLDKLSDNMECSVPLEKQIAEEEEEEIEMLLENYLQRCESIHGQAERLLDSAREMEDSIAVNLSSRRLEVSRVELLLQVGTFCVAIGALIAGIFGMNLKSYLETNAWAFWATTGGIVVGAVAGFFIMYSYLKTRKIL", "text": "FUNCTION: Magnesium transporter that may mediate the influx of magnesium in chloroplast. SUBCELLULAR LOCATION: Plastid. Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35.5) family."}
{"protein": "MRMADHFEETTMGTFLADYYLWTKSLHVISVLAWMAGLFYLPRLFVYHAEVVKAGTETDALFQTMERRLLRAIMNPAMIATWIFGLLLVFTPGIVDWSMLWPWTKAACVLAMTGFHMWLAARRRDFAAGANRHKGRTYRMMNELPTLLMLVIVFSAVAKWNYWGF", "text": "FUNCTION: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX. Is involved in the biosynthesis of tetrapyrrole molecules like heme and chlorophyll. Does not use oxygen or artificial electron acceptors such as menadione or benzoquinone. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HemJ family."}
{"protein": "MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRSRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGF", "text": "FUNCTION: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored- polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin family."}
{"protein": "MKIRHWSALSLFVLPALAQAEALTGEVHRQPLNIQAIVMFLLFVGGTLYITYWASKRTRSRQDYYTAGGRITGFQNGLAIAGDYMSAASFLGISALVYASGYDGLIYSIGFLIGWPIILFLIAERLRNLGRYTFADVASYRLQQRPIRTLSACGSLVVVALYLIAQMVGAGKLIQLLFGLNYHVAVVLVGILMVLYVLFGGMLATTWVQIIKAVMLLSGATFMAIMVMKSVNFNFNTLFSEAVKVHPKGLSIMSPGGLVSDPISALSLGLALMFGTAGLPHILMRFFTVSDAKEARKSVFYATGFIGYFYILTFIIGFGAILLVGPNQTFKDAAGALLGGNNMAAVHLANAVGGSFFLGFISAVAFATILAVVAGLTLAGASAVSHDLYASVIKKGKANERDELRVSKITVIILGIVAIGLGILFEKQNIAFMVGLAFSIAASCNFPIIIISMYWDKLTTRGAMIGGWLGLSTAVILMILGPTIWVTILGHEKPIYPYEYPALFSMIAAFIGTWFFSITDNSETGKQERLLFKSQFVRSQTGLGASKGGAH", "text": "FUNCTION: Transports acetate. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family."}
{"protein": "MEDDNSNNNNNNNVIAPFIVKTYQMVNDPSTDWLITWGPAHNSFIVVDPLDFSQRILPAYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEHFLRGQKHLLNNIARRKHARGMYGQDLEDGEIVREIERLKEEQRELEAEIQRMNRRIEATEKRPEQMMAFLYKVVEDPDLLPRMMLEKERTKQQQQVSDKKKRRVTMSTVKSEEEEVEEDEGRVFRVMSSSTPSPSSTENLYRNHSPDGWIVPMTQGQFGSYETGLVAKSMLSNSTSSTSSSLTSTFSLPESVNGGGGGGCGSIQGERRYKETATFGGVVESNPPTTPPYPFSLFRGGF", "text": "FUNCTION: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HSF family. Class C subfamily."}
{"protein": "MSEDEEKVKLRRLEPAIQKFTKIVIPTDLERLRKHQINIEKYQRCRVWDKLHEEHINAGRTVQQLRSNIREMEKLCLKVRKDDLGLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETFLQPSLTRSMTVGGTFHSTEDEADPQSMTQIYALPEIPRDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIEDHVNTAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGVVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRRKQKMMEKLASSCPDLPSQTDKKCS", "text": "FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane. May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Smooth endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein Cytoplasm, cytosol Mitochondrion membrane; Multi-pass membrane protein Note=Has a hairpin-like insertion into membranes. Localizes to the completed autophagosome membrane upon cell starvation. SIMILARITY: Belongs to the syntaxin family."}
{"protein": "MKLLTALSELISIFLFTTIFIFLARKVAIKIGLVDKPNFRKRHQGVIPLVGGISVFAGICFMFGLSDYYIPHLSLYLICAGVLVFVGAMDDRFDISVKIRAVVQAVIAVVMMVIAKLHLGSLGYIFGPWELVLGPFGYFLTLFAVWAAINAFNMVDGIDGLLGGLSSVSFAAMGLILWFDGQTSLAMWCFAMIAAILPYIMLNLGILGRRYKVFMGDAGSTLIGFTVIWLLLETTQGKTHSISPVTALWIIAIPLMDMVAIMYRRLRKGMSPFSPDRQHIHHLVMRAGFTSRQAFVLITLAAAILAGVGVTAEYSHFVPEWVMLVLFLLAFFLYGYCIKRAWKVARFIKRVKRRLRRQRKNRPNLTK", "text": "FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA subfamily."}
{"protein": "MAIIMAESSYERRIKALYEKQIRMEALEGKFIKKVFKFNSVLLDIKETSARHQRKVGKMQKVVTERREELGRRVTFMGHLTQEVEAIKLRNLAMKDQIKQQKMLNNQRKNEIMERIHTLSKTTGTYVNQEALPARVKGVTVIPGDRRNQLIPFDLNATDDEGLNSLCQHLESLNVDVSQWQQLVSLAMDVALGARAPTTPPKEAANCKSIIEIDLTSPTS", "text": "FUNCTION: Acts as a component of the essential kinetochore-associated Ndc80 complex, which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the SPC25 family."}
{"protein": "MLPRKLKIDSTELAEITNELVQFLNCLVLRSGGLKKEHIWVRNGRILDERTVFFEEKTMADVQIDCEGLILSPGFIDLQLNGGFGIDFSTYNSDDKEYQEGLALVAKQLLAHGVTSFSPTVITSSPETYHKILPLLKPSNASSEGAGNLGAHLEGPFISADKRGCHPEQLVITSLSPNPVEIIEHVYGSTENIAIVTMAPELEGAQEAIEYFVSTGTTVSVGHSSAKLGPGEMAVLSGAKMITHLFNAMQSYHHRDPGLIGLLTSSKLTPDHPLYYGIISDGIHTHDSALRIAYHTNSAGLVLVTDAIAALGMSDGVHKLGTQTIHVKGLEAKLDGTNTTAGSVASMPYCIRHLMKATGCPIEFALQSATHKPATLLGVSDEKGTLDVGRLADFVLIDKNVTVKATFCSGKRVFLAQD", "text": "SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. NagA family."}
{"protein": "MARSRGERTPAARRITSRNARFQQWQALLGNRNKRTRAGEFLVMGVRPISLAVEHGWPVRTLLYDGQRELSKWARELLRTVRTEQIAMAPDLLMELGEKNEAPPEVVAVVEMPADDLDRIPVREDFLGVLFDRPTSPGNIGSIIRSADALGAHGLIVAGHAADVYDPKSVRSSTGSLFSLPAVRVPSPGEVMDWVEARRAAGTPIVLVGTDEHGDCDVFDFDFTQPTLLLIGNETAGLSNAWRTLCDYTVSIPMAGSASSLNAANAATAILYEAVRQRISGRTATTP", "text": "FUNCTION: Specifically methylates the 2'-O-ribose position of uridine- 2479 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TsnR/AvirB family."}
{"protein": "MDHLDLTQLTTCVSDLAAQSSSLAAKCHQIDTNGASRTMDKVSPSLAREILQLKESMAATAGKLQRMVQEPPDFLQRLAHQAQLLACIQWLAEFQILAFIPLDRSVPIEDIAELASVPKEHLSRIVRLTATAGFLQEPPSEMGHVAHTPLSTQFVTELSYLDAAMFLADLAAPTALQMTKTTKRFGQSPSPSHSAYNMARGTAAPFANMWDDHSIKLRRQWPAYLKHVVNSQAKSSSSDLLESLGCMDRLQGAIQCIVEVGAESAERAILLARRYPSAQFAVQLSGPAIPGGVWTAGPPDQAQKEVLIAGRIDVSRRAVGSPQPISEAALYILDLSISSLNLGQPKEHVSAELRAHLDILRLNRNSALVLISFILPDTRTGSLEEETMTSLRELCMLQLHNQQLLSFKELSELIHNTNDRMGHLSVVREAFSGTRDAIALEIHYQAHSV", "text": "FUNCTION: Transcriptional coactivator; part of the gene cluster that mediates the biosynthesis of dibenzodioxocinones such as pestalotiollide B, a novel class of inhibitors against cholesterol ester transfer protein (CEPT). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MKHWFFLIILFFMNCSWGQDPFDKTQRNRSQFDNAQTVMEQTEIISSDVPNNLCGADENRQAAEIPLNALKLVGVVISKDKAFALLQDQGLQVYSVLEGVDVAQEGYIVEKINQNNVQFMRKLGEQCDSSEWKKLSF", "text": "FUNCTION: Involved in transformation (competence for DNA uptake)."}
{"protein": "MQRQRGFTLLEIMVVIVILGVLASLVVPNLMGNKEKADRQKVVSDLVALEGALDMYKLDNSRYPTTEQGLQALVSAPSAEPHARNYPEGGYIRRLPQDPWGSDYQLLSPGQHGQVDIFSLGPDGVPESNDDIGNWTIGKK", "text": "FUNCTION: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP G family."}
{"protein": "MNVTITSPFWKRRRDQIVESVIPYQWGVMNDEIDTTVPDDPAGNQLADSKSHAVANLKVAAGELDDEFHGMVFQDSDVYKWLEEAAYALAYHPDPELKALCDRTVDLIARAQQSDGYLDTPYQIKSGVWADRPRFSLIQQSHEMYVMGHYIEAAVAYHQVTGNEQALEVAKKMADCLDANFGPEEGKIHGADGHPEIELALAKLYEETGEKRYLTLSQYLIDVRGQDPQFYAKQLKAMNGDNIFHDLGFYKPTYFQAAEPVRDQQTADGHAVRVGYLCTGVAHVGRLLGDQGLIDTAKRFWKNIVTRRMYVTGAIGSTHVGESFTYDYDLPNDTMYGETCASVAMSMFAQQMLDLEPKGEYADVLEKELFNGSIAGISLDGKQYYYVNALETTPDGLDNPDRHHVLSHRVDWFGCACCPANIARLIASVDRYIYTERDGGKTVLSHQFIANTAEFASGLTVEQRSNFPWDGHVEYTVSLPASATDSSVRFGLRIPGWSRGSYTLTVNGKPAVGSLEDGFVYLVVNAGDTLEIALELDMSVKFVRANSRVRSDAGQVAVMRGPLVYCAEQVDNPGDLWNYRLADGVTGADAAVAFQADLLGGVDTVDLPAVREHADEDDAPLYVDADEPRAGEPATLRLVPYYSWANREIGEMRVFQRR", "text": "FUNCTION: Beta-L-arabinofuranosidase that removes the beta-L- arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara- beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl- beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. SIMILARITY: Belongs to the glycosyl hydrolase 127 family."}
{"protein": "MAAAIGLRVVGRRLGLGLGRTPRRALWGGHSKKEEKEVEENSIIPQEKKEPSLICPPPRSRKYVPPENIQSILEARVKEICGPSLAGNWLQTSLKDNRLKYQLLAQLAAELGHAVPNSQLHLMCSAQDVLTFYSTPVKDMLKFDELCAAELPPNLKIAWER", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL50 family."}
{"protein": "MTKSNGEEPRMGGRMERLQQGVRKRTLLAKKKVQSLTKEDVKSYLFRNAFVLLTVTAVIVGTILGFALRPYKMSYREVKYFSFPGELLMRMLQMLVLPLIISSLVTGMAALDSKASGKMGMRAVVYYMTTTIIAVVIGIIIVIIIHPGKGTKENMYREGKIVQVTAADAFLDLIRNMFPPNLVEACFKQFKTSYEKRSFKVPIQSNETLLGAVINNVSEAMETLTRIREEMVPVPGSVNGVNALGLVVFSMCFGFVIGNMKEQGQALREFFDSLNEAIMRLVAVIMWYAPLGILFLIAGKIVEMEDMGVIGGQLAMYTVTVIVGLLIHAVIVLPLLYFLVTRKNPWVFIGGLLQALITALGTSSSSATLPITFKCLEENNGVDKRITRFVLPVGATINMDGTALYEALAAIFIAQVNNFDLNFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELKNRDVEMGNSVIEENEMKKPYQLIAQDNEPEKPVADSETKM", "text": "FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:7903437, PubMed:28032905). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (PubMed:15363892, PubMed:15390100, PubMed:16880397). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. SLC1A3 subfamily."}
{"protein": "MGSIGEPNRLLCWSIYVTKKPDQSEEDHHNHVSKVNAPMMIPFLKKYGIVRYTVKHNDAHSKPKQAALMAGQPEENVLAYDTVFEMIVKDIESIQTMQKDEEFLRTTIPDHFNFADMTRSKGSLTWIEEFTF", "text": "FUNCTION: Dehydratase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin (PubMed:29844193). The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction with oxygen molecules (PubMed:11701851). These reactive oxygen species cause damage to various cellular components including lipids, proteins and nucleic acids (PubMed:11701851). The first step of cercosporin biosynthesis is performed by the polyketide synthase CTB1 which catalyzes the formation of nor-toralactone (Probable). The starter unit acyltransferase (SAT) domain of CTB1 initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain. The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (Probable). The bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (Probable). The O-methyltransferase CTB2 further methylates the nascent OH-6 of the CBT3 product, blocking further oxidation at this site before the reductase CTB6 reduces the 2-oxopropyl ketone at position C7, giving naphthalene (Probable). The FAD-dependent monooxygenase CTB5 in concert with the multicopper oxidase CTB12 are responsible for homodimerization of naphthalene with CTB7 installing the dioxepine moiety, finally producing cercosporin (Probable). The fasciclin domain- containing protein CTB11 might act with CTB5 and CTB12 whereas the roles of CTB9 and CTB10 have still to be elucidated (By similarity). SIMILARITY: Belongs to the tpcK family."}
{"protein": "MAADVVGDVYVLVEHPFEYTGKDGRRVAIRPNERYRLLRRSTEHWWHVRREPGGRPFYLPAQYVRELPALGNPAAAAPPGPHPSPAAPEPLAYDYRFVSAAATAGPDGAPEESGGRASSLCGPAQRGAATQRSSLAPGLPACLYLRPAAPVRPAQSLNDLACAAVSPPAGLLGSSGSFKACSVAGSWVCPRPLARSDSENVYEVIQDLHVPPPEESAEQVDDPPEPVYANIERQPRATSPGAAAAPLPSPVWETHTDAGTGRPYYYNPDTGVTTWESPFEAAEGAASPATSPASVDSHVSLETEWGQYWDEESRRVFFYNPLTGETAWEDEAENEPEEELEMQPGLSPGSPGDPRPPTPETDYPESLTSYPEEDYSPVGSFGEPGPTSPLTTPPGWSCHVSQDKQMLYTNHFTQEQWVRLEDPHGKPYFYNPEDSSVRWELPQVPVPAPRSIHKSSQDGDTPAQASPPEEKVPAELDEVGSWEEVSPATAAVRTKTLDKAGVLHRTKTADKGKRLRKKHWSASWTVLEGGVLTFFKDSKTSAAGGLRQPSKFSTPEYTVELRGATLSWAPKDKSSRKNVLELRSRDGSEYLIQHDSEAIISTWHKAIAQGIQELSAELPPEESESSRVDFGSSERLGSWQEKEEDARPNAAAPALGPVGLESDLSKVRHKLRKFLQRRPTLQSLREKGYIKDQVFGCALAALCERERSRVPRFVQQCIRAVEARGLDIDGLYRISGNLATIQKLRYKVDHDERLDLDDGRWEDVHVITGALKLFFRELPEPLFPFSHFRQFIAAIKLQDQARRSRCVRDLVRSLPAPNHDTLRMLFQHLCRVIEHGEQNRMSVQSVAIVFGPTLLRPEVEETSMPMTMVFQNQVVELILQQCADIFPPH", "text": "FUNCTION: Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein."}
{"protein": "MYGGICLCVLLAVLAISSSGQHISRSLNGNSLAAAIEQNFPEKHRPARTPDSNQRVESNIDEKANLGVLLARYLQKARRGTNGKPPDPKKESQDYLGWMDFGRRSAEEYEYSS", "text": "FUNCTION: Cholecystokinin-22: hypotensive neuropeptide that binds cholecystokinin receptor type A receptor (CCKAR). FUNCTION: Cholecystokinin-8: hypotensive neuropeptide that binds cholecystokinin receptor type A receptor (CCKAR). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family."}
{"protein": "MESSVPLGNSVRTGAACGRIMAVPSKAAQGDARARWKLLGQALRKERLDDSLQKVSVRRFNSFRLFSVVEMKEIKREADCQTWFQYTCVFCPQYSLCLRHNSGISNVADILTSFDNTGNVCVWPSEEVMAYYCLKHKDIFRGLAVCELGGGMTCLAGLMVAISADVKEVLLTDGNEKAIKNVSDIIRRPQNEEMFKDRLVSSRVLRWDNETDVSQLEGHFDIVICADCLFLDQYRACLVDAIKRLLKPSGKAMVFAPPRGNTLSQFCNLAEAAGFSIQRHENYDEHISNFHSKLKEKEAAVYDENLHYPFLLVLCKTR", "text": "FUNCTION: Catalyzes the trimethylation of 'Lys-116' in calmodulin. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family."}
{"protein": "MDITKENYYEELDNIAKNIKDSCFISFDAEFSAILTKESFKYSLFDTNEERYNKYKTQISTMKMMQVGLTMFQYDRELDAYLATGYTFHLCPQLIGTINQSLIFQASTLKFLCKHNFDFNKFIYEGLPYLSKSDEALLNRYRIENNLFDYVSESLEFDEEKQINQCSSEVSKWLSSSIEDTMYLDIDNAICRYLLHLELRQRYPGILTTDSLGNSKKILIYRDKNVEGAKNAPIAILEDNLIAYLLGFLHVIKLLETHKKPIVGHNMFLDMLFLHNQFIGPLPDSYTMFKKNINSVFPTIFDTKYISHAMSKKLTFSESWKSNALQDLYEFFAERKCKKLEYGINIVRLTTPFDIKQSYHEAGWDAYCSGYCFIRLGHWAACENRGKSHVIGPREKLAALAPYCNKVNVIRGGVSYMNFSENDPPRNRPVLLHVKCLKDTVIDVEKVASLLGSFGSIDIKPCGKRAALVATGAQFMVDKILKTYENNRDYRISKYSVYKHSVAGRFAIWSGSIVTGGLALYLIHKKFKSILL", "text": "FUNCTION: 3'-5' exonuclease that specifically cleaves precursor piRNAs (pre-piRNAs) at their 3' ends (PubMed:26919431). Trims pre-piRNAs to their mature size, a process required for piRNAs maturation and stabilization, and subsequent pre-piRNAs 2'-O-methylation (PubMed:26919431). The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (PubMed:26919431). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CAF1 family."}
{"protein": "MSTEKILTPESQLKKTKAQQKTAEQIAAERAARKAANKEKRAIILERNAAYQKEYETAERNIIQAKRDAKAAGSYYVEAQHKLVFVVRIKGINKIPPKPRKVLQLLRLTRINSGTFVKVTKATLELLKLIEPYVAYGYPSYSTIRQLVYKRGFGKINKQRVPLSDNAIIEANLGKYGILSIDDLIHEIITVGPHFKQANNFLWPFKLSNPSGGWGVPRKFKHFIQGGSFGNREEFINKLVKAMN", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MVAAKENKFLTVAPFECAWSDDLKFREAGRGCVAFDAFAHNDVTVVFRENVGTQHYHYKKDNSPHYIVIIGSNRNRRLKIQVDGKSVVDEEASDLCRCSLEFQSYWISIYDGLISIGKGRYPFQNLVFKWQDPKPNCNVQYVGLSSWDKHVGYRNVSVFPVTHNHILLWKQVDCREVRGDESGDEKVVEEGTGYDYEQWGLGNFLESWQLSDTVFLVGEEEMDVPAHKVILQASGNFPLRSSDGDVIQLRGVSYPILHALLQYIYTGRTQILESELAPLRDLSSKFEVMSLVRQCEESIDHFKLSKTAFDSCRKVKLLCPISHPLSGFMFPSAFPVDVGKLVKLYSTGEYSDIKIYLSDHSLTFQSHKVILSLWSVAFAKMFTNGMSESHSSTIYLTDVSPEAFKAMMNFMYSGELNMEDTVNFGTELIHLLFLADRFGVVPLHQECCKMLLECLSEDSVCSVLQVVSSISSCKLIEEMCKRKFSMHFDYCTTASLDFVLLDQTTFSDILESADLTVTSEEKILNAVLMWCMKAEESHSWGVIDEMMNYADPKSLFKERLQSLDDLLPHVRFSLLPYELLKRLENSNLSKEIPVFNRLLKEAASFLTSGLISPGNEPISRFQHRRSSFKELQYIRDGDSNGVLHFVGTSYGSHQWVNPVLAKKINITSSSPTSRFTDPKALASKAYAGTSFAGPRMEDGHISSWWVVDLGEEHQLMCNYYTFRQDGSRAFTRFWKFQGSMDGKTWTDLRVHEDDQTMCKAGQFASWPITAANALLPFRFFRLVLTGPTADTSTPWNFCICYLELYGYFR", "text": "FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin- protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins."}
{"protein": "MIVIGRSIVHPYITNEYEPFAAEKQQILSIMAGNQEVYSFRTADELSFDLNLRVNIITSALELFQSGFQFRTFQQSFCNPQFWERTSLGGFQLLPNIAPSIAIQDIFKNGKLYGTECATAMIIIFYKALLSLYEEKTFNRLFANLLLYTWDYDRDLKLITKTSGDIVPGDLVYFKNPQVNPATIEWQGENAIYLGNFFFYGHGVGVKTKEEIIYSLNERRIPYAFISAYLTDFITRIDSRMMSQYAPPNTPQTSIGFIPIRDDAIVATVGHTTTIY", "text": "FUNCTION: Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. SIMILARITY: Belongs to the bacillus TGase family."}
{"protein": "MASVYENSYMIVLIFLLLGILLPVVALTLGRMLRPSKPSAAKATTYESGIEPFHDANIRFHARYYIFALLFVIFDVETLFLYPWAVAYDKLGLFALIEMFIFVVMLLVGLAYAWKKKVLQWL", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family."}
{"protein": "QKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG", "text": "FUNCTION: Ubiquitin Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin family."}
{"protein": "MRTLGAMAIMLVVMGTVIFLSFILRSRDILCGKTMKSHVISAVETSQLMVDHAVYNTMKRNLKKREVLSPAQLLSFFKLPESTSGAISRAAEIMETSIQVMKREQSQFSTDALSADILGTIANLSGCLPFMLPPRCPDTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPKGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQSTSTAAFWGGVDCQLTCENQNPCFPIQLPSNSSGTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSSAGLLRVNTLHLDAGRAYLPFATAACAPEPGTPRTNRTPCFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQYVGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEHTELPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKLQVQGQLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKHSLPRVICDNTGLTRVPVDAFRIGKFPQDFESCEDIPSMDLELWRETFPQDDKCVFPEEVDNGNFVHCEESGKLVLVYSCFHGYKLQGQEQVTCTQKGWDSEPPVCKDVNECADLTHPPCHPSAQCKNTKGSFQCVCTDPYVLGEDEKTCIDSGRLPRASWVSIALGALLIGGLASLTWIVICRWTHADKKATLPITERVTTQSGCRKSQGRGISPHKAAAQDTGQEPASGSRVLLCE", "text": "FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peroxidase family. XPO subfamily."}
{"protein": "MKNDHINYQQNLSQSPILNSNKNQTQQNQQQQQQQQQQNPQQQQQFQHQQVPQLSPQQIPFSEPLKNNLTLQHQQQQQQHQQLAGGQHGSLLRKSYSSRFHEKPQGELTKIANFQDVSPEERPSLFLLKLKQCCYVYDFSDNTYMVSKGVKQEALLQCVNFLSTNDQPLHESIYKMVFEMVAVNLFRPLPPRINPYGVMYDPEEDEPILEAAWPHIQVVYEVLLRFIDSPTFNTHIAKNYVDDRFVLQMLDLFDSEDPRERDYLKTTLHRIYGKFLGLRGFIRTAIRNLFCTFVYESHQHNGISEILEVLGSIINGFLVPLKDEHKQFLIKVLIPLHKPKSYSVYCSHLGYCMSQFIEKEPSLAEPIFKSILRLWPCGNSQKEVLFLSEMEDLLGLVSDEQFAKFRNQFFRQMTKCFQSEHFQVAERALYLFSNENIVLLIASKNNFTLALETFYKPLHENSISHWNRSIRNLSISSLKLFMEIDMDLFNKISEKYKESKKKQQQIQQREKFKQNAPETQKSKQINQNNNNNNNNINNNNNNNNNNNGSTETKADKPSMIRRKSLLPVDPSTIAALSSHRSLEDIMSTNSNSGNDDDDENNHTNHDSEIENEVKEDFRVPVNNRYTFT", "text": "FUNCTION: Involved in developmental cell fate decision. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 family."}
{"protein": "MLPINNNFSLPQNSFYNTISGTYADYFSAWDKWEKQALPGEERDEAVSRLKECLINNSDELRLDRLNLSSLPDNLPAQITLLNVSYNQLTNLPELPVTLKKLYSASNKLSELPVLPPALESLQVQHNELENLPALPDSLLTMNISYNEIVSLPSLPQALKNLRATRNFLTELPAFSEGNNPVVREYFFDRNQISHIPESILNLRNECSIHISDNPLSSHALPALQRLTSSPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYPQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLALRLPENGSQLHHS", "text": "FUNCTION: Effector E3 ubiquitin ligase that interferes with host's ubiquitination pathway and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell (PubMed:18005683, PubMed:20831869, PubMed:24248594, PubMed:29024643, PubMed:29144452, PubMed:31216343, PubMed:33303953). Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), a ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG (PubMed:18005683). Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection (PubMed:18005683, PubMed:20010814). Mediates polyubiquitination of host U2AF1, leading to its proteasomal degradation (PubMed:15950937). Catalyzes 'Lys-48'- linked polyubiquitination and subsequent degradation of a subset of host guanylate-binding proteins (GBP1, GBP2, GBP4 and GBP6), thereby suppressing host cell defense (PubMed:29024643, PubMed:29144452, PubMed:31216343, PubMed:33303953). In contrast, host GBP3 and GBP7 are not ubiquitinated by IpaH9.8 (PubMed:29024643, PubMed:29144452, PubMed:31216343). Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme (PubMed:18005683). SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus Note=Secreted via Mxi-Spa type III secretion system (TTSS), and delivered into the host cytoplasm (PubMed:11115111, PubMed:11418613). Transported into the host nucleus (PubMed:11418613). This transport is independent of cytosolic factors, but dependent on temperature and partly on ATP/GTP (PubMed:11418613). SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family."}
{"protein": "MIPGKYRSVSGRAANNVNCGLHLVIQTSSLSDKNKVEFRLNRETPPFPGRLLQHDLERNYSSRQGDHISLVSSSMPAFPILQRSSEEKTLYSDRLTLERQKLTVCPIIDGEEHLRLLNFQHNFITRIQNISNLQRLIFLDLYDNQIEEISGLSTLKSLRVLLLGKNRIKKISNLENLKNLDVLDLHGNQITKIENVNHLCDLRVLNLARNLLSHVDNLNGLDSLTELNLRHNQITFVRDVDNLPCLQRLFLSFNNITSFESVSCLAESTSLSDITFDGNPIAQESWYKHTVLQNMMQLRQLDMKRITEEERRVASVVPKKEEEKKRESHKQSLLKEKKRLTINNVARKWDLQQRVANIASTQDRKDSESPPQESCQLDGGNISAFPEEAGSLDAGLSSALQGLSVTETHLVEIDGETLSLYGSGALECLDRNWSVQTAGMVTTVSFTFIEFDEIVQVLPKLKMKFPNSLHLKFRETNLVMLQQFNALAQLRRVDQLTIDPQGNPVVNFTLWKYYVLFRLSHFSMQKINGTEVTQNDMIMAERLFGILAHVASSELPQYRMISILGDARKKQFRYLLESKGKKPGIICEETSDSKRFLGENTNRATLNYTTREFYHEKLEEIKDKKKFCRLYVEDLVKEATAINMKNEALQKLWPQMFIELVRDAVIEIRSKDSYMKLCLQQITDQK", "text": "FUNCTION: Subunit of the tubulin polyglutamylase complex (TPGC). The complex mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Note=Associated with microtubules."}
{"protein": "MQTILVLTTFLSAWFLAVGFDVFWNVPSQQCKKYGMKFVPLLEQYSILVNKEDNFKGDKITIFYESQLGLYPHIGANDESFNGGIPQLGDLKAHLEKSAVDIRRDILDKSATGLRIIDWEAWRPIWEFNWSSLRKYQDKMKKVVRQFNPTAHESTVAKLAHNEWENSSKSWMLSTLQLGKQLRPNSVWCYYLFPDCYNYDGNSVQEFQCSEAIRKGNDRLKWLWEESTAVCPSIYIKEGQLTNYTLQKRIWFTNGRLQEALRVAQPKARIYPYINYSIKPGMMVPEVEFWRLIAQIASLGMDGAVIWGSSASVGSKNHCAQLMKYIADVLGPATLRIKENVARCSKQACSGRGRCTWPKDTSVIAWKFLVEKEDYDFYLGDIECKCVEGYEGRYCEQKTK", "text": "FUNCTION: Spider venom endo-hyaluronidase that is able to degrade purified hyaluronic acid (HA) and chondroitin sulfate (CS). Has no activity on dermatan sulfate (DS) and heparan sulfate (HS). Also increases the dermonecrotic effect of the dermonecrotic toxin (AC P0CE80), when injected in rabbit skin, supporting the hypothesis that venom hyaluronidases are spreading factors. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 56 family."}
{"protein": "MMAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTVEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQTLPSSPTTTKSSPSDPMTTSRANQVKIIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGSPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALNTLASYGYNLNTLGLGLSQAAATGALAAAAASANPAAAAANLLATYASEASASGSTAGGTAGTFALGSLAAATAATNGYFGAASPLAASAILGTEKSTDGSKDVVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFVPGTRNRKVTITGTPAATQAAQYLITQRITYEQGVRAANPQKVG", "text": "FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY- 3' and regulates splicing in only a subset of regulated exons (PubMed:10811881). Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3' clusters results in a local and asymmetric action to regulate spliceosome assembly and alternative splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and exon inclusion. With NOVA1, they perform unique biological functions in different brain areas and cell types. Autoregulates its own expression by acting as a splicing repressor. Acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine receptor alpha-2 chain splice variant (alpha-2N) in developing spinal cord (By similarity). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MRSHILGRIELDQERLGRDLEYLATVPTVEEEYDEFSNGFWKNIPLYNASGGSEDRLYRDLEGSPAQPTKHAEQVPYLNEIITTVYNGERLQMARTRNLKNAVVIPHRDFVELDRELDQYFRTHLMLEDSPLAFHSDDDTVIHMRAGEIWFLDAAAVHSAVNFAEFSRQSLCVDLAFDGAFDEKEAFADATVYAPNLSPDVRERKPFTKEREAGILALSGVIGRENFRDILFLLSKVHYTYDVHPGETFEWLVSVSKGAGDDKMVEKAERIRDFAIGARALGERFSLTTW", "text": "FUNCTION: Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp). D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L- proline, cis-4-hydroxy-D-proline, and 3,4-dehydro-DL-proline are not substrates. SIMILARITY: Belongs to the L-proline cis-4-/cis-3-hydroxylase family."}
{"protein": "MFPFYSCWRTGLLLLLLAVAVRESWQTEEKTCDLVGEKGKESEKELALVKRLKPLFNKSFESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKETVVGRLNETHIFNGSNWIMLIYKGGDEYDNHCGKEQRRAVVMISCNRHTLADNFNPVSEERGKVQDCFYLFEMDSSLACSPEISHLSVGSILLVTFASLVAVYVVGGFLYQRLVVGAKGMEQFPHLAFWQDLGNLVADGCDFVCRSKPRNVPAAYRGVGDDQLGEESEERDDHLLPM", "text": "FUNCTION: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane protein."}
{"protein": "DVCDSLVEGRCIHNGCWCDEEAPHGNCCDTAGCTAWWWCPGTKWD", "text": "FUNCTION: Mu-conotoxins block voltage-gated sodium channels. This toxin reversibly blocks voltage-gated sodium channel in cephalopods, with no alteration in the voltage dependence of sodium conductance or on the kinetics of inactivation (By similarity). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MIQVEENEHIQTLVYQLNKEGKSICGDSFFMKADDKELICAVADGLGSGSLANESSAAIKDLVENYASEDVESIIERCNQAMKNKRGATASILKINFEQRQFTYCSVGNVRFILHSPSGESFYPLPISGYLSGKPQKYKTHTATYEKGSKFIIHTDGLNVPDIRSHLKKGQSVEEISNSLKMYTTSRKDDLTYILGQLS", "text": "FUNCTION: Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels."}
{"protein": "MEWYPEAAANAERYTQIVWYK", "text": "FUNCTION: Helicopsin exhibits robust neurotoxic activity as shown by immediate death (about 8 minutes) of mice due to respiratory paralysis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family."}
{"protein": "MSDLTDIQEEITRHEQQLVVARQKLKDAERAVEVYPDDVIKNTLQARQQTVSALEDKLADYKRRMADAVSRKKMDTKPTDPTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIGVYVIGFTIPIILKALYMLSTRGRQTVKENKGTRIRFKDDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPTQIQVRNIMSPVMGVIGFSFFVKDWPEKIREFMEKECPFIKPEVKPGTPAQEVEFLKRNRVYFMTRQDVLDKNHVADIDKLIDYAASGDPTSPDDIKSPNAPWVFACAPDRSPPTCIYVAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKRKSSFYQSYLRRTQSMGIQLDQRIILLYMLEWGKEMVDHFHLGDDMDPELRGLAQSLIDQKVKEISNQEPLKI", "text": "FUNCTION: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm, host perinuclear region Host Golgi apparatus, host cis-Golgi network Note=Internal protein of virus particle. SIMILARITY: Belongs to the hantavirus nucleocapsid protein family."}
{"protein": "MKATIIFLLLAQVSWAGPFQQRGLFDFMLEDEASGIGPEDRIHEVLDLEPLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKISPGAFTPLVKLERLYLSKNHLKELPEKMPKTLQELRVHENEITKVRKAVFNGLNQMIVVELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITTIPPGLPPSLTELHLDGNKITKVDAASLRGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLIKVPGGLADHKYIQVVYLHNNNISAVGSNDFCPPGYNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK", "text": "FUNCTION: May affect the rate of fibrils formation. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily."}
{"protein": "MKRIFGAKNNKEPPPSIQDASDRINKRGDSVEEKVKRLDAELCKYKDQIKRTRPGPALEAIKARAMRVLKQKKMYEGQRDMLYNQTFNLDQVSFAAEGLKDAQQTMTALKSANKELKGMMKTVKIQDIDNLQDDMMDLMDESSEIQETLGRSYNVPDDIDEDDLLGELDALEADMGNETEADGVPSYLQPDKEPDLNDELNLPSAPMGHTGAPPGRAQAEDEWGLPAVPRASLRG", "text": "FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. SUBCELLULAR LOCATION: Endosome, multivesicular body membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNF7 family."}
{"protein": "MSDYNYKPTLWTRADALKVHEDDPTTTQPVIDIAFPVMSEEVFIWDTMPLRDFDGEIISVNGWCIIFTLTADRNTDNPQFQDENGNYDITRDWEDRHGRARICYWYSRTGKDWIFGGRVMAEGVAPTTREWAGTPILLNDRGDIDLYYTCVTPGATIAKVRGKIVTSDQSVSLEGFQQVTSLFSADGTIYQTEEQNAFWNFRDPSPFIDRNDGKLYMLFEGNVAGPRGSHEITQAEMGNVPPGYEDVGGAKYQAGCVGLAVAKDLSGSEWQILPPLITAVGVNDQTERPHFVFQDGKYYLFTISHKYTFADNLTGPDGVYGFVSDKLTGPYTPMNSSGLVLGNPSSQPFQTYSHYVMPNGLVTSFIDSVPWKGKDYRIGGTEAPTVKILLKGDRSFIVDSFDYGYIPAMKDITLK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 68 family."}
{"protein": "MAAPPQLRALLVVVNALLRKRRYHAALAVLKGFRNGAVYGAKIRAPHALVMTFLFRNGSLQEKLWAILQATYIHSWNLARFVFTYKGLRALQSYIQGKTYPAHAFLAAFLGGILVFGENNNINSQINMYLLSRVLFALSRLAVEKGYIPEPRWDPFPLLTAVVWGLVLWLFEYHRSTLQPSLQSSMTYLYEDSNVWHDISDFLVYNKSRPSN", "text": "SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family."}
{"protein": "MAGVDSGKLIGSEIHGFHTLQDLDIQTMLDEAYSRWLRPNEIHALLCNHKFFTINVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHVYYAHGEDTPTFVRRCYWLLDKSQEHIVLVHYRETHEVHAAPATPGNSYSSSITDHLSPKIVAEDTSSGVHNTCNTGFEVRSNSLGSRNHEIRLHEINTLDWDELLVPADISNQSHPTEEDMLYFTEQLQTAPRGSVKQGNHLAGYNGSVDIPSFPGLEDPVYQNNNSCGAGEFSSQHSHCGVDPNLQRRDFSATVTDQPGDALLNNGYGSQDSFGRWVNNFISDSPGSVDDPSLEAVYTPGQDSSTPPTVFHSHSDIPEQVFNITDVSPAWAYSTEKTKILVTGFFHDSFQHLGRSNLICICGELRVPAEFLQMGVYRCFLPPQSPGVVNLYLSVDGNKPISQLFSFEHRSVQFIEKAIPQDDQLYKWEEFEFQVRLAHLLFTSSNKISVLTSKISPENLLEAKKLASRTSHLLNSWAYLMKSIQANEVPFDQARDHLFELTLKNRLKEWLLEKVIENRNTKEYDSKGLGVIHLCAVLGYTWSILLFSWANISLDFRDKQGWTALHWAAYYGREKMVAALLSAGARPNLVTDPTKEFLGGCTAADLAQQKGYDGLAAFLAEKCLVAQFKDMQTAGNISGNLETIKAEKSSNPGNANEEEQSLKDTLAAYRTAAEAAARIQGAFREHELKVRSSAVRFASKEEEAKNIIAAMKIQHAFRNFEVRRKIAAAARIQYRFQTWKMRREFLNMRKKAIRIQAAFRGFQVRRQYQKITWSVGVLEKAILRWRLKRKGFRGLQVSQPDEKEGSEAVEDFYKTSQKQAEERLERSVVKVQAMFRSKKAQQDYRRMKLAHEEAQLEYDGMQELDQMATEES", "text": "FUNCTION: Transcription activator (PubMed:14581622). Binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved in response to cold. Contributes together with CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2 (PubMed:28351986). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CAMTA family."}
{"protein": "MSQAYSSSQRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGFGSKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGTTRTPSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL", "text": "FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (PubMed:25358400). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z- line structures (PubMed:24200904, PubMed:25394388, PubMed:26724190). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line Cytoplasm Cell membrane, sarcolemma Nucleus Note=Localizes in the intercalated disks which occur at the Z line of cardiomyocytes (PubMed:24200904, PubMed:26724190). Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes (By similarity). SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MESKALLLVVLGVWLQSLTAFRGGVAAADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG", "text": "FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side Secreted Secreted, extracellular space, extracellular matrix Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non- coated endocytic vesicles (By similarity). SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MATSRLEINFVRLLSRCESLASEKRAETEWRLEKYVGALEEMFVALKKSPSKPTPETLTDYNRKVDFLKGLLEAEKLPSPAEKSLANQFLAPGRTPTISSERTPASKTVHIQSKARCAGEMRKELMSSGVSNSALLENDLRHRKSLPVDERQSAAELDQILQHHHNLQEKLADDMLNLARNLKNNTLAAQNIIKQDNQTLTQSMRQADVNFEKLKTESERLEQHAKKSVNWFLWLMLIVVSFTFISMILFIRLFPRLR", "text": "FUNCTION: SNARE that may be involved in targeting and fusion of Golgi- derived retrograde transport vesicles with the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the USE1 family."}
{"protein": "MCALDRRERPLNSQSVNKYILNVQNIYRNSPVPVCVRNKNRKILYANGAFIELFSREDKPLSGESYIRLQVEIFLSSLELECQALGHGSAFCRRFNFHGEIYQIRMENVSFYNDESVVLWQINPFPDYPFFALNQSGSNTNTSDKLTIWNDLSPGTLVVFSFYMLGVGHATIARELGITDRASEDRIKPVKRKIKEFFEHFDLFRVSCIYKGEIDSLLSIIREFYGVK", "text": "FUNCTION: Together with ArcA, is essential for positively regulating the expression of transfer genes that are involved in the conjugal transfer of DNA between bacterial cells. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MAEKEEGKVAAEGGAEAEADEEVEVKFRLFDGSDIGPLRCNAVATTVAALKDRVVADWPKDKTIVPKTANDVKLISGGKILENDKNIAQCRAPFGDLPSTAITMHVVVQPSSAKSKPDKKTNKLPKTTRCSCTIL", "text": "FUNCTION: May serve as docking site to facilitate the association of other proteins to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor."}
{"protein": "MARQLFTPPITNPRFDPNQSIRESYKNTTGGMQFQQNLHEDQNDNERSSCDGDENSTTGERLENNKSPILTKQEIDEALNTVTNLPPELSKLIDIFIDDLKQPKYVRPLSVLQLSSLFQSFYIKFDKASFQHVSSANNNGYYFSGGGSSSFLAAKETLSSGLSGIFGRSRSSSGNSLMRPRRSSSLFSNESISNSTNATQMLSPEEIKKQLKINELNNMKIEKYMELCERDVFKKILIVGTSVSSPNKMKTFKPHQLQTFKVGNLFRNSVEFTEYNKLLNEKILCLSKLSTMNKINLIKFLSLNNGIDPEPKFEEIKDILYEFTYHSISPCEKIKALLKLHEIMTYSQEMSNDDYLSLLIYYIITIVPRDIFLNAEFIRLFRYKKKLVETESFALTNLEAALVFVEGLTKNDFSNELQDKLTVNESKILENSISSRVSLPSKTAIMHKNNGNNGSNLGDIVTPTIQRPDVTRSNSYDGFRTVFDSSLKNIIGKIRSYTPPHPNNTSNNNLHSSNNLNIPRSSSQLSMELSNRDTTEMSRDGSRSTSSSSRSSASLEHGNREFTGDLTVTASINGADKKEFQKSWKKYKGYKFEDLTICELRDLFEIYQKMMQ", "text": "FUNCTION: Putative GTPase-activating protein. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "IVGGEDANVQDHPFTVALVTPDGQQFCGGTLAAPNKVVTAAHCTVGSQPADINVVSGRTVMSSNIGTVSKVTNVWVHPEYQDAAKGFDVSVLTLEAPVKEAPIELAKADDAGYAPDTAATILGWGNTSEGGQQADHLQKATVPVNSDDTCKQAYGEYTPNAMVCAGVPEGGVDTCQGDSGGPMVVNNKLIGVTSWGEGCARPGKPGVYARVGAYYDVLMEQINAGAV", "text": "SIMILARITY: Belongs to the peptidase S1 family."}
{"protein": "MAMAAASWASSSSFTRFLRPLLSRNSSPSPISYSLHRYKSANCLFFSASSNKPPKLAVYAQARRVLSSKTKGDEIATPADLSFVVPLKIVEYPDPILRAKNKRIDNFDANLKKLVDEMFDIMYKTDGIGLSAPQVGMNVQLMVFNAAGERGEGEEIVLVNPRVSRYSRRIIPYEEGCLSFPMIHGDVKRPESVKVDAQDINGTRFEISLSALPARVFQHEFDHLQGVLFFDKMTDEVLDTIREKLVALEKKYEDRTGLPTPESINTRKIKKAAVGFGKS", "text": "FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the polypeptide deformylase family."}
{"protein": "MAEKPLFHYDEARGRMESVRWLLAAAGVEYEEKFIHTNEDLEKLRSDGVLMFQQVPMVEVDGMKLVQTRAIMNYFSSKYNLYGKDMKERALIDMYSEGLADLNEMFILYPFDPPGVKEANIALMKEKATNRYFPAFEKVFESHGQDYLVGNKLSKADVHLVEMIYNMEELDTNILANFPLLQALKTRISDMPTIKKFLQPGSQRQPPVDEKSIQKTRKIFKF", "text": "FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Alpha family."}
{"protein": "MSSTPAAGSAAEVATSSATSNAPSAPSTTASNVSNTSQPTTAGTPQARGGRGSNANGGASGSNAGGGDEPRKEAKTTPRISRALGTSAKRIQKELAEITLDPPPNCSAGPKGDNLYEWVSTILGPPGSVYEGGVFFLDIHFSPEYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYLQNREEHDRIARLWTKRYAT", "text": "FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MAPTRHWVTPLLLLCCSGICGAIQWLGLTVNGSRVAWNESEHCRLLDGLVPDQSQLCKRNLELMQSVVNAAKQTKLTCQMTLSDMRWNCSSVENAPSFTPDLSKGTRESAFVYALASATLSHTIARACASGELPTCSCGATPAEVPGTGFRWGGCGDNLHYGLNMGSAFVDAPMKSSKSAGTQATKIMNLHNNAVGRQVLMDSLETKCKCHGVSGSCSVKTCWKGLQDLPHIANELKSKYLGATKVIHRQTGTRRQLVPRELDIRPVRESELVYLVSSPDYCTKNPKLGSYGTQDRLCNKTSVGSDSCNLMCCGRGYNAYTETIVERCQCKYHWCCYVMCKKCERTVERYVCK", "text": "FUNCTION: Ligand for the frizzled7 transmembrane receptor. Primarily acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC, or by JNK and dvl2/dsh. Depending on the cellular context, can also signal via the canonical Wnt pathway mediated by beta-catenin and dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally initiates dorsal/ventral axis formation by a canonical route, which signals via lrp6. In a complex with wnt5a, activates the canonical and non-canonical processes involved in axis formation. In the non- canonical pathway, acts through fzd7/fz7 to induce phosphorylation of dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate convergent extension movements during gastrulation. Interactions with the secreted Wnt antagonist sfrp5 to coordinate foregut development, acting via a non-canonical Wnt pathway whereby sfrp5 restricts wnt11b activity to prevent inappropriate foregut formation. Mediates cardiogenesis via non-canonical Wnt signaling involving JNK-activation and PKC. Acts redundantly with wnt11/wnt11r during pronephros induction. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family."}
{"protein": "METEDDLCNTNWGSSSSKSREPGSSDCGNSTFAGFTSQQKWEDASILDYEMGVEPGLQESIQANVDFLQGVRAQAWDPRTMLSNLSFMEQKIHQLQDLVHLLVGRGGQLQGRQDELAAQQQQLITTDLTSIIIQLISTAGSLLPSVKHNMSTAPGPFTGQPGSAVFPYVREANNVASQSQNNNNCGAREFDLPKPVLVDEREGHVVEEHEMKDEDDVEEGENLPPGSYEILQLEKEEILAPHTHFCTICGKGFKRDANLRMHMRGHGDEYKTAAALAKPNKESVPGSEPMLIKRYSCPFLGCKRNKEHKKFQPLKTILCVKNHYKRTHCDKSFTCSRCHTKKFSVIADLKTHEKHCGKNKWLCSCGTTFSRKDKLFGHIALFQGHTPAIPLEETKPSASTSTQRGSSEGGNNNQGMVGFNLGSASNANQETTQPGMTDGRICFEESFSPMNFDTCNFGGFHEFPRLMFDDSESSFQMLIANACGFSPRNVGESVSDTSL", "text": "FUNCTION: Probable transcription factor. Together with STOP2, plays a critical role in tolerance to major stress factors in acid soils such as proton H(+) and aluminum ion Al(3+). Required for the expression of genes in response to acidic stress (e.g. ALMT1 and MATE), and Al- activated citrate exudation. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "AFSGILAEADIAAALKACEAAGTFNYKAFFAKVGLTGKSADDIKKAFFVIDQDKSGFIEEDELKLFLQVFSAGARALTDDETKAFLKAGDSDGDGAIGVDEWAALVKA", "text": "FUNCTION: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity). SIMILARITY: Belongs to the parvalbumin family."}
{"protein": "MTHIVRFIGLLLLNASSLRGRRVSGIQH", "text": "FUNCTION: Involved in control of the biosynthesis of leucine. FUNCTION: Involved in control of the biosynthesis of leucine."}
{"protein": "MTEVETIIKTVLKTGGYRLGSKSTLKSLRNGEAKAVIVASNCPEEVLEKIKSYDVKILVYNGTNMELGALCGKPFSVAAMAITEEI", "text": "SIMILARITY: Belongs to the eukaryotic ribosomal protein eL30 family."}
{"protein": "MRNKKILKEDELLSETQQAAFHQIAMEPFEINVPKPKRRNGVNFSLAVVVIYLILLTAGAGLLVVQVLNLQARLRVLEMYFLNDTLAAEDSPSFSLLQSAHPGEHLAQGASRLQVLQAQLTWVRVSHEHLLQRVDNFTQNPGMFRIKGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENSVSVRIVGSSNRGRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYKVGAGTGQIWLDNVQCRGTESTLWSCTKNSWGHHDCSHEEDAGVECSV", "text": "FUNCTION: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria (PubMed:9468508). Also plays a role in binding of unopsonized particles by alveolar macrophages (By similarity). Binds to the secretoglobin SCGB3A2 (PubMed:12847263). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein."}
{"protein": "MGFVKVVKNKAYFKRYQVKFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNKFGLDKIYEGQVEVTGDEYNVESVDGKPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHIMGQNVADYMRYLMEEDEDAYKKQFSQYIKNNITPDGMEEMYKKAHAAIRDNPVHEKKPKREVKKKRVNSTKMSLAQKKDRVAQKKASFLRAQERAADS", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the universal ribosomal protein uL18 family."}
{"protein": "MSSISTESSSNLSLLENGGGGSDKPTAETSRRVRRTVSASSLIRKRSDLKLISRVRWEFMRRILTNLQEVLLGTKLFILFPAVPLAVVAHRYDCPRAWVFALSLLGLTPLAERISFLTEQIAFHTGPTVGGLMNATCGNATEMIIAILAVGQRKMRIVKLSLLGSILSNLLFVLGTSLFLGGISNLRKHQSFDPRQGDMNSMLLYLALLCQTLPMIMRFTMEAEEYDGSDVVVLSRASSFVMLIAYLAFLIFHLFSSHLSPPPPPLPQREDVHDDDVSDKEEEGAVIGMWSAIFWLIIMTLLVALLSDYLVSTIQDAADSWGLSVGFIGIILLPIVGNAAEHAGAVIFAFRNKLDITLGIALGSATQIALFVVPVTVLVAWTMGIEMDLNFNLLETACFALSILVTSLVLQDGTSNYMKGLVLLLCYVVIAACFFVSNSPSSKLLF", "text": "FUNCTION: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase. Cation selectivity transport in tobacco root tonoplast vesicles is Cd(2+)>Zn(2+)>>Ca(2+)>>>Mn(2+). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/proton exchanger (CAX) subfamily."}
{"protein": "MSVIGLWLVTVTATLSLFVWQLIFLLSIPKSIVVCLIAESLFFVAWFFYWTVIYPRYLTPFRHLPTPASRSILTGNQNGLFTENSWDVARRVSQTVPNSGLIRYYVALSNERILVTNTRALSDVLTNHSHDFGKSNLAKFALKRLTGNGLGFLEGNEHKVHRKNLMPAFTRKHVKELTPIFWDKAMEMVKGMEAEVRCGKDTSTQGTGIVEIHDWATRATLDIIGTAGFGYDFGTLHNPSNEIGQQYKKMFLEPSTAFNWLELLGNYIDFRFLMTLPVKKNRDLTAGSNFMREIAKKVIRERRHELFQRMTSQAGNMKNTKKDIITTALASDCFTDDQLVDHVMAFLVAGHESTATAFEWAMYELGHRPEMQKRVRDEVRTYLPSPSAGGVKNITFESVPYLQAICNEVLRLYPFLPFATRVAEKDTWVADQFVPKGTIVAYAAHISNRDSELWSGPALDAFDPERWMEPGKESSGGANSNYAMLTFSAGPKSCIGEAWTRAELPCLVGAMVGSFEIELVEGKQADGTVYPTVDFKMGKVLKSRDGVFVRLRRLEDW", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells (PubMed:22252016, PubMed:27983606). The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 (PubMed:22252016, PubMed:27983606). Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin (PubMed:27983606). Prefusarielin is oxygenated at C15 and C16 by FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme (PubMed:27983606). The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism (PubMed:27983606). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MPPPPEDEAIAHKGHFYGVYLLCSQSLDSRYRAKCYVGFTVNPKRRIKQHNRGCDFGGAKKTSKKGPWQMVMIVHGFPNNISALQFEWAWQQPTLSTRLKIFPDLKRKKPKETHFDYNFRILNRMLGVGPWHRLALTIRWLETDYERAFDLPIPCHMEIVSGKVSISASQRKLEEATGTAPPVAWAHECHLCMQSIEQPERSRLGCTNPTCRLTCHMLCLASYLLGDEPGQYIPIGGECPLCETRLSWSALLQRKRLQLGVPEEMQDNEEEDLSDDGPDVDSDVEVQEFSD", "text": "FUNCTION: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX1 family."}
{"protein": "MVHLTPALLLASAAFAAAAPASQIFERQCSVAGNYPTAAVSKLPDPFTTAAGQKITTKADFDCRKAEISKILQQYELGTYPGKPDKVEGSLSGNTLTVRITVGSQTVSFSASIKKPSSGSGPFPAIIGIGGISIPIPSTVATITFPNDDFAQQSGTSSRGRGKFYTLFGSSHSAGALIAWAWGVDRLVDALEQVQSTSGIDPKRLGVTGCSRNGKGAFVAGALVDRIALTIPQESGAGGAACWRISDSEKSAGKNIQTASQIVTENVWFSPAFNAYTRQTTNIPADHHMLAALTVPRGLIAFENDIDWLGPVSTTACMQAGRLIYKAYGVSNHMGFSLVGGHGHCQFPSSQQSELTSYINYFLLKAGTAPGAVERSSAKVDLKSWAPWDVPALS", "text": "FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O- methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family."}
{"protein": "MAKIKARDLRGKKKEELLKQLDDLKNEPSQLRVAKVTGGAASKLTKICVVRKSIARVLTVINQTQKENLRKFYKGKKYKPLDLRPRKTRALRRRLNKHEESLRTKKQQRKDLLYSIRKFAVKA", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL29 family."}
{"protein": "MDFKYTEEKETIKINNIMIHKYTVLYTSNCIMDIYSEEEKITCFSNRLVFLERGVNISVRMQKQILSEKPYVAFRLNGDMLRHLKDALMIIYGMSKIDTNACRSMSRKIMTTEVNKTLLDELKNINSHDNSAFISSLIYLISKLENNEKIIESIYISSVSFFSDKVRNLIEKDLSRKWTLGIIADAFNASEITIRKRLESENTNFNQILMQLRMSKAALLLLENSYQISQISNMIGISSASYFIRIFNKHYGVTPKQFFTYFKGG", "text": "FUNCTION: Required for the expression of the CS1 and CS2 adhesins of enterotoxygenic E.coli. SUBCELLULAR LOCATION: Cytoplasm."}
{"protein": "MGKLLELEGNLFEVMKEIRDELGSPNDLTIREVALAGSFTRCAVVFLCGLTDKDNVYKYVVRTLQYEEVQNEAAVVQTLLDRFISIAEVGKKTTFPDIINAILAGDTVILIDNIQTAIIINSRAWEKRSLEPPVTEDLIRGPRVGLNEDINVNKMLIRRSLRDPKLRFQSYIMGKRSQKEVTLVYIEDIINPHIVKELDRRLQSIVTDVVLETGTIEQLIQDNNLSPFPQFLNTERPDNIIASLAKGKAAILVDGSPFALIAPLVFVDIFQSVEDHYERWVIGTLLRFLRMGSGIIAVLLPAMYVALVSYHQGLIPSKLAYSIAGAREGVPFPAYIETLMMALTMELIREAGIRLPKPMGQTIGIVGGLVIGEAAVNAGIVNPFLVIIIAVTAIATFSLPVYSITITFRILLFVFVLAATAFGLYGIILALIALAIHITNLTSVGIPYTTPIAPAFYKDWKEEFIRMPKSMLKDRPEYLQTKDSTIRPKERK", "text": "FUNCTION: Contributes to the L-alanine germination response. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GerABKA family."}
{"protein": "MAGQTVIVSGLNPAAILQSTIGGAPPSTAAAAAENGDTTRKVVPLSKDALQDFMVSIITQKLQGEKKPFYVLDLGEVVSLMDQWNVALPNVRPFYAVKCNPEPSFLSMLAAMGSNFVCASRAEIEYVLSLGISPERIVFANPCKPESDIIFAEKVGVNLTTYDSEDEVYKIKKHHPKCELLLRIKPMNDGNARCPMGPKYGALPEEIEPLLRIAQASRLTVSGVSFHIGSGDADSNAYLGAIAAAKQVFETAAKFGMSKMNVLDIGGGFTSGHQFTTAATAVKSALQQHFSNEPELTIIAEPGRFFAETAFTLATTIIGKRVRGDLREYWINDGLYGSMNCVLYDHATVTATPLACMSNRVNLNCSGSKMFPSTIFGPTCDALDTVLRDYHVPELQVNDWVIFPNMGAYTKAAGSNFNGFNTSAIVTHLAYAYPS", "text": "FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family."}
{"protein": "MRDNIAKGITAGSNTQQTTYDPTRTEATLTTATTFALRRYDLAGRALYDLDFSKLNPQTPTRDQTGQITFNPFGGFGLSGAAPQQWNEVKDKVPVEVAQDPSNPYRFAVLLVPRSVVYYEQLQRGLALPNQGSSSGSGQQNTTIGAYGLKVKNAEADTAKSNEKLQGYESKSSNGSSSTSTTQRGGSSNENKVKALQVAVKKKSGSQGNSGDQGTEQVELESNDLANAPIKRGSNNNQQVQLKADDFGTAPSSSGSGTQDGTPTPWTPWLTTEQIHNDPAKFAASILILYDAPYARNRTAIDRVDHLDPKVMTANYPPSWRTPKWNHHGLWDWKARDVLLQTTGFFNPRRHPEWFDGGQTVADNEKTGFDVDNSENTKQGFQKEADSDKSAPIALPFEAYFANIGNLTWFEQALLVFGICLS", "text": "SIMILARITY: Belongs to the adhesin P1 family."}
{"protein": "MRKRISAIIMTLFMVLVSCNSGGVAEDPKTVYLTSIANLGKGFLDVFVTFGDMVTGAFGIKADTKKSDIGKYFTDIESTMTSVKKKLQDEVAKNGNYPKVKTAVDEFVAILGKIEKGAKEASKGATGDVIIGNTVKNGDAVPGEATSVNSLVKGIKEIVGVVLKEGKADADATKDDSKKDIGKLFTATTDANRADNAAAQAAAASIGAVTGADILQAIVQSKENPVANSTDGIEKATDAAEIAVAPAKDNKKEIKDGAKKDAVIAAGIALRAMAKNGTFSIKNNEDAAVTTINSAAASAVNKILSTLIIAIRNTVDSGLKTINEALATVKQEDKSVEATNTAEATTSGQQAKN", "text": "FUNCTION: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the variable large protein (Vlp) family. Delta subfamily."}
{"protein": "MEDQPKDREAEVAGPWFSKWERQCLAEAEQAEQLSPELQEEAAADAAGLKIERQRLWHLFQISATAVAQLYKDSGCQQPGLSMWDPFQNAAMAVTSLYKESGDAYQRSFELGVQVGYQRRVRDVLEWVKKGRSIIRREDLISFLCGKVPPTPQPPRTPRMSPRPPAAASTQAAATESGTPVGVDLQPFHEAIALHGLSGAMASISMRSGPPGSSSQDGGIASSGRWKSSFLENDPNSLSSEELTLLLDSGGVRKRTSAQFGDGSADSPLHKRNRMV", "text": "FUNCTION: Together with HAPSTR1 plays a central regulatory role in the cellular response to molecular stressors, such as DNA damage, nutrient scarcity, and protein misfolding. Regulates these multiple stress response signaling pathways by stabilizing HAPSTR1, but also independently of HAPSTR1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HAPSTR1 family."}
{"protein": "MMKCLFLLCLCLLPIVVFSSTFTSQNLIDLPSESPLPKPVLDTNGKELNPDSSYRIISIGRGALGGDVYLGKSPNSDAPCPDGVFRYNSDVGPSGTPVRFIPLSGGIFEDQLLNIQFNIPTVKLCVSYTIWKVGNLNAYFRTMLLETGGTIGQADSSYFKIVKLSNFGYNLLYCPITPPFLCPFCRDDNFCAKVGVVIQNGKRRLALVNENPLDVLFQEV", "text": "FUNCTION: Inhibitor of cathepsin D (aspartic protease) and trypsin (serine protease). May protect the plant by inhibiting proteases of invading organisms. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family."}
{"protein": "MDLASRYKGVVGMVFGDNQSSNEDSYIQRLLDRISNGTLPDDRRTAIVELQSVVAESNAAQLAFGAAGFPVIVGILKDQRDDLEMVRGALETLLGALTPIDHARAQKTEVQAALMNSDLLSREAENITLLLSLLEEEDFYVRYYTLQILTALLMNSQNRLQEAILTTPRGITRLMDMLMDREVIRNEALLLLTHLTREAEEIQKIVVFEGAFEKIFSIIKEEGGSDGDVVVQDCLELLNNLLRSSSSNQILLRETMGFEPIISILKLRGITYKFTQQKTVNLLSALETINMLIMGRADTEPGKDSNKLANRTVLVQKKLLDYLLMLGVESQWAPVAVRCMTFKCIGDLIDGHPKNRDILASKVLGEDRQVEPALNSILRIILQTSSIQEFVAADYVFKTFCEKNTEGQTMLASTLIPQPHPTSRDHLEDDVHMSFGSMLLRGLCSGEADGDLETCCRAASILSHVVKDNLRCKEKALKIVLESPMPSMGTPEPLFQRIVRYLAVASSMKSKEKSSTLGKSYIQQIILKLLVTWTVDCPTAVQCFLDSRHHLTFLLELVTDPAATVCIRGLASILLGECVIYNKSIENGKDAFSVVDAVGQKMGLTSYFSKFEEMQNSFIFSPSKKPPQGYKPLTRTPTPSEAEINEVDEVDEMVKGNEDHPMLLSLFDASFIGLVKSLEGNIRERIVDVYSRPKSEVAVVPADLEQKSGENEKDYINRLKAFIEKQCSEIQNLLARNAALAEDVASSGRNEQSQGSEQRASTVMDKVQMESIRRELQETSQRLETVKAEKAKIESEASSNKNMAAKLEFDLKSLSDAYNSLEQANYHLEQEVKSLKGGESPMQFPDIEAIKEEVRKEAQKESEDELNDLLVCLGQEESKVEKLSAKLIELGVDVDKLLEDIGDESEAQAESEED", "text": "FUNCTION: Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus. Functions in the anterograde transport of storage protein precursors from the endoplasmic reticulum (ER) to the Golgi complex. SUBCELLULAR LOCATION: Golgi apparatus Golgi apparatus, Golgi stack Note=Concentrates only on one side of the Golgi bodies."}
{"protein": "MDLINSTDYLINASTLVRNSTQFLAPASKMIIALSLYISSIIGTITNGLYLWVLRFKMKQTVNTLLFFHLILSYFISTMILPFMATSQLQDNHWNFGTALCKVFNGTLSLGMFTSVFFLSAIGLDRYLLTLHPVWSQQHRTPRWASSIVLGVWISAAALSIPYLIFRETHHDRKGKVTCQNNYAVSTNWESKEMQASRQWIHVACFISRFLLGFLLPFFIIIFCYERVASKVKERSLFKSSKPFKVMMTAIISFFVCWMPYHIHQGLLLTTNQSLLLELTLILTVLTTSFNTIFSPTLYLFVGENFKKVFKKSILALFESTFSEDSSVERTQT", "text": "FUNCTION: Orphan receptor; could be a chemoattractant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "MKNLRNRSFLTLLDFSRQEVEFLLTLSEDLKRAKYIGTEKPMLKNKNIALLFEKDSTRTRCAFEVAAHDQGAHVTYLGPTGSQMGKKETAKDTARVLGGMYDGIEYRGFSQRTVETLAQYSGVPVWNGLTDEDHPTQVLADFLTAKEVLKKEYADINFTYVGDGRNNVANALMQGAAIMGMNFHLVCPKELNPTEELLNRCERIATENGGNILITDDIDKGVKDSDVIYTDVWVSMGEPDEVWQERLKLLKPYQVNQALLEKTGNPNVIFEHCLPSFHNAETKIGQQIYEKYGISEMEVTDDVFESKASVVFQEAENRMHTIKAVMVATLGEF", "text": "FUNCTION: Has vitronectin and fibronectin-binding activity. FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
{"protein": "MTSKPSNDRLHSYLDLQPEVAAALSQGRPVVALESTIISHGMPYPQNVEMARGVEQIVRDNGAVPATIAVLGGRLKVGLSADELELLATDKAVQKISTRDLPVTVALGGHGATTVASTMRIAALAGIRVFATGGTGGVHRGAGETMDISADLLELARTDVCVVSAGVKSILDIGLTLEVLETQGVPAITLGADEFPAFYSRRSGFSSPLTVQTPAEAARVLKVKWDLGLTGGVLLANPVPETAEIPAEEMETHITRALADMAALGLSGKDTTPYLLGRIVELTGGRSLETNIALVRHNAAAAAQVAAEYARLG", "text": "FUNCTION: Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase family."}
{"protein": "MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVTKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKVLCG", "text": "FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Restricts the CLOCK and BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism. SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MALLTPEDLENINRQLHEADSTVRRVTGLDIKGVCKDFYGTTPCCEKVGIVPVTSGNGIIGNFSESLRAITEYFGFDSFVTTMPDVSGYYEAVRNGAQIILMADDNTFLAHNLKNGKIANNQPCTGIIYAEIASRYMKADSKDVLAVGLGKVGFPGAAHLVNKGFRVYGYDADKALLEKTVSDLGITPFEPENPRRFSIIFEATPCADTVPESVISDNCVISTPGIPCAISRELQEKYGVELIMEPLGIGTASMLYSIL", "text": "FUNCTION: Likely catalyzes the NAD(P)-dependent oxidative deamination of (3R)-3-methyl-D-ornithyl-N6-L-lysine, resulting in the formation of pyrrolysine after spontaneous dehydration and cyclization of the intermediate. Is required for the biosynthesis of pyrrolysine. SIMILARITY: Belongs to the PylD family."}
{"protein": "MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGDLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQPPSKNSTIPVQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLNEVITSHGAIEADKENVRQEPYSLPQGFMWDTLDLGNAEVLRELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDATKTSGLRPMEPRDIKAVQELTNTYLKQFHLAPVMDEEEVAHWFLPQEHIIDTFVVENSSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTESEKVGLVLQ", "text": "FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3'. Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the NMT family."}
{"protein": "MAQVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGEDD", "text": "FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. SIMILARITY: Belongs to the annexin family."}
{"protein": "MASDSDTEEFFDAPEDVNLSCSPAVSPLKSETFILKEEATYSKKAETRNIELKQDDSKEIIDSIIEESQKCSDTENENPVVEEKTEVLHETLIGDSVKTKQDLLSNIPELVVTESTFHDGVEDPLQQQISEYLEPDISRSQDAGPSADSAYVPSAIENIVDLTQDLKITEELKIAEEPEIPLIQEETKDPSKNIVEDVFSKLPTSDIIEQLPPAKPPRQICVEPDIVASTKKSGPNRPPQPINAPPPRPPPPARPAPPPRKKKGDTDFDRSSGFEYQKDGFLAGGLLSPNTLTENMNRDSQPSLDLASATSGEKIVTAQENGKAADGQLSSQSSECLGPQRPRSNSGRELTDDEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLYIMRRTKEYVSNDAAQSDDEEKPQSHQSETDGGKLKQKTTQLKKFLGKSVKRAKHLAEEYGERAVNKVKSVRDEVFHTDQDDPSSSDDEGMPYTRPVKFKAAHGFKGPYDFEQIKVVQDLSGEHVGAVWTMKFSHCGRLLASAGQDNVVRIWVLKNAFDYFNNMRIKYNTEGRVSPSPSQESLNSSKSDTDGGVFSGTDDVDPDDKNAPFRQVPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEIDGQTKLITAANFCQNGKHAVIGTYDGRCIFYDTEHLKYHTQIHVRSTRGRNRVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGCVNSSSQIKASFSHDFTYIVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPGLMVSAETSSEKQEGDQAEPVENIPSGALKSDHTEVLLSADFTGAIKVFINKKKNIS", "text": "FUNCTION: Downstream effector for rab11. May be involved in vesicle recycling (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network."}
{"protein": "MFLQYYLNEQGDRVYTLKKFDPMGQQTCSAHPARFSPDDKYSRHRITIKKRFKVLMTQQPRPVL", "text": "FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, Cajal body Note=Also localized to Cajal bodies (coiled bodies). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, Cajal body Note=Also localized to Cajal bodies (coiled bodies). SIMILARITY: Belongs to the NOP10 family."}
{"protein": "MSCFPVLFVMMLLVSQSVWAFPGPETRDGSVQDAESRRVRSAEEDCCENPVCKHTPGCPKGS", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the teretoxin A (TA) superfamily."}
{"protein": "MRDDSGPPLEEDQARPPRALPPVPSAIQVCSSFVENNSRMDQQDDLVGEDDIPLSHPKKKKSRTKSSLATASSEGHAEPVVNRRAEGSEPPAAELKEHPEAPAPRRQKKIRPPPELETSLTERPSSPSLLRNENGIDAEPREEAVIPKPRRKAKKTQPAEPQYASELGVEDEDILTDEQSTLEHHSRFTAPTGVSQPVGKVFVEKSRRFQAADRSELIKTTENIDVSMDVKPSWTTRDVALSVHRAFRMVGLFSHGFLAGCAVWNTVVIYVLAGDQLSNVSNLLQQYKPLAYPFQSLLYLLLALSTVSAFDRTDFAKISVAIRNFLALEPTALASFLYFTALILSLSQQMTSDRIHLYEPSVNGSLWAAEAEEPILVPWIIVNLVVALLVGLSWLFLSYRPGMDLSEELMFFSDVDEHPETGTKASP", "text": "FUNCTION: Component of the transition zone in primary cilia. Required for ciliogenesis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Cell projection, cilium Note=Localizes at the proximal region of primary cilia were observed, consistent with localization to the transition zone. SIMILARITY: Belongs to the TMEM237 family."}
{"protein": "MSPLQLNGKSRGTSPGNAEPLPIFDALCRSLPVGTADEQFWWKLTGRHLARMMLEAGYPEHRQVECLLFHRFKVVPTFGPQPQSAEPWYRSRVAASAGDGAPISYSWRFGTADRKPYIRNYIEPLGPLTGTAADPNNDVATRAFLQDLTTTLPNLDLSLFWTFEPHLVSRFSDKADREKYAGPSVLTGVELSPDSDAIEIKMYLYPRIPEQISQLLSTIIPKAMREAYGDDVCLDSLNLVKDFLSNHPDGRQLSPRGTTGIDCCKVQDSRVKFYVATNNTSFDHIATVMTIGGRRPLSTEVLDKLRELWYELNGLPSDFPTSEQVPTDQGQEGPSGHHGVGFYYDIQPRLALPDVKAFINVRKHAKSDLAAAETVIGFLERHGQGHHNPRAYLNVLRDIVPAEELETRVGAQAFYSVAVKKEELDITAYFIPQVYRRFASVQVELNGQRRSRFE", "text": "FUNCTION: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of neosartoricin, a prenylated anthracenone that exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576, PubMed:23368997). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (PubMed:23368997). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (PubMed:23368997). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (PubMed:23368997). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (PubMed:23368997). There is no gene encoding O-acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-acetylation leading to neosartoricin may be catalyzed by an unidentified O-acetyltransferase (PubMed:23368997). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family."}
{"protein": "MATAGGGSGADPGSRGLLRLLSFCVLLAGLCRGNSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEEDLQWVLTDGPNPPYMVLLESKHFTRDLMEKLKGRTSRIAGLAVSLTKPSPASGFSPSVQCPNDGFGVYSNSYGPEFAHCREIQWNSLGNGLAYEDFSFPIFLLEDENETKVIKQCYQDHNLSQNGSAPTFPLCAMQLFSHMHAVISTATCMRRSSIQSTFSINPEIVCDPLSDYNVWSMLKPINTTGTLKPDDRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALQKAPDVTTLPRNVMFVFFQGETFDYIGSSRMVYDMEKGKFPVQLENVDSFVELGQVALRTSLELWMHTDPVSQKNESVRNQVEDLLATLEKSGAGVPAVILRRPNQSQPLPPSSLQRFLRARNISGVVLADHSGAFHNKYYQSIYDTAENINVSYPEWLSPEEDLNFVTDTAKALADVATVLGRALYELAGGTNFSDTVQADPQTVTRLLYGFLIKANNSWFQSILRQDLRSYLGDGPLQHYIAVSSPTNTTYVVQYALANLTGTVVNLTREQCQDPSKVPSENKDLYEYSWVQGPLHSNETDRLPRCVRSTARLARALSPAFELSQWSSTEYSTWTESRWKDIRARIFLIASKELELITLTVGFGILIFSLIVTYCINAKADVLFIAPREPGAVSY", "text": "FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid- beta precursor protein) (PubMed:10993067, PubMed:12679784, PubMed:25043039, PubMed:26280335, PubMed:30598546, PubMed:30630874). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Cytoplasmic vesicle membrane; Single-pass type I membrane protein Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the nicastrin family."}
{"protein": "MKFAWLLAPDTYWDEKKTFITAALESGIDHIVDTADSGRIKKLGNLTLISPDEDADIVLVGRDGEGDGTLELPETLEYSRDIEMASELSESGRQVAAYVEIRSKAHEELARRLGRVVDYLILVGEDWKIIPLENIIADLQEEDVKLIAAVADVDEARVALETLEHGTDGVLIEPADISQIKDIAALLENIESETYELKPATITRIEPIGSGDRVCVDTCSIMGIGEGMLVGSYSQGLFLVHSESLESEYVASRPFRVNAGPVQAYVMVPGGRTRYLSELETGDEVIIVDRDGRSRSAIVGRVKIEKRPLMLVEAEYEGMKVRTLLQNAETIRLVNDKGEPVSVSELGEGDRVLVYFDESARHFGMAIKETIIEK", "text": "FUNCTION: Catalyzes the oxidative deamination and cyclization of 2- amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3- dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis. SIMILARITY: Belongs to the archaeal-type DHQ synthase family."}
{"protein": "MAQPLVAAPSSSSITSPIPRKLCSSLLTPSSLSLSSNPRNSLQFLNSKLFLSPPSTSHRRLSIVAMAPKPGKAKKVIGVIKLALEAGKATPAPPVGPALGSKGVNIMAFCKDYNARTADKPGFVIPVEITVFDDKSFTFILKTPPASVLLLKASGAEKGSKDPQMEKVGKITIDQLRGIATEKLPDLNCTTIESAMRIIAGTAANMGIDIDPPILVKKKKEVIF", "text": "FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL11 family."}
{"protein": "MAPLLAAAMNHAAHPVLRSHLGPNNESFSRHHLSSSPQSSKRRFNLSFTPRSARVGNQNGVQLLSPSEIPRRDWFPSDFIFGAATSAYQIEGAWNEDGKGESNWDHFCHNFPERIMDGSNADIGANSYHMYKTDVRLLKEMGMDAYRFSISWPRILPKGTVEGGINQDGIDYYKRLINLLLENGIEPYVTIFHWDVPQALEEKYGGFLDKTQKRIVNDYKNFAKVCFDNFGDKVKNWLTFNEPQTFTSFSYGTGVFAPGRCSPGLDCAIPTGNSLVEPYIAGHNILLAHAEAVDLYNKYYKGENGRIGLAFDVMGRVPYGTSFLDEQAKERSMDINLGWFLEPVVRGDYPFSMRSLARERLPFFSDKQQEKLVGSYNMLGINYYTSIFSKHIDISPKYSPVLNTDDAYASQETYGPDGKPIGPPMGNPWIYLYPEGLKDILMIMKNKYGNPPIYITENGIGDVDTKEKPLPMEAALNDYKRLDYIQRHISTLKESIDLGANVHGYFAWSLLDNFEWYAGYTERYGIVYVDRKNNYTRYMKESAKWLKEFNTAKKPSKKIITPA", "text": "FUNCTION: Beta-glucosidase acting poorly on artificial aryl beta- glucosides. Has no activity toward the chromogenic substrate 6-bromo-2- naphthyl-beta-D-glucoside (6BNGlc). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the glycosyl hydrolase 1 family."}
{"protein": "MMTRESIDKRAGRRGPNLNIVLTCPECKVYPPKIVERFSEGDVVCALCGLVLSDKLVDTRSEWRTFSNDDHNGDDPSRVGEASNPLLDGNNLSTRIGKGETTDMRFTKELNKAQGKNVMDKKDNEVQAAFAKITMLCDAAELPKIVKDCAKEAYKLCHDEKTLKGKSMESIMAASILIGCRRAEVARTFKEIQSLIHVKTKEFGKTLNIMKNILRGKSEDGFLKIDTDNMSGAQNLTYIPRFCSHLGLPMQVTTSAEYTAKKCKEIKEIAGKSPITIAVVSIYLNILLFQIPITAAKVGQTLQVTEGTIKSGYKILYEHRDKLVDPQLIANGVVSLDNLPGVEKK", "text": "FUNCTION: General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIB family."}
{"protein": "MVLPDSNIMKNGSIKRLRDSQIENSPYSRPIKKITPNSSHEDLSATISNEGSLNFTPRTSRQESLYNMKKIFQKTYSQTKLGLFSSKKQVNTLETAIPTTPKQQLPTPTTSPEKNNILWSTPNSLTSLRTISNDLDDCRNRNLITDFSELSIINSSSSSIYSTQQSHPIFEIPEIVDNIVKQLYLIENEQDLLNGHHKKDVNRENTSTVVSCLAVSKTWNKVSKGYLMRDLKFTKSTSLTNFLSQCSTKKTTPQSLILHKMSDINNNNSRGLEIIIDPKQLRHLEYYVCPNILPPVNWFQSLTKLEKLILPGNKLINDSYLIQICRYLPNLKVLDLRACDNITDAGIVAVGTHCKQLVSCNIGRHRNGSSITGLSVVALAKNTMIRTLGLAGCDITDASMWELAQKCGKNIERLSLNNCNKLTNFSLPMLFAFNYFPNLNVLEIQNIAKITDVRHMVRYKIWKRSQRIPILIKGCDRITKLIHEEERQIKAQSLKTARKDMTLWVNQLENE", "text": "FUNCTION: Negative regulator of the mitotic exit network (MEN), required for multiple cell cycle checkpoints. Required for daughter cell separation and chromosome stability. Involved in copper sensitivity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AMN1 family."}
{"protein": "MTKQPFYKSLYVQVLVAIAIGIALGHWYPETAVAMKPFGDGFVKLIKMAIAPIIFCTVVTGIAGMQSMKSVGKTGGMALLYFEVVSTVALIIGLVVVNVVQPGAGMHVDPNTLDTSKIAAYAAAGEKQSTVDFLMNVIPGTVVGAFANGDILQVLFFSVLFGYALHRLGSYGKPVFEFIERVSHVMFNIINVIMKVAPIGAFGAMAFTIGAYGVGSLVQLGQLMLCFYITCILFVLIVLGGIARAHGFSILRFIRYIREELLIVLGTSSSESALPRMIDKMEKLGCNKSVVGLVIPTGYSFNLDGTSIYLTMAAVFIAQATDTPMDITHQITLLLVLLIASKGAAGVTGSGFIVLAATLSAVGHLPVAGLALILGIDRFMSEARALTNLVGNGVATVVVSKWCKQLDEGTLQRELAGEGNASSPASDIPVGGREAV", "text": "FUNCTION: Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the inner membrane. FUNCTION: Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family."}
{"protein": "MHRSGTTMAWNVFKFCTALRGLGSIMILLVLGVVGVTYYAVVLTNYGPALSQGGLDSLAALTILILFHFLLAMLLWSYFSVVFTDPGVVPPNWRPSTDEERGESDPLNSLDFVGLQSDSSSSNPRVRFCRKCNQLKPSRCHHCSVCGRCVLKMDHHCVWVVNCVGALNYKYFLLFLFYTFLETTLVTLVLMPHFIAFFSDEEIPGTPGTLATTFLAFVLNLAFALSVMGFLIMHISLVAGNTTTIEAYEKKTTTKWRYDLGKKKNFEQVFGMDKRYWLIPGYTEEDLRRMPELQGLEYPSKPDFDSQ", "text": "FUNCTION: Palmitoyl acyltransferase. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family."}
{"protein": "MSEVNPKIVIEAALFASAEPLTPERLQQLFDEQNPISLSEIKNLLSELKEDYRERGVDLQEVASGYRFQARPDFSPWLQRLWEKKPARYSRALLETLALIVYRQPISRGEIEEVRGVAVSSDIIKKLLDREWISVVAHRDVPGKPALFGTTKTFLDYFNLKSLEELPPLEDVVDLEKIEAQFGEQLALVVEKKAAEGTEPSALPLAEED", "text": "FUNCTION: May participate in chromosomal partitioning during cell division. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ScpB family."}
{"protein": "VIGGDECNINEHRFLALLYSERFQCGGTLINEEWVLTAAHCDMGNMYIYLGVHNVSVQYDDEQRRYPKKKYFCLSSRNYNQWDNDIMLIRLNRPVRNSAHIAPLSLPSGPPSVGSVCRVMGWGTITSPNETYPDVPHCANINILDYEVCRAAYAGLPATSRTLCAGILEGGKDSCRGDSGGPLICNGEIQGIVSWGGNICAQPREPGLYTKVFDYIDWIQSIIAGNTTVNCPP", "text": "FUNCTION: Snake venom serine protease that has fibrinogenolytic activities. Preferentially cleaves the Bbeta-chain (FGB) and more slowly the Aa-chain (FGA) of fibrinogen, but does not affect the gamma- chain. Has also fibrinolytic activity. May play a role in antithrombotic reaction as well as thrombolytic reaction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily."}
{"protein": "MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE", "text": "FUNCTION: Involved in the degradation of L-fucose and D-arabinose (PubMed:13898172). Catalyzes the reversible cleavage of L-fuculose 1- phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L- lactaldehyde (PubMed:13898172, Ref.8, Ref.9, PubMed:10821675, PubMed:11054289). Also able to catalyze the reversible cleavage of D- ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1- phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively (PubMed:4928018). FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes and has a strong preference for L- configurated alpha-hydroxy aldehydes (PubMed:13898172, Ref.8, PubMed:10821675). FucA generates a vicinal diol unit having the absolute (3R,4R)-cis configuration (D-erythro) (Ref.8, PubMed:10821675). FUNCTION: Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily. SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily."}
{"protein": "MNEQTSRLNRERRFLVLLGLICLSLIGGALYMQVVLGEAPCPLCILQRYALLFIAVFAFIAAAMPGRRSLTFFEALVVLSAIGGIVAAGNHVYILANPMVSCGIDTLQPIVDDLPLAKLWPLAFQVDGFCSTPYPPILGLSLAQWALVAFVLTAVLVPLGIYRNRRQA", "text": "FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family."}
{"protein": "MSDELIHVVIALGLVISFGLGAITAGVLR", "text": "FUNCTION: May initiate with G9P the virion concomitant assembly-budding process, by interacting with the packaging signal of the viral genome. The assembly-budding takes place at the host inner membrane. In turn, G7P and G9P are present at the end of the filamentous virion that emerges first from the bacterial host (By similarity). SUBCELLULAR LOCATION: Virion Host membrane; Single-pass membrane protein Note=Prior to assembly, is found associated with the bacterial host inner membrane. There are about five copies of this protein per mature phage that are located on the tail side of the filamentous virion with G9P (By similarity). SIMILARITY: Belongs to the inovirus G7P protein family."}
{"protein": "MENRNTHTHPENKAEAPTVQSSSGLSSTKKKTDLEAAVAAGQNGRADATERDSRKKPAAPRGPEKEPRHTASSQERSGEPQTQEQRPSARSKTTQDGPRELQTGQEQARPSGDFVASEGRPQPAMQTKDQQKRWQSAEAKDVQSTESCQGNTDHDLGKPCTSDSRSHPQKTNSLSEGGRPQARLQEPMPAPSSGTHKDNPQEAVPPKPKVTAEEKKAPPVLPTVPRTHKDRGEAVESKASPRPPPPPPSPPPPPPPEERDVEKKELGQGQKQRQPALAAAGTQGPGNFRRGFMKCLLEVEEQEEATHRRTLKSRALTARRSPKTVTSVPTSGPVNSSVPPLPPTLHEPSTSAPATVPSWVKPPAPGQAPIPMGTPSSVLPTPAQDQSWRWPELLPQGNERNLNYAKTRQESEEHGLFKLYQNWEERTEEHLTLKQEEAFRSYFDIFNGPGEVDARSLKNILLLIGFTFTPAQVEEALMSADVNGDGHVDFKDFLAVMTDTKRFFCSVEQNVLMDMSPPNPYTLFFEILSLLVEMLALPEVALEEITNYYQKKLKEGSSKAREMETAMGGIRQRKKIPYSSQQVENLEVPERRVLRILSRLKQQNYAANLQSPYAQVPCIPLCPRLDKKAVRRKQASHNHSVLDQCVPTSLGPDLHGFFLQPGQQGSREHSSDSRKWLSSVPARTH", "text": "FUNCTION: Involved in the differentiation of haploid spermatids."}
{"protein": "METTTTERRRLFATEKVGGRAVYRLQAATVAAGILLVLYYRATRVPAAGEGRAAWLGMAAAELWFAVYWVITQSVRWCPVRRRTFKNRLAERYKENLPGVDVFVCTADPHAEPPSLVISTILSVMAYNYPSEKISVYLSDDGGSILTFYALWEASMFAKKWLPFCRRYNIEPRSPAAYFSESEGHHNLCSPKEWSFIKNLYEEMRERIDSAVMSGKIPEEIKLKHKGFDEWNSEMTSKNHQPIVQVLIDGKSQNAVDDDGNVLPTLVYMAREKSPQYHHNFKAGALNALIRVSALISDSPVILNVDCDMYSNNSDSIRDALCFFLDEEMSHKIGFVQYPQNYNNMTKNNIYGNSLNVINHVEMRGLDSAGGCLYIGTGCFHRREILCGKKFSKDYKEDWGRGIKERGHENIDEIEEKAKSLATCTYELRTQWGNEIGVKYGCPVEDVITGLAIHCRGWESVYMEPQRAAFVGVAPATLAQTILQHKRWSEGNFTIFLSKHNTFLFGHGKISLQLQMGYCIYGLWAANSLPTIYYVMIPALGLVKGTPLFPEIMSPWATPFIYVFCVKTLYSLYEALLSGDTLKGWWNGQRMWMVKRITSYLYGFIDTIRKLLGLSKMSFEITAKVSDGDEAKRYEQEILEFGSSSPEFVIIATVALLNFVCLVAGLSKIMAGVWNVFLPQVILCGLIVITNIPIYEAMFVRKDKGRIPLPVTLASIGFVMLAFLLPIV", "text": "FUNCTION: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like E subfamily."}
{"protein": "MSRSPSPDSPPAVRDDEEKDAREQSDSPTSNTDDPKSPSESPKSNRSQESSRKDSRESGKRRDSHEDEKMPLTPPNRSSEASPQHRRHRESRSPSRSRSRSHRSHSRSQYRRSRSRSRDRRSRSRSRDRRSHSRSRDRRSPARRRSPVRAKSPAQAVKPTEEPEKKKNDPKDLLRTRTGGAYIPPAKLRLMQQQITDKSSEQYQRMNWERMKKKIHGLVNRVNAKNLVQIVRELLQENVIRSKGLLCRDIIQAQAFSPGFSNVYAALAAVINSKFPHIGELLLRRLIVQFKRSFRRNDRGVTVNVIKFIAHLINQQVAHEVLALEIMILMLEEPTDDSVEVAIAFLKECGAKLMEIAPAALNSVYDRLRAILMETERSENALDRRIQYMIETAMQIRKDKFAAYPAVVEDLDLIEEEDQIIHTLNLEDAVDPENGLNVFKLDPEFEKNENVYEEIRKEIIGDADISSDEEEEVEDDDEESEAEEAPRKTTEIIDNTDQNLTAFRREVYLTLQSSLDYQEAAHKLLKMKIPDNLQVNVILKFIQKKSEFQNELCAMLVDCCAQQRTYERFYGMLIERFCRLRLEYQQCFEKLCQDTYATVHRIDITKLRNLARLVAHLLSTDAIEWKILADVKMTEEDTTSAGRIYIKFIFMELVEAMGMVKLHTRVTDPTLAHCFVGMFPRTDPQDARFAINFFTMIGLGGLTLELREWLNRGLKKKKGIIDELKAAQSSSDSSSDSSDSSDSSDSSGSSDSSDDSSSSSSSDSSKEPPKKKKKSGTVLKKKETDTNDHKEARGDSRAERRNDEEKLKRRSDEGRRDRSAENREPRRGRDRRDSGDDRHDRGRRDRSKEKEDRGDKRSQRHDSREEDRRERKDRDRRDRSEERDNRRDRKERSRSRDRRDHRDRSRSRERNEKRRHDDDRRREEKVGSDDRRRRH", "text": "FUNCTION: Required for early embryogenesis and tissue differentiation. Required for pre-mRNA splicing and for exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the CWC22 family."}
{"protein": "MNTVIAFILIFGTLVFFHELGHLILAQRAGILCREFAIGFGPKIFSFKKNETVYTIRLLPIGGFVRMAGEDPEMIEVKPGYTVGLLFDSENKVEKIIINQKEKYPDALVIEVEQADLEHQMRITGYEHGNEDHLSSFSVSETSFFIVDGEEVQIAPYNRQFHSKTVWQRIKAIAAGPIMNFILAYVILVMLGLMQGVPSDEPVLGKLIDNGRAAEAGLQEGDRIQTINGENMRSWTDIVNTVREHPEKELKIVLMRDNVKLTKYVTPEAVKAGDETVGRFGAYNPVKTGVLTSISYGATETATVAQSIVTNLGKLVTGQFSIDMLAGPVGIYDMTDQVAKTGVINLLKLAAFLSINLGIVNLLPIPALDGGRLLFLFIEAIRGKPINREKEAFVVFIGVAFLMLLMLVVTWNDIQRLFL", "text": "FUNCTION: Is responsible for Site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family."}
{"protein": "METAVYAKSTRNEKVLNCLCQKPDALFKLICFPWAGGGSTHFAKWGRKINGLLEVHAVRLAGRETRFEEPFSNDIYQIAEEVVTALLPIIRDKAFAFFGHSFGSYIAFITALHLKEKYKMEPLHIFVSSASAPHSEFRPQVPDINKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIPLLKADVDIVKKFIFDKPSKALLSRDITCFIGSEDVVKDIEGWKDITSGKFDVLKLPGDHFYLMEPNNEDFIKNYIVKCLELSSLDYF", "text": "FUNCTION: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the thioesterase family."}
{"protein": "MPSIEDELFPSTPGKFKIDRSNRQLHRCFASTSTMFLWALFLIALTASYLSFQSFVDSGSRYLTASWGGIQWEKQVRTSAQIHRSGGISVLVTGATGFVGSHVSLALRKRGDGVVGLDNFNNYYDPSLKRARRSLLSSRGIFVVEGDLNDAKLLAKLFDVVAFTHVMHLAAQAGVRYALENPQSYVHSNIAGLVNLLEICKAANPQPAIVWASSSSVYGLNEKVPFSESDRTDQPASLYAATKKAGEEITHTYNHIYGLAITGLRFFTVYGPWGRPDMAYFSFTRNILQGKPITIYRGKNRVDLARDFTYIDDIVKGCLGSLDSSGKSTGSGGKKRGAAPYRIFNLGNTSPVTVPILVDILEKHLKVKAKRNFVEMPGNGDVPFTHANISSARNEFGYKPTTDLETGLKKFVRWYLSYYGYNTKAKLVH", "text": "FUNCTION: UDP-D-glucuronate 4-epimerase involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family."}
{"protein": "MERARDRLHLRRTTEQHVPEVEVQVKRRRTASLNNQECHVYLRRSQQQQVPVVDFQAELIQAFLAETPRGG", "text": "SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNURF family."}
{"protein": "MSESLHLTRNGPILEITLDRPKANAIDAKTSFAMGEAFLNFRDDPELRVAIITGGGEKFFSAGWDLKAAAEGEAPDADFGSGGFAGLTEIFDLDKPVIAAVNGYAFGGGFELALAADFIVCAENASFALPEAKLGIVPDSGGVLRLPKLLPPAIVNEMVMTGRRMSAEEALRWGVVNRVVSQSELMDSARELAQQLVNSAPLAIAALKEIYRATSEMPVEEGYRYIRSGVLKHYPSVLHSEDALEGPQAFAEKRDPVWKGR", "text": "FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family."}
{"protein": "MPIGELAIGAVLGVGAQAIYDRFRKARDISFVHRLCATILSIEPFLVQIDKRSKVEGSPLREVNERLTCFLELAYVFVEAYPKLRRRQVLRKYRYIKAIETIELALRSIIVVDFQVDQWDDIKEIKAKISEMDTKLAEVISACSKIRA", "text": "FUNCTION: Disease resistance (R) protein that induces localized, salicylic acid-dependent defenses (PubMed:11141561). Confers resistance to powdery mildew (e.g. Erysiphe cichoracearum UCSC1) (PubMed:11141561, PubMed:15155802, PubMed:17565954). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the plant RPW8 protein family."}
{"protein": "MTPLFDLEEPPKRVLLVDGHHLAYRTFYALSLTTSRGEPVQMVYGFARSLLKALKEDGQAVVVVFDAKAPSFRHEAYEAYKAGRAPTPEDFPRQLALVKRLVDLLGLVRLEAPGYEADDVLGTLAKKAEREGMEVRILTGDRDFFQLLSEKVSVLLPDGTLVTPKDVQEKYGVPPERWVDFRALTGDRSDNIPGVAGIGEKTALRLLAEWGSVENLLKNLDRVKPDSLRRKIEAHLEDLHLSLDLARIRTDLPLEVDFKALRRRTPDLEGLRAFLEELEFGSLLHEFGLLGGEKPREEAPWPPPEGAFVGFLLSRKEPMWAELLALAAASEGRVHRATSPVEALADLKEARGFLAKDLAVLALREGVALDPTDDPLLVAYLLDPANTHPEGVARRYGGEFTEDAAERALLSERLFQNLFPRLSEKLLWLYQEVERPLSRVLAHMEARGVRLDVPLLEALSFELEKEMERLEGEVFRLAGHPFNLNSRDQLERVLFDELGLTPVGRTEKTGKRSTAQGALEALRGAHPIVELILQYRELSKLKSTYLDPLPRLVHPRTGRLHTRFNQTATATGRLSSSDPNLQNIPVRTPLGQRIRKAFVAEEGWLLLAADYSQIELRVLAHLSGDENLKRVFREGKDIHTETAAWMFGLDPALVDPKMRRAAKTVNFGVLYGMSAHRLSQELGIDYKEAEAFIERYFQSFPKVRAWIERTLEEGRTRGYVETLFGRRRYVPDLASRVRSVREAAERMAFNMPVQGTAADLMKIAMVKLFPRLKPLGAHLLLQVHDELVLEVPEDRAEEAKALVKEVMENAYPLDVPLEVEVGVGRDWLEAKQD", "text": "FUNCTION: Has 5'-3' exonuclease activity and no 3'-5' exonuclease activity. SIMILARITY: Belongs to the DNA polymerase type-A family."}
{"protein": "MIIKPRVRGFICVTAHPTGCEANVKKQIDYVTTEGPIANGPKRVLVIGASTGYGLAARITAAFGCGADTLGVFFERPGEEGKPGTSGWYNSAAFHKFAAQKGLYAKSINGDAFSDEIKQLTIDAIKQDLGQVDQVIYSLASPRRTHPKTGEVFNSALKPIGNAVNLRGLDTDKEVIKESVLQPATQSEIDSTVAVMGGEDWQMWIDALLDAGVLAEGAQTTAFTYLGEKITHDIYWNGSIGAAKKDLDQKVLAIRESLAAHGGGDARVSVLKAVVTQASSAIPMMPLYLSLLFKVMKEKGTHEGCIEQVYSLYKDSLCGDSPHMDQEGRLRADYKELDPEVQNQVQQLWDQVTNDNIYQLTDFVGYKSEFLNLFGFGIDGVDYDADVNPDVKIPNLIQG", "text": "FUNCTION: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). FUNCTION: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). SIMILARITY: Belongs to the TER reductase family."}
{"protein": "MLLCWIVSLLLATVGGKEVCYGHLGCFSNDKPWAGMLQRPLKIFPWSPEDIDTRFLLYTNENPNNYQKISATEPDTIKFSNFQLDRKTRFIVHGFIDKGEDGWLLDMCKKMFQVEKVNCICVDWRRGSRTEYTQASYNTRVVGAEIAFLVQVLSTEMGYSPENVHLIGHSLGAHVVGEAGRRLEGHVGRITGLDPAEPCFQGLPEEVRLDPSDAMFVDVIHTDSAPIIPYLGFGMSQKVGHLDFFPNGGKEMPGCQKNILSTIVDINGIWEGTQNFVACNHLRSYKYYASSILNPDGFLGYPCSSYEKFQQNDCFPCPEEGCPKMGHYADQFEGKTATVEQTVYLNTGDSGNFTRWRYKVSVTLSGAKKLSGYILVALYGNNGNSKQYEIFKGSLKPEARHVRDIDVDINVGEIQKVKFLWNNKVINLFRPTLGASQITVQSGVDGKEYNFCSSDTVREDVLQSLYPC", "text": "FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8656075, PubMed:9822688). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8656075). Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:9822688). May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (PubMed:8656075, PubMed:9822688). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (PubMed:32963038). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (PubMed:32963038). SUBCELLULAR LOCATION: Secreted Zymogen granule membrane; Peripheral membrane protein Cell projection, neuron projection Note=Localizes to neurite tips in neuronal cells. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."}
{"protein": "MSTYSLSETHKAMLEHSLVESDPQVAEIMKKEVQRQRESIILIASENVTSRAVFDALGSPMSNKYSEGLPGARYYGGNQHIDEIEVLCQNRALEAFHLDPKQWGVNVQCLSGSPANLQVYQAIMPVHGRLMGLDLPHGGHLSHGYQTPQRKISAVSTYFETMPYRVNIDTGLIDYDTLEKNAQLFRPKVLVAGTSAYCRLIDYERMRKIADSVGAYLVVDMAHISGLIASEVIPSPFLYADVVTTTTHKSLRGPRGAMIFFRRGVRSVDAKTGKETLYDLEDKINFSVFPGHQGGPHNHTITALAVALKQAASPEFKEYQQKVVANAKALEKKLKELGYKLVSDGTDSHMVLVDLRPIGVDGARVEFLLEQINITCNKNAVPGDKSALTPGGLRIGTPAMTSRGFGEADFEKVAVFVDEAVKLCKEIQASLPKEANKQKDFKAKIATSDIPRINELKQEIAAWSNTFPLPVEGWRYDAGL", "text": "FUNCTION: Interconversion of serine and glycine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family."}
{"protein": "SIAELCKVLTTGPLNADTEVVVGCPAPYLTLARSQLPDSVGVAAQNCYKVAKGAFTGEISPAMLKDLNIGWVILGHSERRAIFGESDELIADKVAHALAEGLKVIACIGETLQEREAGQTEAVCFRQTKAIADKVKDWSNVVVAYEPVWAIGTGKTATPEQAQEVHVALRKWFTDNVSADVSASIRIQYGGSVTAANCRELAAKPD", "text": "SIMILARITY: Belongs to the triosephosphate isomerase family."}
{"protein": "MSNYVIEKTLNNNVIICTDENQHHEVVLIGKGIGFNKKKGMELSDSVMIDKVYKLEQKKDQDHYKALVEIADDNVLQTIIEAMDIITHADRTVVDKDLMVALTDHILFAYKRIKQHQFIKNPFLIETKQLYSESYQIAVSVIEHLNKLLDIEFPEDEIGFIALHIASSKDDLSLHEVRLTNEIINKSILIMEHDLKYKIDTNSIQYQRFIRHIQFLIRRLQKGEIIQVNDEFGNMLKAHYPLCYNIAVKIIKMMQQHLDVEVYEAELIYLTLHINHFTQQNEKNTNV", "text": "FUNCTION: Mediates positive regulation of the ptsG/glcA and glcB genes by functioning as an antiterminator factor of transcription via its interaction with the RNA-antiterminator (RAT) sequence located upstream of the ptsG/glcA gene. SIMILARITY: Belongs to the transcriptional antiterminator BglG family. GlcT subfamily."}
{"protein": "MFEELDAEDGGEEQEMPMNVPEFGGGGEDIDDILGDAPDLPDDEYSNSVPQGAADGSIENDERRMRNDGAGSTNEDDEEPIEPTYLGDAIDSLMMHWCQLLTNVSVKAPVPPPSTLNHVKEVAEVCSKHFRDASVDVNNEFTRLGVQWEMEQPYSQYAIEEENLDEAIERQETIIAAAREMLNSRIQIYNEAHPNAGKHFTT", "text": "FUNCTION: Plays a role in normal growth and development. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly localizes to the nucleus."}
{"protein": "MATFADLPDSVLLEIFSYLPVRDRIRISRVCHHWKKLVDDRWLWRHVDLTLYTMRPKVMWHLLRRYMASRLHSLRMGGYLFSGSQAPQLSPALMRALGQKCPNLKRLCLHVANLSMVPITSLPCTLRTLELHSCEISMAWLHKEQDPTVLPLLECIVLDRVPAFRDEHLQGLTRFRALRSLVLGGTYRVTETGLDMGLQELNYLQRLEVLGCTLSADSTLLAISRHLRDVRKIRLTVRGLSAPGLSVLEGMPALESLCLLGPLVTPEMPSPQEILASCLTMPKLRVLELQGLGWEGQEAERILSKGLPHCMVIVRALPKESMDWWM", "text": "FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia (By similarity)."}
{"protein": "MSLTITSSVTHPELKDLSTVRNEQKELNISPVHDVNVTKATATFGMGCFWGAESLYGATRGVLRTTVGYAGGSSDLPTYRKMGDHTEVLEIDYDPTVISFKELLDLFWNNHEYGLTTPIKRQYASLILYHDEEQKQVAHASKLEEQERRAPEIITTEIASKENFYPAEAYHQKYRLQGHKDLASSLNLSPKLLQTSYVATKLNGYLAGVGGIEQFKAEAETMGLTPTQRQYCYYHVEQNEGQGLYC", "text": "FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reduction of methionine sulfoxide in proteins to methionine (PubMed:12145281, PubMed:30529269). Does not catalyze the reverse reaction involving the oxidation of methionine residues (PubMed:30529269). SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family."}
{"protein": "MKFPCLSFRQPYAGLILNGVKTLETRWRPLLSSVQKYTIAIHIAHKDWEDDEWQEVLMERLGMTWTQIQTLLQAGEKYGRGVIAGLIDIGETFQCPETLTAEEAVELETQAVLTNLQLKYLTQVSNPRWLLEPIPRKGGKDIFQVDIPEHLIPLEKE", "text": "FUNCTION: May play a role in cell protection during the inflammatory response. In epithelial cells, negatively regulates IL6 production and apoptosis through the regulation of MT2A expression. SIMILARITY: Belongs to the EOLA family."}
{"protein": "MFSCQSLYKFSHSFRKRIPVMFQRAQQKSSLLHTQNESSHQPSLNKLGGFSSASLNFNSSRSSTNDDQQTFSSQSDNLPSSPITLPAKRGRSAASLKQLDNTVGFDVSKPSLPVFENSGLGSKYSTEIANGVYIDENDFDDDLLLENDIDQKPIPWSSSPIEHTKLTKSMLSSEKRSKNHLSKIYEDHTSEKGASSVISSNITRQGIKRSRTLPWAVDPYRYGDPDPKRTSTSADISQHTVSNDSSNKLSNGRSSSLDSLAKKRMSKSKSTPQISKKFSVPLNSASKSPIGSSLFKTSDSRKKSVPSIFLSDEQKRILDMVVEQQHSIFFTGSAGTGKSVLLRKIIEVLKSKYRKQSDRVAVTASTGLAACNIGGVTLHSFAGVGLARESVDLLVSKIKKNKKCVNRWLRTRVLIIDEVSMVDAELMDKLEEVARVIRKDSKPFGGIQLVLTGDFFQLPPVPENGKESKFCFESQTWKSALDFTIGLTHVFRQKDEEFVKMLNELRLGKLSDESVRKFKVLNRTIEYEDGLLPTELFPTRYEVERSNDMRMQQINQNPVTFTAIDSGTVRDKEFRDRLLQGCMAPATLVLKVNAQVMLIKNIDDQLVNGSLGKVIGFIDDETYQMEKKDAEMQGRNAFEYDSLDISPFDLPDVKQKKYKLIAMRKASSTAIKWPLVRFKLPNGGERTIVVQRETWNIELPNGEVQASRSQIPLILAYAISIHKAQGQTLDRVKVDLGRVFEKGQAYVALSRATTQEGLQVLNFSPAKVMAHPKVVQFYKQLASVNGLPIRNENKAPVQMRGVKNK", "text": "FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Involved in the maintenance of mitochondrial (mtDNA). Required for both repair of mitochondrial DNA and recognition of a recombinogenic signal characterized by a 26-bp palindromic at sequence in the ery region of mitochondrial DNA. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. Required for the completion of S-phase. SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus Note=Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair. SIMILARITY: Belongs to the helicase family. PIF1 subfamily."}
{"protein": "FFGWLIRGAIHAGKAIHGLIHRRRH", "text": "FUNCTION: Has antibacterial activity against Gram-positive bacteria B.subtilis ATCC 6633, L.garvieae ATCC 49156 and S.iniae F-8502, and Gram-negative bacteria E.coli WT-2, V.anguillarum ATCC 19264, V.penaeicida KHA, V.harveyi ATCC 14126, V.vulnificus ATCC 33148 and A.salmonicida NCMB 1102. Has hemolytic activity against human red blood cells. Seems to disrupt the membranes by adopting an alpha helical conformation. May play a significant role in innate host defense. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pleurocidin family."}
{"protein": "MTVDVLVARSDELDLASNTSDTTINATVVKDETIITRPPPTLTRSWSLPNASTRRTDNPAPPVLTRASSLPVKLVEPATDIDSDSSSVWTWAWSDEMQGPATSKRCGTRWIARLLPFFMLMLVGYATYDVVVYCCVEYFIQEIRKTATAIVLIVFYTIFFILMVAAYIRCYVTIQFNTGFVPWTAAREAAESERNERSTNGGDVESLQWSPADTNPDSPGLEAFYSKDVFICESDGLPKWCSECRSWKPDRAHHSSEYGRCVYKMDHVCPWMGGIISETSFNFFIQFTFYCACYCVLIVSTNAYVVTLRRNAGQSVEGRVVVGLALGSLFGLFSIAMTVTALRFVFQNITNVDLFRKNQTFRLAVRVPTGTRSTDQFTTITYPLSPPGDDSRAPGTAHSNGVDQSDGAGSIATNRMAARDQRAKRTFAILQTQSGENPWHVGYRNNFKSVMGETIFEWFLPLRHSPCTRHDSMVSDYEFGPLVEELKRRYGLAEEDAEKGANETTSS", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA5 subfamily."}
{"protein": "MSGDVEVYLSQVHDGSVSSGFRALYEERLLLDVTLLIEEHHFQAHKALLATQSDYFRVMFTADMRERDQDKIHMKGLTAAGFGHVLRFMYYGSLELSMLTVQEILQAAMYVQLTEAVEFCCSFLLAKICLENCAEVMRLLEDFSVGVEGVQEQLDAFLLENFVPLMARPDFLSYLSLEKLMAYLDSDQLSRYPEIELYEAVQAWLRHDRRRWRHTDAVVQNLRFCLMTPANIFEKVKTSEFYRYSRQLRLEVDQALSYFHQVNEQPLAETKSNRIRSVRPQTAVFRGMIGHSMVNSKILLLHRPKVWWELEGPQVPLRPDCLAIVNNFAFLLGGEELGPDGEFHASSKVYRYDPRQNSWLRMADMSVPRSEFAVGVIGKYIYAVAGRTRDETFYSTERYDIVEDKWEFVDPYPVNKYGHEGTVLNGKLYITGGITSSSTSKQVCVFDPGREGSSEHRTRRTPILTNCWENKSKMNYARCFHKMISHNGKLYVFGGVCVILRASFESQGCPSTEVYDPETDEWTILASMPIGRSGHGVAVLDKQIMVLGGLCYNGHYSDSILTFDPEENKWKEDEYPRMPCKLDGLQVCSLHFPEYVLEHVRRCS", "text": "FUNCTION: Substrate-specific adapter for an E3 ubiquitin-protein ligase complex. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MATQNADVTDATDYKKPPAETEQKALTIQPRSNKAPSDEELVRIINAAQKRGLTPAAFVQAAIVFTMDKGATDSTIFTGKYNTFPMKSLALRCKDAGVPVHKLCYFYTKPAYANRRVANQPPARWTNENVPKANKWAAFDTFDALLDPYVVPSSVPYDEPTPEDRQVNEIFKKDNLSQAASRNQLLGTQASITRGRLNGAPALPNNGQYFIEAPQ", "text": "FUNCTION: Required for genome encapsidation. Forms ribonucleoprotein complexes along with TGB1 helicase and viral RNA. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the potexvirus capsid protein family."}
{"protein": "MGSLPSRRKSLPSPSLSSSVQGQGPVTMEAERSKATAVALGSFPAGGPAELSLRLGEPLTIVSEDGDWWTVLSEVSGREYNIPSVHVAKVSHGWLYEGLSREKAEELLLLPGNPGGAFLIRESQTRRGSYSLSVRLSRPASWDRIRHYRIHCLDNGWLYISPRLTFPSLQALVDHYSELADDICCLLKEPCVLQRAGPLPGKDIPLPVTVQRTPLNWKELDSSLLFSEAATGEESLLSEGLRESLSFYISLNDEAVSLDDA", "text": "FUNCTION: Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane. Cytoplasmic vesicle. Note=Localized to the plasma membrane and intracellular vesicles, including late endosomal vesicles. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Note=May be cytoplasmic and is not localized to membranes."}
{"protein": "MSRPLPYHIHFFSGLLTCWILCTSSAHKCTVRHEVADCSHLKLTQIPDDLPTNITVLNLTHNQLRRLPPANFTRYSQLTTLDGGFNSISKLEPELCQSLPWLEILNLQHNEISQLSDKTFIFCMNLTELHLMSNSIQKIKNDPFKNLKNLIKLDLSHNGLSSTKLGTQLQLENLQELLLSNNKISSLTPGEFDFLGNSSLKRLELSSNQIKEFSPGCFHTLGELSGLSLNNAKLSPSLTEKLCLELSNTSIENLSLSSNQLDTISHTTFDGLKQTNLTTLDLSRNSLRVMGNDSFAWLPHLEYLSLEYNNIEHLSSRSFYGLSNLRRLDLRRSFTRQSISLTSLPKIDDFSFQWLKCLEYLNMDDNNFPGIKRNTFTGLVRLKFLSLSNSFSSLRTLTNETFLSLAGCPLLLLDLTKNKISKIQSGAFSWLGHLEVLDLGLNEIGQELTGQEWRGLDNIVEIYLSYNKYLELTTNSFTSVPSLQRLMLRRVALKNVDCSPSPFRPLPNLVILDLSNNNIANINDELLKGLEKLEILDLQHNNLARLWKHANPGGPVQFLKGLFHLHILNLGSNGFDEIPVEAFKDLRELKSIDLGMNNLNILPQSVFDNQVSLKSLSLQKNLITSVQKTVFGPAFRNLSYLDMRFNPFDCTCESIAWFVNWINITHTNISELSNHYLCNTPPQYHGYPVMLFDVSPCKDSAPFELLFMININILLIFIFIVLLIHFEGWRISFYWNVSVHRVLGFKEIDRAEQFEYAAYIIHAYKDRDWVWKHSSPMEDEDHTLRFCLEERDFEAGVLELEAIVNSIRRSRKIIFVVTQNLLKDPLCKRFKVHHAVQQAIEQNLDSIILIFLEEIPDYKLNHALCLRRGMFKSHCILNWPVQKERVNAFHHKLKVALGSRNSAH", "text": "FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll- like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane Early endosome. SIMILARITY: Belongs to the Toll-like receptor family."}
{"protein": "MSIDIDIIKARAKNEYRLSKVRGEAMISVRIPGGILPAHLLTVARDIAETWGNGQIHLTTRQKLAMPGIRYEDIDNVNAALEPFLREIEIELCDVQVEDTKAGYLAIGGRNIVACQGNRICQKANTDTTGLSRRLEKLVYPSPYHLKTVIVGCPNDCAKASMADLGIIGVAKMRFTADRCIGCGACVKACSHHAVGCLALKNGKAVKEESACIGCGECVLACPTLAWQRKPDQLWQVRLGGRTSKKTPRVGKLFLNWVTEDVIKQVIVNLYEFEKEMLGGKPIYLHMGHLIDKGGYLRFKERVLRGVQLNPEAMVAERIYWAEDESVARMHLKPAGH", "text": "FUNCTION: This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine (By similarity). FUNCTION: This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family."}
{"protein": "MHSSSSFIITSLEEEEKKPPAHHLHQQSIEDVGSVTSSATLLLLDSATWMMPSSTTQPHISEISGNECAACAQPILDRYVFTVLGKCWHQSCLRCCDCRAPMSMTCFSRDGLILCKTDFSRRYSQRCAGCDGKLEKEDLVRRARDKVFHIRCFQCSVCQRLLDTGDQLYIMEGNRFVCQSDFQTATKTSTPTSIHRPVSNGSECNSDVEEDNVDACDEVGLDDGEGDCGKDNSDDSNSAKRRGPRTTIKAKQLETLKNAFAATPKPTRHIREQLAAETGLNMRVIQVWFQNRRSKERRMKQLRFGGYRQSRRPRRDDIVDMFPNDQQFYPPPPPSNVQFFCDPYTTSPNNPETIQMAPQFAVPTENMNMVPEPYTEQSATPPEFNEDTFACIYSTDLGKPTPVSW", "text": "FUNCTION: Probable transcription factor which is required for asymmetric division of vulval blast cells (PubMed:1970421, PubMed:15466489). Involved in olfactory plasticity probably by regulating the expression of transcription factor mbr-1 in RIF neurons (PubMed:19561603). Plays a role in the chemorepulsive response toward ascaroside pheromones mediated by the ADL sensory neurons, probably by regulating E-box motif 5'-CANNTG-3' containing target genes in the ADL neurons (PubMed:29672507). Plays a role in the differentiation of the ADL sensory neurons (PubMed:29672507). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MASAGKPTLDDSRRATGSPKMKARENAKDTLCRNVTIYGRCRYEDKGCAFNHDPHKVNTTYQSDSRRRLNVDSPSFTPSLLSSNGSSPTTASVTAKKAATISPKAANAAPFQPRNITSRSNTSTPSGRAETMTPDWSVAEVQEFVPQGFDTAHMASLQGNSNGGVPSTSPFDPFVTASNPLSAASAVGPVQANPFAHDTAAAAAALGGAFFAGQSGFQQPVQYHLYAPIGPHSQNTLGYQRNVHDLFLPNDFREELQKKAAATLQTLPNTQLPAQVDYFHSLVPLDLNHQKNATIFGFPSWVYKAQSSKDGNFYALRRLEGFRLTNEKAIRSVQAWKRVCNGSVVTVHDAFTSRSFQDSSLIFVTDYHPLSKTLAEQHLGAGNRFQGRHNTHIPEQVLWGYMTQIANGLKAIHSNGLAARILDPSKVLVTGKNRIRLNACAIMDVVQYDTQRSIAELQRQDLVNFGQLIVTLGANTPSVMHNPTKAMEHFTRAYSPQLKNSVFWLLNGLQKDQDRNIDIFITGISSQLMSTFDSALHLDDELTSDLSRELENGRLVRLVTKLNFVNERPEYEHDRQWSENGERYFLKMFRDYVFHQVDAQGDPVVDLGHVLSCLNKLDAGTDEKITLVSRDEQSCFVVSYKDIKKALESSFQALLKPTRRLH", "text": "FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit pan2 to mRNA via its interaction with RNA and with pab1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family."}
{"protein": "MMMNSMIRQGWQQVLRRFSIPTSGDRLIVSNSTDQPIGLFGAFDTSLQTLSQVTNDPEVLKQKSNIPTHLDVASVLEASPRSFPWVFLTNSFCTFGGSIHAQNLQAFATAEFKSGFCYMNLLIPLSFDIIDAHADSFRGFVEQLPDTLGAYPSLSMVLNVMLHAATRFPEIVASPIPTIAFDAESLQFHVTDKRGVPGMWNILKACRVYELLSLAADGIGCEYMLYPVGAAPQYSFWKKSMDHFTSDRFVEFLAMQDLLASALEQDYATHDARDALLSALQNAGYTNVVARERRFPNGHDPSIVWLNLSEAPISEKLTELKRYLLVGHRSDDTADITHNVHQHVFEVLKTMSVQFSKTTNAYNRARFEVNHKVIWNAEYGRGPQQNAELEALVLFLNRQSLEIENILHRTTSPVVVTSWKPDVPPAAPEIKEEEPTHAIATPITEAPSHVTPVEVVNLPPTRSYWAETLVGILTAILGTVFAFLTRALIRAKRLRRKSTFPWVTLNSGDDDDDQSGGGGGGPQTPGGQPPVPHTRGTHQSRFSVQDIASDTSLLSVDLDEDTLSQYDETFQKIRRALFETSFADILQNSARWISTLEAMALADGNAPYTLLAQYLNGIEEAYTNFRNTGHISRATLSGFFALEDNLRAAGIAFGTTTPTQTIQNQFADSPARRWKTRFEQIACELGDASIKSLADLADIIDTERERGDLTQFDVLAASSISSLCRAVRIISDTTDPNAQLALVENATAMQNNINAILGTNVSIPFLSATRRLLITRRVQEAGAESRSGATPETVQQLADAELAKIVSEANMYNEMAASQRDIANATREATIREHVLSPVNALANVGMAAAFFRSGGLRSRAFNPAMPTMPGGPAAAGRPMFQAFRGRGHRLNR", "text": "SIMILARITY: Belongs to the bymoviruses polyprotein 2 family."}
{"protein": "MLLLADMDVVNQLVAGGQFRVVKEPLGFVKVLQWVFAIFAFATCGSYTGELRLSVECANKTESALNIEVEFEYPFRLHQVYFDAPSCVKGGTTKIFLVGDYSSSAEFFVTVAVFAFLYSMGALATYIFLQNKYRENNKGPMMDFLATAVFAFMWLVSSSAWAKGLSDVKMATDPENIIKEMPMCRQTGNTCKELRDPVTSGLNTSVVFGFLNLVLWVGNLWFVFKETGWAAPFMRAPPGAPEKQPAPGDAYGDAGYGQGPGGYGPQDSYGPQGGYQPDYGQPASGGGGGYGPQGDYGQQGYGQQGAPTSFSNQM", "text": "FUNCTION: Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Synapse, synaptosome. SIMILARITY: Belongs to the synaptophysin/synaptobrevin family."}
{"protein": "MGLSFTKLLGRLFSKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVGEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNISSKA", "text": "FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
{"protein": "MSDLDRLASRAAIQDLYSDKLIAVDKRQEGRLASIWWDDAEWTIEGIGTYKGPEGALDLANNVLWPMFHECIHYGTNLRLEFVSADKVNGIGDVLLLGNLVEGNQSILIAAVFTDEYERRDGVWKFSKRNACTNYFTPLAGIHFAPPGIHFAPSGA", "text": "FUNCTION: Catalyzes the conversion of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) to 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) via gamma- pentachlorocyclohexene (gamma-PCCH) (PubMed:12450824). Proceeds by two successive 1,2-anti conformationally dependent dehydrochlorinations (By similarity). Also shows activity with alpha- and delta-HCH, giving alpha- and delta-PCCH respectively, but not with the beta isomer (PubMed:12450824). FUNCTION: Catalyzes the conversion of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) to 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) via gamma- pentachlorocyclohexene (gamma-PCCH), proceeding by two successive 1,2- anti conformationally dependent dehydrochlorinations (PubMed:11099497). Also shows activity with alpha- and delta-HCH, giving alpha- and delta- PCCH respectively, but not with the beta isomer (Ref.6). Is involved in the degradation pathway that allows S.japonicum UT26 to grow on gamma- HCH as the sole source of carbon and energy (PubMed:7686793). SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the HCH dehydrochlorinase family."}
{"protein": "MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYTDLKDRPFFPGLVKYMNSGPVVAMVWEGLNVVKTGRLMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFKPEELVDYKSCAHDWVYE", "text": "FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically. Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not. Exhibits histidine protein kinase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, lamellipodium Cell projection, ruffle Nucleus Note=Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates. SIMILARITY: Belongs to the NDK family."}
{"protein": "MCNKNNTFEKNLDISHKPEPLILFNKDNNIWNSKYFRIPNIQLLNDGTILTFSDIRYNGPDDHAYIDIASARSTDFGKTWSYNIAMKNNRIDSTYSRVMDSTTVITNTGRIILIAGSWNTNGNWAMTTSTRRSDWSVQMIYSDDNGLTWSNKIDLTKDSSKVKNQPSNTIGWLGGVGSGIVMDDGTIVMPAQISLRENNENNYYSLIIYSKDNGETWTMGNKVPNSNTSENMVIELDGALIMSTRYDYSGYRAAYISHDLGTTWEIYEPLNGKILTGKGSGCQGSFIKATTSNGHRIGLISAPKNTKGEYIRDNIAVYMIDFDDLSKGVQEICIPYPEDGNKLGGGYSCLSFKNNHLGIVYEANGNIEYQDLTPYYSLINKQ", "text": "FUNCTION: Sialidases have been suggested to be pathogenic factors in microbial infections. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 33 family."}
{"protein": "MSGQEDWESEIDNPPACVPNLSNSEPAFKASNQNYFSSNNAFNRTTERGFGNRKASDDCNQNFEFSERGFGKQRAGSDANQNFESSERGFGNRRGKGRGGFGTFGKDSNGKQESGDFTNDDNRTIDDNRRRGGFQRRGGFNDETSGRGRRGVRGGTSFSGFGREDGNEQSGFTSNDGFNNETSGFGSGRRGSRGDSSFSGDRESDRGRGFGRGGFRGRNEDIGVESGKGQEGFERSEQGPRVTYIPPPPPAEESDIFKHYQTGINFDKYDDIVVEVSGSDVPPAILTFEEANLCDSLAKNVCKSGYVKLTPIQKHSIPIIVAGRDLMACAQTGSGKTAAFLLPILAHLMVKGVESSAFQTLKEPEAIIVAPTRELINQIYLDARKFSYGTCVRPVVIYGGTQMFHSLKQISEGCNILCATPGRLLDVIRKEKIGLTKLRYLVLDEADRMLDMGFREDIENLLKSSGMPSKEERQTLMFSATFPSSIQSLAREILKPDYLFVVVGQVGGACSDVEQMVIEVDEFGKKDKLMEILQEIGSERTMVFVKTKKKADFIATFLCQEKVPSTSIHGDREQKERETALRDFRTGQCPVIVATSVAARGLDIENVSYVINFDIPDDIDEYVHRIGRTGRCGNTGRAISFFDKRGDDEQRIARSLVKVLSDAHQEVPAWLEEVAFSAHGSSAYNPRSNKFASTDDRKRGDSRGDYSTSGFSPSAAQAEEEDWG", "text": "FUNCTION: Probable ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. SUBCELLULAR LOCATION: Cytoplasm Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA subfamily."}
{"protein": "MALHTVLIILSLLPMLEAQNPEHANFTIGEPITNETLSWLSDKWFFMGAAFRKLEYRQAIQTMQSEFFYLTTNLINDTIELRESQTIGDQCVYNSTHLGFQRENGTFSKYEGGVETFAHLIVLRKHGAFMLAFDLKDEKKRGLSLYAKRPDITPELREVFQKAVTHVGMDESEIIFVDWKKDRCGQQEKKQLELGKETKKDPEEGQA", "text": "FUNCTION: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family."}
{"protein": "MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNRIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK", "text": "FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2- phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M-band. SIMILARITY: Belongs to the enolase family."}
{"protein": "MKLKLYEYLGLIIGLLIALEPSYIHPDEHFQTLEPIFTAWTGAKGTATWEFLPENPCRSITILRLYYTPLLWLNQHIFHLKPLGLLYLYRLQNYLLYTAVVIFFLEFCEVSITHKTKAKFFIRTSYVTWVFQSHTFSNSLETIILLLFLFTCQYCIYEVRSRHYATFSSCFLLGALISIGTFNRVTFPAYLILPLLSVFYHCFLSHWIGVAYTAISTALVSALIILFDTKAYSSTDCKSWVIAPLNNLLYNMKVDNIAQHGLHPRYTHLLINLPLICGPIILLFISQKAVLKLPALSCISGILMLSLFRHQELRFIIPVLPLLCASMNLDNFDTFFQAETIITSWLVFNIVMGLIMGVFHQAGIIPLISYFSGEEFPVHIWWKTYSPPTWMYSNPDLTVSTTNFKENVEFVDNIPWHVVSNHVVDLKGSDIELLNKTLTKFSENTDSIQLIMPNTVLDKLTPLQSQWKFITEWETQQHLDLDHIDMPDWTTIKPGLRLYNVSLIV", "text": "FUNCTION: Alpha-1,2-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is essential in fungi (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ subfamily."}
{"protein": "MDTVKERVLAPGKEKMRNLAGKTLGHMHRVMERKQKTGEVIELTEDGRPMHMPEKKAPLVDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVDMVNNSTIHKGGKIIIKGKAKFNWDPETVGMIHGSFFWGYTVTQIPGGYISSRLAANRVFGAAILLTSTLNMFIPSAARVHYGCVMFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTSFCGSYAGAVVAMPLAGILVQYSGWSSVFYIYGSFGIVWYMFWILVSYESPADHPTITDEERTYIEESIGESAKLLGAMEKYKTPWRKFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGMVSALPHLVMTIIVPIGGQLADYLRSKNILTTTTVRKIMNCGGFGMEATLLLVVGFSHSKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGAMTKNKTREEWQNVFLIASLVHYGGVIFYGIFASGEKQPWADPEETSDEKCGFIDEDELAEETGDITLSHAPFGAQGALGAPAKTYGATTQLNGGWAKGWEKTEEFIQEDAERTYTGDGYS", "text": "FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as a uniporter which transports preferentially L-glutamate but also, phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane therefore affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, functions as a vesicular K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular L-glutamate uptake. The vesicular H(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Also involved in the regulation of retinal hyaloid vessel regression during postnatal development (By similarity). May also play a role in the endocrine L-glutamatergic system of other tissues such as pineal gland and pancreas (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Membrane; Multi-pass membrane protein Synapse, synaptosome Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily."}
{"protein": "MEIMDSGEPFLQWDKNLSELSEAGENDILYSTHFTDLLDDLSQEALLGQLLSDPFLSGRGDAMDTEEELTRASPVPPHIQAEHSYSLCGDSRPQSPLSHLPGEPGSDAADSESDEWPMEQEDKGIKMEPLLCVPLPALTLTVTPAGSAPEPVIDSCDSAQSLSLPQVKEDSNSPQIKLEPHEVDQFLNLSPKGLECLQMPPTPPSSVGSDSEGSQSPVHPCAPASPTQTPAVLKVAPRAPSSLSSSPLLTAPHKLQGSGPLLLTEEEKRTLIAEGYPVPTKLPLSKAEEKALKKIRRKIKNKISAQESRRKKKEYVDALEKKVETCSNENHELRRKVENLECTNKSLLQQLHSLQAVVAGKVPRSCRVTGTQTSTCLMVVVLCFSLFLGSFYPGLSPCSSITKADLSREISIHDSYTTTVKSRSLLSIQEPGGLDEPHPIGLGGEYPEWDRQADVMAAWRFEQQHKEEEAELHKAEHRPLLLSTNETHAQKAILIDLHTHRSNETAKVIQLDRTVNETS", "text": "FUNCTION: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/mbtps1 and S2P/mbtps2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis. May protect neuroblastoma cells from ER stress-induced death. In vitro activates transcription of target genes via direct binding to the CRE site. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element- binding protein 3-like protein 1) is transported into the nucleus. SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 2]: Nucleus Note=Upon ER stress, translocated into the nucleus. SIMILARITY: Belongs to the bZIP family. ATF subfamily."}
{"protein": "MEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDREQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYQPLGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDATPACLP", "text": "FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, microtubule organizing center Note=Enriched at the centrosomes during mitosis. Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis (By similarity). Localized at centrioles and in the nucleus at interphase (By similarity). Colocalizes with nubp-1 at prometaphase (By similarity). SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily."}
{"protein": "MAKKILYQDNARRALERGMEIMVEAVSVTLGPKGRNVVLEKSYGSPQIVNDGVTIAKEIKLLDHIENTGVSLIRQAASKTNDVAGDGTTTATVLAYAMVKEGLKNVAAGANPISIKLGMEKASQYLVTQINEFAQPVEDIQSIQQVASISAGNDEIIGSLIADALSKVGKEGVISLEEGKGIVTELEITEGMKLEKGFISPYFITNTEKMEVSYDNPYILLTDKRITLVQQDLLPILEQITKTKRPLLIIAEDVEKEALATLILNKLRGIINVVAVRAPGFGELRKQMLEDIAILTGGTVITQDAGLSLDNIQLNLLGQARRIIVNKDSTTIVSDGQTLNEINIRCEQLRKQVNIADTGYEKEKLQDRIAKLSGGIAVIRVGAVTETEMKDKKLRLEDAINATRAAVEEGIVPGGGATLTHLSENLVTWAKNNLKEDELIGAMIISRAILAPLRRIAENAGINGPVIIEKVQQQEFEIGYNAAKNTFGNMYTEGIVDPAKVTRSGLQNATSIASMILTTECIIVDDVKSSNES", "text": "FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chaperonin (HSP60) family."}
{"protein": "MALPRAMRPGGSHPNNFLFNTLPVIDNPVERQRAMAVFERESLRDAFEMLTPIAPSLKNAFLIFNEDGLLIHTSVGGEQVYIPIQTNNMESYSWKKAPPAVFLANVDGRRGLLDAFKAKTQTNVSKVVFEIENYSPSRILTQTVFSARDQTEEDTEMGSDAEGATQTVSSRLVKHEFNNYALMLPTRQPDVSMSLSKAQLNKILGVCKQAGDPITFQCLFDDTLQVRSGDRQVVFSVDYQHADNCGVESSSSLLEKMPMKTKKSAPEPIRGISGRRLFTLVLDEDTNFKQLIQKLKLKNAGAVLNFFLDPDSIPMIGLSTKQPFSVMMFFMCSYPTQPCQVGFSPAAFSSTPMGAGVKRRASEEEESDQPPKKLFPDGKLFKSNFVLLMDKTGAKIPCPEQPMHF", "text": "FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high-affinity direct interactions with DNA. Facilitates the origin-binding protein loading onto DNA thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA (By similarity). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae DNA polymerase processivity factor family."}
{"protein": "MSEEVSKRVEEEADTPGLEGQSDDSSDEGDASGDTEMDFLRSLFSRTLGLSPGDKVLDELTLDSVARYILSGKCKNIICMVGAGISTSAGIPDFRSPGTGLYANLQKYNLPYPEAIFQIDYFKKHPEPFFALARELYPGQFKPTVYHYFIKMLKDKGLLRRCYSQNIDTLERVAGLEGEDLIEAHGTFHTSHCVSFLCRKEYSMDWMKNQIFSEEIPKCDSCGSLVKPDIVFFGESLPSRFFTSMKADFPQCDLLIIMGTSLQVQPFASLVSRVSNRCPRLLINMEKTGQSEFGMGLFSFGGGMDFDSDKAYRDVAHLSTCDDGCMTLAELLGWKKELEEMVKREHALIDSKDAKKTDKEASQSSKSAVAEAEKTDKTE", "text": "FUNCTION: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (By similarity). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter (PubMed:24940000). Thereby contributes to regulate expression of vegfa, a key regulator of angiogenesis (PubMed:24940000). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the sirtuin family. Class I subfamily."}
{"protein": "MADSVDRVFVHALNTVKKIPKTGASRPPPTDRLRLYGLYKQAMEGDVDGVMERPTAASGLASDELQREKDKWDAWNLQKGLSRTESKRRYIEALIDTMHRYATTPDAEELVSELEFVWNQIKDNSPSSSLSSPRPNQSTGAGAQQPQQEPEQASDGEGPLKELRPMSEYDEAELRSQRQVDLEDDEVDVPTSDRSSGRWQRKVERALTTMSAEVAALREQIMTGREWRTKKERSVPAWVKWFAWLLVKHIFADLVILSVVLLWLRKRKDQRLEDIVRAGVRLMREYVRNVLPSRG", "text": "FUNCTION: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy (By similarity). Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways (By similarity). Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole (By similarity). Binds palmytoyl-CoA but not oleyl-CoA (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATG37 family."}
{"protein": "MAAEEKDPLSFFAAYGSSSSDSDSSDEEKEAEKTKNRATKRPFPTETKKLPGPDELFRSVSRPAFLYNPLNKQIDWESRVKRAPEEPPKEFKVWKTNAVPPPESYQVAEKKAPPPELDMAIKWSNVYQDNGDDAPHANQAKCLPEEEAQEDSPPSDDEQENATKKHKV", "text": "SIMILARITY: Belongs to the UPF0690 family."}
{"protein": "MRSLLLLSIVFFVVTVSANKTRELCMKSLEHAKVDTSNEARQDGIDLYKHMFENYPPLRKYFKNREEYTAEDVQNDPFFAKQGQKILLACHVLCATYDDRETFNAYTRELLDRHARDHVHMPPEVWTDFWKLFEEYLGKKTTLDEPTKQAWHEIGREFAKEINKHGRHAVRHQCMRSLQHIDIGHSETAKQNGIDLYKHMFENYPSMREAFKDRENYTAEDVQKDPFFVKQGQRILLACHLLCASYDDEETFHMYVHELMERHERLGVQLPDQHWTDFWKLFEEFLEKKSHLCEHTKHAWAVIGKEFAYEATRHGKEHHEHKEEHKEEHKEEHKEEQH", "text": "FUNCTION: Has an extremely high oxygen affinity. In a vacuum, it takes several minutes to release its oxygen compared to milliseconds for a normal globin. Could be used as an oxygen scavenger for sterol biosynthesis. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the globin family."}
{"protein": "MKIRSLLANCYLYFLSAIAFFLQWVKPESKVTLLISFEANAKAILEEYEQGQYSYKLNILYTQQASAIAESFPNVDAYLLQEKNPIHLIKAVYLMFNSKVIITDNYFLLTSVLNKRKQTKCIQVWHANGSLKKFGLEDITNMQRTKTDIKRFQKVYSSYDYLTVGSEEMANIFKKSFGIKDNQLLKIGVPLTDPYYRENKKKISDTLNIQRKKIILYAPTFRDYNMQSIQLPFTEEQLIHQLKEEYVLFVKLHPAIQNNIDIKYSSDYIKDVSNYALFDLLMAADILITDYSSVPFEFSILNKPILFYTYDLKLYQQKRGLVDNYLSIIPGRACYDSESLINEIQTPFNYSKIKVFSDRWNKYSDGNSSQNLLNFIENLIS", "text": "FUNCTION: Catalyzes the addition of a single glycerol phosphate residue to the prenoldiphosphate-linked disaccharide, as a primer for polymerisation by TagF. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase family."}
{"protein": "MTRQSLWDLSETDVEDGEIRINVGGFKRRLRSHTLLRFPETRLGRLLLCHSREAILELCDDYDDVQREFYFDRNPELFPYVLHFYHTGKLHVMAELCVFSFSQEIEYWGINEFFIDSCCSYSYHGRKVEPEQEKWDEQSDQESTTSSFDEILAFYNDASKFDGQPLGNFRRQLWLALDNPGYSVLSRVFSVLSILVVLGSIITMCLNSLPDFQIPDSQGNPGEDPRFEIVEHFGIAWFTFELVARFAVAPDFLKFFKNALNLIDLMSIVPFYITLVVNLVVESSPTLANLGRVAQVLRLMRIFRILKLARHSTGLRSLGATLKYSYKEVGLLLLYLSVGISIFSVVAYTIEKEENEGLATIPACWWWATVSMTTVGYGDVVPGTTAGKLTASACILAGILVVVLPITLIFNKFSHFYRRQKQLESAMRSCDFGDGMKEVPSVNLRDYYAHKVKSLMASLTNMSRSSPSELSLDDSLH", "text": "FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2. SIMILARITY: Belongs to the potassium channel family. S (TC 1.A.1.2) subfamily. Kv9.2/KCNS2 sub-subfamily."}
{"protein": "MAEEQDLSEVELSPVGSEEPRCLSPGSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGEAEQGGTAAIQAHYKSAHLDHRHPGEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSMGEGGKPHIDFGNVDIGEISHEVMSNMETFDVAELDQYLPPNGHPGHVSSYSAAGYGLGSALAVASGHSAWISKPPGVALPTVSPPGVDAKAQVKTETAGPQGPPHYTDQPSTSQIAYTSLSLPHYGSAFPSISRPQFDYSDHQPSGPYYGHSGQASGLYSAFSYMGPSQRPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP", "text": "FUNCTION: Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3 (PubMed:21965087). Transcriptional activator of MBP, via binding to the gene promoter (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side."}
{"protein": "MTQAFFFLLLVSLVASTLSKEFNFCPRAIDEVCPVKEKRNECCSSKECRFGEMCCSEPCGNVCRVKSDTPLGFPAKEDSNCKVGEIKKKWYQKVWSKITKWG", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom protein 11 family. 02 (wap-2) subfamily."}
{"protein": "MSDKLKSNKKLEGETFMKEGDKLSKTNIFRWKADWDSAALAYEKAANAFRSAKIYDSAKYCFLRLSLCQTHMDVYYLAAKSMENASAMAKELKETQECANLLLESCKLYRTNGNSFQAADTMTKAAKLLEDIDLNQTIKLLTDACELFELDDKDHFSGDTFKQTISMLLKHKKYTEAVDLMILQNRVFVKLEQNHDLHKSCLSVITISLATDDIVASKKYYEQFLDYPSFIHSQEGTTAQELITAFDNHDVDGVKKIVSRHIFNFLDNQVAKIAKNLSISKDSLNPTINSTAPQQQYSNTTTTTTNNTNNNNPTSQQDDDEDVL", "text": "FUNCTION: May be required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus (By similarity). Involved in vesicle fusion with nsfA and probably SNARE proteins. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNAP family."}
{"protein": "MGAFPSPPPWGWSTGFITTPLTTGRLPSQHLDPALPKLFWFTPTLPTCPTVAKQFWDTKRTSPDGNLKVADLPSFAISFATAPAALANCPPLPRVISMLCMAVPKGISVEVDSSFLSKNPFPNCTSFFQSIRLSRCI", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf72 family."}
{"protein": "MAADGVDERSPLLSASHSGSVTPTAPPYLQDSSPRAELPPPYTAIVSPDASGIPVINCRVCQSLINLDGKLHQHVVKCTVCNEATPIKNPPAGKKYVRCPCNCLLICKDTSRRIGCPRPNCRRIINLGPVMLVSEEQPAQPALPVQPEGTRVVCGHCGNTFLWMELRFNTLAKCPHCKKISSVGSALPRRRCCAYITIGMMCIFIGIGLTVGTQDFARRFHATYVSWAIAYLLGLVCLIRACYWGAIRVSYPEHSFA", "text": "FUNCTION: Catalyzes the hydrolysis of phosphatidylinositol-4,5- bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5- monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity). Negatively regulates the phagocytosis of large particles by reducing phagosomal phosphatidylinositol 4,5-bisphosphate accumulation during cup formation (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein."}
{"protein": "MRLLLWVLLVTLVTFLSSGDAAPVDSNKQLERAAINKVTSRNLANDNSLKHEKRFLRGDRSNIVNLKDGDENEERKIGQKMTTALKSIKVWYLKWEQKILLPGFKKMAKKEMTYSKLMDRFRVRMMNSGRWGTPSGFKRYGRLYKDYLISINRADLTV", "text": "FUNCTION: Secreted effector that completely suppresses elicitor-induced cell death in host and enhances virulence of P.parasitica. SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family."}
{"protein": "MGAVPGVVLLLMLAVLGIRAAPAPEECHKLTKPVTKADVQSVSGDWVLVWSVANTTERWICENLTSSYVEFKLHSDIIEYTERNLFLGNSCISFYSNLSASTEKQQQFSLNNLQMEEKGVVRPFNDNGTVKFFETCVDCLSMEYSGDIGRFLLIYRRDGVHQNVEVLKAAQDESQKLAECLGFSIDEPFIYDGVSDFCHKKSPEECHKLTKPVTKADVQSVSGDWVLVWSIDENSTISDDWKKLKTSYVEQRVDSGVIRFTERNMLKNNSCMTFKTNMTAGPESQNTFIYTSGKMEENGVVTVLDENGTVKFFETCADCLSMEYSGFFGHFLLIYRRDGVHQNVEVLKAAQDESQKLAECLGFSIDEPFIYDGVSDFCHKKSSPEVKPEQD", "text": "FUNCTION: Binds both saxitoxin and tetradotoxin. May play a role in toxin accumulation and/or excretion. SUBCELLULAR LOCATION: Secreted."}
{"protein": "MTALNWKPFIYGGLASITAECGTFPIDLTKTRLQVQGQPNDAKYKEIRYRGMMHAIVRIWREEGVKALYSGIAPAMLRQASYGTIKIGTYQSLKRLFVDCPEDETLVLNAFCGVLSGVVSSCIANPTDVLKIRMQAQGNVMQGGMIVNFINIYQQEGTRGLWKGVSLTAQRAAIVVGVELPVYDITKKHLILSGLMGDTVYTHFLSSFTCGLAGALASNPVDVVRTRMMNQRSIRDASNSSYKGTLDCLLQTWKNEGFFALYKGFWPNWLRLGPWNIIFFITYEQLKKLNL", "text": "FUNCTION: Antiporter that transports inorganic anions (sulfate, sulfite, thiosulfate and phosphate) and, to a lesser extent, a variety of dicarboxylates (e.g. malonate, malate and citramalate) and, even more so, aspartate. The sulfate/sulfate exchange is much higher than the phosphate/phosphate and malate/malate exchanges. The transport affinities is higher for sulfate and thiosulfate than for any other substrate. May catalyze the export of sulfite and thiosulfate (the hydrogen sulfide degradation products) from the mitochondria, thereby modulating the level of the hydrogen sulfide. Also may mediate a very low unidirectional transport of sulfate. FUNCTION: Probable transporter. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."}
{"protein": "MSSVTWAPGNYPSTRRSDHVDTYQSASKGEVPVPDPYQWLEESTDEVDKWTTAQADLAQSYLDQNADIQKLAEKFRASRNYAKFSAPTLLDDGHWYWFYNRGLQSQSVLYRSKEPALPDFSKGDDNVGDVFFDPNVLAADGSAGMVLCKFSPDGKFFAYAVSHLGGDYSTIYVRSTSSPLSQASVAQGVDGRLSDEVKWFKFSTIIWTKDSKGFLYQRYPARERHEGTRSDRNAMMCYHKVGTTQEEDIIVYQDNEHPEWIYGADTSEDGKYLYLYQFKDTSKKNLLWVAELDEDGVKSGIHWRKVVNEYAADYNIITNHGSLVYIKTNLNAPQYKVITIDLSKDEPEIRDFIPEEKDAKLAQVNCANEEYFVAIYKRNVKDEIYLYSKAGVQLTRLAPDFVGAASIANRQKQTHFFLTLSGFNTPGTIARYDFTAPETQRFSILRTTKVNELDPDDFESTQVWYESKDGTKIPMFIVRHKSTKFDGTAAAIQYGYGGFATSADPFFSPIILTFLQTYGAIFAVPSIRGGGEFGEEWHKGGRRETKVNTFDDFIAAAQFLVKNKYAAPGKVAINGASNGGLLVMGSIVRAPEGTFGAAVPEGGVADLLKFHKFTGGQAWISEYGNPSIPEEFDYIYPLSPVHNVRTDKVMPATLITVNIGDGRVVPMHSFKFIATLQHNVPQNPHPLLIKIDKSWLGHGMGKPTDKNVKDAADKWGFIARALGLELKTVE", "text": "FUNCTION: Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino- acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530). SIMILARITY: Belongs to the peptidase S9A family."}
{"protein": "MTISPPEREPKVRVVVDNDPVPTSFEKWAKPGHFDRTLARGPQTTTWIWNLHALAHDFDTHTSDLEDISRKIFSAHFGHLAVVFIWLSGMYFHGAKFSNYEAWLADPTGIKPSAQVVWPIVGQGILNGDVGGGFHGIQITSGLFQLWRASGITNEFQLYCTAIGGLVMAGLMLFAGWFHYHKRAPKLEWFQNVESMLNHHLAGLLGLGSLAWAGHQIHVSLPINKLLDAGVAAKDIPLPHEFILNPSLMAELYPKVDWGFFSGVIPFFTFNWAAYSDFLTFNGGLNPVTGGLWLSDTAHHHLAIAVLFIIAGHMYRTNWGIGHSLKEILEAHKGPFTGAGHKGLYEVLTTSWHAQLAINLAMMGSLSIIVAQHMYAMPPYPYLATDYPTQLSLFTHHMWIGGFLVVGGAAHGAIFMVRDYDPAMNQNNVLDRVLRHRDAIISHLNWVCIFLGFHSFGLYVHNDTMRAFGRPQDMFSDTGIQLQPVFAQWVQNLHTLAPGGTAPNAAATASVAFGGDVVAVGGKVAMMPIVLGTADFMVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSGWDHVFLGLFWMYNCISVVIFHFSWKMQSDVWGTVAPDGTVSHITGGNFAQSAITINGWLRDFLWAQASQVIGSYGSALSAYGLLFLGAHFIWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSIIQGRAVGVAHYLLGGIATTWAFFLARIISVG", "text": "FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family. SIMILARITY: Belongs to the PsaA/PsaB family."}
{"protein": "MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG", "text": "FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN) (PubMed:11106397, PubMed:12496260). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments (PubMed:12496260). Has no direct bacteriolytic activity (PubMed:12496260). FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family."}
{"protein": "MTLGSGGSSVVVPRNFRLLEELERGEKGIGDGTVSYGMDDGDDIYMRSWTGTIIGPHNTVHEGRIYQLKLFCDKDYPEKPPTVRFHSRVNMACVNHETGVVDPKKFGLLANWQREYTMEDILVQLKKEMSTSHNRKLVQPPEGTCF", "text": "FUNCTION: Has no ubiquitin ligase activity on its own. The heterodimer with UBC catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. May play a role in the control of progress through the cell cycle and differentiation. Involved in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family."}
{"protein": "MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRTVRFGTKLGSDIKLEDSLWVSLTDQHVQLPIAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTAGNASGIADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA", "text": "FUNCTION: In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta- oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. Also catalyzes the condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could be involved in the production of ketone bodies. Also displays hydrolase activity on various fatty acyl-CoAs (By similarity). Thereby, could be responsible for the production of acetate in a side reaction to beta- oxidation (By similarity). Abolishes BNIP3-mediated apoptosis and mitochondrial damage (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MKISSGTINFSTIPNQVKKLITSIREHTKNGLASKITSVKNTHTSLNEKFKTGKDSPIEFTLPQKIKDFFQPKDKNTLNKTLITVKNIKDTNNTGKKNISEEDASKMTAAFMRKHIANQSRDYNYRVTGAAPLPGGVSVSANNRPTVSEGRTPPVSPSLSLQATSSPSSPADWAKKLTDAVLRQQAGEPLTTADRDFSNADFRNIKFSKILPPNFMKRDGDIIKGFNFSNSKFTYSDISHLHFDECRFTYSTLNDVVCSNTKFSNSDMNEVSLLYSITTQQQPSFINTTLKNTLIPHKANLSDVILNEPDNSSPPSVSGGGNFIRLGDIWLQMPLLWTENAVDGFLNHEHNNGKSILMTINNLPDKYRQEKVRAMEDLVKSFRSGRLTEARIRPVESSLVSVLAHPPYTQSALISEWIRPVQERFFAHQCQTYNDVPLPAPDTYYQQRILPVLLDSFDRNSAAMTTHSGLFNQVILHCMTGVDCTDGIRQKAAALYEQYLAHPAVSPHIHNGLFGNYDGSPDWTTRAADNFLLLSSQDSDTAMMLSTDTLLTMLNPTPDTAWDNFYLLRAGENVSTAQISPVELFRHDFPVFLAAFNQQAVQRRFGELIDIILSTEEHGELNQQFIAATNQKHSTVKLIDDASVSRLNTIFDPLLPEGKLSPAHYQHILSAYHLTDATPQKQAETLFCLSTAFARYSSSAIFGTEHDSPPALRGYAEALMQKAWELSPAIFPSSEQFTDWSDRFHGLHGAFTCTSVVADSMQRHARKYFPSVLSSILPLAWA", "text": "FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. SUBCELLULAR LOCATION: Secreted Host cell Note=Secreted via type III secretion system 1 (SPI-1 TTSS), and delivered into the host cell. SIMILARITY: Belongs to the SopA E3 ligase family."}
{"protein": "MTKEEGRTYFESLCEEEQSLQESQTHLLNILDILSVLADPRSSDDLLTESLKKLPDLHRELINSSIRLRYDKYQTREAQLLEDTKTGRDVAAGVQNPKSISEYYSTFEHLNRDTLRYINLLKRLSVDLAKQVEVSDPSVTVYEMDKWVPSEKLQGILEQYCAPDTDIRGVDAQIKNYLDQIKMARAKFGLENKYSLKERLSTLTKELNHWRKEWDDIEMLMFGDDAHSMKKMIQKIDSLKSEINAPSESYPVDKEGDIVLE", "text": "FUNCTION: Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export- competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MTSAVVDSGGTILELSSNGVENQEESEKVSEYPAVIVEPVPSARLEQGYAAQVLVYDDETYMMQDVAEEQEVETENVETVEASVHSSNAHCTDKTIEAAEALLHMESPTCLRDSRSPVEVFVPPCVSTPEFIHAAMRPDVITETVVEVSTEESEPMDTSPIPTSPDSHEPMKKKKVGRKPKTQQSPISNGSPELGIKKKPREGKGNTTYLWEFLLDLLQDKNTCPRYIKWTQREKGIFKLVDSKAVSKLWGKHKNKPDMNYETMGRALRYYYQRGILAKVEGQRLVYQFKDMPKNIVVIDDDKSETCNEDLAGTTDEKSLERVSLSAESLLKAASSVRSGKNSSPINCSRAEKGVARVVNITSPGHDASSRSPTTTASVSATAAPRTVRVAMQVPVVMTSLGQKISTVAVQSVNAGAPLITSTSPTTATSPKVVIQTIPTVMPASTENGDKITMQPAKIITIPATQLAQCQLQTKSNLTGSGSINIVGTPLAVRALTPVSIAHGTPVMRLSMPTQQASGQTPPRVISAVIKGPEVKSEAVAKKQEHDVKTLQLVEEKPADGNKTVTHVVVVSAPSAIALPVTMKTEGLVTCEK", "text": "FUNCTION: Isoform 1 transcriptionally activates the LYN and BLK promoters and acts synergistically with RUNX1 to transactivate the BLK promoter. FUNCTION: Isoform 2 may function in repression of RUNX1-mediated transactivation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family."}
{"protein": "MGVVLFIFLVLFPLATLQLDADQPVERHAENKQLLNPDERRGIILHALRKRCCHSSWCKHLC", "text": "FUNCTION: Shows excitatory effect on mice by intracranial injection, followed by rigid paralysis of the rear legs and recovering after 30 min. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily."}
{"protein": "MASILNTLRFLEKTSFYNCNDSITKEKIKIKHKGMSFVFYKPKHSTVVKYLSGGGIYHDDLVVLGKVTINDLKMMLFYMDLSYHGVTSSGVIYKLGSSIDRLSLNRTIVTKVNNYDDTFFDDDD", "text": "SIMILARITY: Belongs to the orthopoxvirus OPG159 protein family."}
{"protein": "MSTSESPSSRFRELSKYINSLTNLLGVDFLSPKLKFNYRTWTTIFAIANYTGFTVFTILNNGGDWRVGLKASLMTGGLFHGLGKFLTCLLKHQDMRRLVLYSQSIYDEYETRGDSYHRTLNSNIDRLLGIMKIIRNGYVFAFCLMELLPLAMLMYDGTRVTAMQYLIPGLPLENNYCYVVTYMIQTVTMLVQGVGFYSGDLFVFLGLTQILTFADMLQVKVKELNDALEQKAEYRALVRVGASIDGAENRQRLLLDVIRWHQLFTDYCRAINALYYELIATQVLSMALAMMLSFCINLSSFHMPSAIFFVVSAYSMSIYCILGTILEFAYDQVYESICNVTWYELSGEQRKLFGFLLRESQYPHNIQILGVMSLSVRTALQIVKLIYSVSMMMMNRA", "text": "FUNCTION: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Heteromeric odorant receptor channel (TC 1.A.69) family. Or67d subfamily."}
{"protein": "MSRQACKKSFSCGSQGFSGHSAVVSGSSRSSCVARSGAASGGACGFRSGAGSLGSHSLYSLGGSKSISISVAAGGSRAGGFSGGRSSCGSGFGSGYGGSLGGSRGMGAGFGGPSGFGGAGGFGRPGSFGPGSCPGGIQEVTINQSLLQPLNVEIDPQIGQVKAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTIRSGSGPQNLEPFFESYISCLRKQLDSLLGAKGSLEGELKSMQDLVEDFKKKYEEEINRRTAAENEFVGLKKDVDGAFMNKVELQAKVDSLTDEINFLRTLYDMELSQIQSHVSDTSVVLSMDNNRCLDLDSIIAEVKAQYEDIAQKSKAEAEALYQTKLGELQTTAGRHGDDLRSTKSEIMDLNRMIQRLRAEIENVKKQNTNMQTSIAEAEQRGERALKDADTKFQDLQVALQKAKEDMARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLSGEFQNAVSISVVSNVTSTSSSGSFRGTGGSNYGGDSSGRSGGSSSSSSRGSSSRGSSGSRLGSGGSISVSQQRMGFNSGGSQTSVGSSYKSGRGGSSSVQFSQTTSSSQQRSK", "text": "FUNCTION: Probably contributes to terminal cornification. SIMILARITY: Belongs to the intermediate filament family."}
{"protein": "MFQYSLWPLLALSGGTGLAYLVVVVVYNLFFHPLRNFPGPWLNSITQVPHTLLMLCGLPHKKHLALHMKYGPVVRIGPNMLSFNHPDAMKDVRGHRKSGEPEHGKDPISVQSNGDNIVGSDRENHTRFRRALAYGFSAQAMLEQEPTFKAYVNQLFQRLHEQSSGGTKPVDISKWYTFTTFDMIGDLAFGESFSCLDNSTYHPWVSLAFESLKSLAFLAEIGRYPRIAPYLGLLVPRGLLTKFAENKELASMKVRKRLDTETDRPDFVGKITQGLKSKGTSMEFNELASNASVLIVAGSETTATLLSAAVYFLCAHPRTLDLLTKEVRSTYTQAHDIDLVSTQGLRYMQAVLDEALRMYPPVAGGGSPRKIAKGGSFVAGHFVPENTLVENDMWAMHYDPKYFTQPHDFIPERWLGDVRFANDRLDAVKPFSIGPRNCIGMNLAYAEMRMMLARTVWEFDIRLSEGSRNWYEESRVYLAWNKPPLNVYLIPR", "text": "FUNCTION: Trichothecene C-15 hydroxylase; part of the core gene cluster that mediates the biosynthesis of trichothecenes, a very large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including T2-toxin (PubMed:11352533, PubMed:9435078). The biosynthesis of trichothecenes begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:3800398). Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4 (PubMed:7651333). TRI4 controls the addition of four oxygens at C-2, C-3, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichotriol (PubMed:16917519). Isotrichotriol then undergoes a non-enzymatic isomerization and cyclization to form isotrichodermol (PubMed:2317042). During this process, the oxygen at the C-2 position becomes the pyran ring oxygen and the hydroxyl group at C-11 is lost (PubMed:2317042). More complex type A trichothecenes are built by modifying isotrichodermol through a series of paired hydroxylation and acetylation or acylation steps (PubMed:11352533). Isotrichodermol is converted to isotrichodermin by the acetyltransferase TRI101 (PubMed:10583973). TRI101 encodes a C-3 transacetylase that acts as a self-protection or resistance factor during biosynthesis and that the presence of a free C-3 hydroxyl group is a key component of Fusarium trichothecene phytotoxicity (PubMed:10583973). A second hydroxyl group is added to C-15 by the trichothecene C-15 hydroxylase TRI11, producing 15-decalonectrin, which is then acetylated by TRI3, producing calonectrin (PubMed:9435078, PubMed:8593041). A third hydroxyl group is added at C-4 by the cytochrome P450 monooxygenase TRI13, converting calonectrin to 3,15-diacetoxyspirpenol, which is subsequently acetylated by the acetyltransferase TRI7 (PubMed:12135578, PubMed:11352533). A fourth hydroxyl group is added to C-8 by the cytochrome P450 monooxygenase TRI1, followed by the addition of an isovaleryl moiety by TRI16 (PubMed:12620849, PubMed:14532047). Finally, the acetyl group is removed from the C-3 position by the trichothecene C-3 esterase TRI8 to produce T-2 toxin (PubMed:12039755). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MGEFNEYDDIDDFFCNDISPLHDEADEFGSTDIALPSQLYGKGPKPRAGESKALRDRNKESGSGTESEAKGDTLATKRGRSSWRRGASESSRSSSLGSSSPSDSSSGRSLSPVRPAKRKRTDEQQPESEANRFLAEMERDIELSAGPGGGETATGKGGRDTDARVYNVGFISRIEGSRNRRVNVKVTGQKQFATFLAIALAAFSKQHNIRKSLKPKYQADQVKIYREGVEVFKFMTCDSFNIEEPYNASATDIEVYIVPVDEATAFEQEWKRKFEERVRMLSNSSFLEVMDDIEDDNDDFLVNEYEKALVNARSLNETELAVREGTPADESSQLLKIVLLGSDNKKVFIHVRPTTTLLKVAEHYRVAKELPPTVQLSLMFDHEEIDLDDTICNIDIEDGDIIEVVVK", "text": "FUNCTION: May be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ESC2). Involved in HMR and telomere silencing via the recruitment or stabilizing of the SIR (silent information regulators) complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus."}
{"protein": "MPNKDDDNLDMGDSNVSRKGGLLPDIIIKILQILAIGIFTVAIMIIVSYFVSKMVVSQSGAPSDFPVFSNEYLGKPPMLIWYESIDEIRGNTLDVPPKTFVVKLALGYAENNVNILNELGRQKVRLKDIIREYFSQRTGQEIKNESQIKAEIKARINSILRNGEIKEIALTQIDIFDM", "text": "FUNCTION: Controls the rotational direction of flagella during chemotaxis. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FliL family."}
{"protein": "MAFSPAHRLLARLGSTSIYKRVWRYWYPLMTRGLGADKIAFLNWAYEEDPPIDLTLEVSDEPNRDHINMYHRTATHVELSGKRVLEVSCGHGGGASYLTRTLHPASYTGLDLNRAGIKLCQRRHNLPGLDFVRGDAENLPFEDESFDVVLKVEASHCYPHFSRFLAEVVRVLRPGGYLLYTDLRPSNEIAEWEADLAGSPLRQLSQREINAEVVRGIEKNSHTSRVLVDRNLPAFLRFADRAVGRQLSRYLEGGELSYRMYCFTKDFAASR", "text": "FUNCTION: Catalyzes the methylation of the lipid moiety of the intermediate compounds phthiotriol and glycosylated phenolphthiotriol dimycoserosates to form phthiocerol dimycocerosates (DIM A) and glycosylated phenolphthiocerol dimycocerosates (PGL). SIMILARITY: Belongs to the methyltransferase superfamily. Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase family."}
{"protein": "MGRRFKFLQKLAFLGQNHRYKALERDEVDTLIDEQYELKAIEREKAVAALPPREACKCSKEELARTFHVDLDSGLSEFAVAQRRLVHGWNEFVTDNTEPVWKKYLDQFRNPLILLLLGSSVVSVLTKEYEDAISIALAVLIVVTVGFIQEYRSEKSLEELTKLVPPECNCLRDGKLRHMLARDLVPGDVVSLSMGDRIPADIRLTEVTDLLVDESSFTGEVEPCSKTDSPLAGGGDLSTLSNVVFMGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTVFSFGIIGLLMLVGWVQGKPLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEVSGIGYSGEGTVCLLPSKEVIKEFSNVSVGKLVEAGCVANNAVVRKNAVMGQPTEGALVVLAMKMNLGSIKDSYIRKKEIPFSSEQKWMAVRCSLKNEDEEDVYFMKGAFEEVIHHCSTYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELGRLTFLGLVGIIDPPRAGVKEAVQALSESDVSVKMVTGDALETALAIGRTIGLCDEKLKAMSGEEVEGMEQDALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAADMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPNPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALKRPPRSVKDTILNRALILKILMSAAVILGGTLFIFWREIPENRTSTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSILGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKLCEKFCSRAKADQMLPEAV", "text": "FUNCTION: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway. Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state. Induces Ca(2+) influx independently of its ATP-driven pump function. At the basolateral membrane of mammary epithelial cells, interacts with Ca(2+) channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May facilitate transepithelial transport of large quantities of Ca(2+) for milk secretion via activation of Ca(2+) influx channels at the plasma membrane and active Ca(2+) transport at the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily."}
{"protein": "MTDLHKEWEKVQEMAFASWVNSVLEKRGGVEKISDVSTDLSDGVKLIFFLESVSGKKFPKKFDLEPKTRILRIQNLHLAMLFVDEDLKVKVQGVAAEEFVDNNKKMILGFLWTLYRKYRISVINEGDKSSEEGLLAWVKKTTDGYSGVNITNFKASFRDGNAYLALAHKFDPSVFKYDEFSGKDQIERLNAAFDFAEKGLGIPKLLDAESLSKGNVDERSIILYTSLFFHAYRAKEEREALEASQNSLANKLASLEQSLEGEKTSQDELARQKKELEESLRLIRQQNEQRNQRIADIQSKIDDALRGIDDEKMAKLDLESRLSKTEKDKAILELKLAETLDENERLRNKIEEDKKRAAAEAEGLGLLRTHIGHQITDIAKWQSFLDNPEAVPYTKTPVNLEAELASLQFEEQAKRLGSKVENENISLEKYLSLKEEELKSAGAPKKRTK", "text": "FUNCTION: Actin-bundling protein. When linked to F-actin the actin filaments form preferentially anti-parallel bundles that associate into meshworks. Plays a major role in cytokinesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the cortexillin family."}
{"protein": "MGNVIRVQHLNYTYPEAKQQALTDVSFDVAKGEWLAIIGHNGSGKSTLAKNLNGLLAPESGTVQVAGMTLSEETVWDIRAKVGIVFQNPDNQFVGATVADDVAFGLENRGVPRPEMIKRVDEALDRVGMTAFADREPARLSGGQKQRVAIAGIVAQRPEIIILDESTSMLDPAGRQEVLGVIRELKDELGLTVLSITHDIDEAAEAHRIILLNDGKINEIGTPSEIFSHGMELLRLGLDVPYSEKLKDALAQRGIAMPKDYMDNERLVDYLWTLHSTM", "text": "FUNCTION: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates including 5-formyltetrahydrofolate and thiamine. Expression of the complex plus FolT or ThiT in Lactococcus lactis subsp. cremoris (strain NZ9000) allows 5-formyltetrahydrofolate or thiamine uptake respectively; 5-formyltetrahydrofolate or thiamine are not taken up in the absence of FolT/ThiT or the EcfA1A2T complex. Deenergized L.lactis subsp. cremoris (treated with 2-deoxyglucose) does not take up substrate. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family."}
{"protein": "MSNRRREFIEYIDSREPVEADIDISDKADRLTDIYDSDTYGLNAMRETLPSHCYKKIREVMQTGSALDPEIADMVANGMKEWAIKQGATHYCHWFLPLNGLAAEKHDSFISIFPGDDKVLLEFSGMQLIKGEPDASSFPSGGIRSTWEARGYTVWDATSPAFIRREKNGAILCIPTAFCSWTGEALDQKTPLLRSMEYVSNESIITLSSLFNEKHKRISPTLGIEQEFFLIDRKFYLARPDLVNCGRTLIGAKPPKGQEMEDHYFGTMNSRIISCIQEVEWKMWRLGMPLKTRHNEVAPGQYEVAPIFERANIAADHNMMLMDILKNVSTKHGLVCLFHEKPFAGVNGSGKHNNWSLSTDGGSNLLEPGHTPSQNARFILFLTAIIRAVDIHADLLRASVAVPGNEHRLGANEAPPAIISIYLGKELDTVINNIINNTDIQAPGSDDMDLGVVGFPPLPKDSTDRNRTSPFAFTGNKFEFRAVGSSQVVNFPCIVLNTIVAESLRFIREEILREMKVSSRQTAFNKIIKDTLIQHVRVVFNGDGYSGDWKELAKSRGLANLPSTPEALTNINSEKNIKLFSESNILSPVELESRQEILFEIYNKSIKIEANSLYDLVSTLVLPACFAHQKNIAESVNSIMPFIQSQKSFSQPNHQYSHLSEVVESVNLLIEANQKLLALIKQTKDFNSEHSLATFLNQSVIPQMNEVRKFSDHLEGIVEDKSWPVPKYSEILFLR", "text": "SIMILARITY: Belongs to the glutamine synthetase family. Type 3 subfamily."}
{"protein": "MMKYFLVLCLVVLGVAAVQAAALEDEKFLNLAESLAMPEESRCKARRYGCTDKAECCSEKCAYPALTCAFNWSCEKVCA", "text": "FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 13 (insecticidal toxin ABC) family. ICK-21 subfamily."}
{"protein": "DLFQFGKMIECANKGSRPSLDYMNYGCYCGK", "text": "FUNCTION: Monomer: The beta chain has no enzymatic activity and is not toxic by itself. FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) that has presynaptic neurotoxicity. Inhibits nerve-evoked twitch contractions but not responses to cholinergic agonists acetylcholine and carbachol and to depolarizing agonist KCl. Causes a fade in tetanic contractions. Displays a triphasic mode of action with depression, enhancement and blockade of neurotransmission. Does not display myotoxic activity such as changes in baseline muscle tension or inhibition of directly stimulated muscle twitches. All subunits are necessary for maximum toxicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily."}
{"protein": "MDSEYYSGDQSDDGGATPVQDERDSGSDGEDDVNEQHSGSDTGSVERHSENETSDREDGLPKGHHVTDSENDEPLNLNASDSESEELHRQKDSDSESEERAEPPASDSENEDVNQHGSDSESEETRKLPGSDSENEELLNGHASDSENEDVGKHPASDSEIEELQKSPASDSETEDALKPQISDSESEEPPRHQASDSENEEPPKPRMSDSESEELPKPQVSDSESEEPPRHQASDSENEELPKPRISDSESEDPPRHQASDSENEELPKPRISDSESEDPPRNQASDSENEELPKPRVSDSESEGPQKGPASDSETEDASRHKQKPESDDDSDRENKGEDTEMQNDSFHSDSHMDRKKFHSSDSEEEEHKKQKMDSDEDEKEGEEEKVAKRKAAVLSDSEDEEKASAKKSRVVSDADDSDSDAVSDKSGKREKTIASDSEEEAGKELSDKKNEEKDLFGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKGETQVKEAEDSDSDDNIKRGKHMDFLSDFEMMLQRKKSMSGKRRRNRDGGTFISDADDVVSAMIVKMNEAAEEDRQLNNQKKPALKKLTLLPAVVMHLKKQDLKETFIDSGVMSAIKEWLSPLPDRSLPALKIREELLKILQELPSVSQETLKHSGIGRAVMYLYKHPKESRSNKDMAGKLINEWSRPIFGLTSNYKGMTREEREQRDLEQMPQRRRMNSTGGQTPRRDLEKVLTGEEKALRPGDPGFCARARVPMPSNKDYVVRPKWNVEMESSRFQATSKKGISRLDKQMRKFTDIRKKSRSAHAVKISIEGNKMPL", "text": "FUNCTION: Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IWS1 family."}
{"protein": "MEKHAEPEKSLGDKEFQEKELHEKPAPAASEDISGDSSVNKEDGPDPINDNYLSGLRLAVVMFALCISNFLVALDTTILATAVPKISSDFNSLQDVGWYTSSYLLTNCAFQLFYGKLYTRFKVKIVFTVAMIIFEIGSLLCGVAPNSPVFIFGRAIAGLGSAGAFSGALIIVIHSVQAEKRAQYSGMIVGMYGLASVAAPLIGGAFTDHVTWRWCFYINLPCGGVAIAGLLFFFHSPPQAAVKETAAGLWAKIAKFDPFGTFFFLCSMICLLLALQMGGSTYPFTDARIIVLLVLFGLLLVAFIVVQFFDKNATIPPRVMKNRSVAFGMIYMFCVGAQFLVLVTFMPIWFQGVRAMSATDSGIRSLPILLSNTFCVVLAGALVSMTGYYIPFMWASVVLTSIGAGLLTTLTVDASTGKWVGYQIIAGIGGGLGYQQGISVAQTVLKGSDMTIGTAVMVFVQLLGGTILVSAANNILVTRLVENLERLAPHINPEIILRAGASGIKTAVSEADYPFVIEAYNIALTKTFQIALIVSCLGAIGAAGVEWKRGSKKGDSDEPAIMAV", "text": "FUNCTION: Efflux pump that might be required for efficient secretion of hypothemycin or other secondary metabolies produced by the hypothemycin gene cluster (PubMed:18567690). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family."}
{"protein": "MKSMLVVTISVWLILAPTSTWAVNTIIYNVGSTTISKYATFLDDLRNEAKDPNLKCYGIPMLPNTNSNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFDTSKCRYHIFNDISGTERQDVETTLCPNSNSRVSKNINYDSRYPTLESKVGVKSRSQVQLGIQILDSDIGKISGVTSFSEKTEAEFLLVAIQISEAARFKYIENQVKTNFNRAFNPNPKVLNLEETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVSGSCQTTYNQNAMFPQLIMSTYYNYMANLGDLFEEF", "text": "FUNCTION: Inhibits protein synthesis in vitro. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily."}
{"protein": "MNARHFLSMMDYTPDELLGLIRRGVELKDLRIRGELFEPLKNRVLGMIFEKSSTRTRLSFEAGMIQLGGQAIFLSHRDTQLGRGEPIADSAKVMSRMLDAVMIRTYAHSNLTEFAANSRVPVINGLSDDLHPCQLLADMQTFLEHRGSIKGKTVAWIGDGNNMCNSYIEAAIQFDFQLRVACPAGYEPNPEFLALAGERVTIVRDPKAAVAGAHLVSTDVWTSMGQEEETARRMALFAPFQVTRASLDLAEKDVLFMHCLPAHRGEEISVDLLDDSRSVAWDQAENRLHAQKALLEFLVAPSHQRA", "text": "FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family."}
{"protein": "MMQKLIAQIEKGKPFFEKLSRNIYLRAIRDGFISAMPVILFSSIFLLIAYVPNIFGFKWDKGMEAILMKPYNYTMGLVAFLVAGTTAKSLTDSFNRKLESTNQINFISTMQAAMCGFLFLASDPAKDGGFLSAFMGTKGLLTAFLSAFVTVIVYNFCVKRNITIKMPKEVPPNISQVFKDLIPFSAVIIILYALDLVIRNSFKSNVAEGILKLFEPLFTAADGWIGVTIIFGAFALFWFVGIHGPSIVEPAIAAITYANIEANFKLLQAGEHADKIITSGTQMFIVTFGGTGATLVVPFMFMWMTKSKRNKAIGRASVVPTFFGVNEPILFGAPLVLNPVFFIPFVLAPIVNVWIFKLFVEVLGMNSFSVNLPWTTPGPLGIIMGTGFGLWSFVLAITLIVVDIIIYYPFLKVYDSEILDEEEGRKESNSDLKEKVAANFDTKKADSILAASGVSDDAAKASNITEQTNVLVLCAGGGTSGLLANALNKAAEEYHVPVKAAAGGYGAHMDIMKEYQLIILAPQVASNYEDIKQDTDRLGIKLAKTQGAEYIKLTRDGQAALDFVQQQFEN", "text": "FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LacEF PTS system is involved in lactose transport, but can also use galactose, isopropyl beta-thio-galactopyranoside and thiomethyl beta-D-galactopyranoside (TMG) as substrates. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MDQSSEKELEKYINNRVQWDSLPSHAKSILDQSHVKYKQYCLKYSIKHQLRWDTNLISSFVTDERLYYQEIVRLSVANLVLYPYHIQDKLVPMLNVTPFKYYLIMMIETMTNSKSYDEIPNFTAVDCIRVLGIGRNQFIDLMNKFRSKGFLFKKKKDVIRGLLPTRSLEKNIEYWWILRYGYPNQDEERQGSLPASELEVLDDLKRSNGINGKQAGIYCRESVISLISKGLVYIDVPIQNQDTISVPPLEGFVMNRVLGDYFENLLYKIFVSIDERTTIQKLSEVLQINVELVKQACSLYCRLGFAKKKNLEPLLPQTPSPSSEGDTHSKWHHSWITYYQENETIIPQPILNNNNNNSNTIDNSNNNNNNNTNITSSSSSNTAINNSSQSSTLENNDNIVEGVVDESFNNGNEEQKRIGFVFDSSITAFLMMGNLGYGLKNHAVTMFERGKLSNEALADFLQELDKIDVEEFVDSEAKLYATNAISLRDTIRHLKNKYRIDDSNSSNSNSSSGGGSGNLQGLDLISCERMNQLDETTRIRVLKKNYSVLISMAPLSIDYCPVISSVPPNFGPAVYEVHSFWFRIYLYSMVGKGPNSILLPKGTRLKRIPTIFKDCEKILVCPIDHDPTTVNLSQLLPSVNETLLSSPVLLSAYTFIKYDTQPKLSKLMSHSRSNSIVSSSKDNQLLYHIPFPLDDLSADNGSPKKYTNIITNNTTTTTTTTTTTNTTNLNNNTIISEDQYNSDNIHTHPILYKIQSTFNLKNSFGYITLLKKETHILLNNNNNNNNKNNINNNKNNNNNNNNNNNNNNNNNNNNNNNNNNNNSITHQKVFEYLPLNVYYGIPIFDDKLNREVCAKIDKFNLLSKENLNRHSMDSRNLSLNLFNFISSTCPPIHPDLDSIDATKINSNLPSVQNIPFPTQIITFVNGNLDL", "text": "SIMILARITY: Belongs to the FAM91 family."}
{"protein": "MHTHNNFKTPSDEDELDDLDEDMVVGVIAEIEQEVLNESDSDNDEYDLVEMGAPVPDNDGDSSYDGNESISSDDSFDPNAADSDSDDSMLDDAGDDASAGGATSSKRRKDDDNPSGSNRQSEATFDLDEDDETDETVRAMIAAIKKPRSAPPEIKLEDFITDICFHPDRDIIALATIIGDVHLYEYDNEANKLLRTIEVHSKACRDVEFTEDGRFLLTCSKDKCVMVTDMETEKLKKLYETAHDDAINTLHVLNENLFATGDDAGTVKLWDLRTKNAIFELKELEDQITQLTTNDQSKLLLATSADGYLTTFNIAARKMYVQSEPYEEELSCMGIYRGDSKLVVGTSKGRLYTYNWGQFGYHCDMYPGIKSPISLMIPITDRIACVAGEDGNIRACHIAPYRNLGVVGQHNMPIESLDVNSNGELIASSSHNNDVRFWNVKYFEDFGDIKYNEKHNAYKEQRHNLPSSKCSNASDFFADLTKEDADDDDAGAGPSNMA", "text": "SIMILARITY: Belongs to the WD repeat WDR55 family."}
{"protein": "MQRLATIAPPQVHEIWALLSQIPDPEIPVLTITDLGMVRNVTQMGEGWVIGFTPTYSGCPATEHLIGAIREAMTTNGFTPVQVVLQLDPAWTTDWMTPDARERLREYGISPPAGHSCHAHLPPEVRCPRCASVHTTLISEFGSTACKALYRCDSCREPFDYFKCI", "text": "FUNCTION: Possible component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit D may have a function related to the maturation of the monooxygenase complex, rather than direct involvement in catalysis. PaaD could assist either in maturation of PaaE or PaaA."}
{"protein": "MWTTTSGLSGRSLRLSITFAAVVGFSLFGYNQGMMAGLLNGDEFVNSFPILKMPDNPTAGEKHYIDVIRGAVTSCYELGCFFGALFSMFCGNRLGRTRLIFMGASILIVGALLTTVCYTGKWEVGQFVIGRVVSGIGNGMNTATIPVWQSECSGAHNRGFLVCFEGAMIAGGTFIAYWVVFGISHAADSVQWRFPVALQIFFALVVATGALMLPDSPSWFVSRGLDNEACEVLGKIKGTSPDSDQVLHDFNLIKTDMESTKSEQSNWKTVFTFGKTQEFQRLLIGCSGQFFQQFTGCNAAIYYSTLLFQENLHMEKYLSLIMGGVFASVYALATIPSFFMIERVGRRKLYLIGFLGQGLSFVITFACLIKETEENSKGAAVGIFLFITFFAFTLLPLPWIYPPEINPLRTRTVGASASTCTNWMCNFAVVMFTPLFAGQSPWGVYLFFALFNFVGLIFGYFFYVETAGRELEEVDIIYAKAHVEGKMPFRVAHDLPKLSFEEIVQQSRELGLDTNDHVMLEKKELGLSSDSAQETEEVYEKQ", "text": "FUNCTION: Major facilitator superfamily transporter that may be involved in A.fumigatus adaptation to azoles such as vorizonazole. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MNLNDRVEGIGNERSIVAKSTERKNKIPPSLKLSPVESVGEKSPTPATVYDLFKKYHKSDSVKPTEEDNMNVGFDKLSTDEKNGFLRKLQMLTVGSKKSSKVDESTPSPANRLLKKIVPSRRTSTEHPNSSNRMHIFGSSRTTKKSIDSERNSQRKKSARRLNFERDAEQKKDSTKTNNSSFVAEMTREYEKIVISKGAPVPINKANRNLYRNPRGSLETPTDSPQKGFSSSTESSPSDSMNQFPSREHFTSANEESPMKRKNFQQEHGNKNRDSDATWFGELPPRDYTSPTFSRKIFVGGVPWDITEAALKDSFGEFGSCAVEWPGQEARYRSGQSNLAPSNGSLRAQTKYTGQAATGYVYMIFEDERAVASLLHECSQEIGGAGEWYFKIRAQRSKSTEIRQVQIIPWVTSDSMFCEDDTLLETGIEPKRTVFVGALHGMMTAQVLHSIMEDCFGAVECVQLDTDKFKYPIGSGRVTFREHGAYFKAIEMGYLHVYTSKFRKRVQIDPFLESTCCMVCNSQSAHCFCRNKNCFKYYCHNCWALDHGKDDDQEVHIPVIVPSSASKAFPGATTRRSQVSSSLSLKNGSNNSQVNNSIPHFPSAGFPIIVGAPAQTLSALYGYIQNGQQLLKPAVFEPPMTPSPSEINKNRRSFTEFSTPPTVFFNSTPVISPQKSVSDGSPLPAYYNSAAFLTPPPTYYGSPNHPTSSNISQPQQPYYGANLYYGFIPPQQHPSAMMRSPNYGQ", "text": "FUNCTION: Cytoplasmic polyadenylation element binding protein that binds to and regulates the translation of specific mRNAs (By similarity). May not be required for oogenesis."}
{"protein": "MMLGPEGGEGYVVKLRGLPWSCSIEDVQNFLSDCTIHDGVAGVHFIYTREGRQSGEAFVELESEDDVKLALKKDRESMGHRYIEVFKSHRTEMDWVLKHSGPNSADSANDGFVRLRGLPFGCTKEEIVQFFSGLEIVPNGITLPVDPEGKITGEAFVQFASQELAEKALGKHKERIGHRYIEVFKSSQEEVRSYSDPPLKFMSVQRPGPYDRPGTARRYIGIVKQAGLDRMRSGAYSAGYGGYEEYSGLSDGYGFTTDLFGRDLSYCLSGMYDHRYGDSEFTVQSTTGHCVHMRGLPYKATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEEAVAAMSKDRANMQHRYIELFLNSTTGASNGAYSSQVMQGMGVSAAQATYSGLESQSVSGCYGAGYSGQNSMGGYD", "text": "FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SUBCELLULAR LOCATION: Nucleus, nucleoplasm."}
{"protein": "MVYSQLQALKRNYYLDWLRNLHKGKPKTFAITFMGVKQICTIEGENLKAIQATNFKDFGLEPMRRKTKGAMPFADKGISTTDGKNWEFARFLVKPFFYREVYASIDRVDPYVRKLFGLLPEEDGVTFDIQPLIQRWFLDLTSEFIFGKTMDSMTYPDRANITWTMLDVLRGGRLRIQMYKFLWAFNWNWWLKAVYEVHDFVNVHIRSTYKELAAREQRIRDGLPVGPERVDLLWYMATHVRDEEELRSQLCLVFVPNNDTTSIFISNCIWHLARDHEAWQKLRKEVLDYGDQPITFESLRSMPYLNGVLNETHRLTPNNIVQVRACLNDSVLPLGGGPDGKSPLYVNKGDLVSVTKTVMYRDPDIWGPDVDVFRPERFFGVRGNWNFLPFGGGPRRCPAQMMVQTESAYMLFQLAKRYSRLECRDPEPYTAVMRIGPSNINGVKIAFYK", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:34947016). IliC catalyzes the ring expansion of the tetramate intermediate to the acyclic 2-pyridone intermediate that contains the trans bis-diene chain (PubMed:34947016). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (PubMed:34947016) (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MEFLLGNPFSTPVGQCLEKATDGSLQSEDWTLNMEICDIINETEEGPKDAIRALKKRLNGNRNYREVMLALTVLETCVKNCGHRFHILVANRDFIDSVLVKIISPKNNPPTIVQDKVLALIQAWADAFRSSPDLTGVVHIYEELKRKGVEFPMADLDALSPIHTPQRSVPEVDPAATMPRSQSQQRTSAGSYSSPPPAPYSAPQAPALSVTGPITANSEQIARLRSELDVVRGNTKVMSEMLTEMVPGQEDSSDLELLQELNRTCRAMQQRIVELISRVSNEEVTEELLHVNDDLNNVFLRYERFERYRSGRSVQNASNGVLNEVTEDNLIDLGPGSPAVVSPMVGNTAPPSSLSSQLAGLDLGTESVSGTLSSLQQCNPRDGFDMFAQTRGNSLAEQRKTVTYEDPQAVGGLASALDNRKQSSEGIPVAQPSVMDDIEVWLRTDLKGDDLEEGVTSEEFDKFLEERAKAAEMVPDLPSPPMEAPAPASNPSGRKKPERSEDALFAL", "text": "FUNCTION: Acts as a MYO6/Myosin VI adapter protein that targets myosin VI to endocytic structures (PubMed:23023224). May also play a role in recruiting clathrin to endosomes (PubMed:16412388). May regulate growth factor-induced mitogenic signaling (PubMed:16479011). SIMILARITY: Belongs to the TOM1 family."}
{"protein": "MEFIQRHIENVKEKKNFAVRLYRHWVDRTIPYTTYRWLTVSGLIALFFIRILLVRGWYIVCYTLAIYLLNLFLAFLTPKFDPSVEQAMKDEEIEEGVLPTSKDDEFRPFIRRLPEFKFWYSSMRATLFALVASFFRIFDVPVFWPILVVYYLVLSFFCFRRQIQHMLKYRYVPFDIGKKKFGSH", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RER1 family."}
{"protein": "MRALLLAFQLLSVVAALTTVNCRLDLSPRQISRKDLLRTHLRLYQVGNFSGQPYSAKATLRDPEGRFRFEDLPVSHDENSTVYFQLVASSQDYNLKPNRVLIEVQGRGEGKEPTVRAFQNVFGREHFPSPEILYPEQLVELEAEPELVISYVHAAPMRNYIVSRRSGILDSGPLAGIFRSKYKMAAVVTIIALLLFPMLVEKFDPATVEAIKEQRLSQTREKYAAVGESNS", "text": "FUNCTION: Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the SOP4 family."}
{"protein": "MGNQQSQPEFVLRAPTEFSEKFVRHLQESTETDTSRYMDMENYIQKRVQDELKQLQLRQKKAIDAIQEEEWKSNAKTIKDSQGSLDSNLLSAEFRSFQEKLEKQSSINDKELKIKLKEVESIRSDLLKCMSEHPDKSLICHPLAEKFAILASKLHNPKVGSV", "text": "FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the MICOS complex subunit Mic19 family."}
{"protein": "DNILYSGETLSPGEFLNNGRYVFIMQEDCNLVLYDVDKPIWATNTGGLDRRCHLSMQSDGNLVVYSPRNNPIWASNTGGENGNYVCVLQKDRNVVIYGTARWATGTNIH", "text": "FUNCTION: D-mannose-binding lectin which binds alpha-D-linked mannose (PubMed:10388566, PubMed:1874921, PubMed:14505313, PubMed:2350177, PubMed:1645507). Displays a high affinity for alpha-(1-6)-mannose oligomers (PubMed:2350177, PubMed:1645507). Able to interact with both terminal and internal alpha-D-mannosyl residues (PubMed:2350177). Displays antiviral activity and therefore may contribute to defense against infections (PubMed:1645507, PubMed:7481093). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MPELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK", "text": "FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:C, however it also acts on thymine glycol:G, 5,6-dihydrouracil:G and 5-hydroxyuracil:G. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Cleaves ssDNA containing an AP site. FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. SIMILARITY: Belongs to the FPG family. SIMILARITY: Belongs to the FPG family."}
{"protein": "MAENGASQETTQVAKHQEVGHKSLLQSDALYQYILETSVYPREPEPMKELREITAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPDDGKILAMDINRENYEIGLPVIQKAGVAHKIDFREGPALPVLDLMVEDKSNHGTYDFIFVDADKDNYINYHKRIIELVKVGGVIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRVS", "text": "FUNCTION: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). Methylates caffeoyl-CoA to feruloyl-CoA, also able to methylate 5-hydroxyferuloyl-CoA (PubMed:26620524). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily."}
{"protein": "MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKGYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGGPEGTVPMPMPMPMPSANTPFSYPLPKGPSDFNGLPMGTYQAFPIIHPPQIPATPPSYESVDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT", "text": "FUNCTION: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (By similarity). Is required for efficient abscission during cytokinesis (By similarity). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (By similarity). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (By similarity). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Midbody Nucleus envelope Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. SIMILARITY: Belongs to the IST1 family."}
{"protein": "MASVSRRLLRRETIPCFSHTVRKLFSTVGSPSFAQRLRDLPKDFPSTNAKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEMKPVSVD", "text": "FUNCTION: Acts as a major beta-cyanoalanine synthase. The cyanoalanine synthesis reaction is more efficient than the cysteine synthase activity. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein. Probably involved in the detoxification of cyanide that arises from ethylene biosynthesis. Maintains a low level of cyanide for proper root hair development. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family."}
{"protein": "MGLPWYRVHTVVLNDPGRLIAVHLMHTALVAGWAGSMALYELAIFDPSDAVLNPMWRQGMFVLPFMARLGVTQSWGGWSITGETAVDPGYWSFEGVAIAHIVLSGLLFLAAVWHWVYWDLELFTDPRTGEPALDLPKMFGIHLFLSGLLCFGFGAFHLSGLWGPGMWVSDPYGLTGHVQPVAPAWGPEGFNPFNPGGIVAHHIAAGVVGIVAGLFHLTVRPPERLYKALRMGNIETVLSSSLAAVFFAAFVVAGTMWYGNAATPVELFGPTRYQWDQGYFRQEIARRVDTAVASGASLEEAWSSIPEKLAFYDYVGNSPAKGGLFRTGQMNKGDGIAQGWLGHAVFKDKNGDVLDVRRLPNFFENFPIVLTDSKGAVRADIPFRRAEAKFSFEETGITASFYGGSLNGQTITDPAQVKKYARKAQLGEAFEFDTETLNSDGVFRTSPRGWFTFGHASFALLFFFGHIWHGSRTLFRDVFAGIEADLGEQIEFGAFQKLGDPTTRKTAA", "text": "FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily."}
{"protein": "MTSALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFSSSQGVEQVVLGLYIVRGDNVAVIGEIDEETDSALDLGNIRAEPLNSVAH", "text": "FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex) (PubMed:28781166). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA (PubMed:10523320). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family."}
{"protein": "MEFRKEEFKKLAGNTLGHLHRILEKKQKNGETIELTEEGQPVVKEEKHQPVVDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVSMVNNNTVYKGNKLVIEQAQFNWDPETVGMIHGSFFWGYIVTQIPGGYICQKFAANRVFGFAIVATSTLNMLIPSAARVHFACVICVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTAFCGSYAGAVVAMPLAGVLVQYSGWSSVFYVYGSFGITWYMFWILVSYESPAQHPTISEEERKYIEESIGESTGFMNPMAKFKAPWRKFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFAISKVGLLSALPHLVMTIIVPIGGQIADFLRTKRIMSTTNVRKMMNCGGFGMEATLLLVVGYSHSRGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGAMTKHKTREEWQYVFLIASLVHYGGVVFYGIFASGEKQPWAEPEETSDEKCGFIHEDELADESEEQTQAHGGYGSYGATQTTSQQNGGWATDWEKKDEFIQDQGKDPYLYGTVAERDLS", "text": "FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake. The vesicular K(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Is necessary for synaptic signaling of visual-evoked responses from photoreceptors (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Cell membrane; Multi-pass membrane protein Synapse, synaptosome. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily."}
{"protein": "MAGTLDLDKGCTVEELLRGCIEAFDDSGKVRDPQLVRMFLMMHPWYIPSSQLAAKLLHIYQQSRKDNSSSLQVKTCHLVRYWISAFPAEFDLNPELAEQIKELKALLDQEGNRRHSSLIDIENVPTYKWKRQVTQRNPVEQKKRKMSLLFDHLEPLELAAHLTYLEYRSFCKILFQDYHSFVTHGCTVDNPVLERFISLFNSVSQWVQLMILSKPTAPQRAGVITHFVHVAEELLHLQNFNTLMAVVGGLSHSSISRLKETHSHVSPETIKLWEGLTELVTATGNYGNYRRRLAACVGFRFPILGVHLKDLVALQLALPDWLDPARTRLNGAKMKQLFSILEELAMVTSLRPPVQANPDLLSLLMVSLDQYQTEDELYQLSLQREPRSKSSPTSPTTCTPPPRPPVLEEWTSAAKPKLDQAIMVEHIEKMVESVFRNFDVDGDGHISQEEFQIIRGNFPYLSAFGDLDQNQDGCISKEEMVSYFLRSSSMLGGRMGFVHNFHESNSLRPVACRHCKALILGIYKQGLKCRACGVNCHKQCKDRLSVECRRRAQSMSLEGSAPSPSPTHTHHRAFSFSLPRPGRRGSRPPEIREEEVQTVEDGVFDIHL", "text": "FUNCTION: Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane; Peripheral membrane protein Synapse, synaptosome Cell projection, ruffle membrane; Peripheral membrane protein Note=Found both in the cytosol and associated with membranes. Enriched at juxtamembrane areas and membrane ruffles. Localizes to the cell bodies and axons of striatal neurons. SIMILARITY: Belongs to the RASGRP family."}
{"protein": "MATSIGVSFSVGDGVPEAEKNAGEPENTYILRPVFQQRFRPSVVKDCIHAVLKEELANAEYSPEEMPQLTKHLSENIKDKLKEMGFDRYKMVVQVVIGEQRGEGVFMASRCFWDADTDNYTHDVFMNDSLFCVVAAFGCFYY", "text": "FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system. Required for proper retrograde ciliary transport. SUBCELLULAR LOCATION: Dynein axonemal particle. SIMILARITY: Belongs to the dynein light chain Tctex-type family."}
{"protein": "MSQKQMKEAFVSNQNGTSVLEITEGLCLPALCILCRGLLIILSQQLCSSLHNSRTRFLVDFAFLIVPLVTTLTIFSSFVLLEYLVAIILGAGLLYEIYCRRTCYARMPFQKICEKFLKVSLESEHIPAISCFRVVNSAFTAVAILAVDFPLFPRRYAKTELYGTGAMDYGVGGFIFGSAMVSPEVRRKYTKGSRFCYLTKSLYSLWPLVFLGVGRLVAIKSVDYQEHLTEYGVHWNFFFTLIAVKLITSLLLLICPLNRSWVVAISIAALYQLALDFTPLKSLILYGTDGSGTRVGLLNANREGIISVLGYVAVHMAGVQTGLYVLKKRSHIKDWIKVACCILLTAIGLFISLYIVQVNVEVASRRMANLAFCIWIVASCLILLSSLLLGDIILSFAKFVIKEAAVPCSWKLIQSPTANKKHLESIVFDAKRKEPTLCLITAMNRNQLLFFLLSNVTTGLVNLSIDTLHSSTPWALCLLNLYMFTNCLIIYVLHLQDKTIKFW", "text": "FUNCTION: Required for the transport of GPI-anchored proteins to the plasma membrane. Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI- anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGW family."}
{"protein": "DLPSGWSSYEGH", "text": "FUNCTION: Inhibits coagulant activity in human plasma, possibly by interfering with one step of hemostasis (modulation of platelet aggregation, or coagulation cascade, for example) (Ref.1). Does not show fibrinogen-clotting activity and does not inhibit ADP-induced platelet aggregation (Ref.1). Also does not show hemorrhagic activity in mice (Ref.1). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family."}
{"protein": "MEPNSPKKIQFAVPLFQSQIAPEAAEQIRKRRPTPASLVILNEHNSPEIDEKRVTNTQESQNASPKQRKQSVYTPPAMKGVKHLKDQNGSAFPEEEESASEREEKWNH", "text": "FUNCTION: May increase cell susceptibility to TNF-induced apoptosis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family."}
{"protein": "MSIVTKSIVNADAEARYLSPGELDRIKSFAASGERRLRIAQILTDNRERIVREAGQQLFQKRPDIVSPGGNAYGEEMTATCLRDLDYYLRLVTYGVVAGDATPIEEIGLVGVKEMYNSLGTPVAAVAEGVRSAKSVATGLLSGDDAAEAGSYFDYVIAALQ", "text": "FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers. SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane; Peripheral membrane protein; Stromal side Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family."}
{"protein": "MNRLMILVFAAVILALASADEDVDIAKRGVPCLCVSDGPRPRGNNLSGIMWMKTGGYGGNGCPKGWHFCGKSRGFFSDCCKR", "text": "FUNCTION: Binds specifically to voltage-gated sodium channels (Nav), thereby delaying their inactivation during signal transduction. Causes death to crabs. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type I subfamily."}
{"protein": "MSVRRPQFSTTERVIKAVPFPPTRRLTLKEVFENGKPKMDLLKNHLVKEGRVEEEVALKIINDGAAILKQEKTMIEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSEMVYDACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLEDIRKLDRFSEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSYPAVCEFLQNNSLLSIIRAHEAQDAGYRMYRKNQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNILNICSDEEMNVTDEEGATTGRKEVIKNKIRAIGKMARVFTVLREESENVLTLKGLTPTGTLPLGVLSGGKQTIETAKQEAAEEREAIRGFTIAHRIRSFEEARGLDRINERMPPRKEASYHHDAGRMHSHSHPPHPQASRRTDHGKKAL", "text": "FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. SUBCELLULAR LOCATION: Mitochondrion Note=Localizes in the mitochondria in a SPATA33-dependent manner. SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily."}
{"protein": "MRGTVSVPKKAEDAKADPPAKKKADTQASSHTLLEGRLGYQLESALLVRALTHRSYAYENGGLPTNERLEFLGDSVLGLVVTDTLYRTHPDLPEGQLAKLRAAVVNSRALAEVGRGLELGSFIRLGRGEEGTGGRDKASILADTLEAVIGAVYLDQGLDAASELVHRLFDPLIEKSSNLGAGLDWKTSLQELTATEGLGVPEYLVTETGPDHEKTFTAAARVGGVSYGTGTGRSKKEAEQQAAESAWRSIRAAADERAKATADAVDADPDEASASA", "text": "FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. May modulate key aspects of gene expression as its absence has extensive effects on the abundance of about 200 different transcripts. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease III family."}
{"protein": "MAEGDNRSTNLLAAETASLEEQLQGWGEVMLMADKVLRWERAWFPPAIMGVVSLVFLIIYYLDPSVLSGVSCFVMFLCLADYLVPILAPRIFGSNKWTTEQQQRFHEICSNLVKTRRRAVGWWKRLFTLKEEKPKMYFMTMIVSLAAVAWVGQQVHNLLLTYLIVTSLLLLPGLNQHGIILKYIGMAKREINKLLKQKEKKNE", "text": "FUNCTION: Positively regulates SLC1A1/EAAC1-mediated glutamate transport by increasing its affinity for glutamate in a PKC activity- dependent manner. Promotes the catalytic efficiency of SLC1A1/EAAC1 probably by reducing its interaction with ARL6IP5, a negative regulator of SLC1A1/EAAC1-mediated glutamate transport (By similarity). Plays a role in the formation and stabilization of endoplasmic reticulum tubules (PubMed:24262037). Negatively regulates apoptosis, possibly by modulating the activity of caspase-9 (CASP9). Inhibits cleavage of CASP9-dependent substrates and downstream markers of apoptosis but not CASP9 itself (PubMed:12754298). May be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation (PubMed:10995579). SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum Note=Predominantly localized to intracytoplasmic membranes. Preferentially localizes at the ER tubules and the edge of the ER sheets, both of which are characterized by a high membrane curvature. SIMILARITY: Belongs to the ARL6ip family."}
{"protein": "MKVFFILIIFSFTLATCQGHCIGSIPLPEMEDGEDVPLRTCVDTHDEKKHLIVSTWKTANSFSCECRQDGMWCCKEYVAVA", "text": "FUNCTION: Shows an slight inhibitory effect toward the metalloproteinase brevilysin H6, but does not inhibit the metalloproteinases thermolysin, HR1A and HR1B. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-microseminoprotein family."}
{"protein": "MDHAAWLNEETGEAAQEAYKYFMRPDPNQREFLGPIEEEDDPLTGMRAKFRMAKVGMVRNAKDEDKKEVKVYLGFNDVTYLPHIRIPNAKPLQGWYQDKHNDKRGSRARPCFSEAILTEPYGGYCTVGCAFCYVNSGFRGYRGTGLISVPVNYGEQVRNMLSKSRTSAAGYFSSFTDPFLPIEDVYHNTQQGAEAFVELGLPIFFLSRLSYPSWAIDLLKRNPYSYAQKSLNTGNDRDWHKLSPGAISLQDHIDEIAELRRQGIYTSIQVNPVVPGIVTHDDIRHLFERLAAVGNNHVIVKFVEAGYSWAPAMIERLHKRFGPERTKAFTDLFTENQAGAQKTIAEPYRVEAHQLYRKWATELGMTYATCYEYRRGKPGTGEPAWLSMGREMITADQCHGQRVPMFTRTDLDQPFQEVKECAPTGCLHCADDNEGKPRCGSELFGAAKALRSPDFKKIVEPTPPEEDGGERKIIPITQID", "text": "FUNCTION: Isomerizes 5-N-alpha-glycinylthymidine (Nalpha-GlyT) into 5- Calpha-glycinylthymidine (Calpha-GlyT) as a step in the pathway leading to thymidine hypermodifications in the viral genome (PubMed:34522950). As a final result of the pathway of hypermodification, 5-aminoethyl-2'- deoxyuridine (5-NedU) substitutes for about 30% of thymidines in the viral DNA (PubMed:34522950, PubMed:29555775). These modifications probably prevent degradation of viral genome by the host restriction- modification antiviral defense system (PubMed:34522950)."}
{"protein": "MATAEVLNIGRKLYEGKTKEVYELLDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFCFAGLVIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVKKNFEWVADRVELLLKSNSQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPITADWGAQDVWSSLRLPSGIGCSTILSPEGSAQFAAQIFGLNNHLVWAKLRASKLNTWISLKQADKKIRECNL", "text": "FUNCTION: Bifunctional phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing two reactions of the de novo purine biosynthetic pathway. SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase family. Class II subfamily. SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase family."}
{"protein": "MQYIKIHALDNVAVALADLAEGTEVSVDNQTVTLRQDVARGHKFALTDIAKGANVIKYGLPIGYALADIAAGVHVHAHNTRTNLSDLDQYRYQPDFQDLPAQAADREVQIYRRANGDVGVRNELWILPTVGCVNGIARQIQNRFLKETNNAEGTDGVFLFSHTYGCSQLGDDHINTRTMLQNMVRHPNAGAVLVIGLGCENNQVAAFRETLGDIDPERVHFMICQQQDDEIEAGIEHLHQLYNVMRNDKREPGKLSELKFGLECGGSDGLSGITANPMLGRFSDYVIANGGTTVLTEVPEMFGAEQLLMDHCRDEATFEKLVTMVNDFKQYFIAHDQPIYENPSPGNKAGGITTLEDKSLGCTQKAGSSVVVDVLRYGERLKTPGLNLLSAPGNDAVATSALAGAGCHMVLFSTGRGTPYGGFVPTVKIATNSELAAKKKHWIDFDAGQLIHGKAMPQLLEEFIDTIVEFANGKQTCNERNDFRELAIFKSGVTL", "text": "FUNCTION: Catalyzes the dehydration of D-altronate. SIMILARITY: Belongs to the UxaA family."}
{"protein": "MTRIIVVTSGKGGVGKTTSSAALATGFAKKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFINVINGEAILNQALIKDKRTEGLFILPASQTRNKNALTKSGIDRVFTQLVNMNFDIIICDSPAGIESGAVLAIYFSDEAIVITNPEVSSVRDSDRILGIIASTSQRSSQNFKPIKEHLLLTRYNPKRVSNGDMLSTEDVLDILRIPLIGVIPEDTSVLKASNQGTPVILNYNSNAGQAYYDTVNRLLGINCPFRFVKDEKKSFLRRLFRR", "text": "FUNCTION: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ParA family. MinD subfamily."}
{"protein": "MTIEYTKNYHHLTRIATFCALLYCNTAFSAELVEYDHTFLMGQNASNIDLSRYSEGNPAIPGVYDVSVYVNDQPIINQSITFVAIEGKKNAQACITLKNLLQFHINSPDINNEKAVLLARDETLGNCLNLTEIIPQASVRYDVNDQRLDIDVPQAWVMKNYQNYVDPSLWENGINAAMLSYNLNGYHSETPGRKNESIYAAFNGGMNLGAWRLRASGNYNWMTDSGSNYDFKNRYVQRDIASLRSQLILGESYTTGETFDSVSIRGIRLYSDSRMLPPTLASFAPIIHGVANTNAKVTITQGGYKIYETTVPPGAFVIDDLSPSGYGSDLIVTIEESDGSKRTFSQPFSSVVQMLRPGVGRWDISGGQVLKDDIQDEPNLFQASYYYGLNNYLTGYTGIQITDNNYTAGLLGLGLNTSVGAFSFDVTHSNVRIPDDKTYQGQSYRVSWNKLFEETSTSLNIAAYRYSTQNYLGLNDALTLIDEVKHPEQDLEPKSMRNYSRMKNQVTVSINQPLKFEKKDYGSFYLSGSWSDYWASGQNRSNYSIGYSNSTSWGSYSVSAQRSWNEDGDTDDSVYLSFTIPIEKLLGTEQRTSGFQSIDTQISSDFKGNNQLNVSSSGYSDNARVSYSVNTGYTMNKASKDLSYVGGYASYESPWGTLAGSISANSDNSRQVSLSTDGGFVLHSGGLTFSNDSFSDSDTLAVVQAPGAQGARINYGNSTIDRWGYGVTSALSPYHENRIALDINDLENDVELKSTSAVAVPRQGSVVFADFETVQGQSAIMNITRSDGKNIPFAADIYDEQGNVIGNVGQGGQAFVRGIEQQGNISIKWLEQSKPVSCLAHYQQSPEAEKIAQSIILNGIRCQIQ", "text": "FUNCTION: Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Probably involved in the export and assembly of fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family."}
{"protein": "MFYYPNVLQRHTGCFATIWLAATRGSRLVKREYLRVNVVKTCEEILNYVLVRVQPPQPGLPRPRFSLYLSAQLQIGVIRVYSQQCQYLVEDIQHILERLHRAQLQIRIDMETELPSLLLPNHLAMMETLEDAPDPFFGMMSVDPRLPSPFDIPQIRHLLEAAIPERVEEIPPEVPTEPREPERIPVTVLPPEAITILEAEPIRMLEIEGERELPEVSRRELDLLIAEEEEAILLEIPRLPPPAPAEVEGIGEALGPEELRLTGWEPGALLMEVTPPEELRLPAPPSPERRPPVPPPPRRRRRRRLLFWDKETQISPEKFQEQLQTRAHCWECPMVQPPERTIRGPAELFRTPTLSGWLPPELLGLWTHCAQPPPKALRRELPEEAAAEEERRKIEVPSEIEVPREALEPSVPLMVSLEISLEAAEEEKSRISLIPPEERWAWPEVEAPEAPALPVVPELPEVPMEMPLVLPPELELLSLEAVHRAVALELQANREPDFSSLVSPLSPRRMAARVFYLLLVLSAQQILHVKQEKPYGRLLIQPGPRFH", "text": "FUNCTION: Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separation in meiosis II (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Chromosome, centromere Note=In meiotic chromosomes, localized along axial elements in prophase from the leptotene to diplotene stages. At later prophase stages, diakinesis and metaphase I, localized along interstitial axes of chromosomes including both centromere and arm regions. No longer detected in arm regions in anaphase I but persists on centromere regions until metaphase II. Localized to centromeres and spindle poles in endopolyploid tumor cells. SIMILARITY: Belongs to the rad21 family."}
{"protein": "MGLEKKSALLEDLIEKCGGCAVVDGGFATQLEIHGAAINDPLWSAVSLIKDPELIKRVHMEYLEAGADVVVTSSYQATIPGFLSRGLSMEESESLLQKSVKLAVEARDRFWDKVSKTSGHSYNRALVAASIGSYGAYLADGSEYSGSYGEDVSLDKLKDFHRRRIQVLVEASPDLLAFETIPNKLEAQACVELLEEENVQIPAWICFTSVDGENAPSGESFQECLETLNKSNNICAVGINCAPPQFMDNLIRKFSKLTQKAIVVYPNSGEVWDGKAKKWLPSQCFGDAEFEMFATKWRDLGAKLIGGCCRTTPSTIKAISRDLKRR", "text": "FUNCTION: Catalyzes methyl transfer from S-methylmethionine to homocysteine. The highest preference is for DL-homocysteine >> DL- cysteine. Has no selenocysteine methyltransferase activity."}
{"protein": "MRSMRALQNALSRAGSHGRRGGWGHPSRGPLLGRGVRYYLGEAAAQGRGTPHSHQPQHSDHDASHSGMLPRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLQDCMSKMQRMVQESSSGGLLDRELFQKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDAKEPTGGKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFHNYDNLRHCARKLDPRREGGEVRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFVKDRWGNIPLDDAVQFNHLEVVKLLQDYHDSYLLSETQAEAAAETLSKENLESMV", "text": "FUNCTION: Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha- ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the glutaminase family."}
{"protein": "ANSVCFTFTDFESGQQDLIFQGDASVGSNKALQLTKVDSKGNPQGGSVGRALYTAPIRLWQSSSLVASFETTFTFSISQGSSTPAAALTFFIASPDTKIPSGSGGRLLGLFGSSNNAGSDNGVVAVEFDTYPNTDIGDPNYRHIGIDVNSIRSKAASKWDWQNGKTATAHISYNSASKRLSVVSSYPNSSPVVVSFDVELNNVGPPDVRVGFSATTGQYTQTNNILAWSFRSSLMGYQAN", "text": "FUNCTION: Binds preferentially to oligosaccharides bearing the sequence Man-alpha-1->2 Man-alpha-1->6 Man-alpha-1->6Man found in early steps of glycoprotein processing in the endoplasmic reticulum. It binds weakly to highly processed oligosaccharide structures. SIMILARITY: Belongs to the leguminous lectin family."}
{"protein": "MAQDIISTISDLVKWIIDTVNKFTKK", "text": "FUNCTION: Lyses erythrocytes and many other mammalian cells. SUBCELLULAR LOCATION: Secreted Host cell membrane Note=In infected cells, it is found in the membrane. SIMILARITY: Belongs to the delta-lysin family."}
{"protein": "MGIIAGIIKVIKSLIEQFTGK", "text": "FUNCTION: Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection. Stimulates the secretion of the chemotactic factor interleukin-8 (IL-8). The ensuing activation process triggers an inflammatory response in the host, thus contributing greatly to virulence. Also possesses hemolytic activity, which may contribute to the development of disease. FUNCTION: Peptide which can recruit, activate and subsequently lyse neutrophils, thus eliminating the main cellular defense against infection. FUNCTION: Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection. SIMILARITY: Belongs to the phenol-soluble modulin alpha peptides family."}
{"protein": "MWYVSTRGVAPRVNFEGALFSGYAPDGGLFMPEELPQLDRGTLCQWSTLSYPGLVKELCALFIGSELLPKDELNDLIDRAFSRFRHREVVHLSRLRNGLNVLELWHGVTYAFKDLSLSCTTQFLQYFLEKREKHVTVVVGTSGDTGSAAIESVQGAKNMDIIVLLPKGHCTKIQELQMTTVLKQNVHVFGVEGNSDELDEPIKTVFADVAFVKKHNLMSLNSINWSRVLVQMAHHFFAYFQCTPSLDTHPLPLVEVVVPTGAAGNLAAGYIAQKIGLPIRLVVAVNRNDIIHRTVQQGDFSLSEAVKSTLASAMDIQVPYNMERVFWLLSGSDSQVTRALMEQFERTQSVNLPKELHSKLSEAVTSVSVSDEAITQTMGRCWDENQYLLCPHSAVAVNYHYQQIDRQQPSTPRCCLAPASAAKFPEAVLAAGLTPETPAEIVALEHKETRCTLMRRGDNWMLMLRDTIEDLSRQWRSHALNTSQ", "text": "FUNCTION: [Isoform 1]: Acts as a catabolic phospho-lyase on both gamma- and beta-phosphorylated substrates. Degrades O-phospho-threonine (PThr) to alpha-ketobutyrate, ammonia and phosphate (By similarity). FUNCTION: [Isoform SOFAT]: Potent inducer of osteoblastic production of IL6. May act to exacerbate inflammation and/or bone turnover under inflammatory conditions. SUBCELLULAR LOCATION: [Isoform SOFAT]: Secreted. Note=Secreted by activated T-cells via a calcineurin-independent pathway. SIMILARITY: Belongs to the threonine synthase family."}
{"protein": "MNLEGKVALVTGASRGIGKAIAELLAERGAKVIGTATSESGAQAISDYLGDNGKGMALNVTNPESIEAVLKAITDEFGGVDILVNNAGITRDNLLMRMKEEEWSDIMETNLTSIFRLSKAVLRGMMKKRQGRIINVGSVVGTMGNAGQANYAAAKAGVIGFTKSMAREVASRGVTVNTVAPGFIETDMTKALNDEQRTATLAQVPAGRLGDPREIASAVAFLASPEAAYITGETLHVNGGMYMI", "text": "FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSFKGFKKGVLRAPQTMRQKFNMGEITQDAVYLDAERRFKEIEMETKKLSEESKKYFNAVNGMLDEQIDFAKAVAEIYKPISGRLSDPSATVPEDNPQGIEASESYQAVVKDLKDTLKPDLELIEKRIVEPAQELLKIIQAIRKMSVKRDHKQLDLDRHKRNLSKYESKKERTVKDEEKMFSAQAEVEIAQQEYDYYNDLLKNELPVLFQMQSDFIKPLFVSFYYMQLNIFYTLYTRMEELKIPYFDLSTDIVEAYTAKKGNIEEQTDAIGITHFKVGHAKSKLEATKRRHAAMNSPPPTGASSIASTGTGGELPAYSPGGYNQPYGDSKYQPPSSPATYQSPVVAATAQSPATYQSPVATGQPPSYLPQTPASAPPPQVGSGLPTCTALYDYTAQAQGDLTFPAGAVIEIIQRTEDANGWWTGKYNGQTGVFPGNYVQL", "text": "FUNCTION: Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level. Plays an important role in virulence. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton."}
{"protein": "MFNMENSAAKGEKAARQLFDLEQDMHDVTKAHEVNANVQSKVQTLTSSLREGASKESFEKQQTLLAGYVALQKVLGRINRKMV", "text": "SIMILARITY: Belongs to the chlamydial CPn_0711/CT_665/TC_0036 family."}
{"protein": "MYYRARHSLPYQKRMENLTWRMMYINNKSIFTNTNNAPKEIFEQSLDPEIDDFDYVAHIKKIGQFNQQKTQQQQDHLQSNLDNHNSIFADNTGFSNNNDRGSSGGGMTSISSLSKKRPAPFSPMIQPEKTTIIPTATNTMSQLSQQLNEFNKFNHPSQTSNFNDVNHHMEISTSHIAPTSSAFEFSLDPLAFEGPNQNFQPEPHHDFNTNSFDSMTSSYERPLFDDFLPRDHHNIQSSSVPTSASSFSTIVPKNTQFSTSASITSPTSTFSNQGNNSSNFHRLNSTVSITATPGNLLRQESMVSLPDYANHLRSMSQTPTMNSSNAPFSHSFNDGGSYFMNNFTGITLPSQPSPQPIHFDNKPKDDHFNTSLSVSQQQPSAKKSKRKSTITKSKKKAASPETTITSTGSTITTKSTNSNSTGKGTATGPAASNTGVSCTNCGTKTTPLWRRNPQGQPLCNACGLFLKLHGVVRPLSLKTDVIKKRQRGNNNGSGNSSGTTNNSNNYNNKSISKKNEIDDGDDLNPTSITNNTGLTNNNNSKSPAKSKKKSNFDNNSNSALNNLDKSKLKINTNEITNISETTSNSSSPVINLNHGGRSSGVFGNTPDYLNGITSPAVSLVKSEIDNPHQLNNSNSNGMLMTMHQSSHQSSLSTTFDHEVESNNEGSNSSGVNTSTANNQDWDWLNMNY", "text": "FUNCTION: Transcriptional regulator of nitrogen utilization required for nitrogen catabolite repression and utilization of isoleucine, tyrosine and tryptophan as nitrogen sources. Controls expression of the MEP2 ammonium permease, the DUR1,2 urea amidolyase, and the transcription factor STP1, which in turn mediates SAP2 expression, a long-known virulence attribute of C.albicans. Influences the filamentation process depending upon the nitrogen sources available. Required for virulence in a mouse systemic infection model. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MHRYKKEASNLIKLATPVLIASVAQTGMGFVDTIMAGGVSAIDMAAVSIAASIWLPSILFGVGLLMALVPVVAQLNGAGRQHKIPFEVHQGLILALLVSVPIIAVLFQTQFIIRFMDVEEAMATKTVGYMHAVIFAVPAYLLFQALRSFTDGMSLTKPAMVIGFIGLLLNIPLNWIFVYGKFGAPELGGVGCGVATAIVYWIMLLLLLFYIVTSKRLAHVKVFETFHKPQPKELIRLFRLGFPVAAALFFEVTLFAVVALLVAPLGSTVVAAHQVALNFSSLVFMFPMSIGAAVSIRVGHKLGEQDTKGAAIAANVGLMTGLATACITALLTVLFREQIALLYTENQVVVALAMQLLLFAAIYQCMDAVQVVAAGSLRGYKDMTAIFHRTFISYWVLGLPTGYILGMTNWLTEQPLGAKGFWLGFIIGLSAAALMLGQRLYWLQKQSDDVQLHLAAK", "text": "FUNCTION: Multidrug efflux pump that functions as a Na(+)/drug antiporter. Confers resistance to norfloxacin, ciprofloxacin, ofloxacin, daunomycin, doxorubicin, streptomycin, kanamycin, ethidium bromide and acriflavine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family."}
{"protein": "MSHRKFSAPRHGHMGFTPKKRSRTYRGRIKAFPKDDASKPIHLTAFLGYKAGMTHIVRDVDKPGSKVNKKEVVEAVSIIETPPMVIAGVTGYIDTPQGPRALTTIWAEHLSEEARRRFYSNWAKSKKKAFTKYAKKWQDEDGKKLIEADFAKLKKYCSSIRVIAHTQMKILRRRQKKAHLVEIQINGGTIEQKVDWAREHLEKQIQVDTVFSQDEMIDTIGVTKGHGFKGVTSRWHTKKLPRKTHKGLRKVACIGAWHPSRVAFTVARAGQKGFHHRTIINNKIYRIGKSALTEEGKNNGSTEFDLTQKTINPMGGFPRYGLVNQDYVMLRGAILGPKKRLITLRKSLITQTKRVAHEKINLKWIDTSSKTGHGRFQTTAEKRAFMGKLKRDFLAEAENKA", "text": "FUNCTION: The L3 protein is a component of the large subunit of cytoplasmic ribosomes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL3 family."}
{"protein": "MAEDGPQKQQLEMPLVLDQDLTQQMRLRVESLKQRGEKKQDGEKLIRPAESVYRLDFIQQQKLQFDHWNVVLDKPGKVTITGTSQNWTPDLTNLMTRQLLDPAAIFWRKEDSDAMDWNEADALEFGERLSDLAKIRKVMYFLITFGEGVEPANLKASVVFNQL", "text": "FUNCTION: May act as a modulator of the olfactory signal-transduction cascade. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the olfactory marker protein family."}
{"protein": "MHSEAREAEARRLLLQETLDAERTFLERNQWGQFATPPSLAGEIMRYTIDLHEETRINFLEPSCGSGSFFSALLRNLGDKKIEHAVGVELDPRFSKAASDLWTGQGLRVIEGDFTSPSLVSGPVASLLVANPPYVRHHHLGIDQKRDLVARCADQLGIKPSGLSGLYLYFVLLSHRLLRADAVSTWLIPSEFMDVNYGTALKEYLATRVQLVRIHQYDAAEVQFDDALVTSSVVVFRNSPPRPGHTAEFSFGGTLSEPKVTHQIPSAALTPEAKWSRYVTGVMPADINLKQTGPKLSDFFKIRRGLATGSNAFFIIPRSEAERLGIKRNFLRPILPSPRKLKGDAITADASGWPDIPEQLALLDCPLPIEDLLLENPALAAYLSTADEKIRGGYLVSKRSPWYKQEQREPAPILLTYMGRGKDDQHPLRFIRNDSDAVATNMYLMLYPTALLQRYLAGDPERIKQVHKALLAITAADLRGGGRVYGGGLHKMEPKELAALPADGIATLDPVLREDISMVSVPPRKRTGRPQMPGPSASEVRAWARANGVCVPDRGRLRPEVWDAWRQAHAGEASPLNIDAGDQVALW", "text": "FUNCTION: A gamma subtype methylase that recognizes the double-stranded sequence 5'-GTCGAC-3', methylates A-5 on both strands, and protects the DNA from cleavage by the SalI endonuclease. SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family."}
{"protein": "MADWVTGKVTKVQNWTDALFSLTVHAPVLPFTAGQFTKLGLEIDGERVQRAYSYVNSPDNPDLEFYLVTVPDGKLSPRLAALKPGDEVQVVSEAAGFFVLDEVPDCETLWMLATGTAIGPYLSILQLGKDLDRFKNLVLVHAARYAADLSYLPLMQELEKRYEGKLRIQTVVSRETAAGSLTGRIPALIESGELESAIGLPMNKETSHVMLCGNPQMVRDTQQLLKETRQMTKHLRRRPGHMTAEHYW", "text": "FUNCTION: Transports electrons between flavodoxin or ferredoxin and NADPH. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family."}
{"protein": "MGTGWRRAFCTTAPRNSDAAAPDLDKQRTGYNLTPSPSPRSCVKLAFLSGGSNPSTPRSTSSPSLRCRTADAQTPTAEQTSTPRSATKSPRLSLAAISNPSSPRSPLKLSLFRNSFKFRSTCGICLNSVKTGQGTAKYTAECSHAFHFPCIADYVRKQGKLVCPVCNSIWKDASLLVPHKNATESPLDDSVSVIQEKRVVVTSSPRAKPRPKQSDYSRFYDDDEPLLSPRFVTIPEADENCGGEEEDDVPQFKGFVVDPNPSFAVKTNEIPVNGRDFGNVQVSLLPEAAVVSVGCGYETRAVALRVKAPPPLTARGGVGRRLLDPSQRAPVDLVVVVDVGGTMNGAKLQMVKRAMRLVISSLGSADRLSIVAVVMTVPKRLLPLKRMTEHGKRSAGAVVDGLLCGQGSNTSEALKKASRVLEDRRERNPVASIVLLTDGQGQLSKVHTNQRSTITNVGSTRFAHIEIPVTEHGFGESGGCSNAPAEEAFAKCIGGLLSVVVQDLRIQIRVGSGSGPCEISAIYLCNGRPTLVSSGSGSVRLGDLYAGEERELLVELRVPSTATRAYQILSVRGLFKDPSTQEVVYGRDQSLRVPQAVRSSSSPRIERLRSLFIATRAVAESRRLVEYGECTSAYHLLTSARALLGQSGTVEAAEYIKVVEAELVEVQWRGQQLMEYQSQHQQQHNQRRRGSERETTTTMTLMDENGEPLTPASAWRAAEKLAKLAMMKKSDLHGFENARF", "text": "FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of root growth. Acts as positive regulator of root gravitropism. Possesses E3 protein ligase activity in vitro."}
{"protein": "MQIITTTFIQKVILGSHQLHEQLSIVEARMIESAIVSMLTESFCENEQTLKYLARLLSPMSYMDVINARRGKKICGYPLCYKSAAENSSDGFFIHSMYCNNYHSKCSLYLMRQLSQTPLHERRGVHLTSYINLEFDDMYSVSLLEELVGSEVPIDTVKSLITSFKDLEFDDTYKNEPLPLDVYFGQLTTDEETCIE", "text": "FUNCTION: Probable RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase that regulates RNA polymerase II transcription. May have functional redundancy with RTR1. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the RPAP2 family."}
{"protein": "MPPEKKRKTEPEDKAEVTQQENDVAESTTEPNNQTVTDSKEEPSVTEAALATTSSSSPPVLSASETAQPDTAATSQSSSTPPTSTSAAESAAAKARERAERFRALQARAKSSSQQNLKKATKESQRLQSDPSQLTALGRRHAIASHKLLKADIEDAGGDFERKRAWDWTVEESERWDKRMKKKEAHRDDTAFRDYNQQAEKSYKRQLRNMGGPDLERYTREKLAAIEKAAAAGTLEIVETEDGEMIAIDKDGTFFSTADSTQFAQHKPDKAAVDRLVADMRKAEEASLKKRRERMANNGDDADVTYINEKNKQFNQKLSRFYNKYTAEIRDSFERGTMV", "text": "FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SYF2 family."}
{"protein": "MASINLIKSLKLYKEKIWSFDFSQGILATGSTDRKIKLVSVKYDDFTLIDVLDETAHKKAIRSVAWRPHTSLLAAGSFDSTVSIWAKEESADRTFEMDLLAIIEGHENEVKGVAWSNDGYYLATCSRDKSVWIWETDESGEEYECISVLQEHSQDVKHVIWHPSEALLASSSYDDTVRIWKDYDDDWECVAVLNGHEGTVWSSDFDKTEGVFRLCSGSDDSTVRVWKYMGDDEDDQQEWVCEAILPDVHKRQVYNVAWGFNGLIASVGADGVLAVYEEVDGEWKVFAKRALCHGVYEINVVKWLELNGKTILATGGDDGIVNFWSLEKAA", "text": "FUNCTION: Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Preferentially localized to the nucleus. SIMILARITY: Belongs to the WD repeat CIA1 family."}
{"protein": "MEARVMTPFTYFSLPMQKQFLANQQAVQGKPYAEFFRSKISVPLSAVEKIQQGPMPLADTLTPSIEDLNRMLAADFISEEAGYALLPGPMAYVQSRKFFPNCTAEMLKWWFMWHPLEAERYTLWFPYAHVENPCVHHERLSDTTLSFEESLYGNTFCASEYVGDRLMHLHIHFRDPCELGFCPDLYRESKIDGSVSALMSLAHEPQVPVSLMAHLFKECPEGLYLTSRYWVGSHPAMQRFPGAERAAQLLEESGLGEVELETLAYEFAVHDMCEFNHLASILPSLHAQFSGAK", "text": "FUNCTION: Hydrolase that specifically degrades the potent antimicrobial compound 2,4-diacetylphloroglucinol (DAPG) to equimolar amounts of mildly toxic monoacetylphloroglucinol (MAPG) and acetate. SIMILARITY: Belongs to the DAPG/phloretin hydrolase family."}
{"protein": "MYGLRTLFSLGLLVGGARLGARVAQVGALGGTCPLGQGLVADGNSQCKQFRTGAAMERGLRYLSQEEAQAVDEELFNEYRFSVDQLMELAGLSCAVAITKAYPVSSFTSNLPTVLVVCGPGNNGGDGLVCARHLKLFKGYEPAIHYPKRPNKTLFENLTTQCQKMDIPFVSEFPSEPEVIDGAYNLVVDAVFGFSFKGAVREPFGNILSTLKRVTVPIASVDIPSGWDVEKGNPEGIQPDMLISLTAPKQSAVHFTGRYHFLGGRFVPKALEKKYSLNLPPYPGTECVQKLP", "text": "FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. SUBCELLULAR LOCATION: Mitochondrion Secreted. SIMILARITY: Belongs to the NnrE/AIBP family."}
{"protein": "MPDRAQVIIRIVPGGGTKTLQQIINQLEYLSRKGKLELQRSARHLDIPVPPDQIRELAQSWVTEAGIYDESQSDDDRQQDLTTHIIVSFPAGTDQTAAYEASREWAAEMFGSGYGGGRYNYLTAYHVDRDHPHLHVVVNRRELLGHGWLKISRRHPQLNYDGLRKKMAEISLRHGIVLDATSRAERGIAERPITYAEHRRLERMQAQKIQFEDTDFDETSPEEDRRDLSQSFDPFRSDPSTGEPDRATRHDKQPLEQHARFQESAGSSIKADARIRVSLESERSAQPSASKIPVIGHFGIETSYVAEASVRKRSGIFGTSRPVTDVAMHTVKRQQRSKRRNDEEAGPSGANRKGLKAAQVDSEANVGEQDTRDDSNKAADPVSASIGTEQPEASPKRPRDRHDGELGGRKRARGNRRDDGRGGT", "text": "FUNCTION: Tumor formation by A.tumefaciens involves the transfer and integration of a defined segment (T-DNA) of Ti plasmid DNA into the plant nuclear genome. The virD operon encodes a site-specific endonuclease that cleaves at a unique site within both 24 bp direct repeats flanking the T-DNA."}
{"protein": "MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDGTQPNGGLSHTGTPKPAGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH", "text": "FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Early endosome Presynapse. SIMILARITY: Belongs to the endophilin family."}
{"protein": "MEGFLTDQQREMMKVATQTADDLPPSQKPHSVLLEHLPKPSGGGKASGASNAVKHRRSHAGRSIRSKKDGGGGKGNWGKLIDTDGDYHIDPNDPNYDSGEEPFELVGATLSDPLDDYKKAAASIINEYFSTGDVDVAAADLIELGSSEYHPYFIKRLVSVAMDRHDKEKEMASVLLSALYADVINPNQIRDGFVLLLESADDFVVDIPDAVNVLALFLARAVVDDILPPAFLPRAAKALPITSKGYQVVQTAEKSYLSAAHHAELVERRWGGQTRTTVEEVKKKIADILNEYVETGETYEACRCVRELGVSFFHHEVVKRALVTALENHAAEAPVLKLLNEAASENLISSSQMVKGFSRLRESLDDLALDIPSARTKFGLIVPKAVSGGWLDASFGYPSGECGRQQNEDEKLKRFKEDIVTIIHEYFNSDDIPELIRSLEDLGAPEYNPIFLKKLITLALDRKNHEKEMASVLLSSLHIEMFTTEDVADGFVMLLESAEDTALDILDASNELALFLARAVIDDVLAPFNLEEISSKLRPNSSGTETVKMARSLIFARHAGERLLRCWGGGSGWAVEDAKDKISNLLEEYESSGLVSEACKCIHELGMPFFNHEVVKKALVMGMEKKKDKMMLDLLQESFSEGLITTNQMTKGFTRVKDGLEDLALDIPNAKEKFNDYVEYGKKNGWVSSSFLTSLTEDANVG", "text": "FUNCTION: Involved in target of rapamycin (TOR)-regulated translation control, especially under energy-deficient conditions (PubMed:29084871). Involved in the regulation of the ethylene-mediated signaling pathway (PubMed:21631530). Involved in salt stress responses (PubMed:21631530). Reduced cotyledons size and early flowering (PubMed:21631530). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the PDCD4 family."}
{"protein": "MSLLAFFLFTILVFSSSCCSATRFQGHRYMQRKTMLDLASKIGINYGRRGNNLPSPYQSINFIKSIKAGHVKLYDADPESLTLLSQTNLYVTITVPNHQITALSSNQTIADEWVRTNILPYYPQTQIRFVLVGNEILSYNSGNVSVNLVPAMRKIVNSLRLHGIHNIKVGTPLAMDSLRSSFPPSNGTFREEITGPVMLPLLKFLNGTNSYFFLNVHPYFRWSRNPMNTSLDFALFQGHSTYTDPQTGLVYRNLLDQMLDSVLFAMTKLGYPHMRLAISETGWPNFGDIDETGANILNAATYNRNLIKKMSASPPIGTPSRPGLPIPTFVFSLFNENQKSGSGTQRHWGILHPDGSPIYDVDFTGQTPLTGFNPLPKPTNNVPYKGQVWCVPVEGANETELEETLRMACAQSNTTCAALAPGRECYEPVSIYWHASYALNSYWAQFRNQSIQCFFNGLAHETTTNPGNDRCKFPSVTL", "text": "FUNCTION: Probable beta-1,3-glucanase that may be involved in the degradation of callose walls around the microspore tetrad during pollen development (Probable). May be required for pollen exine formation (PubMed:21849515). SIMILARITY: Belongs to the glycosyl hydrolase 17 family."}
{"protein": "MTEGVLPGLYLGNFIDAKDLDQLGRNKITHIISIHESPQPLLQDITYLRIPVADTPEVPIKKHFKECINFIHCCRLNGGNCLVHCFAGISRSTTIVTAYVMTVTGLGWRDVLEAIKATRPIANPNPGFRQQLEEFGWASSQKGARHRTSKTSGAQCPPMTSATCLLAARVALLSAALVREATGRTAQRCRLSPRAAAERLLGPPPHVAAGWSPDPKYQICLCFGEEDPGPTQHPKEQLIMADVQVQLRPGSSSCTLSASTERPDGSSTPGNPDGITHLQCSCLHPKRAASSSCTR", "text": "FUNCTION: May dephosphorylate MAPK13, ATF2, ERBB3, PDGFRB and SNX6 (PubMed:22792334). FUNCTION: [Isoform 3]: May play a role in the regulation of oligodendrocyte differentiation. May play a role in the regulation of myelin formation (By similarity). Involved in the regulation of Erk1/2 phosphorylation in Schwann cells; the signaling may be linked to the regulation of myelination (By similarity). SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Lipid-anchor; Cytoplasmic side. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily."}
{"protein": "MSRHSQDERLGLPQPPALLPLLLLLLAVAVPLSQAGVYYATAYWMPTEKTIQVKNVLDRKGDAYGFYNNSVKTTGWGILEIKAGYGSQSLSNEIIMFAAGFLEGYLTAPHMDDHFTNLYPQLIKKRSMLNKVQDFLTKQDQWTRENIKYYKSDPFWRHADYVMAQMDGLFAGATKRAVLEGKKPMTLFQIQFLNAIGDLLDLIPSLSPTKNSSLKFFKRWDMGHCSALIKVLPGFENIFFAHSSWYTYAAMLRIYKHWDFNIVDKDTSSSRLSFSSYPGFLESLDDFYLLSSGLVLLQTTNSVYNKTLLQHVVPQSLLAWQRVRVASMMANNGKQWAEVFSKYNSGTYNNQYMVLDLKKVNLNHSLDEGTLYIVEQIPTYVEYSEQTAVLRRGYWPSYNIPFHEKVYNWSGYPILVKKLGLDYSYDLASRAKIFRRDQGKVTDMESMKYIMRYNNYKQDPYSKGDPCNTVCCREDLNSHSPSPGGCYDTKVADIYLASKYKAYAISGPTVQGGLPVFHWSRFNKTLHEGMPEAYNFDFITMKPIL", "text": "FUNCTION: Exhibits a weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids (By similarity). However, in view of the small size of the putative binding pocket, it has been proposed that it may act rather as an amidase or a peptidase (PubMed:23934913). SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the phospholipase B-like family."}
{"protein": "MKIDIHTHILPKEWPDLEKRFGYGGWVQLQQQGKGEAKMIKDGKLFRVIQQNCWDPEVRIREMNQKGVTVQALSTVPVMFSYWAKPKDTLELCQFLNNDLAATVARYPRRFVGLGTLPMQAPELAVEEMERCVKALGFPGIQIGSHINTWDLNDPELFPIYAAAERLNCSLFVHPWDMQMDGRMAKYWLPWLVGMPSETTMAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTIGRIAHGFNMRPDLCAQDNPSDPRKYLGSFYTDSLVHDPLSLKLLTDVIGKDKVMLGTDYPFPLGEQEPGKLIESMAEFDEETKDKLTAGNALAFLGLERKLFE", "text": "FUNCTION: Converts alpha-amino-beta-carboxymuconate-epsilon- semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. ACMSD family."}
{"protein": "MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSRGGRGGSRRLDCKMIRLAECVSVVPVTVESPPEPGAVAFRLDTAQRSHLLAADAVSSTAWVQTLCRTAFPKGGWALAQTENQPKFSALEMLENSLYSPTWEGSQFWVTSQKTEASERCGLQGSYILRVEAEKLTLLTLGAQSQILEPLLFWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTSQGNDIFQAVEAAIQQQKAQGKVGQAQDILRTDSHDGETEGKTVPPPVPQDPLGSPPALYAEPLDSLRIPPGPSQDSVYSDPLGSTPAGAGEGVHSKKPLYWDLYGHVQQQLLKTKLTDSKEDPIYDEPEGLAPAPPRGLYDLPQEPRDAWWCQARLKEEGYELPYNPATDDYAVPPPRSPKPAPAPKPQGLILPESGTTRGSGSKGFSSDTALYSQVQKSGTSGAWDCGLSKVGNDRAGVKSEGST", "text": "FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DOK family. Type A subfamily."}
{"protein": "MTRHQTHLPFHIVQEGNSIDKPPYSYVALIAMAIDASPDKRMTLNQIYKFIEAKFPYYRDADAKRKQGWQNSIRHNLSLNDCFVKKARDGQSCANDRKGNYWQMVADNAPQFDNGNFKRRRVKRLGIGKMGYANTTETTETGTILQQQLPFFNGLKWPQNIQTMDPFQFFKFQYPNSITDSANTSQINNSSSSSSSFDTSIYTSAFPIPTSHFDTNLVAPSQPPPVVSDVEVVPSDTVKEEVLVDMKPLIPGISSTTFLTSLQMTDPRSIEQQQLLSTASNMYPNAFMPPYTNWSCQPTTTFTGLSFDDPSLYGYGQQFPASS", "text": "FUNCTION: Probable transcription factor (PubMed:14993191, PubMed:20553900). Binds to the DNA sequence motif 5'- [TA]TGTT[TG]T[TG][ATG]TT-3' (PubMed:20553900). Regulates sexual dimorphism in the gonad, promoting male gonadal cell fates in chromosomally (XO) male animals, yet plays a role in gonadogenesis in both sexes; probably acts downstream of terminal regulator of sex determination tra-1, to control early gonadogenesis (PubMed:14993191). Positively modulates expression of homeobox protein egl-5, probably acting indirectly, during early gonadal development (PubMed:20553900). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MDAVNFSILAPRYGSHPMMSAWSGIGTSDMNGGAFNWGGIWSGIKNFGSNVKNWGSRAWNSQTGKLLRQKLNDTKVREKLVEGISTGVHGALDIANQEIAKQIERRLERHEPLEPEVEEETVETKSEAKAPLVVEMPLKRPRDEDLVITADEPPSYEETIKTMAPLVPMTRPHPSMARPVIADRPTTLELKPSDQPPPYSPQSSNMPVTAPVRSRGWQGTLANIVGVGLSNVKRRRCF", "text": "FUNCTION: [Endosome lysis protein]: Structural component of the virion that provides increased stability to the particle shell through its interaction with the core-capsid bridging protein and the hexon-linking protein VIII. Fibers shedding during virus entry into host cell allows the endosome lysis protein to be exposed as a membrane-lytic peptide. Exhibits pH-independent membrane fragmentation activity and probably mediates viral rapid escape from host endosome via organellar membrane lysis. It is not clear if it then remains partially associated with the capsid and involved in the intracellular microtubule-dependent transport of capsid to the nucleus, or if it is lost during endosomal penetration. FUNCTION: [Pre-protein VI]: During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a chaperone to promote the formation of the icosahedral capsid. FUNCTION: [Protease cofactor]: Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio. SUBCELLULAR LOCATION: [Pre-protein VI]: Host nucleus Host cytoplasm Note=Shuttles between host cytoplasm and nucleus. SUBCELLULAR LOCATION: [Endosome lysis protein]: Virion Note=Associates with the base of each peripentonal hexon on the capsid interior. Present in around 360 copies per virion. SIMILARITY: Belongs to the adenoviridae protein VI family."}
{"protein": "MDSKHSMISLKQKLSGLLDVIPKQSEIIYADYPLYGNVGDLFIMKGTEAFFKEHGIRVRKRWNPDNFPIGRKLDPNLIIVCQGGGNFGDLYPYYQGFREKIVQTYPNHKIVILPQSIYFQNKDNLKRTAEIFSKHANLHIMTREKASYATAQAYFTTNHIQLLPDMAHQLFPVIPTQQPSNQKLRFIRTDHEANQALQEHAEAESYDWRTVLSASDRRTIAFLQTLNVLNKKAGNPLPIAYIWEKYSDYIVQKAIRFFSRYESVETSRLHGHILSSLLQKENTVIDNSYGKNANYFHTWMEGVPSTRLIQHASKKENLPAHM", "text": "FUNCTION: May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles. SIMILARITY: Belongs to the polysaccharide pyruvyl transferase family."}
{"protein": "MAGRQQELPTITPYLQETSPERAPSLPPKKKLRKNVQVPDRVPVLPPSPEVVPDSEEEEEEVVYTGFSHPGVQVVQKASGKRYVRRLEPKGVPPPSEENNEEEEPSTSKAVTSVVLNPQAEPLVSAWEKGMDLMIKLMEKYHVEAEEKNGFKFLPEQSNVYRKICQTWLNEEHRGLPLTFTSHKTFVEMMGRFLRAYVESYAGVKNNEWEPTGCAIWLHGCTEQEGVLRCYHGLEMIQKEQLVEMDVASENAQRALKEHPSRAKVVQNRWGRSVVQLKNDDARCCVEDVSCATNVFSAKSCGLFFSEGTKAQTAFLQIEAFMQAEYPKMQNGLKRLLMVMRCDCLYKPTGVPQLGRQMCKATPFALSNVDSLRAEEVTDKVALASIQYPCVLVYQCANPVYRNSRGGQGPNCDFKISAPDLLGALQLVRRLWGENVDGPLPKMLIPEFKWSSRLQYRNVALPASHGDGEKEPF", "text": "FUNCTION: Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP- independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its relese from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP. SUBCELLULAR LOCATION: Host nucleus Note=Accumulates in infected cells. SIMILARITY: Belongs to the adenoviridae E2A DNA-binding protein family."}
{"protein": "MAVEKTNSSSSLAEVIDRILDKGIVIDAWVRVSLVGIELLAIEARIVIASVETYLKYAEAVGLTQSAAVPA", "text": "FUNCTION: Gas vesicles (GV) are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GVs are highly permeable to gas (Ref.7). GvpA forms the protein shell (PubMed:6409075, PubMed:3098234, PubMed:1527496, PubMed:3141741, PubMed:14695294, PubMed:20858439, Ref.5, PubMed:22147705). The ratio of GvpA:GvpC is estimated to be 33:1 and more recently 25:1 (PubMed:3141741, PubMed:8254305). SUBCELLULAR LOCATION: Gas vesicle shell Note=Both the N- and C-termini of the protein (but not interior sequences between Ser-5 and Glu-58) are accessible to proteases; GVs remain intact after trypsin treatment. SIMILARITY: Belongs to the gas vesicle protein type A family."}
{"protein": "MAGHLASDFAFSPPPGGGDGSAGLEPGWVDPRTWLSFQGPPGGPGIGPGSEVLGISPCPPAYEFCGGMAYCGPQVGLGLVPQVGVETLQPEGQAGARVESNSEGTSSEPCADRPNAVKLEKVEPTPEESQDMKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSLKNMCKLRPLLEKWVEEADNNENLQEICKSETLVQARKRKRTSIENRVRWSLETMFLKCPKPSLQQITHIANQLGLEKDVVRVWFCNRRQKGKRSSIEYSQREEYEATGTPFPGGAVSFPLPPGPHFGTPGYGSPHFTTLYSVPFPEGEAFPSVPVTALGSPMHSN", "text": "FUNCTION: Transcription factor that binds to the octamer motif (5'- ATTTGCAT-3') (PubMed:1972777, PubMed:1690859, PubMed:1967980, PubMed:17525163, PubMed:23376973). Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (PubMed:15863505, PubMed:17097055, PubMed:17496161, PubMed:19740739). Critical for early embryogenesis and for embryonic stem cell pluripotency (PubMed:1972777, PubMed:1690859, PubMed:17496161, PubMed:18662995, PubMed:19740739, PubMed:29153991, PubMed:23376973, PubMed:32703285). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Expressed in a diffuse and slightly punctuate pattern (By similarity). Colocalizes with MAPK8 and MAPK9 in the nucleus (PubMed:29153991). SIMILARITY: Belongs to the POU transcription factor family. Class-5 subfamily."}
{"protein": "MASVVPLKEKKLLEVKLGELPSWILMRDFTPSGIAGAFQRGYYRYYNKYVNVKKGSIAGLSMVLAAYVFLNYCRSYKELKHERLRKYH", "text": "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase F chain family."}
{"protein": "MFQNNPLLAQLKKNLHAKTPRVEGIVKSTERGFGFLEVDAQKSYFIPPKNMKNVMHGDKISAVLKIEKDREIAEPEKLIEPFLNRFVGKIEKKDNKLFIFPDYPFLKDFIACRPKKSCVHVFQTGDWAVAKLIQHKLNGNHIFYAELIEEIVKANNPLIPWWVTLSRHNLERKEPKIEKDDLILKNNSHREDLTHLNFITIDNFNTKDIDDALFIEEIHNGNLRLIVAIADPTSYIKSGSKLDITAAKRGFTNYLPGFNVPMLPRSLSEDICSLNPHERRPVLACCITILKDGNICSKINFFLAWIKSKSKLSYDNVSDWIEKKSSWKPETKSIENQILLLHRLCLLRIKWRTSNAVLFQDSLEYRFQFSETGIVEDVVIEKRRIAHKIIEESMIIANISAANFLSKNLGFGIYNTHAGFDPINAENVVSFLNNYNLKFTVKEITTLKGFCNLRRVLNILSDNYINSRIRRYQSFGDFSITPSPHFALGLVEYATWTSPIRKYSDMINHRLLKSIINQDTNITKPSEDIKLKISEQKRRNRIAERDISDWLYTLLLQKKEFKNKKFNAEIIDVSRSGIRAKLLENGANVFIPALFLHPIREELVFNQETGKVFIKGVLYYKISDLITVVLSEIRLQTRSIIARIDH", "text": "FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily."}
{"protein": "MALIAPSPRVLRAREAPAAGALQPPAAACSTVAGGGGAAGRPLGMWSGGGGGGGGKGRRRERGDGMLRAEAYFWDVSKPVEMEEIDSMEKLDDALRWSVENKQPIIIDWMASWCRKCIYLKPRLEKIAGEFPGVRFYFVDVNKVPQTVVKRGNITKMPTIQLWKDGEWAAEVIGGHKAWLVMDEVREMIQKHK", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions. SIMILARITY: Belongs to the thioredoxin family."}
{"protein": "MVAFWTCRNAWFQHLPFAKRGDENAPSGPRRLRPWFLVLALGLAACSEDKSAPQQAAPLPPIPVGVIKITERPTHPQLSFVGRVEATDSVDLIARVDGFLDKRTFTEGQAVKTGDLLFVLQKDALQAALDAAQANLAKAQADADNLKLQTERARSLYKQKTVSQAMLDDRVAAEKQALAVVQQAQASLEQAQINLGYTDIRAPFSGRIGMANFSVGALVGPSSGPLATIVSQDPIYVTFPVSDKTILDLTEGGRTATDRSNVAVSLTLSNGMTYPQTGAIDFTGIKINPNTDTLMVRAQFPNPNNVLIDGQYVQVTAASKHPVEALLVPQKAIMTDQSGNYVLAVGEDNKVIQRQITQGSTFGSNVVVKSGLAVGDQVVVDGLQRIRPGQKVDPQIVDATTPAQKAMSVGN", "text": "FUNCTION: May contribute to resistance to some drugs, such as deoxycholate, sodium dodecyl sulfate and nalidixic acid, in the absence of BepD and BepE. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family."}
{"protein": "MSLTVRVIAPDRTVWDAPAQEVILPSTTGQLGILPGHAPLLSALDTGVLRVRADKEWLAIAVLGGFAEVENNEVTVLVNAAERGDKIDLEEARAAFSQADERLKGVKEDDRQGKFQATQAYRRARARLQAAGGLVSV", "text": "FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family."}
{"protein": "MSQIKDRVEKLIQTNPVMMFSKSFCPYCKKAKATLKELNVEPGICELDEDSEGRAIQDYLKEKTSQNTVPNIFIKGQHVGGCDDLLAAKDNGSLSKMIAAL", "text": "FUNCTION: Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. May play a role in protection against oxidative stress caused by superoxide in vivo by regulating the redox state of the protein sulfhydryl groups. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the glutaredoxin family."}
{"protein": "MAGGAMVQTVGGKTYPGKMTAFVFFTCLVASSGGLIFGYDIGISGGVTSMDSFLSEFFPSVYAQAKASKDTNQYCKFDSQLLTLFTSSLYLAALATSFVAAWVTRVFGRKWSMFCGGVTFLAGSALNGAATDVMMLILGRILLGIGVGFANQSVPLYLSEMAPANLRGMLNIGFQLMTTIGILSANLINYATSSIEGGWGWRIGLGLAGVPALIITLGALVLPDTPNSLIARGYAGDAKRVLVKIRGTDDVHDEYDDMVAASEEAASIEHPWRNILHRKYRPQLTIAILIPCFQQLTGINVIMFYAPVLFLTIGFAGDASLMSAVITGLVNMFATVVSIISVDRLGRRVLFLQGGTQMFISQVVVGTLIALQFGVAGVGEMSRSYAILLVLFICMYVAGFAWSWGPLGWLVPSEVFALEIRSAGQSIAVCVNMMLTFVIGQAFLTMLCHLKFGLFYFFAGWMLVMTTFVALFLPETKGVPIEEMNHVWSRHWFWGSYVTAHDVAGAGAGGGGNRRSHNV", "text": "FUNCTION: Mediates active uptake of hexoses by sugar:proton symport. Can transport glucose, xylose and 3-O-methylglucose (PubMed:12723603). May play a role at the early stage of seed development (Ref.5). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."}
{"protein": "MKKFINQFSASLKNNILVFLAFPFVWTSCARDNPLSSENSNISPNAAARAAVTGTTKANIKLFSFTEVNDTNPLNNLNFTLKNSGKPLVDMVVLFSANINYDAANDKVFVSNNPNVQHLLTNRAKYLKPLQDKGIKVILSILGNHDRSGIANLSTARAKAFAQELKNTCDLYNLDGVFFDDEYSAYQTPPPSGFVTPSNNAAARLAYETKQAMPNKLVTVYVYSRTSSFPTAVDGVNAGSYVDYAIHDYGGSYDLATNYPGLAKSGMVMSSQEFNQGRYATAQALRNIVTKGYGGHMIFAMDPNRSNFTSGQLPALKLIAKELYGDELVYSNTPYSKDW", "text": "FUNCTION: Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins. Does not hydrolyze complex bi- or triantennary glycans. The presence of a core-bound fucose impedes endo F1 hydrolysis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 18 family."}
{"protein": "MKQRRRRNGCSSSNTISLLLLFFLVFFSRTSTSTSCRRRTVKHLSTTSTSSTPLESRITSKVIVISIVSGILTGLVSALVLAFLVRSIVKFMKQTPILKGPVVFSPKITPKSLHAALSNGIQLLGSDLNGKYYKMVLDNGLVVAVKRLGSLEGVGSPESSSSKSVKRRLQKELELLAGLRHRNLMSLRAYVRESDEFSLVYDYMPNGSLEDVMNKVRTKEVELGWEIRLRVAVGIVKGLQYLHFSCETQILHYNLKPTNVMLDSEFEPRLADCGLAKIMPSSHTAVSCYSAPESSQSNRYTDKSDIFSFGMILGVLLTGRDPTHPFCEESASGGSLGQWLKHLQQSGEAREALDKTILGEEVEEDEMLMALRITIICLSDFPADRPSSDELVHMLTQLHSF", "text": "FUNCTION: Involved in the perception of CLV3 and CLV3-like (CLE) peptides, that acts as a extracellular signals regulating meristems maintenance. Modulates root, shoot and flower apical meristems maintenance and floral organ development regulation, probably via CLAVATA (CLV)-like pathways involving at least CLV3 and CLE19. In complex with CLV2, perceives secreted CLV3-like effector proteins from plant-parasitic cyst nematodes as ligand mimics of the plant CLE signaling pathway (PubMed:21265896). This recognition is required for proper feeding structure (syncytium) development and ultimately successful nematode infection (PubMed:21265896). CLE14 perception by CLV2/CRN complex triggers root meristem differentiation (PubMed:20697738, PubMed:28586647). Required for the sensing of the root CLE peptides (e.g. CLE8, CLE9/CLE10, CLE11, CLE13, CLE14, CLE16, CLE17, CLE18, CLE20, CLE21, CLE25, CLE26, CLE40, CLE41/CLE44 and CLE45), which involves also CLV2 and leads to root growth regulation, mostly in the phloem and protophloem (PubMed:28607033). Promotes the accumulation of BAM3, especially at later stages of protophloem development (PubMed:28607033). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=Requires CLV2 for export from the endoplasmic reticulum and localization to the plasma membrane. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MRKFPLFSSSLSFLLLILFKENDIIVVMEKKKLRINMLSSSEKVAGQGVSGAYRELVRLLHRAAKDQLIVTENLPIEADVTHFHTIDFPYYLSTFQKKRSGRKIGYVHFLPATLEGSLKIPFFLKGIVKRYVFSFYNRMEHLVVVNPMFIEDLVAAGIPREKVTYIPNFVNKEKWHPLPQEEVVRLRTDLGLSDNQFIVVGAGQVQKRKGIDDFIRLAEELPQITFIWAGGFSFGGMTDGYEHYKTIMENPPKNLIFPGIVSPERMRELYALADLFLLPSYNELFPMTILEAASCEAPIMLRDLDLYKVILEGNYRATAGREEMKEAILEYQANPAVLKDLKEKAKNISREYSEEHLLQIWLDFYEKQAALGRK", "text": "FUNCTION: Galactosyltransferase involved in the biosynthesis of the bilayer-forming membrane lipid alpha-galactosyl-glucosyldiacylglycerol which is involved in maintaining constant nonbilayer/bilayer conditions (curvature packing stress). Also involved in the beta-lactam resistance. Catalyzes the transfer of a galactosyl residue from UDP-Gal to alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn- glycerol) acceptor to form the corresponding galactosyl-glycosyl-DAG product (3-O-alpha-(D-galactopyranosyl-alpha-(1->2)-D-glucopyranosyl)- 1,2-diacyl-sn-glycerol). It can only use UDP-Gal as sugar donor and alpha-glucosyl-DAG is the preferred sugar acceptor. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily."}
{"protein": "MYPSGGVMLGLLAALQVAVQGTGAMPCQPGFTENEYNVMTADVITEGQVLLKVDFVDCGRGSGLRFESGDPADFRIDADGTVMAARTLQLTDRKGQSLEIKAKDENSQEQWMVHINFTQPKQVPVILFPRHSVLVKGDDSVNRVKRDWVIPPVNVLENSRKQFPEELVKIQSDKDKSNTLRYSVTGPGADQNPTGLFIIDPISGLLSVTKPLDREHIPNFHLRAHAVDINGNQMENPIDIIINVIDMNDNRPEFTHQIWNGTVDEGAKPGTFVMTVTSQDKDDPNTANGMLRYKILSQTPESPSSNMFTINNKTGKIITVAAGLDREKVPQYTLIIQATDMEGNPTYGLSNTATAVIRLLDVNDNAPEFTRETFHGEVPENRVNVIVTNLTVTDKDEPGTPAWNAVYRIISGDPTGRFSIPTDPVTNEGLVTVVKPVDFEMNRSFMLTVVADNEVPLASGIHRTRQSTATVSIRVIDVNESPNFDPNPKQIKLEEGLPQWSMLTTFTAHDPDRYMQQTISYSKLYDPANWLEIDPNNGRISTIAVLDRESPYVKNNLYNATFMASDNGVPRASGTGTLQIYLLDINDNAPRVFPQEAEVCERPEPNAINITAVDGDLNPNAGPYAFELPNRPSDIRRNWTLTRISGDHAQLSLKISYLESGIYELPISITDSGNLPMSNTTYLRIKVCQCDHHGDCVDMERIMAAGLGTGAIIAILICIIILLVLVLMFVMWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTLEPDMIKPVGIRRLDERPMHSEPNYPIRSAAPHPGDIGEFIHEGLKAADTDPTAPPYDSLLVFDYEGSGSTAGSLSSLHSSSSGGDQDYDYLNDWGPRFRKLADMYGGNDD", "text": "FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion (By similarity). Cadherins contribute to the sorting of heterogeneous cell types, and thereby play an important role during embryonic development (PubMed:12091300). Required for normal neural tube morphogenesis (PubMed:12091300, PubMed:21115806). Required to allow mid- and hindbrain neurons to reach and maintain their appropriate positions within the neural tube by restricting neuronal motility within the embryonic mid- and hindbrain (PubMed:12091300). Functions with protocadherin pcdh19 to coordinate cell adhesion and cell movements during neurulation (PubMed:21115806). pcdh19 shows little cell adhesion activity on its own but exhibits robust homophilic cell adhesion when in a complex with cdh2 and appears to mediate the adhesion while cdh2 acts as a cell adhesion cofactor in the complex (PubMed:21115806, PubMed:22184198, PubMed:33004519). Contributes to neural progenitor cell patterning by promoting homophilic cell interactions (PubMed:33004519). Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell membrane, sarcolemma Cell junction Cell surface Cell junction, desmosome Cell junction, adherens junction."}
{"protein": "MVEHYHSTYYYEIAINIPLNKLFFYKFNLNLEIGIRVMVNFNGSNKIGIIIKKYFENEFKEKFEFKIKEIIKIIDTTKIITEHNIDLAHWISKKTFSGFGETLFFGLPQNSKAKKNQTLPSINEHPDHKKCLELNNEQQNIYKEIIGSEKTNVFYLFGIPGSGKTEIFIKLCEYYLALEQQVLFLIPEISLGYQIIKRIKYALNMHHKIYEYNSKVPNSDKNLIWNKVKNGESLVVIGIKSVLMLPFTKLKLIIMDEEHETTYKSENIPRFHSRHISFFLQKKFNAKFVMGSATPSLEAYHAMKNNQIKKIIMQNKFSQSKIEDIKIINMKKEPSTISSELLYSIQKSLNEKRQSLIFINKRGYLKNLECNECGHIICCPNCSFGLIYHKKENKLLCHYCSYKTKTASHCPQCESKDIKYKTYGIQLVEKELKKFLPNAKIARIDSDITKIENIDSINKFENKEIDILIGTQIIAKGFNFENIKTLGIINADIGMGLPDFRSGERIFTTLSQIMGRAARFKDDNIIIIQTKNPNYYAIKYAYKNQYEQFYEEELDIRKKLNYPPFNKIIRIIFRSKNEESAKQKCWEFFEKSKEFLQEEIEHLGPSEAIMKKISKNYRYNIIYLSKSYSLLEKLVNKTKEKVKMTSTVYIEIDYYPISLI", "text": "FUNCTION: Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. SIMILARITY: Belongs to the helicase family. PriA subfamily."}
{"protein": "MANYPQLNKEVQQGEIKVVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEFSLNAFNLYGALSMANSGPNTNGSQFFIVQMKEVPQNMLSQLTDGGWPQPIVDAYGEKGGTPWLDQKHTVFGQIIDGETTLEDIANTKVGPQDKPLHDVVIESIDVEE", "text": "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SIMILARITY: Belongs to the cyclophilin-type PPIase family."}
{"protein": "MGTVLSLSPASSAKGRRPGGLPEEKKKAPPAGDEALGGYGAPPVGKGGKGESRLKRPSVLISALTWKRLVAASAKKKKGSKKVTPKPASTGPDPLVQQRNRENLLRKGRDPPDGGGTAKPLAVPVPTVPAAAATCEPPSGGSAAAQPPGSGGGKPPPPPPPAPQVAPPVPGGSPRRVIVQASTGELLRCLGDFVCRRCYRLKELSPGELVGWFRGVDRSLLLQGWQDQAFITPANLVFVYLLCRESLRGDELASAAELQAAFLTCLYLAYSYMGNEISYPLKPFLVEPDKERFWQRCLRLIQRLSPQMLRLNADPHFFTQVFQDLKNEGEAAASGGGPPSGGAPAASSAARDSCAAGTKHWTMNLDR", "text": "FUNCTION: Activator of CDK5/TPKII. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the cyclin-dependent kinase 5 activator family."}
{"protein": "MLRPGALRLRGLALRGSPRRPSSAGLREGQESPASPPEWKDRAETVIIGGGCVGVSLAYHLAKAGMRDVVLMEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYERLEEETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTNWHATEQYIIEPEKIHELFPLLNMNKILAGLYNPGDGHIDPYSLTMALAAGARKYGALLKYPAPVTSLKPRPDGTWDVETPQGSVRANRIVNAAGFWAREVGKMIGLDHPLIPVQHQYVVTSTIPEVKALKRELPVLRDLEGSYYLRQERDGLLFGPYESQEKMKLQASWVTHGVPPGFGKELFESDLDRISDHLEAAMEMIPVLKKADIINVVNGPITYSPDILPMVGPHQGVRNYWVATGFGYGIIHAGGVGKFLSDWILHGEPPFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYKTLKSKCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVGVIDLSPFGKFNIKGRDSTQLLDHLFANVIPKVGFTNISHMLTPRGRVYAELTVSQQSPGEFLLITGSGSELHDLRWIEEAAFRGGYDVEIQNITDEFGVLGVAGPYARRVLQKLTSEDLSDDAFKFLQTKSFNISDIPVTAIRISYTGELGWELYHRREDSATLYERIMSAGQEEGIGDFGTYALNALRLEKAFRAWGSEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKTEGLKRRLVCLTVATDDVDPEGNESIWYKGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPATIIQEPLVLTEPARARLQKDGKKTNLEKGPSRTTKL", "text": "FUNCTION: Catalyzes the demethylation of N,N-dimethylglycine to sarcosine. Also has activity with sarcosine in vitro. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvT family."}
{"protein": "MNIRNSLILIISTILFFSIINGSLSLDPTCVGAPDGQVYLFSSWDFKGDRYVYNVSQGYLSLSDGFRGNVQSFISGADVCFVKWYPIEQYQITAGESHRNYAALTNFGQRMDAIIPGNCSNIVCSPK", "text": "SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Dictyostelium gerABC family."}
{"protein": "MAAADGVGEAAQGGDPGQPEPPPPPQPHPPPPPPQPPQEEAAAASPIDDGFLSLDSPTYVLYRDRPEWADIDPVPQNDGPNPVVQIIYSEKFQDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYISAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILTQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAILEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTESDPPTNVQQ", "text": "FUNCTION: Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic- aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation. SIMILARITY: Belongs to the protein prenyltransferase subunit alpha family."}
{"protein": "MRLFRQLSIQWKITILSFGIVAFALMMVSISLLGYVTSIKEDELSNRTMITAQLVAQNHTVQQWVDAKPEEASRTLQPIVERIRVINDHDYIVLLNMDRIRITHPIPERLQTPFVGGDEDPAFAEHIYLSKAKTEGVVTVRAFMPILNQQREQVGVAVVGSVLPSYADMIQEFWQPALLIGLITALFGFWGSWLLASHIKRQTFNMEPDELAHLLVERDASFNAIHEGVVAINKHEKITIMNEAARRMLGVKEKAIGRNIHEVIPDTKLPEILSIGKPLYQREFYIQGRLVFSNRIPIQIDGETVGAIAIFQDKSDVDRLAEELTGVQAFVDALRVQNHEYSNKLHTIAGLIQLDEGKKALQYIFDLEEEQEEFSGVVMQKIHNDSLAGLLLGKVSRGKELGVQVIIEKDSEFIDHPEGVTTHDLVVIVGNLIDNSLDAFSSTQDQNKTVHVFIGEENDFLKIRVRDNGEGIREEVREKMFVRGFSTKSTSGRGIGLFLIQAIVERVEGKIEVESELNIGTTFSIYLPKKRG", "text": "FUNCTION: Member of the two-component regulatory system DctS/DctR. Probably activates DctR by phosphorylation. Essential for expression of dctP (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein."}
{"protein": "MSSIQGKGTAGPSPEGIPNSREDGEMNPEGVTISGQTVSFTSVSKSASADDIQQVALPIIQSDSLASSPILGGAIGEIEVADMVAEVVENNEANVQQLDEDLEAIFQAIDAGEEQLESLEVKNKSSLKGVRYSSGRHGMDRNKSSSLSPERTRLANIRTSLRSTASRMRHHAGLVSSSLADLQKQLRSISQEDLKAALGKDSEAVLSRLRKLGLDVNKKGEWRLRTNGDIGRLNQSIHDLSLLVENVNDEGILSLNKEASEEEVNACCSSGSKACQFLQEHLMSALRAIYQQILRFLNWISRKIGVGSKRTDDYYTRPGVFTNPYASYLGANPPINDPRSLRERLRGGGALSGEDTLFSMPQDDSVDSESVSDDDRGSR", "text": "SIMILARITY: Belongs to the chlamydial CPn_0499/CT_392/TC_0671 family."}
{"protein": "METLVSSIFWTLAPWKNMLLLKHGRIEILDQNTMYGWYELPKQEFLSSKQPVQIFTTKKYWILFRIGPERRRKAGMPTGVYYIEFTR", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf15 family."}
{"protein": "MATNQEAGRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAQHPWNIMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPDDGKILAMDINKENYELGLPVIQKAGVAHKIDFKEGPALPVLDQMIEDGKYHGSFDFIFVDADKDNYLNYHKRLIDLVKVGGIIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRLS", "text": "FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5- hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily."}
{"protein": "MSTSDSIVSSQTKQSSWRKSDTTWTLGLFGTAIGAGVLFFPIRAGFGGLIPILLMLVLAYPIAFYCHRALARLCLSGSNPSGNITETVEEHFGKTGGVVITFLYFFAICPLLWIYGVTITNTFMTFWENQLGFAPLNRGFVALFLLLLMAFVIWFGKDLMVKVMSYLVWPFIASLVLISLSLIPYWNSAVIDQVDLGSLSLTGHDGILITVWLGISIMVFSFNFSPIVSSFVVSKREEYEKDFGRDFTERKCSQIISRASMLMVAVVMFFAFSCLFTLSPANMAEAKAQNIPVLSYLANHFASMTGTKTTFAITLEYAASIIALVAIFKSFFGHYLGTLEGLNGLILKFGYKGDKTKVSLGKLNTLSMIFIMGSTWVVAYANPNILDLIEAMGAPIIASLLCLLPMYAIRKAPSLAKYRGRLDNVFVTVIGLLTILNIVYKLF", "text": "FUNCTION: Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family. SdaC/TdcC subfamily."}
{"protein": "MAERRGSSGANGVLNSLNPQRFTSQIPSIGGNTNKKGVPGTNAALTDMINKSLARNGRSSLSRPVPEVRKSLRRSLRSSQRPSIVPGGGPSAYGALQSTRDPRPLRDKNYQAVLQQEIFDYLQSRKFDIETGHAISLKSLKQPTQKDFICIFRWLYRRLDPGYSFKRSLETEVYSILKTIQYPFLDTINKSQISAVGGSNWHKFLGMLHWLMNTSQRLDSCLHKLDESKTMQLTQDITILNQPVTTLDEQDEKHEQYELMVERLFIEYISKCYKSFINMEDDFSPFKEELEIGFDRFVHIIETDINNLGRQEEMLQQDCEMFAARCEGLKLARSKHQALKGDLVKFQNYINAMKNKAEDWPRKLNQMVEEINEKKGLIKDIHAEIDKLRQALSQEDIQEIDQMNQQRDTFSKMLDTVSSKLDNLTGSVKSQKLNLESSSKVFLDTLEKFNASINGFVLARNNLQHPINPAELLIPVKANITLTDSTAITPSTILEGCTDILSSIKPNLLKVNKEIDERISALQTENNQLEKELRGLRDTITSKGHMLESMENELSNIKSEYDEYQQVSHSKLLSQRIEIEKLERKIQNDRHKTQQRVAQAEQEIEDAAFKLKELTLKIQQERVVLHRKLIKVIEYVVSFKMDVQGSIEALHDFSVEQLESL", "text": "FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Note=Associated with kinetochores. SIMILARITY: Belongs to the NDC80/HEC1 family."}
{"protein": "MNKQLTNNGFRLTQRGLQIGKYMYRTYQNVKRIQKGGPDSFKAAEDFVKDTSEIGVIAVKMSQFLSARSDIVDERTLKVIERLQSEVPPEKESPPDFTFYEWYKEPIASASIATVYKGKRKTDNSDVILKRVRPEVKQRIMEDLPLFIIVLDIAKFFGVPGAENMLEIVRECQPVLLGELNLKLEAKAMSLFKKKFASIPWLTIPTVYEAGETYMISEYVPSKKITAAYPNEMLARRLFELYIYMTIDIGLVHADPHAGNIGIKKDGTFVLYDFGAIIDVRNAKQYIAKCLKSVVIGDTDGVVRSLEDMGVIKSGGSVARLKKAIPKIKKIMESEDFNVELSKLPEFTSNENRIFELTTRYIYLIRSLTIVEGIISYHDRDFSLTKYIKKYNDIIDDIVEVPAIDIVKEIAGDFLTTPASLKNMNDLVFSMKDEISTEIADAKKIARYGFAMFLLIEIIKML", "text": "SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein kinase family."}
{"protein": "VGTRVVRIEDQQLITQGGTYVEDL", "text": "FUNCTION: Active with aldehydes and formate esters as substrates."}
{"protein": "MAGVSPAVFGCPDVTLGRNTAVREVQENVTSVDSLTLVSSNTDFAFSLYRKLVLKNPDENVVFSPFSICTALALLSLGAKSNTLKEILEGLKFNLTETPEPDIHQGFRYLLDLLSQPGNQVQISTGSALFIEKHLQILAEFKEKARALYQAEAFTADFQQPLKATKLINDYVSNHTQGKIKELISGLKESTLMVLVNYIYFKGKWKNPFDPNDTFKSEFYLDEKRSVIVSMMKTGYLTTPYFRDEELSCTVVELKYTGNASAMFILPDQGRMQQVEASLQPETLRKWKNSLKPRMIHELRLPKFSISTDYSLEHILPELGIREVFSTQADLSAITGTKDLRVSQVVHKAVLDVAETGTEAAAATGMAGVGCCAVFDFLEIFFNRPFLMIISDTKAHIALFMAKVTNPERSMNFPNGEGASSQRLESKRLCFGDPLCLIGQ", "text": "FUNCTION: Serine and cysteine protease inhibitor. Can inhibit lysosomal papain-like proteases including the cathepsins B, G, H, K, L and V. Ineffective against elastase, granzyme A, granzyme B, or caspases 3, 8 or 9. Inhibition of cytoplasmic cathepsin B following release from the lysosome may protect cells from apoptosis. This may facilitate the survival of progenitor T-cells and the subsequent development of long term memory CD8 T-cells. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the serpin family."}
{"protein": "MFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLTMAMRDSGTVLDWKSLHLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHTGGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLTDMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGKLAKDDAEARAKLQAVLDNGKAAEVFGRMVAAQKGPTDFVENYAKYLPTAMLTKAVYADTEGFVSEMDTRALGMAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLAVIHAKDENNWQEAAKAVKAAIKLADKAPESTPTVYRRISE", "text": "FUNCTION: The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. FUNCTION: The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family."}
{"protein": "MALPLPSGLTPSEVAFLCEMELVTVVPRQRLESIELLTGTTPALRPPHRSNLPLWLAILLKKQRRANIVPPPWLHPDSLRDIVHQETMVDRKGWAPPPPPPARADSRGNARNPFMDDETVLSPPFLPSCTSDAPAGALPYHWFEVAEMLLAHASDDISSSSEVRSLLRDLQEVRAAKMRSSTAQLEGGVDGVMSLRGVGAMELAESRGFVIGVVEGVRKLGASTETTRREEEEEGGGQESDEQSDEDMGL", "text": "FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GINS2/PSF2 family."}
{"protein": "MLKRKKVKPITLRDVTIIDDGKLRKAITAASLGNAMEWFDFGVYGFVAYALGKVFFPGADPSVQMVAALATFSVPFLIRPLGGLFFGMLGDKYGRQKILAITIVIMSISTFCIGLIPSYDTIGIWAPILLLICKMAQGFSVGGEYTGASIFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTIVGEANFLDWGWRIPFFIALPLGIIGLYLRHALEETPAFQQHVDKLEQGDREGLQDGPKVSFKEIATKYWRSLLTCIGLVIATNVTYYMLLTYMPSYLSHNLHYSEDHGVLIIIAIMIGMLFVQPVMGLLSDRFGRRPFVLLGSVALFVLAIPAFILINSNVIGLIFAGLLMLAVILNCFTGVMASTLPAMFPTHIRYSALAAAFNISVLVAGLTPTLAAWLVESSQNLMMPAYYLMVVAVVGLITGVTMKETANRPLKGATPAASDIQEAKEILVEHYDNIEQKIDDIDHEIADLQAKRTRLVQQHPRIDE", "text": "FUNCTION: Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response (By similarity). FUNCTION: Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Metabolite:H+ Symporter (MHS) family (TC 2.A.1.6) family."}
{"protein": "MELVLVFLCSLLAPMVLASTAEKEKEMDPFHYDYQTLRIGGLVFAVVLFSVGILLILSRRCKCSFNQKPRAPGDEEAQVENLITANATEPQKAEN", "text": "SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the FXYD family."}
{"protein": "MDPEYSELFERLNKQLDNVEDVLKPLKDAESIFELAEGKSELEQAKLYITMSYAINSTLYSFYKLNGIDASERPVMQELQRVKNYISKIQQAEKNVNPKTEAVNTSNAAISSSSSNRPKVAKDAATRIIKHHT", "text": "FUNCTION: Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the C1D family."}
{"protein": "MDLLQFLAFLFVLLLSGMGATGTLRTSLDPSLEIYKKMFEVKRREQLLALKNLAQLNDIHQQYKILDVMLKGLFKVLEDSRTVLTAADVLPDGPFPQDEKLKDAFSHVVENTAFFGDVVLRFPRIVHYYFDHNSNWNLLIRWGISFCNQTGVFNQGPHSPILSLMAQELGISEKDSNFQNPFKIDRTEFIPSTDPFQKALREEEKRRKKEEKRKEIRKGPRISRSQSEL", "text": "FUNCTION: In the nucleus, enhances stability of the PCAF histone acetyltransferase (HAT) complex member TADA2A and thus promotes PCAF- mediated H3K14 and H4K8 HAT activity. May inhibit TADA2A-mediated TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and transcriptional activity. May also promote TADA2A-mediated XRCC6 acetylation thus facilitating cell apoptosis in response to DNA damage. FUNCTION: In extracellular secreted form, promotes proliferation and activation of CD8(+) T cells, suggesting a cytokine-like function (PubMed:25125657). Enhances cytotoxic anti-tumor activity of CD8(+) T cells (PubMed:25125657). May inhibit ERK and JNK signaling activity (PubMed:18087676, PubMed:23070808). May suppress cell migration and invasion activity, via its effects on ERK and JNK signaling (PubMed:23070808). Has a critical role in the regulation of osteogenesis and bone development (PubMed:32181939). SUBCELLULAR LOCATION: Nucleus Cytoplasm Secreted Endoplasmic reticulum Note=Accumulates in the nucleus in response to UV irradiation (PubMed:22644376). SIMILARITY: Belongs to the CCDC134 family."}
{"protein": "MGSVNSRGHKAQVVMLGLDCAGKTTILYKLKGNRLVDTLPTVGFNVEPLEAPGHVSLTLWDIGGQTQLRATWKDYLEGIDLLVYVLDSTDEARLPEAVAELEEVLEDPNMAGVPFLVLANKQEAPDALPLLEIRNRLDLERFQDHCWELRACSALTGQGLQEARQSLLHLLRS", "text": "FUNCTION: May play a role in apoptosis. May act as a tumor suppressor (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Arf family."}
{"protein": "MEIQSGPQPGSPGRAERLNARLLDEFVSLHGPTLRASGVPERLWGRLLHKLEHEVFDAGEMFGIMQVEEVEEAEDEAAREAQRKQPNPGGELCYKVIVTSESGVRADDPNSIFLIDHAWTCRVEHARKQLQQVPGLLHRMANLMGIEFHGEVPSPEVVALVLEEMWKFNQTYQLAHGTAEEKVPVWYIMDEFGSRIQHSDMPSFATAPFFYMPQQVAYTLLWPLRDLDTGEEVTRDFAYGEADPLIRKCMLLPWAPADMLDLSFSTPEPPAKYYQAILEENKEKLPLAISPVARPQGHVFRVHCDVQQVLGHLTHPRFTFTDSEADADIFFHFSHFKDYMKLSQESPQVLLNQFPCENLLTVKDCLASIARRAGGPEGPPWLPRTFNLRTELPQFVSYFQHRERRGEDNHWICKPWNLARSLDTHVTNNLHSIIRHRESTPKVVSKYIESPVLFLREDVGNVKFDIRYIVLLRSVRPLRLFAYDVFWLRFSNRPFALDDLDDYEKHFTVMNYDPDVVLKQVHYNEFIPQFEKQYPEFPWSDVQAEIFKAFTELFQVACAKPPPMGLCDYPSSRAMYAIDLMLNWDNHPDGKRVMQPQILEVNFNPDCERACRYHPSFFNDVFSTLFLDETDNCHVTRII", "text": "FUNCTION: Negatively regulates post-translational modifications of tubulin, including detyrosination of the C-terminus and polyglutamylation of glutamate residues. Also, indirectly promotes histone H4 trimethylation at 'Lys-20' (H4K20me3). Probably by controlling tubulin and/or histone H4 post-translational modifications, plays a role in mitosis and in maintaining chromosome number stability. During RNA virus-mediated infection, acts as a negative regulator of the RIG-I pathway by preventing MAVS binding to TBK1 and IKBKE. SUBCELLULAR LOCATION: Cytoplasm Midbody Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Nucleus Note=Predominantly localizes in the cytoplasm. SIMILARITY: Belongs to the tubulin--tyrosine ligase family."}
{"protein": "MSNKKGQSPKEESIAKMLICKVHIGTKNLENKMKRYVYTRAKDGVHIINLAKTYEKLQLAARIIVAISNPADVVVVSARPFGSRAVLKFAQYTGAQAIAGRWTPGMLTNQIIQKFTEPRLLIVTDPRTDAQSVKESAYANIPVIALCDSDSPLEHVDIAIPCNNKGKESIALMYWLLAQEVLYLKGVIPRSEPWNVMVDMFLWRDPEQFELKNLANEENTPTAPHLIENQYAAEAPYDEWTKKEEWNDNTNEDWKNPIAAEEW", "text": "FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (Probable). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (Probable). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (Probable). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS2 family."}
{"protein": "MEHHQIYRHKKFDMGRKIEKCDLQLKEELISRSGTPCTSRSPFDAANQSVSLGFSDQDADFPPLPKRRRLGSSSSSVSYQSASPIITEAIQDIFKYHVNMVRKFPKKERSPKDQERRNKNTIACRMSRRKKKFDDLQIEQQYKECSDEHLKIAEQSLRARVYLNHLKQLVKQEDHPLVSSRRVPEENTKSNFSIDYLIGGIKQEHA", "text": "FUNCTION: Plays a role in inducing apoptosis and is involved in the repair of head patterning defects in the embryo caused by extra maternal copies of the homeotic gene bicoid."}
{"protein": "MSITKNDKNTRTTGRPTLNEVARRAGVSPITASRALRGVASVAEELAQKVRDAARELGYVANPAARALASAQSHSVAVLVPSLANLLFIETLEAIHAVLRPQGLEVLIGNFHYSRNEEEDLIRNYLAYQPRGLLLTGFERTESARRMIEASGIPCVYMMDLDSGSGLNCVGFSQLRAGEAAAEHLLARGRRRLAYIGAQLDQRTLLRGEGFRRALQKAGCYDPGLEILTPRPSSVALGGELFVQLLASQPQVDGVFFCNDDLAQGALLEALRRGVKVPEQIAVLGFNDLPGSDCTVPRLSSIRTPREAIGRRAAEQLLALIAGKEVRDSALDMGFELMAREST", "text": "FUNCTION: Involved in the regulation of glucose metabolism. Represses its own expression as well as that of the gluconate permease GntP (PubMed:28752954). It employs an effector mediated de-repression mechanism: in the absence of ligand, GntR binds to the gntR and gntP promoters and represses their expression. The release of promoter bound GntR is induced by gluconate and 6-phosphogluconate that bind with similar apparent affinities to the GntR/DNA complex. The release of GntR leads to transcription of the genes (PubMed:28752954)."}
{"protein": "MSEAQETHVEQLPESVVDAPVEEQHQEPPQAPDAPQEPQVPQESAPQESAPQEPPAPQEQNDVPPPSNAPIYEGEESHSVQDYQEAHQHHQPPEPQPYYPPPPPGEHMHGRPPMHHRQEGELSNTRLFVRPFPLDVQESELNEIFGPFGPMKEVKILNGFAFVEFEEAESAAKAIEEVHGKSFANQPLEVVYSKLPAKRYRITMKNLPEGCSWQDLKDLARENSLETTFSSVNTRDFDGTGALEFPSEEILVEALERLNNIEFRGSVITVERDDNPPPIRRSNRGGFRGRGGFRGGFRGGFRGGFSRGGFGGPRGGFGGPRGGYGGYSRGGYGGYSRGGYGGSRGGYDSPRGGYDSPRGGYSRGGYGGPRNDYGPPRGSYGGSRGGYDGPRGDYGPPRDAYRTRDAPRERSPTR", "text": "FUNCTION: Involved in mRNA processing and export (PubMed:1429834, PubMed:8675010, PubMed:15542855, PubMed:19061647). Required for efficient splicing of a large set of pre-mRNAs by efficient co- transcriptional recruitment of the splicing machinery (PubMed:19061647, PubMed:23209445). Remains associated with the mRNP during early steps of translation elongation (PubMed:15542855). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, Stress granule Note=Nuclear at steady state and its import is mediated by the karyopherin MTR10 (PubMed:14676199, PubMed:15542855). Export is dependent on active transcription and the export of mRNAs in general (PubMed:8675010, PubMed:14676199). SIMILARITY: Belongs to the RRM GAR family."}
{"protein": "MDSRLLVIAAPLLVAASWALFNIGRLAIQQIQRLSA", "text": "FUNCTION: Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbY family."}
{"protein": "MFDFNGTLPLMMFQFFLLVAVLNAVFFKPLTQAIDERDGFIRTNNTEARERLAKAKSLTEQYEQELAGTRKQSQQVLADAQAEAQKIAQTQITEAQKQVQAEVMKAQAELESQKQSAFSELEKQVDTLSQQILNKLLGSTLA", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MASSSYTSLLVLVALVTAASAQLSPTFYDTSCPRALATIKSGVMAAVTSDPRMGASLLRLHFHDCFVQGCDASVLLSGMEQNAIPNAGSLRGFGVIDSIKTQIEAICKQTVSCADILTVAARDSVVALGGPSWTVPLGRRDSIDANENEANTDLPGFNSSRAELEAAFLKKGGLNTVDMVALSGAHTIGQAQCSTFRARIYGGDTNINAAYAASLRANCPQTVGSGDGSLANLDTTTANTFDNAYYTNLMSQKGLLHSDQVLFNNDTTDNTVRNFASNPAAFSSSFTTAMIKMGNIAPKTGTQGQIRLSCSRVNS", "text": "FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. FUNCTION: Involved in defense response to powdery meldew fungus. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily."}
{"protein": "MRKIWELKKKEAQKEKNASGISPAQIRIQKDVTDLEIPSTMSTSWPDPIKLNVLHLEIRPDEGYYKGGKFKFRIQIDDNYPHDPPKVKCLNKIYHPNIDIEGNVCLNILRQDWNPVLNLNSILVGLQFLFLSPNAEDPLNKEAAADLHKDPQGFASRVRTAMKGGLVNGISFDNVMA", "text": "FUNCTION: Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3- ULA1 E1 complex and catalyzes its covalent attachment to other proteins. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBC12 subfamily."}
{"protein": "MKWKLFYFFTLLTFTPAYFFIEQNQWVILASFLVIVNLISLTVHWKFGLLLISCSAALLAYCQLMPEFQLAKLMKANWLRTPFISWLDQHTSGVFNQYLKLFLINETTKNTLYQSAIQLNIVHLFVISGFHLSFLFGVMERWLYKRFYINKITGFVMLLLYLFLVGFAFSALRVFVSKLLRQMFPKQLPENNLGLTALLIILMSPGALHNFGFNFSFLACFVLFAINKVKLWKPLQAVLTSTLILIVVSPITLHLNRKLNALSVFHNLLFTPIALFYFCASWLLLPLIPWMGNSLVGFYWPLPWLSQWALNTTVFLNLPKPNWVFYLVYYGLWGLLYTVGTVFYYDRSLWCRYWVNSPAVKPTAQPSRL", "text": "SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To B.subtilis ComEC."}
{"protein": "MLTKNLLLCFAAAKAVLAVPHDSVVERSDALHKLSERSTPSSTGENNGYYYSFWTDGGGDVTYTNGNAGSYSVEWSNVGNFVGGKGWNPGSAKDITYSGTFTPSGNGYLSVYGWTTDPLIEYYIVESYGDYNPGSGGTYKGTVTSDGSVYDIYTATRTNAPSIQGTATFTQYWSVRQNKRVGGTVTTSNHFNAWAKLGMNLGTHNYQILATEGYQSSGSSSITIQ", "text": "FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family."}
{"protein": "MPCQDTVSLSIQHTSVYVQHSCCVSTSTSASTSATALGLGCLACGIVGVLVVAGGLCCLINGRCPSCRRLALRSRSWKSPPASLCTNQPLAFNLRDLTRSDIRCTSDPRSVELLSDVHSVVSHRERPPAYDSLDFEPTEYTPEAFQ", "text": "SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the aquareoviridae NS5 protein family."}
{"protein": "ILKKDNYSYISFYNALIHEGYKDLAALLHSGIPVISSSNGGKDSVGGITS", "text": "FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase 9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity)."}
{"protein": "MPKAAASLASLLPQLWHRPVQPPPFLHRALSSSSPLLRRHRAALHSPAAPLSAAAVSTSAATVEAPATAAYPVYGRLLPCPLQDDPPRIEHLVAREDEVAVDFISRSLTLPPLYVADLIKFGAVYYALVAPQPPPHAAPEHVRIFREVTEPSVLCRRKSIKGKTVREAQKTFRVTDPNQRLEAGTYLRVHVHPKRFPRCYEIDWKSRVIAVTDNYVVLDKPAATSVGGATDNIEESCVVFTSRALGLETPLMTTHQIDNCSEGCVVLSKTKEFCSVFHGMIREKQVNKRYLALTTAPVSTGIITHYMRPINRAPRLVSEDHIKGWHVCQMEILDCKKVPWPSSLIRKVHKVDNCGWPQQEAAYECKINLLTGKTHQIRAQLAAIGTPIVGDSAYMTAAMAAIVNPSINPFGRWGQNYDSEDEKAAAVEAWISCHGKEPKSVIGLQASEISWDYEGEHHSYKAGVPWWRQDAVESDLI", "text": "SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the pseudouridine synthase RluA family."}
{"protein": "MVDSDPVEFPPENRRGQLFGKYEVGKLVGCGAFAKVYHGRSTATGQSVAIKVVSKQRLQKGGLNGNIQREIAIMHRLRHPSIVRLFEVLATKSKIFFVMEFAKGGELFAKVSKGRFCEDLSRRYFQQLISAVGYCHSRGIFHRDLKPENLLLDEKLDLKISDFGLSALTDQIRPDGLLHTLCGTPAYVAPEVLAKKGYDGAKIDIWSCGIILFVLNAGYLPFNDHNLMVMYRKIYKGEFRIPKWTSPDLRRLLTRLLDTNPQTRITIEEIIHDPWFKQGYDDRMSKFHLEDSDMKLPADETDSEMGARRMNAFDIISGSPGFNLSGLFGDARKYDRVERFVSAWTAERVVERLEEIVSAENLTVAKKETWGMKIEGQKGNFAMVVEINQLTDELVMIEVRKRQRAAASGRDLWTDTLRPFFVELVHESDQTDPEPTQVHTTS", "text": "FUNCTION: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Targeted to the tonoplast when interacting with CBL2 or CBL3 and to the cell membrane when interacting with CBL8. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily."}
{"protein": "MGGRMRALQFHGGHKAQIIDTPRPEAPPGWAVVKVHYCCLCGSDLWLYRGKWHGNRYPIVPGHEWAGVVDSAPEGYESWVGRPVTGDLIVGCQGCGPCRDGLPVMCENLIEIGFTVDGGCAGYVAVPITNLYLLPEGMDLAAASQTEPLAVALHAVDRINLRPAERVAVLGAGGIGQLILQSARATGATVTLATDLVAERRKIAEESGAAAAVHPSELPELTSYADKVDVVFEASGDPESVVRALDLVRPGGRVCLVGYQVGAEHALETARLPLSYASLVGVMGPGGKYREAVDLLANGAIDTQPILTDIVTLDDYAPAIDRAINRTDGTVRVVFDLRNE", "text": "FUNCTION: Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. DOIA dehydrogenase subfamily."}
{"protein": "MSHQTGIKANAELLKFFGKCKDGKTRVLKVSIENEELRLVSHSDVKRDWEKDYDTLVRPLIEESTPCYILYRLDYKIPTGYAWLLMSWVPESATVRQKMLYASTKATLKLEFGSGHIKEELNATSKEETTLQGYQKHKVDFNTPAPLTSREEELAELRKTEVKTDFGIDTKQQTLGGINCPIADAVAQALHDMRRGGYNYLQFRIDLEEEKIHLVKADNIELTGLPAQIPTDHARYHLYIFKHHHEGNYLESVVFVYSMPGYSCSIRERMMYSSCKGPFSATIEKHGIQVAKKLEIDNGAELTEEFLHEELHPRKLNLRPQFSKPKGPPSRGAKRLTKPQAVE", "text": "FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cell cortex. SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin subfamily."}
{"protein": "MTVDSKPQLQRLAADVDVDLMCRLLEEDGAFILKDLLPLDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVATTCPTFRNNILINPVIHAICEGYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHHQPLEAPPISLSVIFPLTEFTEENGATEVILGSHRWMEVGTPERDQAVLATMDPGDVLVVRQRVVHAGGGNRTTTGDPRRVVLAYFNSCQLTPFETYRTMPRETVESMTVLGQRMLGWRTMKPSDPNIVGINIIDDKRLENVLQLKATDLPA", "text": "FUNCTION: Verruculogen synthase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:23109474). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmPS/ftmA (By similarity). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (By similarity). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6- hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (By similarity). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (By similarity). FtmPT2/FtmH catalyzes the prenylation of 12,13- dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (By similarity). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (By similarity). Finally, verruculogen is further converted to fumitremorgin A by the verruculogen prenyltransferase ftmPT3 (PubMed:23109474). SIMILARITY: Belongs to the PhyH family."}
{"protein": "MAGSATIVAGLLLLVACACCIFPIDSVTIPSSCCTSFISKKIPENRVVSYQLANGSICPKAGVIFITKKGHKICTDPKLLWVQRHIQKLDAKKNQPSKGAKAVRTKFAVQRRRGNSTEV", "text": "FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils (PubMed:15647285). Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line. Binds to CCR3 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family."}
{"protein": "MELVVEPLNLHLNAETGSTLLDVLRSNEVPISYSCMSGRCGTCRCRVIAGHLRDNGPETGRPQAGKGTYVLACQAVLTEDCTIEIPESDEIVVHPARIVKGTVTAIDEATHDIRRLRIKLAKPLEFSPGQYATVQFTPECVRPYSMAGLPSDAEMEFQIRAVPGGHVSNYVFNELSVGASVRISGPLGTAYLRRTHTGPMLCVGGGTGLAPVLSIVRGALESGMSNPIHLYFGVRSEQDIYDEERLHALAARFPNLKVNVVVATGPAGPGRRSGLVTDLIGRDLPNLAGWRAYLCGAPAMVEALNLLVARLGIVPGHIHADAFYPSGV", "text": "FUNCTION: Component of two multicomponent enzyme systems which are involved in the catabolism of naphthalene (PubMed:9573207, PubMed:11872705). Plays a role as an electron transfer component for both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase (NDO) systems, by transferring electrons from NAD(P)H to the oxygenase component via the ferredoxin NagAb (PubMed:9573207, PubMed:11872705). The electron transport chain from the two systems can use both NADH and NADPH as electron donors at approximately similar rates (PubMed:11872705). SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family."}
{"protein": "MDSNASLPLNVSGGTQATPAGLVVLDVFSYLILVVTFVLGVLGNGLVIWVTGFRMTHTVTTISYLNLALADFSFTSTLPFFIVTKALGGHWPFGWFLCKFVFTIVDINLFGSVFLIALIALDRCICVLHPVWAQNHRNVSLAKKVIVGPWICALLLTLPVIIRVTTLSHPRAPGKMACTFDWSPWTEDPAEKLKVAISMFMVRGIIRFIIGFSTPMSIVAVCYGLIATKIHRQGLIKSSRPLRVLSFVVASFLLCWSPYQIAALIATVRIRELLLGMGKDLRIVLDVTSFVAFFNSCLNPMLYVFMGQDFRERLIHSLPASLERALSEDSAQTSDTGTNSTSAPAEAELQAI", "text": "FUNCTION: High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors. Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing ROS release (By similarity). Receptor for cathepsin CTSG, leading to increased phagocyte chemotaxis (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Internalizes in presence of its ligand, TAFA4. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."}
{"protein": "AGCKNFFWKTFTSC", "text": "FUNCTION: Somatostatin inhibits the release of somatotropin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatostatin family."}
{"protein": "MREKYLLHCPGCGRLFPDNYTLDCPLGCNALLRTVYAEHRLTLRDLPGIFRYSSWLPIEGHLRIDAGPVSYASEGLARELGLSNLTVTFSGYWPERGGRMETCSFKELEAQPTVLRLGEKGAGVLQISSAGNTGRAFCQVSALTGAPVVVVVPASAADRLWTTVPAPNVCLITVEGDYSDSIAFGREVCSLPGIVPEGGAKNVARRDGMGTVMLDAALFAGRLPDAYFQAIGSGTGGIAAWEAAERLVADGRFGSRLPTLHLSQNLPFVPMVRAWEAGRREIVPEVDMPDAEASIVRVSADVLTNRHPPWEVRGGVYDALAASGGRMYAVANDDTRSAGRLFEATEEIDLDPAAAVAVASLIRAAEEGFIGPDDHILLNVTGGGYARAAEDLDRYPVEPYLRVRAGEAFAGDVRDAVRGWLAEQEVVVRA", "text": "FUNCTION: Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate. SIMILARITY: Belongs to the threonine synthase family. Cysteate synthase subfamily."}
{"protein": "MATATVLEKANIGVFTNTKHDLWVADAKPTLEEVKNGQGLQPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGQVVAVAPDVTSLKPGDRVAVEPNIICNACEPCLTGRYNGCENVQFLSTPPVDGLLRRYVNHPAIWCHKIGDMSYEDGALLEPLSVSLAGIERSGLRLGDPCLVTGAGPIGLITLLSARAAGASPIVITDIDEGRLEFAKSLVPDVRTYKVQIGLSAEQNAEGIINVFNDGQGSGPGALRPRIAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMTVPFMRLSTWEIDLQYQYRYCNTWPRAIRLVRNGVIDLKKLVTHRFLLEDAIKAFETAANPKTGAIKVQIMSSEDDVKAASAGQKI", "text": "FUNCTION: Catalyzes the NAD-dependent oxidation of L-arabinitol to L- xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active with NADP as cosubstrate. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family."}
{"protein": "MAEWHKIIEDISKNNKFEDAAIVDYKTTKNVLAAIPNRTFAKINPGEVIPLITNHNILKPLIGQKFCIVYTNSLMDENTYAMELLTGYAPVSPIVIARTHTALIFLMGKPTTSRRDVYRTCRDHATRVRATGN", "text": "FUNCTION: More likely to influence phosphoinositide metabolism than actin assembly. SIMILARITY: Belongs to the profilin family."}
{"protein": "MESISQLQPPMGVNFLNIAPTYIPNTKVECHYTTPFGMKRSTRDWIGIFKVDTSSIRDYETFVWAVPPESSGERSVSHCSVQFQAYYLPRPGEQQYHFRYVDQYGSVRGCSDAFVFGEPRPMEELVTLEDEDSCMDMLLVVPKATFLQNQLEMAQQERNDLMRARLALEEEVILKEKRINHLEATLETSEKSCFSLKEQCQDLVMREQLAIEEQSLLSCQEAELRERILQLQGEIKIMNKKMQEKDRELEGTVAIKLSLENKKVVLKQHLAETTVEIKRYQLQVDSLREKLRSTQDMLSASQQKALLMGEELAAISSIRDRTISDLHKSRLETADLAIKVSDLSVKYKEGMGQWWQEKTALNHSMEAKRDQIVNLKAEKLSLENSLQAERSQRQALQCKLNQETDARQVQLSENRRQLSELKSALKVAQMEKQQLREERQGILQYARSLEERLDKLADELWKEDKMLMEEITDLNPPTLPVDHSDSDDESPGDERVSQQLEACSLDEQDLTINLPGFPCELYKVVINQPAPIACQLQPLPEDNSDSW", "text": "FUNCTION: May function as a coactivator for aryl hydrocarbon and nuclear receptors. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Detected in the cytoplasm at stages I- II. Detected in the nucleus and the cytoplasm, except for the germ plasm, of almost all cells in cleaving embryos (By similarity). SIMILARITY: Belongs to the CALCOCO family."}
{"protein": "MFVSIPSIRKTVMSLCAVPLMAACAFAPGMRFDPQRPLDPADNASVPKITQITPDLVRGGQAQVPRENVDVDQLLAKATPYRIGTGDILSIVVWDHPELVFPTQTYSIGSAYDIANFAGTPNVPGYVVSTGGDIQFPYAGVIKVAGRTQNEVRDEITRAIARVVKDPQVTVRVLAYRSQRIYVDGEVKTPGQQSIDDVPMTLVEALNRAGGINVTTGDNSRIRVTRGGKQWVLSMPALMHQGIDPASVLLRGGDIVRVEPREDSKVFVTGEVVRPSTVLPRNGKLTLSEALGEAGGVSPVSSDPRNVYVIRRAAEGEPQVYHLDAKSPVALALAEGFELRPKDVVYVDAGGLVRWSRVINLLVPTATPLIGAAAVAK", "text": "FUNCTION: Probably involved in polymerization and/or export of exopolysaccharide EPS I which functions as a virulence factor. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BexD/CtrA/VexA family."}
{"protein": "MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR", "text": "FUNCTION: Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self- renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (By similarity). Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex (PubMed:27720643, PubMed:28541300). SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha (By similarity). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). FUNCTION: Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self- renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (By similarity). Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (By similarity). Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha (PubMed:12810571). FUNCTION: Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self- renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (PubMed:27749823). Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (By similarity). Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha (By similarity). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the PHF5 family."}
{"protein": "MMNRAYSLRNSRAPTASQLLNPPPPSSSTRSGRLFAPLSHTMRINHAATFTPDLAKRLAVLVKMEKNVMRSMEVTIRGRRDCARQLSYWGEDCDDDISDVTDKLGVLFYEMAELENYLIDRYDQYRMTLKSIRNIESSVQPSREKKQKLLDQIYALKHKDPESPRLVTMEQELVREEAACLVAEAQLSNTTREKFKQAMTFNLDALHEHAEKLNLIATYGRHLLNLIDDTPVTPGEARPAYDGYETSRQIVMDAEHALSSWVPSQPAVNFVKPQIEDDAQSDARSWNEYEAQGEPVPVEQVTHLQDDVQSDTSEIIENEPGMHPHVHAERMSRIASESSDAVPQQTAVQVA", "text": "FUNCTION: Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase ksg1/ppk21 activity and regulating their downstream CWI pathways pck2-MAP kinase pathway and protein kinase gad8 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress (By similarity)."}
{"protein": "MCWRPLCRLWSYLVYVQAVPCQIFQDDTKTLIKTIVTRINDISHTSVSAKQRVTGLDFIPGLHPILSLSKMDQTLAVYQQVLTSLPSQNVLQIANDLENLRDLLHLLAFSKSCSLPQTSGLQKPESLDGVLEASLYSTEVVALSRLQGSLQDILQQLDISPEC", "text": "FUNCTION: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the leptin family."}
{"protein": "MATRGGPMVAGTDGNDFEFRQRVAGTYQISLLNKSRLKYCIFFHALLFFVMLAKLTSDILDHLDIFVLEIEELEVPPPLWWEYVWAASLLTSFLGLSAARGNKVREMQKYMVAILLFAILPLFYCFAYYFSDVWEFATLDKSVELDETDIFVWRGYPYGVFWYAFCFVGFQVHGFTLYFAYNLVKAWKARTATRKFQ", "text": "FUNCTION: Required for endoplasmic reticulum organization and proper vesicular traffic during vitellogenesis. Required for oocyte and bristle growth. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the jagunal family."}
{"protein": "MGDIARQAPDKDTGEDIYQYLLERITNLENRNLELREQFRQMESEKRYVETQKIRYERELRKLKSEIEQLRSPPLVIGTVTDVIDNSRVIVRSSAGPRFLVRTSQLIDPDLLKPGVRCTLNQQSLAIVDVLPTSYDAQIYGMELVESPEETYENIGGLEPQIEEIREAVELPLTKPQLFEKVGISPPKGVLLYGPPGTGKTLLARAVAHQTNAHFLRVVGSELVQKYIGEGARLVRELFDLAKQRAPSIIFIDEIDAIGAHRNDSTTSGDREVQRTLMQLLAEMDGFDNRGDVKIVAATNRIDILDRALLRPGRFDRMIEIPLPDHQGRLAILKIHTQYMNIGEDVNLSEVSRLTEGKNGADLRAICMEAGMFAIRMERDAVNSEDFMKAIDKLALDFDRHHFHTTFGEMFA", "text": "FUNCTION: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AAA ATPase family."}
{"protein": "MDRNPSPPSSDDESAPEGDCIGDTIYSKHWFFSTLTRLIEAVSEDKSQEGQEDEAPGDLDEELEDEICKVWDMSMNEEVALFLQGFNAPEILLGVIAKSKCSRLTEMCVGILGNMSCFLEPCMAISTHQSLGEVLLLLLSDADPPTLLETSRLFLTCLSQADVAGTWVERFRKDPSVRENLCFIMSSSTNVDLLVKVGELLDRLFDMDEDLMLAWIRSDCAPRETSAVTENEDRAAPLEMVSCLLEAAKQLRSESPEGLEIYMHVLQLLTTADTGIQAIVQSPDGGEQTWDFLLDLTCNDLCQPNDPPLIVQEQKGILSSVLAVMSAMFVWRAEQGHKVEKSLPLISSLAQVLENLEECRKKCPESDAREGPDARHDNSHLQILKDVSCEFLSNILSELSKDSVLQGISLGHITERRCQCALRNLLPLYSTSVGTFLAAVGEADRSLADTLRRETPVRAEQT", "text": "FUNCTION: Plays a role in promoting cell proliferation in response to pro-inflammatory stimuli. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SAAL1 family."}
{"protein": "MDVNILTMFVTVSALALACSLWIASYLRNWRKKGVYPPVVGTMLNHAINFERLHDYHTDQAQRYKTFRVVYPTCSYVFTTDPVNVEHILKTNFANYDKGTFNYDIMKDLLGDGIFNVDGDKWRQQRKLASSEFASKVLKDFSSGVFCNNAAKLANILAQAAKLNLSVEMQDLFMRSSLDSICKVVFGIDINSLSSSKAESGPEASFAKAFDVANAMVFHRHMVGSFWKVQRFFNVGSEAILRDNIKMVDDFLYKVIHFRRQEMFSAEKENVRPDILSRYIIISDKETDGKVSDKYLRDVILNFMVAARDTTAIALSWFIYMLCKHQHVQEKLLEEIISSTSVHEDQYSTECNDIASFAQSLTDEALGKMHYLHASLSETLRLYPALPVDGKYVVNEDTLPDGFKVKKGDSVNFLPYAMGRMSYLWGDDAKEFKPERWIQDGIFHPKSPFKFPAFQAGPRTCLGKDFAYLQMKIVAAVLVRFFKFEAVKTKEVRYRTMLTLHMNEDGLNVQVTPRLNSD", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MADKITDEYAVGIDPEIYANNPAYSSLFNPYIHKQTIIADHVSVQCHIDLNGIDAVGSKFGNLNAHAGNFTSLCAPNCLPERFALVAYTVEYAFLHDDETDNAADQEALLLENKMLHQALNQSGMTSVSTRVSDKAQRKSEVQAKIAAEYLRLDPVFGEWFLNKWQTFTACVKDVRSLEFPSLDDYLEFRIVDAAADWTLYNFRWGSGITLTPEEEKLADPMSYVAYAELCLVNDLFSWDKEYASHIKSNGDVPLVNAVHIVAVTQGLTHCAAKAVVQAEVRAHEERFCQLKEQYEATDKPSHEVLRWLRLLEHSMAGNWVWSLCVPRYCKVDRNPYKDHLEKYGSDAVRVLTPLDRLCWSKQEIKEMKRNQLKEPSSSTYKTHFSPLEPNPGPEQTRLTISQTQQQRPVLNPYTYINSLPSKNVRQTLIAALNSWYKVPVKSLLIIEGAVNFLHNSSLLLDDIQDGSVLRRGRPVAHQIFGVGQTINTATYLMNEALYLIQMLSPSAVSAYTDEMRNLQLGQGRDLYWSYHTHVPTPAQYISMVDGKTGGLFRLISRLMRSEATKNSDLDISQFATLLGRHFQIRDDYQNLQSEDVTNPHIVSLYAPRANMLLQYTKNKGFCDDLDEGKVSFPVILSMQSPGFSNTALSSVFKGSRKGETLSLEMKQYMLEEITARGAFSETKAVLRKLHTELLSLLMETEKKAGGVENWALRLLIMKLDIVEEKKVAPPKSDSHWGVNQRRAWKGGQKNGRPIDKACFLRAMEEALQK", "text": "FUNCTION: Bifunctional terpene synthase converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into a cyclopiane-type diterpene (PubMed:30179018). The C-terminal prenyltransferase (PT) domain of PcCS catalyzes formation of geranylgeranyl pyrophosphate (GGPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GGPP to the cyclopiane-type diterpene (PubMed:30179018). SIMILARITY: In the N-terminal section; belongs to the terpene synthase family. SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase family."}
{"protein": "MVCARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGKCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPSSSEQSLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCGGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEETEEEEEEEDQDYSFPISSTLEW", "text": "FUNCTION: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH). SUBCELLULAR LOCATION: Secreted."}
{"protein": "MLSTKFTLRSHKSSVTYIYQDPRTPFNLFTADSSGLIINWDLTIRRPKKSWQAHTDTILTISTIHNHLLTHSRDNTIKIWDESYSCILEIPCNALNFSNICVINDLLITPASINSNNLDVYKIDKDWQITRLIFDFDVYKLVNKGEIIEEIGSSGTSRNDFGIIMQMKIIHTNTTTTTSENNSDYIIYVGFESGDIVGLQLILPRARILSTTGNTNDKTLINQSAKFILQYHNSTHVPNPVICLSNLDSVLVSGSTTNKVIIHSDPIEIMKMDHSGIQAIVNFKNDRLIFGYWNGYIQYGDISINQSLPKLGNTEQEKSKLTKKLTFMTILNESNQETLQSPTGKSKYSVLLKSKRNLVSPLLLAGYEDGSILAYNI", "text": "FUNCTION: Component of the ASTRA complex involved in chromatin remodeling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat ASA1 family."}
{"protein": "MAAETLLSSLLGLLLLGLLLPATLTGGVGSLNLEELSEMRYGIEILPLPVMGGQSQASDVVIVSSKYKQRYECRLPAGAIHFQREREEETPAYQGPGIPELLSPMKDAPCLLKTKDWWTYEFCYGRHIQQYHMEDSEIKGEVLYLGYYQSAFDWDDETAKASKQHRLKRYHSQTYGNGSKCDLNGRPREAEVRFLCDEGAGISGDYIDRVDEPLSCSYVLTIRTPRLCPHPLLRPPPSAAPQAILCHPALQPEEYMAYVQRQADSKQYGDRAIEGRQDPDPPVWSETKPGVVPPKKAGASPAKENSKESDFWKMLHEPEEQPPEKEETQAEEQEPNLEATDPPPTSPDDFQNNVQVKVIRSPADLIRLIEELKGGTRKGKPNTGQEQPGDSATEVPSREPEMKEKGDPEQQNEVEEEEDDEDEDEDEDERQLLGEFEKELEGILLPSDRERLRAEVKAGMERELENIIQETEKELDPDGLKKESERDRAILALTSTLNKLIKRLEEKQSPELMKKHRKRRVVPKKPPPSPQSTEEDPEHRVRVRVTKLRHGGPNQDLTVLEMKRENPQLKQIEGLVKDLLEREGLTAEGKIEIKIVRPGTEGTEEDARWLTDEDTKNLKEIFFNILVQGAEEAQKERQRQKELESNYRRVWGSPGGEGTGDLDEFDF", "text": "FUNCTION: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the OS-9 family."}
{"protein": "MHHVNKYFNQTMVIEALKMSFYKLNPKQLIKNPIMFVVEVGMLLTLILICFPDIFGTSYLSRGYLITIFIILLITILFANFSEAFAEGRGKAQADSLRQAQSNLTARLIEENGAYRIVNATELKAGQNIRVENGETIPADGVVINGLATVDESAITGESAPVIKESGGDFDGVIGGTLVTSDWLEIRVESEAGTSFLDKMIALVEGAERNKTPNEIALFTLLTTLTIIFLVVIVTLYPIASYLHLILPIAMLIALTVCLIPTTIGGLLSAIGIAGMDRVTQFNVLAKSGRAVEVCGDVDVMILDKTGTITYGNRIASEFLPVNQQMMEKLIVAAYMSSIYDDTPEGKSIVRLAKQMYINELPKDIDGTYKPFTAETRMSGIITNEISVFKGAPNSMINLVKQQQGNIPLNIESICMDVSSKGGTPLIVIENNVMLGVIYLKDVIKDGLVERFAELRKMGIETVMCTGDNALTAATIAKEAGVDRFVAECKPEDKIKVIKDEQAKGHIVAMTGDGTNDAPALAQANIGLAMNSGTISAKEAANLIDLDSNPTKLIEVVKIGKQLLMTRGALTTFSLANDVAKYFAILPALMMSTIPEMTSLNIMHLSSPKSAIISALIFNALIIVALIPIAMKGVKVKGYSIDRIFINNMLIYGLGGLIVPFLGIKLIDMIVQFFV", "text": "FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily."}
{"protein": "MRKKLTALVLSALPLAAVADVSLYGEIKAGVEGRNYQLQLTEAQAANGGASGQVKVTKVTKAKSRIRTKISDFGSFIGFKGSEDLGDGLKAVWQLEQDVSVAGGGATQWGNRESFIGLAGEFGTLRAGRVANQFDDASQAIDPWDSNNDVASQLGIFKRHDDMPVSVRYDSPEFSGFSGSVQFVPIQNSKSAYTPAYYTKNTNNNLTLVPAVVGKPGSDVYYAGLNYKNGGFAGNYAFKYARHANVGRNAFELFLIGSGSDQAKGTDPLKNHQVHRLTGGYEEGGLNLALAAQLDLSENGDKTKNSTTEIAATASYRFGNAVPRISYAHGFDFIERGKKGENTSYDQIIAGVDYDFSKRTSAIVSGAWLKRNTGIGNYTQINAASVGLRHKF", "text": "FUNCTION: Serves as a slightly cation selective porin. Major antigen on the gonococcal cell surface and it may have pathogenic properties in addition to its porin activity. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Gram-negative porin family."}
{"protein": "MKSKLIILLTLVPFSSFSTGNNFEINKTRVIYSDSTPSVQISNNKAYPLIIQSNVWDESNNKNHDFIATPPIFKMESESRNIIKIIKTTINLPDSQESMRWLCIESMPPIEKSTKINRKEGRTDSINISIRGCIKLIYRPASVPSPVFNNIVEKLKWHKNGKYLVLKNNTPYYISFSEVFFDSDKVNNAKDILYVKPYSEKKIDISNRIIKKIKWAMIDDAGAKTKLYESIL", "text": "FUNCTION: Involved in the biogenesis of the CS6 fimbria. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the periplasmic pilus chaperone family."}
{"protein": "MKFGCLSFRQPYAGFVLNGIKTVETRWRPLLSSQRNCTIAVHIAHRDWEGDAWRELLVERLGMTPAQIQALLRKGEKFGRGVIAGLVDIGETLQCPEDLTPDEVVELENQAVLTNLKQKYLTVISNPRWLLEPIPRKGGKDVFQVDIPEHLIPLGHEV", "text": "FUNCTION: May play a role in cell protection during the inflammatory response. In epithelial cells, negatively regulates IL6 production and apoptosis through the regulation of MT2A expression (PubMed:24916366). SIMILARITY: Belongs to the EOLA family."}
{"protein": "MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPRVTPKGINGIDFKGEAITFKATTVGIPATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDEIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSVSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATRAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF", "text": "FUNCTION: Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus Endoplasmic reticulum Note=Preferentially localized to the Golgi apparatus."}
{"protein": "MDGCKKELPRLQEPEEDEDCYILNVQSSSDDTSGSSVARRAPKRQASCILNVQSRSGDTSGSSVARRAPKRQASSVVVIDSDSDEECHTHEEKKAKLLEINSDDESPECCHVKPAIQEPPIVISDDDNDDDNGNDLEVPDDNSDDSEAPDDNSDDSEAPDDNSDDSEAPDDNSDDSEAPDDNSDDSDVPDDNSDDSSDDNSDDSSDDNSDDSDVPDDKSDDSDVPDDSSDDSDVPDDSSDDSEAPDDSSDDSEAPDDSSDDSEAPDDSSDDSEAPDDSSDDSEASDDSSDDSEASDDSSDDSEAPDDKSDDSDVPEDKSDDSDVPDDNSDDLEVPVPAEDLCNEGQIASDEEELVEAAAAVSQHDSSDDAGEQDLGENLSKPPSDPEANPEVSERKLPTEEEPAPVVEQSGKRKSKTKTIVEPPRKRQTKTKNIVEPPRKRQTKTKNIVEPLRKRKAKTKNVSVTPGHKKRGPSKKKPGAAKVEKRKTRTPKCKVPGCFLQDLEKSKKYSGKNLKRNKDELVQRIYDLFNRSVCDKKLPEKLRIGWNNKMVKTAGLCSTGEMWYPKWRRFAKIQIGLKVCDSADRIRDTLIHEMCHAASWLIDGIHDSHGDAWKYYARKSNRIHPELPRVTRCHNYKINYKVHYECTGCKTRIGCYTKSLDTSRFICAKCKGSLVMVPLTQKDGTRIVPHV", "text": "FUNCTION: May play a role in DNA-protein cross-links (DPCs) clearance through a SUMO-dependent recruitment to sites of DPCs, ensuring the genomic stability by protecting germ cells and early embryos from various sources of damage (PubMed:30914427). Can resolve the topoisomerase II (TOP2A) DPCs (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, PML body Chromosome Note=Co-localizes with SUMO2 at PML bodies in all interphase cells (PubMed:30914427). Localizes on condensed chromosomes in spermatocytes in G2 and M during meiotic prophase (By similarity). SIMILARITY: Belongs to the serine-aspartate repeat-containing protein (SDr) family."}
{"protein": "MAAVALPLLLLLASPATPTPARDPFSPQLGDTQRCQQRCRQRHPGLPPAQPEPEGPSESPNNKAVLINACERGCRLFSICRFVARSSRPNATETECEAACTEAYVKAKEQQACSEGCWGQIPEPETQLEQKELALDPPSGSLSLRHLFTMLCSDLMSSAQDLISSTWTYSLQTDNRKTQPVVENFAFQGSRLQRVEVTWRGSHPKALEVHMDPMSPLEKVRRAKPHLKTSKAKVESEDQQESDFLSCMSRRSGLPRWVLFCCLFLSVLIILWLSCCTLVTTPGQHLKFQPLTAEQHKGLLVESNWPLYPPLPPAYEDSPPPYKLKLDLTTL", "text": "FUNCTION: Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of APP. Inhibits APP transport to the cell surface and further shedding (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type I membrane protein. SIMILARITY: Belongs to the TMEM59 family."}
{"protein": "MASITSRASARASCSQANTRAGRVALSGGALLRPARPARSFVPARKQQQGAVRRGGALSARASAVEDIRKVLSDSSSPVAGQKYDYILVGGGTAACVLANRLSADGSKRVLVLEAGPDNTSRDVKIPAAITRLFRSPLDWNLFSELQEQLAERQIYMARGRLLGGSSATNATLYHRGAAGDYDAWGVEGWSSEDVLSWFVQAETNADFGPGAYHGSGGPMRVENPRYTNKQLHTAFFKAAEEVGLTPNSDFNDWSHDHAGYGTFQVMQDKGTRADMYRQYLKPVLGRRNLQVLTGAAVTKVNIDQAAGKAQALGVEFSTDGPTGERLSAELAPGGEVIMCAGAVHTPFLLKHSGVGPSAELKEFGIPVVSNLAGVGQNLQDQPACLTAAPVKEKYDGIAISDHIYNEKGQIRKRAIASYLLGGRGGLTSTGCDRGAFVRTAGQALPDLQVRFVPGMALDPDGVSTYVRFAKFQSQGLKWPSGITMQLIACRPQSTGSVGLKSADPFAPPKLSPGYLTDKDGADLATLRKGIHWARDVARSSALSEYLDGELFPGSGVVSDDQIDEYIRRSIHSSNAITGTCKMGNAGDSSSVVDNQLRVHGVEGLRVVDASVVPKIPGGQTGAPVVMIAERAAALLTGKATIGASAAAPATVAA", "text": "FUNCTION: Catalyzes the decarboxylation of free fatty acids to n- alkanes or n-alkenes in response to blue light (PubMed:28860382, PubMed:30106504, PubMed:30673222). Substrate preference is toward fatty acids with C16 or C17 chains (PubMed:28860382, PubMed:30106504, PubMed:30673222). Saturated fatty acids are converted to alkanes, not alkenes (PubMed:28860382). The decarboxylation is initiated through electron abstraction from the fatty acid by the photo-excited FAD (PubMed:28860382). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the GMC oxidoreductase family."}
{"protein": "MTTKKTSPDLLLVIITLLLLTIGLIMVYSASAVWADYKFDDSFFFAKRQLLFAGIGVIAMFFIMNVDYWTWRTWSKLLMVICFFLLVLVLIPGVGMVRNGSRSWIGVGAFSIQPSEFMKLAMIAFLAKFLSEKQKNITSFRRGFVPALGIVFSAFLIIMCQPDLGTGTVMVGTCIVMIFVAGARIAHFVFLGLIGLSGFVGLVLSAPYRIKRITSYLNPWEDPLGSGFQIIQSLYAVGPGGLFGMGLGQSRQKFFYLPEPQTDFIFAILSEELGFIGGTLILLLFSVLLWRGIRIALGAPDLYGSFVAVGIISMIAIQVMINIGVVTGLIPVTGITLPFLSYGGSSLTLMLMAVGVLLNVSRYSRY", "text": "FUNCTION: May play an essential role not only during sporulation, but also during vegetative growth. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SEDS family. SpoVE subfamily."}
{"protein": "MAFDISVNASKTINALVYFSTQQDKLVIRNEVNDIHYTVEFDRDKVVDTFISYNRHNDSIEIRGVLPEETNIGRVVNTPVSMTYLYNKYSFKPILAEYIRHRNTISGNIYSALMTLDDLVIKQYGDIDLLFNEKLKVDSDSGLFDFVNFVKDMICCDSRIVVALSSLVSKHWELTNKKYRCMALAEHIADSIPISELSRLRYNLCKYLRGHTDSIEDEFDHFEDDDLSTCSAVTDRETDV", "text": "FUNCTION: BCL2-like protein which disrupts the host immune response by inhibiting the TLR4 signaling pathway leading to NF-kappa-B activation. Acts close to the plasma membrane and targets several host TIR-domain containing adapter proteins including MYD88, TIRAP, TRIF and TICAM2. In turn, blocks the host NF-kappa-B and TRIF-mediated IRF3 activation. SIMILARITY: Belongs to the orthopoxvirus OPG176 family."}
{"protein": "MDKSDSLLQSSSKGLRSSIFFQGSSRILTFFLNQLTIRLTSPSAYAFSSIHFEILQSTILFLSRESVRLAMQRIPSENAIITSTSTESNKSKKLSDQLQLIKNTSLISVYIGIVISLLVSLFYFYSLPNFPYSKTCIFIYTVSSFIELLSEPYYEVLQWRQKFSKTASAEGLGTIICSLLSFAISVLGRNKAPSSLPFALGNLSEKVTIFFTLRYFAKQPFSIFLHKVGENERYIFWDSSTLRIICSHTYQVLLKHLITKGDKIMVAWYASPSAQGPYALASNYGSLLARIVFRPVEDHSHIVFAQLTHYKNKKDEKKALNLLAWILKLYSYMSLFILFGSNYSDIVLLFGAGSKWASPDSSSILSWYAMYIPFMAANGVLEAFYVSAANSSQLYDQGKCYLASAVFYFITGKFLLSWFNLGSHGLILANILNLSLRICFALRFILHNYKDFSLPRSLPRPFLLALSILLSIISSFLVKHWRESKVPFLVYFLSAPSLAILYSCFIILVDKDVRGYAKILLSKYYIK", "text": "FUNCTION: May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RFT1 family."}
{"protein": "MEKTEESVGIRVYTATPPQKPSPSPPSRSPKPVLISSLPSLPSGAAAGGGRGRKRRMVAQGVQKTVSKTSMLVNFLPTGTLLMFEMVLPSIYRDGDCNGINTLMIHLLLLLCAMSCFFFHFTDSFKASDGKIYYGFVTPRGLAVFMKPPPPEFGGGDVIAEAEIPVTDDRYKLTVNDFVHAVMSVLVFMAIAFSDRRVTGCLFPGKEKEMDQVMESFPIMVGIVCSALFLVFPTTRYGVGCMTG", "text": "FUNCTION: Involved in membrane remodeling. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Vacuole membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the plant DMP1 protein family."}
{"protein": "MMDVSSWKEMEVALVSFDNADQIVEDPCYSNDLSPASQSRKGHPSCANLLSNWRILINSENANNETIFSRFSAEFSEHLVGERVGMEEGDQRVIINIAGLRFETRLKTLNQFPETLLGDPEKRMRYFDSMRNEYFFDRNRPSFDGILYYYQSGGKIRRPANVPIDVFADEITFYELGDEAMDQFREDEGFIKDPETLLPTNDFHRQFWLLFEYPESSSAARGVALVSVLVIVISIIIFCMETLPEFREEREYKSTQELSKNTTDTLLAHSTFTDPFFVIETACIIWFSFELFVRFIVCPSKTEFFKNIMNIIDIVSIIPYFVTLTTELIQQSELNGQQNMSLAILRIIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEVDEPQSHFSSIPDGFWWAVVTMTTVGYGDMCPTTLGGKIVGTLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEKQILPGEVERILNSVVTGNDSMESLNKTNGGYPRDKAKK", "text": "FUNCTION: Mediates voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. The channel activity is up-regulated by cAMP (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.8/KCNA10 sub-subfamily."}
{"protein": "MSPHEVIGTVPKNSTTFRTQADEHDDHEEALQNLRTGKYEDWPNEAAFDGLTEERGPIKIAVTGNIPTWAAGSLYRTGPGLYKIDTDAGTTFEMSHWFDGLAHTHRFDIIPNEEGSVDIFYSSRRQAEEMMDVIKKQGTWPYYSFGQKADPCLGFFAKAMAAFKGLREPSGEKWHNNVNVAVHVNPPGLEAVRNIVGTRKPAVAENDANVLGHRPELPKSIWVSTDNSTMKQIDPQTLEPIGWATQDVLHPELTGAMSCAHAQRDPDTGDFFNFNLEFGPKPTYRVFRVDASSGKTEILATIREPSVSPAYIHSLFLSPSFVILCIPTSHFGLSGTQIPWERNLVDAIKPYDPSRKTQWIVIDRKHSKGVVARFETDGRFFFHTVNSFEEKAGSDSSDINLYCDVIDFGSHEFIHSLYLDVILNRDSAAKKFYEDEQRARNSLAHLTRYHFIINPDSPTTNLPVTPTPDPKNHEAFRIPAPHAGEIPTINPLYATRKHRYVYSLPFRGRGTITDAIVKTDTVTREALFWDNPKGHTPGEAIFIPRPGGEEEDDGVLLSLVLDGEKGKSYLLCLDAKTMAEMGRAEVDFAIALGFHGAHVPSGRTLTRVEGPEY", "text": "FUNCTION: Torulene dioxygenase; part of pathway that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation (PubMed:17610084). Cao-2 mediates the cleavage of torulene into beta- apo-4'-carotenal, the aldehyde corresponding to the acidic neurosporaxanthin (PubMed:17610084). Is not able to use gamma-carotene (that it is not desaturated at the C4'-C5' bond) as substrate, which suggests a high specificity of cao-2 in cleaving the C4'-C5' double bond (PubMed:17610084). Neurosporaxanthin is synthesized from geranyl- geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme al-2 first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase al-1 then introduces 5 desaturations to lead to 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene. Al-2 cyclase activity then converts 3,4- didehydrolycopene into torulene. Al-2 can also convet lycopene into gamma-carotene which in turn is converted to beta-carotene by an additional al-2 cyclization reaction. Torulene is the substrate of the dioxidase cao-2 that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase ylo-1 mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the carotenoid oxygenase family."}
{"protein": "MTVTYTARVANARFGGFSQLLLLWRGSIYKLLWRELLCFLGLYMALSAAYRFLLAEEQKRYFEKLVIYCDQYASLIPVSFVLGFYVTLVVHRWWNQYLCMPLPDALMCIVAGTVHGRDDRGRLYRRTLMRYAGLSAVLILRSVSTAVFKRFPTIDHVVEAGFMTREERKKFENLNSSYNKYWVPCVWFSSLAAQARREGRIRDNSALKLLLEELNVFRSKCGMLFHYDWISIPLVYTQVVTIAVYSYFLACLIGRQFLDPAQGYKDHTLDLCVPIFTLLQFFFYAGWLKVAEQLINPFGEDDDDFETNFLIDRNFQVSMLAVDEMYDDLAMLEKDLYWDAAEARAPYTAATAFLLQQPSFQGSTFDIALAKEDMQFQRLDGVDGPLGEVHGDFLQRLLPAGAGSVGPLGRRLSLLRRKNSCVSEASTAASCGCAGAADGGGVECGCGDPLLDPSLREPELEPPACPEPPAPIPGPTPEPFTTVSIPGPRAPAPPWLPSPIGEEEESPA", "text": "FUNCTION: Forms calcium-sensitive chloride channels. Permeable to bicarbonate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the anion channel-forming bestrophin (TC 1.A.46) family. Calcium-sensitive chloride channel subfamily."}
{"protein": "MKTIMIRDDVYKKLLEIKGDKSFSEIIEELIEESLSVRRKKIEKYFGILNEEEARGLAKEIEEMRKRTDEDIARKLSNY", "text": "FUNCTION: Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC12 (Potential). SIMILARITY: Belongs to the UPF0330 family."}
{"protein": "MQLRITSRKKLTALLCALGLISIVAIYPRQTVNFFYSTAVQITDYIHFYGYRPVKSFAIHIPASYTIHGIDVSRWQERIDWQRVAKMRDNGIRLQFAFIKATEGEKLVDPYFSRNWQLSRENGLLRGAYHYFSPSVAAPVQARLFLQTVDFSQGDFPAVLDVEERGKLSAKELRKRVSQWLKMVEKSTGKKPVIYSGAVFYHTNLAGYFNEYPWWVAHYYQRRPDNDGMAWRFWQHSDRGQVDGINGSVDFNVFNGTEEELQAFVDGIKETP", "text": "SIMILARITY: Belongs to the glycosyl hydrolase 25 family."}
{"protein": "MDPLSSVQPASYVGFDTITNQIEHRLLKKGFQFNIMVVGQSGLGKSTLINTLFASHLIDSATGDDISALPVTKTTEMKISTHTLVEDRVRLNINVIDTPGFGDFIDNSKAWEPIVKYIKEQHSQYLRKELTAQRERFITDTRVHAILYFLQPNGKELSRLDVEALKRLTEIANVIPVIGKSDTLTLDERTEFRELIQNEFEKYNFKIYPYDSEELTDEELELNRSVRSIIPFAVVGSENEIEINGETFRGRKTRWSAINVEDINQCDFVYLREFLIRTHLQDLIETTSYIHYEGFRARQLIALKENANSRSSAHMSSNAIQR", "text": "FUNCTION: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Bud neck Note=Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family."}
{"protein": "MLLVIDVGNTNTVLGVYHDGKLEYHWRIETSRHKTEDEFGMILRSLFDHSGLMFEQIDGIIISSVVPPIMFALERMCTKYFHIEPQIVGPGMKTGLNIKYDNPKEVGADRIVNAVAAIHLYGNPLIVVDFGTATTYCYIDENKQYMGGAIAPGITISTEALYSRAAKLPRIEITRPDNIIGKNTVSAMQSGILFGYVGQVEGIVKRMKWQAKQEPKVIATGGLAPLIANESDCIDIVDPFLTLKGLELIYERNRVGSV", "text": "FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Cannot utilize a phosphoryl donor other than ATP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type III pantothenate kinase family."}
{"protein": "MKVELVFIPSPGVGHIRATTALAKLLVASDNRLSVTLIVIPSRVSDDASSSVYTNSEDRLRYILLPARDQTTDLVSYIDSQKPQVRAVVSKVAGDVSTRSDSRLAGIVVDMFCTSMIDIADEFNLSAYIFYTSNASYLGLQFHVQSLYDEKELDVSEFKDTEMKFDVPTLTQPFPAKCLPSVMLNKKWFPYVLGRARSFRATKGILVNSVADMEPQALSFFSGGNGNTNIPPVYAVGPIMDLESSGDEEKRKEILHWLKEQPTKSVVFLCFGSMGGFSEEQAREIAVALERSGHRFLWSLRRASPVGNKSNPPPGEFTNLEEILPKGFLDRTVEIGKIISWAPQVDVLNSPAIGAFVTHCGWNSILESLWFGVPMAAWPIYAEQQFNAFHMVDELGLAAEVKKEYRRDFLVEEPEIVTADEIERGIKCAMEQDSKMRKRVMEMKDKLHVALVDGGSSNCALKKFVQDVVDNVP", "text": "FUNCTION: Possesses quercetin 3-O-glucosyltransferase activity in vitro. Also active in vitro on benzoates and benzoate derivatives. SIMILARITY: Belongs to the UDP-glycosyltransferase family."}
{"protein": "MLLTKREKHLLAAFQNYGKLSLKQMIDLLKVSQRTVYRTISDLTDSLNTINISIIKENQNYFLVGELANLASIISLDTYEQYERLNLITYKLLMSFSSITNEQLQEEFNVSNVTIIQDIAEIEKRLADFDLRLDRKKGYRLVGNKNTLRRLLAILLTNNLSISDFGAGAYGHFEVLDKAKLELAKQIFQSSQEDLPDLDAKMSEFFIILLALSGWRDNEAVGHSISKAALDFSQKVYTEFSQKTNQFYSIQEILYYASILDELVIKRQETPLFHEKFDSAFFYNISNLIDKVSLYTKINFAKDKTLFHFLFNHIRLNLAVPQIFEDKSNNTIAHEVVQGNEYLHRVVSLLVQDIFPKYLQKEPEYELITLHFASSLRRSPDIYPIKILLLTDERPLARELLITRIKTIAPFVDKVVVKELAQYETKDKDYYNCVLATKPLVDKAVKMVSTYPDAKEMLQLQDYLQNVQAHQKIIIRDEQTNKQGYNLQNYFLATQQLLQEFSYQEIDNPADFETSVPKIMETIAAVSDKTYLSSKLLKCFAVSPLAIPETHLALLHTQSSKVITSCFKIYDLKRPVTALSMNYEKETVTRILVMLTRLDETKEMRDLMTAISQSIIENHLYTEIYKTGNKDIIYQLLNQIFTEKIKKLET", "text": "FUNCTION: Not necessary for mannitol utilization. May be involved in regulation of the mannitol phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS)."}
{"protein": "MNLINSTKIFSSLMIASVENNTAIFSLNTDILETNLINLLVIFFLLIYQGRPFFTALLEERRKTVLDKIKKSENSYNEALEKLKEAKSKLAQAELAAKQIYEEAEAVAESIKKTGLAQLEKDIKRIEETTQASINTQQLSVITYLRQQVALLALRRVVSQLKNYLKPELHSQFIDRKILQLRKQK", "text": "FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family."}
{"protein": "MYGKIIFVLLLSGIVSISASSTTGVAMHTSTSSSVTKSYISSQTNGITLINWWAMARVIFEVMLVVVGMIILISYCIR", "text": "FUNCTION: This protein is a minor sialoglycoprotein in human erythrocyte membranes. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the glycophorin-A family."}
{"protein": "MALDQSFEDAALLGELYGEGAFCFKSKKPEPITVSVPSDDTDDSNFDCNICLDSVQEPVVTLCGHLFCWPCIHKWLDVQSFSTSDEYQRHRQCPVCKSKVSHSTLVPLYGRGRCTTQEEGKNSVPKRPVGPVYRLEMPNSPYASTDLRLSQRVHFNSPQEGYYPVSGVMSSNSLSYSAVLDPVMVMVGEMVATRLFGTRVMDRFAYPDTYNLAGTSGPRMRRRIMQADKSLGRIFFFFMCCVVLCLLLF", "text": "FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of aquaporin PIP2-1. Forms a ubiquitin ligase complex in cooperation with the E2 enzymes UCB8/UCB10. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein."}
{"protein": "MAAAQTFSANCDPVNFHNLQSYPSESVTYSCKMGNVSSLMEKQDFPNEGFNLDFRPFPEPSCKRGLHQKEFLSYLNITKKEGKNNKKFPSGLGFRREHSLQAEENDYPVFYHKDHRGTEFSKSSLPERGHSDKSRFGPSALKSNVKAFMSIQSLHQSTNKLSKSNGSLNTLGCVGSPPCRGPLQPSNSHSNNPSESGNDEDDDSLSDSKQNSINSLNSYSPSFTVARGQISASLGHINHIGGSLDRASRGLRDTMAGEKGTLSCRNMATLSRLQCSGEPPPPYEYSESVEDVARQLEKRLQEKGMEAQQLRRNASDNDDPFTQVFEDKRRLWMEELDELKQMYMSKLQQISQQALRSQRALQLQLYKVQQEKKRLQEELNSLQGENEELRQKQSQSDNSGPNLEDSKWEISQKAGEISFLKQQLRDSQAEINLKLGEVVSLKVQLREAKALVKEKEKESAELSDCLQALEDVKSQTPVDLPRDSSDTIDVERLRAELMLERRQNEAQILIFETERKVWKEEKDKVLRYQKEIQSSYLEMYQRNQALERQVLELRQGVGQSLSSPASWMDTVET", "text": "FUNCTION: Plays a role in axon and dendrite arborization during cranial nerve development (PubMed:24044555). Also important for neural crest migration and early development of other anterior structures including eye, brain and cranial cartilage (PubMed:28104388). SUBCELLULAR LOCATION: Cytoplasmic vesicle Cell projection, axon Cell projection, dendrite Note=In developing neurons, accumulates in early growth cones and at branching points of axons and dendrites. SIMILARITY: Belongs to the N4BP3 family."}
{"protein": "MATLNSNPEILLRKRRNAERTRVEKQEAARRRAEAEVRQRRARQHKFVRAEALVASTLATEREKTRIQRVSKRAAKQRAGHVTGGEWLVRVRAAADGGLEREKTAYDGRATLLFVVRVRGPAAAKIPRKAHRVLTLLRLAEVNTGVFVRLTAEVFPLLQVVAPYVVVGRPSLASIRALVQKRARVVHQRAGEAAPVEMVLNDNGVVEERLGDEGVICVEDIIHEIATMGEAFAKCNFFLLPFKLGREVSGFSALSRLQKLKQREEASQTRPVSNAAAAPLVEVDVDELIGRLN", "text": "FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May act as a specificity factor that binds precursor rRNAs and tethers the enzymes that carry out the early 5' to 3' exonucleolytic reactions that generate the mature rRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the universal ribosomal protein uL30 family."}
{"protein": "MIGKRQTSTLNWDTVFAVPISVVNKAIKDKKSSPENFEFEDSSGSKCKGDFGDWQIITGGDGSNIRMKIPIYNFKAELVDDKYGIFNGNGGFESGEMNIQVKLKYFPHDKISKYKDVELVDLKVRSESADPIDPVVVMLSLKNLNGFYFNFLNEFGEDLQDIIEMFFIELVKQWLTENISLFNHIFSVVNLNLYIDQYSQWSWSRPSYVSYAYTDIEGDLDKSLLGVLCMTGGRNPDLRQQKVDPHAVPESSQCGFLIYEERVLRDLLLPTLPMKFKNSTVEDYEVINASGESGQYQYILRLKKGRSVSLDRVEANGSKYDPYMTEMSISLSNDVLKLEATTETSVGMGGKVGCDTINWYKLVLAKNGNGEQTISYEEVGEPTVINYVIKEGENWVWDVIAAIIAILATAVLAIFTGGAAFFIGGIVIAIITGFIAKTPDIILNWNLETSPSIDMMLENSTSQIIWNARDIFELDYVALNGPLQLGGELTV", "text": "FUNCTION: Expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. SIMILARITY: Belongs to the TULIP P47 family."}
{"protein": "MRLHEILKHLCEPAHMPPVNPEIAGVVYDSRAVTPGALFVAYRGFHTDGHAYIPQALERGAAAVVYEDPAWDGRVPVPALRVPNARVALAPLAAAFYGHPGRRMRIVGVTGTDGKTTTTFLTSVALEAGGAITGLMGTVDFKIGERMWTNDSRQSTPEAPEVQALLRDMAEAGCSYAVIEATSHALSARWNRLAGSAFDIAVFTNVTQEHLDFHGTVEQYRRDKARLFEMLAEFNDAAAPFKQRKIAVVNADDPHHRMFLDAAPVSAERLTYAVHAHADVRAEDVRSTRDGLRFRVTTPWGAADARLRLTGDFNVWNALAALTVACAEGVPLERCLAALERVPGVRGRMERIEAGQPFTVLVDYAHTPGAFEKLFRIVRPLTEGQVIAVFGSAGERDRAKRPLQGEIAGRFCDLVIVTDEDPRLEDRAAIIAEIAAGAEAVGKRIGETCLCIPDRALAIRTAFAYARPGDIVLLLGKGHEGSIIYGTTPVPWDEAAEARRALAELGYGG", "text": "FUNCTION: Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family. MurE subfamily."}
{"protein": "MKSVYPMSSPSSAVFADQGLSGKANQTQPPPPLGLVVPASKPGAKKPLRKNAWQVAPNLLVSFRYAWAGVSYAFATQRNFRIHTFTGVAVITAASLLHLEAIAVAVLALTSCLVMILELLNTALESVVDLTVGQSYHELAKIAKDCAAGAVLLAAIAAVIVGGCLLLPPLLSLMV", "text": "FUNCTION: Catalyzes the ATP-dependent phosphorylation of sn-l,2- diacylglycerol (DAG) to phosphatidic acid. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bacterial diacylglycerol kinase family."}
{"protein": "MAVISLLQGLSVGQQIGTAAAISVFVLTSIVVYGCYLHPLSHVPGPFLAKFSPIWGMRALYRMKFNSELQALHEKYGPVVRVAPNEVSFATLEAETAIYANQEDGRFSKAGTFLTLFSDLVLNAPTLITIPDPALHKRLHKVIQQAFTPQALASQEPIQKLHIEKAIPDFDETADKGYHIDLADKLETMFWEIIGDLAFGEPLMAGKRPTYEKLKQLGKGSMPMVEALSFMLVMPGVAPTLEMARSFLSAMPMSSQLSKLVPSTKLRDCVERKDGREDFLSAIMGSEKQGLTLDADAFFSNAMGLTLAGYQTTATTLASTFYHVLRYTDAYKTLCTEIRSAFNDEAEITGERLARLPFLNACIRETLRLLPPANGKTAQRTAPSCTIADTYIPAGTIVSADLYTIQRSPKYFVDPARFHPERWLEDAEKNGFNGDNRSASRPFLIGSRACIGRHMAQQSIRLIMATLLWRYDFELLDPDGFIWERDAGSSLIYTDYKLPVHVKRFQ", "text": "FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of terpestacin (PubMed:29185768). The bifunctional terpene synthase tpcA converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene preterpestacin I (PubMed:29185768). The C-terminal prenyltransferase (PT) domain of tpcA catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into preterpestacin I (PubMed:29185768). The cytochrome P450 monooxygenase tpcB then hydroxylates preterpestacin I to yield 24- hydroxypreterpstacin I (renamed as preterpestacin II) whereas the cytochrome P450 monooxygenase tpcC further hydroxylates preterpestacin II to yield 16,17-dihydroxypreterpestacin II (renamed as preterpestacin III) (PubMed:29417814). Finally, the FAD-dependent monooxygenase tpcD converts preterpestacin III into terpestacin (PubMed:29417814). SIMILARITY: Belongs to the cytochrome P450 family."}
{"protein": "MPVYQYKARDRQGRLVEATIEAEDLRTAARLLRDRGLFVAEIKEPGKGLQAEVRIPALERGPGLKDLAIFSRQLATMLGAGLTLLQALAILERQTENRKFREILKQVRTDVEGGMAFSEALSKHKIFSRLYVNLVRAGETSGGLDLILDRLASFLEKELELRGKIRSAMTYPVIVFVFAVGVAYFLLTGIVPQFAQILTDLGSELPLLTRFLIAVSDLLRAATLPLLLLAVALFFAYRWYYGTPQGRRVIDRLKLRLPVFGNLNRKTAVARFSRTLALLLSSGVNIVEALDITKGTAGNSVVEEIVEAAKLKIQQGDPLNLTLAQHPFVFPPMVSSMVAIGEETGALDTMLSKVADFYEREVDEAVASLTAAIEPLMIIFLGVIVGMIVAGMFLPLFKIIGTLSVQ", "text": "FUNCTION: Essential inner membrane component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface- associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Controls both pilus assembly and disassembly and plays an important role in PilB localization to the complex and ATPase activity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GSP F family."}
{"protein": "MSILISPDNNTGWGLCSAGMYGGAKRRSSQHPVRVRGHYRAPWGAYTRGVISRRTTVDDVIDSVVADAQRYTRPVATSTVDSVIDSVVANARRYAQRKRRLQRRRRRPTAAMTAARAVLRRAQRIGRRAMRRAAASASAGRARRQAARQAAAAIASMAQPRRGNIYWVRDASGVRVPVRSRPPRS", "text": "FUNCTION: Plays a role in the inhibition of host immune response within the nucleus. Interacts with cellular nucleosomes and immobilizes the host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1 release out of the cell and thus decreases inflammation. Also plays a role in the wrapping and condensation of the viral DNA. May also promote viral genome import into the nucleus. SUBCELLULAR LOCATION: [Histone-like nucleoprotein]: Virion Note=Located inside the capsid in association with the viral DNA (core). Present in about 1070 copies per virion. SUBCELLULAR LOCATION: [Pre-histone-like nucleoprotein]: Host nucleus, host nucleolus. SIMILARITY: Belongs to the adenoviridae histone-like nucleoprotein family."}
{"protein": "MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMWGVRLVEGILHAPEAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDIKTGHSKGFGFVRFTDYETQVKVMSQRHMIDGRWCDCKLPNSKQSPDEPLRSRKVFVGRCTEDMTADELQQFFAQYGEVVDVFIPKPFRAFAFVTFADDQVAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERGGRFGGNPGGFGNQGGFGNSRGGGGGLGNNQGSNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQPQGNMQREQNQGFSSGNNSYGGSNSGAAIGWGSASNAGSSSGFNGGFGSSMDSKSSGWGM", "text": "FUNCTION: Probably involved in transcriptional repression (By similarity). May play a role in the maintenance of the circadian clock periodicity (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, Stress granule Mitochondrion Note=Continuously travels in and out of the nucleus. Localizes to stress granules in response to oxidative stress. A small subset localizes in mitochondria."}
{"protein": "MPVQPPSKDTEEMEAEGDSAAEMNGEEEESEEERSGSQTESEEESSEMDDEDYERRRSECVSEMLDLEKQFSELKEKLFRERLSQLRLRLEEVGAERAPEYTEPLGGLQRSLKIRIQVAGIYKGFCLDVIRNKYECELQGAKQHLESEKLLLYDTLQGELQERIQRLEEDRQSLDLSSEWWDDKLHARGSSRSWDSLPPSKRKKAPLVSGPYIVYMLQEIDILEDWTAIKKARAAVSPQKRKSDGP", "text": "FUNCTION: Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. SIMILARITY: Belongs to the BRMS1 family."}
{"protein": "MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHAHIRKTNPRGSGGAEAPEEERKHLMARRGQTYGRRHDDPNADLPPRLRPAKDVGLLFMAFNSNLGNQFEFTQQIWANNPAFPFPPDGSQPGLDPVIGQGARAPQKYAPEWGHNNVAEATDPIPQAVTMKGGEYFFMPSLAFLRSL", "text": "FUNCTION: Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn- dependent oxidase mode of action that expands its substrate scope in vitro; is thus able to catalyze the O(2)- and Mn-dependent oxidative decarboxylation of 4-methoxymandelate to anisaldehyde. SUBCELLULAR LOCATION: Secreted Note=Although no signal sequence is found, the secretory machinery for actinomycetes is not fully characterized, and the low pH optimum for DyP2 along with the observation that many DyPs have been isolated from the secreted protein fraction imply that DyP2 could be secreted and still possibly play a role in extracellular oxidation chemistry (PubMed:23054399). SIMILARITY: Belongs to the DyP-type peroxidase family."}
{"protein": "MANQVIKCKAAVAWEAGKPLSIEEVEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGNYPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAALNAAKVEPGSTCAVFGLGGVGLAVIMGCKMAGAARIIGVDINKDKFARAKEFGASECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGISVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHSLPFDQINEAFDLMHAGKSIRTVVKL", "text": "FUNCTION: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Class-III ADH is remarkably ineffective in oxidizing ethanol. Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily."}
{"protein": "MTNRLETKYENLSSIFRLKGHDYQKQFFHLYAHRLAEMTRLLTPLAQKKWGNKEPIKKLCELRGEQDVHCILIGTIFKHQAHKPSILRDISEENQLAPQPPRQNYSDPEDKIVLEDELQRVRLQGKLNGQLLATGVVCAALGGTDSDGFFNVEDILFYESGPQKPLAPIKRSRLLVLASGLDQLQAHKFVEALNLFQYWLAGSLGNNKEAGSMVRLIVAGNSVRASAMAHVPTLQVARTQANANDTVQAVSQLDQWFASWARSLPVDIMPGPYDPANFMLPQQPFHKCMFPQAAQLATFQAVTNPYSCRLDEALVVGTSGQNVSDLLRSTSLDSALEALRCTLTWGHVAPTAPDTLACYPYIESDPFILRECPHVYYAGNCESFATELHEGSEGKRTRLVCVPSFSKTQSVAVVDLDTLDCRMVNFSVDAE", "text": "FUNCTION: Accessory component of both the DNA polymerase delta complex and possibly the DNA polymerase zeta complex (By similarity). As a component of the delta complex, participates in high fidelity genome replication, including lagging strand synthesis, DNA recombination and repair (By similarity). Appears to promote the function of the DNA pol- delta complex accessory subunit PolD3 in both embryonic and postembryonic somatic cells (PubMed:31100062). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Note=In embryos, accumulates in the nucleus during interphase but disperses into the nucleoplasm at the onset of mitosis. SIMILARITY: Belongs to the DNA polymerase delta/II small subunit family."}
{"protein": "MQSRIVGLAPAFSLFPNLNTPHKTFTFHQILVLIITFTAYASFHASRKPPSIVKSVLGPPSLNSSSIDNGWAPFNGTQGTKRLGELDLAFLSSYALGMYFAGHLGDRIDLRYFLVFGMMGSGILTLVFGLGYWMNVHTLGFYMSVQIVCGLFQSIGWPCVVSVVGNWCGKEKRGLIMGLWNSHTSVGNILGSVIASSVLDFGWGWSFVLPGVLVLVSGVVVFMFLVVSPNDLGFEELGKEIEIEMSLGENVEESLRKHEAEGAVLLENVDDSSFAIGFLEAWRLPGVAPYAFCLFFSKLVAYTFLYWLPYYLRHTAVAGVNLSHKTAGILSTVFDVGGVLGGISAGFISDKIKARALTSITFLALSIPALIMYRVYGSVSMFINIVLMFISGLLVNGPYALITTAVAADLGTQDSIKGNGRALATVTAIIDGTGSVGAALGPLLAGYISSRGWNSVFFMLIVSIFFAGLFLVRLAKSEINTMRSGELIASSVP", "text": "SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family."}
{"protein": "MSEASKSIMDLLSEVVKITDMTMDNEAVNKLKPQIKINPFYRAVQDVLVEQKSKIDLSTKMMKDLEAQENDERLDTMLKAEGVAGPDDSLLRIQEAAGTDQYEYRQQLLKVRRELENETKAFDKHCKKWCEYVEDVLQQQGEFRPITQQSTEKFMNKMSGKFNKVCFVLKQTACEEVIQLKKRYLDARRKRRNFSKTSTEILNEYFLANINHPYPSEEVKQALAMQCNISVAQVSNWFGNKRIRYKKTMAKNEDERRENRKPEDRPPPGAPGAPYSLVPNAFAGMMNPYQMMLPGHQFPIGVAPFNFSMYNPEMMAQYQQSLQNPNQTR", "text": "FUNCTION: Plays a role in regulating gene expression in dopaminergic neurons, acting redundantly with homeobox protein ceh-20 in head neurons (PubMed:23788625). May activate dopamine pathway genes in concert with ETS domain-containing protein ast-1, and homeobox proteins ceh-43 and ceh-20 (PubMed:23788625). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/PBX homeobox family."}
{"protein": "MKVSLAGQTVDVKKILNEIPKRTVTAALLEGGEIVAVEEADDEHAERKLVRRHDVEGKVVFVTARPCLYCARELAEAGVAGVVYLGRGRGLGPYYLARSGVEVVEVHPDEPLGYDPVDRLDVLLTFGGNPYLTEEDVAARVYCLLTGRGFDADIAPAPENLSGRVEIMVTRGDPDEAVELLKEELPVFRIRRFLISGEFDRDELRERILEDIEPRILDPFAVRARIARAGAFSSSREAEVFIGDVLTSVGREVNLNDPRTVVTVDVLGPRVSVGVEKR", "text": "FUNCTION: Catalyzes the deamimation of cytosine to uracil at position 8 of tRNA in 30 different tRNAs. This editing guarantees the proper folding and functionality of the tRNAs. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family."}
{"protein": "MANWLNQLQSLLGQSSSSTSSSADQGLVKLLVPGALGGLAGLLVANKSARKLLTKYGTNALLVGGGAVAGTVLWNKYKDKIRAAHQDEPQFGAQSTPLDERTARLILALVFAAKSDGHIDAKERAAIDQQLRGAGVEEQGRVLIEQAIEQPLDPQRLATGVRNEEEALEIYFLSCAAIDIDHFMERSYLNALGDALKIPQDVRDGIERDLEQQKRTLAE", "text": "SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein."}
{"protein": "MEKPKYKRIVLKLSGEALAGEQGNGINPTVIQSIAKQVKEIAELEVEVAVVVGGGNLWRGKTGSDLGMDRATADYMGMLATVMNSLALQDSLETLGIQSRVQTSIEMRQVAEPYIRRKAIRHLEKKRVVIFAAGTGNPYFSTDTTAALRAAEIEADVILMAKNNVDGVYNADPRKDESAVKYESLSYLDVLKDGLEVMDSTASSLCMDNDIPLIVFSIMEEGNIKRAVIGESIGTIVRGK", "text": "FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP or dATP as the most efficient phosphate donors. Is also able to phosphorylate 5-fluoro-UMP and 6-aza-UMP. SUBCELLULAR LOCATION: Cytoplasm Note=Is predominantly localized near the bacterial membranes. SIMILARITY: Belongs to the UMP kinase family."}
{"protein": "MVQIDLPAESAVRIRYPTLTKKLRKRSTLVIIVGLLLLCIITSTHISHNFSGSDTPKCRSIYMYPSYARIDGFDSRHTKLAKKYHLYLYREQGKDKEPKHGDEIQLDGIPVLFIPGNAGSFKQARSIAAASANLYFDHKSTIQNSNAKNMDYFTADFNEDFTAFHGQTMLDQAVYLNDAVRYILSMYAQSAAYKESNRPLPKSVILLGHSMGGIVARLMLTLPNHIPESVNTILTLSSPHSTAPVTFDGDILKLYDRVNSYWTSAMNDMGSYFRNNVSVISITGGILDDILPADYTNLQGIVPESNGFTTFTTTIPELWTPIDHLAIVWCDQLRYLLAKYILEIVNDDAGGKTATLDIRMRKGRKFFLSGLERITDADKLIDKNLSAPAVDFSDTESVPENHLLVLNSSESMSTGYAFNISKSVDYSFEMLTSLVQFDIFFCKDIYGKDCINGFSSFSKVPHSTSLQKFPTDSSWGESVSPFRFISLNGSLLQGFQIIVFQGSMKKKEDFVLAKYSDDKSIETASDGLWKLSLFPFRMSLKNKHSFVHGLAFPNLWSSLISFNLKTTFSDEIDSMFRPMMRQYVNNPYETKWHLLAASSSHEINMHNISPFIPLDDTIDKSLNLMFFIPPGEEISLRLSINWKLTLKMLYIRFRLAFASIPISIIALVLCYQFYYYDSPDSKFISFDTGLMNVLNNHSLLIFLFLSVGPIAINHKAILTLLHYLDPISLSKPSSDSHMLNNNYMLGLRETFVWWIGPVFFIISVALLFIILRLINVIEFAVIKISSAITRYTRITFPDPLNDMTHHKLLFNNRQLLGVCFISLGVMVYVPYQFAFILVSLIQMWNCMKLAVFTNRNNAKYSNIHNYNVSFLMLTIFMIPINAPIVVVFLRNFAIRWETAFRSHHNFLAIAPTLLLTLRNSQCNIPIIKNRMNWLIVVSILGYLSFYSFMYGIRNLYWVYHISNILNGVLFFLTIL", "text": "FUNCTION: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GPI inositol-deacylase family."}
{"protein": "MENQFKNNNNSSSIETSNQFSNKKTNRLDSFVSVSELHEEAKRLLPKMAYDYYASGSNDQITLAENENAFSRIKLVPRSLVDVSKVNTKTRIFGRDISTPILIAPWAMQRMASQRGELDTVEASKEFNTIMTLSSLSTTSVEDLSSATNGNPGWFQLYVFKDRKVSEELVKRAESIGYSALVLTVDTPFLGKRTADFKNSFKLPNGLSLKIFEKLMLSNLDGGLNQYIATMIDPSLTWNDLKWLKSITKLPILVKGIMCPKDAELALQYGADGIIVSNHGGRQLDTCPSTIEVLPYISKVVRGRVPLILDGGIRRGTDVLKALAFGANAVCIGRPIIWGLSTGGKDGVLKVLNLLNSELQLAMALTGITNISDINNSIIWDQNKYIKL", "text": "FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2. May use other 2-hydroxyacids as substrates. SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family."}
{"protein": "MLKVGLPLGACARSWKSVRMASCGMARRNPLDNKVALVTASTDGIGFAIARRLAQDGAHVVVSSRKQQNVDRAVATLKGEGLSVTGTVCHVGKAEDRERLVATAVKLHGGVDILISNAAVSPFFGSLMDVPEEVWDKILDVNVKATALLTKAVVPEMAKRGGGSIVIVSSIAAYSPFPSLGPYNVSKTALLGLTKNLALELAESNVRVNCLAPGLIRTSFSRVLWEDPARQESIKATFQIKRIGKPEECAGIVSFLCSEDASYITGETVVVAGGSLSHL", "text": "FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Reduces all-trans-retinal and 9-cis retinal. Reduces 3- ketosteroids and benzil into 3alpha-hydroxysteroids and S-benzoin, respectively, in contrast to the stereoselectivity of primates DHRS4s which produce 3beta-hydroxysteroids and R-benzoin. In the reverse reaction, catalyzes the NADP-dependent oxidation of 3alpha- hydroxysteroids and alcohol, but with much lower efficiency. Involved in the metabolism of 3alpha-hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family."}
{"protein": "MSLLRIRKPKTRKGKKVLLAREPQLIESARTMLFLDGRKCGGNVKLCMKDLQALKKPLVKVLNRKNDITPFDDPSSLEFLTMKNDAALFTFGSTSKKRPDNIILGRIFENEVLDMFELGIKRYQAISEFKNEKIGACVKPCLVFNGPKWAQTEELRRLRNLFIDTFQREKVDSIRLQGIEHVLSFTVTDDMNILMRSYRILLKKSGQRTPRIELEEIGPSADFSIRRTKIASEDLYKQARKQPKQLKVGKKKNISTDALGNTKGRVHLGKQQTGSIQTRRVKALRKTPEEKKENRQRKKVALKAAAAEALASQGNNPFSS", "text": "FUNCTION: Required for normal assembly of the mitotic spindle. May be involved in both centrosome-dependent and centrosome-independent spindle assembly programs. SUBCELLULAR LOCATION: Nucleus, nucleolus Note=Found in the nucleolus during interphase. SIMILARITY: Belongs to the RPF2 family."}
{"protein": "MVDHISPRASPGPIRSSQTRRARKLRDSCTSCASSKVRCTKEKPACARCIERGLACQYMVSKRMGRNPRAPSPLDSTRRPSESLPSAGSEQGLPAHNTYSTPHAHTQAHTHAHSHPQPHPQSHPQSNQPPHALPTPNGSSSVSAIFSHQSPPPLVETQGLGGDLAGQAQSTLSSLTVDSEFGGSLQSMEHGNHADFLAESTGSLFDAFLEVGTPMIDPFLESAPLPPFQARYCCFSLALQTLTCLFPHAPLGCQLRLTDGEDSSCNLMTTDMVISGNKKATDAVRKILGCSCAQDGYLLSMVVLIVLKVLGWYAAAAGTQCTSTAAGGETNSGSCSNSPATVSSGCLTEERVLHHPSMVGEDCVDEEDQPRVAAQLVLSELHRVQSLVNLLAKRLQEGGDDAAGIPAHHPASPFSLLGFSGLEANLRHRLRAVSSDIIDYLHRE", "text": "FUNCTION: Involved in the regulation of aflatoxin biosynthesis. May have a role in nitrate assimilation and sclerotial morphogenesis. SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MLSLLTRPFLPIFCFLYGPQSEGSTRIQCLRRFVTFLLGLVLGFLLWKLAALNFTLGRLFVNGATDLYVFIIFVLVTGTIFMLSLPVRAVILLIFVALVGKSGRTYLRAVAFAFIISGPIANLVENAGEVARVFVCTTVLTYNLSKTRFDLMAKPFTNTLKHMRGDVEEIRHTFYELQEVLVDLKYAVENSDIEDEKYGDKNTKPIYERWGRETSRMNVSEIGNGGKELPTPAAVQERFQRNMRNRCKHQLRSGHRACLEVFRNGYRKCTTNFPSMIAKAICWPYRVDIICELDLFGNPDKICDPSAVVPQNFGETYVELLKAEKKLFDNSSQIVVNYEIKDEQFAKSQLKSAERTGQAFKEDFERQKRIFNKVMGILQKILCLFMLRMVYVSINYYVKYLNDVEFDNFYITKYFKHVDQRRKEQRIDAILPLRTYEKSKYIDVDHIFSRTHHESTTVCFNLLQFLLELVTAGLFILIDHLVVELLQIVRKRSKIVYQQDGEHEVRFNISGVGQMARLLRTTMHNFNIHEKVSTSLSNKECLPNAHVLPKKMYYQLILLYLIIIVLIYQSTTFLRMRRVICSFFYYKREKQRILFLYNRILRNRLRSLEFLIHDAEDNLATHRIQQQVNVFLWLRFSCPVAFGWIRHFKFAKRTCMICRGLEDSTFTVCGNCGLPYCDDCAEDLNSVCFQCGVVLTRGAEGSESSVEVYTYRKEK", "text": "FUNCTION: Component of the sperm acrosome membrane (PubMed:17092953). Required for breakdown of the sperm plasma membrane after sperm entry into the egg, which is an essential prerequisite for successful fertilization (PubMed:9630751, PubMed:17092953). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Multi-pass membrane protein Cytoplasm Cytoplasmic vesicle membrane; Multi-pass membrane protein Note=Has diffuse cytoplasmic expression in primary spermatocytes. In post-meiotic spermatids, detected in clusters of vesicle-like structures adjacent to the nucleus. In late spermatids, a single vesicle-like spot is found near the nucleus, which probably corresponds to the acroblast. In mature sperm, localizes to the apical tip of the sperm head (acrosome)."}
{"protein": "MESLPVFPNKFKAALAAKQVQIGCWSALSNPISTEVLGLAGFDWLVLDGEHAPNDISTFIPQLMALKGSASAPVVRVPTNEPVIIKRLLDIGFYNFLIPFVETKEEAEQAVASTRYPPEGIRGVSVSHRANMFGTVADYFAQSNKNITILVQIESQQGVDNVDAIAATEGVDCIFVGPSDLAAALGHLGNASHPDVQKAIQHIFNRASAHGKPSGILAPVEADARRYLEWGATFVAVGSDLGVFRSATQKLADTFKK", "text": "FUNCTION: Catalyzes the reversible retro-aldol cleavage of both 5-keto- 4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde. SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase subfamily."}
{"protein": "MSLESLFQHIIFSEHQAEESRRVMREVRSEITRCRGKIKKATEDLSEEKIKLESKVQQLSEKSFLLELLKTHENALERQLSEIISERDTLLQACEAIKNKTTEEEERFIKEITDFNDNYEITKKRDTLMKENIEMEMADLDSQADVLRREMKSVERNRGQLWELQKLKNELLQELFTLQKKLKVLKDEETEAICITKQLEAEKTKVRDKPQHDPECVRLKRELDLYKAEDMESVYRALQAEVDLLELALAPKDPQDSNSLSHEPPHT", "text": "SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium Note=In caput spermatozoa, localized in the middle piece, predominantly concentrated at the mitochondrial sheath of the flagella and to a lesser extent with outer dense fibers (ODF) (By similarity). Colocalized with TEKT2 at the perinuclear region (PubMed:24394471). SIMILARITY: Belongs to the CCDC172 family."}
{"protein": "MKGKNVQLLFALVVIILLFPTGASASPHAVSVGKGSYATEFPEIDFGGINDPGFRDQQGEPPATIYRSDRVTGPMQTNSWWGSLAVDRFSMNQYPHPFSVRHRAEGLHVFYDAPHNMVVHENREAGTWHIHGAIGTDFTIKHSGTANFEQAVVDDYNDWYVRGLLENGAHQMAITYGVGSPYIFVEYEDGSAVLDFDIAPDVWEMNGHVIGFSTHDHKHYAAFAPPGQNWSGIGSKTLTNNADYIAIAKLPEKDGNMLAKFEQYAYSVVRDAVADWTYDEATGTVTTTFEVTTEAKVQGAPDGTIFALYPHQYRHLASSSENQLLQNYQYEIIRGTMIGLEGKRFTTELTYPGVLPSLPDLGDYDRERLIGYLHDATSDYPTGSDTYELGKYIGKLATLAPIADQMGEYELAEQFRGELKDILEDWLQATNASGQLKGKNLFYYNENWGTILGYHAAHSSATRINDHHFHYGYFVKAAAEIARADQEWAKSENWGGMIDLLIRDFMADRDDDLFPYLRMFDPYSGNSWADGLATFDAGNNQESSSEAMHAWTNVILWAEATGNKALRDRAIYLYTTEMSAINEYFFDVHQEIFPEEYGPEIVTINWGGKMDHATWWNSGKVEKYAINWLPFHGGSLYLGHHPDYVDRAYEELRRDIGSTDWNLWSNLVWMYRAFTNPDDALQQMEASIDDYGLFDPGNEKIIERGSTKAQTYHWIHNLAELGRVDPTVTANHPIYAVFNKNGNRTYIVYNFSDSPITVQFSDGHSIQVEPHSFNIGNGDGPTNPDPSEPDLKNPYERIQAEAYDAMSGIQTEGTDDDGGGDNIGWINDGDWVKYERVHFERDASSIEVRVASDTPGGRIEIRTGSPTGTLLGDVQVPNTGGWQQWQTVTGNVQIQPGTYDVYLVFKGSPEYDLMNVNWFVFRANGQGNGDSHTHPDYTAGIRGITGNEVTIFFAPTTEARYVDVHLKVNNGQQLNYRMTERNGEWERVVENLSSGDVLEYSFTYEKLGPQYTTEWFTYSR", "text": "FUNCTION: Cleaves internal linkages in 1,3-beta-glucan (PubMed:15501830, PubMed:28827308, PubMed:28781080). May contribute to plant biomass degradation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 81 family."}
{"protein": "MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTEYPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANR", "text": "FUNCTION: Catalyzes the dehydrogenation of Glutaryl-CoA to glutaconyl- CoA. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family."}
{"protein": "MTTKQPTRFEAVIGIETHVQLNSRTKAFCRCAYEYGAEPNTRVCPTCMGHPGTLPVLNSAVVKKGIAIGTALGAKIRRTSKFDRKQYFYPDLPKGYQISQFDEPLCYDGSIDVVLPVEDGGEVKRVGITRAHLEEDAGKLTHAKGEDGKKYSYADFNRAGVALLEIVTEPDLRTGREVAAYGSELRRIVRFLDACDGDMSRGSMRNDVNVSIRPVGRERFGTKVEVKNMNSFNAMARAIDYEIARQEELIRSGRGDEIVQETRTWDEAAQKTVAMRKKEGLADYRYFPEPDIPKLRLSEEFISNVVASMPELPSMVRARYAALGLPPADVQVLVEDKELVTYFDAALSSSAKPSAKQVANWLTGDIMAHLKNSKMENVSQLPLSPEALGEFCAMIDAGEISGKIGKDLLPELLEKGGSAKKLVADRGLSQVSDPREIEALVDGVLEANAGQLEQYRAGKTKLKGFFVGACLKASGGRANPSLVDRILQAKLDGVPIDVA", "text": "FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). SUBCELLULAR LOCATION: Mitochondrion Plastid, chloroplast. SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily."}
{"protein": "MSGGLAPSKSTVYVSNLPFSLTNNDLYRIFSKYGKVVKVTIMKDKDTRRSKGVAFILFLDKDSAQNCTRAINNKQLFGRVIKASIAIDNGRAAEFIRRRNYFDKSKCYECGESGHLSYACPKNMLGEREPPKKKEKKKKKKIPEPEEEIEEVEESEDEGEDPALDSLSQAIAFQQAKIEEEQKKWKPSSGGPSTSDDSRRPRIKKSTYFSDEEELSD", "text": "SUBCELLULAR LOCATION: Nucleus, nucleoplasm."}
{"protein": "MSSSRPASSSSSRNRQSSQARVLAQTTLDAELNAEYEESGDSFDYSKLVEAQRDGPPVQQGRSEKVIAYLQHIQKGKLIQTFGCLLALDEKSFNVIAFSENAPEMLTTVSHAVPSVDDPPRLGIGTNVRSLFSDQGATALHKALGFADVSLLNPILVQCKTSGKPFYAIVHRATGCLVVDFEPVKPTEFPATAAGALQSYKLAAKAISKIQSLPGGSMEMLCNTVVKEVFDLTGYDRVMAYKFHEDDHGEVFSEITKPGLEPYLGLHYPATDIPQAARFLFMKNKVRMICDCRARSIKVIEAEALPFDISLCGSALRAPHSCHLQYMENMNSIASLVMAVVVNENEEDDEAESEQPAQQQKKKKLWGLLVCHHESPRYVPFPLRYACEFLAQVFAVHVNREFELEKQLREKNILKMQTMLSDMLFREASPLTIVSGNPNIMDLVKCDGAALLYGGKVWRLRNAPTESQIHDIAFWLSDVHRDSTGLSTDSLHDAG", "text": "FUNCTION: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion. SIMILARITY: Belongs to the phytochrome family."}
{"protein": "MAASARRASQLLGSAASRLLHARGFAAAAAAAPSPAVFVDKSTRVICQGITGKNGTFHTEQAIEYGTTMVGGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPPPFAAAAIMEAMEAELDLVVCITEGIPQHDMVKVKAALNKQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGRVGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFVDDPQTEGIVLIGEIGGTAEEDAAAFIQESKTQKPVVAFIAGLTAPPGRRMGHAGAIVSGGKGTAQDKIKALREAGVTVVESPAKIGSTMFEIFKQRGMLE", "text": "FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family."}
{"protein": "MEVQTECSEPPPCDPQPPGKLNKAAFKLFGKRKSGSSMPSIFSVRNKGESTGKAAGKTLELVRSKTHDGLITDTPSELDSHRKEESASSDQLHAGTPDGVSTAPLRSSITKSFSFFSLLRRSSSRAGDGTTTVGRRGRGLKGLFSSMRWRRKPQIQEDTLEVAKEVKEGDLILSSSSGSVKTEKDMTLTLEPLPQVFEESPLPGDSDKWKVASMQGIQGTNEVECGNCGPSVSQQHTVTEESPAPSPLRVQTGGLQNHKHSSSTHLSSIPTCALTPPMEHSTADPQSEQSVDRLCSMFTDVTSLKSFDSLTGCGDIIADPEEDSGNGGSATSSGTGSSSGGCMGRRLSGAGTNSERCSPAKPPLPPQVSSLASIHASCYMPAHQRPRAAPKKPQGSGVVAYMGGGEEMASPEGVDDADMQGLWHMLPQKDEDSPAPRRAEPVLHHAPARLEKRPPQVKALGLSKIPVSGSSKTGKQQPSRPSPPPVDKELQDAPPSDEGYWDSPTPGPEDEDSTFLRRDGLLRDSCSGDALYDLYDPDSPSAAGSDDDASSPTKSAGDLKMNLPSPKCSSSATSSFRSMKGSTSLPRDSKIPISVRQTPPSHSSSQGALSSNLSPTSTTPPKKTDAPPRTKIPVSKVPVRRSGGKSTSTSQSRK", "text": "FUNCTION: Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Note=Translocates to the cell membrane following binding to PtdIns(4,5)P2. SIMILARITY: Belongs to the Amer family."}
{"protein": "MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSELFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSHNEST", "text": "FUNCTION: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules (By similarity). Through its action on microtubules, may participate in the refinement of axons by negatively regulating axonal and leading processes branching (By similarity). Plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus (By similarity). Regulates voltage-gated sodium channels transport and function (PubMed:15282281, PubMed:33245860). May also play a role in MAPK signaling (By similarity). Required for the development of axonal initial segment-targeting inhibitory GABAergic synapses made by chandelier neurons (By similarity). FUNCTION: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules (By similarity). Through its action on microtubules, may participate in the refinement of axons by negatively regulating axonal and leading processes branching (By similarity). Plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus (By similarity). Regulates voltage-gated sodium channels transport and function (By similarity). May also play a role in MAPK signaling (By similarity). Required for the development of axonal initial segment- targeting inhibitory GABAergic synapses made by chandelier neurons (By similarity). SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm Nucleus. SUBCELLULAR LOCATION: Cell projection, filopodium Cell projection, growth cone Cell projection, dendrite Cell membrane, sarcolemma Cytoplasm Note=Not secreted. Localizes to the lateral membrane and intercalated disks of myocytes. SUBCELLULAR LOCATION: Cell projection, filopodium Cell projection, growth cone Cell projection, dendrite Cell membrane, sarcolemma Cytoplasm Nucleus Note=Not secreted. Localizes to the lateral membrane and intercalated disks of myocytes. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Nucleus. SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm Nucleus. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm Nucleus. SIMILARITY: Belongs to the heparin-binding growth factors family."}
{"protein": "MTTAQFYCQYCTASLLGKKYVLKDDSLFCVTCYDRVFSNYCEECKKPIESDSKDLCYKDRHWHGGCFKCTKCNHSLVEKPFAAKDERLLCTECYSNECSSKCFHCKRTIMPGSRKMEFKGNYWHETCFVCENCRQPIGTKPLISKESGNFCVPCFEKEFAHYCNFCKKVITSGGITFCDQLWHKECFLCSGCRKDLCEEQFMSRDDYPFCVDCYNHLYANKCVACSKPISGLTGAKFICFQDSQWHSECFNCGKCSVSLVGKGFLTQNKEIFCQKCGSGMDSDI", "text": "FUNCTION: May be involved in the regulation of spermatogenesis. Stimulates CREM transcriptional activity in a phosphorylation- independent manner (By similarity). SUBCELLULAR LOCATION: Nucleus. Note=Nuclei of round and elongated spermatids."}
{"protein": "MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDQFLILLDVKHFSPEELTVKVLDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKVQSSMDDGHSERAIPVSREEKPSSVPSS", "text": "FUNCTION: Contributes to the transparency and refractive index of the lens. In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. SIMILARITY: Belongs to the small heat shock protein (HSP20) family."}
{"protein": "MSDEEVEHVEEQYEEEEEAQEEAPSPAEVHEPAPEVHVPEEVHEDALEDMREEEEEEEKPRPKLTAPKIPEGEKVDFDDIQKKRQNKDLMELQALIDSHFEARKKEEEELVALKERIEKRRAERAEQQRIRAEKERERQNRLAEEKARREEEDAKRRAEEDLKKKKALSSMGANYSSYLAKADQKRGKKQTAREMKKKILAERRKPLNIDHLSDEKLRDKAKELWDTLYQLETDKFEFGEKLKRQKYDIMNVRARVEMLAKFSKKAGTTAKGKVGGRWK", "text": "FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. SIMILARITY: Belongs to the troponin T family."}
{"protein": "MLKTSFLLSKRNAVSLSRVLATGISGRNVRHLTLQPSEHYDVAIVGGGIVGLATARELILRHPKLTFCVLEKEKELSMHQSGHNSGVIHCGIYYTPGSLKAKLCVQGLDLTYQYCDEHNIPYKKCGKLIVAVEDKEIPLLNNLYERGKKNGVKDLTMVDKRGIKEIEPHCEGMFAIVSPNTGIVDWAQVALAYGDDFRKGGGDIFTGYEVTDFKCASESGKSQEKEAGLTHPVTVFSNNKQTIKCRYVITCGGLYSDRLAEKSGCNREPRIVPFRGDYLVLKPEKCHLVKGNIYPVPDPNFPFLGVHFTPRMDGSVWLGPNAVLAFAREGYNLLDINLRDLADALAFRGLRQLMFKYFSFGVGEYYRGLNHAAQVKQLQKYIPSVTADDVVSGPSGVRAQALDRDGNLVDDFVFDGGVGEIGSRVLHVRNAPSPAATSSLAIARMVADKAAERFTL", "text": "SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the L2HGDH family."}
{"protein": "MSACQSPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGVWMVNVHCSGGLRMMAACRETLEAFSGPRPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAQKAGMDGLVCSAQEAPALKAAHPGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPISQAADPAKALAAIVAELG", "text": "FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily."}
{"protein": "MKKKLAAGLTASAIVGTTLVVTPAEAATIKVKSGDSLWKLAQTYNTSVAALTSANHLSTTVLSIGQTLTIPGSKSSTSSSTSSSTTKKSGSSVYTVKSGDSLWLIANEFKMTVQELKKLNGLSSDLIRAGQKLKVSGTVSSSSSSSKKSNSNKSSSSSSKSSSNKSSSSSSSTGTYKVQLGDSLWKIANKVNMSIAELKVLNNLKSDTIYVNQVLKTKSSGSDTSSKDNSSKSNQTSATTKYTVKSGDSLWKIANNYNLTVQQIRNINNLKSDVLYVGQVLKLTGKASSGSSSSSSSSSNASSGTTTTYTVKSGDSLWVIAQKFNVTAQQIREKNNLKTDVLQVGQKLVISGKASSSSSSGSSNTTSSTSAKINTMISAAKAQLGVPYRWGGTTPSGFDCSGFIYYVLNKVTSVSRLTAAGYWNTMKSVSQPAVGDFVFFSTYKAGPSHVGIYLGNGEFINANDSGVVISNMNNSYWKQRYLGAKRYF", "text": "FUNCTION: Cell wall hydrolase that cleaves gamma-D-glutamate-meso- diaminopimelate bonds in peptidoglycan. LytF is necessary and sufficient for vegetative daughter cell separation, and also seems to play a role in cell autolysis. SUBCELLULAR LOCATION: Secreted, cell wall Note=LytF is localized at cell separation sites and cell poles of rod-shaped cells during vegetative growth. SIMILARITY: Belongs to the peptidase C40 family."}
{"protein": "MSPSATDNSDGPDATVLTLRKVLTSESEPLARRFRALFSLKYLACQQPATEKTLPAIQAIAAAFTSPSALLKHELAYCLGQTRNPESVPYLQEVVKDTEQDTMCRHEAAEALGALGYEDSLEILKVLRDNKDEPDVIRETCDIAVDRILWENSEQRKAEKLKASDFTSIDPAPPLPMATSEPSIPDIEKRLLDTSLPLFQRYRAMFALRDLASPPDLPTATHAVEALAKGLKDPSALFRHEIAFVFGQLSHPASIPSLTEALSDQNEVGMVRHEAAEALGSLGDCEGVEDTLKKFLNDPEQVVRDSVIVALDMAEYEKNGEIEYALVPDSGVAAA", "text": "FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L- lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the deoxyhypusine hydroxylase family."}
{"protein": "MASLFAIGFSKFSPQPTSDYSKLLKVFHPKPYSLKFLFLKTLNPTRFFKVRANDGTEPSDKLQQYFQNQDYDKKYGFLENIDSFTIPKGLSEETIRLISKLKKEPAWILEYRLKAYAKFLKLEEPKWSDNRYPLLDLQDMCFYSAPKKKPTLNSSDIADEADDPKLLEEFDRLDVPLTKKKKCSPKVAVDAVYNSESIAITNKEPLEKSGVIFCSISEAIRKYPDLIKKYLGRVVPSDDNYYAALNTAVFSDGSFCYIPKNTRCPMPLSSYFRMNSIENTGQFERTLIVAEEGSFVEYSEGCTAISHDKNQLHAAVVELYCAEGAEIKYSTRGLCAGDRSKISWTQVEKGFAITWKYPSVVLEGDDSVGEAENARNTSTCDSMLIGDNAAANTYPYIQVKNPSARIEHEASTSKIGEDQIFYFQQRGIDHERALAAMISGFCRDVFNKLPNEFGAEVNQLLSIKLEGSVG", "text": "SIMILARITY: Belongs to the UPF0051 (ycf24) family."}
{"protein": "MASHASCIFCKIIKGEIPSFKLIETAKTYSFLDIQPIAEAHVLIIPKHHGAKLHNIPDDYLSDILPVVKKLTKVLKLDENNTPEGEGYNVLQNNGRIAHQVVDHVHFHLIPKKDEATGLGVGWPAEATDFDKLGKLHEKLKEELAKVDNEKL", "text": "FUNCTION: Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2. SIMILARITY: Belongs to the HINT family."}
{"protein": "MSCCGGSCGCGSACKCGNGCGGCKRYPDLENTATETLVLGVAPAMNSQYEASGETFVAENDACKCGSDCKCNPCTCK", "text": "FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals (Probable). Functions as metal chelator of copper (Cu) and zinc (Zn). Functions cooperatively with the phytochelatin synthase PCS1 to protect plants from Cu and cadmium toxicity (PubMed:18287486). Plays a role in Cu homeostasis, specifically in the remobilization of Cu from senescing leaves. The mobilization of Cu from internal sources is important for seed development (PubMed:24635746). SIMILARITY: Belongs to the metallothionein superfamily. Type 15 family."}
{"protein": "MPESLIAGIPVHFPFEPYPVQRAYMEKVIQCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRTRQSEHQQQMVKIEKADFSGLAGGATGGELSDLGKTMGRANNWGVPKVIYASRTHSQLTQAMRELKRTAYANMRSVVLGSRDQLCIHPEVMREQGNSNKTNMCKLRVHSKTCTFQMRVESRKDHPDLRGPSIMDIEDLVKVGQRLKICPYFASRELVPQADITFMPYNYLLDPKARKANKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDVTHIMQVFASGESQDMAGDEPKDFTLDDLTLLKEMLLELEKAIDAVVVDNAAEGTTFPASLMYELLGKANFTYGNVATIVSLLDKLVQYLLVASQQMSIRKGGTFTMLSDLLTIVFANKQDVMSKVYASFKVHVQMEESKQGHGKQQGAKQQGGWLGKGTIAAASGTSKVAKIINFWCFNPGFGMEQLLNTQVRSVILTSGTLAPLKPLIAELAIPVAQHLENPHIVDQSQVYVKIIGTGPDRQQLISNYANRDNPKYISSLGQTILNVSRIVPDGLLVFFPSYPMLNKCVDAWQASGLWADISCKKPIFLEPRSKDQFTSTMEEFYQAIRDSKGAVFMAVCRGKVSEGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANRTRENQLLSGQEWYNLDATRAVNQAIGRVIRHRNDYGAILLCDSRFKDASQVQQLSKWIRGHLGDRPQCSPFGPIVRELRQFFKNAEANMKLPDERETDAPLETVCKTEDEPLAAIPKLKREPGSNATFKSANESAIKVEMANSIKTWTPADYASAAGRKLGGAAPSAMDFMSRLDSNVSSIDFNCCTDSKSGSSDLVKIHKRERSSPTLPESSSQVSKKRYKLVENIKVEPSSSQAKAAPEERADFLRALRSLVTQDQFRRFGKALLEYKNGTYESFQDLMAILLDVLSAPKVRYMLVGMRKYLKNEHKDEFDRRVGSL", "text": "FUNCTION: ATP-dependent DNA helicase implicated in DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily."}
{"protein": "METMLFSPYTIRGVTIKNRIVMSPMCMYSCDTEDGKVRNWHKIHYPTRAVGQVGLIIVEATAVAAQGRISSRDLGIWSDEHVDGLRELASLVKEHGAKIGIQLAHAGRKSEVDGEIIAPSAIPFSEKTRTPKEMTKADIEETIQAFQNGARRAKEAGFDIIEIHGAHGYLINEFLSPLSNRRQDEYGGSPENRYRFLGEIIDAVREVWDGPLFVRISASDYHPEGLTVKDYVPYAKRMKEQGVDLIDVSSGAVVPAKIRVYPGYQVPFAETIRREANIATGAVGLITSGLQAEEILRNGRADLVFLARELLRNPYWPYAAAKELGTTISASVQYERGWRF", "text": "FUNCTION: Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes. SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily."}
{"protein": "MAAFSSSSSAPMLIRSVLFVSLLSAAFVFDSGEAGAAHRVVDPEWHPATATWYGSADGDGSDGGACGYGTLVDVVPMKTRVGAVSPVLFKGGEGCGACYKVRCLDASICSRRAVTVIVTDECPGGVCAFGRTHFDLSGAAFARLAVAGHGGQLQNRGEISVVYRRTACKYGGKNIAFHVNEGSTTFWLSLLVEFEDGDGDIGSMQLKQANSAQWQDMKHIWGATWSLTPGPLVGPFSVRLTTLTTRQTLSAQDVIPKNWTPKATYTSRLNFA", "text": "FUNCTION: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin B subfamily."}
{"protein": "MAAGTLYTYPENWRAFKALIAAQYSGAQVRVLSAPPHFHFGQTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYVSNEELRGSTPEAAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVRRILGLLDAHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAVLGEVKLCEKMAQFDAKKFAETQPKKDTPRKEKGSREEKQKPQAERKEEKKAAAPAPEEEMDECEQALAAEPKAKDPFAHLPKSTFVLDEFKRKYSNEDTLSVALPYFWEHFDKDGWSLWYSEYRFPEELTQTFMSCNLITGMFQRLDKLRKNAFASVILFGTNNSSSISGVWVFRGQELAFPLSPDWQVDYESYTWRKLDPGSEETQTLVREYFSWEGAFQHVGKAFNQGKIFK", "text": "FUNCTION: Probably plays a role in anchoring the complex to other cellular components."}
{"protein": "MASTALSTASNPTQLCRTRASSLCKPVKGLGFGRERIPRNITCMAGSISADRVPDMSKRELMNLLLLGAISLPTFGMLVPYGSFLVPAGSGSNAGGVAAKDKLGNDILVEDWLKTHGPNDRTLAQGLKGDPTYLVVESDKTLATYGINAVCTHLGCVVPWNAAENKFLCPCHGSQYNNQGKVVRGPAPLSLALVHADVDDGKVVFVPWVETDFRTGDNPWWK", "text": "FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer. SIMILARITY: Belongs to the Rieske iron-sulfur protein family."}
{"protein": "MRSALPLVLFSLVALCGRGDCRVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIQLQLSLAQLISVNEREQIMTTNIWLKQEWTDYRLAWNSSRYEGVNILRIPANRVWLPDIVLYNNADGSYEVSLYTNVVVRSNGSVMWLPPAICKSACKIEVKHFPFDQQNCTLKFRSWTYDHTEIDMVLKMPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLNVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFIKRPRQQPSRAPQSSLARLTKSEATTTTTLAMGPTSSSNLYGNSMYFVNPGLAAPKSPVASDSAGIPRDFRLRSSGRFRQDVQEALEGVSFIAQHMKSDDLDQSVIEDWKYVAMVVDRLFLWVFVVVCVLGTVGLFLPPLFQTHTPSEEP", "text": "FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi- pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-4/CHRNB4 sub- subfamily."}
{"protein": "GNATSERLPTDPVYPXV", "text": "FUNCTION: Putative component of the large subunit of mitochondrial ribosome. SUBCELLULAR LOCATION: Mitochondrion."}
{"protein": "MGIQGGSVLFGLLLILAVFCHSGHSLQCYSCPYSTARCTTTTNCTSNLDSCLIAKAGLRVYYRCWKFEDCTFRQLSNQLSENELKYHCCRENLCNFNGILENGGTTLSKKTVLLLVTPFLAAAWSLHP", "text": "FUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor."}
{"protein": "MATIHKLFKSPFFDFEFLRLLAMAPYEGAEIGEVLEAAAKIKDQDPESWYSTLLETGGKAEAIAKQAEASGDRVGARRAYLRSSNYLRAAQFMLNEGPIGHDERVLPTLERAIANFRKGVQYRDGKTIFLEIPYEGGKTLPGYLYLPPAARRIPGRKIPILLNSGGGDSTQEEIYFVNPAYGPDLGYAVLTFEGPGQGIVLRRDKLPMRPDWESVTGPVLDHLFDLATRHPELELDLDHIAVTGASMGGYFALRAAADPRIKACVSVDGFYSLSSFVGGRMPGPLFNGFMSGWLSDWMFNGILGVLKKLAFQARWEFNHLRWATGSTTDADVMRSFGAYTLQKADGTEYLADVKCPTLVTGAGASFYFDPATTTDKIYDCLTSLQDGVDKEKWIATDVAYGGLQAKIGAFGYSAQKTFEWLDQRFGIQREPLAASSRLEDLVSRL", "text": "FUNCTION: Alpha/beta hydrolase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L- phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual- functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566). SIMILARITY: Belongs to the AB hydrolase superfamily. FUS2 hydrolase family."}
{"protein": "MERSPDVSPGPSRSFKEELLCAVCYDPFRDAVTLRCGHNFCRGCVSRCWEVQVSPTCPVCKDRASPADLRTNHTLNNLVEKLLREEAEGARWTSYRFSRVCRLHRGQLSLFCLEDKELLCCSCQADPRHQGHRVQPVKDTAHDFRAKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGRIRQEFDKLREFLRVEEQAILDAMAEETRQKQLLADEKMKQLTEETEVLAHEIERLQMEMKEDDVSFLMKHKSRKRRLFCTMEPEPVQPGMLIDVCKYLGSLQYRVWKKMLASVESVPFSFDPNTAAGWLSVSDDLTSVTNHGYRVQVENPERFSSAPCLLGSRVFSQGSHAWEVALGGLQSWRVGVVRVRQDSGAEGHSHSCYHDTRSGFWYVCRTQGVEGDHCVTSDPATSPLVLAIPRRLRVELECEEGELSFYDAERHCHLYTFHARFGEVRPYFYLGGARGAGPPEPLRICPLHISVKEELDG", "text": "FUNCTION: E3 ubiquitin-protein ligase that participates in multiple biological processes including cell death, glucose metabolism, and in particular, the innate immune response. Mediates 'Lys-63'-linked polyubiquitination of TRAF3 thereby promoting type I interferon production via RIG-I signaling pathway (PubMed:32562145). Can also catalyze 'Lys-48'-linked polyubiquitination and proteasomal degradation of viral proteins such as influenza virus PB2 (PubMed:32562145). Acts as a negative feedback regulator of TLR7- and TLR9-triggered signaling. Mechanistically, promotes the 'Lys-48'-linked ubiquitination of IRF7 and induces its degradation via a proteasome-dependent pathway (PubMed:25907537). Reduces FGFR1-dependent tyrosine phosphorylation of PKM, inhibiting PKM-dependent lactate production, glucose metabolism, and cell growth (PubMed:25263439). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Found predominantly in cytoplasm with a granular distribution. Found in punctuate nuclear bodies (By similarity). SIMILARITY: Belongs to the TRIM/RBCC family."}
{"protein": "MSALPNYFRITALLRTQRYGLAIGLLFMAPSVWAQLPGIVTQPLPNGGQSWTLSVQTLVLLTSLTFLPAALLMMTSFTRIIIVLSLLRNALGTPTAPPNQVLLGLTLFLTFFVMSPVLNRVYDEAYLPFSQDQISMEVAIERGAEPVREFMLRQTRETDLALFTRLAEIPEIQGPEAVPMRVLLPAFVTSELKTAFQIGFTVFIPFLIIDLVVASVLMALGMMMVPPATISLPFKLMLFVLVDGWQLLLGSLAQSFYS", "text": "FUNCTION: Plays a role in the flagellum-specific transport system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Bacterial flagellum basal body. SIMILARITY: Belongs to the FliP/MopC/SpaP family."}
{"protein": "NLYQFGNMIQCANHGRRPTRHYMDYGCYCGKGGSGTPVDELDRCCQTHDDCYGEAEKLPACNYMMSGPYYNTYSYECNEGELTCKDNNDECKAFICNCDRTAAICFARAPYNDANWNIDTKTRCQ", "text": "FUNCTION: Snake venom phospholipase A2 (PLA2) that blocks neuromuscular transmission, but that does not produce blockade by virtue of a selective action on nerve endings. Instead, the toxin acts both on nerve and on muscle. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily."}
{"protein": "MHKNGNNGPVIDTKWHYLGPDSEKYGPYMSKDMLFWLQAGYFNDGLQLKTENEPNYHTLGEWSQLLGTHPFSMPVHSLDATIAQMNSMRPHGAMMMVPPGLQNQFQPPMPMRFPPFLPMPLLHQMNQNGPPMGAQMHSQPPSEPIDAGSLSHTPDSENETRLNEQTLQQPPSWLIALGLAGHGRKPHHHQQILAHQHIPQMQHANVATDQVVMKSVECQTEPVEISKEQASRVLSELLGQMVIIN", "text": "FUNCTION: Involved in negative regulation of early and late embryonic Notch signaling."}
{"protein": "MVSRRVQALLDQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLETGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA", "text": "FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. L- isoaspartyl/D-aspartyl protein methyltransferase family."}
{"protein": "MIKFLSALILLLVTTAAQAERIRDLTSVQGVRQNSLIGYGLVVGLDGTGDQTTQTPFTTQTLNNMLSQLGITVPTGTNMQLKNVAAVMVTASLPPFGRQGQTIDVVVSSMGNAKSLRGGTLLMTPLKGVDSQVYALAQGNILVGGAGASAGGSSVQVNQLNGGRITNGAVIERELPSQFGVGNTLNLQLNDEDFSMAQQIADTINRVRGYGSATALDARTIQVRVPSGNSSQVRFLADIQNMQVNVTPQDAKVVINSRTGSVVMNREVTLDSCAIAQGNLSVTVNRQANVSQPDTPFGGGQTVVTPQTQIDLRQSGGSLQSVRSSASLNNVVRALNALGATPMDLMSILQSMQSAGCLRAKLEII", "text": "FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Periplasm. Bacterial flagellum basal body. SUBCELLULAR LOCATION: Periplasm Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgI family. SIMILARITY: Belongs to the FlgI family."}
{"protein": "MDIQQGGNDLISLAATIRTELQQKLSSKARIHLPFDEDRTEFDKANLRFTQYERPTYLAIVDPVCEDDVIEAVKYARGKGIPFTPRGGHHSVTTTMGRFQNGICINMRPLNQMRWYAEKRHVTIGGGAITDEFVRFVHDLGMEVTFGAGLGRLQGKYGFLNDNMVSCKLVLADGSTVIASKDSHPDLFWALRGAGHNFGIALEATFQVYPQAHGGIHHTWDLEYTLDQCDEVFRTLNSVYESMPAELAIFILWLRQSSGRKHIILVNLVWSGPAAGADPYVQRFESLQPVLNSGRKSVPWPELPFSTYKEINKLFCNPEIWLRGPYKMMGAACVERFDLKTTREFFESVKSLSEEWEDRGWFSAMFECLPDQRVREISDDATAFPWRAGSNHFLMLNATPKRMEDRKVFEDHLNYWKRRFIETSGYGRLQQYVSYGNGTSTMKDPPEALYGYEPWRLEKLRNLKQKYDPDNVFRWYQPLLEP", "text": "FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of alternapyrone derivatives (PubMed:16356847). Alternapyrone is a decaketide with octa-methylation from methionine on every C2 unit except the third unit (PubMed:16356847). All the domains in the polyketide synthase alt5 are apparently involved in alternapyrone synthesis, that is, the 8 CMeT, 7 KR, 7 DH, and 4 ER reactions in the 9 KS-mediated condensation steps required for alternapyrone synthesis (PubMed:16356847). the alternapyrone produced by alt5 might be intensively modified by cytochrome P450 monooxygenases alt1, alt2 and alt3 and FAD-dependent oxidoreductase alt4 present in the alt gene cluster (PubMed:16356847). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family."}
{"protein": "VLLLSQDYGKYKEVAELTRTQILAASYELHK", "text": "FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Plays a critical role in central nervous system development and function. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, myofibril, sarcomere, M line Cytoplasm, cytosol Cell membrane Note=Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes. SIMILARITY: Belongs to the spectrin family."}
{"protein": "MTTGLSTAGAQDIGRSSVRPYLEECTRRFQEMFDRHVVTRPTKVELTDAELREVIDDCNAAVAPLGKTVSDERWISYVGVVLWSQSPRHIKDMEAFKAVCVLNCVTFVWDDMDPALHDFGLFLPQLRKICEKYYGPEDAEVAYEAARAFVTSDHMFRDSPIKAALCTTSPEQYFRFRVTDIGVDFWMKMSYPIYRHPEFTEHAKTSLAARMTTRGLTIVNDFYSYDREVSLGQITNCFRLCDVSDETAFKEFFQARLDDMIEDIECIKAFDQLTQDVFLDLIYGNFVWTTSNKRYKTAVNDVNSRIQ", "text": "FUNCTION: Catalyzes the cyclization of the linear isoprenoid intermediate geranylgeranyl diphosphate to tricycclic cyclooctat-9-en- 7-ol in the cyclooctatin biosynthesis pathway. Cyclooctatin is a potent inhibitor of lysophospholipase. SIMILARITY: Belongs to the terpene synthase family."}
{"protein": "MDYDLLRSKKSIKRVESTKSNPWWWDSHIGLKNSKWLENNLDEMDRSVKRMVKLIEEDADSFAKKAEMYYQSRPELIALVDEFHRMYRALAERYENITGELRKGSPLELQSQGSGLSDISASDLSALWTSNEVNRLGRPPSGRRAPGFEYFLGNGGLPSDLYHKDGDDSASITDSELESDDSSVTNYPGYVSIGSDFQSLSKRIMDLEIELREAKERLRMQLEGNTESLLPRVKSETKFVDFPAKLAACEQELKDVNEKLQNSEDQIYILKSQLARYLPSGLDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEEKIHRDDQFKELEANVRYLEDERRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRCIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEKREVIRQLCFSLDYSRDEYKRLRIAFSGHPPTRPSSILAS", "text": "FUNCTION: Plant-specific actin binding protein. Associates with F-actin at the tonoplast. May be part of a membrane-cytoskeletal adapter complex. SUBCELLULAR LOCATION: Vacuole membrane Note=Arranged into short filaments and foci. SIMILARITY: Belongs to the NET family."}
{"protein": "MRQTIKYEFWVGLFLLLGIGALVFLGLRVANVQGFAETKSYTVTATFDNIGGLKVRAPLKIGGVVIGRVSAITLDEKSYLPKVSIAINQEYNEIPENSSLSIKTSGLLGEQYIALTMGFDDGDTAMLKNGSQIQDTTSAMVLEDLIGQFLYGSKKSDGNEKSESTEQ", "text": "FUNCTION: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the MlaD family."}
{"protein": "MAIELNQIWDFPIKEFHPFPRALLGVGAHDIIGVEAKNLGFKRTLLMTTGLRGSGIIEELTGKIEYQGVEVVLYDKVESNPKDYNVMEAAALYQQERCDSIISIGGGSSHDAAKGARVVIAHDGRNINEFEGFAKSTNKQNPPHIAVSTTAGTGSETSWAYVITDTSDMEHPHKWVGFDEATIVTLAIDDPLLYYTCPQHFTAYCGFDVLAHGSEPYVSRLDFAPSLGNALYSVELVAKHLREAVFEPRNLKAREGMMNAQYIAGQAFNSGGLGIVHSISHAVSAFFDSHHGLNNAIALPRVWEYNLPSRYERYAQLATAMGVDTRNMTTVQAADAAVEAAIRLSQDVGIPDNFSQVRVDSYDKNRMNTGKYAGKGEVIKGDDKSVLAISEHIQGDWCTPGNPREVTVDSMIPVVGHAINGTY", "text": "FUNCTION: Catalyzes the oxidation of methanol to yield formaldehyde. While the in vivo electron acceptor is not known, N,N-dimethyl-4- nitrosoaniline (NDMA) can serve this function in vitro and is reduced to 4-(hydroxylamino)-N,N-dimethylaniline. It is also able to use ethanol and formaldehyde with an activity comparable to methanol, and has a weak activity with methylamine as substrate. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family."}
{"protein": "MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELQNASRTPSGTLVRVQLLGQFPQWLAENAARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVSVKVRLGWDSGEKKFEIADAVQQAGATELVVHGRTKEQGYRAEHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYNEPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLSYLRKEYDEATELFQHVRVLNNSPDIARAIQAIDIEKL", "text": "FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. DusC specifically modifies U16 in tRNAs. SIMILARITY: Belongs to the Dus family. DusC subfamily."}
{"protein": "MSDAQDSRVGSMFGPYHLKRLLGRGGMGEVYEAEHTVKEWTVAVKLMTAEFSKDPVFRERMKREARIAGRLQEPHVVPIHDYGEVDGQMFLEMRLVEGTDLDSVLKRFGPLTPPRAVAIITQIASALDAAHADGVMHRDVKPQNILITRDDFAYLVDFGIASATTDEKLTQLGTAVGTWKYMAPERFSNDEVTYRADIYALACVLHECLTGAPPYRADSAGTLVSSHLMGPIPQPSAIRPGIPKAFDAVVARGMAKKPEDRYASAGDLALAAHEALSDPDQDHAADILRRSQESTLPAPPKPVPPPTMPATAMAPRQPPAPPVTPPGVQPAPKPSYTPPAQPGPAGQRPGPTGQPSWAPNSGPMPASGPTPTPQYYQGGGWGAPPSGGPSPWAQTPRKTNPWPLVAGAAAVVLVLVLGAIGIWIAIRPKPVQPPQPVAEERLSALLLNSSEVNAVMGSSSMQPGKPITSMDSSPVTVSLPDCQGALYTSQDPVYAGTGYTAINGLISSEPGDNYEHWVNQAVVAFPTADKARAFVQTSADKWKNCAGKTVTVTNKAKTYRWTFADVKGSPPTITVIDTQEGAEGWECQRAMSVANNVVVDVNACGYRITNQAGQIAAKIVDKVNKE", "text": "FUNCTION: May regulate bacterial growth in response to external signals to facilitate adaptation to the host environment. In vitro, phosphorylates several substrates such as EmbR, DevR (DosR), DacB1 and Rv0681. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family."}
{"protein": "MLLYKDVISGDELVSDAYDLKEVDDIVYEADCQMVTVKQGGDVDIGANPSAEDAEENAEEGTETVNNLVYSFRLSPTSFDKKSYMSYIKGYMKAIKARLQESNPERVPVFEKNAIGFVKKILANFKDYDFYIGESMDPDAMVVLMNYREDGITPYMIFFKDGLVSEKF", "text": "FUNCTION: Involved in calcium binding and microtubule stabilization (By similarity). May be a guanine nucleotide-free chaperone (GFC). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCTP family."}
{"protein": "MPKLIWIPESVVEAMLKDASRWHDLETGGTFMGYWSDANVAVITKMIDGGSEAIRTRKSFSPDREWEQSEIDRHYRVSGRVDTYIGDWHTHPNAQSGEPSWTDRRCLRTIIRSPEARAPRPVMILLCGGPENWLPHAWIGQLTRRALLFERVETTAATISTYKT", "text": "SIMILARITY: Belongs to the peptidase M67B family."}
{"protein": "MRLGVLDVGSNTVHLLVVDAHRGGHPTPMSSTKATLRLAEATDSSGKITKRGADKLISTIDEFAKIAISSGCAELMAFATSAVRDAENSEDVLSRVRKETGVELQALRGEDESRLTFLAVRRWYGWSAGRILNLDIGGGSLEVSSGVDEEPEIALSLPLGAGRLTREWLPDDPPGRRRVAMLRDWLDAELAEPSVTVLEAGSPDLAVATSKTFRSLARLTGAAPSMAGPRVKRTLTANGLRQLIAFISRMTAVDRAELEGVSADRAPQIVAGALVAEASMRALSIEAVEICPWALREGLILRKLDSEADGTALIESSSVHTSVRAVGGQPADRNAANRSRGSKP", "text": "FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Prefers short-chain length polyphosphates as substrates. Can also hydrolyze ATP and ADP substrates, but lacks GTPase activity. Cannot hydrolyze pppGpp to ppGpp. FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Required for long-term survival of M.tuberculosis in necrotic lung lesions. SIMILARITY: Belongs to the GppA/Ppx family."}
{"protein": "MEEECRVLSIQSHVVRGYVGNRAATFPLQVLGFEVDAVNSVQFSNHTGYSHWKGQVLNSDELQELYDGLKLNHVNQYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVMGDQRNGEGAMYVPDDLLPVYREKVVPVADIITPNQFEAELLTGRKIHSQEEALEVMDMLHSMGPDTVVITSSNLLSPRGSDYLMALGSQRTRAPDGSVVTQRIRMEMHKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSAMHHVLQRTIKCAKAKSGEGVKPSPAQLELRMVQSKKDIESPEIVVQATVL", "text": "FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (PubMed:14722069) (By similarity). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the pyridoxine kinase family."}
{"protein": "MGQTITTPLSLTLDHWSEVRARAHNQGVEVRKKKWITLCEAEWVMMNVGWPREGTFSLDNISQVEKKIFAPGPYGHPDQVPYITTWRSLATDPPSWVRPFLPPPKPPTPLPQPLSPQPSAPLTSSLYPVLPKSDPPKPPVLPPDPSSPLIDLLTEEPPPYPGGHGPPPSGPRTPTASPIASRLRERRENPAEESQALPLREGPNNRPQYWPFSASDLYNWKSHNPPFSQDPVALTNLIESILVTHQPTWDDCQQLLQALLTGEERQRVLLEARKQVPGEDGRPTQLPNVIDETFPLTRPNWDFATPAGREHLRLYRQLLLAGLRGAARRPTNLAQVKQVVQGKEETPAAFLERLKEAYRMYTPYDPEDPGQAASVILSFIYQSSPDIRNKLQRLEGLQGFTLSDLLKEAEKIYNKRETPEEREERLWQRQEERDKKRHKEMTKVLATVVAQNRDKDREESKLGDQRKIPLGKDQCAYCKEKGHWVRDCPKRPRKKPANSTLLNLGD", "text": "FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre- integration complex (PIC) which tethers the latter to mitotic chromosomes. FUNCTION: [Matrix protein p15]: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex. FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex. FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4- like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release. FUNCTION: [Nucleocapsid protein p10-Gag]: Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization. SUBCELLULAR LOCATION: [Gag polyprotein]: Virion Host cell membrane; Lipid-anchor Host late endosome membrane; Lipid-anchor Host endosome, host multivesicular body Note=These locations are probably linked to virus assembly sites. SUBCELLULAR LOCATION: [Matrix protein p15]: Virion. SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Gag]: Virion. SUBCELLULAR LOCATION: [Capsid protein p30]: Virion. SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm Note=Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on."}
{"protein": "MESESHWLWLFNTESGKLSVKLSDTDVFDTPYKPSQLVNIHFNEQMMDIEDATTFQIVSETLEAYPADKMPCAPQNAALNATAWCRFGRPQMPQSWHFQKSDISEWPLERRLCELNSGFDQGLFLILDTDDEFATCLLLSEGMQLSAIKSLRQYHVIKVTLNRLLPATVDLALSAQSNWGQQLA", "text": "FUNCTION: Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ZapC family."}
{"protein": "NQKCSGNPRRYNGKSCASTTNYHDSHKGACGCGPASGDAQFGWNAGSFVAAASQMYFDSGNKGWCGQHCGQCIKLTTTGGYVPGQGGPVREGLSKTFMITNLCPNIYPNQDWCNQGSQYGGHNKYGYELHLDLENGRSQVTGMGWNNPETTWEVVNCDSEHNHDHRTPSNSMYGQCQCAHQ", "text": "FUNCTION: Active towards the soluble carboxymethylcellulose (CMC). Possesses expansin activity too. SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family."}
{"protein": "MGDSPKCLRDSLREALRRREDKLCRRKLTILPSSSVDFSSNDFLSLSTSPAYRARFLDILQQAPPLHPFASGGSRLLDGNSAYAEELENFIAAFHNAPSGLLFNSGYDANVGVFSSIPQPGDLIVYDELIHASAHEGMRLSRAGKRIKFPHSSPDGLRAVLQAEITADPRLLQGRRNVFIAFESVYSMDGDVAPIREFVEIVDQLLPYGNGYFLVDEAHATGVFGPRGSGVVQELGLEDRMFVRVHTFGKALASHGAIVLCCADTRDYLINYARSLIYTTALGFPFLASIRAAYELLVEGKTEQLQHKLGQLIAHFRTGLDNLNHKDSSTFEVEHFTNSPIFSLRSSVPRVLASVCQEQGYTVRAIMPPTVPAGKERVRVCLHAGNTVEEVDGLLETIATWLQRMEKQKARL", "text": "FUNCTION: 8-amino-7-oxononanoate synthase; part of the cluster involved in the biosynthesis of biotin (also known as vitamin B8 or vitamin H), a water-soluble vitamin that functions as a prosthetic group of many carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase (PubMed:20713166). Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7- oxononanoate (AON) (By similarity). SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily."}
{"protein": "MGKFQSKHAAAACKRRESPEGDSFVVPAYGSGRRGAEETDRRAGSGVEHRSRDKQELLNGDPKEGPFWDDKGSLEVVLPPEKSEGHEGQGQLFSTDDGEKAASREGPLRLSKKHLNIDALQCDVSVEEDNRQEWTFTLYDFDNSGKVTREDMSSLMHTIYEVVDASVNHSSGSSKTLRVKLTVSPEPSSKKECPLTGQDREPTRGRTEIELTDEPRVADRRLSAYSRKPNADPQPCSVRVPYCVDENTERRNHYLDLAGIENYTSKFGPGSPPEQARQEHHGRATHIPSRSRSQESDAHAIHHRRSQVLAEHVIPANEPATRALAAQPRIKGQEKQFLRSPKGPGKPLGTPGSGKPGKALSYCLQAVPLPQSAQDGHHLPQPPPQPPPQPYGHKRYRQKAREGHSPLKGHGQPTMVEHEVVRDLPPMLGPEGYVMPVVQRHEHHHHHEHHHHHHHHHFHPS", "text": "FUNCTION: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity. Required for processing of TGFA and for targeting of TGFA to the basolateral membrane of polarized epithelial cells (By similarity). SUBCELLULAR LOCATION: Cell membrane Cytoplasm Cytoplasmic vesicle. SIMILARITY: Belongs to the NKD family."}
{"protein": "MDVAKQFSSYLKQENKTENTVQGYTSGIRQYIKWFEGSYDRKLTKLYRQNILEYISYLKNVKMLNAKSINHKISSLAKFNEFLIQKGSQQDQVILKTDMIKVQTVYASPTQIVELDVKKFLQSVLEDNNKRNYAIATLLAYTGVRISEALSIKMNDFNLQTGECIIRSGKGGKQRIVLLNSKVLSAIKDYLIDRKTYSTAHESPYLFISKKREKLDRTVVNRIFKSYSNVITPHQLRHFFCTNAIEKGFSIHEVANQAGHSNIHTTLLYTNPNQLQLKNKMELL", "text": "FUNCTION: Resolvase catalyzes the resolution (a site-specific recombination) of the cointegrated replicon to yield the final transposition products. SIMILARITY: Belongs to the 'phage' integrase family."}
{"protein": "MAVLAALLRGGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPTTKLGSIAMQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPARQAVLGAGLPISTPRTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARDEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTITAANASTLNDGAAALVLMTAGAAKRLNVTPLARIVAFADAAVEPIDFPIAPVHAVSMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL", "text": "FUNCTION: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA. Thereby, it plays a major role in ketone body metabolism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family."}
{"protein": "MTDTTVAVPGAVRLNTATVTQYLSSQSSLVASLTGDGGGRRRAVLLRSAPQWDGPAEPAWGEGRTAGIAVAPSPLAVHELVLDHLAARRPGPPVLVVLTDREQHELDPAILARVHKLRIDTVDGWDVVREAFGARQIDPRLKDVNWAAEALLDATPPGSWPAVPGGWLSRQYALTALAQRRLRLGRYDTEGGPRRPGDDRLDAQALLHWSTRPGAPERLLTLRGPERAGLTAFLGEEDQAGLAGRTLLALVDAERGEDAAAFGLVCAALWQHAEPAPETYRARGRAERYFGDRPPATGDQLDALVTVFGRATEEHVTTLLAAGHRTAGTDADQAREARRTTGTVLDRAAALARQFGAEEAVAASPVLRGGLEARFTAVGRALAAGDTTAVADAVRRLENHRLAAEPEESARIERARMGQRLARWLATDPPTDALTVADALRRHVAETGWADLALEHIEAGGDQGPVLKAAYDTLGTRVRDRRRQIDASFARSLAAWTQSGTQPGSMLTVETFLDRVVGPLVRRGEERRTLMLVLDGMSAAIANELGEELRRSWAEFDPLPEGDTPYRRAMAAALPTVTAVSRTSLFAGTLTKGTQADEKRLFPALKLWGGAPAAVFHKDDLRTETAGETFGPALTEALADGRTHVAVVLNAIDDRLAKEQKLGDGAWRIDDVPGLRDLLRVAATQGMAVVLTSDHGHVVDRHGTKVDPAAAPESARHRLIGGGPLAEREITLSGPRVIWPEPGASIVALWDADSRYTALKAGYHGGASLAEVTIPALAFLPFGAEPPKGWRELGDQRPVWWAPEETGKAPLPDEYTARPVAATASAPKKPTAKAKKDQAEVARMHHGALFDVALTTEGDDALLTPTVVSRTETLVTALLDSETYQAQLGGLARKPQQEQVHKALTTLLDSGGTLPVTALAQRVGMPVTRGVGFAAVLGQLLNYDGVQVLETLPDGRTLRLHAALLREQFALGAG", "text": "FUNCTION: BREX systems (bacteriophage exclusion) provide immunity against bacteriophage. Part of a type 2 BREX system (Probable). Previously called the phage growth limitation (Pgl) system, it confers protection against bacteriophage phiC31. The bacteria allows one cycle of phage infection, but subsequent cycles are impaired, protecting the original bacterial colony (PubMed:7642495). The system undergoes high rates (10(-3) to 10(-4)) of phase reversion, i.e. loss and regain of phiC31 resistance (PubMed:8446035). When the pglW-pglX-pglY-pglZ genes are transformed into a susceptible S.lividans (strain 1326) they confer resistance to infection by phage phiC31 and phiBT1; all 4 genes are necessary (PubMed:11972785). FUNCTION: Probably an antitoxin component of a type II toxin-antitoxin (TA) system. Inhibits the toxic activity of its cognate toxin PglX. SIMILARITY: Belongs to the alkaline phosphatase superfamily."}
{"protein": "MVYCPYNKEHKMLRKKLQQHILKCRVIYKDTVELMVCPFNSSHLIPEPQFFQHTQSCEDRNIIVHYQTSAPAVLSEDTRHAKIESEENWDDDESVPDYDPQVYCSRANIVREPNGLFPAQRRAFIEQEKRRHFGEDYEEEKKPRKAKARADLRPTPYEHRRPYSRRQ", "text": "FUNCTION: Acts via the piwi-interacting RNA (piRNA) pathway which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and piwi proteins and governs the methylation and subsequent repression of transposons. Required for repression of transposons and neighboring genes in ovarian somatic and germline cells. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the UPF0224 (FAM112) family."}
{"protein": "MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT", "text": "FUNCTION: Viroporin that forms a homopentameric ion channel displaying low ion selectivity. May play a role in virus morphogenesis and pathogenicity at various stages of the viral life cycle. Accumulates at the membrane of the Golgi apparatus in infected cells and may facilitate virus release by modifying the secretory pathway. May enhance host membrane permeability and disrupt cellular ion homeostasis, which can be sensed as damage-associated molecular patterns/danger signals, triggering NLRP3 inflammasome activation and inflammatory immune response. Also inhibits host TNFA-mediated signaling pathway and may delay apoptosis, allowing time for the virus to replicate. FUNCTION: Viroporin that forms a homopentameric ion channel displaying low ion selectivity (PubMed:18369195, PubMed:22621926, PubMed:25100835, PubMed:27817112). May play a role in virus morphogenesis and pathogenicity at various stages of the viral life cycle. Accumulates at the membrane of the Golgi apparatus in infected cells and may facilitate virus release by modifying the secretory pathway (PubMed:15105532, PubMed:23229815). May enhance host membrane permeability and disrupt cellular ion homeostasis, which can be sensed as damage-associated molecular patterns/danger signals, triggering NLRP3 inflammasome activation and inflammatory immune response (PubMed:23229815). Also inhibits host TNFA-mediated signaling pathway and may delay apoptosis, allowing time for the virus to replicate (PubMed:17494063). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Host cell membrane; Single-pass type II membrane protein Host Golgi apparatus membrane; Single-pass type II membrane protein Host endoplasmic reticulum membrane; Single-pass type II membrane protein Note=Present in very small amount in the virion. Detected in lipid rafts of host Golgi apparatus membrane. SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Host cell membrane; Single-pass type II membrane protein Host Golgi apparatus membrane; Single-pass type II membrane protein. Host endoplasmic reticulum membrane; Single-pass type II membrane protein. Note=Present in very small amount in the virion. Detected in lipid rafts of host Golgi apparatus membrane. SIMILARITY: Belongs to the orthopneumovirus small hydrophobic protein family."}
{"protein": "MKAVIYHAFSHKEAKDHDVQELGTQRAEAFVRAFLKQSIPHMSQQDCESHLQRKAVILEYFTRLKPKPRPKKKSKGLSAKQRRELRLFDIKPEQQRYSLFLPLHELWKQYIRDLCNGLKPDTQPQMIQAKLLKADLHGAVISVTKSKCPSYVGVTGILLQETKHVFKIITKEDHLKVIPKQNCVFTIEIDDFISYIYGSKFQLRASERSAKKFKAKGTIDL", "text": "FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 1 family."}
{"protein": "MILTVKPLQGKECNVQVTEDEKVSTVKELVSERLNIPPNQQRLLYKGKALADEHRLSDYSIGPEAKLNLVVRPAGERSGVTGMASSNSAVGGVWQTLSTVLAKHFSPADAAKVQEQLIKDYERSLRQLSLDDIERLAVRLLHPDSEGMDTSYLD", "text": "FUNCTION: As part of a cytosolic protein quality control complex, the bag6/bat3 complex, maintains misfolded and hydrophobic patches- containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The bag6/bat3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The bag6/bat3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus."}
{"protein": "YIINVPPRCPPGSKFVKNKCRVIVP", "text": "FUNCTION: Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities (By similarity). Displays antimicrobial activity against bacteria and fungi (By similarity). Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secapin family."}
{"protein": "MNSLVALVLLGQIIGSTLSSQVRGDLECDEKDAKEWTDTGVRYINEHKLHGYKYALNVIKNIVVVPWDGDWVAVFLKLNLLETECHVLDPTPVKNCTVRPQHNHAVEMDCDVKIMFNVDTFKEDVFAKCHSTPDSVENVRRNCPKCPILLPSNNPQVVDSVEYVLNKHNEKLSDHVYEVLEISRGQHKYEPEAYYVEFAIVEVNCTAQELHDDHHHCHPNTAGEDHIGFCRATVFRSHASLEKPKDEQFESDCVILHVKEGHAHSHLIQQHVEKDSISPEHNNTALNFVHPHNDTSTSHESHEHLAEVPVAFVKKELPKDISDRHTTPVKGCPGKVHHFEL", "text": "FUNCTION: Potent inhibitor of hemorrhagic activity but also proteolytic activities of atrolysin C and jararhagin. Inhibition occurs by formation of a non-covalent complex between BJ46a and the proteinases at their metalloproteinase domains. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the fetuin family."}
{"protein": "MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH", "text": "FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis (biotin, thiamine, molybdopterin). Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine, then delivers the sulfur to an acceptor protein such as CyaY, IscU, IscX, MoaD/MoeB, ThiI, or TusA. Transfers sulfur to acceptor proteins via a transpersulfidation reaction; the flexibility of the persulfide sulfur-carrying Cys-328 allows it to reach different partners docked on the homodimer surface. May function as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to an acceptor protein. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Transfers sulfur onto 'Cys- 456' of ThiI and onto 'Cys-19' of TusA in transpersulfidation reactions. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily."}
{"protein": "MMEGYYIIENPGVVPAERRFRMKDLKAWGYDLHLGTIEGERAYFVSKVGERREGEKYQVGGKEYYIEETQKDIPGNARLLARIVIERGNPYLEFWLEEEDTKFPLAKEDPRIILKRIWEKEKLNQLLKHVRAIGLTTDFYKDNVFIKSIPLPYEEYPPKVRRVLREVRDIHRDLTGFGRFVFQYFGEVEKAHNYRLHWTLPTLHLFDVDIANEVDKILGMLD", "text": "SIMILARITY: Belongs to the UPF0128 family."}
{"protein": "QGLIPFPRV", "text": "FUNCTION: Mediates visceral muscle contractile activity (myotropic activity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the periviscerokinin family."}
{"protein": "MDSLTLFFTGALVAVGIYWFLCVLGPAERKGKRAVDLSGGSISAEKVQDNYKQYWSFFRRPKEIETAEKVPDFVDTFYNLVTDIYEWGWGQSFHFSPSIPGKSHKDATRLHEEMAVDLIQVKPGQKILDVGCGVGGPMRAIASHSRANVVGITINEYQVNRARLHNKKAGLDALCEVVCGNFLQMPFDDNSFDGAYSIEATCHAPKLEEVYAEIYRVLKPGSMYVSYEWVTTEKFKAEDDEHVEVIQGIERGDALPGLRAYVDIAETAKKVGFEIVKEKDLASPPAEPWWTRLKMGRLAYWRNHIVVQILSAVGVAPKGTVDVHEMLFKTADYLTRGGETGIFSPMHMILCRKPESPEESS", "text": "FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to the methylene group of 24-methylene lophenol to form 24-ethylidene lophenol. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family."}
{"protein": "MTSDEAKKARFCLHGGPSYEGYSFGAPVSVGGEVVFTTSLVGYPDSMTDPSYKGQILVFTQPLIGNYGVPDGSVRDQYGLLKYMESSKVHVSAIVVAEYAWEYSHWTAVQSLGDWCRKEGVAAIGGIDTRAVVQYLRESGSTMGRVDVEGAAASARVVDPSKVNLVAQVSTKSPFYIPGKPSRVNYDVALVDCGVKENILRCLVVRGVNVTVFPYDYDVCSIAHHFDGVFISNGPGDPIHYRNSTVANLRRLLQDPDLQQVPIFGICMGHQLLALAAGASTVKMKYGNRAHNIPALDLSTGQCHITSQNHGYAVDAATLPRDEFVPLFVNLNDKSNEGIIHVSRPIYSTQFHPEGKGGPMDCSFLFDEYVERMRCYRKLFRQEPFIRFPVIGLPKARVL", "text": "SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CarA family."}
{"protein": "MSNESTRVTVSRGCTASDECAQALERTNDELDRESSVSESRSDEESHEKLSRRRFPTLGIGIWLDLKDRIPYYKSDWVDAFNYRVIPSIVDTYFNNLLPAIAFAQDMFDRTDNSYGVNEVLLSSAMAGIVFGVLGGQPLCIVGVTGPISIFNYTVYEIIKPLNTSYFGFMFWICMWSMIFHLVLAFTNAVCLLQYVTTFPCDIFGLFINVVYIQKGIQILTRQFSAKSGEKSVQDGFASVVVALVMTAFGLFFKLFHYYPLFSHRIRTFISDYSTALSVLFWSSFTHFGGYLHDVKFKKLPITKAFFPTSKVNRPQNTWLAYEPIPVKDVFIALPFGIFLTILFYFDHNVSSLMAQRHQYKLKKPSSFHYDFALLGLTTCISGVLGIPAPNGLIPQAPLHTETLLVRDSNQKVISCVEQRFTNTFQGLMILGTMTRPLLVCLGEIPQAVLSGLFFIMGINGLMTNSIIQRLVFLFSDPNRRDNTSPLMKVSKKSMLIFLSFSLTGFAGEFAITNTIAAIGFPLVLLLSVLVSFSFAYIFPTEELKILDTNVAQKFTIKNLLLENIRDAKFCDKHED", "text": "FUNCTION: Functions in boric acid/borate export across the plasma membrane, and thereby protects yeast cells from boron toxicity. Involved in the trafficking of proteins to the vacuole. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family."}
{"protein": "MAWRSGLCETDSRTLKQFLQEECMWKLVGKSRKHREYRAVACRSTIFSPEDDSSCILCQLLLLYRDGEWIICFCCNGRYQGHYGVNHVHRRRRRICHLPTLYQLSFGGPLGPASIDFLPSFSQVTSSMTCDGITPDVIYEVCMLVPQDEAKRILVKGHGAMDLTCQKAVTLGGAGAWLLPRPEGYTLFFYILCYDLFTSCGNRCDIPSMTRLMAAATACGQAGCSFCTDHEGHVDPTGNYVGCTPDMGRCLCYVPCGPMTQSLIHNEEPATFFCESDDAKYLCAVGSKTAAQVTLGDGLDYHIGVKDSEGRWLPVKTDVWDLVKVEEPVSRMIVCSCPVLKNLVH", "text": "FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparing capsid uncoating (By similarity). Additionally, antagonizes the viral DNA-triggered antiviral immune response by targeting host STING1 and preventing its dimerization and trafficking (PubMed:32238587). SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 2 family."}
{"protein": "MRILVTNDDGIQSKGIIVLAELLSEEHEVFVVAPDKERSATGHSITIHVPLWMKKVFISERVVAYSTTGTPADCVKLAYNVVMDKRVDLIVSGVNRGPNMGMDILHSGTVSGAMEGAMMNIPSIAISSANYESPDFEGAARFLIDFLKEFDFSLLDPFTMLNINVPAGEIKGWRFTRQSRRRWNDYFEERVSPFGEKYYWMMGEVIEDDDRDDVDYKAVREGYVSITPIHPFLTNEQCLKKLREVYD", "text": "FUNCTION: Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SurE nucleotidase family."}
{"protein": "MDGLGEKKPWGKLSRLLGAETESSSELFLYKKEWTIGRKKACDLSFPGNKLVSGEHCKITVNEESGSVSLEDTSTNGTVINKLKVVKKQTYPLKNGDVIYVVYRKNEPEQNVAYLYKSLNQAEDSMQNPADTSGSEEADTQTLSSQDDQLSYEEPQPSTSTSSLFSTPTTSASEPACTLLYKSQASVPGVQLESGEKSGESLEGHSSTSDATAHEKGSLGPPKKRMRTEDLWTGNKNLVSASCSKGASDESKTPSMKPDKMEETLTCIICQELLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPEKCRSEEDRCSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYTVCRQCPGYVRHNIQPPPYPPPSDTEASRTQGDAPSTSTNFPTATQEYVCPSHGSHVICTCCFQPMPDRRAEREHNSHVAPQQCTICLEPFCHMYWGCNRMGCFGCLAPFCELNLGDKCLDGVLNNNNYESDILKNYLASRGLTWKDMLNESLSAAQRGVFMLPDYRINGTTVLCYFCGLRNFRILTYQYRQNIPASELPVTVTSRPNCYWGRNCRTQVKAHHAMKFNHICEQTRFKN", "text": "FUNCTION: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys- 48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. May also promote the formation of 'Lys- 63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating ubc13-mms2 (ube2n-ube2v2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress. SUBCELLULAR LOCATION: Nucleus, PML body. SIMILARITY: Belongs to the CHFR family."}
{"protein": "MDRRDAMALSGSGSYYIQRGIPGSGPPPPQTQPTFHGSQGFHHFTNSISPFGSNPNPNPNPGGVSTGFVSPPLPVDSSPADSSAAAAGALVAPPSGDTSVKRKRGRPRKYGQDGGSVSLALSPSISNVSPNSNKRGRGRPPGSGKKQRLSSIGEMMPSSTGMSFTPHVIVVSIGEDIASKVISFSHQGPRAICVLSASGAVSTATLLQPAPSHGTIIYEGLFELISLSTSYLNTTDNDYPNRTGSLAVSLASPDGRVIGGGIGGPLIAASQVQVIVGSFIWAIPKGKIKKREETSEDVQDTDALENNNDNTAATSPPVPQQSQNIVQTPVGIWSTGSRSMDMHHPHMDIDLMRG", "text": "FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). SUBCELLULAR LOCATION: Nucleus."}
{"protein": "MAKRTKKVGIVGKYGTRYGASLRKMVKKIEISQHAKYTCSFCGKTKMKRRAVGIWHCGSCMKTVAGGAWTYNTTSAVTVKSAIKRLKEMKDQ", "text": "FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43 family."}